data_9NOU
# 
_entry.id   9NOU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9NOU         pdb_00009nou 10.2210/pdb9nou/pdb 
WWPDB D_1000293564 ?            ?                   
EMDB  EMD-49617    ?            ?                   
# 
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 2025-05-14 ? 
2 'Structure model' 1 1 2025-05-21 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
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 2 'Structure model' 'Data collection'     
2 2 '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 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 2 '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 2 'Structure model' '_citation.country'                 
2 2 'Structure model' '_citation.journal_abbrev'          
3 2 'Structure model' '_citation.journal_id_ASTM'         
4 2 'Structure model' '_citation.journal_id_CSD'          
5 2 'Structure model' '_citation.journal_id_ISSN'         
6 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
7 2 'Structure model' '_citation.title'                   
8 2 'Structure model' '_citation_author.name'             
9 2 '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                        9NOU 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Human sweet taste receptor (TAS1R2 + TAS1R3) VFT domains from the combined datasets' 
_pdbx_database_related.db_id          EMD-49617 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              cz2195@columbia.edu 
_pdbx_contact_author.name_first         Charles 
_pdbx_contact_author.name_last          Zuker 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5201-8718 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Juen, Z.'            1 ? 
'Lu, Z.'              2 ? 
'Yu, R.'              3 ? 
'Chang, A.N.'         4 ? 
'Wang, B.'            5 ? 
'Fitzpatrick, A.W.P.' 6 ? 
'Zuker, C.S.'         7 ? 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Cell 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1097-4172 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'The structure of human sweetness.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.cell.2025.04.021 
_citation.pdbx_database_id_PubMed   40339580 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Juen, Z.'            1 ? 
primary 'Lu, Z.'              2 ? 
primary 'Yu, R.'              3 ? 
primary 'Chang, A.N.'         4 ? 
primary 'Wang, B.'            5 ? 
primary 'Fitzpatrick, A.W.P.' 6 ? 
primary 'Zuker, C.S.'         7 ? 
# 
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 'Taste receptor type 1 member 3'         58379.551 1  ? ? ? ? 
2 polymer     man 'Taste receptor type 1 member 2'         59725.098 1  ? ? ? ? 
3 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   15 ? ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Sweet taste receptor T1R3'                               
2 'G-protein coupled receptor 71,Sweet taste receptor T1R2' 
# 
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 
;MKTIIALSYIFCLVFADYKDDDDKAAAAPLCLSQQLRMKGDYVLGGLFPLGEAEEAGLRSRTRPSSPVCTRFSSNGLLWA
LAMKMAVEEINNKSDLLPGLRLGYDLFDTCSEPVVAMKPSLMFLAKAGSRDIAAYCNYTQYQPRVLAVIGPHSSELAMVT
GKFFSFFLMPQVSYGASMELLSARETFPSFFRTVPSDRVQLTAAAELLQEFGWNWVAALGSDDEYGRQGLSIFSALAAAR
GICIAHEGLVPLPRADDSRLGKVQDVLHQVNQSSVQVVLLFASVHAAHALFNYSISSRLSPKVWVASEAWLTSDLVMGLP
GMAQMGTVLGFLQRGAQLHEFPQYVKTHLALATDPAFCSALGEREQGLEEDVVGQRCPQCDCITLQNVSAGLNHHQTFSV
YAAVYSVAQALHNTLQCNASGCPAQDPVKPWQLLENMYNLTFHVGGLPLRFDSSGNVDMEYDLKLWVWQGSVPRLHDVGR
FNGSLRTERLKIRWHTSDNQKPVSRCSRQCQEGQVRRVKGFHSCCYDC
;
;MKTIIALSYIFCLVFADYKDDDDKAAAAPLCLSQQLRMKGDYVLGGLFPLGEAEEAGLRSRTRPSSPVCTRFSSNGLLWA
LAMKMAVEEINNKSDLLPGLRLGYDLFDTCSEPVVAMKPSLMFLAKAGSRDIAAYCNYTQYQPRVLAVIGPHSSELAMVT
GKFFSFFLMPQVSYGASMELLSARETFPSFFRTVPSDRVQLTAAAELLQEFGWNWVAALGSDDEYGRQGLSIFSALAAAR
GICIAHEGLVPLPRADDSRLGKVQDVLHQVNQSSVQVVLLFASVHAAHALFNYSISSRLSPKVWVASEAWLTSDLVMGLP
GMAQMGTVLGFLQRGAQLHEFPQYVKTHLALATDPAFCSALGEREQGLEEDVVGQRCPQCDCITLQNVSAGLNHHQTFSV
YAAVYSVAQALHNTLQCNASGCPAQDPVKPWQLLENMYNLTFHVGGLPLRFDSSGNVDMEYDLKLWVWQGSVPRLHDVGR
FNGSLRTERLKIRWHTSDNQKPVSRCSRQCQEGQVRRVKGFHSCCYDC
;
B ? 
2 'polypeptide(L)' no no 
;MKTIIALSYIFCLVFAYPYDVPDYAAAAEPAENSDFYLPGDYLLGGLFSLHANMKGIVHLNFLQVPMCKEYEVKVIGYNL
MQAMRFAVEEINNDSSLLPGVLLGYEIVDVCYISNNVQPVLYFLAHEDNLLPIQEDYSNYISRVVAVIGPDNSESVMTVA
NFLSLFLLPQITYSAISDELRDKVRFPALLRTTPSADHHIEAMVQLMLHFRWNWIIVLVSSDTYGRDNGQLLGERVARRD
ICIAFQETLPTLQPNQNMTSEERQRLVTIVDKLQQSTARVVVVFSPDLTLYHFFNEVLRQNFTGAVWIASESWAIDPVLH
NLTELRHLGTFLGITIQSVPIPGFSEFREWGPQAGPPPLSRTSQSYTCNQECDNCLNATLSFNTILRLSGERVVYSVYSA
VYAVAHALHSLLGCDKSTCTKRVVYPWQLLEEIWKVNFTLLDHQIFFDPQGDVALHLEIVQWQWDRSQNPFQSVASYYPL
QRQLKNIQDISWHTINNTIPMSMCSKRCQSGQKKKPVGIHVCCF
;
;MKTIIALSYIFCLVFAYPYDVPDYAAAAEPAENSDFYLPGDYLLGGLFSLHANMKGIVHLNFLQVPMCKEYEVKVIGYNL
MQAMRFAVEEINNDSSLLPGVLLGYEIVDVCYISNNVQPVLYFLAHEDNLLPIQEDYSNYISRVVAVIGPDNSESVMTVA
NFLSLFLLPQITYSAISDELRDKVRFPALLRTTPSADHHIEAMVQLMLHFRWNWIIVLVSSDTYGRDNGQLLGERVARRD
ICIAFQETLPTLQPNQNMTSEERQRLVTIVDKLQQSTARVVVVFSPDLTLYHFFNEVLRQNFTGAVWIASESWAIDPVLH
NLTELRHLGTFLGITIQSVPIPGFSEFREWGPQAGPPPLSRTSQSYTCNQECDNCLNATLSFNTILRLSGERVVYSVYSA
VYAVAHALHSLLGCDKSTCTKRVVYPWQLLEEIWKVNFTLLDHQIFFDPQGDVALHLEIVQWQWDRSQNPFQSVASYYPL
QRQLKNIQDISWHTINNTIPMSMCSKRCQSGQKKKPVGIHVCCF
;
A ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        2-acetamido-2-deoxy-beta-D-glucopyranose 
_pdbx_entity_nonpoly.comp_id     NAG 
# 
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   LYS n 
1 3   THR n 
1 4   ILE n 
1 5   ILE n 
1 6   ALA n 
1 7   LEU n 
1 8   SER n 
1 9   TYR n 
1 10  ILE n 
1 11  PHE n 
1 12  CYS n 
1 13  LEU n 
1 14  VAL n 
1 15  PHE n 
1 16  ALA n 
1 17  ASP n 
1 18  TYR n 
1 19  LYS n 
1 20  ASP n 
1 21  ASP n 
1 22  ASP n 
1 23  ASP n 
1 24  LYS n 
1 25  ALA n 
1 26  ALA n 
1 27  ALA n 
1 28  ALA n 
1 29  PRO n 
1 30  LEU n 
1 31  CYS n 
1 32  LEU n 
1 33  SER n 
1 34  GLN n 
1 35  GLN n 
1 36  LEU n 
1 37  ARG n 
1 38  MET n 
1 39  LYS n 
1 40  GLY n 
1 41  ASP n 
1 42  TYR n 
1 43  VAL n 
1 44  LEU n 
1 45  GLY n 
1 46  GLY n 
1 47  LEU n 
1 48  PHE n 
1 49  PRO n 
1 50  LEU n 
1 51  GLY n 
1 52  GLU n 
1 53  ALA n 
1 54  GLU n 
1 55  GLU n 
1 56  ALA n 
1 57  GLY n 
1 58  LEU n 
1 59  ARG n 
1 60  SER n 
1 61  ARG n 
1 62  THR n 
1 63  ARG n 
1 64  PRO n 
1 65  SER n 
1 66  SER n 
1 67  PRO n 
1 68  VAL n 
1 69  CYS n 
1 70  THR n 
1 71  ARG n 
1 72  PHE n 
1 73  SER n 
1 74  SER n 
1 75  ASN n 
1 76  GLY n 
1 77  LEU n 
1 78  LEU n 
1 79  TRP n 
1 80  ALA n 
1 81  LEU n 
1 82  ALA n 
1 83  MET n 
1 84  LYS n 
1 85  MET n 
1 86  ALA n 
1 87  VAL n 
1 88  GLU n 
1 89  GLU n 
1 90  ILE n 
1 91  ASN n 
1 92  ASN n 
1 93  LYS n 
1 94  SER n 
1 95  ASP n 
1 96  LEU n 
1 97  LEU n 
1 98  PRO n 
1 99  GLY n 
1 100 LEU n 
1 101 ARG n 
1 102 LEU n 
1 103 GLY n 
1 104 TYR n 
1 105 ASP n 
1 106 LEU n 
1 107 PHE n 
1 108 ASP n 
1 109 THR n 
1 110 CYS n 
1 111 SER n 
1 112 GLU n 
1 113 PRO n 
1 114 VAL n 
1 115 VAL n 
1 116 ALA n 
1 117 MET n 
1 118 LYS n 
1 119 PRO n 
1 120 SER n 
1 121 LEU n 
1 122 MET n 
1 123 PHE n 
1 124 LEU n 
1 125 ALA n 
1 126 LYS n 
1 127 ALA n 
1 128 GLY n 
1 129 SER n 
1 130 ARG n 
1 131 ASP n 
1 132 ILE n 
1 133 ALA n 
1 134 ALA n 
1 135 TYR n 
1 136 CYS n 
1 137 ASN n 
1 138 TYR n 
1 139 THR n 
1 140 GLN n 
1 141 TYR n 
1 142 GLN n 
1 143 PRO n 
1 144 ARG n 
1 145 VAL n 
1 146 LEU n 
1 147 ALA n 
1 148 VAL n 
1 149 ILE n 
1 150 GLY n 
1 151 PRO n 
1 152 HIS n 
1 153 SER n 
1 154 SER n 
1 155 GLU n 
1 156 LEU n 
1 157 ALA n 
1 158 MET n 
1 159 VAL n 
1 160 THR n 
1 161 GLY n 
1 162 LYS n 
1 163 PHE n 
1 164 PHE n 
1 165 SER n 
1 166 PHE n 
1 167 PHE n 
1 168 LEU n 
1 169 MET n 
1 170 PRO n 
1 171 GLN n 
1 172 VAL n 
1 173 SER n 
1 174 TYR n 
1 175 GLY n 
1 176 ALA n 
1 177 SER n 
1 178 MET n 
1 179 GLU n 
1 180 LEU n 
1 181 LEU n 
1 182 SER n 
1 183 ALA n 
1 184 ARG n 
1 185 GLU n 
1 186 THR n 
1 187 PHE n 
1 188 PRO n 
1 189 SER n 
1 190 PHE n 
1 191 PHE n 
1 192 ARG n 
1 193 THR n 
1 194 VAL n 
1 195 PRO n 
1 196 SER n 
1 197 ASP n 
1 198 ARG n 
1 199 VAL n 
1 200 GLN n 
1 201 LEU n 
1 202 THR n 
1 203 ALA n 
1 204 ALA n 
1 205 ALA n 
1 206 GLU n 
1 207 LEU n 
1 208 LEU n 
1 209 GLN n 
1 210 GLU n 
1 211 PHE n 
1 212 GLY n 
1 213 TRP n 
1 214 ASN n 
1 215 TRP n 
1 216 VAL n 
1 217 ALA n 
1 218 ALA n 
1 219 LEU n 
1 220 GLY n 
1 221 SER n 
1 222 ASP n 
1 223 ASP n 
1 224 GLU n 
1 225 TYR n 
1 226 GLY n 
1 227 ARG n 
1 228 GLN n 
1 229 GLY n 
1 230 LEU n 
1 231 SER n 
1 232 ILE n 
1 233 PHE n 
1 234 SER n 
1 235 ALA n 
1 236 LEU n 
1 237 ALA n 
1 238 ALA n 
1 239 ALA n 
1 240 ARG n 
1 241 GLY n 
1 242 ILE n 
1 243 CYS n 
1 244 ILE n 
1 245 ALA n 
1 246 HIS n 
1 247 GLU n 
1 248 GLY n 
1 249 LEU n 
1 250 VAL n 
1 251 PRO n 
1 252 LEU n 
1 253 PRO n 
1 254 ARG n 
1 255 ALA n 
1 256 ASP n 
1 257 ASP n 
1 258 SER n 
1 259 ARG n 
1 260 LEU n 
1 261 GLY n 
1 262 LYS n 
1 263 VAL n 
1 264 GLN n 
1 265 ASP n 
1 266 VAL n 
1 267 LEU n 
1 268 HIS n 
1 269 GLN n 
1 270 VAL n 
1 271 ASN n 
1 272 GLN n 
1 273 SER n 
1 274 SER n 
1 275 VAL n 
1 276 GLN n 
1 277 VAL n 
1 278 VAL n 
1 279 LEU n 
1 280 LEU n 
1 281 PHE n 
1 282 ALA n 
1 283 SER n 
1 284 VAL n 
1 285 HIS n 
1 286 ALA n 
1 287 ALA n 
1 288 HIS n 
1 289 ALA n 
1 290 LEU n 
1 291 PHE n 
1 292 ASN n 
1 293 TYR n 
1 294 SER n 
1 295 ILE n 
1 296 SER n 
1 297 SER n 
1 298 ARG n 
1 299 LEU n 
1 300 SER n 
1 301 PRO n 
1 302 LYS n 
1 303 VAL n 
1 304 TRP n 
1 305 VAL n 
1 306 ALA n 
1 307 SER n 
1 308 GLU n 
1 309 ALA n 
1 310 TRP n 
1 311 LEU n 
1 312 THR n 
1 313 SER n 
1 314 ASP n 
1 315 LEU n 
1 316 VAL n 
1 317 MET n 
1 318 GLY n 
1 319 LEU n 
1 320 PRO n 
1 321 GLY n 
1 322 MET n 
1 323 ALA n 
1 324 GLN n 
1 325 MET n 
1 326 GLY n 
1 327 THR n 
1 328 VAL n 
1 329 LEU n 
1 330 GLY n 
1 331 PHE n 
1 332 LEU n 
1 333 GLN n 
1 334 ARG n 
1 335 GLY n 
1 336 ALA n 
1 337 GLN n 
1 338 LEU n 
1 339 HIS n 
1 340 GLU n 
1 341 PHE n 
1 342 PRO n 
1 343 GLN n 
1 344 TYR n 
1 345 VAL n 
1 346 LYS n 
1 347 THR n 
1 348 HIS n 
1 349 LEU n 
1 350 ALA n 
1 351 LEU n 
1 352 ALA n 
1 353 THR n 
1 354 ASP n 
1 355 PRO n 
1 356 ALA n 
1 357 PHE n 
1 358 CYS n 
1 359 SER n 
1 360 ALA n 
1 361 LEU n 
1 362 GLY n 
1 363 GLU n 
1 364 ARG n 
1 365 GLU n 
1 366 GLN n 
1 367 GLY n 
1 368 LEU n 
1 369 GLU n 
1 370 GLU n 
1 371 ASP n 
1 372 VAL n 
1 373 VAL n 
1 374 GLY n 
1 375 GLN n 
1 376 ARG n 
1 377 CYS n 
1 378 PRO n 
1 379 GLN n 
1 380 CYS n 
1 381 ASP n 
1 382 CYS n 
1 383 ILE n 
1 384 THR n 
1 385 LEU n 
1 386 GLN n 
1 387 ASN n 
1 388 VAL n 
1 389 SER n 
1 390 ALA n 
1 391 GLY n 
1 392 LEU n 
1 393 ASN n 
1 394 HIS n 
1 395 HIS n 
1 396 GLN n 
1 397 THR n 
1 398 PHE n 
1 399 SER n 
1 400 VAL n 
1 401 TYR n 
1 402 ALA n 
1 403 ALA n 
1 404 VAL n 
1 405 TYR n 
1 406 SER n 
1 407 VAL n 
1 408 ALA n 
1 409 GLN n 
1 410 ALA n 
1 411 LEU n 
1 412 HIS n 
1 413 ASN n 
1 414 THR n 
1 415 LEU n 
1 416 GLN n 
1 417 CYS n 
1 418 ASN n 
1 419 ALA n 
1 420 SER n 
1 421 GLY n 
1 422 CYS n 
1 423 PRO n 
1 424 ALA n 
1 425 GLN n 
1 426 ASP n 
1 427 PRO n 
1 428 VAL n 
1 429 LYS n 
1 430 PRO n 
1 431 TRP n 
1 432 GLN n 
1 433 LEU n 
1 434 LEU n 
1 435 GLU n 
1 436 ASN n 
1 437 MET n 
1 438 TYR n 
1 439 ASN n 
1 440 LEU n 
1 441 THR n 
1 442 PHE n 
1 443 HIS n 
1 444 VAL n 
1 445 GLY n 
1 446 GLY n 
1 447 LEU n 
1 448 PRO n 
1 449 LEU n 
1 450 ARG n 
1 451 PHE n 
1 452 ASP n 
1 453 SER n 
1 454 SER n 
1 455 GLY n 
1 456 ASN n 
1 457 VAL n 
1 458 ASP n 
1 459 MET n 
1 460 GLU n 
1 461 TYR n 
1 462 ASP n 
1 463 LEU n 
1 464 LYS n 
1 465 LEU n 
1 466 TRP n 
1 467 VAL n 
1 468 TRP n 
1 469 GLN n 
1 470 GLY n 
1 471 SER n 
1 472 VAL n 
1 473 PRO n 
1 474 ARG n 
1 475 LEU n 
1 476 HIS n 
1 477 ASP n 
1 478 VAL n 
1 479 GLY n 
1 480 ARG n 
1 481 PHE n 
1 482 ASN n 
1 483 GLY n 
1 484 SER n 
1 485 LEU n 
1 486 ARG n 
1 487 THR n 
1 488 GLU n 
1 489 ARG n 
1 490 LEU n 
1 491 LYS n 
1 492 ILE n 
1 493 ARG n 
1 494 TRP n 
1 495 HIS n 
1 496 THR n 
1 497 SER n 
1 498 ASP n 
1 499 ASN n 
1 500 GLN n 
1 501 LYS n 
1 502 PRO n 
1 503 VAL n 
1 504 SER n 
1 505 ARG n 
1 506 CYS n 
1 507 SER n 
1 508 ARG n 
1 509 GLN n 
1 510 CYS n 
1 511 GLN n 
1 512 GLU n 
1 513 GLY n 
1 514 GLN n 
1 515 VAL n 
1 516 ARG n 
1 517 ARG n 
1 518 VAL n 
1 519 LYS n 
1 520 GLY n 
1 521 PHE n 
1 522 HIS n 
1 523 SER n 
1 524 CYS n 
1 525 CYS n 
1 526 TYR n 
1 527 ASP n 
1 528 CYS n 
2 1   MET n 
2 2   LYS n 
2 3   THR n 
2 4   ILE n 
2 5   ILE n 
2 6   ALA n 
2 7   LEU n 
2 8   SER n 
2 9   TYR n 
2 10  ILE n 
2 11  PHE n 
2 12  CYS n 
2 13  LEU n 
2 14  VAL n 
2 15  PHE n 
2 16  ALA n 
2 17  TYR n 
2 18  PRO n 
2 19  TYR n 
2 20  ASP n 
2 21  VAL n 
2 22  PRO n 
2 23  ASP n 
2 24  TYR n 
2 25  ALA n 
2 26  ALA n 
2 27  ALA n 
2 28  ALA n 
2 29  GLU n 
2 30  PRO n 
2 31  ALA n 
2 32  GLU n 
2 33  ASN n 
2 34  SER n 
2 35  ASP n 
2 36  PHE n 
2 37  TYR n 
2 38  LEU n 
2 39  PRO n 
2 40  GLY n 
2 41  ASP n 
2 42  TYR n 
2 43  LEU n 
2 44  LEU n 
2 45  GLY n 
2 46  GLY n 
2 47  LEU n 
2 48  PHE n 
2 49  SER n 
2 50  LEU n 
2 51  HIS n 
2 52  ALA n 
2 53  ASN n 
2 54  MET n 
2 55  LYS n 
2 56  GLY n 
2 57  ILE n 
2 58  VAL n 
2 59  HIS n 
2 60  LEU n 
2 61  ASN n 
2 62  PHE n 
2 63  LEU n 
2 64  GLN n 
2 65  VAL n 
2 66  PRO n 
2 67  MET n 
2 68  CYS n 
2 69  LYS n 
2 70  GLU n 
2 71  TYR n 
2 72  GLU n 
2 73  VAL n 
2 74  LYS n 
2 75  VAL n 
2 76  ILE n 
2 77  GLY n 
2 78  TYR n 
2 79  ASN n 
2 80  LEU n 
2 81  MET n 
2 82  GLN n 
2 83  ALA n 
2 84  MET n 
2 85  ARG n 
2 86  PHE n 
2 87  ALA n 
2 88  VAL n 
2 89  GLU n 
2 90  GLU n 
2 91  ILE n 
2 92  ASN n 
2 93  ASN n 
2 94  ASP n 
2 95  SER n 
2 96  SER n 
2 97  LEU n 
2 98  LEU n 
2 99  PRO n 
2 100 GLY n 
2 101 VAL n 
2 102 LEU n 
2 103 LEU n 
2 104 GLY n 
2 105 TYR n 
2 106 GLU n 
2 107 ILE n 
2 108 VAL n 
2 109 ASP n 
2 110 VAL n 
2 111 CYS n 
2 112 TYR n 
2 113 ILE n 
2 114 SER n 
2 115 ASN n 
2 116 ASN n 
2 117 VAL n 
2 118 GLN n 
2 119 PRO n 
2 120 VAL n 
2 121 LEU n 
2 122 TYR n 
2 123 PHE n 
2 124 LEU n 
2 125 ALA n 
2 126 HIS n 
2 127 GLU n 
2 128 ASP n 
2 129 ASN n 
2 130 LEU n 
2 131 LEU n 
2 132 PRO n 
2 133 ILE n 
2 134 GLN n 
2 135 GLU n 
2 136 ASP n 
2 137 TYR n 
2 138 SER n 
2 139 ASN n 
2 140 TYR n 
2 141 ILE n 
2 142 SER n 
2 143 ARG n 
2 144 VAL n 
2 145 VAL n 
2 146 ALA n 
2 147 VAL n 
2 148 ILE n 
2 149 GLY n 
2 150 PRO n 
2 151 ASP n 
2 152 ASN n 
2 153 SER n 
2 154 GLU n 
2 155 SER n 
2 156 VAL n 
2 157 MET n 
2 158 THR n 
2 159 VAL n 
2 160 ALA n 
2 161 ASN n 
2 162 PHE n 
2 163 LEU n 
2 164 SER n 
2 165 LEU n 
2 166 PHE n 
2 167 LEU n 
2 168 LEU n 
2 169 PRO n 
2 170 GLN n 
2 171 ILE n 
2 172 THR n 
2 173 TYR n 
2 174 SER n 
2 175 ALA n 
2 176 ILE n 
2 177 SER n 
2 178 ASP n 
2 179 GLU n 
2 180 LEU n 
2 181 ARG n 
2 182 ASP n 
2 183 LYS n 
2 184 VAL n 
2 185 ARG n 
2 186 PHE n 
2 187 PRO n 
2 188 ALA n 
2 189 LEU n 
2 190 LEU n 
2 191 ARG n 
2 192 THR n 
2 193 THR n 
2 194 PRO n 
2 195 SER n 
2 196 ALA n 
2 197 ASP n 
2 198 HIS n 
2 199 HIS n 
2 200 ILE n 
2 201 GLU n 
2 202 ALA n 
2 203 MET n 
2 204 VAL n 
2 205 GLN n 
2 206 LEU n 
2 207 MET n 
2 208 LEU n 
2 209 HIS n 
2 210 PHE n 
2 211 ARG n 
2 212 TRP n 
2 213 ASN n 
2 214 TRP n 
2 215 ILE n 
2 216 ILE n 
2 217 VAL n 
2 218 LEU n 
2 219 VAL n 
2 220 SER n 
2 221 SER n 
2 222 ASP n 
2 223 THR n 
2 224 TYR n 
2 225 GLY n 
2 226 ARG n 
2 227 ASP n 
2 228 ASN n 
2 229 GLY n 
2 230 GLN n 
2 231 LEU n 
2 232 LEU n 
2 233 GLY n 
2 234 GLU n 
2 235 ARG n 
2 236 VAL n 
2 237 ALA n 
2 238 ARG n 
2 239 ARG n 
2 240 ASP n 
2 241 ILE n 
2 242 CYS n 
2 243 ILE n 
2 244 ALA n 
2 245 PHE n 
2 246 GLN n 
2 247 GLU n 
2 248 THR n 
2 249 LEU n 
2 250 PRO n 
2 251 THR n 
2 252 LEU n 
2 253 GLN n 
2 254 PRO n 
2 255 ASN n 
2 256 GLN n 
2 257 ASN n 
2 258 MET n 
2 259 THR n 
2 260 SER n 
2 261 GLU n 
2 262 GLU n 
2 263 ARG n 
2 264 GLN n 
2 265 ARG n 
2 266 LEU n 
2 267 VAL n 
2 268 THR n 
2 269 ILE n 
2 270 VAL n 
2 271 ASP n 
2 272 LYS n 
2 273 LEU n 
2 274 GLN n 
2 275 GLN n 
2 276 SER n 
2 277 THR n 
2 278 ALA n 
2 279 ARG n 
2 280 VAL n 
2 281 VAL n 
2 282 VAL n 
2 283 VAL n 
2 284 PHE n 
2 285 SER n 
2 286 PRO n 
2 287 ASP n 
2 288 LEU n 
2 289 THR n 
2 290 LEU n 
2 291 TYR n 
2 292 HIS n 
2 293 PHE n 
2 294 PHE n 
2 295 ASN n 
2 296 GLU n 
2 297 VAL n 
2 298 LEU n 
2 299 ARG n 
2 300 GLN n 
2 301 ASN n 
2 302 PHE n 
2 303 THR n 
2 304 GLY n 
2 305 ALA n 
2 306 VAL n 
2 307 TRP n 
2 308 ILE n 
2 309 ALA n 
2 310 SER n 
2 311 GLU n 
2 312 SER n 
2 313 TRP n 
2 314 ALA n 
2 315 ILE n 
2 316 ASP n 
2 317 PRO n 
2 318 VAL n 
2 319 LEU n 
2 320 HIS n 
2 321 ASN n 
2 322 LEU n 
2 323 THR n 
2 324 GLU n 
2 325 LEU n 
2 326 ARG n 
2 327 HIS n 
2 328 LEU n 
2 329 GLY n 
2 330 THR n 
2 331 PHE n 
2 332 LEU n 
2 333 GLY n 
2 334 ILE n 
2 335 THR n 
2 336 ILE n 
2 337 GLN n 
2 338 SER n 
2 339 VAL n 
2 340 PRO n 
2 341 ILE n 
2 342 PRO n 
2 343 GLY n 
2 344 PHE n 
2 345 SER n 
2 346 GLU n 
2 347 PHE n 
2 348 ARG n 
2 349 GLU n 
2 350 TRP n 
2 351 GLY n 
2 352 PRO n 
2 353 GLN n 
2 354 ALA n 
2 355 GLY n 
2 356 PRO n 
2 357 PRO n 
2 358 PRO n 
2 359 LEU n 
2 360 SER n 
2 361 ARG n 
2 362 THR n 
2 363 SER n 
2 364 GLN n 
2 365 SER n 
2 366 TYR n 
2 367 THR n 
2 368 CYS n 
2 369 ASN n 
2 370 GLN n 
2 371 GLU n 
2 372 CYS n 
2 373 ASP n 
2 374 ASN n 
2 375 CYS n 
2 376 LEU n 
2 377 ASN n 
2 378 ALA n 
2 379 THR n 
2 380 LEU n 
2 381 SER n 
2 382 PHE n 
2 383 ASN n 
2 384 THR n 
2 385 ILE n 
2 386 LEU n 
2 387 ARG n 
2 388 LEU n 
2 389 SER n 
2 390 GLY n 
2 391 GLU n 
2 392 ARG n 
2 393 VAL n 
2 394 VAL n 
2 395 TYR n 
2 396 SER n 
2 397 VAL n 
2 398 TYR n 
2 399 SER n 
2 400 ALA n 
2 401 VAL n 
2 402 TYR n 
2 403 ALA n 
2 404 VAL n 
2 405 ALA n 
2 406 HIS n 
2 407 ALA n 
2 408 LEU n 
2 409 HIS n 
2 410 SER n 
2 411 LEU n 
2 412 LEU n 
2 413 GLY n 
2 414 CYS n 
2 415 ASP n 
2 416 LYS n 
2 417 SER n 
2 418 THR n 
2 419 CYS n 
2 420 THR n 
2 421 LYS n 
2 422 ARG n 
2 423 VAL n 
2 424 VAL n 
2 425 TYR n 
2 426 PRO n 
2 427 TRP n 
2 428 GLN n 
2 429 LEU n 
2 430 LEU n 
2 431 GLU n 
2 432 GLU n 
2 433 ILE n 
2 434 TRP n 
2 435 LYS n 
2 436 VAL n 
2 437 ASN n 
2 438 PHE n 
2 439 THR n 
2 440 LEU n 
2 441 LEU n 
2 442 ASP n 
2 443 HIS n 
2 444 GLN n 
2 445 ILE n 
2 446 PHE n 
2 447 PHE n 
2 448 ASP n 
2 449 PRO n 
2 450 GLN n 
2 451 GLY n 
2 452 ASP n 
2 453 VAL n 
2 454 ALA n 
2 455 LEU n 
2 456 HIS n 
2 457 LEU n 
2 458 GLU n 
2 459 ILE n 
2 460 VAL n 
2 461 GLN n 
2 462 TRP n 
2 463 GLN n 
2 464 TRP n 
2 465 ASP n 
2 466 ARG n 
2 467 SER n 
2 468 GLN n 
2 469 ASN n 
2 470 PRO n 
2 471 PHE n 
2 472 GLN n 
2 473 SER n 
2 474 VAL n 
2 475 ALA n 
2 476 SER n 
2 477 TYR n 
2 478 TYR n 
2 479 PRO n 
2 480 LEU n 
2 481 GLN n 
2 482 ARG n 
2 483 GLN n 
2 484 LEU n 
2 485 LYS n 
2 486 ASN n 
2 487 ILE n 
2 488 GLN n 
2 489 ASP n 
2 490 ILE n 
2 491 SER n 
2 492 TRP n 
2 493 HIS n 
2 494 THR n 
2 495 ILE n 
2 496 ASN n 
2 497 ASN n 
2 498 THR n 
2 499 ILE n 
2 500 PRO n 
2 501 MET n 
2 502 SER n 
2 503 MET n 
2 504 CYS n 
2 505 SER n 
2 506 LYS n 
2 507 ARG n 
2 508 CYS n 
2 509 GLN n 
2 510 SER n 
2 511 GLY n 
2 512 GLN n 
2 513 LYS n 
2 514 LYS n 
2 515 LYS n 
2 516 PRO n 
2 517 VAL n 
2 518 GLY n 
2 519 ILE n 
2 520 HIS n 
2 521 VAL n 
2 522 CYS n 
2 523 CYS n 
2 524 PHE 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' 1 528 human ? 'TAS1R3, T1R3, TR3'        ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? human 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 524 human ? 'TAS1R2, GPR71, T1R2, TR2' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? human 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PHE 'L-peptide linking'          y PHENYLALANINE                            ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'          y PROLINE                                  ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking'          y SERINE                                   ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking'          y THREONINE                                ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'          y TRYPTOPHAN                               ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'          y TYROSINE                                 ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'          y VALINE                                   ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
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   -6  ?   ?   ?   B . n 
A 1 2   LYS 2   -5  ?   ?   ?   B . n 
A 1 3   THR 3   -4  ?   ?   ?   B . n 
A 1 4   ILE 4   -3  ?   ?   ?   B . n 
A 1 5   ILE 5   -2  ?   ?   ?   B . n 
A 1 6   ALA 6   -1  ?   ?   ?   B . n 
A 1 7   LEU 7   0   ?   ?   ?   B . n 
A 1 8   SER 8   1   ?   ?   ?   B . n 
A 1 9   TYR 9   2   ?   ?   ?   B . n 
A 1 10  ILE 10  3   ?   ?   ?   B . n 
A 1 11  PHE 11  4   ?   ?   ?   B . n 
A 1 12  CYS 12  5   ?   ?   ?   B . n 
A 1 13  LEU 13  6   ?   ?   ?   B . n 
A 1 14  VAL 14  7   ?   ?   ?   B . n 
A 1 15  PHE 15  8   ?   ?   ?   B . n 
A 1 16  ALA 16  9   ?   ?   ?   B . n 
A 1 17  ASP 17  10  ?   ?   ?   B . n 
A 1 18  TYR 18  11  ?   ?   ?   B . n 
A 1 19  LYS 19  12  ?   ?   ?   B . n 
A 1 20  ASP 20  13  ?   ?   ?   B . n 
A 1 21  ASP 21  14  ?   ?   ?   B . n 
A 1 22  ASP 22  15  ?   ?   ?   B . n 
A 1 23  ASP 23  16  ?   ?   ?   B . n 
A 1 24  LYS 24  17  ?   ?   ?   B . n 
A 1 25  ALA 25  18  ?   ?   ?   B . n 
A 1 26  ALA 26  19  ?   ?   ?   B . n 
A 1 27  ALA 27  20  ?   ?   ?   B . n 
A 1 28  ALA 28  21  ?   ?   ?   B . n 
A 1 29  PRO 29  22  ?   ?   ?   B . n 
A 1 30  LEU 30  23  23  LEU LEU B . n 
A 1 31  CYS 31  24  24  CYS CYS B . n 
A 1 32  LEU 32  25  25  LEU LEU B . n 
A 1 33  SER 33  26  26  SER SER B . n 
A 1 34  GLN 34  27  27  GLN GLN B . n 
A 1 35  GLN 35  28  28  GLN GLN B . n 
A 1 36  LEU 36  29  29  LEU LEU B . n 
A 1 37  ARG 37  30  30  ARG ARG B . n 
A 1 38  MET 38  31  31  MET MET B . n 
A 1 39  LYS 39  32  32  LYS LYS B . n 
A 1 40  GLY 40  33  33  GLY GLY B . n 
A 1 41  ASP 41  34  34  ASP ASP B . n 
A 1 42  TYR 42  35  35  TYR TYR B . n 
A 1 43  VAL 43  36  36  VAL VAL B . n 
A 1 44  LEU 44  37  37  LEU LEU B . n 
A 1 45  GLY 45  38  38  GLY GLY B . n 
A 1 46  GLY 46  39  39  GLY GLY B . n 
A 1 47  LEU 47  40  40  LEU LEU B . n 
A 1 48  PHE 48  41  41  PHE PHE B . n 
A 1 49  PRO 49  42  42  PRO PRO B . n 
A 1 50  LEU 50  43  43  LEU LEU B . n 
A 1 51  GLY 51  44  44  GLY GLY B . n 
A 1 52  GLU 52  45  45  GLU GLU B . n 
A 1 53  ALA 53  46  46  ALA ALA B . n 
A 1 54  GLU 54  47  ?   ?   ?   B . n 
A 1 55  GLU 55  48  ?   ?   ?   B . n 
A 1 56  ALA 56  49  ?   ?   ?   B . n 
A 1 57  GLY 57  50  ?   ?   ?   B . n 
A 1 58  LEU 58  51  ?   ?   ?   B . n 
A 1 59  ARG 59  52  ?   ?   ?   B . n 
A 1 60  SER 60  53  ?   ?   ?   B . n 
A 1 61  ARG 61  54  54  ARG ARG B . n 
A 1 62  THR 62  55  55  THR THR B . n 
A 1 63  ARG 63  56  56  ARG ARG B . n 
A 1 64  PRO 64  57  57  PRO PRO B . n 
A 1 65  SER 65  58  58  SER SER B . n 
A 1 66  SER 66  59  59  SER SER B . n 
A 1 67  PRO 67  60  60  PRO PRO B . n 
A 1 68  VAL 68  61  61  VAL VAL B . n 
A 1 69  CYS 69  62  62  CYS CYS B . n 
A 1 70  THR 70  63  63  THR THR B . n 
A 1 71  ARG 71  64  64  ARG ARG B . n 
A 1 72  PHE 72  65  65  PHE PHE B . n 
A 1 73  SER 73  66  66  SER SER B . n 
A 1 74  SER 74  67  67  SER SER B . n 
A 1 75  ASN 75  68  68  ASN ASN B . n 
A 1 76  GLY 76  69  69  GLY GLY B . n 
A 1 77  LEU 77  70  70  LEU LEU B . n 
A 1 78  LEU 78  71  71  LEU LEU B . n 
A 1 79  TRP 79  72  72  TRP TRP B . n 
A 1 80  ALA 80  73  73  ALA ALA B . n 
A 1 81  LEU 81  74  74  LEU LEU B . n 
A 1 82  ALA 82  75  75  ALA ALA B . n 
A 1 83  MET 83  76  76  MET MET B . n 
A 1 84  LYS 84  77  77  LYS LYS B . n 
A 1 85  MET 85  78  78  MET MET B . n 
A 1 86  ALA 86  79  79  ALA ALA B . n 
A 1 87  VAL 87  80  80  VAL VAL B . n 
A 1 88  GLU 88  81  81  GLU GLU B . n 
A 1 89  GLU 89  82  82  GLU GLU B . n 
A 1 90  ILE 90  83  83  ILE ILE B . n 
A 1 91  ASN 91  84  84  ASN ASN B . n 
A 1 92  ASN 92  85  85  ASN ASN B . n 
A 1 93  LYS 93  86  86  LYS LYS B . n 
A 1 94  SER 94  87  87  SER SER B . n 
A 1 95  ASP 95  88  88  ASP ASP B . n 
A 1 96  LEU 96  89  89  LEU LEU B . n 
A 1 97  LEU 97  90  90  LEU LEU B . n 
A 1 98  PRO 98  91  91  PRO PRO B . n 
A 1 99  GLY 99  92  92  GLY GLY B . n 
A 1 100 LEU 100 93  93  LEU LEU B . n 
A 1 101 ARG 101 94  94  ARG ARG B . n 
A 1 102 LEU 102 95  95  LEU LEU B . n 
A 1 103 GLY 103 96  96  GLY GLY B . n 
A 1 104 TYR 104 97  97  TYR TYR B . n 
A 1 105 ASP 105 98  98  ASP ASP B . n 
A 1 106 LEU 106 99  99  LEU LEU B . n 
A 1 107 PHE 107 100 100 PHE PHE B . n 
A 1 108 ASP 108 101 101 ASP ASP B . n 
A 1 109 THR 109 102 102 THR THR B . n 
A 1 110 CYS 110 103 103 CYS CYS B . n 
A 1 111 SER 111 104 104 SER SER B . n 
A 1 112 GLU 112 105 105 GLU GLU B . n 
A 1 113 PRO 113 106 106 PRO PRO B . n 
A 1 114 VAL 114 107 107 VAL VAL B . n 
A 1 115 VAL 115 108 108 VAL VAL B . n 
A 1 116 ALA 116 109 109 ALA ALA B . n 
A 1 117 MET 117 110 110 MET MET B . n 
A 1 118 LYS 118 111 111 LYS LYS B . n 
A 1 119 PRO 119 112 112 PRO PRO B . n 
A 1 120 SER 120 113 113 SER SER B . n 
A 1 121 LEU 121 114 114 LEU LEU B . n 
A 1 122 MET 122 115 115 MET MET B . n 
A 1 123 PHE 123 116 116 PHE PHE B . n 
A 1 124 LEU 124 117 117 LEU LEU B . n 
A 1 125 ALA 125 118 118 ALA ALA B . n 
A 1 126 LYS 126 119 119 LYS LYS B . n 
A 1 127 ALA 127 120 120 ALA ALA B . n 
A 1 128 GLY 128 121 121 GLY GLY B . n 
A 1 129 SER 129 122 122 SER SER B . n 
A 1 130 ARG 130 123 123 ARG ARG B . n 
A 1 131 ASP 131 124 124 ASP ASP B . n 
A 1 132 ILE 132 125 125 ILE ILE B . n 
A 1 133 ALA 133 126 126 ALA ALA B . n 
A 1 134 ALA 134 127 127 ALA ALA B . n 
A 1 135 TYR 135 128 128 TYR TYR B . n 
A 1 136 CYS 136 129 129 CYS CYS B . n 
A 1 137 ASN 137 130 130 ASN ASN B . n 
A 1 138 TYR 138 131 131 TYR TYR B . n 
A 1 139 THR 139 132 132 THR THR B . n 
A 1 140 GLN 140 133 133 GLN GLN B . n 
A 1 141 TYR 141 134 134 TYR TYR B . n 
A 1 142 GLN 142 135 135 GLN GLN B . n 
A 1 143 PRO 143 136 136 PRO PRO B . n 
A 1 144 ARG 144 137 137 ARG ARG B . n 
A 1 145 VAL 145 138 138 VAL VAL B . n 
A 1 146 LEU 146 139 139 LEU LEU B . n 
A 1 147 ALA 147 140 140 ALA ALA B . n 
A 1 148 VAL 148 141 141 VAL VAL B . n 
A 1 149 ILE 149 142 142 ILE ILE B . n 
A 1 150 GLY 150 143 143 GLY GLY B . n 
A 1 151 PRO 151 144 144 PRO PRO B . n 
A 1 152 HIS 152 145 145 HIS HIS B . n 
A 1 153 SER 153 146 146 SER SER B . n 
A 1 154 SER 154 147 147 SER SER B . n 
A 1 155 GLU 155 148 148 GLU GLU B . n 
A 1 156 LEU 156 149 149 LEU LEU B . n 
A 1 157 ALA 157 150 150 ALA ALA B . n 
A 1 158 MET 158 151 151 MET MET B . n 
A 1 159 VAL 159 152 152 VAL VAL B . n 
A 1 160 THR 160 153 153 THR THR B . n 
A 1 161 GLY 161 154 154 GLY GLY B . n 
A 1 162 LYS 162 155 155 LYS LYS B . n 
A 1 163 PHE 163 156 156 PHE PHE B . n 
A 1 164 PHE 164 157 157 PHE PHE B . n 
A 1 165 SER 165 158 158 SER SER B . n 
A 1 166 PHE 166 159 159 PHE PHE B . n 
A 1 167 PHE 167 160 160 PHE PHE B . n 
A 1 168 LEU 168 161 161 LEU LEU B . n 
A 1 169 MET 169 162 162 MET MET B . n 
A 1 170 PRO 170 163 163 PRO PRO B . n 
A 1 171 GLN 171 164 164 GLN GLN B . n 
A 1 172 VAL 172 165 165 VAL VAL B . n 
A 1 173 SER 173 166 166 SER SER B . n 
A 1 174 TYR 174 167 167 TYR TYR B . n 
A 1 175 GLY 175 168 168 GLY GLY B . n 
A 1 176 ALA 176 169 169 ALA ALA B . n 
A 1 177 SER 177 170 170 SER SER B . n 
A 1 178 MET 178 171 171 MET MET B . n 
A 1 179 GLU 179 172 172 GLU GLU B . n 
A 1 180 LEU 180 173 173 LEU LEU B . n 
A 1 181 LEU 181 174 174 LEU LEU B . n 
A 1 182 SER 182 175 175 SER SER B . n 
A 1 183 ALA 183 176 176 ALA ALA B . n 
A 1 184 ARG 184 177 177 ARG ARG B . n 
A 1 185 GLU 185 178 178 GLU GLU B . n 
A 1 186 THR 186 179 179 THR THR B . n 
A 1 187 PHE 187 180 180 PHE PHE B . n 
A 1 188 PRO 188 181 181 PRO PRO B . n 
A 1 189 SER 189 182 182 SER SER B . n 
A 1 190 PHE 190 183 183 PHE PHE B . n 
A 1 191 PHE 191 184 184 PHE PHE B . n 
A 1 192 ARG 192 185 185 ARG ARG B . n 
A 1 193 THR 193 186 186 THR THR B . n 
A 1 194 VAL 194 187 187 VAL VAL B . n 
A 1 195 PRO 195 188 188 PRO PRO B . n 
A 1 196 SER 196 189 189 SER SER B . n 
A 1 197 ASP 197 190 190 ASP ASP B . n 
A 1 198 ARG 198 191 191 ARG ARG B . n 
A 1 199 VAL 199 192 192 VAL VAL B . n 
A 1 200 GLN 200 193 193 GLN GLN B . n 
A 1 201 LEU 201 194 194 LEU LEU B . n 
A 1 202 THR 202 195 195 THR THR B . n 
A 1 203 ALA 203 196 196 ALA ALA B . n 
A 1 204 ALA 204 197 197 ALA ALA B . n 
A 1 205 ALA 205 198 198 ALA ALA B . n 
A 1 206 GLU 206 199 199 GLU GLU B . n 
A 1 207 LEU 207 200 200 LEU LEU B . n 
A 1 208 LEU 208 201 201 LEU LEU B . n 
A 1 209 GLN 209 202 202 GLN GLN B . n 
A 1 210 GLU 210 203 203 GLU GLU B . n 
A 1 211 PHE 211 204 204 PHE PHE B . n 
A 1 212 GLY 212 205 205 GLY GLY B . n 
A 1 213 TRP 213 206 206 TRP TRP B . n 
A 1 214 ASN 214 207 207 ASN ASN B . n 
A 1 215 TRP 215 208 208 TRP TRP B . n 
A 1 216 VAL 216 209 209 VAL VAL B . n 
A 1 217 ALA 217 210 210 ALA ALA B . n 
A 1 218 ALA 218 211 211 ALA ALA B . n 
A 1 219 LEU 219 212 212 LEU LEU B . n 
A 1 220 GLY 220 213 213 GLY GLY B . n 
A 1 221 SER 221 214 214 SER SER B . n 
A 1 222 ASP 222 215 215 ASP ASP B . n 
A 1 223 ASP 223 216 216 ASP ASP B . n 
A 1 224 GLU 224 217 217 GLU GLU B . n 
A 1 225 TYR 225 218 218 TYR TYR B . n 
A 1 226 GLY 226 219 219 GLY GLY B . n 
A 1 227 ARG 227 220 220 ARG ARG B . n 
A 1 228 GLN 228 221 221 GLN GLN B . n 
A 1 229 GLY 229 222 222 GLY GLY B . n 
A 1 230 LEU 230 223 223 LEU LEU B . n 
A 1 231 SER 231 224 224 SER SER B . n 
A 1 232 ILE 232 225 225 ILE ILE B . n 
A 1 233 PHE 233 226 226 PHE PHE B . n 
A 1 234 SER 234 227 227 SER SER B . n 
A 1 235 ALA 235 228 228 ALA ALA B . n 
A 1 236 LEU 236 229 229 LEU LEU B . n 
A 1 237 ALA 237 230 230 ALA ALA B . n 
A 1 238 ALA 238 231 231 ALA ALA B . n 
A 1 239 ALA 239 232 232 ALA ALA B . n 
A 1 240 ARG 240 233 233 ARG ARG B . n 
A 1 241 GLY 241 234 234 GLY GLY B . n 
A 1 242 ILE 242 235 235 ILE ILE B . n 
A 1 243 CYS 243 236 236 CYS CYS B . n 
A 1 244 ILE 244 237 237 ILE ILE B . n 
A 1 245 ALA 245 238 238 ALA ALA B . n 
A 1 246 HIS 246 239 239 HIS HIS B . n 
A 1 247 GLU 247 240 240 GLU GLU B . n 
A 1 248 GLY 248 241 241 GLY GLY B . n 
A 1 249 LEU 249 242 242 LEU LEU B . n 
A 1 250 VAL 250 243 243 VAL VAL B . n 
A 1 251 PRO 251 244 244 PRO PRO B . n 
A 1 252 LEU 252 245 245 LEU LEU B . n 
A 1 253 PRO 253 246 246 PRO PRO B . n 
A 1 254 ARG 254 247 ?   ?   ?   B . n 
A 1 255 ALA 255 248 ?   ?   ?   B . n 
A 1 256 ASP 256 249 ?   ?   ?   B . n 
A 1 257 ASP 257 250 ?   ?   ?   B . n 
A 1 258 SER 258 251 ?   ?   ?   B . n 
A 1 259 ARG 259 252 ?   ?   ?   B . n 
A 1 260 LEU 260 253 ?   ?   ?   B . n 
A 1 261 GLY 261 254 ?   ?   ?   B . n 
A 1 262 LYS 262 255 255 LYS LYS B . n 
A 1 263 VAL 263 256 256 VAL VAL B . n 
A 1 264 GLN 264 257 257 GLN GLN B . n 
A 1 265 ASP 265 258 258 ASP ASP B . n 
A 1 266 VAL 266 259 259 VAL VAL B . n 
A 1 267 LEU 267 260 260 LEU LEU B . n 
A 1 268 HIS 268 261 261 HIS HIS B . n 
A 1 269 GLN 269 262 262 GLN GLN B . n 
A 1 270 VAL 270 263 263 VAL VAL B . n 
A 1 271 ASN 271 264 264 ASN ASN B . n 
A 1 272 GLN 272 265 265 GLN GLN B . n 
A 1 273 SER 273 266 266 SER SER B . n 
A 1 274 SER 274 267 267 SER SER B . n 
A 1 275 VAL 275 268 268 VAL VAL B . n 
A 1 276 GLN 276 269 269 GLN GLN B . n 
A 1 277 VAL 277 270 270 VAL VAL B . n 
A 1 278 VAL 278 271 271 VAL VAL B . n 
A 1 279 LEU 279 272 272 LEU LEU B . n 
A 1 280 LEU 280 273 273 LEU LEU B . n 
A 1 281 PHE 281 274 274 PHE PHE B . n 
A 1 282 ALA 282 275 275 ALA ALA B . n 
A 1 283 SER 283 276 276 SER SER B . n 
A 1 284 VAL 284 277 277 VAL VAL B . n 
A 1 285 HIS 285 278 278 HIS HIS B . n 
A 1 286 ALA 286 279 279 ALA ALA B . n 
A 1 287 ALA 287 280 280 ALA ALA B . n 
A 1 288 HIS 288 281 281 HIS HIS B . n 
A 1 289 ALA 289 282 282 ALA ALA B . n 
A 1 290 LEU 290 283 283 LEU LEU B . n 
A 1 291 PHE 291 284 284 PHE PHE B . n 
A 1 292 ASN 292 285 285 ASN ASN B . n 
A 1 293 TYR 293 286 286 TYR TYR B . n 
A 1 294 SER 294 287 287 SER SER B . n 
A 1 295 ILE 295 288 288 ILE ILE B . n 
A 1 296 SER 296 289 289 SER SER B . n 
A 1 297 SER 297 290 290 SER SER B . n 
A 1 298 ARG 298 291 291 ARG ARG B . n 
A 1 299 LEU 299 292 292 LEU LEU B . n 
A 1 300 SER 300 293 293 SER SER B . n 
A 1 301 PRO 301 294 294 PRO PRO B . n 
A 1 302 LYS 302 295 295 LYS LYS B . n 
A 1 303 VAL 303 296 296 VAL VAL B . n 
A 1 304 TRP 304 297 297 TRP TRP B . n 
A 1 305 VAL 305 298 298 VAL VAL B . n 
A 1 306 ALA 306 299 299 ALA ALA B . n 
A 1 307 SER 307 300 300 SER SER B . n 
A 1 308 GLU 308 301 301 GLU GLU B . n 
A 1 309 ALA 309 302 302 ALA ALA B . n 
A 1 310 TRP 310 303 303 TRP TRP B . n 
A 1 311 LEU 311 304 304 LEU LEU B . n 
A 1 312 THR 312 305 305 THR THR B . n 
A 1 313 SER 313 306 306 SER SER B . n 
A 1 314 ASP 314 307 307 ASP ASP B . n 
A 1 315 LEU 315 308 308 LEU LEU B . n 
A 1 316 VAL 316 309 309 VAL VAL B . n 
A 1 317 MET 317 310 310 MET MET B . n 
A 1 318 GLY 318 311 311 GLY GLY B . n 
A 1 319 LEU 319 312 312 LEU LEU B . n 
A 1 320 PRO 320 313 313 PRO PRO B . n 
A 1 321 GLY 321 314 314 GLY GLY B . n 
A 1 322 MET 322 315 315 MET MET B . n 
A 1 323 ALA 323 316 316 ALA ALA B . n 
A 1 324 GLN 324 317 317 GLN GLN B . n 
A 1 325 MET 325 318 318 MET MET B . n 
A 1 326 GLY 326 319 319 GLY GLY B . n 
A 1 327 THR 327 320 320 THR THR B . n 
A 1 328 VAL 328 321 321 VAL VAL B . n 
A 1 329 LEU 329 322 322 LEU LEU B . n 
A 1 330 GLY 330 323 323 GLY GLY B . n 
A 1 331 PHE 331 324 324 PHE PHE B . n 
A 1 332 LEU 332 325 325 LEU LEU B . n 
A 1 333 GLN 333 326 326 GLN GLN B . n 
A 1 334 ARG 334 327 327 ARG ARG B . n 
A 1 335 GLY 335 328 328 GLY GLY B . n 
A 1 336 ALA 336 329 329 ALA ALA B . n 
A 1 337 GLN 337 330 330 GLN GLN B . n 
A 1 338 LEU 338 331 331 LEU LEU B . n 
A 1 339 HIS 339 332 332 HIS HIS B . n 
A 1 340 GLU 340 333 333 GLU GLU B . n 
A 1 341 PHE 341 334 334 PHE PHE B . n 
A 1 342 PRO 342 335 335 PRO PRO B . n 
A 1 343 GLN 343 336 336 GLN GLN B . n 
A 1 344 TYR 344 337 337 TYR TYR B . n 
A 1 345 VAL 345 338 338 VAL VAL B . n 
A 1 346 LYS 346 339 339 LYS LYS B . n 
A 1 347 THR 347 340 340 THR THR B . n 
A 1 348 HIS 348 341 341 HIS HIS B . n 
A 1 349 LEU 349 342 342 LEU LEU B . n 
A 1 350 ALA 350 343 343 ALA ALA B . n 
A 1 351 LEU 351 344 344 LEU LEU B . n 
A 1 352 ALA 352 345 345 ALA ALA B . n 
A 1 353 THR 353 346 346 THR THR B . n 
A 1 354 ASP 354 347 347 ASP ASP B . n 
A 1 355 PRO 355 348 348 PRO PRO B . n 
A 1 356 ALA 356 349 349 ALA ALA B . n 
A 1 357 PHE 357 350 350 PHE PHE B . n 
A 1 358 CYS 358 351 351 CYS CYS B . n 
A 1 359 SER 359 352 352 SER SER B . n 
A 1 360 ALA 360 353 353 ALA ALA B . n 
A 1 361 LEU 361 354 354 LEU LEU B . n 
A 1 362 GLY 362 355 ?   ?   ?   B . n 
A 1 363 GLU 363 356 ?   ?   ?   B . n 
A 1 364 ARG 364 357 ?   ?   ?   B . n 
A 1 365 GLU 365 358 ?   ?   ?   B . n 
A 1 366 GLN 366 359 ?   ?   ?   B . n 
A 1 367 GLY 367 360 ?   ?   ?   B . n 
A 1 368 LEU 368 361 ?   ?   ?   B . n 
A 1 369 GLU 369 362 ?   ?   ?   B . n 
A 1 370 GLU 370 363 ?   ?   ?   B . n 
A 1 371 ASP 371 364 ?   ?   ?   B . n 
A 1 372 VAL 372 365 ?   ?   ?   B . n 
A 1 373 VAL 373 366 ?   ?   ?   B . n 
A 1 374 GLY 374 367 ?   ?   ?   B . n 
A 1 375 GLN 375 368 368 GLN GLN B . n 
A 1 376 ARG 376 369 369 ARG ARG B . n 
A 1 377 CYS 377 370 370 CYS CYS B . n 
A 1 378 PRO 378 371 371 PRO PRO B . n 
A 1 379 GLN 379 372 372 GLN GLN B . n 
A 1 380 CYS 380 373 373 CYS CYS B . n 
A 1 381 ASP 381 374 374 ASP ASP B . n 
A 1 382 CYS 382 375 375 CYS CYS B . n 
A 1 383 ILE 383 376 376 ILE ILE B . n 
A 1 384 THR 384 377 377 THR THR B . n 
A 1 385 LEU 385 378 378 LEU LEU B . n 
A 1 386 GLN 386 379 379 GLN GLN B . n 
A 1 387 ASN 387 380 380 ASN ASN B . n 
A 1 388 VAL 388 381 381 VAL VAL B . n 
A 1 389 SER 389 382 382 SER SER B . n 
A 1 390 ALA 390 383 383 ALA ALA B . n 
A 1 391 GLY 391 384 384 GLY GLY B . n 
A 1 392 LEU 392 385 385 LEU LEU B . n 
A 1 393 ASN 393 386 386 ASN ASN B . n 
A 1 394 HIS 394 387 387 HIS HIS B . n 
A 1 395 HIS 395 388 388 HIS HIS B . n 
A 1 396 GLN 396 389 389 GLN GLN B . n 
A 1 397 THR 397 390 390 THR THR B . n 
A 1 398 PHE 398 391 391 PHE PHE B . n 
A 1 399 SER 399 392 392 SER SER B . n 
A 1 400 VAL 400 393 393 VAL VAL B . n 
A 1 401 TYR 401 394 394 TYR TYR B . n 
A 1 402 ALA 402 395 395 ALA ALA B . n 
A 1 403 ALA 403 396 396 ALA ALA B . n 
A 1 404 VAL 404 397 397 VAL VAL B . n 
A 1 405 TYR 405 398 398 TYR TYR B . n 
A 1 406 SER 406 399 399 SER SER B . n 
A 1 407 VAL 407 400 400 VAL VAL B . n 
A 1 408 ALA 408 401 401 ALA ALA B . n 
A 1 409 GLN 409 402 402 GLN GLN B . n 
A 1 410 ALA 410 403 403 ALA ALA B . n 
A 1 411 LEU 411 404 404 LEU LEU B . n 
A 1 412 HIS 412 405 405 HIS HIS B . n 
A 1 413 ASN 413 406 406 ASN ASN B . n 
A 1 414 THR 414 407 407 THR THR B . n 
A 1 415 LEU 415 408 408 LEU LEU B . n 
A 1 416 GLN 416 409 409 GLN GLN B . n 
A 1 417 CYS 417 410 410 CYS CYS B . n 
A 1 418 ASN 418 411 411 ASN ASN B . n 
A 1 419 ALA 419 412 412 ALA ALA B . n 
A 1 420 SER 420 413 413 SER SER B . n 
A 1 421 GLY 421 414 414 GLY GLY B . n 
A 1 422 CYS 422 415 415 CYS CYS B . n 
A 1 423 PRO 423 416 416 PRO PRO B . n 
A 1 424 ALA 424 417 417 ALA ALA B . n 
A 1 425 GLN 425 418 418 GLN GLN B . n 
A 1 426 ASP 426 419 419 ASP ASP B . n 
A 1 427 PRO 427 420 420 PRO PRO B . n 
A 1 428 VAL 428 421 421 VAL VAL B . n 
A 1 429 LYS 429 422 422 LYS LYS B . n 
A 1 430 PRO 430 423 423 PRO PRO B . n 
A 1 431 TRP 431 424 424 TRP TRP B . n 
A 1 432 GLN 432 425 425 GLN GLN B . n 
A 1 433 LEU 433 426 426 LEU LEU B . n 
A 1 434 LEU 434 427 427 LEU LEU B . n 
A 1 435 GLU 435 428 428 GLU GLU B . n 
A 1 436 ASN 436 429 429 ASN ASN B . n 
A 1 437 MET 437 430 430 MET MET B . n 
A 1 438 TYR 438 431 431 TYR TYR B . n 
A 1 439 ASN 439 432 432 ASN ASN B . n 
A 1 440 LEU 440 433 433 LEU LEU B . n 
A 1 441 THR 441 434 434 THR THR B . n 
A 1 442 PHE 442 435 435 PHE PHE B . n 
A 1 443 HIS 443 436 436 HIS HIS B . n 
A 1 444 VAL 444 437 437 VAL VAL B . n 
A 1 445 GLY 445 438 438 GLY GLY B . n 
A 1 446 GLY 446 439 439 GLY GLY B . n 
A 1 447 LEU 447 440 440 LEU LEU B . n 
A 1 448 PRO 448 441 441 PRO PRO B . n 
A 1 449 LEU 449 442 442 LEU LEU B . n 
A 1 450 ARG 450 443 443 ARG ARG B . n 
A 1 451 PHE 451 444 444 PHE PHE B . n 
A 1 452 ASP 452 445 445 ASP ASP B . n 
A 1 453 SER 453 446 446 SER SER B . n 
A 1 454 SER 454 447 447 SER SER B . n 
A 1 455 GLY 455 448 448 GLY GLY B . n 
A 1 456 ASN 456 449 449 ASN ASN B . n 
A 1 457 VAL 457 450 450 VAL VAL B . n 
A 1 458 ASP 458 451 451 ASP ASP B . n 
A 1 459 MET 459 452 452 MET MET B . n 
A 1 460 GLU 460 453 453 GLU GLU B . n 
A 1 461 TYR 461 454 454 TYR TYR B . n 
A 1 462 ASP 462 455 455 ASP ASP B . n 
A 1 463 LEU 463 456 456 LEU LEU B . n 
A 1 464 LYS 464 457 457 LYS LYS B . n 
A 1 465 LEU 465 458 458 LEU LEU B . n 
A 1 466 TRP 466 459 459 TRP TRP B . n 
A 1 467 VAL 467 460 460 VAL VAL B . n 
A 1 468 TRP 468 461 461 TRP TRP B . n 
A 1 469 GLN 469 462 462 GLN GLN B . n 
A 1 470 GLY 470 463 463 GLY GLY B . n 
A 1 471 SER 471 464 464 SER SER B . n 
A 1 472 VAL 472 465 465 VAL VAL B . n 
A 1 473 PRO 473 466 466 PRO PRO B . n 
A 1 474 ARG 474 467 467 ARG ARG B . n 
A 1 475 LEU 475 468 468 LEU LEU B . n 
A 1 476 HIS 476 469 469 HIS HIS B . n 
A 1 477 ASP 477 470 470 ASP ASP B . n 
A 1 478 VAL 478 471 471 VAL VAL B . n 
A 1 479 GLY 479 472 472 GLY GLY B . n 
A 1 480 ARG 480 473 473 ARG ARG B . n 
A 1 481 PHE 481 474 474 PHE PHE B . n 
A 1 482 ASN 482 475 475 ASN ASN B . n 
A 1 483 GLY 483 476 476 GLY GLY B . n 
A 1 484 SER 484 477 477 SER SER B . n 
A 1 485 LEU 485 478 478 LEU LEU B . n 
A 1 486 ARG 486 479 479 ARG ARG B . n 
A 1 487 THR 487 480 480 THR THR B . n 
A 1 488 GLU 488 481 481 GLU GLU B . n 
A 1 489 ARG 489 482 482 ARG ARG B . n 
A 1 490 LEU 490 483 483 LEU LEU B . n 
A 1 491 LYS 491 484 484 LYS LYS B . n 
A 1 492 ILE 492 485 485 ILE ILE B . n 
A 1 493 ARG 493 486 486 ARG ARG B . n 
A 1 494 TRP 494 487 487 TRP TRP B . n 
A 1 495 HIS 495 488 488 HIS HIS B . n 
A 1 496 THR 496 489 489 THR THR B . n 
A 1 497 SER 497 490 490 SER SER B . n 
A 1 498 ASP 498 491 491 ASP ASP B . n 
A 1 499 ASN 499 492 492 ASN ASN B . n 
A 1 500 GLN 500 493 493 GLN GLN B . n 
A 1 501 LYS 501 494 494 LYS LYS B . n 
A 1 502 PRO 502 495 495 PRO PRO B . n 
A 1 503 VAL 503 496 496 VAL VAL B . n 
A 1 504 SER 504 497 497 SER SER B . n 
A 1 505 ARG 505 498 498 ARG ARG B . n 
A 1 506 CYS 506 499 499 CYS CYS B . n 
A 1 507 SER 507 500 500 SER SER B . n 
A 1 508 ARG 508 501 501 ARG ARG B . n 
A 1 509 GLN 509 502 502 GLN GLN B . n 
A 1 510 CYS 510 503 503 CYS CYS B . n 
A 1 511 GLN 511 504 ?   ?   ?   B . n 
A 1 512 GLU 512 505 ?   ?   ?   B . n 
A 1 513 GLY 513 506 ?   ?   ?   B . n 
A 1 514 GLN 514 507 ?   ?   ?   B . n 
A 1 515 VAL 515 508 ?   ?   ?   B . n 
A 1 516 ARG 516 509 ?   ?   ?   B . n 
A 1 517 ARG 517 510 510 ARG ARG B . n 
A 1 518 VAL 518 511 511 VAL VAL B . n 
A 1 519 LYS 519 512 512 LYS LYS B . n 
A 1 520 GLY 520 513 513 GLY GLY B . n 
A 1 521 PHE 521 514 514 PHE PHE B . n 
A 1 522 HIS 522 515 515 HIS HIS B . n 
A 1 523 SER 523 516 516 SER SER B . n 
A 1 524 CYS 524 517 517 CYS CYS B . n 
A 1 525 CYS 525 518 518 CYS CYS B . n 
A 1 526 TYR 526 519 519 TYR TYR B . n 
A 1 527 ASP 527 520 520 ASP ASP B . n 
A 1 528 CYS 528 521 521 CYS CYS B . n 
B 2 1   MET 1   -8  ?   ?   ?   A . n 
B 2 2   LYS 2   -7  ?   ?   ?   A . n 
B 2 3   THR 3   -6  ?   ?   ?   A . n 
B 2 4   ILE 4   -5  ?   ?   ?   A . n 
B 2 5   ILE 5   -4  ?   ?   ?   A . n 
B 2 6   ALA 6   -3  ?   ?   ?   A . n 
B 2 7   LEU 7   -2  ?   ?   ?   A . n 
B 2 8   SER 8   -1  ?   ?   ?   A . n 
B 2 9   TYR 9   0   ?   ?   ?   A . n 
B 2 10  ILE 10  1   ?   ?   ?   A . n 
B 2 11  PHE 11  2   ?   ?   ?   A . n 
B 2 12  CYS 12  3   ?   ?   ?   A . n 
B 2 13  LEU 13  4   ?   ?   ?   A . n 
B 2 14  VAL 14  5   ?   ?   ?   A . n 
B 2 15  PHE 15  6   ?   ?   ?   A . n 
B 2 16  ALA 16  7   ?   ?   ?   A . n 
B 2 17  TYR 17  8   ?   ?   ?   A . n 
B 2 18  PRO 18  9   ?   ?   ?   A . n 
B 2 19  TYR 19  10  ?   ?   ?   A . n 
B 2 20  ASP 20  11  ?   ?   ?   A . n 
B 2 21  VAL 21  12  ?   ?   ?   A . n 
B 2 22  PRO 22  13  ?   ?   ?   A . n 
B 2 23  ASP 23  14  ?   ?   ?   A . n 
B 2 24  TYR 24  15  ?   ?   ?   A . n 
B 2 25  ALA 25  16  ?   ?   ?   A . n 
B 2 26  ALA 26  17  ?   ?   ?   A . n 
B 2 27  ALA 27  18  ?   ?   ?   A . n 
B 2 28  ALA 28  19  ?   ?   ?   A . n 
B 2 29  GLU 29  20  ?   ?   ?   A . n 
B 2 30  PRO 30  21  ?   ?   ?   A . n 
B 2 31  ALA 31  22  ?   ?   ?   A . n 
B 2 32  GLU 32  23  ?   ?   ?   A . n 
B 2 33  ASN 33  24  ?   ?   ?   A . n 
B 2 34  SER 34  25  25  SER SER A . n 
B 2 35  ASP 35  26  26  ASP ASP A . n 
B 2 36  PHE 36  27  27  PHE PHE A . n 
B 2 37  TYR 37  28  28  TYR TYR A . n 
B 2 38  LEU 38  29  29  LEU LEU A . n 
B 2 39  PRO 39  30  30  PRO PRO A . n 
B 2 40  GLY 40  31  31  GLY GLY A . n 
B 2 41  ASP 41  32  32  ASP ASP A . n 
B 2 42  TYR 42  33  33  TYR TYR A . n 
B 2 43  LEU 43  34  34  LEU LEU A . n 
B 2 44  LEU 44  35  35  LEU LEU A . n 
B 2 45  GLY 45  36  36  GLY GLY A . n 
B 2 46  GLY 46  37  37  GLY GLY A . n 
B 2 47  LEU 47  38  38  LEU LEU A . n 
B 2 48  PHE 48  39  39  PHE PHE A . n 
B 2 49  SER 49  40  40  SER SER A . n 
B 2 50  LEU 50  41  41  LEU LEU A . n 
B 2 51  HIS 51  42  42  HIS HIS A . n 
B 2 52  ALA 52  43  ?   ?   ?   A . n 
B 2 53  ASN 53  44  ?   ?   ?   A . n 
B 2 54  MET 54  45  ?   ?   ?   A . n 
B 2 55  LYS 55  46  ?   ?   ?   A . n 
B 2 56  GLY 56  47  ?   ?   ?   A . n 
B 2 57  ILE 57  48  ?   ?   ?   A . n 
B 2 58  VAL 58  49  ?   ?   ?   A . n 
B 2 59  HIS 59  50  ?   ?   ?   A . n 
B 2 60  LEU 60  51  ?   ?   ?   A . n 
B 2 61  ASN 61  52  ?   ?   ?   A . n 
B 2 62  PHE 62  53  53  PHE PHE A . n 
B 2 63  LEU 63  54  54  LEU LEU A . n 
B 2 64  GLN 64  55  55  GLN GLN A . n 
B 2 65  VAL 65  56  56  VAL VAL A . n 
B 2 66  PRO 66  57  57  PRO PRO A . n 
B 2 67  MET 67  58  58  MET MET A . n 
B 2 68  CYS 68  59  59  CYS CYS A . n 
B 2 69  LYS 69  60  60  LYS LYS A . n 
B 2 70  GLU 70  61  61  GLU GLU A . n 
B 2 71  TYR 71  62  62  TYR TYR A . n 
B 2 72  GLU 72  63  63  GLU GLU A . n 
B 2 73  VAL 73  64  64  VAL VAL A . n 
B 2 74  LYS 74  65  65  LYS LYS A . n 
B 2 75  VAL 75  66  66  VAL VAL A . n 
B 2 76  ILE 76  67  67  ILE ILE A . n 
B 2 77  GLY 77  68  68  GLY GLY A . n 
B 2 78  TYR 78  69  69  TYR TYR A . n 
B 2 79  ASN 79  70  70  ASN ASN A . n 
B 2 80  LEU 80  71  71  LEU LEU A . n 
B 2 81  MET 81  72  72  MET MET A . n 
B 2 82  GLN 82  73  73  GLN GLN A . n 
B 2 83  ALA 83  74  74  ALA ALA A . n 
B 2 84  MET 84  75  75  MET MET A . n 
B 2 85  ARG 85  76  76  ARG ARG A . n 
B 2 86  PHE 86  77  77  PHE PHE A . n 
B 2 87  ALA 87  78  78  ALA ALA A . n 
B 2 88  VAL 88  79  79  VAL VAL A . n 
B 2 89  GLU 89  80  80  GLU GLU A . n 
B 2 90  GLU 90  81  81  GLU GLU A . n 
B 2 91  ILE 91  82  82  ILE ILE A . n 
B 2 92  ASN 92  83  83  ASN ASN A . n 
B 2 93  ASN 93  84  84  ASN ASN A . n 
B 2 94  ASP 94  85  85  ASP ASP A . n 
B 2 95  SER 95  86  86  SER SER A . n 
B 2 96  SER 96  87  87  SER SER A . n 
B 2 97  LEU 97  88  88  LEU LEU A . n 
B 2 98  LEU 98  89  89  LEU LEU A . n 
B 2 99  PRO 99  90  90  PRO PRO A . n 
B 2 100 GLY 100 91  91  GLY GLY A . n 
B 2 101 VAL 101 92  92  VAL VAL A . n 
B 2 102 LEU 102 93  93  LEU LEU A . n 
B 2 103 LEU 103 94  94  LEU LEU A . n 
B 2 104 GLY 104 95  95  GLY GLY A . n 
B 2 105 TYR 105 96  96  TYR TYR A . n 
B 2 106 GLU 106 97  97  GLU GLU A . n 
B 2 107 ILE 107 98  98  ILE ILE A . n 
B 2 108 VAL 108 99  99  VAL VAL A . n 
B 2 109 ASP 109 100 100 ASP ASP A . n 
B 2 110 VAL 110 101 101 VAL VAL A . n 
B 2 111 CYS 111 102 102 CYS CYS A . n 
B 2 112 TYR 112 103 103 TYR TYR A . n 
B 2 113 ILE 113 104 104 ILE ILE A . n 
B 2 114 SER 114 105 105 SER SER A . n 
B 2 115 ASN 115 106 106 ASN ASN A . n 
B 2 116 ASN 116 107 107 ASN ASN A . n 
B 2 117 VAL 117 108 108 VAL VAL A . n 
B 2 118 GLN 118 109 109 GLN GLN A . n 
B 2 119 PRO 119 110 110 PRO PRO A . n 
B 2 120 VAL 120 111 111 VAL VAL A . n 
B 2 121 LEU 121 112 112 LEU LEU A . n 
B 2 122 TYR 122 113 113 TYR TYR A . n 
B 2 123 PHE 123 114 114 PHE PHE A . n 
B 2 124 LEU 124 115 115 LEU LEU A . n 
B 2 125 ALA 125 116 116 ALA ALA A . n 
B 2 126 HIS 126 117 117 HIS HIS A . n 
B 2 127 GLU 127 118 118 GLU GLU A . n 
B 2 128 ASP 128 119 119 ASP ASP A . n 
B 2 129 ASN 129 120 120 ASN ASN A . n 
B 2 130 LEU 130 121 121 LEU LEU A . n 
B 2 131 LEU 131 122 122 LEU LEU A . n 
B 2 132 PRO 132 123 123 PRO PRO A . n 
B 2 133 ILE 133 124 124 ILE ILE A . n 
B 2 134 GLN 134 125 125 GLN GLN A . n 
B 2 135 GLU 135 126 126 GLU GLU A . n 
B 2 136 ASP 136 127 127 ASP ASP A . n 
B 2 137 TYR 137 128 128 TYR TYR A . n 
B 2 138 SER 138 129 129 SER SER A . n 
B 2 139 ASN 139 130 130 ASN ASN A . n 
B 2 140 TYR 140 131 131 TYR TYR A . n 
B 2 141 ILE 141 132 132 ILE ILE A . n 
B 2 142 SER 142 133 133 SER SER A . n 
B 2 143 ARG 143 134 134 ARG ARG A . n 
B 2 144 VAL 144 135 135 VAL VAL A . n 
B 2 145 VAL 145 136 136 VAL VAL A . n 
B 2 146 ALA 146 137 137 ALA ALA A . n 
B 2 147 VAL 147 138 138 VAL VAL A . n 
B 2 148 ILE 148 139 139 ILE ILE A . n 
B 2 149 GLY 149 140 140 GLY GLY A . n 
B 2 150 PRO 150 141 141 PRO PRO A . n 
B 2 151 ASP 151 142 142 ASP ASP A . n 
B 2 152 ASN 152 143 143 ASN ASN A . n 
B 2 153 SER 153 144 144 SER SER A . n 
B 2 154 GLU 154 145 145 GLU GLU A . n 
B 2 155 SER 155 146 146 SER SER A . n 
B 2 156 VAL 156 147 147 VAL VAL A . n 
B 2 157 MET 157 148 148 MET MET A . n 
B 2 158 THR 158 149 149 THR THR A . n 
B 2 159 VAL 159 150 150 VAL VAL A . n 
B 2 160 ALA 160 151 151 ALA ALA A . n 
B 2 161 ASN 161 152 152 ASN ASN A . n 
B 2 162 PHE 162 153 153 PHE PHE A . n 
B 2 163 LEU 163 154 154 LEU LEU A . n 
B 2 164 SER 164 155 155 SER SER A . n 
B 2 165 LEU 165 156 156 LEU LEU A . n 
B 2 166 PHE 166 157 157 PHE PHE A . n 
B 2 167 LEU 167 158 158 LEU LEU A . n 
B 2 168 LEU 168 159 159 LEU LEU A . n 
B 2 169 PRO 169 160 160 PRO PRO A . n 
B 2 170 GLN 170 161 161 GLN GLN A . n 
B 2 171 ILE 171 162 162 ILE ILE A . n 
B 2 172 THR 172 163 163 THR THR A . n 
B 2 173 TYR 173 164 164 TYR TYR A . n 
B 2 174 SER 174 165 165 SER SER A . n 
B 2 175 ALA 175 166 166 ALA ALA A . n 
B 2 176 ILE 176 167 167 ILE ILE A . n 
B 2 177 SER 177 168 168 SER SER A . n 
B 2 178 ASP 178 169 169 ASP ASP A . n 
B 2 179 GLU 179 170 170 GLU GLU A . n 
B 2 180 LEU 180 171 171 LEU LEU A . n 
B 2 181 ARG 181 172 172 ARG ARG A . n 
B 2 182 ASP 182 173 173 ASP ASP A . n 
B 2 183 LYS 183 174 174 LYS LYS A . n 
B 2 184 VAL 184 175 175 VAL VAL A . n 
B 2 185 ARG 185 176 176 ARG ARG A . n 
B 2 186 PHE 186 177 177 PHE PHE A . n 
B 2 187 PRO 187 178 178 PRO PRO A . n 
B 2 188 ALA 188 179 179 ALA ALA A . n 
B 2 189 LEU 189 180 180 LEU LEU A . n 
B 2 190 LEU 190 181 181 LEU LEU A . n 
B 2 191 ARG 191 182 182 ARG ARG A . n 
B 2 192 THR 192 183 183 THR THR A . n 
B 2 193 THR 193 184 184 THR THR A . n 
B 2 194 PRO 194 185 185 PRO PRO A . n 
B 2 195 SER 195 186 186 SER SER A . n 
B 2 196 ALA 196 187 187 ALA ALA A . n 
B 2 197 ASP 197 188 188 ASP ASP A . n 
B 2 198 HIS 198 189 189 HIS HIS A . n 
B 2 199 HIS 199 190 190 HIS HIS A . n 
B 2 200 ILE 200 191 191 ILE ILE A . n 
B 2 201 GLU 201 192 192 GLU GLU A . n 
B 2 202 ALA 202 193 193 ALA ALA A . n 
B 2 203 MET 203 194 194 MET MET A . n 
B 2 204 VAL 204 195 195 VAL VAL A . n 
B 2 205 GLN 205 196 196 GLN GLN A . n 
B 2 206 LEU 206 197 197 LEU LEU A . n 
B 2 207 MET 207 198 198 MET MET A . n 
B 2 208 LEU 208 199 199 LEU LEU A . n 
B 2 209 HIS 209 200 200 HIS HIS A . n 
B 2 210 PHE 210 201 201 PHE PHE A . n 
B 2 211 ARG 211 202 202 ARG ARG A . n 
B 2 212 TRP 212 203 203 TRP TRP A . n 
B 2 213 ASN 213 204 204 ASN ASN A . n 
B 2 214 TRP 214 205 205 TRP TRP A . n 
B 2 215 ILE 215 206 206 ILE ILE A . n 
B 2 216 ILE 216 207 207 ILE ILE A . n 
B 2 217 VAL 217 208 208 VAL VAL A . n 
B 2 218 LEU 218 209 209 LEU LEU A . n 
B 2 219 VAL 219 210 210 VAL VAL A . n 
B 2 220 SER 220 211 211 SER SER A . n 
B 2 221 SER 221 212 212 SER SER A . n 
B 2 222 ASP 222 213 213 ASP ASP A . n 
B 2 223 THR 223 214 214 THR THR A . n 
B 2 224 TYR 224 215 215 TYR TYR A . n 
B 2 225 GLY 225 216 216 GLY GLY A . n 
B 2 226 ARG 226 217 217 ARG ARG A . n 
B 2 227 ASP 227 218 218 ASP ASP A . n 
B 2 228 ASN 228 219 219 ASN ASN A . n 
B 2 229 GLY 229 220 220 GLY GLY A . n 
B 2 230 GLN 230 221 221 GLN GLN A . n 
B 2 231 LEU 231 222 222 LEU LEU A . n 
B 2 232 LEU 232 223 223 LEU LEU A . n 
B 2 233 GLY 233 224 224 GLY GLY A . n 
B 2 234 GLU 234 225 225 GLU GLU A . n 
B 2 235 ARG 235 226 226 ARG ARG A . n 
B 2 236 VAL 236 227 227 VAL VAL A . n 
B 2 237 ALA 237 228 228 ALA ALA A . n 
B 2 238 ARG 238 229 229 ARG ARG A . n 
B 2 239 ARG 239 230 230 ARG ARG A . n 
B 2 240 ASP 240 231 231 ASP ASP A . n 
B 2 241 ILE 241 232 232 ILE ILE A . n 
B 2 242 CYS 242 233 233 CYS CYS A . n 
B 2 243 ILE 243 234 234 ILE ILE A . n 
B 2 244 ALA 244 235 235 ALA ALA A . n 
B 2 245 PHE 245 236 236 PHE PHE A . n 
B 2 246 GLN 246 237 237 GLN GLN A . n 
B 2 247 GLU 247 238 238 GLU GLU A . n 
B 2 248 THR 248 239 239 THR THR A . n 
B 2 249 LEU 249 240 240 LEU LEU A . n 
B 2 250 PRO 250 241 241 PRO PRO A . n 
B 2 251 THR 251 242 242 THR THR A . n 
B 2 252 LEU 252 243 243 LEU LEU A . n 
B 2 253 GLN 253 244 244 GLN GLN A . n 
B 2 254 PRO 254 245 245 PRO PRO A . n 
B 2 255 ASN 255 246 246 ASN ASN A . n 
B 2 256 GLN 256 247 247 GLN GLN A . n 
B 2 257 ASN 257 248 248 ASN ASN A . n 
B 2 258 MET 258 249 249 MET MET A . n 
B 2 259 THR 259 250 250 THR THR A . n 
B 2 260 SER 260 251 251 SER SER A . n 
B 2 261 GLU 261 252 252 GLU GLU A . n 
B 2 262 GLU 262 253 253 GLU GLU A . n 
B 2 263 ARG 263 254 254 ARG ARG A . n 
B 2 264 GLN 264 255 255 GLN GLN A . n 
B 2 265 ARG 265 256 256 ARG ARG A . n 
B 2 266 LEU 266 257 257 LEU LEU A . n 
B 2 267 VAL 267 258 258 VAL VAL A . n 
B 2 268 THR 268 259 259 THR THR A . n 
B 2 269 ILE 269 260 260 ILE ILE A . n 
B 2 270 VAL 270 261 261 VAL VAL A . n 
B 2 271 ASP 271 262 262 ASP ASP A . n 
B 2 272 LYS 272 263 263 LYS LYS A . n 
B 2 273 LEU 273 264 264 LEU LEU A . n 
B 2 274 GLN 274 265 265 GLN GLN A . n 
B 2 275 GLN 275 266 266 GLN GLN A . n 
B 2 276 SER 276 267 267 SER SER A . n 
B 2 277 THR 277 268 268 THR THR A . n 
B 2 278 ALA 278 269 269 ALA ALA A . n 
B 2 279 ARG 279 270 270 ARG ARG A . n 
B 2 280 VAL 280 271 271 VAL VAL A . n 
B 2 281 VAL 281 272 272 VAL VAL A . n 
B 2 282 VAL 282 273 273 VAL VAL A . n 
B 2 283 VAL 283 274 274 VAL VAL A . n 
B 2 284 PHE 284 275 275 PHE PHE A . n 
B 2 285 SER 285 276 276 SER SER A . n 
B 2 286 PRO 286 277 277 PRO PRO A . n 
B 2 287 ASP 287 278 278 ASP ASP A . n 
B 2 288 LEU 288 279 279 LEU LEU A . n 
B 2 289 THR 289 280 280 THR THR A . n 
B 2 290 LEU 290 281 281 LEU LEU A . n 
B 2 291 TYR 291 282 282 TYR TYR A . n 
B 2 292 HIS 292 283 283 HIS HIS A . n 
B 2 293 PHE 293 284 284 PHE PHE A . n 
B 2 294 PHE 294 285 285 PHE PHE A . n 
B 2 295 ASN 295 286 286 ASN ASN A . n 
B 2 296 GLU 296 287 287 GLU GLU A . n 
B 2 297 VAL 297 288 288 VAL VAL A . n 
B 2 298 LEU 298 289 289 LEU LEU A . n 
B 2 299 ARG 299 290 290 ARG ARG A . n 
B 2 300 GLN 300 291 291 GLN GLN A . n 
B 2 301 ASN 301 292 292 ASN ASN A . n 
B 2 302 PHE 302 293 293 PHE PHE A . n 
B 2 303 THR 303 294 294 THR THR A . n 
B 2 304 GLY 304 295 295 GLY GLY A . n 
B 2 305 ALA 305 296 296 ALA ALA A . n 
B 2 306 VAL 306 297 297 VAL VAL A . n 
B 2 307 TRP 307 298 298 TRP TRP A . n 
B 2 308 ILE 308 299 299 ILE ILE A . n 
B 2 309 ALA 309 300 300 ALA ALA A . n 
B 2 310 SER 310 301 301 SER SER A . n 
B 2 311 GLU 311 302 302 GLU GLU A . n 
B 2 312 SER 312 303 303 SER SER A . n 
B 2 313 TRP 313 304 304 TRP TRP A . n 
B 2 314 ALA 314 305 305 ALA ALA A . n 
B 2 315 ILE 315 306 306 ILE ILE A . n 
B 2 316 ASP 316 307 307 ASP ASP A . n 
B 2 317 PRO 317 308 308 PRO PRO A . n 
B 2 318 VAL 318 309 309 VAL VAL A . n 
B 2 319 LEU 319 310 310 LEU LEU A . n 
B 2 320 HIS 320 311 311 HIS HIS A . n 
B 2 321 ASN 321 312 312 ASN ASN A . n 
B 2 322 LEU 322 313 313 LEU LEU A . n 
B 2 323 THR 323 314 314 THR THR A . n 
B 2 324 GLU 324 315 315 GLU GLU A . n 
B 2 325 LEU 325 316 316 LEU LEU A . n 
B 2 326 ARG 326 317 317 ARG ARG A . n 
B 2 327 HIS 327 318 318 HIS HIS A . n 
B 2 328 LEU 328 319 319 LEU LEU A . n 
B 2 329 GLY 329 320 320 GLY GLY A . n 
B 2 330 THR 330 321 321 THR THR A . n 
B 2 331 PHE 331 322 322 PHE PHE A . n 
B 2 332 LEU 332 323 323 LEU LEU A . n 
B 2 333 GLY 333 324 324 GLY GLY A . n 
B 2 334 ILE 334 325 325 ILE ILE A . n 
B 2 335 THR 335 326 326 THR THR A . n 
B 2 336 ILE 336 327 327 ILE ILE A . n 
B 2 337 GLN 337 328 328 GLN GLN A . n 
B 2 338 SER 338 329 329 SER SER A . n 
B 2 339 VAL 339 330 330 VAL VAL A . n 
B 2 340 PRO 340 331 331 PRO PRO A . n 
B 2 341 ILE 341 332 332 ILE ILE A . n 
B 2 342 PRO 342 333 333 PRO PRO A . n 
B 2 343 GLY 343 334 334 GLY GLY A . n 
B 2 344 PHE 344 335 335 PHE PHE A . n 
B 2 345 SER 345 336 336 SER SER A . n 
B 2 346 GLU 346 337 337 GLU GLU A . n 
B 2 347 PHE 347 338 338 PHE PHE A . n 
B 2 348 ARG 348 339 339 ARG ARG A . n 
B 2 349 GLU 349 340 340 GLU GLU A . n 
B 2 350 TRP 350 341 341 TRP TRP A . n 
B 2 351 GLY 351 342 342 GLY GLY A . n 
B 2 352 PRO 352 343 ?   ?   ?   A . n 
B 2 353 GLN 353 344 ?   ?   ?   A . n 
B 2 354 ALA 354 345 ?   ?   ?   A . n 
B 2 355 GLY 355 346 ?   ?   ?   A . n 
B 2 356 PRO 356 347 ?   ?   ?   A . n 
B 2 357 PRO 357 348 ?   ?   ?   A . n 
B 2 358 PRO 358 349 ?   ?   ?   A . n 
B 2 359 LEU 359 350 ?   ?   ?   A . n 
B 2 360 SER 360 351 ?   ?   ?   A . n 
B 2 361 ARG 361 352 ?   ?   ?   A . n 
B 2 362 THR 362 353 ?   ?   ?   A . n 
B 2 363 SER 363 354 ?   ?   ?   A . n 
B 2 364 GLN 364 355 ?   ?   ?   A . n 
B 2 365 SER 365 356 ?   ?   ?   A . n 
B 2 366 TYR 366 357 ?   ?   ?   A . n 
B 2 367 THR 367 358 358 THR THR A . n 
B 2 368 CYS 368 359 359 CYS CYS A . n 
B 2 369 ASN 369 360 360 ASN ASN A . n 
B 2 370 GLN 370 361 361 GLN GLN A . n 
B 2 371 GLU 371 362 362 GLU GLU A . n 
B 2 372 CYS 372 363 363 CYS CYS A . n 
B 2 373 ASP 373 364 364 ASP ASP A . n 
B 2 374 ASN 374 365 365 ASN ASN A . n 
B 2 375 CYS 375 366 366 CYS CYS A . n 
B 2 376 LEU 376 367 367 LEU LEU A . n 
B 2 377 ASN 377 368 368 ASN ASN A . n 
B 2 378 ALA 378 369 369 ALA ALA A . n 
B 2 379 THR 379 370 370 THR THR A . n 
B 2 380 LEU 380 371 371 LEU LEU A . n 
B 2 381 SER 381 372 372 SER SER A . n 
B 2 382 PHE 382 373 373 PHE PHE A . n 
B 2 383 ASN 383 374 374 ASN ASN A . n 
B 2 384 THR 384 375 375 THR THR A . n 
B 2 385 ILE 385 376 376 ILE ILE A . n 
B 2 386 LEU 386 377 377 LEU LEU A . n 
B 2 387 ARG 387 378 378 ARG ARG A . n 
B 2 388 LEU 388 379 379 LEU LEU A . n 
B 2 389 SER 389 380 380 SER SER A . n 
B 2 390 GLY 390 381 381 GLY GLY A . n 
B 2 391 GLU 391 382 382 GLU GLU A . n 
B 2 392 ARG 392 383 383 ARG ARG A . n 
B 2 393 VAL 393 384 384 VAL VAL A . n 
B 2 394 VAL 394 385 385 VAL VAL A . n 
B 2 395 TYR 395 386 386 TYR TYR A . n 
B 2 396 SER 396 387 387 SER SER A . n 
B 2 397 VAL 397 388 388 VAL VAL A . n 
B 2 398 TYR 398 389 389 TYR TYR A . n 
B 2 399 SER 399 390 390 SER SER A . n 
B 2 400 ALA 400 391 391 ALA ALA A . n 
B 2 401 VAL 401 392 392 VAL VAL A . n 
B 2 402 TYR 402 393 393 TYR TYR A . n 
B 2 403 ALA 403 394 394 ALA ALA A . n 
B 2 404 VAL 404 395 395 VAL VAL A . n 
B 2 405 ALA 405 396 396 ALA ALA A . n 
B 2 406 HIS 406 397 397 HIS HIS A . n 
B 2 407 ALA 407 398 398 ALA ALA A . n 
B 2 408 LEU 408 399 399 LEU LEU A . n 
B 2 409 HIS 409 400 400 HIS HIS A . n 
B 2 410 SER 410 401 401 SER SER A . n 
B 2 411 LEU 411 402 402 LEU LEU A . n 
B 2 412 LEU 412 403 403 LEU LEU A . n 
B 2 413 GLY 413 404 404 GLY GLY A . n 
B 2 414 CYS 414 405 405 CYS CYS A . n 
B 2 415 ASP 415 406 406 ASP ASP A . n 
B 2 416 LYS 416 407 407 LYS LYS A . n 
B 2 417 SER 417 408 408 SER SER A . n 
B 2 418 THR 418 409 409 THR THR A . n 
B 2 419 CYS 419 410 410 CYS CYS A . n 
B 2 420 THR 420 411 411 THR THR A . n 
B 2 421 LYS 421 412 412 LYS LYS A . n 
B 2 422 ARG 422 413 413 ARG ARG A . n 
B 2 423 VAL 423 414 414 VAL VAL A . n 
B 2 424 VAL 424 415 415 VAL VAL A . n 
B 2 425 TYR 425 416 416 TYR TYR A . n 
B 2 426 PRO 426 417 417 PRO PRO A . n 
B 2 427 TRP 427 418 418 TRP TRP A . n 
B 2 428 GLN 428 419 419 GLN GLN A . n 
B 2 429 LEU 429 420 420 LEU LEU A . n 
B 2 430 LEU 430 421 421 LEU LEU A . n 
B 2 431 GLU 431 422 422 GLU GLU A . n 
B 2 432 GLU 432 423 423 GLU GLU A . n 
B 2 433 ILE 433 424 424 ILE ILE A . n 
B 2 434 TRP 434 425 425 TRP TRP A . n 
B 2 435 LYS 435 426 426 LYS LYS A . n 
B 2 436 VAL 436 427 427 VAL VAL A . n 
B 2 437 ASN 437 428 428 ASN ASN A . n 
B 2 438 PHE 438 429 429 PHE PHE A . n 
B 2 439 THR 439 430 430 THR THR A . n 
B 2 440 LEU 440 431 431 LEU LEU A . n 
B 2 441 LEU 441 432 432 LEU LEU A . n 
B 2 442 ASP 442 433 433 ASP ASP A . n 
B 2 443 HIS 443 434 434 HIS HIS A . n 
B 2 444 GLN 444 435 435 GLN GLN A . n 
B 2 445 ILE 445 436 436 ILE ILE A . n 
B 2 446 PHE 446 437 437 PHE PHE A . n 
B 2 447 PHE 447 438 438 PHE PHE A . n 
B 2 448 ASP 448 439 439 ASP ASP A . n 
B 2 449 PRO 449 440 440 PRO PRO A . n 
B 2 450 GLN 450 441 441 GLN GLN A . n 
B 2 451 GLY 451 442 442 GLY GLY A . n 
B 2 452 ASP 452 443 443 ASP ASP A . n 
B 2 453 VAL 453 444 444 VAL VAL A . n 
B 2 454 ALA 454 445 445 ALA ALA A . n 
B 2 455 LEU 455 446 446 LEU LEU A . n 
B 2 456 HIS 456 447 447 HIS HIS A . n 
B 2 457 LEU 457 448 448 LEU LEU A . n 
B 2 458 GLU 458 449 449 GLU GLU A . n 
B 2 459 ILE 459 450 450 ILE ILE A . n 
B 2 460 VAL 460 451 451 VAL VAL A . n 
B 2 461 GLN 461 452 452 GLN GLN A . n 
B 2 462 TRP 462 453 453 TRP TRP A . n 
B 2 463 GLN 463 454 454 GLN GLN A . n 
B 2 464 TRP 464 455 455 TRP TRP A . n 
B 2 465 ASP 465 456 456 ASP ASP A . n 
B 2 466 ARG 466 457 457 ARG ARG A . n 
B 2 467 SER 467 458 458 SER SER A . n 
B 2 468 GLN 468 459 459 GLN GLN A . n 
B 2 469 ASN 469 460 460 ASN ASN A . n 
B 2 470 PRO 470 461 461 PRO PRO A . n 
B 2 471 PHE 471 462 462 PHE PHE A . n 
B 2 472 GLN 472 463 463 GLN GLN A . n 
B 2 473 SER 473 464 464 SER SER A . n 
B 2 474 VAL 474 465 465 VAL VAL A . n 
B 2 475 ALA 475 466 466 ALA ALA A . n 
B 2 476 SER 476 467 467 SER SER A . n 
B 2 477 TYR 477 468 468 TYR TYR A . n 
B 2 478 TYR 478 469 469 TYR TYR A . n 
B 2 479 PRO 479 470 470 PRO PRO A . n 
B 2 480 LEU 480 471 471 LEU LEU A . n 
B 2 481 GLN 481 472 472 GLN GLN A . n 
B 2 482 ARG 482 473 473 ARG ARG A . n 
B 2 483 GLN 483 474 474 GLN GLN A . n 
B 2 484 LEU 484 475 475 LEU LEU A . n 
B 2 485 LYS 485 476 476 LYS LYS A . n 
B 2 486 ASN 486 477 477 ASN ASN A . n 
B 2 487 ILE 487 478 478 ILE ILE A . n 
B 2 488 GLN 488 479 479 GLN GLN A . n 
B 2 489 ASP 489 480 480 ASP ASP A . n 
B 2 490 ILE 490 481 481 ILE ILE A . n 
B 2 491 SER 491 482 482 SER SER A . n 
B 2 492 TRP 492 483 483 TRP TRP A . n 
B 2 493 HIS 493 484 484 HIS HIS A . n 
B 2 494 THR 494 485 485 THR THR A . n 
B 2 495 ILE 495 486 486 ILE ILE A . n 
B 2 496 ASN 496 487 487 ASN ASN A . n 
B 2 497 ASN 497 488 488 ASN ASN A . n 
B 2 498 THR 498 489 489 THR THR A . n 
B 2 499 ILE 499 490 490 ILE ILE A . n 
B 2 500 PRO 500 491 491 PRO PRO A . n 
B 2 501 MET 501 492 492 MET MET A . n 
B 2 502 SER 502 493 493 SER SER A . n 
B 2 503 MET 503 494 494 MET MET A . n 
B 2 504 CYS 504 495 495 CYS CYS A . n 
B 2 505 SER 505 496 496 SER SER A . n 
B 2 506 LYS 506 497 497 LYS LYS A . n 
B 2 507 ARG 507 498 ?   ?   ?   A . n 
B 2 508 CYS 508 499 ?   ?   ?   A . n 
B 2 509 GLN 509 500 ?   ?   ?   A . n 
B 2 510 SER 510 501 ?   ?   ?   A . n 
B 2 511 GLY 511 502 ?   ?   ?   A . n 
B 2 512 GLN 512 503 ?   ?   ?   A . n 
B 2 513 LYS 513 504 ?   ?   ?   A . n 
B 2 514 LYS 514 505 ?   ?   ?   A . n 
B 2 515 LYS 515 506 506 LYS LYS A . n 
B 2 516 PRO 516 507 507 PRO PRO A . n 
B 2 517 VAL 517 508 508 VAL VAL A . n 
B 2 518 GLY 518 509 509 GLY GLY A . n 
B 2 519 ILE 519 510 510 ILE ILE A . n 
B 2 520 HIS 520 511 511 HIS HIS A . n 
B 2 521 VAL 521 512 512 VAL VAL A . n 
B 2 522 CYS 522 513 513 CYS CYS A . n 
B 2 523 CYS 523 514 514 CYS CYS A . n 
B 2 524 PHE 524 515 515 PHE PHE A . n 
# 
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 NAG 1 601 522 NAG NAG B . 
D 3 NAG 1 602 523 NAG NAG B . 
E 3 NAG 1 603 524 NAG NAG B . 
F 3 NAG 1 604 525 NAG NAG B . 
G 3 NAG 1 605 526 NAG NAG B . 
H 3 NAG 1 606 527 NAG NAG B . 
I 3 NAG 1 607 528 NAG NAG B . 
J 3 NAG 1 608 529 NAG NAG B . 
K 3 NAG 1 601 519 NAG NAG A . 
L 3 NAG 1 602 520 NAG NAG A . 
M 3 NAG 1 603 521 NAG NAG A . 
N 3 NAG 1 604 522 NAG NAG A . 
O 3 NAG 1 605 523 NAG NAG A . 
P 3 NAG 1 606 524 NAG NAG A . 
Q 3 NAG 1 607 525 NAG NAG 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                     9NOU 
_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                         9NOU 
_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                   9NOU 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9NOU 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.80 
_refine.ls_d_res_low                             ? 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
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' ? 0.004 ? 7804  ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.571 ? 10609 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 6.601 ? 1321  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.047 ? 1232  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.004 ? 1338  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9NOU 
_struct.title                        'Human sweet taste receptor (TAS1R2 + TAS1R3) VFT domains from the combined datasets' 
_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        9NOU 
_struct_keywords.text            'Sweet, taste, receptor, GPCR, TAS1R2, TAS1R3, T1R2, T1R3, 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 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 3 ? 
M N N 3 ? 
N N N 3 ? 
O N N 3 ? 
P N N 3 ? 
Q N N 3 ? 
# 
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 TS1R3_HUMAN Q7RTX0 ? 1 
;APLCLSQQLRMKGDYVLGGLFPLGEAEEAGLRSRTRPSSPVCTRFSSNGLLWALAMKMAVEEINNKSDLLPGLRLGYDLF
DTCSEPVVAMKPSLMFLAKAGSRDIAAYCNYTQYQPRVLAVIGPHSSELAMVTGKFFSFFLMPQVSYGASMELLSARETF
PSFFRTVPSDRVQLTAAAELLQEFGWNWVAALGSDDEYGRQGLSIFSALAAARGICIAHEGLVPLPRADDSRLGKVQDVL
HQVNQSSVQVVLLFASVHAAHALFNYSISSRLSPKVWVASEAWLTSDLVMGLPGMAQMGTVLGFLQRGAQLHEFPQYVKT
HLALATDPAFCSALGEREQGLEEDVVGQRCPQCDCITLQNVSAGLNHHQTFSVYAAVYSVAQALHNTLQCNASGCPAQDP
VKPWQLLENMYNLTFHVGGLPLRFDSSGNVDMEYDLKLWVWQGSVPRLHDVGRFNGSLRTERLKIRWHTSDNQKPVSRCS
RQCQEGQVRRVKGFHSCCYDC
;
21 
2 UNP TS1R2_HUMAN Q8TE23 ? 2 
;AEPAENSDFYLPGDYLLGGLFSLHANMKGIVHLNFLQVPMCKEYEVKVIGYNLMQAMRFAVEEINNDSSLLPGVLLGYEI
VDVCYISNNVQPVLYFLAHEDNLLPIQEDYSNYISRVVAVIGPDNSESVMTVANFLSLFLLPQITYSAISDELRDKVRFP
ALLRTTPSADHHIEAMVQLMLHFRWNWIIVLVSSDTYGRDNGQLLGERVARRDICIAFQETLPTLQPNQNMTSEERQRLV
TIVDKLQQSTARVVVVFSPDLTLYHFFNEVLRQNFTGAVWIASESWAIDPVLHNLTELRHLGTFLGITIQSVPIPGFSEF
REWGPQAGPPPLSRTSQSYTCNQECDNCLNATLSFNTILRLSGERVVYSVYSAVYAVAHALHSLLGCDKSTCTKRVVYPW
QLLEEIWKVNFTLLDHQIFFDPQGDVALHLEIVQWQWDRSQNPFQSVASYYPLQRQLKNIQDISWHTINNTIPMSMCSKR
CQSGQKKKPVGIHVCCF
;
19 
# 
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 9NOU B 28 ? 528 ? Q7RTX0 21 ? 521 ? 21 521 
2 2 9NOU A 28 ? 524 ? Q8TE23 19 ? 515 ? 19 515 
# 
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 9NOU MET B 1  ? UNP Q7RTX0 ? ? 'expression tag' -6 1  
1 9NOU LYS B 2  ? UNP Q7RTX0 ? ? 'expression tag' -5 2  
1 9NOU THR B 3  ? UNP Q7RTX0 ? ? 'expression tag' -4 3  
1 9NOU ILE B 4  ? UNP Q7RTX0 ? ? 'expression tag' -3 4  
1 9NOU ILE B 5  ? UNP Q7RTX0 ? ? 'expression tag' -2 5  
1 9NOU ALA B 6  ? UNP Q7RTX0 ? ? 'expression tag' -1 6  
1 9NOU LEU B 7  ? UNP Q7RTX0 ? ? 'expression tag' 0  7  
1 9NOU SER B 8  ? UNP Q7RTX0 ? ? 'expression tag' 1  8  
1 9NOU TYR B 9  ? UNP Q7RTX0 ? ? 'expression tag' 2  9  
1 9NOU ILE B 10 ? UNP Q7RTX0 ? ? 'expression tag' 3  10 
1 9NOU PHE B 11 ? UNP Q7RTX0 ? ? 'expression tag' 4  11 
1 9NOU CYS B 12 ? UNP Q7RTX0 ? ? 'expression tag' 5  12 
1 9NOU LEU B 13 ? UNP Q7RTX0 ? ? 'expression tag' 6  13 
1 9NOU VAL B 14 ? UNP Q7RTX0 ? ? 'expression tag' 7  14 
1 9NOU PHE B 15 ? UNP Q7RTX0 ? ? 'expression tag' 8  15 
1 9NOU ALA B 16 ? UNP Q7RTX0 ? ? 'expression tag' 9  16 
1 9NOU ASP B 17 ? UNP Q7RTX0 ? ? 'expression tag' 10 17 
1 9NOU TYR B 18 ? UNP Q7RTX0 ? ? 'expression tag' 11 18 
1 9NOU LYS B 19 ? UNP Q7RTX0 ? ? 'expression tag' 12 19 
1 9NOU ASP B 20 ? UNP Q7RTX0 ? ? 'expression tag' 13 20 
1 9NOU ASP B 21 ? UNP Q7RTX0 ? ? 'expression tag' 14 21 
1 9NOU ASP B 22 ? UNP Q7RTX0 ? ? 'expression tag' 15 22 
1 9NOU ASP B 23 ? UNP Q7RTX0 ? ? 'expression tag' 16 23 
1 9NOU LYS B 24 ? UNP Q7RTX0 ? ? 'expression tag' 17 24 
1 9NOU ALA B 25 ? UNP Q7RTX0 ? ? 'expression tag' 18 25 
1 9NOU ALA B 26 ? UNP Q7RTX0 ? ? 'expression tag' 19 26 
1 9NOU ALA B 27 ? UNP Q7RTX0 ? ? 'expression tag' 20 27 
2 9NOU MET A 1  ? UNP Q8TE23 ? ? 'expression tag' -8 28 
2 9NOU LYS A 2  ? UNP Q8TE23 ? ? 'expression tag' -7 29 
2 9NOU THR A 3  ? UNP Q8TE23 ? ? 'expression tag' -6 30 
2 9NOU ILE A 4  ? UNP Q8TE23 ? ? 'expression tag' -5 31 
2 9NOU ILE A 5  ? UNP Q8TE23 ? ? 'expression tag' -4 32 
2 9NOU ALA A 6  ? UNP Q8TE23 ? ? 'expression tag' -3 33 
2 9NOU LEU A 7  ? UNP Q8TE23 ? ? 'expression tag' -2 34 
2 9NOU SER A 8  ? UNP Q8TE23 ? ? 'expression tag' -1 35 
2 9NOU TYR A 9  ? UNP Q8TE23 ? ? 'expression tag' 0  36 
2 9NOU ILE A 10 ? UNP Q8TE23 ? ? 'expression tag' 1  37 
2 9NOU PHE A 11 ? UNP Q8TE23 ? ? 'expression tag' 2  38 
2 9NOU CYS A 12 ? UNP Q8TE23 ? ? 'expression tag' 3  39 
2 9NOU LEU A 13 ? UNP Q8TE23 ? ? 'expression tag' 4  40 
2 9NOU VAL A 14 ? UNP Q8TE23 ? ? 'expression tag' 5  41 
2 9NOU PHE A 15 ? UNP Q8TE23 ? ? 'expression tag' 6  42 
2 9NOU ALA A 16 ? UNP Q8TE23 ? ? 'expression tag' 7  43 
2 9NOU TYR A 17 ? UNP Q8TE23 ? ? 'expression tag' 8  44 
2 9NOU PRO A 18 ? UNP Q8TE23 ? ? 'expression tag' 9  45 
2 9NOU TYR A 19 ? UNP Q8TE23 ? ? 'expression tag' 10 46 
2 9NOU ASP A 20 ? UNP Q8TE23 ? ? 'expression tag' 11 47 
2 9NOU VAL A 21 ? UNP Q8TE23 ? ? 'expression tag' 12 48 
2 9NOU PRO A 22 ? UNP Q8TE23 ? ? 'expression tag' 13 49 
2 9NOU ASP A 23 ? UNP Q8TE23 ? ? 'expression tag' 14 50 
2 9NOU TYR A 24 ? UNP Q8TE23 ? ? 'expression tag' 15 51 
2 9NOU ALA A 25 ? UNP Q8TE23 ? ? 'expression tag' 16 52 
2 9NOU ALA A 26 ? UNP Q8TE23 ? ? 'expression tag' 17 53 
2 9NOU ALA A 27 ? UNP Q8TE23 ? ? 'expression tag' 18 54 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_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,E,F,G,H,I,J,K,L,M,N,O,P,Q 
# 
_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   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
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 LEU A 32  ? GLN A 35  ? LEU B 25  GLN B 28  5 ? 4  
HELX_P HELX_P2  AA2 SER A 73  ? LYS A 93  ? SER B 66  LYS B 86  1 ? 21 
HELX_P HELX_P3  AA3 GLU A 112 ? LEU A 124 ? GLU B 105 LEU B 117 1 ? 13 
HELX_P HELX_P4  AA4 ASN A 137 ? TYR A 141 ? ASN B 130 TYR B 134 5 ? 5  
HELX_P HELX_P5  AA5 SER A 153 ? LEU A 168 ? SER B 146 LEU B 161 1 ? 16 
HELX_P HELX_P6  AA6 MET A 178 ? ALA A 183 ? MET B 171 ALA B 176 5 ? 6  
HELX_P HELX_P7  AA7 SER A 196 ? GLY A 212 ? SER B 189 GLY B 205 1 ? 17 
HELX_P HELX_P8  AA8 ASP A 223 ? GLY A 241 ? ASP B 216 GLY B 234 1 ? 19 
HELX_P HELX_P9  AA9 VAL A 263 ? SER A 273 ? VAL B 256 SER B 266 1 ? 11 
HELX_P HELX_P10 AB1 SER A 283 ? SER A 297 ? SER B 276 SER B 290 1 ? 15 
HELX_P HELX_P11 AB2 SER A 313 ? GLY A 318 ? SER B 306 GLY B 311 1 ? 6  
HELX_P HELX_P12 AB3 GLY A 321 ? MET A 325 ? GLY B 314 MET B 318 5 ? 5  
HELX_P HELX_P13 AB4 GLU A 340 ? ALA A 352 ? GLU B 333 ALA B 345 1 ? 13 
HELX_P HELX_P14 AB5 ASP A 354 ? LEU A 361 ? ASP B 347 LEU B 354 1 ? 8  
HELX_P HELX_P15 AB6 CYS A 377 ? ASP A 381 ? CYS B 370 ASP B 374 5 ? 5  
HELX_P HELX_P16 AB7 THR A 384 ? LEU A 392 ? THR B 377 LEU B 385 5 ? 9  
HELX_P HELX_P17 AB8 HIS A 395 ? LEU A 415 ? HIS B 388 LEU B 408 1 ? 21 
HELX_P HELX_P18 AB9 LYS A 429 ? GLN A 432 ? LYS B 422 GLN B 425 5 ? 4  
HELX_P HELX_P19 AC1 LEU A 433 ? TYR A 438 ? LEU B 426 TYR B 431 1 ? 6  
HELX_P HELX_P20 AC2 ARG A 489 ? ILE A 492 ? ARG B 482 ILE B 485 5 ? 4  
HELX_P HELX_P21 AC3 MET B 67  ? TYR B 71  ? MET A 58  TYR A 62  5 ? 5  
HELX_P HELX_P22 AC4 LYS B 74  ? ASP B 94  ? LYS A 65  ASP A 85  1 ? 21 
HELX_P HELX_P23 AC5 VAL B 117 ? ALA B 125 ? VAL A 108 ALA A 116 1 ? 9  
HELX_P HELX_P24 AC6 ASN B 152 ? SER B 164 ? ASN A 143 SER A 155 1 ? 13 
HELX_P HELX_P25 AC7 SER B 177 ? ASP B 182 ? SER A 168 ASP A 173 5 ? 6  
HELX_P HELX_P26 AC8 SER B 195 ? PHE B 210 ? SER A 186 PHE A 201 1 ? 16 
HELX_P HELX_P27 AC9 ASP B 222 ? ALA B 237 ? ASP A 213 ALA A 228 1 ? 16 
HELX_P HELX_P28 AD1 THR B 259 ? SER B 276 ? THR A 250 SER A 267 1 ? 18 
HELX_P HELX_P29 AD2 LEU B 290 ? GLN B 300 ? LEU A 281 GLN A 291 1 ? 11 
HELX_P HELX_P30 AD3 ASP B 316 ? ASN B 321 ? ASP A 307 ASN A 312 1 ? 6  
HELX_P HELX_P31 AD4 LEU B 322 ? THR B 323 ? LEU A 313 THR A 314 5 ? 2  
HELX_P HELX_P32 AD5 GLU B 324 ? HIS B 327 ? GLU A 315 HIS A 318 5 ? 4  
HELX_P HELX_P33 AD6 GLY B 343 ? GLY B 351 ? GLY A 334 GLY A 342 1 ? 9  
HELX_P HELX_P34 AD7 ASN B 374 ? SER B 381 ? ASN A 365 SER A 372 1 ? 8  
HELX_P HELX_P35 AD8 PHE B 382 ? GLY B 390 ? PHE A 373 GLY A 381 1 ? 9  
HELX_P HELX_P36 AD9 VAL B 393 ? GLY B 413 ? VAL A 384 GLY A 404 1 ? 21 
HELX_P HELX_P37 AE1 TYR B 425 ? TRP B 434 ? TYR A 416 TRP A 425 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?   ? A CYS 31  SG  ? ? ? 1_555 A CYS 358 SG ? ? B CYS 24  B CYS 351 1_555 ? ? ? ? ? ? ? 2.032 ? ?               
disulf2  disulf ?   ? A CYS 69  SG  ? ? ? 1_555 A CYS 110 SG ? ? B CYS 62  B CYS 103 1_555 ? ? ? ? ? ? ? 2.032 ? ?               
disulf3  disulf ?   ? A CYS 136 SG  ? ? ? 1_555 B CYS 368 SG ? ? B CYS 129 A CYS 359 1_555 ? ? ? ? ? ? ? 2.027 ? ?               
disulf4  disulf ?   ? A CYS 243 SG  ? ? ? 1_555 A CYS 524 SG ? ? B CYS 236 B CYS 517 1_555 ? ? ? ? ? ? ? 2.024 ? ?               
disulf5  disulf ?   ? A CYS 377 SG  ? ? ? 1_555 A CYS 380 SG ? ? B CYS 370 B CYS 373 1_555 ? ? ? ? ? ? ? 2.031 ? ?               
disulf6  disulf ?   ? A CYS 417 SG  ? ? ? 1_555 A CYS 422 SG ? ? B CYS 410 B CYS 415 1_555 ? ? ? ? ? ? ? 2.032 ? ?               
disulf7  disulf ?   ? A CYS 506 SG  ? ? ? 1_555 A CYS 525 SG ? ? B CYS 499 B CYS 518 1_555 ? ? ? ? ? ? ? 2.025 ? ?               
disulf8  disulf ?   ? A CYS 510 SG  ? ? ? 1_555 A CYS 528 SG ? ? B CYS 503 B CYS 521 1_555 ? ? ? ? ? ? ? 2.029 ? ?               
disulf9  disulf ?   ? B CYS 68  SG  ? ? ? 1_555 B CYS 111 SG ? ? A CYS 59  A CYS 102 1_555 ? ? ? ? ? ? ? 2.029 ? ?               
disulf10 disulf ?   ? B CYS 242 SG  ? ? ? 1_555 B CYS 522 SG ? ? A CYS 233 A CYS 513 1_555 ? ? ? ? ? ? ? 2.034 ? ?               
disulf11 disulf ?   ? B CYS 372 SG  ? ? ? 1_555 B CYS 375 SG ? ? A CYS 363 A CYS 366 1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf12 disulf ?   ? B CYS 414 SG  ? ? ? 1_555 B CYS 419 SG ? ? A CYS 405 A CYS 410 1_555 ? ? ? ? ? ? ? 2.032 ? ?               
disulf13 disulf ?   ? B CYS 504 SG  ? ? ? 1_555 B CYS 523 SG ? ? A CYS 495 A CYS 514 1_555 ? ? ? ? ? ? ? 2.034 ? ?               
covale1  covale one ? A ASN 92  ND2 ? ? ? 1_555 G NAG .   C1 ? ? B ASN 85  B NAG 605 1_555 ? ? ? ? ? ? ? 1.440 ? N-Glycosylation 
covale2  covale one ? A ASN 137 ND2 ? ? ? 1_555 H NAG .   C1 ? ? B ASN 130 B NAG 606 1_555 ? ? ? ? ? ? ? 1.427 ? N-Glycosylation 
covale3  covale one ? A ASN 271 ND2 ? ? ? 1_555 E NAG .   C1 ? ? B ASN 264 B NAG 603 1_555 ? ? ? ? ? ? ? 1.440 ? N-Glycosylation 
covale4  covale one ? A ASN 292 ND2 ? ? ? 1_555 D NAG .   C1 ? ? B ASN 285 B NAG 602 1_555 ? ? ? ? ? ? ? 1.441 ? N-Glycosylation 
covale5  covale one ? A ASN 387 ND2 ? ? ? 1_555 I NAG .   C1 ? ? B ASN 380 B NAG 607 1_555 ? ? ? ? ? ? ? 1.443 ? N-Glycosylation 
covale6  covale one ? A ASN 418 ND2 ? ? ? 1_555 F NAG .   C1 ? ? B ASN 411 B NAG 604 1_555 ? ? ? ? ? ? ? 1.442 ? N-Glycosylation 
covale7  covale one ? A ASN 439 ND2 ? ? ? 1_555 J NAG .   C1 ? ? B ASN 432 B NAG 608 1_555 ? ? ? ? ? ? ? 1.444 ? N-Glycosylation 
covale8  covale one ? A ASN 482 ND2 ? ? ? 1_555 C NAG .   C1 ? ? B ASN 475 B NAG 601 1_555 ? ? ? ? ? ? ? 1.440 ? N-Glycosylation 
covale9  covale one ? B ASN 93  ND2 ? ? ? 1_555 L NAG .   C1 ? ? A ASN 84  A NAG 602 1_555 ? ? ? ? ? ? ? 1.456 ? N-Glycosylation 
covale10 covale one ? B ASN 257 ND2 ? ? ? 1_555 O NAG .   C1 ? ? A ASN 248 A NAG 605 1_555 ? ? ? ? ? ? ? 1.445 ? N-Glycosylation 
covale11 covale one ? B ASN 301 ND2 ? ? ? 1_555 P NAG .   C1 ? ? A ASN 292 A NAG 606 1_555 ? ? ? ? ? ? ? 1.443 ? N-Glycosylation 
covale12 covale one ? B ASN 321 ND2 ? ? ? 1_555 N NAG .   C1 ? ? A ASN 312 A NAG 604 1_555 ? ? ? ? ? ? ? 1.451 ? N-Glycosylation 
covale13 covale one ? B ASN 377 ND2 ? ? ? 1_555 Q NAG .   C1 ? ? A ASN 368 A NAG 607 1_555 ? ? ? ? ? ? ? 1.442 ? N-Glycosylation 
covale14 covale one ? B ASN 437 ND2 ? ? ? 1_555 M NAG .   C1 ? ? A ASN 428 A NAG 603 1_555 ? ? ? ? ? ? ? 1.439 ? N-Glycosylation 
covale15 covale one ? B ASN 496 ND2 ? ? ? 1_555 K NAG .   C1 ? ? A ASN 487 A NAG 601 1_555 ? ? ? ? ? ? ? 1.439 ? N-Glycosylation 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  NAG C .   ? ASN A 482 ? NAG B 601 ? 1_555 ASN B 475 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG D .   ? ASN A 292 ? NAG B 602 ? 1_555 ASN B 285 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG E .   ? ASN A 271 ? NAG B 603 ? 1_555 ASN B 264 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG F .   ? ASN A 418 ? NAG B 604 ? 1_555 ASN B 411 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  NAG G .   ? ASN A 92  ? NAG B 605 ? 1_555 ASN B 85  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6  NAG H .   ? ASN A 137 ? NAG B 606 ? 1_555 ASN B 130 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7  NAG I .   ? ASN A 387 ? NAG B 607 ? 1_555 ASN B 380 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
8  NAG J .   ? ASN A 439 ? NAG B 608 ? 1_555 ASN B 432 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
9  NAG K .   ? ASN B 496 ? NAG A 601 ? 1_555 ASN A 487 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
10 NAG L .   ? ASN B 93  ? NAG A 602 ? 1_555 ASN A 84  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
11 NAG M .   ? ASN B 437 ? NAG A 603 ? 1_555 ASN A 428 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
12 NAG N .   ? ASN B 321 ? NAG A 604 ? 1_555 ASN A 312 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
13 NAG O .   ? ASN B 257 ? NAG A 605 ? 1_555 ASN A 248 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
14 NAG P .   ? ASN B 301 ? NAG A 606 ? 1_555 ASN A 292 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
15 NAG Q .   ? ASN B 377 ? NAG A 607 ? 1_555 ASN A 368 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
16 CYS A 31  ? CYS A 358 ? CYS B 24  ? 1_555 CYS B 351 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
17 CYS A 69  ? CYS A 110 ? CYS B 62  ? 1_555 CYS B 103 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
18 CYS A 136 ? CYS B 368 ? CYS B 129 ? 1_555 CYS A 359 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
19 CYS A 243 ? CYS A 524 ? CYS B 236 ? 1_555 CYS B 517 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
20 CYS A 377 ? CYS A 380 ? CYS B 370 ? 1_555 CYS B 373 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
21 CYS A 417 ? CYS A 422 ? CYS B 410 ? 1_555 CYS B 415 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
22 CYS A 506 ? CYS A 525 ? CYS B 499 ? 1_555 CYS B 518 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
23 CYS A 510 ? CYS A 528 ? CYS B 503 ? 1_555 CYS B 521 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
24 CYS B 68  ? CYS B 111 ? CYS A 59  ? 1_555 CYS A 102 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
25 CYS B 242 ? CYS B 522 ? CYS A 233 ? 1_555 CYS A 513 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
26 CYS B 372 ? CYS B 375 ? CYS A 363 ? 1_555 CYS A 366 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
27 CYS B 414 ? CYS B 419 ? CYS A 405 ? 1_555 CYS A 410 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
28 CYS B 504 ? CYS B 523 ? CYS A 495 ? 1_555 CYS A 514 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 8 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 6 ? 
AA8 ? 8 ? 
AA9 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA4 7 8 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA7 5 6 ? parallel      
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA8 3 4 ? parallel      
AA8 4 5 ? parallel      
AA8 5 6 ? anti-parallel 
AA8 6 7 ? anti-parallel 
AA8 7 8 ? anti-parallel 
AA9 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ARG A 37  ? MET A 38  ? ARG B 30  MET B 31  
AA1 2 LEU A 102 ? ASP A 108 ? LEU B 95  ASP B 101 
AA1 3 TYR A 42  ? PHE A 48  ? TYR B 35  PHE B 41  
AA1 4 ALA A 147 ? GLY A 150 ? ALA B 140 GLY B 143 
AA1 5 GLN A 171 ? SER A 173 ? GLN B 164 SER B 166 
AA1 6 PHE A 190 ? ARG A 192 ? PHE B 183 ARG B 185 
AA2 1 GLY A 51  ? GLU A 52  ? GLY B 44  GLU B 45  
AA2 2 ARG A 71  ? PHE A 72  ? ARG B 64  PHE B 65  
AA3 1 ASP A 131 ? ALA A 133 ? ASP B 124 ALA B 126 
AA3 2 LEU B 130 ? PRO B 132 ? LEU A 121 PRO A 123 
AA4 1 CYS A 243 ? VAL A 250 ? CYS B 236 VAL B 243 
AA4 2 TRP A 215 ? SER A 221 ? TRP B 208 SER B 214 
AA4 3 VAL A 277 ? PHE A 281 ? VAL B 270 PHE B 274 
AA4 4 VAL A 303 ? ALA A 306 ? VAL B 296 ALA B 299 
AA4 5 VAL A 328 ? GLN A 333 ? VAL B 321 GLN B 326 
AA4 6 TYR A 461 ? TRP A 468 ? TYR B 454 TRP B 461 
AA4 7 PRO A 473 ? PHE A 481 ? PRO B 466 PHE B 474 
AA4 8 LEU A 485 ? THR A 487 ? LEU B 478 THR B 480 
AA5 1 THR A 441 ? VAL A 444 ? THR B 434 VAL B 437 
AA5 2 LEU A 447 ? ARG A 450 ? LEU B 440 ARG B 443 
AA6 1 VAL A 518 ? LYS A 519 ? VAL B 511 LYS B 512 
AA6 2 CYS A 525 ? TYR A 526 ? CYS B 518 TYR B 519 
AA7 1 TYR B 37  ? LEU B 38  ? TYR A 28  LEU A 29  
AA7 2 TYR B 105 ? VAL B 110 ? TYR A 96  VAL A 101 
AA7 3 LEU B 43  ? SER B 49  ? LEU A 34  SER A 40  
AA7 4 VAL B 144 ? GLY B 149 ? VAL A 135 GLY A 140 
AA7 5 GLN B 170 ? THR B 172 ? GLN A 161 THR A 163 
AA7 6 LEU B 189 ? ARG B 191 ? LEU A 180 ARG A 182 
AA8 1 CYS B 242 ? LEU B 249 ? CYS A 233 LEU A 240 
AA8 2 TRP B 214 ? SER B 220 ? TRP A 205 SER A 211 
AA8 3 VAL B 280 ? PHE B 284 ? VAL A 271 PHE A 275 
AA8 4 ALA B 305 ? ALA B 309 ? ALA A 296 ALA A 300 
AA8 5 GLY B 329 ? ILE B 336 ? GLY A 320 ILE A 327 
AA8 6 LEU B 457 ? TRP B 462 ? LEU A 448 TRP A 453 
AA8 7 PHE B 471 ? TYR B 478 ? PHE A 462 TYR A 469 
AA8 8 GLN B 483 ? LYS B 485 ? GLN A 474 LYS A 476 
AA9 1 ASN B 437 ? LEU B 440 ? ASN A 428 LEU A 431 
AA9 2 HIS B 443 ? PHE B 446 ? HIS A 434 PHE A 437 
# 
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 MET A 38  ? N MET B 31  O TYR A 104 ? O TYR B 97  
AA1 2 3 O GLY A 103 ? O GLY B 96  N TYR A 42  ? N TYR B 35  
AA1 3 4 N GLY A 45  ? N GLY B 38  O ILE A 149 ? O ILE B 142 
AA1 4 5 N VAL A 148 ? N VAL B 141 O VAL A 172 ? O VAL B 165 
AA1 5 6 N GLN A 171 ? N GLN B 164 O PHE A 191 ? O PHE B 184 
AA2 1 2 N GLU A 52  ? N GLU B 45  O ARG A 71  ? O ARG B 64  
AA3 1 2 N ILE A 132 ? N ILE B 125 O LEU B 131 ? O LEU A 122 
AA4 1 2 O ALA A 245 ? O ALA B 238 N VAL A 216 ? N VAL B 209 
AA4 2 3 N LEU A 219 ? N LEU B 212 O LEU A 279 ? O LEU B 272 
AA4 3 4 N VAL A 278 ? N VAL B 271 O VAL A 303 ? O VAL B 296 
AA4 4 5 N TRP A 304 ? N TRP B 297 O LEU A 329 ? O LEU B 322 
AA4 5 6 N LEU A 332 ? N LEU B 325 O ASP A 462 ? O ASP B 455 
AA4 6 7 N TYR A 461 ? N TYR B 454 O PHE A 481 ? O PHE B 474 
AA4 7 8 N ARG A 480 ? N ARG B 473 O ARG A 486 ? O ARG B 479 
AA5 1 2 N PHE A 442 ? N PHE B 435 O LEU A 449 ? O LEU B 442 
AA6 1 2 N LYS A 519 ? N LYS B 512 O CYS A 525 ? O CYS B 518 
AA7 1 2 N LEU B 38  ? N LEU A 29  O TYR B 105 ? O TYR A 96  
AA7 2 3 O VAL B 108 ? O VAL A 99  N GLY B 46  ? N GLY A 37  
AA7 3 4 N GLY B 45  ? N GLY A 36  O ILE B 148 ? O ILE A 139 
AA7 4 5 N VAL B 147 ? N VAL A 138 O ILE B 171 ? O ILE A 162 
AA7 5 6 N GLN B 170 ? N GLN A 161 O LEU B 190 ? O LEU A 181 
AA8 1 2 O LEU B 249 ? O LEU A 240 N VAL B 219 ? N VAL A 210 
AA8 2 3 N LEU B 218 ? N LEU A 209 O PHE B 284 ? O PHE A 275 
AA8 3 4 N VAL B 281 ? N VAL A 272 O ILE B 308 ? O ILE A 299 
AA8 4 5 N TRP B 307 ? N TRP A 298 O LEU B 332 ? O LEU A 323 
AA8 5 6 N GLY B 333 ? N GLY A 324 O VAL B 460 ? O VAL A 451 
AA8 6 7 N GLN B 461 ? N GLN A 452 O GLN B 472 ? O GLN A 463 
AA8 7 8 N SER B 476 ? N SER A 467 O LYS B 485 ? O LYS A 476 
AA9 1 2 N PHE B 438 ? N PHE A 429 O ILE B 445 ? O ILE A 436 
# 
_pdbx_entry_details.entry_id                   9NOU 
_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     N 
_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 108 ? ? -123.30 -64.77  
2 1 PRO A 141 ? ? -67.48  -176.18 
3 1 ASN A 360 ? ? 34.16   52.28   
4 1 PRO A 440 ? ? -59.26  -7.06   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9NOU 
_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                    9NOU 
_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                  2.8 
_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               776095 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.5 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Human sweet taste receptor (TAS1R2 + TAS1R3) VFT domains' 
_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                        9NOU 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             1200 
_em_imaging.nominal_defocus_max             2000 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
_em_imaging.objective_aperture              ? 
_em_imaging.microscope_serial_number        ? 
_em_imaging.microscope_version              ? 
# 
_em_vitrification.entry_id              9NOU 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9NOU 
_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 B MET -6  ? A MET 1   
2   1 Y 1 B LYS -5  ? A LYS 2   
3   1 Y 1 B THR -4  ? A THR 3   
4   1 Y 1 B ILE -3  ? A ILE 4   
5   1 Y 1 B ILE -2  ? A ILE 5   
6   1 Y 1 B ALA -1  ? A ALA 6   
7   1 Y 1 B LEU 0   ? A LEU 7   
8   1 Y 1 B SER 1   ? A SER 8   
9   1 Y 1 B TYR 2   ? A TYR 9   
10  1 Y 1 B ILE 3   ? A ILE 10  
11  1 Y 1 B PHE 4   ? A PHE 11  
12  1 Y 1 B CYS 5   ? A CYS 12  
13  1 Y 1 B LEU 6   ? A LEU 13  
14  1 Y 1 B VAL 7   ? A VAL 14  
15  1 Y 1 B PHE 8   ? A PHE 15  
16  1 Y 1 B ALA 9   ? A ALA 16  
17  1 Y 1 B ASP 10  ? A ASP 17  
18  1 Y 1 B TYR 11  ? A TYR 18  
19  1 Y 1 B LYS 12  ? A LYS 19  
20  1 Y 1 B ASP 13  ? A ASP 20  
21  1 Y 1 B ASP 14  ? A ASP 21  
22  1 Y 1 B ASP 15  ? A ASP 22  
23  1 Y 1 B ASP 16  ? A ASP 23  
24  1 Y 1 B LYS 17  ? A LYS 24  
25  1 Y 1 B ALA 18  ? A ALA 25  
26  1 Y 1 B ALA 19  ? A ALA 26  
27  1 Y 1 B ALA 20  ? A ALA 27  
28  1 Y 1 B ALA 21  ? A ALA 28  
29  1 Y 1 B PRO 22  ? A PRO 29  
30  1 Y 1 B GLU 47  ? A GLU 54  
31  1 Y 1 B GLU 48  ? A GLU 55  
32  1 Y 1 B ALA 49  ? A ALA 56  
33  1 Y 1 B GLY 50  ? A GLY 57  
34  1 Y 1 B LEU 51  ? A LEU 58  
35  1 Y 1 B ARG 52  ? A ARG 59  
36  1 Y 1 B SER 53  ? A SER 60  
37  1 Y 1 B ARG 247 ? A ARG 254 
38  1 Y 1 B ALA 248 ? A ALA 255 
39  1 Y 1 B ASP 249 ? A ASP 256 
40  1 Y 1 B ASP 250 ? A ASP 257 
41  1 Y 1 B SER 251 ? A SER 258 
42  1 Y 1 B ARG 252 ? A ARG 259 
43  1 Y 1 B LEU 253 ? A LEU 260 
44  1 Y 1 B GLY 254 ? A GLY 261 
45  1 Y 1 B GLY 355 ? A GLY 362 
46  1 Y 1 B GLU 356 ? A GLU 363 
47  1 Y 1 B ARG 357 ? A ARG 364 
48  1 Y 1 B GLU 358 ? A GLU 365 
49  1 Y 1 B GLN 359 ? A GLN 366 
50  1 Y 1 B GLY 360 ? A GLY 367 
51  1 Y 1 B LEU 361 ? A LEU 368 
52  1 Y 1 B GLU 362 ? A GLU 369 
53  1 Y 1 B GLU 363 ? A GLU 370 
54  1 Y 1 B ASP 364 ? A ASP 371 
55  1 Y 1 B VAL 365 ? A VAL 372 
56  1 Y 1 B VAL 366 ? A VAL 373 
57  1 Y 1 B GLY 367 ? A GLY 374 
58  1 Y 1 B GLN 504 ? A GLN 511 
59  1 Y 1 B GLU 505 ? A GLU 512 
60  1 Y 1 B GLY 506 ? A GLY 513 
61  1 Y 1 B GLN 507 ? A GLN 514 
62  1 Y 1 B VAL 508 ? A VAL 515 
63  1 Y 1 B ARG 509 ? A ARG 516 
64  1 Y 1 A MET -8  ? B MET 1   
65  1 Y 1 A LYS -7  ? B LYS 2   
66  1 Y 1 A THR -6  ? B THR 3   
67  1 Y 1 A ILE -5  ? B ILE 4   
68  1 Y 1 A ILE -4  ? B ILE 5   
69  1 Y 1 A ALA -3  ? B ALA 6   
70  1 Y 1 A LEU -2  ? B LEU 7   
71  1 Y 1 A SER -1  ? B SER 8   
72  1 Y 1 A TYR 0   ? B TYR 9   
73  1 Y 1 A ILE 1   ? B ILE 10  
74  1 Y 1 A PHE 2   ? B PHE 11  
75  1 Y 1 A CYS 3   ? B CYS 12  
76  1 Y 1 A LEU 4   ? B LEU 13  
77  1 Y 1 A VAL 5   ? B VAL 14  
78  1 Y 1 A PHE 6   ? B PHE 15  
79  1 Y 1 A ALA 7   ? B ALA 16  
80  1 Y 1 A TYR 8   ? B TYR 17  
81  1 Y 1 A PRO 9   ? B PRO 18  
82  1 Y 1 A TYR 10  ? B TYR 19  
83  1 Y 1 A ASP 11  ? B ASP 20  
84  1 Y 1 A VAL 12  ? B VAL 21  
85  1 Y 1 A PRO 13  ? B PRO 22  
86  1 Y 1 A ASP 14  ? B ASP 23  
87  1 Y 1 A TYR 15  ? B TYR 24  
88  1 Y 1 A ALA 16  ? B ALA 25  
89  1 Y 1 A ALA 17  ? B ALA 26  
90  1 Y 1 A ALA 18  ? B ALA 27  
91  1 Y 1 A ALA 19  ? B ALA 28  
92  1 Y 1 A GLU 20  ? B GLU 29  
93  1 Y 1 A PRO 21  ? B PRO 30  
94  1 Y 1 A ALA 22  ? B ALA 31  
95  1 Y 1 A GLU 23  ? B GLU 32  
96  1 Y 1 A ASN 24  ? B ASN 33  
97  1 Y 1 A ALA 43  ? B ALA 52  
98  1 Y 1 A ASN 44  ? B ASN 53  
99  1 Y 1 A MET 45  ? B MET 54  
100 1 Y 1 A LYS 46  ? B LYS 55  
101 1 Y 1 A GLY 47  ? B GLY 56  
102 1 Y 1 A ILE 48  ? B ILE 57  
103 1 Y 1 A VAL 49  ? B VAL 58  
104 1 Y 1 A HIS 50  ? B HIS 59  
105 1 Y 1 A LEU 51  ? B LEU 60  
106 1 Y 1 A ASN 52  ? B ASN 61  
107 1 Y 1 A PRO 343 ? B PRO 352 
108 1 Y 1 A GLN 344 ? B GLN 353 
109 1 Y 1 A ALA 345 ? B ALA 354 
110 1 Y 1 A GLY 346 ? B GLY 355 
111 1 Y 1 A PRO 347 ? B PRO 356 
112 1 Y 1 A PRO 348 ? B PRO 357 
113 1 Y 1 A PRO 349 ? B PRO 358 
114 1 Y 1 A LEU 350 ? B LEU 359 
115 1 Y 1 A SER 351 ? B SER 360 
116 1 Y 1 A ARG 352 ? B ARG 361 
117 1 Y 1 A THR 353 ? B THR 362 
118 1 Y 1 A SER 354 ? B SER 363 
119 1 Y 1 A GLN 355 ? B GLN 364 
120 1 Y 1 A SER 356 ? B SER 365 
121 1 Y 1 A TYR 357 ? B TYR 366 
122 1 Y 1 A ARG 498 ? B ARG 507 
123 1 Y 1 A CYS 499 ? B CYS 508 
124 1 Y 1 A GLN 500 ? B GLN 509 
125 1 Y 1 A SER 501 ? B SER 510 
126 1 Y 1 A GLY 502 ? B GLY 511 
127 1 Y 1 A GLN 503 ? B GLN 512 
128 1 Y 1 A LYS 504 ? B LYS 513 
129 1 Y 1 A LYS 505 ? B LYS 514 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
NAG C1   C N R 247 
NAG C2   C N R 248 
NAG C3   C N R 249 
NAG C4   C N S 250 
NAG C5   C N R 251 
NAG C6   C N N 252 
NAG C7   C N N 253 
NAG C8   C N N 254 
NAG N2   N N N 255 
NAG O1   O N N 256 
NAG O3   O N N 257 
NAG O4   O N N 258 
NAG O5   O N N 259 
NAG O6   O N N 260 
NAG O7   O N N 261 
NAG H1   H N N 262 
NAG H2   H N N 263 
NAG H3   H N N 264 
NAG H4   H N N 265 
NAG H5   H N N 266 
NAG H61  H N N 267 
NAG H62  H N N 268 
NAG H81  H N N 269 
NAG H82  H N N 270 
NAG H83  H N N 271 
NAG HN2  H N N 272 
NAG HO1  H N N 273 
NAG HO3  H N N 274 
NAG HO4  H N N 275 
NAG HO6  H N N 276 
PHE N    N N N 277 
PHE CA   C N S 278 
PHE C    C N N 279 
PHE O    O N N 280 
PHE CB   C N N 281 
PHE CG   C Y N 282 
PHE CD1  C Y N 283 
PHE CD2  C Y N 284 
PHE CE1  C Y N 285 
PHE CE2  C Y N 286 
PHE CZ   C Y N 287 
PHE OXT  O N N 288 
PHE H    H N N 289 
PHE H2   H N N 290 
PHE HA   H N N 291 
PHE HB2  H N N 292 
PHE HB3  H N N 293 
PHE HD1  H N N 294 
PHE HD2  H N N 295 
PHE HE1  H N N 296 
PHE HE2  H N N 297 
PHE HZ   H N N 298 
PHE HXT  H N N 299 
PRO N    N N N 300 
PRO CA   C N S 301 
PRO C    C N N 302 
PRO O    O N N 303 
PRO CB   C N N 304 
PRO CG   C N N 305 
PRO CD   C N N 306 
PRO OXT  O N N 307 
PRO H    H N N 308 
PRO HA   H N N 309 
PRO HB2  H N N 310 
PRO HB3  H N N 311 
PRO HG2  H N N 312 
PRO HG3  H N N 313 
PRO HD2  H N N 314 
PRO HD3  H N N 315 
PRO HXT  H N N 316 
SER N    N N N 317 
SER CA   C N S 318 
SER C    C N N 319 
SER O    O N N 320 
SER CB   C N N 321 
SER OG   O N N 322 
SER OXT  O N N 323 
SER H    H N N 324 
SER H2   H N N 325 
SER HA   H N N 326 
SER HB2  H N N 327 
SER HB3  H N N 328 
SER HG   H N N 329 
SER HXT  H N N 330 
THR N    N N N 331 
THR CA   C N S 332 
THR C    C N N 333 
THR O    O N N 334 
THR CB   C N R 335 
THR OG1  O N N 336 
THR CG2  C N N 337 
THR OXT  O N N 338 
THR H    H N N 339 
THR H2   H N N 340 
THR HA   H N N 341 
THR HB   H N N 342 
THR HG1  H N N 343 
THR HG21 H N N 344 
THR HG22 H N N 345 
THR HG23 H N N 346 
THR HXT  H N N 347 
TRP N    N N N 348 
TRP CA   C N S 349 
TRP C    C N N 350 
TRP O    O N N 351 
TRP CB   C N N 352 
TRP CG   C Y N 353 
TRP CD1  C Y N 354 
TRP CD2  C Y N 355 
TRP NE1  N Y N 356 
TRP CE2  C Y N 357 
TRP CE3  C Y N 358 
TRP CZ2  C Y N 359 
TRP CZ3  C Y N 360 
TRP CH2  C Y N 361 
TRP OXT  O N N 362 
TRP H    H N N 363 
TRP H2   H N N 364 
TRP HA   H N N 365 
TRP HB2  H N N 366 
TRP HB3  H N N 367 
TRP HD1  H N N 368 
TRP HE1  H N N 369 
TRP HE3  H N N 370 
TRP HZ2  H N N 371 
TRP HZ3  H N N 372 
TRP HH2  H N N 373 
TRP HXT  H N N 374 
TYR N    N N N 375 
TYR CA   C N S 376 
TYR C    C N N 377 
TYR O    O N N 378 
TYR CB   C N N 379 
TYR CG   C Y N 380 
TYR CD1  C Y N 381 
TYR CD2  C Y N 382 
TYR CE1  C Y N 383 
TYR CE2  C Y N 384 
TYR CZ   C Y N 385 
TYR OH   O N N 386 
TYR OXT  O N N 387 
TYR H    H N N 388 
TYR H2   H N N 389 
TYR HA   H N N 390 
TYR HB2  H N N 391 
TYR HB3  H N N 392 
TYR HD1  H N N 393 
TYR HD2  H N N 394 
TYR HE1  H N N 395 
TYR HE2  H N N 396 
TYR HH   H N N 397 
TYR HXT  H N N 398 
VAL N    N N N 399 
VAL CA   C N S 400 
VAL C    C N N 401 
VAL O    O N N 402 
VAL CB   C N N 403 
VAL CG1  C N N 404 
VAL CG2  C N N 405 
VAL OXT  O N N 406 
VAL H    H N N 407 
VAL H2   H N N 408 
VAL HA   H N N 409 
VAL HB   H N N 410 
VAL HG11 H N N 411 
VAL HG12 H N N 412 
VAL HG13 H N N 413 
VAL HG21 H N N 414 
VAL HG22 H N N 415 
VAL HG23 H N N 416 
VAL HXT  H N N 417 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
NAG C1  C2   sing N N 235 
NAG C1  O1   sing N N 236 
NAG C1  O5   sing N N 237 
NAG C1  H1   sing N N 238 
NAG C2  C3   sing N N 239 
NAG C2  N2   sing N N 240 
NAG C2  H2   sing N N 241 
NAG C3  C4   sing N N 242 
NAG C3  O3   sing N N 243 
NAG C3  H3   sing N N 244 
NAG C4  C5   sing N N 245 
NAG C4  O4   sing N N 246 
NAG C4  H4   sing N N 247 
NAG C5  C6   sing N N 248 
NAG C5  O5   sing N N 249 
NAG C5  H5   sing N N 250 
NAG C6  O6   sing N N 251 
NAG C6  H61  sing N N 252 
NAG C6  H62  sing N N 253 
NAG C7  C8   sing N N 254 
NAG C7  N2   sing N N 255 
NAG C7  O7   doub N N 256 
NAG C8  H81  sing N N 257 
NAG C8  H82  sing N N 258 
NAG C8  H83  sing N N 259 
NAG N2  HN2  sing N N 260 
NAG O1  HO1  sing N N 261 
NAG O3  HO3  sing N N 262 
NAG O4  HO4  sing N N 263 
NAG O6  HO6  sing N N 264 
PHE N   CA   sing N N 265 
PHE N   H    sing N N 266 
PHE N   H2   sing N N 267 
PHE CA  C    sing N N 268 
PHE CA  CB   sing N N 269 
PHE CA  HA   sing N N 270 
PHE C   O    doub N N 271 
PHE C   OXT  sing N N 272 
PHE CB  CG   sing N N 273 
PHE CB  HB2  sing N N 274 
PHE CB  HB3  sing N N 275 
PHE CG  CD1  doub Y N 276 
PHE CG  CD2  sing Y N 277 
PHE CD1 CE1  sing Y N 278 
PHE CD1 HD1  sing N N 279 
PHE CD2 CE2  doub Y N 280 
PHE CD2 HD2  sing N N 281 
PHE CE1 CZ   doub Y N 282 
PHE CE1 HE1  sing N N 283 
PHE CE2 CZ   sing Y N 284 
PHE CE2 HE2  sing N N 285 
PHE CZ  HZ   sing N N 286 
PHE OXT HXT  sing N N 287 
PRO N   CA   sing N N 288 
PRO N   CD   sing N N 289 
PRO N   H    sing N N 290 
PRO CA  C    sing N N 291 
PRO CA  CB   sing N N 292 
PRO CA  HA   sing N N 293 
PRO C   O    doub N N 294 
PRO C   OXT  sing N N 295 
PRO CB  CG   sing N N 296 
PRO CB  HB2  sing N N 297 
PRO CB  HB3  sing N N 298 
PRO CG  CD   sing N N 299 
PRO CG  HG2  sing N N 300 
PRO CG  HG3  sing N N 301 
PRO CD  HD2  sing N N 302 
PRO CD  HD3  sing N N 303 
PRO OXT HXT  sing N N 304 
SER N   CA   sing N N 305 
SER N   H    sing N N 306 
SER N   H2   sing N N 307 
SER CA  C    sing N N 308 
SER CA  CB   sing N N 309 
SER CA  HA   sing N N 310 
SER C   O    doub N N 311 
SER C   OXT  sing N N 312 
SER CB  OG   sing N N 313 
SER CB  HB2  sing N N 314 
SER CB  HB3  sing N N 315 
SER OG  HG   sing N N 316 
SER OXT HXT  sing N N 317 
THR N   CA   sing N N 318 
THR N   H    sing N N 319 
THR N   H2   sing N N 320 
THR CA  C    sing N N 321 
THR CA  CB   sing N N 322 
THR CA  HA   sing N N 323 
THR C   O    doub N N 324 
THR C   OXT  sing N N 325 
THR CB  OG1  sing N N 326 
THR CB  CG2  sing N N 327 
THR CB  HB   sing N N 328 
THR OG1 HG1  sing N N 329 
THR CG2 HG21 sing N N 330 
THR CG2 HG22 sing N N 331 
THR CG2 HG23 sing N N 332 
THR OXT HXT  sing N N 333 
TRP N   CA   sing N N 334 
TRP N   H    sing N N 335 
TRP N   H2   sing N N 336 
TRP CA  C    sing N N 337 
TRP CA  CB   sing N N 338 
TRP CA  HA   sing N N 339 
TRP C   O    doub N N 340 
TRP C   OXT  sing N N 341 
TRP CB  CG   sing N N 342 
TRP CB  HB2  sing N N 343 
TRP CB  HB3  sing N N 344 
TRP CG  CD1  doub Y N 345 
TRP CG  CD2  sing Y N 346 
TRP CD1 NE1  sing Y N 347 
TRP CD1 HD1  sing N N 348 
TRP CD2 CE2  doub Y N 349 
TRP CD2 CE3  sing Y N 350 
TRP NE1 CE2  sing Y N 351 
TRP NE1 HE1  sing N N 352 
TRP CE2 CZ2  sing Y N 353 
TRP CE3 CZ3  doub Y N 354 
TRP CE3 HE3  sing N N 355 
TRP CZ2 CH2  doub Y N 356 
TRP CZ2 HZ2  sing N N 357 
TRP CZ3 CH2  sing Y N 358 
TRP CZ3 HZ3  sing N N 359 
TRP CH2 HH2  sing N N 360 
TRP OXT HXT  sing N N 361 
TYR N   CA   sing N N 362 
TYR N   H    sing N N 363 
TYR N   H2   sing N N 364 
TYR CA  C    sing N N 365 
TYR CA  CB   sing N N 366 
TYR CA  HA   sing N N 367 
TYR C   O    doub N N 368 
TYR C   OXT  sing N N 369 
TYR CB  CG   sing N N 370 
TYR CB  HB2  sing N N 371 
TYR CB  HB3  sing N N 372 
TYR CG  CD1  doub Y N 373 
TYR CG  CD2  sing Y N 374 
TYR CD1 CE1  sing Y N 375 
TYR CD1 HD1  sing N N 376 
TYR CD2 CE2  doub Y N 377 
TYR CD2 HD2  sing N N 378 
TYR CE1 CZ   doub Y N 379 
TYR CE1 HE1  sing N N 380 
TYR CE2 CZ   sing Y N 381 
TYR CE2 HE2  sing N N 382 
TYR CZ  OH   sing N N 383 
TYR OH  HH   sing N N 384 
TYR OXT HXT  sing N N 385 
VAL N   CA   sing N N 386 
VAL N   H    sing N N 387 
VAL N   H2   sing N N 388 
VAL CA  C    sing N N 389 
VAL CA  CB   sing N N 390 
VAL CA  HA   sing N N 391 
VAL C   O    doub N N 392 
VAL C   OXT  sing N N 393 
VAL CB  CG1  sing N N 394 
VAL CB  CG2  sing N N 395 
VAL CB  HB   sing N N 396 
VAL CG1 HG11 sing N N 397 
VAL CG1 HG12 sing N N 398 
VAL CG1 HG13 sing N N 399 
VAL CG2 HG21 sing N N 400 
VAL CG2 HG22 sing N N 401 
VAL CG2 HG23 sing N N 402 
VAL OXT HXT  sing N N 403 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2025-03-10 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9NOU 
_em_admin.last_update        2025-05-21 
_em_admin.map_release_date   2025-05-14 
_em_admin.title              'Human sweet taste receptor (TAS1R2 + TAS1R3) VFT domains from the combined datasets' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     NONE 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          9606 
_em_entity_assembly_recombinant.organism             'Homo sapiens' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         59 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? ?      ? 
'IMAGE ACQUISITION'        ? 2  ? ? 1 ?      ? 
MASKING                    ? 3  ? ? ? ?      ? 
'CTF CORRECTION'           ? 4  1 ? ? ?      ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ?      ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?      ? 
'MODEL FITTING'            ? 7  ? ? ? ?      ? 
'MODEL REFINEMENT'         ? 8  ? ? ? PHENIX ? 
OTHER                      ? 9  ? ? ? ?      ? 
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ?      ? 
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? ?      ? 
CLASSIFICATION             ? 12 1 ? ? ?      ? 
RECONSTRUCTION             ? 13 1 ? ? ?      ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'Howard Hughes Medical Institute (HHMI)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9NOU 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . LEU A 1 30  ? 189.601 213.838 99.811  1.00 104.84 ? 23  LEU B N   1 
ATOM   2    C CA  . LEU A 1 30  ? 190.987 213.456 100.054 1.00 108.43 ? 23  LEU B CA  1 
ATOM   3    C C   . LEU A 1 30  ? 191.415 212.331 99.123  1.00 109.79 ? 23  LEU B C   1 
ATOM   4    O O   . LEU A 1 30  ? 192.592 211.984 99.067  1.00 109.75 ? 23  LEU B O   1 
ATOM   5    C CB  . LEU A 1 30  ? 191.180 213.027 101.509 1.00 106.48 ? 23  LEU B CB  1 
ATOM   6    C CG  . LEU A 1 30  ? 192.465 213.475 102.207 1.00 102.23 ? 23  LEU B CG  1 
ATOM   7    C CD1 . LEU A 1 30  ? 192.712 214.952 101.965 1.00 102.76 ? 23  LEU B CD1 1 
ATOM   8    C CD2 . LEU A 1 30  ? 192.399 213.176 103.694 1.00 96.04  ? 23  LEU B CD2 1 
ATOM   9    N N   . CYS A 1 31  ? 190.442 211.761 98.409  1.00 107.33 ? 24  CYS B N   1 
ATOM   10   C CA  . CYS A 1 31  ? 190.661 210.619 97.516  1.00 103.39 ? 24  CYS B CA  1 
ATOM   11   C C   . CYS A 1 31  ? 191.374 209.476 98.241  1.00 99.27  ? 24  CYS B C   1 
ATOM   12   O O   . CYS A 1 31  ? 192.126 208.700 97.649  1.00 97.13  ? 24  CYS B O   1 
ATOM   13   C CB  . CYS A 1 31  ? 191.403 211.044 96.239  1.00 108.01 ? 24  CYS B CB  1 
ATOM   14   S SG  . CYS A 1 31  ? 193.217 211.106 96.269  1.00 121.48 ? 24  CYS B SG  1 
ATOM   15   N N   . LEU A 1 32  ? 191.105 209.358 99.541  1.00 99.65  ? 25  LEU B N   1 
ATOM   16   C CA  . LEU A 1 32  ? 191.641 208.288 100.372 1.00 95.88  ? 25  LEU B CA  1 
ATOM   17   C C   . LEU A 1 32  ? 190.878 206.982 100.219 1.00 87.30  ? 25  LEU B C   1 
ATOM   18   O O   . LEU A 1 32  ? 191.496 205.922 100.096 1.00 85.45  ? 25  LEU B O   1 
ATOM   19   C CB  . LEU A 1 32  ? 191.633 208.707 101.845 1.00 96.17  ? 25  LEU B CB  1 
ATOM   20   C CG  . LEU A 1 32  ? 192.791 208.204 102.706 1.00 84.08  ? 25  LEU B CG  1 
ATOM   21   C CD1 . LEU A 1 32  ? 194.084 208.896 102.321 1.00 89.83  ? 25  LEU B CD1 1 
ATOM   22   C CD2 . LEU A 1 32  ? 192.488 208.413 104.178 1.00 82.48  ? 25  LEU B CD2 1 
ATOM   23   N N   . SER A 1 33  ? 189.544 207.033 100.225 1.00 82.72  ? 26  SER B N   1 
ATOM   24   C CA  . SER A 1 33  ? 188.746 205.828 100.044 1.00 82.17  ? 26  SER B CA  1 
ATOM   25   C C   . SER A 1 33  ? 188.927 205.210 98.665  1.00 80.21  ? 26  SER B C   1 
ATOM   26   O O   . SER A 1 33  ? 188.690 204.008 98.507  1.00 80.88  ? 26  SER B O   1 
ATOM   27   C CB  . SER A 1 33  ? 187.269 206.139 100.286 1.00 91.58  ? 26  SER B CB  1 
ATOM   28   O OG  . SER A 1 33  ? 186.441 205.102 99.794  1.00 95.18  ? 26  SER B OG  1 
ATOM   29   N N   . GLN A 1 34  ? 189.341 205.993 97.669  1.00 82.59  ? 27  GLN B N   1 
ATOM   30   C CA  . GLN A 1 34  ? 189.641 205.458 96.349  1.00 81.60  ? 27  GLN B CA  1 
ATOM   31   C C   . GLN A 1 34  ? 190.848 204.532 96.351  1.00 76.60  ? 27  GLN B C   1 
ATOM   32   O O   . GLN A 1 34  ? 191.039 203.787 95.384  1.00 72.50  ? 27  GLN B O   1 
ATOM   33   C CB  . GLN A 1 34  ? 189.883 206.600 95.360  1.00 82.55  ? 27  GLN B CB  1 
ATOM   34   C CG  . GLN A 1 34  ? 188.623 207.323 94.920  1.00 87.51  ? 27  GLN B CG  1 
ATOM   35   C CD  . GLN A 1 34  ? 188.551 207.498 93.417  1.00 97.90  ? 27  GLN B CD  1 
ATOM   36   O OE1 . GLN A 1 34  ? 188.469 206.524 92.670  1.00 95.71  ? 27  GLN B OE1 1 
ATOM   37   N NE2 . GLN A 1 34  ? 188.583 208.747 92.965  1.00 103.96 ? 27  GLN B NE2 1 
ATOM   38   N N   . GLN A 1 35  ? 191.658 204.563 97.406  1.00 76.62  ? 28  GLN B N   1 
ATOM   39   C CA  . GLN A 1 35  ? 192.861 203.752 97.512  1.00 73.69  ? 28  GLN B CA  1 
ATOM   40   C C   . GLN A 1 35  ? 192.650 202.495 98.341  1.00 63.82  ? 28  GLN B C   1 
ATOM   41   O O   . GLN A 1 35  ? 193.623 201.815 98.678  1.00 61.59  ? 28  GLN B O   1 
ATOM   42   C CB  . GLN A 1 35  ? 194.000 204.585 98.095  1.00 75.94  ? 28  GLN B CB  1 
ATOM   43   C CG  . GLN A 1 35  ? 194.578 205.580 97.115  1.00 83.81  ? 28  GLN B CG  1 
ATOM   44   C CD  . GLN A 1 35  ? 195.647 206.442 97.737  1.00 93.35  ? 28  GLN B CD  1 
ATOM   45   O OE1 . GLN A 1 35  ? 195.358 207.298 98.571  1.00 94.11  ? 28  GLN B OE1 1 
ATOM   46   N NE2 . GLN A 1 35  ? 196.894 206.216 97.344  1.00 96.86  ? 28  GLN B NE2 1 
ATOM   47   N N   . LEU A 1 36  ? 191.406 202.178 98.684  1.00 62.64  ? 29  LEU B N   1 
ATOM   48   C CA  . LEU A 1 36  ? 191.081 200.907 99.312  1.00 55.94  ? 29  LEU B CA  1 
ATOM   49   C C   . LEU A 1 36  ? 191.041 199.758 98.316  1.00 49.84  ? 29  LEU B C   1 
ATOM   50   O O   . LEU A 1 36  ? 190.747 198.628 98.711  1.00 51.65  ? 29  LEU B O   1 
ATOM   51   C CB  . LEU A 1 36  ? 189.734 200.998 100.036 1.00 55.56  ? 29  LEU B CB  1 
ATOM   52   C CG  . LEU A 1 36  ? 189.565 202.052 101.131 1.00 53.19  ? 29  LEU B CG  1 
ATOM   53   C CD1 . LEU A 1 36  ? 188.404 201.687 102.027 1.00 53.79  ? 29  LEU B CD1 1 
ATOM   54   C CD2 . LEU A 1 36  ? 190.831 202.204 101.948 1.00 48.47  ? 29  LEU B CD2 1 
ATOM   55   N N   . ARG A 1 37  ? 191.313 200.023 97.041  1.00 50.27  ? 30  ARG B N   1 
ATOM   56   C CA  . ARG A 1 37  ? 191.316 199.005 96.002  1.00 51.92  ? 30  ARG B CA  1 
ATOM   57   C C   . ARG A 1 37  ? 192.469 199.260 95.044  1.00 59.92  ? 30  ARG B C   1 
ATOM   58   O O   . ARG A 1 37  ? 192.652 200.390 94.581  1.00 61.07  ? 30  ARG B O   1 
ATOM   59   C CB  . ARG A 1 37  ? 189.995 199.004 95.229  1.00 57.12  ? 30  ARG B CB  1 
ATOM   60   C CG  . ARG A 1 37  ? 189.636 197.665 94.624  1.00 61.12  ? 30  ARG B CG  1 
ATOM   61   C CD  . ARG A 1 37  ? 189.181 197.794 93.183  1.00 67.95  ? 30  ARG B CD  1 
ATOM   62   N NE  . ARG A 1 37  ? 187.866 198.410 93.064  1.00 71.32  ? 30  ARG B NE  1 
ATOM   63   C CZ  . ARG A 1 37  ? 187.647 199.608 92.542  1.00 73.97  ? 30  ARG B CZ  1 
ATOM   64   N NH1 . ARG A 1 37  ? 188.639 200.352 92.080  1.00 65.74  ? 30  ARG B NH1 1 
ATOM   65   N NH2 . ARG A 1 37  ? 186.402 200.070 92.478  1.00 72.73  ? 30  ARG B NH2 1 
ATOM   66   N N   . MET A 1 38  ? 193.242 198.216 94.746  1.00 59.74  ? 31  MET B N   1 
ATOM   67   C CA  . MET A 1 38  ? 194.179 198.257 93.631  1.00 65.11  ? 31  MET B CA  1 
ATOM   68   C C   . MET A 1 38  ? 194.279 196.864 93.034  1.00 63.38  ? 31  MET B C   1 
ATOM   69   O O   . MET A 1 38  ? 194.353 195.877 93.770  1.00 59.20  ? 31  MET B O   1 
ATOM   70   C CB  . MET A 1 38  ? 195.567 198.762 94.048  1.00 63.35  ? 31  MET B CB  1 
ATOM   71   C CG  . MET A 1 38  ? 196.700 198.170 93.221  1.00 68.28  ? 31  MET B CG  1 
ATOM   72   S SD  . MET A 1 38  ? 198.378 198.549 93.749  1.00 88.36  ? 31  MET B SD  1 
ATOM   73   C CE  . MET A 1 38  ? 198.216 198.507 95.516  1.00 71.95  ? 31  MET B CE  1 
ATOM   74   N N   . LYS A 1 39  ? 194.278 196.789 91.706  1.00 65.90  ? 32  LYS B N   1 
ATOM   75   C CA  . LYS A 1 39  ? 194.331 195.514 91.013  1.00 65.76  ? 32  LYS B CA  1 
ATOM   76   C C   . LYS A 1 39  ? 195.691 194.851 91.201  1.00 64.15  ? 32  LYS B C   1 
ATOM   77   O O   . LYS A 1 39  ? 196.683 195.490 91.560  1.00 64.41  ? 32  LYS B O   1 
ATOM   78   C CB  . LYS A 1 39  ? 194.046 195.701 89.524  1.00 71.80  ? 32  LYS B CB  1 
ATOM   79   C CG  . LYS A 1 39  ? 192.612 196.097 89.202  1.00 85.43  ? 32  LYS B CG  1 
ATOM   80   C CD  . LYS A 1 39  ? 191.614 195.354 90.075  1.00 90.87  ? 32  LYS B CD  1 
ATOM   81   C CE  . LYS A 1 39  ? 190.219 195.398 89.472  1.00 94.43  ? 32  LYS B CE  1 
ATOM   82   N NZ  . LYS A 1 39  ? 189.162 195.425 90.518  1.00 94.86  ? 32  LYS B NZ  1 
ATOM   83   N N   . GLY A 1 40  ? 195.726 193.550 90.949  1.00 59.05  ? 33  GLY B N   1 
ATOM   84   C CA  . GLY A 1 40  ? 196.965 192.804 91.047  1.00 51.58  ? 33  GLY B CA  1 
ATOM   85   C C   . GLY A 1 40  ? 196.763 191.400 90.530  1.00 54.79  ? 33  GLY B C   1 
ATOM   86   O O   . GLY A 1 40  ? 195.645 190.987 90.205  1.00 56.54  ? 33  GLY B O   1 
ATOM   87   N N   . ASP A 1 41  ? 197.874 190.667 90.448  1.00 56.17  ? 34  ASP B N   1 
ATOM   88   C CA  . ASP A 1 41  ? 197.803 189.274 90.021  1.00 54.67  ? 34  ASP B CA  1 
ATOM   89   C C   . ASP A 1 41  ? 196.983 188.444 90.997  1.00 52.33  ? 34  ASP B C   1 
ATOM   90   O O   . ASP A 1 41  ? 196.165 187.613 90.586  1.00 51.90  ? 34  ASP B O   1 
ATOM   91   C CB  . ASP A 1 41  ? 199.210 188.698 89.876  1.00 58.12  ? 34  ASP B CB  1 
ATOM   92   C CG  . ASP A 1 41  ? 199.942 189.248 88.672  1.00 64.97  ? 34  ASP B CG  1 
ATOM   93   O OD1 . ASP A 1 41  ? 199.810 188.663 87.576  1.00 69.44  ? 34  ASP B OD1 1 
ATOM   94   O OD2 . ASP A 1 41  ? 200.648 190.267 88.819  1.00 62.13  ? 34  ASP B OD2 1 
ATOM   95   N N   . TYR A 1 42  ? 197.187 188.656 92.296  1.00 47.65  ? 35  TYR B N   1 
ATOM   96   C CA  . TYR A 1 42  ? 196.423 187.996 93.352  1.00 44.42  ? 35  TYR B CA  1 
ATOM   97   C C   . TYR A 1 42  ? 195.897 189.096 94.266  1.00 45.49  ? 35  TYR B C   1 
ATOM   98   O O   . TYR A 1 42  ? 196.673 189.848 94.858  1.00 51.15  ? 35  TYR B O   1 
ATOM   99   C CB  . TYR A 1 42  ? 197.277 186.986 94.103  1.00 41.40  ? 35  TYR B CB  1 
ATOM   100  C CG  . TYR A 1 42  ? 197.678 185.794 93.270  1.00 45.81  ? 35  TYR B CG  1 
ATOM   101  C CD1 . TYR A 1 42  ? 196.782 184.767 93.021  1.00 45.03  ? 35  TYR B CD1 1 
ATOM   102  C CD2 . TYR A 1 42  ? 198.948 185.702 92.722  1.00 47.92  ? 35  TYR B CD2 1 
ATOM   103  C CE1 . TYR A 1 42  ? 197.140 183.679 92.260  1.00 50.10  ? 35  TYR B CE1 1 
ATOM   104  C CE2 . TYR A 1 42  ? 199.314 184.618 91.959  1.00 46.42  ? 35  TYR B CE2 1 
ATOM   105  C CZ  . TYR A 1 42  ? 198.407 183.609 91.731  1.00 54.92  ? 35  TYR B CZ  1 
ATOM   106  O OH  . TYR A 1 42  ? 198.769 182.523 90.968  1.00 65.60  ? 35  TYR B OH  1 
ATOM   107  N N   . VAL A 1 43  ? 194.572 189.200 94.363  1.00 41.69  ? 36  VAL B N   1 
ATOM   108  C CA  . VAL A 1 43  ? 193.975 190.240 95.188  1.00 41.55  ? 36  VAL B CA  1 
ATOM   109  C C   . VAL A 1 43  ? 193.666 189.693 96.578  1.00 35.18  ? 36  VAL B C   1 
ATOM   110  O O   . VAL A 1 43  ? 193.097 188.613 96.745  1.00 38.33  ? 36  VAL B O   1 
ATOM   111  C CB  . VAL A 1 43  ? 192.713 190.804 94.514  1.00 46.79  ? 36  VAL B CB  1 
ATOM   112  C CG1 . VAL A 1 43  ? 191.988 191.759 95.442  1.00 40.82  ? 36  VAL B CG1 1 
ATOM   113  C CG2 . VAL A 1 43  ? 193.078 191.496 93.213  1.00 51.04  ? 36  VAL B CG2 1 
ATOM   114  N N   . LEU A 1 44  ? 194.063 190.453 97.590  1.00 37.50  ? 37  LEU B N   1 
ATOM   115  C CA  . LEU A 1 44  ? 193.753 190.147 98.975  1.00 35.35  ? 37  LEU B CA  1 
ATOM   116  C C   . LEU A 1 44  ? 192.411 190.754 99.356  1.00 35.65  ? 37  LEU B C   1 
ATOM   117  O O   . LEU A 1 44  ? 191.868 191.607 98.654  1.00 49.77  ? 37  LEU B O   1 
ATOM   118  C CB  . LEU A 1 44  ? 194.846 190.666 99.912  1.00 35.95  ? 37  LEU B CB  1 
ATOM   119  C CG  . LEU A 1 44  ? 196.008 189.706 100.141 1.00 33.99  ? 37  LEU B CG  1 
ATOM   120  C CD1 . LEU A 1 44  ? 197.171 190.399 100.818 1.00 32.75  ? 37  LEU B CD1 1 
ATOM   121  C CD2 . LEU A 1 44  ? 195.515 188.558 100.983 1.00 30.84  ? 37  LEU B CD2 1 
ATOM   122  N N   . GLY A 1 45  ? 191.868 190.287 100.472 1.00 30.01  ? 38  GLY B N   1 
ATOM   123  C CA  . GLY A 1 45  ? 190.644 190.826 101.011 1.00 27.74  ? 38  GLY B CA  1 
ATOM   124  C C   . GLY A 1 45  ? 190.872 191.444 102.375 1.00 31.53  ? 38  GLY B C   1 
ATOM   125  O O   . GLY A 1 45  ? 191.779 191.076 103.111 1.00 42.49  ? 38  GLY B O   1 
ATOM   126  N N   . GLY A 1 46  ? 190.026 192.411 102.702 1.00 30.21  ? 39  GLY B N   1 
ATOM   127  C CA  . GLY A 1 46  ? 190.171 193.109 103.961 1.00 27.42  ? 39  GLY B CA  1 
ATOM   128  C C   . GLY A 1 46  ? 188.856 193.368 104.657 1.00 33.37  ? 39  GLY B C   1 
ATOM   129  O O   . GLY A 1 46  ? 187.893 193.821 104.035 1.00 43.93  ? 39  GLY B O   1 
ATOM   130  N N   . LEU A 1 47  ? 188.800 193.071 105.951 1.00 25.95  ? 40  LEU B N   1 
ATOM   131  C CA  . LEU A 1 47  ? 187.632 193.361 106.775 1.00 32.18  ? 40  LEU B CA  1 
ATOM   132  C C   . LEU A 1 47  ? 188.099 194.205 107.951 1.00 35.71  ? 40  LEU B C   1 
ATOM   133  O O   . LEU A 1 47  ? 188.654 193.674 108.917 1.00 35.34  ? 40  LEU B O   1 
ATOM   134  C CB  . LEU A 1 47  ? 186.952 192.077 107.252 1.00 34.22  ? 40  LEU B CB  1 
ATOM   135  C CG  . LEU A 1 47  ? 186.495 191.082 106.181 1.00 35.66  ? 40  LEU B CG  1 
ATOM   136  C CD1 . LEU A 1 47  ? 185.925 189.832 106.822 1.00 36.41  ? 40  LEU B CD1 1 
ATOM   137  C CD2 . LEU A 1 47  ? 185.482 191.710 105.238 1.00 28.64  ? 40  LEU B CD2 1 
ATOM   138  N N   . PHE A 1 48  ? 187.873 195.511 107.872 1.00 39.59  ? 41  PHE B N   1 
ATOM   139  C CA  . PHE A 1 48  ? 188.323 196.448 108.888 1.00 41.66  ? 41  PHE B CA  1 
ATOM   140  C C   . PHE A 1 48  ? 187.141 197.254 109.400 1.00 45.12  ? 41  PHE B C   1 
ATOM   141  O O   . PHE A 1 48  ? 186.197 197.520 108.651 1.00 49.08  ? 41  PHE B O   1 
ATOM   142  C CB  . PHE A 1 48  ? 189.391 197.406 108.335 1.00 35.46  ? 41  PHE B CB  1 
ATOM   143  C CG  . PHE A 1 48  ? 190.585 196.711 107.743 1.00 33.87  ? 41  PHE B CG  1 
ATOM   144  C CD1 . PHE A 1 48  ? 190.561 196.249 106.442 1.00 37.58  ? 41  PHE B CD1 1 
ATOM   145  C CD2 . PHE A 1 48  ? 191.729 196.520 108.489 1.00 35.18  ? 41  PHE B CD2 1 
ATOM   146  C CE1 . PHE A 1 48  ? 191.655 195.612 105.905 1.00 35.76  ? 41  PHE B CE1 1 
ATOM   147  C CE2 . PHE A 1 48  ? 192.820 195.877 107.955 1.00 31.57  ? 41  PHE B CE2 1 
ATOM   148  C CZ  . PHE A 1 48  ? 192.783 195.425 106.663 1.00 31.87  ? 41  PHE B CZ  1 
ATOM   149  N N   . PRO A 1 49  ? 187.162 197.654 110.674 1.00 44.29  ? 42  PRO B N   1 
ATOM   150  C CA  . PRO A 1 49  ? 186.082 198.490 111.227 1.00 46.93  ? 42  PRO B CA  1 
ATOM   151  C C   . PRO A 1 49  ? 186.246 199.961 110.857 1.00 53.92  ? 42  PRO B C   1 
ATOM   152  O O   . PRO A 1 49  ? 186.537 200.816 111.696 1.00 61.47  ? 42  PRO B O   1 
ATOM   153  C CB  . PRO A 1 49  ? 186.213 198.244 112.738 1.00 44.74  ? 42  PRO B CB  1 
ATOM   154  C CG  . PRO A 1 49  ? 187.266 197.186 112.912 1.00 47.42  ? 42  PRO B CG  1 
ATOM   155  C CD  . PRO A 1 49  ? 188.124 197.260 111.711 1.00 45.32  ? 42  PRO B CD  1 
ATOM   156  N N   . LEU A 1 50  ? 186.061 200.261 109.571 1.00 52.16  ? 43  LEU B N   1 
ATOM   157  C CA  . LEU A 1 50  ? 186.266 201.621 109.086 1.00 56.31  ? 43  LEU B CA  1 
ATOM   158  C C   . LEU A 1 50  ? 185.225 202.578 109.653 1.00 67.72  ? 43  LEU B C   1 
ATOM   159  O O   . LEU A 1 50  ? 185.534 203.737 109.952 1.00 70.07  ? 43  LEU B O   1 
ATOM   160  C CB  . LEU A 1 50  ? 186.240 201.635 107.560 1.00 58.63  ? 43  LEU B CB  1 
ATOM   161  C CG  . LEU A 1 50  ? 187.403 200.920 106.877 1.00 51.08  ? 43  LEU B CG  1 
ATOM   162  C CD1 . LEU A 1 50  ? 187.191 200.858 105.381 1.00 56.47  ? 43  LEU B CD1 1 
ATOM   163  C CD2 . LEU A 1 50  ? 188.693 201.633 107.193 1.00 50.48  ? 43  LEU B CD2 1 
ATOM   164  N N   . GLY A 1 51  ? 183.985 202.114 109.806 1.00 72.71  ? 44  GLY B N   1 
ATOM   165  C CA  . GLY A 1 51  ? 182.920 202.956 110.297 1.00 77.47  ? 44  GLY B CA  1 
ATOM   166  C C   . GLY A 1 51  ? 182.235 202.344 111.503 1.00 78.31  ? 44  GLY B C   1 
ATOM   167  O O   . GLY A 1 51  ? 182.478 201.197 111.875 1.00 74.53  ? 44  GLY B O   1 
ATOM   168  N N   . GLU A 1 52  ? 181.369 203.146 112.117 1.00 83.34  ? 45  GLU B N   1 
ATOM   169  C CA  . GLU A 1 52  ? 180.557 202.728 113.249 1.00 87.20  ? 45  GLU B CA  1 
ATOM   170  C C   . GLU A 1 52  ? 179.114 203.156 113.016 1.00 92.28  ? 45  GLU B C   1 
ATOM   171  O O   . GLU A 1 52  ? 178.827 204.048 112.214 1.00 93.29  ? 45  GLU B O   1 
ATOM   172  C CB  . GLU A 1 52  ? 181.077 203.309 114.572 1.00 87.81  ? 45  GLU B CB  1 
ATOM   173  C CG  . GLU A 1 52  ? 182.588 203.438 114.656 1.00 90.46  ? 45  GLU B CG  1 
ATOM   174  C CD  . GLU A 1 52  ? 183.039 204.289 115.826 1.00 94.96  ? 45  GLU B CD  1 
ATOM   175  O OE1 . GLU A 1 52  ? 182.184 204.960 116.441 1.00 94.92  ? 45  GLU B OE1 1 
ATOM   176  O OE2 . GLU A 1 52  ? 184.248 204.282 116.134 1.00 96.61  ? 45  GLU B OE2 1 
ATOM   177  N N   . ALA A 1 53  ? 178.202 202.500 113.726 1.00 88.72  ? 46  ALA B N   1 
ATOM   178  C CA  . ALA A 1 53  ? 176.778 202.783 113.596 1.00 91.26  ? 46  ALA B CA  1 
ATOM   179  C C   . ALA A 1 53  ? 176.444 204.188 114.089 1.00 93.92  ? 46  ALA B C   1 
ATOM   180  O O   . ALA A 1 53  ? 175.354 204.701 113.839 1.00 88.20  ? 46  ALA B O   1 
ATOM   181  C CB  . ALA A 1 53  ? 175.963 201.750 114.355 1.00 85.05  ? 46  ALA B CB  1 
ATOM   182  N N   . ARG A 1 61  ? 165.210 196.790 111.570 1.00 70.13  ? 54  ARG B N   1 
ATOM   183  C CA  . ARG A 1 61  ? 165.000 196.870 110.128 1.00 76.79  ? 54  ARG B CA  1 
ATOM   184  C C   . ARG A 1 61  ? 163.840 195.988 109.679 1.00 81.57  ? 54  ARG B C   1 
ATOM   185  O O   . ARG A 1 61  ? 163.730 194.831 110.085 1.00 74.68  ? 54  ARG B O   1 
ATOM   186  C CB  . ARG A 1 61  ? 166.277 196.479 109.381 1.00 77.78  ? 54  ARG B CB  1 
ATOM   187  C CG  . ARG A 1 61  ? 167.138 195.468 110.114 1.00 81.13  ? 54  ARG B CG  1 
ATOM   188  C CD  . ARG A 1 61  ? 168.508 195.340 109.470 1.00 79.96  ? 54  ARG B CD  1 
ATOM   189  N NE  . ARG A 1 61  ? 168.442 194.705 108.160 1.00 80.49  ? 54  ARG B NE  1 
ATOM   190  C CZ  . ARG A 1 61  ? 168.614 193.407 107.951 1.00 67.64  ? 54  ARG B CZ  1 
ATOM   191  N NH1 . ARG A 1 61  ? 168.867 192.576 108.947 1.00 59.51  ? 54  ARG B NH1 1 
ATOM   192  N NH2 . ARG A 1 61  ? 168.533 192.932 106.712 1.00 60.65  ? 54  ARG B NH2 1 
ATOM   193  N N   . THR A 1 62  ? 162.976 196.550 108.839 1.00 81.39  ? 55  THR B N   1 
ATOM   194  C CA  . THR A 1 62  ? 161.832 195.839 108.289 1.00 78.47  ? 55  THR B CA  1 
ATOM   195  C C   . THR A 1 62  ? 162.110 195.269 106.903 1.00 73.39  ? 55  THR B C   1 
ATOM   196  O O   . THR A 1 62  ? 161.630 194.176 106.588 1.00 70.57  ? 55  THR B O   1 
ATOM   197  C CB  . THR A 1 62  ? 160.611 196.774 108.250 1.00 85.71  ? 55  THR B CB  1 
ATOM   198  O OG1 . THR A 1 62  ? 160.000 196.818 109.545 1.00 73.30  ? 55  THR B OG1 1 
ATOM   199  C CG2 . THR A 1 62  ? 159.580 196.313 107.226 1.00 82.80  ? 55  THR B CG2 1 
ATOM   200  N N   . ARG A 1 63  ? 162.897 195.958 106.091 1.00 70.33  ? 56  ARG B N   1 
ATOM   201  C CA  . ARG A 1 63  ? 163.280 195.520 104.760 1.00 68.66  ? 56  ARG B CA  1 
ATOM   202  C C   . ARG A 1 63  ? 164.665 194.900 104.821 1.00 66.03  ? 56  ARG B C   1 
ATOM   203  O O   . ARG A 1 63  ? 165.462 195.228 105.705 1.00 64.68  ? 56  ARG B O   1 
ATOM   204  C CB  . ARG A 1 63  ? 163.283 196.692 103.767 1.00 68.97  ? 56  ARG B CB  1 
ATOM   205  C CG  . ARG A 1 63  ? 162.179 197.709 103.978 1.00 69.95  ? 56  ARG B CG  1 
ATOM   206  C CD  . ARG A 1 63  ? 160.835 197.150 103.557 1.00 72.74  ? 56  ARG B CD  1 
ATOM   207  N NE  . ARG A 1 63  ? 160.736 197.033 102.108 1.00 75.93  ? 56  ARG B NE  1 
ATOM   208  C CZ  . ARG A 1 63  ? 160.445 198.036 101.293 1.00 70.45  ? 56  ARG B CZ  1 
ATOM   209  N NH1 . ARG A 1 63  ? 160.203 199.253 101.753 1.00 65.56  ? 56  ARG B NH1 1 
ATOM   210  N NH2 . ARG A 1 63  ? 160.396 197.814 99.982  1.00 65.68  ? 56  ARG B NH2 1 
ATOM   211  N N   . PRO A 1 64  ? 164.980 193.988 103.900 1.00 61.49  ? 57  PRO B N   1 
ATOM   212  C CA  . PRO A 1 64  ? 166.331 193.387 103.868 1.00 62.59  ? 57  PRO B CA  1 
ATOM   213  C C   . PRO A 1 64  ? 167.358 194.314 103.228 1.00 72.56  ? 57  PRO B C   1 
ATOM   214  O O   . PRO A 1 64  ? 167.940 194.044 102.174 1.00 76.25  ? 57  PRO B O   1 
ATOM   215  C CB  . PRO A 1 64  ? 166.106 192.105 103.056 1.00 59.25  ? 57  PRO B CB  1 
ATOM   216  C CG  . PRO A 1 64  ? 164.626 191.997 102.825 1.00 54.22  ? 57  PRO B CG  1 
ATOM   217  C CD  . PRO A 1 64  ? 164.087 193.369 102.913 1.00 59.02  ? 57  PRO B CD  1 
ATOM   218  N N   . SER A 1 65  ? 167.599 195.445 103.882 1.00 76.05  ? 58  SER B N   1 
ATOM   219  C CA  . SER A 1 65  ? 168.542 196.446 103.412 1.00 77.26  ? 58  SER B CA  1 
ATOM   220  C C   . SER A 1 65  ? 169.773 196.436 104.304 1.00 78.94  ? 58  SER B C   1 
ATOM   221  O O   . SER A 1 65  ? 169.662 196.466 105.533 1.00 80.64  ? 58  SER B O   1 
ATOM   222  C CB  . SER A 1 65  ? 167.911 197.843 103.401 1.00 74.59  ? 58  SER B CB  1 
ATOM   223  O OG  . SER A 1 65  ? 167.772 198.359 104.714 1.00 75.28  ? 58  SER B OG  1 
ATOM   224  N N   . SER A 1 66  ? 170.942 196.387 103.680 1.00 84.16  ? 59  SER B N   1 
ATOM   225  C CA  . SER A 1 66  ? 172.191 196.373 104.428 1.00 86.03  ? 59  SER B CA  1 
ATOM   226  C C   . SER A 1 66  ? 172.412 197.733 105.075 1.00 84.42  ? 59  SER B C   1 
ATOM   227  O O   . SER A 1 66  ? 172.384 198.751 104.374 1.00 80.50  ? 59  SER B O   1 
ATOM   228  C CB  . SER A 1 66  ? 173.358 196.025 103.513 1.00 87.55  ? 59  SER B CB  1 
ATOM   229  O OG  . SER A 1 66  ? 173.192 196.614 102.236 1.00 91.08  ? 59  SER B OG  1 
ATOM   230  N N   . PRO A 1 67  ? 172.615 197.801 106.389 1.00 89.12  ? 60  PRO B N   1 
ATOM   231  C CA  . PRO A 1 67  ? 172.826 199.100 107.032 1.00 90.12  ? 60  PRO B CA  1 
ATOM   232  C C   . PRO A 1 67  ? 174.130 199.736 106.577 1.00 91.54  ? 60  PRO B C   1 
ATOM   233  O O   . PRO A 1 67  ? 175.090 199.051 106.220 1.00 90.12  ? 60  PRO B O   1 
ATOM   234  C CB  . PRO A 1 67  ? 172.857 198.757 108.525 1.00 82.55  ? 60  PRO B CB  1 
ATOM   235  C CG  . PRO A 1 67  ? 173.276 197.331 108.571 1.00 82.94  ? 60  PRO B CG  1 
ATOM   236  C CD  . PRO A 1 67  ? 172.691 196.687 107.349 1.00 83.06  ? 60  PRO B CD  1 
ATOM   237  N N   . VAL A 1 68  ? 174.151 201.064 106.586 1.00 95.77  ? 61  VAL B N   1 
ATOM   238  C CA  . VAL A 1 68  ? 175.318 201.838 106.183 1.00 101.48 ? 61  VAL B CA  1 
ATOM   239  C C   . VAL A 1 68  ? 175.836 202.613 107.388 1.00 99.36  ? 61  VAL B C   1 
ATOM   240  O O   . VAL A 1 68  ? 175.075 203.304 108.075 1.00 94.57  ? 61  VAL B O   1 
ATOM   241  C CB  . VAL A 1 68  ? 174.995 202.775 105.002 1.00 99.19  ? 61  VAL B CB  1 
ATOM   242  C CG1 . VAL A 1 68  ? 174.737 201.960 103.746 1.00 93.66  ? 61  VAL B CG1 1 
ATOM   243  C CG2 . VAL A 1 68  ? 173.783 203.642 105.313 1.00 97.04  ? 61  VAL B CG2 1 
ATOM   244  N N   . CYS A 1 69  ? 177.132 202.479 107.652 1.00 96.04  ? 62  CYS B N   1 
ATOM   245  C CA  . CYS A 1 69  ? 177.782 203.154 108.766 1.00 95.04  ? 62  CYS B CA  1 
ATOM   246  C C   . CYS A 1 69  ? 178.414 204.446 108.269 1.00 101.02 ? 62  CYS B C   1 
ATOM   247  O O   . CYS A 1 69  ? 179.323 204.418 107.434 1.00 100.57 ? 62  CYS B O   1 
ATOM   248  C CB  . CYS A 1 69  ? 178.844 202.259 109.407 1.00 93.54  ? 62  CYS B CB  1 
ATOM   249  S SG  . CYS A 1 69  ? 178.203 200.873 110.382 1.00 97.73  ? 62  CYS B SG  1 
ATOM   250  N N   . THR A 1 70  ? 177.929 205.574 108.785 1.00 103.38 ? 63  THR B N   1 
ATOM   251  C CA  . THR A 1 70  ? 178.443 206.888 108.425 1.00 102.45 ? 63  THR B CA  1 
ATOM   252  C C   . THR A 1 70  ? 179.486 207.408 109.402 1.00 98.70  ? 63  THR B C   1 
ATOM   253  O O   . THR A 1 70  ? 180.401 208.123 108.989 1.00 101.08 ? 63  THR B O   1 
ATOM   254  C CB  . THR A 1 70  ? 177.287 207.896 108.327 1.00 104.56 ? 63  THR B CB  1 
ATOM   255  O OG1 . THR A 1 70  ? 176.354 207.453 107.334 1.00 105.72 ? 63  THR B OG1 1 
ATOM   256  C CG2 . THR A 1 70  ? 177.791 209.280 107.939 1.00 100.31 ? 63  THR B CG2 1 
ATOM   257  N N   . ARG A 1 71  ? 179.385 207.038 110.676 1.00 93.83  ? 64  ARG B N   1 
ATOM   258  C CA  . ARG A 1 71  ? 180.369 207.442 111.670 1.00 91.94  ? 64  ARG B CA  1 
ATOM   259  C C   . ARG A 1 71  ? 181.743 206.895 111.307 1.00 91.42  ? 64  ARG B C   1 
ATOM   260  O O   . ARG A 1 71  ? 181.863 205.836 110.688 1.00 94.61  ? 64  ARG B O   1 
ATOM   261  C CB  . ARG A 1 71  ? 179.947 206.948 113.051 1.00 92.79  ? 64  ARG B CB  1 
ATOM   262  C CG  . ARG A 1 71  ? 180.784 207.472 114.200 1.00 95.65  ? 64  ARG B CG  1 
ATOM   263  C CD  . ARG A 1 71  ? 179.909 208.113 115.258 1.00 101.03 ? 64  ARG B CD  1 
ATOM   264  N NE  . ARG A 1 71  ? 178.662 207.384 115.447 1.00 103.41 ? 64  ARG B NE  1 
ATOM   265  C CZ  . ARG A 1 71  ? 177.458 207.892 115.223 1.00 106.37 ? 64  ARG B CZ  1 
ATOM   266  N NH1 . ARG A 1 71  ? 177.300 209.135 114.799 1.00 106.15 ? 64  ARG B NH1 1 
ATOM   267  N NH2 . ARG A 1 71  ? 176.385 207.133 115.430 1.00 101.44 ? 64  ARG B NH2 1 
ATOM   268  N N   . PHE A 1 72  ? 182.784 207.633 111.679 1.00 87.61  ? 65  PHE B N   1 
ATOM   269  C CA  . PHE A 1 72  ? 184.151 207.295 111.312 1.00 83.27  ? 65  PHE B CA  1 
ATOM   270  C C   . PHE A 1 72  ? 184.886 206.700 112.506 1.00 86.34  ? 65  PHE B C   1 
ATOM   271  O O   . PHE A 1 72  ? 184.792 207.210 113.626 1.00 86.38  ? 65  PHE B O   1 
ATOM   272  C CB  . PHE A 1 72  ? 184.878 208.536 110.776 1.00 87.35  ? 65  PHE B CB  1 
ATOM   273  C CG  . PHE A 1 72  ? 186.385 208.468 110.857 1.00 89.30  ? 65  PHE B CG  1 
ATOM   274  C CD1 . PHE A 1 72  ? 187.061 208.742 112.037 1.00 88.09  ? 65  PHE B CD1 1 
ATOM   275  C CD2 . PHE A 1 72  ? 187.127 208.220 109.717 1.00 89.62  ? 65  PHE B CD2 1 
ATOM   276  C CE1 . PHE A 1 72  ? 188.436 208.689 112.092 1.00 85.69  ? 65  PHE B CE1 1 
ATOM   277  C CE2 . PHE A 1 72  ? 188.505 208.173 109.766 1.00 84.59  ? 65  PHE B CE2 1 
ATOM   278  C CZ  . PHE A 1 72  ? 189.160 208.411 110.956 1.00 81.34  ? 65  PHE B CZ  1 
ATOM   279  N N   . SER A 1 73  ? 185.637 205.630 112.253 1.00 84.83  ? 66  SER B N   1 
ATOM   280  C CA  . SER A 1 73  ? 186.466 204.978 113.259 1.00 76.47  ? 66  SER B CA  1 
ATOM   281  C C   . SER A 1 73  ? 187.924 205.077 112.839 1.00 70.32  ? 66  SER B C   1 
ATOM   282  O O   . SER A 1 73  ? 188.280 204.684 111.724 1.00 70.41  ? 66  SER B O   1 
ATOM   283  C CB  . SER A 1 73  ? 186.063 203.515 113.442 1.00 71.91  ? 66  SER B CB  1 
ATOM   284  O OG  . SER A 1 73  ? 186.901 202.871 114.385 1.00 68.72  ? 66  SER B OG  1 
ATOM   285  N N   . SER A 1 74  ? 188.764 205.603 113.733 1.00 67.04  ? 67  SER B N   1 
ATOM   286  C CA  . SER A 1 74  ? 190.166 205.832 113.402 1.00 67.87  ? 67  SER B CA  1 
ATOM   287  C C   . SER A 1 74  ? 190.978 204.545 113.387 1.00 65.85  ? 67  SER B C   1 
ATOM   288  O O   . SER A 1 74  ? 191.879 204.401 112.553 1.00 63.02  ? 67  SER B O   1 
ATOM   289  C CB  . SER A 1 74  ? 190.783 206.825 114.387 1.00 73.74  ? 67  SER B CB  1 
ATOM   290  O OG  . SER A 1 74  ? 191.376 206.153 115.484 1.00 69.88  ? 67  SER B OG  1 
ATOM   291  N N   . ASN A 1 75  ? 190.684 203.609 114.293 1.00 65.18  ? 68  ASN B N   1 
ATOM   292  C CA  . ASN A 1 75  ? 191.432 202.357 114.329 1.00 54.45  ? 68  ASN B CA  1 
ATOM   293  C C   . ASN A 1 75  ? 191.243 201.561 113.047 1.00 50.76  ? 68  ASN B C   1 
ATOM   294  O O   . ASN A 1 75  ? 192.194 200.960 112.538 1.00 56.34  ? 68  ASN B O   1 
ATOM   295  C CB  . ASN A 1 75  ? 191.013 201.521 115.536 1.00 55.56  ? 68  ASN B CB  1 
ATOM   296  C CG  . ASN A 1 75  ? 191.721 201.935 116.804 1.00 60.09  ? 68  ASN B CG  1 
ATOM   297  O OD1 . ASN A 1 75  ? 192.839 202.448 116.765 1.00 60.76  ? 68  ASN B OD1 1 
ATOM   298  N ND2 . ASN A 1 75  ? 191.079 201.702 117.942 1.00 63.43  ? 68  ASN B ND2 1 
ATOM   299  N N   . GLY A 1 76  ? 190.020 201.526 112.521 1.00 47.07  ? 69  GLY B N   1 
ATOM   300  C CA  . GLY A 1 76  ? 189.789 200.804 111.283 1.00 45.37  ? 69  GLY B CA  1 
ATOM   301  C C   . GLY A 1 76  ? 190.601 201.358 110.130 1.00 47.38  ? 69  GLY B C   1 
ATOM   302  O O   . GLY A 1 76  ? 191.205 200.603 109.364 1.00 49.18  ? 69  GLY B O   1 
ATOM   303  N N   . LEU A 1 77  ? 190.638 202.685 109.998 1.00 50.86  ? 70  LEU B N   1 
ATOM   304  C CA  . LEU A 1 77  ? 191.432 203.301 108.942 1.00 52.12  ? 70  LEU B CA  1 
ATOM   305  C C   . LEU A 1 77  ? 192.920 203.068 109.161 1.00 48.89  ? 70  LEU B C   1 
ATOM   306  O O   . LEU A 1 77  ? 193.668 202.851 108.204 1.00 53.40  ? 70  LEU B O   1 
ATOM   307  C CB  . LEU A 1 77  ? 191.133 204.795 108.863 1.00 59.59  ? 70  LEU B CB  1 
ATOM   308  C CG  . LEU A 1 77  ? 192.013 205.578 107.889 1.00 64.21  ? 70  LEU B CG  1 
ATOM   309  C CD1 . LEU A 1 77  ? 191.730 205.163 106.454 1.00 64.07  ? 70  LEU B CD1 1 
ATOM   310  C CD2 . LEU A 1 77  ? 191.815 207.066 108.072 1.00 67.44  ? 70  LEU B CD2 1 
ATOM   311  N N   . LEU A 1 78  ? 193.370 203.111 110.416 1.00 50.51  ? 71  LEU B N   1 
ATOM   312  C CA  . LEU A 1 78  ? 194.779 202.862 110.700 1.00 50.41  ? 71  LEU B CA  1 
ATOM   313  C C   . LEU A 1 78  ? 195.175 201.441 110.330 1.00 51.10  ? 71  LEU B C   1 
ATOM   314  O O   . LEU A 1 78  ? 196.251 201.212 109.768 1.00 55.25  ? 71  LEU B O   1 
ATOM   315  C CB  . LEU A 1 78  ? 195.068 203.136 112.172 1.00 57.94  ? 71  LEU B CB  1 
ATOM   316  C CG  . LEU A 1 78  ? 195.236 204.624 112.469 1.00 63.42  ? 71  LEU B CG  1 
ATOM   317  C CD1 . LEU A 1 78  ? 195.099 204.908 113.950 1.00 68.27  ? 71  LEU B CD1 1 
ATOM   318  C CD2 . LEU A 1 78  ? 196.570 205.103 111.941 1.00 60.36  ? 71  LEU B CD2 1 
ATOM   319  N N   . TRP A 1 79  ? 194.311 200.472 110.627 1.00 51.37  ? 72  TRP B N   1 
ATOM   320  C CA  . TRP A 1 79  ? 194.606 199.085 110.288 1.00 38.38  ? 72  TRP B CA  1 
ATOM   321  C C   . TRP A 1 79  ? 194.537 198.855 108.783 1.00 36.54  ? 72  TRP B C   1 
ATOM   322  O O   . TRP A 1 79  ? 195.339 198.096 108.225 1.00 42.96  ? 72  TRP B O   1 
ATOM   323  C CB  . TRP A 1 79  ? 193.648 198.168 111.036 1.00 35.10  ? 72  TRP B CB  1 
ATOM   324  C CG  . TRP A 1 79  ? 193.780 198.311 112.515 1.00 43.37  ? 72  TRP B CG  1 
ATOM   325  C CD1 . TRP A 1 79  ? 194.889 198.710 113.197 1.00 45.27  ? 72  TRP B CD1 1 
ATOM   326  C CD2 . TRP A 1 79  ? 192.768 198.073 113.497 1.00 45.88  ? 72  TRP B CD2 1 
ATOM   327  N NE1 . TRP A 1 79  ? 194.635 198.728 114.543 1.00 46.01  ? 72  TRP B NE1 1 
ATOM   328  C CE2 . TRP A 1 79  ? 193.340 198.341 114.755 1.00 46.18  ? 72  TRP B CE2 1 
ATOM   329  C CE3 . TRP A 1 79  ? 191.437 197.656 113.437 1.00 44.73  ? 72  TRP B CE3 1 
ATOM   330  C CZ2 . TRP A 1 79  ? 192.627 198.205 115.941 1.00 51.33  ? 72  TRP B CZ2 1 
ATOM   331  C CZ3 . TRP A 1 79  ? 190.733 197.522 114.615 1.00 43.30  ? 72  TRP B CZ3 1 
ATOM   332  C CH2 . TRP A 1 79  ? 191.327 197.795 115.850 1.00 49.57  ? 72  TRP B CH2 1 
ATOM   333  N N   . ALA A 1 80  ? 193.593 199.510 108.106 1.00 39.02  ? 73  ALA B N   1 
ATOM   334  C CA  . ALA A 1 80  ? 193.555 199.441 106.651 1.00 38.45  ? 73  ALA B CA  1 
ATOM   335  C C   . ALA A 1 80  ? 194.828 200.015 106.044 1.00 43.47  ? 73  ALA B C   1 
ATOM   336  O O   . ALA A 1 80  ? 195.373 199.462 105.082 1.00 53.67  ? 73  ALA B O   1 
ATOM   337  C CB  . ALA A 1 80  ? 192.324 200.176 106.124 1.00 35.73  ? 73  ALA B CB  1 
ATOM   338  N N   . LEU A 1 81  ? 195.325 201.119 106.602 1.00 39.82  ? 74  LEU B N   1 
ATOM   339  C CA  . LEU A 1 81  ? 196.560 201.709 106.099 1.00 40.99  ? 74  LEU B CA  1 
ATOM   340  C C   . LEU A 1 81  ? 197.762 200.829 106.415 1.00 43.49  ? 74  LEU B C   1 
ATOM   341  O O   . LEU A 1 81  ? 198.726 200.792 105.646 1.00 52.29  ? 74  LEU B O   1 
ATOM   342  C CB  . LEU A 1 81  ? 196.747 203.109 106.679 1.00 50.81  ? 74  LEU B CB  1 
ATOM   343  C CG  . LEU A 1 81  ? 195.918 204.208 106.014 1.00 47.90  ? 74  LEU B CG  1 
ATOM   344  C CD1 . LEU A 1 81  ? 195.913 205.459 106.866 1.00 48.93  ? 74  LEU B CD1 1 
ATOM   345  C CD2 . LEU A 1 81  ? 196.442 204.506 104.624 1.00 51.15  ? 74  LEU B CD2 1 
ATOM   346  N N   . ALA A 1 82  ? 197.729 200.121 107.546 1.00 41.89  ? 75  ALA B N   1 
ATOM   347  C CA  . ALA A 1 82  ? 198.791 199.164 107.850 1.00 37.58  ? 75  ALA B CA  1 
ATOM   348  C C   . ALA A 1 82  ? 198.823 198.035 106.829 1.00 40.20  ? 75  ALA B C   1 
ATOM   349  O O   . ALA A 1 82  ? 199.896 197.654 106.342 1.00 42.70  ? 75  ALA B O   1 
ATOM   350  C CB  . ALA A 1 82  ? 198.607 198.604 109.259 1.00 35.73  ? 75  ALA B CB  1 
ATOM   351  N N   . MET A 1 83  ? 197.651 197.494 106.486 1.00 42.85  ? 76  MET B N   1 
ATOM   352  C CA  . MET A 1 83  ? 197.579 196.470 105.447 1.00 33.56  ? 76  MET B CA  1 
ATOM   353  C C   . MET A 1 83  ? 198.059 197.012 104.108 1.00 34.06  ? 76  MET B C   1 
ATOM   354  O O   . MET A 1 83  ? 198.767 196.322 103.365 1.00 41.32  ? 76  MET B O   1 
ATOM   355  C CB  . MET A 1 83  ? 196.150 195.949 105.323 1.00 28.19  ? 76  MET B CB  1 
ATOM   356  C CG  . MET A 1 83  ? 195.874 195.198 104.038 1.00 29.11  ? 76  MET B CG  1 
ATOM   357  S SD  . MET A 1 83  ? 194.793 193.790 104.311 1.00 43.92  ? 76  MET B SD  1 
ATOM   358  C CE  . MET A 1 83  ? 194.290 193.406 102.641 1.00 30.44  ? 76  MET B CE  1 
ATOM   359  N N   . LYS A 1 84  ? 197.675 198.246 103.784 1.00 35.39  ? 77  LYS B N   1 
ATOM   360  C CA  . LYS A 1 84  ? 198.103 198.868 102.537 1.00 40.37  ? 77  LYS B CA  1 
ATOM   361  C C   . LYS A 1 84  ? 199.617 199.034 102.488 1.00 43.18  ? 77  LYS B C   1 
ATOM   362  O O   . LYS A 1 84  ? 200.246 198.776 101.454 1.00 49.77  ? 77  LYS B O   1 
ATOM   363  C CB  . LYS A 1 84  ? 197.406 200.216 102.388 1.00 45.77  ? 77  LYS B CB  1 
ATOM   364  C CG  . LYS A 1 84  ? 197.458 200.803 101.010 1.00 57.59  ? 77  LYS B CG  1 
ATOM   365  C CD  . LYS A 1 84  ? 196.397 201.869 100.864 1.00 62.63  ? 77  LYS B CD  1 
ATOM   366  C CE  . LYS A 1 84  ? 197.024 203.238 100.832 1.00 73.40  ? 77  LYS B CE  1 
ATOM   367  N NZ  . LYS A 1 84  ? 198.272 203.245 100.021 1.00 69.05  ? 77  LYS B NZ  1 
ATOM   368  N N   . MET A 1 85  ? 200.217 199.471 103.596 1.00 41.81  ? 78  MET B N   1 
ATOM   369  C CA  . MET A 1 85  ? 201.664 199.631 103.650 1.00 43.42  ? 78  MET B CA  1 
ATOM   370  C C   . MET A 1 85  ? 202.366 198.289 103.506 1.00 48.67  ? 78  MET B C   1 
ATOM   371  O O   . MET A 1 85  ? 203.367 198.177 102.787 1.00 53.37  ? 78  MET B O   1 
ATOM   372  C CB  . MET A 1 85  ? 202.060 200.315 104.958 1.00 46.32  ? 78  MET B CB  1 
ATOM   373  C CG  . MET A 1 85  ? 203.450 199.977 105.458 1.00 50.62  ? 78  MET B CG  1 
ATOM   374  S SD  . MET A 1 85  ? 203.832 200.789 107.019 1.00 65.78  ? 78  MET B SD  1 
ATOM   375  C CE  . MET A 1 85  ? 205.618 200.781 106.974 1.00 63.66  ? 78  MET B CE  1 
ATOM   376  N N   . ALA A 1 86  ? 201.843 197.254 104.169 1.00 47.01  ? 79  ALA B N   1 
ATOM   377  C CA  . ALA A 1 86  ? 202.420 195.922 104.030 1.00 38.89  ? 79  ALA B CA  1 
ATOM   378  C C   . ALA A 1 86  ? 202.366 195.452 102.584 1.00 41.49  ? 79  ALA B C   1 
ATOM   379  O O   . ALA A 1 86  ? 203.364 194.967 102.041 1.00 50.28  ? 79  ALA B O   1 
ATOM   380  C CB  . ALA A 1 86  ? 201.692 194.935 104.940 1.00 33.37  ? 79  ALA B CB  1 
ATOM   381  N N   . VAL A 1 87  ? 201.211 195.611 101.934 1.00 39.36  ? 80  VAL B N   1 
ATOM   382  C CA  . VAL A 1 87  ? 201.058 195.140 100.561 1.00 36.09  ? 80  VAL B CA  1 
ATOM   383  C C   . VAL A 1 87  ? 201.991 195.897 99.625  1.00 40.90  ? 80  VAL B C   1 
ATOM   384  O O   . VAL A 1 87  ? 202.654 195.298 98.769  1.00 48.10  ? 80  VAL B O   1 
ATOM   385  C CB  . VAL A 1 87  ? 199.589 195.260 100.116 1.00 35.65  ? 80  VAL B CB  1 
ATOM   386  C CG1 . VAL A 1 87  ? 199.480 195.171 98.607  1.00 42.95  ? 80  VAL B CG1 1 
ATOM   387  C CG2 . VAL A 1 87  ? 198.745 194.187 100.770 1.00 33.52  ? 80  VAL B CG2 1 
ATOM   388  N N   . GLU A 1 88  ? 202.066 197.221 99.772  1.00 46.78  ? 81  GLU B N   1 
ATOM   389  C CA  . GLU A 1 88  ? 202.904 198.010 98.875  1.00 49.28  ? 81  GLU B CA  1 
ATOM   390  C C   . GLU A 1 88  ? 204.383 197.707 99.077  1.00 52.77  ? 81  GLU B C   1 
ATOM   391  O O   . GLU A 1 88  ? 205.143 197.633 98.105  1.00 55.86  ? 81  GLU B O   1 
ATOM   392  C CB  . GLU A 1 88  ? 202.625 199.498 99.070  1.00 56.32  ? 81  GLU B CB  1 
ATOM   393  C CG  . GLU A 1 88  ? 201.275 199.937 98.531  1.00 66.33  ? 81  GLU B CG  1 
ATOM   394  C CD  . GLU A 1 88  ? 201.043 201.424 98.683  1.00 76.84  ? 81  GLU B CD  1 
ATOM   395  O OE1 . GLU A 1 88  ? 201.837 202.081 99.388  1.00 75.52  ? 81  GLU B OE1 1 
ATOM   396  O OE2 . GLU A 1 88  ? 200.065 201.936 98.099  1.00 78.85  ? 81  GLU B OE2 1 
ATOM   397  N N   . GLU A 1 89  ? 204.817 197.521 100.326 1.00 53.25  ? 82  GLU B N   1 
ATOM   398  C CA  . GLU A 1 89  ? 206.229 197.245 100.553 1.00 60.37  ? 82  GLU B CA  1 
ATOM   399  C C   . GLU A 1 89  ? 206.583 195.804 100.207 1.00 54.38  ? 82  GLU B C   1 
ATOM   400  O O   . GLU A 1 89  ? 207.757 195.497 99.971  1.00 56.96  ? 82  GLU B O   1 
ATOM   401  C CB  . GLU A 1 89  ? 206.600 197.567 101.996 1.00 57.49  ? 82  GLU B CB  1 
ATOM   402  C CG  . GLU A 1 89  ? 206.382 196.437 102.956 1.00 52.63  ? 82  GLU B CG  1 
ATOM   403  C CD  . GLU A 1 89  ? 207.245 196.572 104.180 1.00 61.77  ? 82  GLU B CD  1 
ATOM   404  O OE1 . GLU A 1 89  ? 207.683 195.532 104.705 1.00 66.23  ? 82  GLU B OE1 1 
ATOM   405  O OE2 . GLU A 1 89  ? 207.479 197.715 104.623 1.00 61.84  ? 82  GLU B OE2 1 
ATOM   406  N N   . ILE A 1 90  ? 205.594 194.909 100.180 1.00 50.23  ? 83  ILE B N   1 
ATOM   407  C CA  . ILE A 1 90  ? 205.810 193.579 99.621  1.00 46.50  ? 83  ILE B CA  1 
ATOM   408  C C   . ILE A 1 90  ? 205.960 193.665 98.109  1.00 51.26  ? 83  ILE B C   1 
ATOM   409  O O   . ILE A 1 90  ? 206.804 192.985 97.513  1.00 50.89  ? 83  ILE B O   1 
ATOM   410  C CB  . ILE A 1 90  ? 204.656 192.646 100.027 1.00 41.25  ? 83  ILE B CB  1 
ATOM   411  C CG1 . ILE A 1 90  ? 204.797 192.235 101.488 1.00 38.39  ? 83  ILE B CG1 1 
ATOM   412  C CG2 . ILE A 1 90  ? 204.625 191.413 99.147  1.00 43.30  ? 83  ILE B CG2 1 
ATOM   413  C CD1 . ILE A 1 90  ? 203.578 191.558 102.039 1.00 37.73  ? 83  ILE B CD1 1 
ATOM   414  N N   . ASN A 1 91  ? 205.143 194.504 97.464  1.00 53.52  ? 84  ASN B N   1 
ATOM   415  C CA  . ASN A 1 91  ? 205.272 194.714 96.025  1.00 53.52  ? 84  ASN B CA  1 
ATOM   416  C C   . ASN A 1 91  ? 206.620 195.329 95.677  1.00 57.82  ? 84  ASN B C   1 
ATOM   417  O O   . ASN A 1 91  ? 207.181 195.053 94.610  1.00 57.04  ? 84  ASN B O   1 
ATOM   418  C CB  . ASN A 1 91  ? 204.140 195.603 95.514  1.00 48.66  ? 84  ASN B CB  1 
ATOM   419  C CG  . ASN A 1 91  ? 202.821 194.875 95.435  1.00 53.02  ? 84  ASN B CG  1 
ATOM   420  O OD1 . ASN A 1 91  ? 202.785 193.655 95.304  1.00 55.24  ? 84  ASN B OD1 1 
ATOM   421  N ND2 . ASN A 1 91  ? 201.725 195.621 95.504  1.00 49.69  ? 84  ASN B ND2 1 
ATOM   422  N N   . ASN A 1 92  ? 207.148 196.177 96.560  1.00 61.89  ? 85  ASN B N   1 
ATOM   423  C CA  . ASN A 1 92  ? 208.460 196.768 96.320  1.00 62.19  ? 85  ASN B CA  1 
ATOM   424  C C   . ASN A 1 92  ? 209.561 195.718 96.395  1.00 64.11  ? 85  ASN B C   1 
ATOM   425  O O   . ASN A 1 92  ? 210.576 195.822 95.696  1.00 64.39  ? 85  ASN B O   1 
ATOM   426  C CB  . ASN A 1 92  ? 208.720 197.889 97.324  1.00 69.48  ? 85  ASN B CB  1 
ATOM   427  C CG  . ASN A 1 92  ? 208.469 199.262 96.741  1.00 81.09  ? 85  ASN B CG  1 
ATOM   428  O OD1 . ASN A 1 92  ? 208.031 199.395 95.599  1.00 81.29  ? 85  ASN B OD1 1 
ATOM   429  N ND2 . ASN A 1 92  ? 208.746 200.294 97.525  1.00 85.42  ? 85  ASN B ND2 1 
ATOM   430  N N   . LYS A 1 93  ? 209.382 194.705 97.240  1.00 63.77  ? 86  LYS B N   1 
ATOM   431  C CA  . LYS A 1 93  ? 210.399 193.676 97.414  1.00 59.70  ? 86  LYS B CA  1 
ATOM   432  C C   . LYS A 1 93  ? 210.582 192.870 96.136  1.00 66.87  ? 86  LYS B C   1 
ATOM   433  O O   . LYS A 1 93  ? 209.634 192.646 95.379  1.00 68.74  ? 86  LYS B O   1 
ATOM   434  C CB  . LYS A 1 93  ? 210.017 192.743 98.563  1.00 54.82  ? 86  LYS B CB  1 
ATOM   435  C CG  . LYS A 1 93  ? 210.498 193.201 99.921  1.00 56.42  ? 86  LYS B CG  1 
ATOM   436  C CD  . LYS A 1 93  ? 210.034 192.260 101.014 1.00 52.54  ? 86  LYS B CD  1 
ATOM   437  C CE  . LYS A 1 93  ? 210.863 190.991 101.028 1.00 54.94  ? 86  LYS B CE  1 
ATOM   438  N NZ  . LYS A 1 93  ? 212.293 191.266 101.325 1.00 63.43  ? 86  LYS B NZ  1 
ATOM   439  N N   . SER A 1 94  ? 211.817 192.431 95.900  1.00 71.07  ? 87  SER B N   1 
ATOM   440  C CA  . SER A 1 94  ? 212.149 191.604 94.747  1.00 69.17  ? 87  SER B CA  1 
ATOM   441  C C   . SER A 1 94  ? 212.163 190.117 95.066  1.00 68.97  ? 87  SER B C   1 
ATOM   442  O O   . SER A 1 94  ? 211.670 189.314 94.268  1.00 71.06  ? 87  SER B O   1 
ATOM   443  C CB  . SER A 1 94  ? 213.511 192.012 94.178  1.00 64.81  ? 87  SER B CB  1 
ATOM   444  O OG  . SER A 1 94  ? 213.363 192.943 93.121  1.00 75.13  ? 87  SER B OG  1 
ATOM   445  N N   . ASP A 1 95  ? 212.713 189.729 96.216  1.00 64.00  ? 88  ASP B N   1 
ATOM   446  C CA  . ASP A 1 95  ? 212.852 188.320 96.556  1.00 68.21  ? 88  ASP B CA  1 
ATOM   447  C C   . ASP A 1 95  ? 211.573 187.703 97.105  1.00 72.04  ? 88  ASP B C   1 
ATOM   448  O O   . ASP A 1 95  ? 211.520 186.480 97.273  1.00 72.30  ? 88  ASP B O   1 
ATOM   449  C CB  . ASP A 1 95  ? 213.987 188.135 97.566  1.00 70.62  ? 88  ASP B CB  1 
ATOM   450  C CG  . ASP A 1 95  ? 213.796 188.966 98.817  1.00 76.17  ? 88  ASP B CG  1 
ATOM   451  O OD1 . ASP A 1 95  ? 213.101 188.497 99.743  1.00 72.93  ? 88  ASP B OD1 1 
ATOM   452  O OD2 . ASP A 1 95  ? 214.342 190.088 98.876  1.00 78.72  ? 88  ASP B OD2 1 
ATOM   453  N N   . LEU A 1 96  ? 210.551 188.505 97.391  1.00 63.97  ? 89  LEU B N   1 
ATOM   454  C CA  . LEU A 1 96  ? 209.262 188.005 97.853  1.00 54.16  ? 89  LEU B CA  1 
ATOM   455  C C   . LEU A 1 96  ? 208.226 188.306 96.783  1.00 56.74  ? 89  LEU B C   1 
ATOM   456  O O   . LEU A 1 96  ? 208.048 189.467 96.400  1.00 62.33  ? 89  LEU B O   1 
ATOM   457  C CB  . LEU A 1 96  ? 208.867 188.639 99.187  1.00 50.24  ? 89  LEU B CB  1 
ATOM   458  C CG  . LEU A 1 96  ? 207.481 188.301 99.731  1.00 44.09  ? 89  LEU B CG  1 
ATOM   459  C CD1 . LEU A 1 96  ? 207.350 186.811 99.951  1.00 41.31  ? 89  LEU B CD1 1 
ATOM   460  C CD2 . LEU A 1 96  ? 207.223 189.051 101.022 1.00 41.67  ? 89  LEU B CD2 1 
ATOM   461  N N   . LEU A 1 97  ? 207.549 187.265 96.309  1.00 53.39  ? 90  LEU B N   1 
ATOM   462  C CA  . LEU A 1 97  ? 206.576 187.373 95.227  1.00 54.25  ? 90  LEU B CA  1 
ATOM   463  C C   . LEU A 1 97  ? 207.195 188.069 94.011  1.00 63.38  ? 90  LEU B C   1 
ATOM   464  O O   . LEU A 1 97  ? 206.803 189.190 93.666  1.00 66.50  ? 90  LEU B O   1 
ATOM   465  C CB  . LEU A 1 97  ? 205.326 188.101 95.693  1.00 50.55  ? 90  LEU B CB  1 
ATOM   466  C CG  . LEU A 1 97  ? 204.330 187.285 96.518  1.00 45.21  ? 90  LEU B CG  1 
ATOM   467  C CD1 . LEU A 1 97  ? 203.001 188.001 96.601  1.00 39.70  ? 90  LEU B CD1 1 
ATOM   468  C CD2 . LEU A 1 97  ? 204.149 185.907 95.920  1.00 46.51  ? 90  LEU B CD2 1 
ATOM   469  N N   . PRO A 1 98  ? 208.159 187.438 93.347  1.00 67.39  ? 91  PRO B N   1 
ATOM   470  C CA  . PRO A 1 98  ? 208.878 188.118 92.266  1.00 67.59  ? 91  PRO B CA  1 
ATOM   471  C C   . PRO A 1 98  ? 208.072 188.147 90.979  1.00 66.74  ? 91  PRO B C   1 
ATOM   472  O O   . PRO A 1 98  ? 207.474 187.149 90.571  1.00 73.75  ? 91  PRO B O   1 
ATOM   473  C CB  . PRO A 1 98  ? 210.151 187.274 92.099  1.00 71.71  ? 91  PRO B CB  1 
ATOM   474  C CG  . PRO A 1 98  ? 210.042 186.144 93.103  1.00 72.10  ? 91  PRO B CG  1 
ATOM   475  C CD  . PRO A 1 98  ? 208.618 186.053 93.511  1.00 68.56  ? 91  PRO B CD  1 
ATOM   476  N N   . GLY A 1 99  ? 208.065 189.311 90.338  1.00 65.43  ? 92  GLY B N   1 
ATOM   477  C CA  . GLY A 1 99  ? 207.387 189.466 89.070  1.00 70.21  ? 92  GLY B CA  1 
ATOM   478  C C   . GLY A 1 99  ? 205.880 189.462 89.145  1.00 75.92  ? 92  GLY B C   1 
ATOM   479  O O   . GLY A 1 99  ? 205.225 189.401 88.099  1.00 79.16  ? 92  GLY B O   1 
ATOM   480  N N   . LEU A 1 100 ? 205.306 189.523 90.344  1.00 73.97  ? 93  LEU B N   1 
ATOM   481  C CA  . LEU A 1 100 ? 203.865 189.492 90.529  1.00 70.24  ? 93  LEU B CA  1 
ATOM   482  C C   . LEU A 1 100 ? 203.434 190.655 91.407  1.00 66.34  ? 93  LEU B C   1 
ATOM   483  O O   . LEU A 1 100 ? 204.145 191.036 92.341  1.00 63.57  ? 93  LEU B O   1 
ATOM   484  C CB  . LEU A 1 100 ? 203.415 188.173 91.159  1.00 66.24  ? 93  LEU B CB  1 
ATOM   485  C CG  . LEU A 1 100 ? 203.854 186.906 90.428  1.00 69.42  ? 93  LEU B CG  1 
ATOM   486  C CD1 . LEU A 1 100 ? 203.364 185.687 91.168  1.00 68.79  ? 93  LEU B CD1 1 
ATOM   487  C CD2 . LEU A 1 100 ? 203.341 186.904 88.999  1.00 71.91  ? 93  LEU B CD2 1 
ATOM   488  N N   . ARG A 1 101 ? 202.265 191.209 91.105  1.00 65.58  ? 94  ARG B N   1 
ATOM   489  C CA  . ARG A 1 101 ? 201.689 192.305 91.869  1.00 59.06  ? 94  ARG B CA  1 
ATOM   490  C C   . ARG A 1 101 ? 200.677 191.752 92.860  1.00 55.79  ? 94  ARG B C   1 
ATOM   491  O O   . ARG A 1 101 ? 199.997 190.762 92.574  1.00 57.48  ? 94  ARG B O   1 
ATOM   492  C CB  . ARG A 1 101 ? 201.022 193.325 90.944  1.00 60.81  ? 94  ARG B CB  1 
ATOM   493  C CG  . ARG A 1 101 ? 201.828 194.594 90.740  1.00 62.35  ? 94  ARG B CG  1 
ATOM   494  C CD  . ARG A 1 101 ? 200.924 195.788 90.464  1.00 68.37  ? 94  ARG B CD  1 
ATOM   495  N NE  . ARG A 1 101 ? 200.893 196.733 91.574  1.00 73.81  ? 94  ARG B NE  1 
ATOM   496  C CZ  . ARG A 1 101 ? 201.901 197.523 91.919  1.00 75.67  ? 94  ARG B CZ  1 
ATOM   497  N NH1 . ARG A 1 101 ? 203.045 197.516 91.256  1.00 67.00  ? 94  ARG B NH1 1 
ATOM   498  N NH2 . ARG A 1 101 ? 201.756 198.343 92.956  1.00 71.47  ? 94  ARG B NH2 1 
ATOM   499  N N   . LEU A 1 102 ? 200.585 192.387 94.022  1.00 49.50  ? 95  LEU B N   1 
ATOM   500  C CA  . LEU A 1 102 ? 199.634 192.005 95.056  1.00 45.87  ? 95  LEU B CA  1 
ATOM   501  C C   . LEU A 1 102 ? 198.628 193.133 95.240  1.00 51.80  ? 95  LEU B C   1 
ATOM   502  O O   . LEU A 1 102 ? 199.015 194.284 95.467  1.00 58.35  ? 95  LEU B O   1 
ATOM   503  C CB  . LEU A 1 102 ? 200.355 191.702 96.368  1.00 44.28  ? 95  LEU B CB  1 
ATOM   504  C CG  . LEU A 1 102 ? 199.650 190.767 97.348  1.00 42.30  ? 95  LEU B CG  1 
ATOM   505  C CD1 . LEU A 1 102 ? 199.527 189.377 96.761  1.00 39.21  ? 95  LEU B CD1 1 
ATOM   506  C CD2 . LEU A 1 102 ? 200.400 190.727 98.666  1.00 40.05  ? 95  LEU B CD2 1 
ATOM   507  N N   . GLY A 1 103 ? 197.341 192.803 95.132  1.00 44.22  ? 96  GLY B N   1 
ATOM   508  C CA  . GLY A 1 103 ? 196.279 193.759 95.342  1.00 44.79  ? 96  GLY B CA  1 
ATOM   509  C C   . GLY A 1 103 ? 195.553 193.523 96.657  1.00 47.47  ? 96  GLY B C   1 
ATOM   510  O O   . GLY A 1 103 ? 195.921 192.676 97.466  1.00 47.91  ? 96  GLY B O   1 
ATOM   511  N N   . TYR A 1 104 ? 194.498 194.306 96.859  1.00 50.10  ? 97  TYR B N   1 
ATOM   512  C CA  . TYR A 1 104 ? 193.677 194.171 98.053  1.00 44.03  ? 97  TYR B CA  1 
ATOM   513  C C   . TYR A 1 104 ? 192.313 194.789 97.789  1.00 47.04  ? 97  TYR B C   1 
ATOM   514  O O   . TYR A 1 104 ? 192.155 195.608 96.881  1.00 51.19  ? 97  TYR B O   1 
ATOM   515  C CB  . TYR A 1 104 ? 194.326 194.835 99.272  1.00 41.28  ? 97  TYR B CB  1 
ATOM   516  C CG  . TYR A 1 104 ? 194.828 196.231 99.005  1.00 47.25  ? 97  TYR B CG  1 
ATOM   517  C CD1 . TYR A 1 104 ? 196.100 196.450 98.506  1.00 47.79  ? 97  TYR B CD1 1 
ATOM   518  C CD2 . TYR A 1 104 ? 194.018 197.331 99.234  1.00 50.09  ? 97  TYR B CD2 1 
ATOM   519  C CE1 . TYR A 1 104 ? 196.553 197.720 98.263  1.00 50.61  ? 97  TYR B CE1 1 
ATOM   520  C CE2 . TYR A 1 104 ? 194.462 198.607 98.985  1.00 52.14  ? 97  TYR B CE2 1 
ATOM   521  C CZ  . TYR A 1 104 ? 195.729 198.797 98.494  1.00 54.49  ? 97  TYR B CZ  1 
ATOM   522  O OH  . TYR A 1 104 ? 196.180 200.070 98.240  1.00 59.19  ? 97  TYR B OH  1 
ATOM   523  N N   . ASP A 1 105 ? 191.333 194.387 98.597  1.00 43.92  ? 98  ASP B N   1 
ATOM   524  C CA  . ASP A 1 105 ? 189.979 194.936 98.564  1.00 39.45  ? 98  ASP B CA  1 
ATOM   525  C C   . ASP A 1 105 ? 189.591 195.246 100.004 1.00 43.84  ? 98  ASP B C   1 
ATOM   526  O O   . ASP A 1 105 ? 188.991 194.410 100.683 1.00 47.32  ? 98  ASP B O   1 
ATOM   527  C CB  . ASP A 1 105 ? 188.997 193.967 97.921  1.00 52.73  ? 98  ASP B CB  1 
ATOM   528  C CG  . ASP A 1 105 ? 188.728 194.288 96.470  1.00 62.47  ? 98  ASP B CG  1 
ATOM   529  O OD1 . ASP A 1 105 ? 189.644 194.802 95.801  1.00 61.64  ? 98  ASP B OD1 1 
ATOM   530  O OD2 . ASP A 1 105 ? 187.601 194.033 96.000  1.00 63.90  ? 98  ASP B OD2 1 
ATOM   531  N N   . LEU A 1 106 ? 189.933 196.442 100.471 1.00 46.03  ? 99  LEU B N   1 
ATOM   532  C CA  . LEU A 1 106 ? 189.607 196.825 101.837 1.00 39.36  ? 99  LEU B CA  1 
ATOM   533  C C   . LEU A 1 106 ? 188.129 197.171 101.935 1.00 39.20  ? 99  LEU B C   1 
ATOM   534  O O   . LEU A 1 106 ? 187.623 198.003 101.177 1.00 53.83  ? 99  LEU B O   1 
ATOM   535  C CB  . LEU A 1 106 ? 190.467 198.006 102.278 1.00 39.66  ? 99  LEU B CB  1 
ATOM   536  C CG  . LEU A 1 106 ? 191.970 197.854 102.041 1.00 43.17  ? 99  LEU B CG  1 
ATOM   537  C CD1 . LEU A 1 106 ? 192.744 199.010 102.645 1.00 44.49  ? 99  LEU B CD1 1 
ATOM   538  C CD2 . LEU A 1 106 ? 192.463 196.539 102.597 1.00 39.80  ? 99  LEU B CD2 1 
ATOM   539  N N   . PHE A 1 107 ? 187.434 196.529 102.867 1.00 33.03  ? 100 PHE B N   1 
ATOM   540  C CA  . PHE A 1 107 ? 185.992 196.656 102.996 1.00 43.53  ? 100 PHE B CA  1 
ATOM   541  C C   . PHE A 1 107 ? 185.632 197.053 104.418 1.00 48.78  ? 100 PHE B C   1 
ATOM   542  O O   . PHE A 1 107 ? 186.136 196.472 105.382 1.00 46.09  ? 100 PHE B O   1 
ATOM   543  C CB  . PHE A 1 107 ? 185.289 195.349 102.623 1.00 41.31  ? 100 PHE B CB  1 
ATOM   544  C CG  . PHE A 1 107 ? 184.952 195.242 101.168 1.00 47.60  ? 100 PHE B CG  1 
ATOM   545  C CD1 . PHE A 1 107 ? 183.933 195.998 100.624 1.00 49.81  ? 100 PHE B CD1 1 
ATOM   546  C CD2 . PHE A 1 107 ? 185.664 194.395 100.342 1.00 49.50  ? 100 PHE B CD2 1 
ATOM   547  C CE1 . PHE A 1 107 ? 183.625 195.903 99.285  1.00 51.17  ? 100 PHE B CE1 1 
ATOM   548  C CE2 . PHE A 1 107 ? 185.362 194.297 99.004  1.00 51.94  ? 100 PHE B CE2 1 
ATOM   549  C CZ  . PHE A 1 107 ? 184.342 195.052 98.474  1.00 54.02  ? 100 PHE B CZ  1 
ATOM   550  N N   . ASP A 1 108 ? 184.757 198.046 104.540 1.00 54.06  ? 101 ASP B N   1 
ATOM   551  C CA  . ASP A 1 108 ? 184.301 198.510 105.843 1.00 53.56  ? 101 ASP B CA  1 
ATOM   552  C C   . ASP A 1 108 ? 183.297 197.510 106.394 1.00 55.45  ? 101 ASP B C   1 
ATOM   553  O O   . ASP A 1 108 ? 182.250 197.268 105.785 1.00 66.48  ? 101 ASP B O   1 
ATOM   554  C CB  . ASP A 1 108 ? 183.681 199.899 105.736 1.00 66.28  ? 101 ASP B CB  1 
ATOM   555  C CG  . ASP A 1 108 ? 182.719 200.198 106.872 1.00 66.03  ? 101 ASP B CG  1 
ATOM   556  O OD1 . ASP A 1 108 ? 183.086 199.970 108.043 1.00 63.41  ? 101 ASP B OD1 1 
ATOM   557  O OD2 . ASP A 1 108 ? 181.596 200.666 106.595 1.00 69.05  ? 101 ASP B OD2 1 
ATOM   558  N N   . THR A 1 109 ? 183.618 196.917 107.537 1.00 52.41  ? 102 THR B N   1 
ATOM   559  C CA  . THR A 1 109 ? 182.680 196.095 108.287 1.00 54.62  ? 102 THR B CA  1 
ATOM   560  C C   . THR A 1 109 ? 182.521 196.706 109.668 1.00 62.16  ? 102 THR B C   1 
ATOM   561  O O   . THR A 1 109 ? 183.489 196.786 110.432 1.00 71.92  ? 102 THR B O   1 
ATOM   562  C CB  . THR A 1 109 ? 183.151 194.640 108.374 1.00 52.27  ? 102 THR B CB  1 
ATOM   563  O OG1 . THR A 1 109 ? 184.021 194.458 109.498 1.00 40.42  ? 102 THR B OG1 1 
ATOM   564  C CG2 . THR A 1 109 ? 183.877 194.239 107.109 1.00 56.38  ? 102 THR B CG2 1 
ATOM   565  N N   . CYS A 1 110 ? 181.313 197.164 109.979 1.00 63.87  ? 103 CYS B N   1 
ATOM   566  C CA  . CYS A 1 110 ? 181.045 197.657 111.317 1.00 65.62  ? 103 CYS B CA  1 
ATOM   567  C C   . CYS A 1 110 ? 181.071 196.485 112.296 1.00 66.72  ? 103 CYS B C   1 
ATOM   568  O O   . CYS A 1 110 ? 181.228 195.323 111.914 1.00 69.54  ? 103 CYS B O   1 
ATOM   569  C CB  . CYS A 1 110 ? 179.712 198.400 111.348 1.00 65.59  ? 103 CYS B CB  1 
ATOM   570  S SG  . CYS A 1 110 ? 179.347 199.292 109.814 1.00 77.88  ? 103 CYS B SG  1 
ATOM   571  N N   . SER A 1 111 ? 180.911 196.788 113.583 1.00 64.01  ? 104 SER B N   1 
ATOM   572  C CA  . SER A 1 111 ? 180.913 195.726 114.580 1.00 71.26  ? 104 SER B CA  1 
ATOM   573  C C   . SER A 1 111 ? 179.752 194.759 114.388 1.00 73.00  ? 104 SER B C   1 
ATOM   574  O O   . SER A 1 111 ? 179.771 193.662 114.957 1.00 70.72  ? 104 SER B O   1 
ATOM   575  C CB  . SER A 1 111 ? 180.874 196.328 115.984 1.00 85.78  ? 104 SER B CB  1 
ATOM   576  O OG  . SER A 1 111 ? 182.116 196.926 116.313 1.00 89.62  ? 104 SER B OG  1 
ATOM   577  N N   . GLU A 1 112 ? 178.746 195.140 113.606 1.00 74.36  ? 105 GLU B N   1 
ATOM   578  C CA  . GLU A 1 112 ? 177.643 194.246 113.304 1.00 72.18  ? 105 GLU B CA  1 
ATOM   579  C C   . GLU A 1 112 ? 178.081 193.190 112.289 1.00 60.99  ? 105 GLU B C   1 
ATOM   580  O O   . GLU A 1 112 ? 178.944 193.448 111.448 1.00 56.91  ? 105 GLU B O   1 
ATOM   581  C CB  . GLU A 1 112 ? 176.457 195.038 112.758 1.00 73.09  ? 105 GLU B CB  1 
ATOM   582  C CG  . GLU A 1 112 ? 175.641 195.746 113.830 1.00 81.96  ? 105 GLU B CG  1 
ATOM   583  C CD  . GLU A 1 112 ? 174.303 196.245 113.316 1.00 96.59  ? 105 GLU B CD  1 
ATOM   584  O OE1 . GLU A 1 112 ? 174.265 196.797 112.195 1.00 93.79  ? 105 GLU B OE1 1 
ATOM   585  O OE2 . GLU A 1 112 ? 173.290 196.088 114.031 1.00 93.58  ? 105 GLU B OE2 1 
ATOM   586  N N   . PRO A 1 113 ? 177.507 191.985 112.354 1.00 60.40  ? 106 PRO B N   1 
ATOM   587  C CA  . PRO A 1 113 ? 177.861 190.949 111.375 1.00 58.65  ? 106 PRO B CA  1 
ATOM   588  C C   . PRO A 1 113 ? 177.049 191.029 110.091 1.00 56.80  ? 106 PRO B C   1 
ATOM   589  O O   . PRO A 1 113 ? 177.483 190.540 109.043 1.00 57.83  ? 106 PRO B O   1 
ATOM   590  C CB  . PRO A 1 113 ? 177.580 189.649 112.135 1.00 53.36  ? 106 PRO B CB  1 
ATOM   591  C CG  . PRO A 1 113 ? 176.484 190.001 113.073 1.00 54.67  ? 106 PRO B CG  1 
ATOM   592  C CD  . PRO A 1 113 ? 176.622 191.467 113.412 1.00 60.29  ? 106 PRO B CD  1 
ATOM   593  N N   . VAL A 1 114 ? 175.870 191.647 110.161 1.00 58.73  ? 107 VAL B N   1 
ATOM   594  C CA  . VAL A 1 114 ? 175.013 191.746 108.983 1.00 59.13  ? 107 VAL B CA  1 
ATOM   595  C C   . VAL A 1 114 ? 175.650 192.644 107.930 1.00 59.20  ? 107 VAL B C   1 
ATOM   596  O O   . VAL A 1 114 ? 175.446 192.455 106.725 1.00 59.97  ? 107 VAL B O   1 
ATOM   597  C CB  . VAL A 1 114 ? 173.606 192.230 109.384 1.00 66.24  ? 107 VAL B CB  1 
ATOM   598  C CG1 . VAL A 1 114 ? 173.624 193.699 109.777 1.00 63.91  ? 107 VAL B CG1 1 
ATOM   599  C CG2 . VAL A 1 114 ? 172.620 191.986 108.254 1.00 63.81  ? 107 VAL B CG2 1 
ATOM   600  N N   . VAL A 1 115 ? 176.429 193.637 108.364 1.00 59.78  ? 108 VAL B N   1 
ATOM   601  C CA  . VAL A 1 115 ? 177.095 194.514 107.410 1.00 56.75  ? 108 VAL B CA  1 
ATOM   602  C C   . VAL A 1 115 ? 178.381 193.875 106.901 1.00 53.95  ? 108 VAL B C   1 
ATOM   603  O O   . VAL A 1 115 ? 178.801 194.128 105.767 1.00 58.45  ? 108 VAL B O   1 
ATOM   604  C CB  . VAL A 1 115 ? 177.342 195.894 108.050 1.00 55.93  ? 108 VAL B CB  1 
ATOM   605  C CG1 . VAL A 1 115 ? 178.048 195.742 109.380 1.00 61.99  ? 108 VAL B CG1 1 
ATOM   606  C CG2 . VAL A 1 115 ? 178.132 196.799 107.116 1.00 50.91  ? 108 VAL B CG2 1 
ATOM   607  N N   . ALA A 1 116 ? 179.017 193.030 107.712 1.00 51.67  ? 109 ALA B N   1 
ATOM   608  C CA  . ALA A 1 116 ? 180.231 192.334 107.304 1.00 49.47  ? 109 ALA B CA  1 
ATOM   609  C C   . ALA A 1 116 ? 179.969 191.140 106.399 1.00 50.01  ? 109 ALA B C   1 
ATOM   610  O O   . ALA A 1 116 ? 180.888 190.707 105.698 1.00 49.53  ? 109 ALA B O   1 
ATOM   611  C CB  . ALA A 1 116 ? 181.003 191.862 108.533 1.00 45.87  ? 109 ALA B CB  1 
ATOM   612  N N   . MET A 1 117 ? 178.755 190.588 106.410 1.00 52.87  ? 110 MET B N   1 
ATOM   613  C CA  . MET A 1 117 ? 178.471 189.416 105.589 1.00 46.59  ? 110 MET B CA  1 
ATOM   614  C C   . MET A 1 117 ? 178.509 189.748 104.102 1.00 50.35  ? 110 MET B C   1 
ATOM   615  O O   . MET A 1 117 ? 178.956 188.929 103.292 1.00 56.97  ? 110 MET B O   1 
ATOM   616  C CB  . MET A 1 117 ? 177.116 188.828 105.972 1.00 49.04  ? 110 MET B CB  1 
ATOM   617  C CG  . MET A 1 117 ? 177.195 187.654 106.931 1.00 58.52  ? 110 MET B CG  1 
ATOM   618  S SD  . MET A 1 117 ? 177.783 186.148 106.135 1.00 64.96  ? 110 MET B SD  1 
ATOM   619  C CE  . MET A 1 117 ? 179.376 185.962 106.923 1.00 56.96  ? 110 MET B CE  1 
ATOM   620  N N   . LYS A 1 118 ? 178.032 190.932 103.723 1.00 48.30  ? 111 LYS B N   1 
ATOM   621  C CA  . LYS A 1 118 ? 178.009 191.305 102.309 1.00 49.85  ? 111 LYS B CA  1 
ATOM   622  C C   . LYS A 1 118 ? 179.399 191.361 101.684 1.00 51.80  ? 111 LYS B C   1 
ATOM   623  O O   . LYS A 1 118 ? 179.573 190.823 100.575 1.00 53.24  ? 111 LYS B O   1 
ATOM   624  C CB  . LYS A 1 118 ? 177.261 192.633 102.147 1.00 55.48  ? 111 LYS B CB  1 
ATOM   625  C CG  . LYS A 1 118 ? 176.541 192.790 100.823 1.00 67.84  ? 111 LYS B CG  1 
ATOM   626  C CD  . LYS A 1 118 ? 175.256 193.581 100.990 1.00 79.87  ? 111 LYS B CD  1 
ATOM   627  C CE  . LYS A 1 118 ? 174.262 192.835 101.860 1.00 80.48  ? 111 LYS B CE  1 
ATOM   628  N NZ  . LYS A 1 118 ? 173.897 191.524 101.264 1.00 75.51  ? 111 LYS B NZ  1 
ATOM   629  N N   . PRO A 1 119 ? 180.413 191.989 102.300 1.00 47.28  ? 112 PRO B N   1 
ATOM   630  C CA  . PRO A 1 119 ? 181.761 191.917 101.713 1.00 46.61  ? 112 PRO B CA  1 
ATOM   631  C C   . PRO A 1 119 ? 182.289 190.502 101.582 1.00 43.00  ? 112 PRO B C   1 
ATOM   632  O O   . PRO A 1 119 ? 183.003 190.209 100.623 1.00 45.62  ? 112 PRO B O   1 
ATOM   633  C CB  . PRO A 1 119 ? 182.605 192.749 102.686 1.00 48.26  ? 112 PRO B CB  1 
ATOM   634  C CG  . PRO A 1 119 ? 181.651 193.693 103.279 1.00 48.39  ? 112 PRO B CG  1 
ATOM   635  C CD  . PRO A 1 119 ? 180.387 192.918 103.442 1.00 44.97  ? 112 PRO B CD  1 
ATOM   636  N N   . SER A 1 120 ? 181.959 189.611 102.519 1.00 39.27  ? 113 SER B N   1 
ATOM   637  C CA  . SER A 1 120 ? 182.393 188.221 102.407 1.00 40.01  ? 113 SER B CA  1 
ATOM   638  C C   . SER A 1 120 ? 181.749 187.530 101.210 1.00 45.77  ? 113 SER B C   1 
ATOM   639  O O   . SER A 1 120 ? 182.423 186.822 100.447 1.00 49.43  ? 113 SER B O   1 
ATOM   640  C CB  . SER A 1 120 ? 182.064 187.478 103.698 1.00 41.37  ? 113 SER B CB  1 
ATOM   641  O OG  . SER A 1 120 ? 182.331 188.289 104.827 1.00 38.05  ? 113 SER B OG  1 
ATOM   642  N N   . LEU A 1 121 ? 180.441 187.724 101.033 1.00 46.87  ? 114 LEU B N   1 
ATOM   643  C CA  . LEU A 1 121 ? 179.755 187.159 99.880  1.00 49.56  ? 114 LEU B CA  1 
ATOM   644  C C   . LEU A 1 121 ? 180.314 187.708 98.576  1.00 52.17  ? 114 LEU B C   1 
ATOM   645  O O   . LEU A 1 121 ? 180.383 186.983 97.579  1.00 53.67  ? 114 LEU B O   1 
ATOM   646  C CB  . LEU A 1 121 ? 178.257 187.438 99.980  1.00 57.23  ? 114 LEU B CB  1 
ATOM   647  C CG  . LEU A 1 121 ? 177.356 186.357 100.576 1.00 57.17  ? 114 LEU B CG  1 
ATOM   648  C CD1 . LEU A 1 121 ? 177.573 186.250 102.069 1.00 53.43  ? 114 LEU B CD1 1 
ATOM   649  C CD2 . LEU A 1 121 ? 175.903 186.655 100.266 1.00 60.56  ? 114 LEU B CD2 1 
ATOM   650  N N   . MET A 1 122 ? 180.709 188.984 98.559  1.00 50.03  ? 115 MET B N   1 
ATOM   651  C CA  . MET A 1 122 ? 181.400 189.521 97.391  1.00 51.76  ? 115 MET B CA  1 
ATOM   652  C C   . MET A 1 122 ? 182.786 188.914 97.222  1.00 53.61  ? 115 MET B C   1 
ATOM   653  O O   . MET A 1 122 ? 183.246 188.730 96.090  1.00 59.89  ? 115 MET B O   1 
ATOM   654  C CB  . MET A 1 122 ? 181.510 191.042 97.492  1.00 57.42  ? 115 MET B CB  1 
ATOM   655  C CG  . MET A 1 122 ? 181.464 191.756 96.153  1.00 67.76  ? 115 MET B CG  1 
ATOM   656  S SD  . MET A 1 122 ? 179.791 191.915 95.509  1.00 99.48  ? 115 MET B SD  1 
ATOM   657  C CE  . MET A 1 122 ? 179.979 191.187 93.888  1.00 87.49  ? 115 MET B CE  1 
ATOM   658  N N   . PHE A 1 123 ? 183.460 188.612 98.333  1.00 47.64  ? 116 PHE B N   1 
ATOM   659  C CA  . PHE A 1 123 ? 184.780 187.994 98.283  1.00 42.33  ? 116 PHE B CA  1 
ATOM   660  C C   . PHE A 1 123 ? 184.717 186.640 97.600  1.00 47.98  ? 116 PHE B C   1 
ATOM   661  O O   . PHE A 1 123 ? 185.613 186.276 96.830  1.00 48.33  ? 116 PHE B O   1 
ATOM   662  C CB  . PHE A 1 123 ? 185.338 187.835 99.697  1.00 39.52  ? 116 PHE B CB  1 
ATOM   663  C CG  . PHE A 1 123 ? 185.949 189.080 100.260 1.00 41.44  ? 116 PHE B CG  1 
ATOM   664  C CD1 . PHE A 1 123 ? 186.445 190.065 99.430  1.00 42.40  ? 116 PHE B CD1 1 
ATOM   665  C CD2 . PHE A 1 123 ? 186.031 189.259 101.628 1.00 31.80  ? 116 PHE B CD2 1 
ATOM   666  C CE1 . PHE A 1 123 ? 187.008 191.205 99.956  1.00 39.30  ? 116 PHE B CE1 1 
ATOM   667  C CE2 . PHE A 1 123 ? 186.592 190.394 102.155 1.00 30.85  ? 116 PHE B CE2 1 
ATOM   668  C CZ  . PHE A 1 123 ? 187.080 191.368 101.320 1.00 37.30  ? 116 PHE B CZ  1 
ATOM   669  N N   . LEU A 1 124 ? 183.669 185.872 97.881  1.00 52.05  ? 117 LEU B N   1 
ATOM   670  C CA  . LEU A 1 124 ? 183.582 184.523 97.340  1.00 51.03  ? 117 LEU B CA  1 
ATOM   671  C C   . LEU A 1 124 ? 182.875 184.451 95.994  1.00 52.43  ? 117 LEU B C   1 
ATOM   672  O O   . LEU A 1 124 ? 182.713 183.351 95.459  1.00 57.63  ? 117 LEU B O   1 
ATOM   673  C CB  . LEU A 1 124 ? 182.893 183.607 98.344  1.00 44.67  ? 117 LEU B CB  1 
ATOM   674  C CG  . LEU A 1 124 ? 183.829 183.366 99.521  1.00 47.59  ? 117 LEU B CG  1 
ATOM   675  C CD1 . LEU A 1 124 ? 183.053 183.159 100.792 1.00 46.15  ? 117 LEU B CD1 1 
ATOM   676  C CD2 . LEU A 1 124 ? 184.736 182.192 99.228  1.00 45.89  ? 117 LEU B CD2 1 
ATOM   677  N N   . ALA A 1 125 ? 182.453 185.579 95.436  1.00 54.21  ? 118 ALA B N   1 
ATOM   678  C CA  . ALA A 1 125 ? 181.889 185.573 94.097  1.00 56.73  ? 118 ALA B CA  1 
ATOM   679  C C   . ALA A 1 125 ? 182.982 185.327 93.066  1.00 64.85  ? 118 ALA B C   1 
ATOM   680  O O   . ALA A 1 125 ? 184.156 185.630 93.287  1.00 66.86  ? 118 ALA B O   1 
ATOM   681  C CB  . ALA A 1 125 ? 181.181 186.895 93.808  1.00 61.41  ? 118 ALA B CB  1 
ATOM   682  N N   . LYS A 1 126 ? 182.587 184.759 91.932  1.00 71.15  ? 119 LYS B N   1 
ATOM   683  C CA  . LYS A 1 126 ? 183.528 184.526 90.848  1.00 70.44  ? 119 LYS B CA  1 
ATOM   684  C C   . LYS A 1 126 ? 184.029 185.858 90.302  1.00 74.57  ? 119 LYS B C   1 
ATOM   685  O O   . LYS A 1 126 ? 183.279 186.832 90.201  1.00 76.62  ? 119 LYS B O   1 
ATOM   686  C CB  . LYS A 1 126 ? 182.869 183.700 89.742  1.00 78.48  ? 119 LYS B CB  1 
ATOM   687  C CG  . LYS A 1 126 ? 183.501 183.831 88.367  1.00 82.80  ? 119 LYS B CG  1 
ATOM   688  C CD  . LYS A 1 126 ? 184.356 182.616 88.049  1.00 83.43  ? 119 LYS B CD  1 
ATOM   689  C CE  . LYS A 1 126 ? 185.184 182.825 86.793  1.00 86.70  ? 119 LYS B CE  1 
ATOM   690  N NZ  . LYS A 1 126 ? 184.334 182.903 85.574  1.00 86.27  ? 119 LYS B NZ  1 
ATOM   691  N N   . ALA A 1 127 ? 185.317 185.900 89.972  1.00 77.25  ? 120 ALA B N   1 
ATOM   692  C CA  . ALA A 1 127 ? 185.925 187.138 89.504  1.00 81.72  ? 120 ALA B CA  1 
ATOM   693  C C   . ALA A 1 127 ? 185.249 187.621 88.228  1.00 84.27  ? 120 ALA B C   1 
ATOM   694  O O   . ALA A 1 127 ? 185.076 186.864 87.269  1.00 84.74  ? 120 ALA B O   1 
ATOM   695  C CB  . ALA A 1 127 ? 187.421 186.934 89.264  1.00 79.67  ? 120 ALA B CB  1 
ATOM   696  N N   . GLY A 1 128 ? 184.873 188.898 88.219  1.00 80.35  ? 121 GLY B N   1 
ATOM   697  C CA  . GLY A 1 128 ? 184.157 189.478 87.105  1.00 86.25  ? 121 GLY B CA  1 
ATOM   698  C C   . GLY A 1 128 ? 182.664 189.236 87.101  1.00 90.32  ? 121 GLY B C   1 
ATOM   699  O O   . GLY A 1 128 ? 181.990 189.655 86.151  1.00 87.08  ? 121 GLY B O   1 
ATOM   700  N N   . SER A 1 129 ? 182.123 188.580 88.125  1.00 91.86  ? 122 SER B N   1 
ATOM   701  C CA  . SER A 1 129 ? 180.702 188.277 88.195  1.00 87.81  ? 122 SER B CA  1 
ATOM   702  C C   . SER A 1 129 ? 180.170 188.687 89.559  1.00 86.32  ? 122 SER B C   1 
ATOM   703  O O   . SER A 1 129 ? 180.889 188.667 90.560  1.00 85.34  ? 122 SER B O   1 
ATOM   704  C CB  . SER A 1 129 ? 180.427 186.788 87.945  1.00 83.59  ? 122 SER B CB  1 
ATOM   705  O OG  . SER A 1 129 ? 179.036 186.524 87.915  1.00 83.83  ? 122 SER B OG  1 
ATOM   706  N N   . ARG A 1 130 ? 178.891 189.054 89.588  1.00 86.56  ? 123 ARG B N   1 
ATOM   707  C CA  . ARG A 1 130 ? 178.244 189.551 90.794  1.00 85.63  ? 123 ARG B CA  1 
ATOM   708  C C   . ARG A 1 130 ? 177.370 188.500 91.468  1.00 83.29  ? 123 ARG B C   1 
ATOM   709  O O   . ARG A 1 130 ? 176.554 188.843 92.329  1.00 79.59  ? 123 ARG B O   1 
ATOM   710  C CB  . ARG A 1 130 ? 177.422 190.800 90.463  1.00 88.01  ? 123 ARG B CB  1 
ATOM   711  C CG  . ARG A 1 130 ? 177.239 191.761 91.628  1.00 92.11  ? 123 ARG B CG  1 
ATOM   712  C CD  . ARG A 1 130 ? 177.641 193.175 91.248  1.00 96.88  ? 123 ARG B CD  1 
ATOM   713  N NE  . ARG A 1 130 ? 179.059 193.416 91.490  1.00 102.81 ? 123 ARG B NE  1 
ATOM   714  C CZ  . ARG A 1 130 ? 179.717 194.494 91.085  1.00 101.93 ? 123 ARG B CZ  1 
ATOM   715  N NH1 . ARG A 1 130 ? 179.113 195.460 90.414  1.00 94.80  ? 123 ARG B NH1 1 
ATOM   716  N NH2 . ARG A 1 130 ? 181.013 194.605 91.361  1.00 100.15 ? 123 ARG B NH2 1 
ATOM   717  N N   . ASP A 1 131 ? 177.521 187.231 91.101  1.00 86.15  ? 124 ASP B N   1 
ATOM   718  C CA  . ASP A 1 131 ? 176.737 186.145 91.668  1.00 83.48  ? 124 ASP B CA  1 
ATOM   719  C C   . ASP A 1 131 ? 177.656 185.149 92.361  1.00 77.83  ? 124 ASP B C   1 
ATOM   720  O O   . ASP A 1 131 ? 178.788 184.926 91.922  1.00 79.47  ? 124 ASP B O   1 
ATOM   721  C CB  . ASP A 1 131 ? 175.926 185.424 90.587  1.00 83.19  ? 124 ASP B CB  1 
ATOM   722  C CG  . ASP A 1 131 ? 174.782 186.263 90.056  1.00 88.81  ? 124 ASP B CG  1 
ATOM   723  O OD1 . ASP A 1 131 ? 174.682 187.449 90.431  1.00 89.51  ? 124 ASP B OD1 1 
ATOM   724  O OD2 . ASP A 1 131 ? 173.979 185.732 89.260  1.00 88.59  ? 124 ASP B OD2 1 
ATOM   725  N N   . ILE A 1 132 ? 177.165 184.554 93.444  1.00 70.63  ? 125 ILE B N   1 
ATOM   726  C CA  . ILE A 1 132 ? 177.842 183.454 94.118  1.00 69.49  ? 125 ILE B CA  1 
ATOM   727  C C   . ILE A 1 132 ? 176.982 182.211 93.936  1.00 73.30  ? 125 ILE B C   1 
ATOM   728  O O   . ILE A 1 132 ? 175.791 182.214 94.268  1.00 74.35  ? 125 ILE B O   1 
ATOM   729  C CB  . ILE A 1 132 ? 178.090 183.755 95.604  1.00 63.58  ? 125 ILE B CB  1 
ATOM   730  C CG1 . ILE A 1 132 ? 178.498 182.484 96.347  1.00 58.78  ? 125 ILE B CG1 1 
ATOM   731  C CG2 . ILE A 1 132 ? 176.862 184.367 96.244  1.00 67.74  ? 125 ILE B CG2 1 
ATOM   732  C CD1 . ILE A 1 132 ? 178.851 182.714 97.794  1.00 55.90  ? 125 ILE B CD1 1 
ATOM   733  N N   . ALA A 1 133 ? 177.578 181.156 93.395  1.00 74.37  ? 126 ALA B N   1 
ATOM   734  C CA  . ALA A 1 133 ? 176.832 179.941 93.122  1.00 75.18  ? 126 ALA B CA  1 
ATOM   735  C C   . ALA A 1 133 ? 176.675 179.107 94.388  1.00 78.68  ? 126 ALA B C   1 
ATOM   736  O O   . ALA A 1 133 ? 177.340 179.333 95.402  1.00 76.34  ? 126 ALA B O   1 
ATOM   737  C CB  . ALA A 1 133 ? 177.521 179.121 92.035  1.00 75.17  ? 126 ALA B CB  1 
ATOM   738  N N   . ALA A 1 134 ? 175.770 178.135 94.318  1.00 77.90  ? 127 ALA B N   1 
ATOM   739  C CA  . ALA A 1 134 ? 175.507 177.199 95.409  1.00 73.84  ? 127 ALA B CA  1 
ATOM   740  C C   . ALA A 1 134 ? 176.013 175.828 94.972  1.00 83.88  ? 127 ALA B C   1 
ATOM   741  O O   . ALA A 1 134 ? 175.285 175.046 94.359  1.00 88.44  ? 127 ALA B O   1 
ATOM   742  C CB  . ALA A 1 134 ? 174.032 177.171 95.761  1.00 68.76  ? 127 ALA B CB  1 
ATOM   743  N N   . TYR A 1 135 ? 177.306 175.609 95.154  1.00 82.29  ? 128 TYR B N   1 
ATOM   744  C CA  . TYR A 1 135 ? 177.911 174.342 94.703  1.00 82.64  ? 128 TYR B CA  1 
ATOM   745  C C   . TYR A 1 135 ? 177.881 173.440 95.903  1.00 82.38  ? 128 TYR B C   1 
ATOM   746  O O   . TYR A 1 135 ? 177.596 173.922 97.007  1.00 81.88  ? 128 TYR B O   1 
ATOM   747  C CB  . TYR A 1 135 ? 179.287 174.710 94.155  1.00 84.99  ? 128 TYR B CB  1 
ATOM   748  C CG  . TYR A 1 135 ? 179.306 175.472 92.840  1.00 80.70  ? 128 TYR B CG  1 
ATOM   749  C CD1 . TYR A 1 135 ? 178.376 175.216 91.844  1.00 81.67  ? 128 TYR B CD1 1 
ATOM   750  C CD2 . TYR A 1 135 ? 180.271 176.436 92.594  1.00 78.34  ? 128 TYR B CD2 1 
ATOM   751  C CE1 . TYR A 1 135 ? 178.401 175.905 90.644  1.00 84.07  ? 128 TYR B CE1 1 
ATOM   752  C CE2 . TYR A 1 135 ? 180.309 177.130 91.399  1.00 80.74  ? 128 TYR B CE2 1 
ATOM   753  C CZ  . TYR A 1 135 ? 179.373 176.863 90.420  1.00 87.62  ? 128 TYR B CZ  1 
ATOM   754  O OH  . TYR A 1 135 ? 179.414 177.556 89.246  1.00 89.71  ? 128 TYR B OH  1 
ATOM   755  N N   . CYS A 1 136 ? 178.162 172.162 95.714  1.00 87.04  ? 129 CYS B N   1 
ATOM   756  C CA  . CYS A 1 136 ? 177.999 171.222 96.844  1.00 95.07  ? 129 CYS B CA  1 
ATOM   757  C C   . CYS A 1 136 ? 179.272 171.242 97.710  1.00 95.25  ? 129 CYS B C   1 
ATOM   758  O O   . CYS A 1 136 ? 179.185 170.780 98.863  1.00 89.40  ? 129 CYS B O   1 
ATOM   759  C CB  . CYS A 1 136 ? 177.589 169.847 96.314  1.00 107.42 ? 129 CYS B CB  1 
ATOM   760  S SG  . CYS A 1 136 ? 175.833 169.688 95.870  1.00 135.95 ? 129 CYS B SG  1 
ATOM   761  N N   . ASN A 1 137 ? 180.391 171.766 97.192  1.00 97.23  ? 130 ASN B N   1 
ATOM   762  C CA  . ASN A 1 137 ? 181.620 171.875 98.038  1.00 91.50  ? 130 ASN B CA  1 
ATOM   763  C C   . ASN A 1 137 ? 182.571 172.977 97.560  1.00 83.75  ? 130 ASN B C   1 
ATOM   764  O O   . ASN A 1 137 ? 182.232 173.678 96.596  1.00 82.07  ? 130 ASN B O   1 
ATOM   765  C CB  . ASN A 1 137 ? 182.327 170.537 98.207  1.00 95.04  ? 130 ASN B CB  1 
ATOM   766  C CG  . ASN A 1 137 ? 182.448 169.765 96.922  1.00 100.96 ? 130 ASN B CG  1 
ATOM   767  O OD1 . ASN A 1 137 ? 182.649 170.347 95.850  1.00 93.58  ? 130 ASN B OD1 1 
ATOM   768  N ND2 . ASN A 1 137 ? 182.326 168.453 97.019  1.00 109.37 ? 130 ASN B ND2 1 
ATOM   769  N N   . TYR A 1 138 ? 183.746 173.082 98.186  1.00 76.37  ? 131 TYR B N   1 
ATOM   770  C CA  . TYR A 1 138 ? 184.623 174.210 97.888  1.00 68.90  ? 131 TYR B CA  1 
ATOM   771  C C   . TYR A 1 138 ? 185.325 174.094 96.541  1.00 72.70  ? 131 TYR B C   1 
ATOM   772  O O   . TYR A 1 138 ? 185.690 175.118 95.954  1.00 69.04  ? 131 TYR B O   1 
ATOM   773  C CB  . TYR A 1 138 ? 185.664 174.351 98.998  1.00 65.97  ? 131 TYR B CB  1 
ATOM   774  C CG  . TYR A 1 138 ? 186.717 173.268 98.978  1.00 67.96  ? 131 TYR B CG  1 
ATOM   775  C CD1 . TYR A 1 138 ? 186.453 172.010 99.501  1.00 71.07  ? 131 TYR B CD1 1 
ATOM   776  C CD2 . TYR A 1 138 ? 187.969 173.496 98.429  1.00 71.02  ? 131 TYR B CD2 1 
ATOM   777  C CE1 . TYR A 1 138 ? 187.408 171.014 99.483  1.00 71.57  ? 131 TYR B CE1 1 
ATOM   778  C CE2 . TYR A 1 138 ? 188.928 172.503 98.405  1.00 73.56  ? 131 TYR B CE2 1 
ATOM   779  C CZ  . TYR A 1 138 ? 188.642 171.266 98.934  1.00 72.64  ? 131 TYR B CZ  1 
ATOM   780  O OH  . TYR A 1 138 ? 189.597 170.279 98.911  1.00 84.71  ? 131 TYR B OH  1 
ATOM   781  N N   . THR A 1 139 ? 185.538 172.875 96.042  1.00 81.49  ? 132 THR B N   1 
ATOM   782  C CA  . THR A 1 139 ? 186.385 172.685 94.868  1.00 79.76  ? 132 THR B CA  1 
ATOM   783  C C   . THR A 1 139 ? 185.807 173.313 93.607  1.00 75.74  ? 132 THR B C   1 
ATOM   784  O O   . THR A 1 139 ? 186.551 173.532 92.646  1.00 72.78  ? 132 THR B O   1 
ATOM   785  C CB  . THR A 1 139 ? 186.629 171.195 94.630  1.00 81.53  ? 132 THR B CB  1 
ATOM   786  O OG1 . THR A 1 139 ? 185.403 170.474 94.804  1.00 89.47  ? 132 THR B OG1 1 
ATOM   787  C CG2 . THR A 1 139 ? 187.661 170.665 95.609  1.00 75.43  ? 132 THR B CG2 1 
ATOM   788  N N   . GLN A 1 140 ? 184.512 173.610 93.586  1.00 79.24  ? 133 GLN B N   1 
ATOM   789  C CA  . GLN A 1 140 ? 183.858 174.141 92.399  1.00 79.43  ? 133 GLN B CA  1 
ATOM   790  C C   . GLN A 1 140 ? 183.844 175.663 92.353  1.00 76.50  ? 133 GLN B C   1 
ATOM   791  O O   . GLN A 1 140 ? 183.373 176.233 91.364  1.00 75.78  ? 133 GLN B O   1 
ATOM   792  C CB  . GLN A 1 140 ? 182.423 173.613 92.316  1.00 82.71  ? 133 GLN B CB  1 
ATOM   793  C CG  . GLN A 1 140 ? 182.277 172.162 92.734  1.00 89.42  ? 133 GLN B CG  1 
ATOM   794  C CD  . GLN A 1 140 ? 180.856 171.657 92.600  1.00 97.88  ? 133 GLN B CD  1 
ATOM   795  O OE1 . GLN A 1 140 ? 180.162 171.968 91.633  1.00 96.59  ? 133 GLN B OE1 1 
ATOM   796  N NE2 . GLN A 1 140 ? 180.413 170.876 93.578  1.00 96.22  ? 133 GLN B NE2 1 
ATOM   797  N N   . TYR A 1 141 ? 184.350 176.332 93.383  1.00 78.53  ? 134 TYR B N   1 
ATOM   798  C CA  . TYR A 1 141 ? 184.335 177.785 93.439  1.00 73.87  ? 134 TYR B CA  1 
ATOM   799  C C   . TYR A 1 141 ? 185.637 178.361 92.900  1.00 70.21  ? 134 TYR B C   1 
ATOM   800  O O   . TYR A 1 141 ? 186.694 177.730 92.959  1.00 71.08  ? 134 TYR B O   1 
ATOM   801  C CB  . TYR A 1 141 ? 184.122 178.271 94.873  1.00 68.62  ? 134 TYR B CB  1 
ATOM   802  C CG  . TYR A 1 141 ? 182.716 178.083 95.386  1.00 70.44  ? 134 TYR B CG  1 
ATOM   803  C CD1 . TYR A 1 141 ? 181.747 179.053 95.186  1.00 65.08  ? 134 TYR B CD1 1 
ATOM   804  C CD2 . TYR A 1 141 ? 182.358 176.931 96.069  1.00 71.00  ? 134 TYR B CD2 1 
ATOM   805  C CE1 . TYR A 1 141 ? 180.462 178.881 95.653  1.00 67.30  ? 134 TYR B CE1 1 
ATOM   806  C CE2 . TYR A 1 141 ? 181.079 176.752 96.540  1.00 70.74  ? 134 TYR B CE2 1 
ATOM   807  C CZ  . TYR A 1 141 ? 180.135 177.729 96.329  1.00 70.13  ? 134 TYR B CZ  1 
ATOM   808  O OH  . TYR A 1 141 ? 178.858 177.548 96.802  1.00 69.54  ? 134 TYR B OH  1 
ATOM   809  N N   . GLN A 1 142 ? 185.547 179.578 92.373  1.00 68.28  ? 135 GLN B N   1 
ATOM   810  C CA  . GLN A 1 142 ? 186.711 180.352 91.946  1.00 69.15  ? 135 GLN B CA  1 
ATOM   811  C C   . GLN A 1 142 ? 186.603 181.736 92.576  1.00 65.83  ? 135 GLN B C   1 
ATOM   812  O O   . GLN A 1 142 ? 186.127 182.689 91.948  1.00 66.25  ? 135 GLN B O   1 
ATOM   813  C CB  . GLN A 1 142 ? 186.799 180.424 90.420  1.00 75.66  ? 135 GLN B CB  1 
ATOM   814  C CG  . GLN A 1 142 ? 187.918 181.309 89.890  1.00 84.76  ? 135 GLN B CG  1 
ATOM   815  C CD  . GLN A 1 142 ? 189.218 180.553 89.696  1.00 94.58  ? 135 GLN B CD  1 
ATOM   816  O OE1 . GLN A 1 142 ? 189.298 179.630 88.886  1.00 95.80  ? 135 GLN B OE1 1 
ATOM   817  N NE2 . GLN A 1 142 ? 190.245 180.942 90.442  1.00 90.51  ? 135 GLN B NE2 1 
ATOM   818  N N   . PRO A 1 143 ? 187.005 181.869 93.839  1.00 62.14  ? 136 PRO B N   1 
ATOM   819  C CA  . PRO A 1 143 ? 186.855 183.153 94.529  1.00 57.39  ? 136 PRO B CA  1 
ATOM   820  C C   . PRO A 1 143 ? 187.698 184.241 93.886  1.00 58.11  ? 136 PRO B C   1 
ATOM   821  O O   . PRO A 1 143 ? 188.730 183.980 93.265  1.00 63.31  ? 136 PRO B O   1 
ATOM   822  C CB  . PRO A 1 143 ? 187.330 182.847 95.953  1.00 57.31  ? 136 PRO B CB  1 
ATOM   823  C CG  . PRO A 1 143 ? 187.146 181.382 96.100  1.00 61.59  ? 136 PRO B CG  1 
ATOM   824  C CD  . PRO A 1 143 ? 187.461 180.811 94.753  1.00 67.50  ? 136 PRO B CD  1 
ATOM   825  N N   . ARG A 1 144 ? 187.235 185.479 94.040  1.00 53.73  ? 137 ARG B N   1 
ATOM   826  C CA  . ARG A 1 144 ? 187.887 186.631 93.438  1.00 51.67  ? 137 ARG B CA  1 
ATOM   827  C C   . ARG A 1 144 ? 188.997 187.217 94.301  1.00 51.98  ? 137 ARG B C   1 
ATOM   828  O O   . ARG A 1 144 ? 189.712 188.110 93.833  1.00 50.91  ? 137 ARG B O   1 
ATOM   829  C CB  . ARG A 1 144 ? 186.842 187.700 93.129  1.00 55.76  ? 137 ARG B CB  1 
ATOM   830  C CG  . ARG A 1 144 ? 186.493 188.582 94.303  1.00 50.57  ? 137 ARG B CG  1 
ATOM   831  C CD  . ARG A 1 144 ? 185.885 189.874 93.822  1.00 61.34  ? 137 ARG B CD  1 
ATOM   832  N NE  . ARG A 1 144 ? 184.520 189.674 93.355  1.00 76.24  ? 137 ARG B NE  1 
ATOM   833  C CZ  . ARG A 1 144 ? 183.878 190.503 92.544  1.00 81.92  ? 137 ARG B CZ  1 
ATOM   834  N NH1 . ARG A 1 144 ? 184.448 191.609 92.095  1.00 82.89  ? 137 ARG B NH1 1 
ATOM   835  N NH2 . ARG A 1 144 ? 182.636 190.214 92.172  1.00 81.11  ? 137 ARG B NH2 1 
ATOM   836  N N   . VAL A 1 145 ? 189.162 186.747 95.534  1.00 50.88  ? 138 VAL B N   1 
ATOM   837  C CA  . VAL A 1 145 ? 190.260 187.161 96.398  1.00 39.79  ? 138 VAL B CA  1 
ATOM   838  C C   . VAL A 1 145 ? 190.989 185.911 96.872  1.00 45.46  ? 138 VAL B C   1 
ATOM   839  O O   . VAL A 1 145 ? 190.354 184.911 97.223  1.00 45.54  ? 138 VAL B O   1 
ATOM   840  C CB  . VAL A 1 145 ? 189.771 188.004 97.590  1.00 34.15  ? 138 VAL B CB  1 
ATOM   841  C CG1 . VAL A 1 145 ? 189.410 189.404 97.130  1.00 39.44  ? 138 VAL B CG1 1 
ATOM   842  C CG2 . VAL A 1 145 ? 188.598 187.354 98.261  1.00 37.75  ? 138 VAL B CG2 1 
ATOM   843  N N   . LEU A 1 146 ? 192.322 185.966 96.854  1.00 43.42  ? 139 LEU B N   1 
ATOM   844  C CA  . LEU A 1 146 ? 193.129 184.813 97.240  1.00 38.25  ? 139 LEU B CA  1 
ATOM   845  C C   . LEU A 1 146 ? 192.963 184.479 98.717  1.00 38.61  ? 139 LEU B C   1 
ATOM   846  O O   . LEU A 1 146 ? 192.868 183.303 99.085  1.00 45.39  ? 139 LEU B O   1 
ATOM   847  C CB  . LEU A 1 146 ? 194.595 185.080 96.910  1.00 41.91  ? 139 LEU B CB  1 
ATOM   848  C CG  . LEU A 1 146 ? 195.617 184.058 97.401  1.00 44.84  ? 139 LEU B CG  1 
ATOM   849  C CD1 . LEU A 1 146 ? 195.708 182.888 96.441  1.00 44.61  ? 139 LEU B CD1 1 
ATOM   850  C CD2 . LEU A 1 146 ? 196.969 184.720 97.572  1.00 40.49  ? 139 LEU B CD2 1 
ATOM   851  N N   . ALA A 1 147 ? 192.933 185.492 99.577  1.00 33.58  ? 140 ALA B N   1 
ATOM   852  C CA  . ALA A 1 147 ? 192.777 185.288 101.009 1.00 29.71  ? 140 ALA B CA  1 
ATOM   853  C C   . ALA A 1 147 ? 192.054 186.493 101.590 1.00 35.34  ? 140 ALA B C   1 
ATOM   854  O O   . ALA A 1 147 ? 191.791 187.477 100.896 1.00 38.59  ? 140 ALA B O   1 
ATOM   855  C CB  . ALA A 1 147 ? 194.129 185.064 101.690 1.00 30.04  ? 140 ALA B CB  1 
ATOM   856  N N   . VAL A 1 148 ? 191.723 186.407 102.874 1.00 33.83  ? 141 VAL B N   1 
ATOM   857  C CA  . VAL A 1 148 ? 191.001 187.461 103.575 1.00 28.62  ? 141 VAL B CA  1 
ATOM   858  C C   . VAL A 1 148 ? 191.754 187.791 104.854 1.00 26.62  ? 141 VAL B C   1 
ATOM   859  O O   . VAL A 1 148 ? 192.079 186.893 105.636 1.00 31.49  ? 141 VAL B O   1 
ATOM   860  C CB  . VAL A 1 148 ? 189.551 187.044 103.891 1.00 26.15  ? 141 VAL B CB  1 
ATOM   861  C CG1 . VAL A 1 148 ? 188.878 188.074 104.778 1.00 22.71  ? 141 VAL B CG1 1 
ATOM   862  C CG2 . VAL A 1 148 ? 188.765 186.849 102.612 1.00 33.38  ? 141 VAL B CG2 1 
ATOM   863  N N   . ILE A 1 149 ? 192.036 189.074 105.063 1.00 23.33  ? 142 ILE B N   1 
ATOM   864  C CA  . ILE A 1 149 ? 192.613 189.554 106.314 1.00 24.97  ? 142 ILE B CA  1 
ATOM   865  C C   . ILE A 1 149 ? 191.435 189.879 107.227 1.00 25.89  ? 142 ILE B C   1 
ATOM   866  O O   . ILE A 1 149 ? 190.865 190.967 107.169 1.00 28.85  ? 142 ILE B O   1 
ATOM   867  C CB  . ILE A 1 149 ? 193.534 190.753 106.093 1.00 25.84  ? 142 ILE B CB  1 
ATOM   868  C CG1 . ILE A 1 149 ? 194.573 190.424 105.021 1.00 22.00  ? 142 ILE B CG1 1 
ATOM   869  C CG2 . ILE A 1 149 ? 194.219 191.150 107.387 1.00 26.31  ? 142 ILE B CG2 1 
ATOM   870  C CD1 . ILE A 1 149 ? 195.340 189.156 105.271 1.00 22.06  ? 142 ILE B CD1 1 
ATOM   871  N N   . GLY A 1 150 ? 191.084 188.922 108.083 1.00 33.21  ? 143 GLY B N   1 
ATOM   872  C CA  . GLY A 1 150 ? 189.778 188.849 108.690 1.00 30.02  ? 143 GLY B CA  1 
ATOM   873  C C   . GLY A 1 150 ? 189.480 189.948 109.680 1.00 35.31  ? 143 GLY B C   1 
ATOM   874  O O   . GLY A 1 150 ? 190.299 190.833 109.934 1.00 37.55  ? 143 GLY B O   1 
ATOM   875  N N   . PRO A 1 151 ? 188.287 189.902 110.264 1.00 38.27  ? 144 PRO B N   1 
ATOM   876  C CA  . PRO A 1 151 ? 187.838 190.998 111.123 1.00 36.08  ? 144 PRO B CA  1 
ATOM   877  C C   . PRO A 1 151 ? 188.636 191.073 112.414 1.00 37.25  ? 144 PRO B C   1 
ATOM   878  O O   . PRO A 1 151 ? 189.251 190.105 112.863 1.00 34.22  ? 144 PRO B O   1 
ATOM   879  C CB  . PRO A 1 151 ? 186.368 190.658 111.404 1.00 40.06  ? 144 PRO B CB  1 
ATOM   880  C CG  . PRO A 1 151 ? 186.031 189.506 110.509 1.00 39.34  ? 144 PRO B CG  1 
ATOM   881  C CD  . PRO A 1 151 ? 187.312 188.805 110.223 1.00 37.55  ? 144 PRO B CD  1 
ATOM   882  N N   . HIS A 1 152 ? 188.623 192.266 113.006 1.00 42.96  ? 145 HIS B N   1 
ATOM   883  C CA  . HIS A 1 152 ? 189.242 192.448 114.312 1.00 43.93  ? 145 HIS B CA  1 
ATOM   884  C C   . HIS A 1 152 ? 188.394 191.821 115.411 1.00 44.13  ? 145 HIS B C   1 
ATOM   885  O O   . HIS A 1 152 ? 188.928 191.212 116.344 1.00 46.29  ? 145 HIS B O   1 
ATOM   886  C CB  . HIS A 1 152 ? 189.458 193.937 114.579 1.00 46.81  ? 145 HIS B CB  1 
ATOM   887  C CG  . HIS A 1 152 ? 190.146 194.225 115.875 1.00 51.58  ? 145 HIS B CG  1 
ATOM   888  N ND1 . HIS A 1 152 ? 189.460 194.538 117.028 1.00 56.02  ? 145 HIS B ND1 1 
ATOM   889  C CD2 . HIS A 1 152 ? 191.459 194.248 116.200 1.00 52.72  ? 145 HIS B CD2 1 
ATOM   890  C CE1 . HIS A 1 152 ? 190.322 194.741 118.008 1.00 58.49  ? 145 HIS B CE1 1 
ATOM   891  N NE2 . HIS A 1 152 ? 191.542 194.571 117.531 1.00 57.23  ? 145 HIS B NE2 1 
ATOM   892  N N   . SER A 1 153 ? 187.074 191.961 115.316 1.00 48.47  ? 146 SER B N   1 
ATOM   893  C CA  . SER A 1 153 ? 186.182 191.446 116.345 1.00 47.30  ? 146 SER B CA  1 
ATOM   894  C C   . SER A 1 153 ? 186.236 189.928 116.393 1.00 47.22  ? 146 SER B C   1 
ATOM   895  O O   . SER A 1 153 ? 186.399 189.265 115.368 1.00 48.49  ? 146 SER B O   1 
ATOM   896  C CB  . SER A 1 153 ? 184.750 191.909 116.087 1.00 53.74  ? 146 SER B CB  1 
ATOM   897  O OG  . SER A 1 153 ? 184.639 193.315 116.202 1.00 63.77  ? 146 SER B OG  1 
ATOM   898  N N   . SER A 1 154 ? 186.109 189.378 117.599 1.00 48.48  ? 147 SER B N   1 
ATOM   899  C CA  . SER A 1 154 ? 186.124 187.930 117.758 1.00 46.98  ? 147 SER B CA  1 
ATOM   900  C C   . SER A 1 154 ? 184.794 187.305 117.354 1.00 51.87  ? 147 SER B C   1 
ATOM   901  O O   . SER A 1 154 ? 184.770 186.206 116.793 1.00 52.01  ? 147 SER B O   1 
ATOM   902  C CB  . SER A 1 154 ? 186.473 187.568 119.198 1.00 55.19  ? 147 SER B CB  1 
ATOM   903  O OG  . SER A 1 154 ? 186.897 186.223 119.286 1.00 62.03  ? 147 SER B OG  1 
ATOM   904  N N   . GLU A 1 155 ? 183.679 187.981 117.639 1.00 58.75  ? 148 GLU B N   1 
ATOM   905  C CA  . GLU A 1 155 ? 182.378 187.486 117.196 1.00 59.37  ? 148 GLU B CA  1 
ATOM   906  C C   . GLU A 1 155 ? 182.246 187.573 115.681 1.00 55.69  ? 148 GLU B C   1 
ATOM   907  O O   . GLU A 1 155 ? 181.746 186.643 115.031 1.00 56.87  ? 148 GLU B O   1 
ATOM   908  C CB  . GLU A 1 155 ? 181.264 188.280 117.876 1.00 61.63  ? 148 GLU B CB  1 
ATOM   909  C CG  . GLU A 1 155 ? 181.077 187.944 119.343 1.00 77.11  ? 148 GLU B CG  1 
ATOM   910  C CD  . GLU A 1 155 ? 181.690 188.989 120.255 1.00 84.16  ? 148 GLU B CD  1 
ATOM   911  O OE1 . GLU A 1 155 ? 182.527 189.782 119.774 1.00 71.84  ? 148 GLU B OE1 1 
ATOM   912  O OE2 . GLU A 1 155 ? 181.334 189.020 121.452 1.00 86.95  ? 148 GLU B OE2 1 
ATOM   913  N N   . LEU A 1 156 ? 182.686 188.691 115.104 1.00 48.33  ? 149 LEU B N   1 
ATOM   914  C CA  . LEU A 1 156 ? 182.711 188.814 113.655 1.00 49.66  ? 149 LEU B CA  1 
ATOM   915  C C   . LEU A 1 156 ? 183.650 187.791 113.041 1.00 44.60  ? 149 LEU B C   1 
ATOM   916  O O   . LEU A 1 156 ? 183.360 187.230 111.979 1.00 42.40  ? 149 LEU B O   1 
ATOM   917  C CB  . LEU A 1 156 ? 183.122 190.229 113.258 1.00 50.72  ? 149 LEU B CB  1 
ATOM   918  C CG  . LEU A 1 156 ? 182.002 191.053 112.640 1.00 44.90  ? 149 LEU B CG  1 
ATOM   919  C CD1 . LEU A 1 156 ? 182.555 192.321 112.034 1.00 55.94  ? 149 LEU B CD1 1 
ATOM   920  C CD2 . LEU A 1 156 ? 181.311 190.210 111.598 1.00 45.40  ? 149 LEU B CD2 1 
ATOM   921  N N   . ALA A 1 157 ? 184.791 187.547 113.689 1.00 45.90  ? 150 ALA B N   1 
ATOM   922  C CA  . ALA A 1 157 ? 185.692 186.502 113.222 1.00 41.39  ? 150 ALA B CA  1 
ATOM   923  C C   . ALA A 1 157 ? 185.006 185.148 113.246 1.00 44.42  ? 150 ALA B C   1 
ATOM   924  O O   . ALA A 1 157 ? 185.158 184.359 112.314 1.00 49.95  ? 150 ALA B O   1 
ATOM   925  C CB  . ALA A 1 157 ? 186.963 186.471 114.067 1.00 42.93  ? 150 ALA B CB  1 
ATOM   926  N N   . MET A 1 158 ? 184.226 184.869 114.290 1.00 45.05  ? 151 MET B N   1 
ATOM   927  C CA  . MET A 1 158 ? 183.498 183.607 114.349 1.00 46.46  ? 151 MET B CA  1 
ATOM   928  C C   . MET A 1 158 ? 182.533 183.475 113.179 1.00 45.55  ? 151 MET B C   1 
ATOM   929  O O   . MET A 1 158 ? 182.529 182.459 112.475 1.00 47.31  ? 151 MET B O   1 
ATOM   930  C CB  . MET A 1 158 ? 182.742 183.496 115.671 1.00 50.88  ? 151 MET B CB  1 
ATOM   931  C CG  . MET A 1 158 ? 182.929 182.164 116.353 1.00 60.26  ? 151 MET B CG  1 
ATOM   932  S SD  . MET A 1 158 ? 184.283 182.239 117.525 1.00 73.59  ? 151 MET B SD  1 
ATOM   933  C CE  . MET A 1 158 ? 183.528 183.241 118.788 1.00 66.13  ? 151 MET B CE  1 
ATOM   934  N N   . VAL A 1 159 ? 181.718 184.505 112.948 1.00 48.14  ? 152 VAL B N   1 
ATOM   935  C CA  . VAL A 1 159 ? 180.711 184.435 111.888 1.00 44.11  ? 152 VAL B CA  1 
ATOM   936  C C   . VAL A 1 159 ? 181.375 184.278 110.523 1.00 46.59  ? 152 VAL B C   1 
ATOM   937  O O   . VAL A 1 159 ? 181.042 183.372 109.744 1.00 44.36  ? 152 VAL B O   1 
ATOM   938  C CB  . VAL A 1 159 ? 179.802 185.676 111.929 1.00 45.52  ? 152 VAL B CB  1 
ATOM   939  C CG1 . VAL A 1 159 ? 178.802 185.642 110.785 1.00 51.90  ? 152 VAL B CG1 1 
ATOM   940  C CG2 . VAL A 1 159 ? 179.087 185.764 113.260 1.00 45.32  ? 152 VAL B CG2 1 
ATOM   941  N N   . THR A 1 160 ? 182.344 185.144 110.221 1.00 47.14  ? 153 THR B N   1 
ATOM   942  C CA  . THR A 1 160 ? 182.950 185.121 108.896 1.00 38.59  ? 153 THR B CA  1 
ATOM   943  C C   . THR A 1 160 ? 183.808 183.881 108.699 1.00 41.75  ? 153 THR B C   1 
ATOM   944  O O   . THR A 1 160 ? 183.894 183.362 107.586 1.00 49.68  ? 153 THR B O   1 
ATOM   945  C CB  . THR A 1 160 ? 183.773 186.385 108.660 1.00 41.65  ? 153 THR B CB  1 
ATOM   946  O OG1 . THR A 1 160 ? 184.731 186.540 109.711 1.00 51.00  ? 153 THR B OG1 1 
ATOM   947  C CG2 . THR A 1 160 ? 182.869 187.603 108.621 1.00 43.81  ? 153 THR B CG2 1 
ATOM   948  N N   . GLY A 1 161 ? 184.456 183.388 109.757 1.00 43.04  ? 154 GLY B N   1 
ATOM   949  C CA  . GLY A 1 161 ? 185.227 182.166 109.634 1.00 40.17  ? 154 GLY B CA  1 
ATOM   950  C C   . GLY A 1 161 ? 184.352 180.951 109.415 1.00 41.38  ? 154 GLY B C   1 
ATOM   951  O O   . GLY A 1 161 ? 184.690 180.069 108.624 1.00 46.74  ? 154 GLY B O   1 
ATOM   952  N N   . LYS A 1 162 ? 183.211 180.890 110.104 1.00 45.73  ? 155 LYS B N   1 
ATOM   953  C CA  . LYS A 1 162 ? 182.261 179.820 109.839 1.00 44.18  ? 155 LYS B CA  1 
ATOM   954  C C   . LYS A 1 162 ? 181.770 179.871 108.402 1.00 47.97  ? 155 LYS B C   1 
ATOM   955  O O   . LYS A 1 162 ? 181.602 178.826 107.766 1.00 48.84  ? 155 LYS B O   1 
ATOM   956  C CB  . LYS A 1 162 ? 181.089 179.910 110.813 1.00 42.71  ? 155 LYS B CB  1 
ATOM   957  C CG  . LYS A 1 162 ? 180.529 178.570 111.232 1.00 48.76  ? 155 LYS B CG  1 
ATOM   958  C CD  . LYS A 1 162 ? 180.857 178.279 112.683 1.00 52.30  ? 155 LYS B CD  1 
ATOM   959  C CE  . LYS A 1 162 ? 180.216 179.301 113.603 1.00 50.60  ? 155 LYS B CE  1 
ATOM   960  N NZ  . LYS A 1 162 ? 180.376 178.933 115.036 1.00 57.33  ? 155 LYS B NZ  1 
ATOM   961  N N   . PHE A 1 163 ? 181.541 181.075 107.871 1.00 49.29  ? 156 PHE B N   1 
ATOM   962  C CA  . PHE A 1 163 ? 181.131 181.193 106.474 1.00 38.22  ? 156 PHE B CA  1 
ATOM   963  C C   . PHE A 1 163 ? 182.249 180.781 105.517 1.00 40.43  ? 156 PHE B C   1 
ATOM   964  O O   . PHE A 1 163 ? 182.008 180.046 104.554 1.00 44.91  ? 156 PHE B O   1 
ATOM   965  C CB  . PHE A 1 163 ? 180.679 182.622 106.184 1.00 37.00  ? 156 PHE B CB  1 
ATOM   966  C CG  . PHE A 1 163 ? 180.225 182.839 104.774 1.00 40.66  ? 156 PHE B CG  1 
ATOM   967  C CD1 . PHE A 1 163 ? 179.220 182.064 104.230 1.00 46.54  ? 156 PHE B CD1 1 
ATOM   968  C CD2 . PHE A 1 163 ? 180.808 183.815 103.990 1.00 42.97  ? 156 PHE B CD2 1 
ATOM   969  C CE1 . PHE A 1 163 ? 178.802 182.262 102.934 1.00 49.61  ? 156 PHE B CE1 1 
ATOM   970  C CE2 . PHE A 1 163 ? 180.391 184.017 102.697 1.00 48.08  ? 156 PHE B CE2 1 
ATOM   971  C CZ  . PHE A 1 163 ? 179.392 183.238 102.165 1.00 49.48  ? 156 PHE B CZ  1 
ATOM   972  N N   . PHE A 1 164 ? 183.475 181.249 105.763 1.00 42.23  ? 157 PHE B N   1 
ATOM   973  C CA  . PHE A 1 164 ? 184.603 181.006 104.869 1.00 40.19  ? 157 PHE B CA  1 
ATOM   974  C C   . PHE A 1 164 ? 185.088 179.566 104.909 1.00 45.21  ? 157 PHE B C   1 
ATOM   975  O O   . PHE A 1 164 ? 185.721 179.114 103.950 1.00 48.36  ? 157 PHE B O   1 
ATOM   976  C CB  . PHE A 1 164 ? 185.772 181.926 105.230 1.00 40.62  ? 157 PHE B CB  1 
ATOM   977  C CG  . PHE A 1 164 ? 185.560 183.364 104.860 1.00 40.48  ? 157 PHE B CG  1 
ATOM   978  C CD1 . PHE A 1 164 ? 184.889 183.709 103.704 1.00 48.05  ? 157 PHE B CD1 1 
ATOM   979  C CD2 . PHE A 1 164 ? 186.034 184.373 105.674 1.00 36.08  ? 157 PHE B CD2 1 
ATOM   980  C CE1 . PHE A 1 164 ? 184.699 185.031 103.368 1.00 39.52  ? 157 PHE B CE1 1 
ATOM   981  C CE2 . PHE A 1 164 ? 185.843 185.694 105.344 1.00 38.24  ? 157 PHE B CE2 1 
ATOM   982  C CZ  . PHE A 1 164 ? 185.175 186.022 104.190 1.00 35.27  ? 157 PHE B CZ  1 
ATOM   983  N N   . SER A 1 165 ? 184.826 178.844 105.999 1.00 46.41  ? 158 SER B N   1 
ATOM   984  C CA  . SER A 1 165 ? 185.330 177.483 106.124 1.00 43.27  ? 158 SER B CA  1 
ATOM   985  C C   . SER A 1 165 ? 184.671 176.539 105.131 1.00 46.37  ? 158 SER B C   1 
ATOM   986  O O   . SER A 1 165 ? 185.263 175.521 104.758 1.00 53.03  ? 158 SER B O   1 
ATOM   987  C CB  . SER A 1 165 ? 185.120 176.992 107.551 1.00 42.91  ? 158 SER B CB  1 
ATOM   988  O OG  . SER A 1 165 ? 186.063 177.592 108.420 1.00 46.01  ? 158 SER B OG  1 
ATOM   989  N N   . PHE A 1 166 ? 183.448 176.849 104.698 1.00 48.12  ? 159 PHE B N   1 
ATOM   990  C CA  . PHE A 1 166 ? 182.804 176.040 103.670 1.00 48.58  ? 159 PHE B CA  1 
ATOM   991  C C   . PHE A 1 166 ? 183.587 176.088 102.366 1.00 45.25  ? 159 PHE B C   1 
ATOM   992  O O   . PHE A 1 166 ? 183.706 175.076 101.667 1.00 48.48  ? 159 PHE B O   1 
ATOM   993  C CB  . PHE A 1 166 ? 181.369 176.515 103.449 1.00 51.15  ? 159 PHE B CB  1 
ATOM   994  C CG  . PHE A 1 166 ? 180.681 175.847 102.297 1.00 50.88  ? 159 PHE B CG  1 
ATOM   995  C CD1 . PHE A 1 166 ? 180.371 174.501 102.344 1.00 53.83  ? 159 PHE B CD1 1 
ATOM   996  C CD2 . PHE A 1 166 ? 180.358 176.562 101.160 1.00 52.75  ? 159 PHE B CD2 1 
ATOM   997  C CE1 . PHE A 1 166 ? 179.744 173.886 101.283 1.00 66.23  ? 159 PHE B CE1 1 
ATOM   998  C CE2 . PHE A 1 166 ? 179.732 175.953 100.097 1.00 56.83  ? 159 PHE B CE2 1 
ATOM   999  C CZ  . PHE A 1 166 ? 179.424 174.613 100.158 1.00 67.76  ? 159 PHE B CZ  1 
ATOM   1000 N N   . PHE A 1 167 ? 184.125 177.253 102.024 1.00 47.55  ? 160 PHE B N   1 
ATOM   1001 C CA  . PHE A 1 167 ? 184.855 177.456 100.782 1.00 47.86  ? 160 PHE B CA  1 
ATOM   1002 C C   . PHE A 1 167 ? 186.355 177.247 100.932 1.00 45.48  ? 160 PHE B C   1 
ATOM   1003 O O   . PHE A 1 167 ? 187.080 177.367 99.940  1.00 47.94  ? 160 PHE B O   1 
ATOM   1004 C CB  . PHE A 1 167 ? 184.593 178.864 100.243 1.00 48.00  ? 160 PHE B CB  1 
ATOM   1005 C CG  . PHE A 1 167 ? 183.145 179.268 100.259 1.00 46.90  ? 160 PHE B CG  1 
ATOM   1006 C CD1 . PHE A 1 167 ? 182.565 179.781 101.405 1.00 43.89  ? 160 PHE B CD1 1 
ATOM   1007 C CD2 . PHE A 1 167 ? 182.370 179.151 99.121  1.00 51.75  ? 160 PHE B CD2 1 
ATOM   1008 C CE1 . PHE A 1 167 ? 181.240 180.153 101.418 1.00 47.31  ? 160 PHE B CE1 1 
ATOM   1009 C CE2 . PHE A 1 167 ? 181.046 179.525 99.129  1.00 51.48  ? 160 PHE B CE2 1 
ATOM   1010 C CZ  . PHE A 1 167 ? 180.481 180.027 100.278 1.00 48.54  ? 160 PHE B CZ  1 
ATOM   1011 N N   . LEU A 1 168 ? 186.830 176.951 102.142 1.00 45.22  ? 161 LEU B N   1 
ATOM   1012 C CA  . LEU A 1 168 ? 188.254 176.751 102.417 1.00 50.19  ? 161 LEU B CA  1 
ATOM   1013 C C   . LEU A 1 168 ? 189.087 177.951 101.976 1.00 46.27  ? 161 LEU B C   1 
ATOM   1014 O O   . LEU A 1 168 ? 190.199 177.808 101.468 1.00 45.84  ? 161 LEU B O   1 
ATOM   1015 C CB  . LEU A 1 168 ? 188.771 175.465 101.771 1.00 54.60  ? 161 LEU B CB  1 
ATOM   1016 C CG  . LEU A 1 168 ? 188.488 174.166 102.522 1.00 46.97  ? 161 LEU B CG  1 
ATOM   1017 C CD1 . LEU A 1 168 ? 189.548 173.139 102.190 1.00 60.34  ? 161 LEU B CD1 1 
ATOM   1018 C CD2 . LEU A 1 168 ? 188.435 174.410 104.017 1.00 39.46  ? 161 LEU B CD2 1 
ATOM   1019 N N   . MET A 1 169 ? 188.542 179.143 102.169 1.00 42.97  ? 162 MET B N   1 
ATOM   1020 C CA  . MET A 1 169 ? 189.278 180.365 101.883 1.00 43.77  ? 162 MET B CA  1 
ATOM   1021 C C   . MET A 1 169 ? 190.151 180.726 103.077 1.00 38.82  ? 162 MET B C   1 
ATOM   1022 O O   . MET A 1 169 ? 189.630 180.865 104.189 1.00 35.66  ? 162 MET B O   1 
ATOM   1023 C CB  . MET A 1 169 ? 188.317 181.500 101.565 1.00 45.39  ? 162 MET B CB  1 
ATOM   1024 C CG  . MET A 1 169 ? 188.939 182.881 101.620 1.00 39.53  ? 162 MET B CG  1 
ATOM   1025 S SD  . MET A 1 169 ? 189.289 183.514 99.978  1.00 42.87  ? 162 MET B SD  1 
ATOM   1026 C CE  . MET A 1 169 ? 187.712 184.251 99.595  1.00 49.49  ? 162 MET B CE  1 
ATOM   1027 N N   . PRO A 1 170 ? 191.466 180.872 102.903 1.00 36.61  ? 163 PRO B N   1 
ATOM   1028 C CA  . PRO A 1 170 ? 192.326 181.200 104.046 1.00 33.10  ? 163 PRO B CA  1 
ATOM   1029 C C   . PRO A 1 170 ? 192.047 182.589 104.584 1.00 31.72  ? 163 PRO B C   1 
ATOM   1030 O O   . PRO A 1 170 ? 192.076 183.572 103.840 1.00 38.75  ? 163 PRO B O   1 
ATOM   1031 C CB  . PRO A 1 170 ? 193.740 181.087 103.466 1.00 30.91  ? 163 PRO B CB  1 
ATOM   1032 C CG  . PRO A 1 170 ? 193.572 181.297 102.018 1.00 31.40  ? 163 PRO B CG  1 
ATOM   1033 C CD  . PRO A 1 170 ? 192.233 180.745 101.655 1.00 32.23  ? 163 PRO B CD  1 
ATOM   1034 N N   . GLN A 1 171 ? 191.767 182.682 105.878 1.00 29.55  ? 164 GLN B N   1 
ATOM   1035 C CA  . GLN A 1 171 ? 191.439 183.944 106.522 1.00 26.43  ? 164 GLN B CA  1 
ATOM   1036 C C   . GLN A 1 171 ? 192.285 184.084 107.776 1.00 28.50  ? 164 GLN B C   1 
ATOM   1037 O O   . GLN A 1 171 ? 192.042 183.396 108.770 1.00 34.48  ? 164 GLN B O   1 
ATOM   1038 C CB  . GLN A 1 171 ? 189.950 184.006 106.860 1.00 31.63  ? 164 GLN B CB  1 
ATOM   1039 C CG  . GLN A 1 171 ? 189.571 185.055 107.879 1.00 31.20  ? 164 GLN B CG  1 
ATOM   1040 C CD  . GLN A 1 171 ? 188.300 184.697 108.605 1.00 36.82  ? 164 GLN B CD  1 
ATOM   1041 O OE1 . GLN A 1 171 ? 187.963 183.524 108.731 1.00 39.12  ? 164 GLN B OE1 1 
ATOM   1042 N NE2 . GLN A 1 171 ? 187.581 185.703 109.078 1.00 37.67  ? 164 GLN B NE2 1 
ATOM   1043 N N   . VAL A 1 172 ? 193.276 184.968 107.729 1.00 27.02  ? 165 VAL B N   1 
ATOM   1044 C CA  . VAL A 1 172 ? 194.115 185.269 108.880 1.00 29.07  ? 165 VAL B CA  1 
ATOM   1045 C C   . VAL A 1 172 ? 193.643 186.584 109.481 1.00 27.39  ? 165 VAL B C   1 
ATOM   1046 O O   . VAL A 1 172 ? 193.480 187.582 108.772 1.00 28.47  ? 165 VAL B O   1 
ATOM   1047 C CB  . VAL A 1 172 ? 195.610 185.319 108.508 1.00 26.68  ? 165 VAL B CB  1 
ATOM   1048 C CG1 . VAL A 1 172 ? 195.821 186.180 107.303 1.00 29.48  ? 165 VAL B CG1 1 
ATOM   1049 C CG2 . VAL A 1 172 ? 196.433 185.834 109.673 1.00 28.38  ? 165 VAL B CG2 1 
ATOM   1050 N N   . SER A 1 173 ? 193.411 186.578 110.787 1.00 30.97  ? 166 SER B N   1 
ATOM   1051 C CA  . SER A 1 173 ? 192.781 187.688 111.477 1.00 32.10  ? 166 SER B CA  1 
ATOM   1052 C C   . SER A 1 173 ? 193.751 188.340 112.451 1.00 33.15  ? 166 SER B C   1 
ATOM   1053 O O   . SER A 1 173 ? 194.665 187.699 112.973 1.00 35.94  ? 166 SER B O   1 
ATOM   1054 C CB  . SER A 1 173 ? 191.531 187.225 112.227 1.00 33.99  ? 166 SER B CB  1 
ATOM   1055 O OG  . SER A 1 173 ? 191.168 188.152 113.229 1.00 32.20  ? 166 SER B OG  1 
ATOM   1056 N N   . TYR A 1 174 ? 193.543 189.630 112.676 1.00 34.31  ? 167 TYR B N   1 
ATOM   1057 C CA  . TYR A 1 174 ? 194.272 190.408 113.663 1.00 35.56  ? 167 TYR B CA  1 
ATOM   1058 C C   . TYR A 1 174 ? 193.325 190.750 114.805 1.00 41.51  ? 167 TYR B C   1 
ATOM   1059 O O   . TYR A 1 174 ? 192.179 191.142 114.573 1.00 51.82  ? 167 TYR B O   1 
ATOM   1060 C CB  . TYR A 1 174 ? 194.828 191.690 113.036 1.00 37.14  ? 167 TYR B CB  1 
ATOM   1061 C CG  . TYR A 1 174 ? 193.754 192.498 112.345 1.00 37.64  ? 167 TYR B CG  1 
ATOM   1062 C CD1 . TYR A 1 174 ? 193.389 192.230 111.035 1.00 30.63  ? 167 TYR B CD1 1 
ATOM   1063 C CD2 . TYR A 1 174 ? 193.088 193.514 113.015 1.00 37.04  ? 167 TYR B CD2 1 
ATOM   1064 C CE1 . TYR A 1 174 ? 192.399 192.954 110.417 1.00 30.99  ? 167 TYR B CE1 1 
ATOM   1065 C CE2 . TYR A 1 174 ? 192.101 194.236 112.404 1.00 34.43  ? 167 TYR B CE2 1 
ATOM   1066 C CZ  . TYR A 1 174 ? 191.759 193.953 111.108 1.00 36.33  ? 167 TYR B CZ  1 
ATOM   1067 O OH  . TYR A 1 174 ? 190.767 194.681 110.507 1.00 41.20  ? 167 TYR B OH  1 
ATOM   1068 N N   . GLY A 1 175 ? 193.781 190.567 116.036 1.00 42.22  ? 168 GLY B N   1 
ATOM   1069 C CA  . GLY A 1 175 ? 193.007 190.980 117.185 1.00 48.37  ? 168 GLY B CA  1 
ATOM   1070 C C   . GLY A 1 175 ? 191.858 190.077 117.574 1.00 49.61  ? 168 GLY B C   1 
ATOM   1071 O O   . GLY A 1 175 ? 191.178 190.370 118.565 1.00 55.46  ? 168 GLY B O   1 
ATOM   1072 N N   . ALA A 1 176 ? 191.606 188.999 116.838 1.00 41.11  ? 169 ALA B N   1 
ATOM   1073 C CA  . ALA A 1 176 ? 190.604 188.020 117.244 1.00 42.11  ? 169 ALA B CA  1 
ATOM   1074 C C   . ALA A 1 176 ? 191.278 186.959 118.101 1.00 49.29  ? 169 ALA B C   1 
ATOM   1075 O O   . ALA A 1 176 ? 192.042 186.136 117.589 1.00 48.28  ? 169 ALA B O   1 
ATOM   1076 C CB  . ALA A 1 176 ? 189.934 187.390 116.029 1.00 42.55  ? 169 ALA B CB  1 
ATOM   1077 N N   . SER A 1 177 ? 190.992 186.972 119.401 1.00 52.74  ? 170 SER B N   1 
ATOM   1078 C CA  . SER A 1 177 ? 191.774 186.208 120.358 1.00 50.99  ? 170 SER B CA  1 
ATOM   1079 C C   . SER A 1 177 ? 191.024 185.080 121.046 1.00 49.86  ? 170 SER B C   1 
ATOM   1080 O O   . SER A 1 177 ? 191.672 184.239 121.675 1.00 55.29  ? 170 SER B O   1 
ATOM   1081 C CB  . SER A 1 177 ? 192.346 187.141 121.437 1.00 53.74  ? 170 SER B CB  1 
ATOM   1082 O OG  . SER A 1 177 ? 193.531 187.776 120.992 1.00 62.73  ? 170 SER B OG  1 
ATOM   1083 N N   . MET A 1 178 ? 189.700 185.022 120.952 1.00 48.63  ? 171 MET B N   1 
ATOM   1084 C CA  . MET A 1 178 ? 188.964 184.048 121.745 1.00 55.72  ? 171 MET B CA  1 
ATOM   1085 C C   . MET A 1 178 ? 189.246 182.629 121.259 1.00 56.46  ? 171 MET B C   1 
ATOM   1086 O O   . MET A 1 178 ? 189.350 182.363 120.060 1.00 60.25  ? 171 MET B O   1 
ATOM   1087 C CB  . MET A 1 178 ? 187.470 184.360 121.721 1.00 58.85  ? 171 MET B CB  1 
ATOM   1088 C CG  . MET A 1 178 ? 187.141 185.594 122.560 1.00 74.04  ? 171 MET B CG  1 
ATOM   1089 S SD  . MET A 1 178 ? 185.396 185.981 122.775 1.00 90.94  ? 171 MET B SD  1 
ATOM   1090 C CE  . MET A 1 178 ? 184.651 184.841 121.632 1.00 72.99  ? 171 MET B CE  1 
ATOM   1091 N N   . GLU A 1 179 ? 189.363 181.711 122.221 1.00 57.56  ? 172 GLU B N   1 
ATOM   1092 C CA  . GLU A 1 179 ? 190.043 180.441 121.979 1.00 58.34  ? 172 GLU B CA  1 
ATOM   1093 C C   . GLU A 1 179 ? 189.256 179.528 121.047 1.00 56.80  ? 172 GLU B C   1 
ATOM   1094 O O   . GLU A 1 179 ? 189.851 178.732 120.313 1.00 60.50  ? 172 GLU B O   1 
ATOM   1095 C CB  . GLU A 1 179 ? 190.311 179.742 123.312 1.00 61.98  ? 172 GLU B CB  1 
ATOM   1096 C CG  . GLU A 1 179 ? 190.807 178.302 123.228 1.00 58.73  ? 172 GLU B CG  1 
ATOM   1097 C CD  . GLU A 1 179 ? 192.135 178.164 122.506 1.00 64.70  ? 172 GLU B CD  1 
ATOM   1098 O OE1 . GLU A 1 179 ? 192.880 179.162 122.414 1.00 59.29  ? 172 GLU B OE1 1 
ATOM   1099 O OE2 . GLU A 1 179 ? 192.438 177.049 122.034 1.00 66.12  ? 172 GLU B OE2 1 
ATOM   1100 N N   . LEU A 1 180 ? 187.925 179.616 121.053 1.00 55.93  ? 173 LEU B N   1 
ATOM   1101 C CA  . LEU A 1 180 ? 187.160 178.624 120.303 1.00 58.16  ? 173 LEU B CA  1 
ATOM   1102 C C   . LEU A 1 180 ? 187.341 178.765 118.794 1.00 53.12  ? 173 LEU B C   1 
ATOM   1103 O O   . LEU A 1 180 ? 186.950 177.856 118.055 1.00 51.94  ? 173 LEU B O   1 
ATOM   1104 C CB  . LEU A 1 180 ? 185.677 178.699 120.692 1.00 60.93  ? 173 LEU B CB  1 
ATOM   1105 C CG  . LEU A 1 180 ? 184.561 177.858 120.066 1.00 66.40  ? 173 LEU B CG  1 
ATOM   1106 C CD1 . LEU A 1 180 ? 184.789 176.372 120.341 1.00 56.07  ? 173 LEU B CD1 1 
ATOM   1107 C CD2 . LEU A 1 180 ? 183.193 178.292 120.558 1.00 67.79  ? 173 LEU B CD2 1 
ATOM   1108 N N   . LEU A 1 181 ? 187.934 179.866 118.329 1.00 49.69  ? 174 LEU B N   1 
ATOM   1109 C CA  . LEU A 1 181 ? 188.316 180.021 116.930 1.00 47.46  ? 174 LEU B CA  1 
ATOM   1110 C C   . LEU A 1 181 ? 189.440 179.083 116.522 1.00 47.48  ? 174 LEU B C   1 
ATOM   1111 O O   . LEU A 1 181 ? 189.731 178.973 115.327 1.00 48.09  ? 174 LEU B O   1 
ATOM   1112 C CB  . LEU A 1 181 ? 188.740 181.465 116.663 1.00 42.82  ? 174 LEU B CB  1 
ATOM   1113 C CG  . LEU A 1 181 ? 187.630 182.488 116.449 1.00 45.87  ? 174 LEU B CG  1 
ATOM   1114 C CD1 . LEU A 1 181 ? 188.180 183.898 116.555 1.00 47.37  ? 174 LEU B CD1 1 
ATOM   1115 C CD2 . LEU A 1 181 ? 186.967 182.265 115.103 1.00 43.34  ? 174 LEU B CD2 1 
ATOM   1116 N N   . SER A 1 182 ? 190.084 178.425 117.480 1.00 44.37  ? 175 SER B N   1 
ATOM   1117 C CA  . SER A 1 182 ? 191.196 177.523 117.225 1.00 44.73  ? 175 SER B CA  1 
ATOM   1118 C C   . SER A 1 182 ? 190.752 176.108 116.889 1.00 48.50  ? 175 SER B C   1 
ATOM   1119 O O   . SER A 1 182 ? 191.602 175.255 116.623 1.00 46.86  ? 175 SER B O   1 
ATOM   1120 C CB  . SER A 1 182 ? 192.126 177.493 118.439 1.00 48.14  ? 175 SER B CB  1 
ATOM   1121 O OG  . SER A 1 182 ? 193.390 176.969 118.093 1.00 55.35  ? 175 SER B OG  1 
ATOM   1122 N N   . ALA A 1 183 ? 189.450 175.839 116.895 1.00 49.80  ? 176 ALA B N   1 
ATOM   1123 C CA  . ALA A 1 183 ? 188.942 174.501 116.620 1.00 45.00  ? 176 ALA B CA  1 
ATOM   1124 C C   . ALA A 1 183 ? 188.989 174.238 115.122 1.00 44.24  ? 176 ALA B C   1 
ATOM   1125 O O   . ALA A 1 183 ? 188.230 174.837 114.356 1.00 46.49  ? 176 ALA B O   1 
ATOM   1126 C CB  . ALA A 1 183 ? 187.521 174.360 117.154 1.00 41.51  ? 176 ALA B CB  1 
ATOM   1127 N N   . ARG A 1 184 ? 189.879 173.340 114.698 1.00 41.07  ? 177 ARG B N   1 
ATOM   1128 C CA  . ARG A 1 184 ? 189.980 172.994 113.286 1.00 39.26  ? 177 ARG B CA  1 
ATOM   1129 C C   . ARG A 1 184 ? 188.785 172.194 112.792 1.00 42.59  ? 177 ARG B C   1 
ATOM   1130 O O   . ARG A 1 184 ? 188.625 172.038 111.578 1.00 43.96  ? 177 ARG B O   1 
ATOM   1131 C CB  . ARG A 1 184 ? 191.267 172.214 113.031 1.00 41.14  ? 177 ARG B CB  1 
ATOM   1132 C CG  . ARG A 1 184 ? 192.528 172.937 113.469 1.00 45.14  ? 177 ARG B CG  1 
ATOM   1133 C CD  . ARG A 1 184 ? 192.751 174.195 112.656 1.00 42.66  ? 177 ARG B CD  1 
ATOM   1134 N NE  . ARG A 1 184 ? 192.184 175.373 113.301 1.00 44.70  ? 177 ARG B NE  1 
ATOM   1135 C CZ  . ARG A 1 184 ? 192.281 176.605 112.825 1.00 42.57  ? 177 ARG B CZ  1 
ATOM   1136 N NH1 . ARG A 1 184 ? 192.914 176.858 111.693 1.00 39.54  ? 177 ARG B NH1 1 
ATOM   1137 N NH2 . ARG A 1 184 ? 191.728 177.606 113.500 1.00 38.90  ? 177 ARG B NH2 1 
ATOM   1138 N N   . GLU A 1 185 ? 187.959 171.673 113.699 1.00 50.64  ? 178 GLU B N   1 
ATOM   1139 C CA  . GLU A 1 185 ? 186.744 170.982 113.285 1.00 53.09  ? 178 GLU B CA  1 
ATOM   1140 C C   . GLU A 1 185 ? 185.776 171.937 112.602 1.00 50.71  ? 178 GLU B C   1 
ATOM   1141 O O   . GLU A 1 185 ? 185.156 171.586 111.592 1.00 53.06  ? 178 GLU B O   1 
ATOM   1142 C CB  . GLU A 1 185 ? 186.086 170.320 114.495 1.00 60.75  ? 178 GLU B CB  1 
ATOM   1143 C CG  . GLU A 1 185 ? 184.641 169.908 114.276 1.00 74.37  ? 178 GLU B CG  1 
ATOM   1144 C CD  . GLU A 1 185 ? 184.141 168.950 115.340 1.00 93.32  ? 178 GLU B CD  1 
ATOM   1145 O OE1 . GLU A 1 185 ? 184.596 167.787 115.358 1.00 99.25  ? 178 GLU B OE1 1 
ATOM   1146 O OE2 . GLU A 1 185 ? 183.289 169.360 116.157 1.00 96.29  ? 178 GLU B OE2 1 
ATOM   1147 N N   . THR A 1 186 ? 185.641 173.153 113.132 1.00 46.89  ? 179 THR B N   1 
ATOM   1148 C CA  . THR A 1 186 ? 184.694 174.125 112.609 1.00 42.19  ? 179 THR B CA  1 
ATOM   1149 C C   . THR A 1 186 ? 185.351 175.318 111.928 1.00 44.57  ? 179 THR B C   1 
ATOM   1150 O O   . THR A 1 186 ? 184.654 176.069 111.237 1.00 46.34  ? 179 THR B O   1 
ATOM   1151 C CB  . THR A 1 186 ? 183.774 174.625 113.733 1.00 47.39  ? 179 THR B CB  1 
ATOM   1152 O OG1 . THR A 1 186 ? 184.383 175.736 114.394 1.00 46.41  ? 179 THR B OG1 1 
ATOM   1153 C CG2 . THR A 1 186 ? 183.528 173.526 114.750 1.00 53.96  ? 179 THR B CG2 1 
ATOM   1154 N N   . PHE A 1 187 ? 186.659 175.512 112.091 1.00 43.24  ? 180 PHE B N   1 
ATOM   1155 C CA  . PHE A 1 187 ? 187.397 176.582 111.417 1.00 38.09  ? 180 PHE B CA  1 
ATOM   1156 C C   . PHE A 1 187 ? 188.637 176.003 110.746 1.00 40.96  ? 180 PHE B C   1 
ATOM   1157 O O   . PHE A 1 187 ? 189.766 176.260 111.178 1.00 43.74  ? 180 PHE B O   1 
ATOM   1158 C CB  . PHE A 1 187 ? 187.788 177.690 112.396 1.00 37.66  ? 180 PHE B CB  1 
ATOM   1159 C CG  . PHE A 1 187 ? 186.626 178.308 113.111 1.00 39.50  ? 180 PHE B CG  1 
ATOM   1160 C CD1 . PHE A 1 187 ? 185.788 179.195 112.463 1.00 41.79  ? 180 PHE B CD1 1 
ATOM   1161 C CD2 . PHE A 1 187 ? 186.385 178.021 114.441 1.00 39.61  ? 180 PHE B CD2 1 
ATOM   1162 C CE1 . PHE A 1 187 ? 184.722 179.764 113.120 1.00 42.58  ? 180 PHE B CE1 1 
ATOM   1163 C CE2 . PHE A 1 187 ? 185.320 178.591 115.102 1.00 43.33  ? 180 PHE B CE2 1 
ATOM   1164 C CZ  . PHE A 1 187 ? 184.487 179.463 114.440 1.00 43.83  ? 180 PHE B CZ  1 
ATOM   1165 N N   . PRO A 1 188 ? 188.464 175.221 109.675 1.00 38.60  ? 181 PRO B N   1 
ATOM   1166 C CA  . PRO A 1 188 ? 189.629 174.642 108.989 1.00 37.28  ? 181 PRO B CA  1 
ATOM   1167 C C   . PRO A 1 188 ? 190.537 175.660 108.321 1.00 45.04  ? 181 PRO B C   1 
ATOM   1168 O O   . PRO A 1 188 ? 191.660 175.299 107.951 1.00 46.16  ? 181 PRO B O   1 
ATOM   1169 C CB  . PRO A 1 188 ? 188.997 173.716 107.943 1.00 38.65  ? 181 PRO B CB  1 
ATOM   1170 C CG  . PRO A 1 188 ? 187.624 173.471 108.422 1.00 42.62  ? 181 PRO B CG  1 
ATOM   1171 C CD  . PRO A 1 188 ? 187.203 174.714 109.115 1.00 40.07  ? 181 PRO B CD  1 
ATOM   1172 N N   . SER A 1 189 ? 190.097 176.902 108.131 1.00 44.58  ? 182 SER B N   1 
ATOM   1173 C CA  . SER A 1 189 ? 190.865 177.866 107.353 1.00 39.22  ? 182 SER B CA  1 
ATOM   1174 C C   . SER A 1 189 ? 190.974 179.211 108.058 1.00 34.87  ? 182 SER B C   1 
ATOM   1175 O O   . SER A 1 189 ? 191.138 180.241 107.405 1.00 36.09  ? 182 SER B O   1 
ATOM   1176 C CB  . SER A 1 189 ? 190.255 178.042 105.964 1.00 35.23  ? 182 SER B CB  1 
ATOM   1177 O OG  . SER A 1 189 ? 189.006 178.701 106.039 1.00 41.29  ? 182 SER B OG  1 
ATOM   1178 N N   . PHE A 1 190 ? 190.900 179.225 109.385 1.00 32.74  ? 183 PHE B N   1 
ATOM   1179 C CA  . PHE A 1 190 ? 191.021 180.456 110.156 1.00 29.99  ? 183 PHE B CA  1 
ATOM   1180 C C   . PHE A 1 190 ? 192.389 180.500 110.815 1.00 32.82  ? 183 PHE B C   1 
ATOM   1181 O O   . PHE A 1 190 ? 192.723 179.627 111.621 1.00 39.78  ? 183 PHE B O   1 
ATOM   1182 C CB  . PHE A 1 190 ? 189.921 180.570 111.212 1.00 32.13  ? 183 PHE B CB  1 
ATOM   1183 C CG  . PHE A 1 190 ? 190.027 181.809 112.053 1.00 34.80  ? 183 PHE B CG  1 
ATOM   1184 C CD1 . PHE A 1 190 ? 189.504 183.009 111.609 1.00 35.94  ? 183 PHE B CD1 1 
ATOM   1185 C CD2 . PHE A 1 190 ? 190.663 181.778 113.282 1.00 37.78  ? 183 PHE B CD2 1 
ATOM   1186 C CE1 . PHE A 1 190 ? 189.608 184.148 112.372 1.00 35.47  ? 183 PHE B CE1 1 
ATOM   1187 C CE2 . PHE A 1 190 ? 190.769 182.916 114.048 1.00 39.62  ? 183 PHE B CE2 1 
ATOM   1188 C CZ  . PHE A 1 190 ? 190.241 184.101 113.593 1.00 38.94  ? 183 PHE B CZ  1 
ATOM   1189 N N   . PHE A 1 191 ? 193.165 181.521 110.487 1.00 31.54  ? 184 PHE B N   1 
ATOM   1190 C CA  . PHE A 1 191 ? 194.455 181.785 111.096 1.00 27.56  ? 184 PHE B CA  1 
ATOM   1191 C C   . PHE A 1 191 ? 194.390 183.115 111.835 1.00 32.29  ? 184 PHE B C   1 
ATOM   1192 O O   . PHE A 1 191 ? 193.424 183.869 111.719 1.00 36.69  ? 184 PHE B O   1 
ATOM   1193 C CB  . PHE A 1 191 ? 195.556 181.783 110.036 1.00 29.03  ? 184 PHE B CB  1 
ATOM   1194 C CG  . PHE A 1 191 ? 195.741 180.455 109.364 1.00 37.07  ? 184 PHE B CG  1 
ATOM   1195 C CD1 . PHE A 1 191 ? 194.919 180.070 108.322 1.00 34.57  ? 184 PHE B CD1 1 
ATOM   1196 C CD2 . PHE A 1 191 ? 196.734 179.587 109.778 1.00 42.81  ? 184 PHE B CD2 1 
ATOM   1197 C CE1 . PHE A 1 191 ? 195.084 178.850 107.709 1.00 37.65  ? 184 PHE B CE1 1 
ATOM   1198 C CE2 . PHE A 1 191 ? 196.902 178.370 109.166 1.00 38.45  ? 184 PHE B CE2 1 
ATOM   1199 C CZ  . PHE A 1 191 ? 196.075 178.001 108.131 1.00 37.07  ? 184 PHE B CZ  1 
ATOM   1200 N N   . ARG A 1 192 ? 195.424 183.396 112.618 1.00 34.72  ? 185 ARG B N   1 
ATOM   1201 C CA  . ARG A 1 192 ? 195.474 184.649 113.354 1.00 33.39  ? 185 ARG B CA  1 
ATOM   1202 C C   . ARG A 1 192 ? 196.924 184.971 113.676 1.00 33.45  ? 185 ARG B C   1 
ATOM   1203 O O   . ARG A 1 192 ? 197.747 184.076 113.880 1.00 40.16  ? 185 ARG B O   1 
ATOM   1204 C CB  . ARG A 1 192 ? 194.631 184.587 114.631 1.00 32.75  ? 185 ARG B CB  1 
ATOM   1205 C CG  . ARG A 1 192 ? 195.305 183.865 115.776 1.00 41.34  ? 185 ARG B CG  1 
ATOM   1206 C CD  . ARG A 1 192 ? 194.408 182.832 116.410 1.00 41.36  ? 185 ARG B CD  1 
ATOM   1207 N NE  . ARG A 1 192 ? 193.279 183.427 117.106 1.00 38.57  ? 185 ARG B NE  1 
ATOM   1208 C CZ  . ARG A 1 192 ? 192.425 182.745 117.854 1.00 43.34  ? 185 ARG B CZ  1 
ATOM   1209 N NH1 . ARG A 1 192 ? 192.562 181.446 118.050 1.00 43.87  ? 185 ARG B NH1 1 
ATOM   1210 N NH2 . ARG A 1 192 ? 191.409 183.384 118.423 1.00 48.77  ? 185 ARG B NH2 1 
ATOM   1211 N N   . THR A 1 193 ? 197.230 186.267 113.698 1.00 29.20  ? 186 THR B N   1 
ATOM   1212 C CA  . THR A 1 193 ? 198.549 186.739 114.081 1.00 31.92  ? 186 THR B CA  1 
ATOM   1213 C C   . THR A 1 193 ? 198.596 187.325 115.481 1.00 42.54  ? 186 THR B C   1 
ATOM   1214 O O   . THR A 1 193 ? 199.588 187.975 115.827 1.00 51.05  ? 186 THR B O   1 
ATOM   1215 C CB  . THR A 1 193 ? 199.065 187.785 113.086 1.00 32.90  ? 186 THR B CB  1 
ATOM   1216 O OG1 . THR A 1 193 ? 197.982 188.620 112.666 1.00 39.30  ? 186 THR B OG1 1 
ATOM   1217 C CG2 . THR A 1 193 ? 199.669 187.100 111.879 1.00 32.35  ? 186 THR B CG2 1 
ATOM   1218 N N   . VAL A 1 194 ? 197.559 187.128 116.285 1.00 43.83  ? 187 VAL B N   1 
ATOM   1219 C CA  . VAL A 1 194 ? 197.578 187.497 117.695 1.00 45.02  ? 187 VAL B CA  1 
ATOM   1220 C C   . VAL A 1 194 ? 197.485 186.214 118.511 1.00 48.07  ? 187 VAL B C   1 
ATOM   1221 O O   . VAL A 1 194 ? 196.848 185.249 118.068 1.00 50.26  ? 187 VAL B O   1 
ATOM   1222 C CB  . VAL A 1 194 ? 196.436 188.464 118.037 1.00 43.24  ? 187 VAL B CB  1 
ATOM   1223 C CG1 . VAL A 1 194 ? 196.714 189.832 117.450 1.00 48.10  ? 187 VAL B CG1 1 
ATOM   1224 C CG2 . VAL A 1 194 ? 195.119 187.921 117.525 1.00 40.71  ? 187 VAL B CG2 1 
ATOM   1225 N N   . PRO A 1 195 ? 198.105 186.141 119.684 1.00 51.00  ? 188 PRO B N   1 
ATOM   1226 C CA  . PRO A 1 195 ? 197.938 184.949 120.520 1.00 52.22  ? 188 PRO B CA  1 
ATOM   1227 C C   . PRO A 1 195 ? 196.507 184.832 121.016 1.00 52.64  ? 188 PRO B C   1 
ATOM   1228 O O   . PRO A 1 195 ? 195.787 185.824 121.144 1.00 54.58  ? 188 PRO B O   1 
ATOM   1229 C CB  . PRO A 1 195 ? 198.921 185.181 121.673 1.00 48.06  ? 188 PRO B CB  1 
ATOM   1230 C CG  . PRO A 1 195 ? 199.148 186.644 121.687 1.00 51.12  ? 188 PRO B CG  1 
ATOM   1231 C CD  . PRO A 1 195 ? 199.056 187.096 120.269 1.00 47.93  ? 188 PRO B CD  1 
ATOM   1232 N N   . SER A 1 196 ? 196.089 183.598 121.278 1.00 48.27  ? 189 SER B N   1 
ATOM   1233 C CA  . SER A 1 196 ? 194.751 183.371 121.792 1.00 48.98  ? 189 SER B CA  1 
ATOM   1234 C C   . SER A 1 196 ? 194.684 183.714 123.279 1.00 59.01  ? 189 SER B C   1 
ATOM   1235 O O   . SER A 1 196 ? 195.698 183.935 123.947 1.00 60.60  ? 189 SER B O   1 
ATOM   1236 C CB  . SER A 1 196 ? 194.325 181.923 121.559 1.00 51.37  ? 189 SER B CB  1 
ATOM   1237 O OG  . SER A 1 196 ? 195.404 181.035 121.779 1.00 56.21  ? 189 SER B OG  1 
ATOM   1238 N N   . ASP A 1 197 ? 193.455 183.769 123.796 1.00 57.39  ? 190 ASP B N   1 
ATOM   1239 C CA  . ASP A 1 197 ? 193.252 184.030 125.215 1.00 53.21  ? 190 ASP B CA  1 
ATOM   1240 C C   . ASP A 1 197 ? 193.766 182.892 126.080 1.00 55.23  ? 190 ASP B C   1 
ATOM   1241 O O   . ASP A 1 197 ? 194.053 183.105 127.264 1.00 58.06  ? 190 ASP B O   1 
ATOM   1242 C CB  . ASP A 1 197 ? 191.770 184.270 125.492 1.00 50.04  ? 190 ASP B CB  1 
ATOM   1243 C CG  . ASP A 1 197 ? 191.317 185.645 125.064 1.00 57.81  ? 190 ASP B CG  1 
ATOM   1244 O OD1 . ASP A 1 197 ? 192.184 186.520 124.868 1.00 58.28  ? 190 ASP B OD1 1 
ATOM   1245 O OD2 . ASP A 1 197 ? 190.094 185.850 124.917 1.00 56.88  ? 190 ASP B OD2 1 
ATOM   1246 N N   . ARG A 1 198 ? 193.894 181.692 125.512 1.00 54.16  ? 191 ARG B N   1 
ATOM   1247 C CA  . ARG A 1 198 ? 194.399 180.561 126.277 1.00 47.15  ? 191 ARG B CA  1 
ATOM   1248 C C   . ARG A 1 198 ? 195.832 180.793 126.730 1.00 46.84  ? 191 ARG B C   1 
ATOM   1249 O O   . ARG A 1 198 ? 196.212 180.372 127.823 1.00 49.26  ? 191 ARG B O   1 
ATOM   1250 C CB  . ARG A 1 198 ? 194.305 179.277 125.458 1.00 53.57  ? 191 ARG B CB  1 
ATOM   1251 C CG  . ARG A 1 198 ? 193.497 178.188 126.131 1.00 59.32  ? 191 ARG B CG  1 
ATOM   1252 C CD  . ARG A 1 198 ? 193.799 176.835 125.529 1.00 64.36  ? 191 ARG B CD  1 
ATOM   1253 N NE  . ARG A 1 198 ? 195.040 176.290 126.064 1.00 71.33  ? 191 ARG B NE  1 
ATOM   1254 C CZ  . ARG A 1 198 ? 195.106 175.383 127.028 1.00 75.91  ? 191 ARG B CZ  1 
ATOM   1255 N NH1 . ARG A 1 198 ? 194.015 174.880 127.580 1.00 75.79  ? 191 ARG B NH1 1 
ATOM   1256 N NH2 . ARG A 1 198 ? 196.298 174.972 127.452 1.00 62.24  ? 191 ARG B NH2 1 
ATOM   1257 N N   . VAL A 1 199 ? 196.646 181.453 125.905 1.00 45.25  ? 192 VAL B N   1 
ATOM   1258 C CA  . VAL A 1 199 ? 198.045 181.671 126.268 1.00 45.68  ? 192 VAL B CA  1 
ATOM   1259 C C   . VAL A 1 199 ? 198.144 182.572 127.493 1.00 45.89  ? 192 VAL B C   1 
ATOM   1260 O O   . VAL A 1 199 ? 198.867 182.275 128.451 1.00 50.17  ? 192 VAL B O   1 
ATOM   1261 C CB  . VAL A 1 199 ? 198.826 182.250 125.077 1.00 54.06  ? 192 VAL B CB  1 
ATOM   1262 C CG1 . VAL A 1 199 ? 200.180 182.756 125.533 1.00 48.41  ? 192 VAL B CG1 1 
ATOM   1263 C CG2 . VAL A 1 199 ? 198.984 181.203 123.991 1.00 47.45  ? 192 VAL B CG2 1 
ATOM   1264 N N   . GLN A 1 200 ? 197.401 183.680 127.492 1.00 46.67  ? 193 GLN B N   1 
ATOM   1265 C CA  . GLN A 1 200 ? 197.459 184.589 128.630 1.00 44.62  ? 193 GLN B CA  1 
ATOM   1266 C C   . GLN A 1 200 ? 196.773 184.002 129.858 1.00 42.97  ? 193 GLN B C   1 
ATOM   1267 O O   . GLN A 1 200 ? 197.198 184.269 130.985 1.00 47.83  ? 193 GLN B O   1 
ATOM   1268 C CB  . GLN A 1 200 ? 196.861 185.948 128.258 1.00 48.48  ? 193 GLN B CB  1 
ATOM   1269 C CG  . GLN A 1 200 ? 195.364 186.086 128.466 1.00 51.36  ? 193 GLN B CG  1 
ATOM   1270 C CD  . GLN A 1 200 ? 194.878 187.497 128.221 1.00 53.91  ? 193 GLN B CD  1 
ATOM   1271 O OE1 . GLN A 1 200 ? 195.416 188.454 128.775 1.00 53.68  ? 193 GLN B OE1 1 
ATOM   1272 N NE2 . GLN A 1 200 ? 193.859 187.636 127.385 1.00 56.34  ? 193 GLN B NE2 1 
ATOM   1273 N N   . LEU A 1 201 ? 195.740 183.176 129.672 1.00 42.23  ? 194 LEU B N   1 
ATOM   1274 C CA  . LEU A 1 201 ? 195.103 182.549 130.825 1.00 39.57  ? 194 LEU B CA  1 
ATOM   1275 C C   . LEU A 1 201 ? 195.989 181.460 131.422 1.00 41.02  ? 194 LEU B C   1 
ATOM   1276 O O   . LEU A 1 201 ? 196.017 181.274 132.643 1.00 42.57  ? 194 LEU B O   1 
ATOM   1277 C CB  . LEU A 1 201 ? 193.736 182.000 130.430 1.00 39.57  ? 194 LEU B CB  1 
ATOM   1278 C CG  . LEU A 1 201 ? 192.646 183.074 130.420 1.00 39.64  ? 194 LEU B CG  1 
ATOM   1279 C CD1 . LEU A 1 201 ? 191.411 182.591 129.695 1.00 47.66  ? 194 LEU B CD1 1 
ATOM   1280 C CD2 . LEU A 1 201 ? 192.303 183.515 131.830 1.00 34.67  ? 194 LEU B CD2 1 
ATOM   1281 N N   . THR A 1 202 ? 196.733 180.742 130.578 1.00 43.23  ? 195 THR B N   1 
ATOM   1282 C CA  . THR A 1 202 ? 197.737 179.805 131.068 1.00 39.27  ? 195 THR B CA  1 
ATOM   1283 C C   . THR A 1 202 ? 198.847 180.534 131.808 1.00 43.58  ? 195 THR B C   1 
ATOM   1284 O O   . THR A 1 202 ? 199.330 180.055 132.838 1.00 48.37  ? 195 THR B O   1 
ATOM   1285 C CB  . THR A 1 202 ? 198.310 178.999 129.903 1.00 39.27  ? 195 THR B CB  1 
ATOM   1286 O OG1 . THR A 1 202 ? 197.271 178.220 129.302 1.00 48.04  ? 195 THR B OG1 1 
ATOM   1287 C CG2 . THR A 1 202 ? 199.410 178.070 130.382 1.00 39.90  ? 195 THR B CG2 1 
ATOM   1288 N N   . ALA A 1 203 ? 199.266 181.693 131.298 1.00 40.11  ? 196 ALA B N   1 
ATOM   1289 C CA  . ALA A 1 203 ? 200.257 182.491 132.010 1.00 38.84  ? 196 ALA B CA  1 
ATOM   1290 C C   . ALA A 1 203 ? 199.729 182.941 133.367 1.00 42.12  ? 196 ALA B C   1 
ATOM   1291 O O   . ALA A 1 203 ? 200.461 182.923 134.363 1.00 39.65  ? 196 ALA B O   1 
ATOM   1292 C CB  . ALA A 1 203 ? 200.667 183.693 131.164 1.00 38.98  ? 196 ALA B CB  1 
ATOM   1293 N N   . ALA A 1 204 ? 198.459 183.348 133.426 1.00 41.49  ? 197 ALA B N   1 
ATOM   1294 C CA  . ALA A 1 204 ? 197.867 183.757 134.697 1.00 39.03  ? 197 ALA B CA  1 
ATOM   1295 C C   . ALA A 1 204 ? 197.792 182.593 135.677 1.00 39.39  ? 197 ALA B C   1 
ATOM   1296 O O   . ALA A 1 204 ? 198.076 182.755 136.870 1.00 44.00  ? 197 ALA B O   1 
ATOM   1297 C CB  . ALA A 1 204 ? 196.479 184.350 134.460 1.00 37.47  ? 197 ALA B CB  1 
ATOM   1298 N N   . ALA A 1 205 ? 197.403 181.411 135.196 1.00 39.38  ? 198 ALA B N   1 
ATOM   1299 C CA  . ALA A 1 205 ? 197.340 180.241 136.065 1.00 36.12  ? 198 ALA B CA  1 
ATOM   1300 C C   . ALA A 1 205 ? 198.726 179.837 136.551 1.00 36.61  ? 198 ALA B C   1 
ATOM   1301 O O   . ALA A 1 205 ? 198.891 179.412 137.699 1.00 44.17  ? 198 ALA B O   1 
ATOM   1302 C CB  . ALA A 1 205 ? 196.664 179.085 135.335 1.00 36.04  ? 198 ALA B CB  1 
ATOM   1303 N N   . GLU A 1 206 ? 199.737 179.964 135.691 1.00 39.03  ? 199 GLU B N   1 
ATOM   1304 C CA  . GLU A 1 206 ? 201.110 179.699 136.104 1.00 37.28  ? 199 GLU B CA  1 
ATOM   1305 C C   . GLU A 1 206 ? 201.579 180.706 137.146 1.00 33.87  ? 199 GLU B C   1 
ATOM   1306 O O   . GLU A 1 206 ? 202.316 180.352 138.071 1.00 35.38  ? 199 GLU B O   1 
ATOM   1307 C CB  . GLU A 1 206 ? 202.030 179.720 134.887 1.00 42.16  ? 199 GLU B CB  1 
ATOM   1308 C CG  . GLU A 1 206 ? 201.894 178.503 134.000 1.00 50.54  ? 199 GLU B CG  1 
ATOM   1309 C CD  . GLU A 1 206 ? 202.822 177.386 134.410 1.00 57.89  ? 199 GLU B CD  1 
ATOM   1310 O OE1 . GLU A 1 206 ? 203.880 177.683 135.003 1.00 55.80  ? 199 GLU B OE1 1 
ATOM   1311 O OE2 . GLU A 1 206 ? 202.489 176.212 134.152 1.00 58.73  ? 199 GLU B OE2 1 
ATOM   1312 N N   . LEU A 1 207 ? 201.180 181.970 136.997 1.00 34.46  ? 200 LEU B N   1 
ATOM   1313 C CA  . LEU A 1 207 ? 201.520 182.981 137.993 1.00 34.08  ? 200 LEU B CA  1 
ATOM   1314 C C   . LEU A 1 207 ? 200.858 182.678 139.330 1.00 33.18  ? 200 LEU B C   1 
ATOM   1315 O O   . LEU A 1 207 ? 201.466 182.861 140.390 1.00 35.69  ? 200 LEU B O   1 
ATOM   1316 C CB  . LEU A 1 207 ? 201.108 184.363 137.489 1.00 34.55  ? 200 LEU B CB  1 
ATOM   1317 C CG  . LEU A 1 207 ? 201.258 185.543 138.448 1.00 29.52  ? 200 LEU B CG  1 
ATOM   1318 C CD1 . LEU A 1 207 ? 202.674 186.071 138.402 1.00 30.68  ? 200 LEU B CD1 1 
ATOM   1319 C CD2 . LEU A 1 207 ? 200.261 186.633 138.118 1.00 32.13  ? 200 LEU B CD2 1 
ATOM   1320 N N   . LEU A 1 208 ? 199.603 182.225 139.298 1.00 31.06  ? 201 LEU B N   1 
ATOM   1321 C CA  . LEU A 1 208 ? 198.926 181.836 140.530 1.00 25.79  ? 201 LEU B CA  1 
ATOM   1322 C C   . LEU A 1 208 ? 199.610 180.644 141.184 1.00 30.40  ? 201 LEU B C   1 
ATOM   1323 O O   . LEU A 1 208 ? 199.812 180.626 142.402 1.00 35.89  ? 201 LEU B O   1 
ATOM   1324 C CB  . LEU A 1 208 ? 197.462 181.510 140.250 1.00 23.48  ? 201 LEU B CB  1 
ATOM   1325 C CG  . LEU A 1 208 ? 196.550 182.645 139.799 1.00 31.50  ? 201 LEU B CG  1 
ATOM   1326 C CD1 . LEU A 1 208 ? 195.104 182.237 139.952 1.00 33.54  ? 201 LEU B CD1 1 
ATOM   1327 C CD2 . LEU A 1 208 ? 196.837 183.902 140.578 1.00 28.09  ? 201 LEU B CD2 1 
ATOM   1328 N N   . GLN A 1 209 ? 199.971 179.636 140.391 1.00 28.88  ? 202 GLN B N   1 
ATOM   1329 C CA  . GLN A 1 209 ? 200.573 178.431 140.950 1.00 30.21  ? 202 GLN B CA  1 
ATOM   1330 C C   . GLN A 1 209 ? 201.972 178.701 141.491 1.00 36.12  ? 202 GLN B C   1 
ATOM   1331 O O   . GLN A 1 209 ? 202.364 178.138 142.520 1.00 44.63  ? 202 GLN B O   1 
ATOM   1332 C CB  . GLN A 1 209 ? 200.598 177.329 139.893 1.00 40.85  ? 202 GLN B CB  1 
ATOM   1333 C CG  . GLN A 1 209 ? 201.391 176.099 140.283 1.00 45.20  ? 202 GLN B CG  1 
ATOM   1334 C CD  . GLN A 1 209 ? 202.039 175.429 139.094 1.00 56.08  ? 202 GLN B CD  1 
ATOM   1335 O OE1 . GLN A 1 209 ? 201.385 174.706 138.343 1.00 56.39  ? 202 GLN B OE1 1 
ATOM   1336 N NE2 . GLN A 1 209 ? 203.331 175.672 138.909 1.00 53.59  ? 202 GLN B NE2 1 
ATOM   1337 N N   . GLU A 1 210 ? 202.742 179.556 140.816 1.00 34.61  ? 203 GLU B N   1 
ATOM   1338 C CA  . GLU A 1 210 ? 204.096 179.848 141.274 1.00 38.14  ? 203 GLU B CA  1 
ATOM   1339 C C   . GLU A 1 210 ? 204.089 180.668 142.557 1.00 40.85  ? 203 GLU B C   1 
ATOM   1340 O O   . GLU A 1 210 ? 204.891 180.418 143.464 1.00 49.90  ? 203 GLU B O   1 
ATOM   1341 C CB  . GLU A 1 210 ? 204.877 180.575 140.180 1.00 39.95  ? 203 GLU B CB  1 
ATOM   1342 C CG  . GLU A 1 210 ? 206.067 181.365 140.695 1.00 46.47  ? 203 GLU B CG  1 
ATOM   1343 C CD  . GLU A 1 210 ? 207.185 181.471 139.679 1.00 64.19  ? 203 GLU B CD  1 
ATOM   1344 O OE1 . GLU A 1 210 ? 207.065 180.865 138.593 1.00 62.66  ? 203 GLU B OE1 1 
ATOM   1345 O OE2 . GLU A 1 210 ? 208.187 182.158 139.967 1.00 60.79  ? 203 GLU B OE2 1 
ATOM   1346 N N   . PHE A 1 211 ? 203.188 181.645 142.658 1.00 33.56  ? 204 PHE B N   1 
ATOM   1347 C CA  . PHE A 1 211 ? 203.157 182.517 143.824 1.00 29.73  ? 204 PHE B CA  1 
ATOM   1348 C C   . PHE A 1 211 ? 202.477 181.876 145.024 1.00 30.27  ? 204 PHE B C   1 
ATOM   1349 O O   . PHE A 1 211 ? 202.480 182.472 146.103 1.00 32.52  ? 204 PHE B O   1 
ATOM   1350 C CB  . PHE A 1 211 ? 202.461 183.832 143.474 1.00 30.60  ? 204 PHE B CB  1 
ATOM   1351 C CG  . PHE A 1 211 ? 203.392 184.886 142.951 1.00 33.62  ? 204 PHE B CG  1 
ATOM   1352 C CD1 . PHE A 1 211 ? 204.753 184.792 143.164 1.00 39.47  ? 204 PHE B CD1 1 
ATOM   1353 C CD2 . PHE A 1 211 ? 202.907 185.968 142.246 1.00 35.32  ? 204 PHE B CD2 1 
ATOM   1354 C CE1 . PHE A 1 211 ? 205.609 185.757 142.683 1.00 41.85  ? 204 PHE B CE1 1 
ATOM   1355 C CE2 . PHE A 1 211 ? 203.760 186.934 141.763 1.00 37.82  ? 204 PHE B CE2 1 
ATOM   1356 C CZ  . PHE A 1 211 ? 205.111 186.827 141.983 1.00 39.95  ? 204 PHE B CZ  1 
ATOM   1357 N N   . GLY A 1 212 ? 201.902 180.690 144.869 1.00 31.74  ? 205 GLY B N   1 
ATOM   1358 C CA  . GLY A 1 212 ? 201.238 180.022 145.964 1.00 29.03  ? 205 GLY B CA  1 
ATOM   1359 C C   . GLY A 1 212 ? 199.792 180.401 146.164 1.00 30.60  ? 205 GLY B C   1 
ATOM   1360 O O   . GLY A 1 212 ? 199.236 180.109 147.227 1.00 39.49  ? 205 GLY B O   1 
ATOM   1361 N N   . TRP A 1 213 ? 199.165 181.043 145.183 1.00 24.59  ? 206 TRP B N   1 
ATOM   1362 C CA  . TRP A 1 213 ? 197.776 181.479 145.298 1.00 26.25  ? 206 TRP B CA  1 
ATOM   1363 C C   . TRP A 1 213 ? 196.872 180.391 144.738 1.00 30.05  ? 206 TRP B C   1 
ATOM   1364 O O   . TRP A 1 213 ? 196.499 180.405 143.566 1.00 37.57  ? 206 TRP B O   1 
ATOM   1365 C CB  . TRP A 1 213 ? 197.572 182.804 144.578 1.00 26.22  ? 206 TRP B CB  1 
ATOM   1366 C CG  . TRP A 1 213 ? 198.455 183.904 145.068 1.00 26.85  ? 206 TRP B CG  1 
ATOM   1367 C CD1 . TRP A 1 213 ? 198.948 184.056 146.327 1.00 28.90  ? 206 TRP B CD1 1 
ATOM   1368 C CD2 . TRP A 1 213 ? 198.921 185.029 144.318 1.00 25.90  ? 206 TRP B CD2 1 
ATOM   1369 N NE1 . TRP A 1 213 ? 199.705 185.194 146.406 1.00 25.91  ? 206 TRP B NE1 1 
ATOM   1370 C CE2 . TRP A 1 213 ? 199.702 185.813 145.185 1.00 26.13  ? 206 TRP B CE2 1 
ATOM   1371 C CE3 . TRP A 1 213 ? 198.755 185.449 142.997 1.00 24.01  ? 206 TRP B CE3 1 
ATOM   1372 C CZ2 . TRP A 1 213 ? 200.315 186.989 144.775 1.00 23.82  ? 206 TRP B CZ2 1 
ATOM   1373 C CZ3 . TRP A 1 213 ? 199.365 186.613 142.592 1.00 23.03  ? 206 TRP B CZ3 1 
ATOM   1374 C CH2 . TRP A 1 213 ? 200.134 187.371 143.477 1.00 22.07  ? 206 TRP B CH2 1 
ATOM   1375 N N   . ASN A 1 214 ? 196.506 179.434 145.589 1.00 28.98  ? 207 ASN B N   1 
ATOM   1376 C CA  . ASN A 1 214 ? 195.631 178.340 145.194 1.00 28.86  ? 207 ASN B CA  1 
ATOM   1377 C C   . ASN A 1 214 ? 194.215 178.495 145.737 1.00 30.37  ? 207 ASN B C   1 
ATOM   1378 O O   . ASN A 1 214 ? 193.428 177.546 145.674 1.00 36.27  ? 207 ASN B O   1 
ATOM   1379 C CB  . ASN A 1 214 ? 196.234 176.999 145.622 1.00 29.96  ? 207 ASN B CB  1 
ATOM   1380 C CG  . ASN A 1 214 ? 196.477 176.912 147.112 1.00 36.89  ? 207 ASN B CG  1 
ATOM   1381 O OD1 . ASN A 1 214 ? 197.587 177.151 147.583 1.00 37.91  ? 207 ASN B OD1 1 
ATOM   1382 N ND2 . ASN A 1 214 ? 195.451 176.541 147.860 1.00 40.71  ? 207 ASN B ND2 1 
ATOM   1383 N N   . TRP A 1 215 ? 193.875 179.673 146.263 1.00 26.18  ? 208 TRP B N   1 
ATOM   1384 C CA  . TRP A 1 215 ? 192.522 179.981 146.740 1.00 26.55  ? 208 TRP B CA  1 
ATOM   1385 C C   . TRP A 1 215 ? 192.183 181.374 146.220 1.00 29.66  ? 208 TRP B C   1 
ATOM   1386 O O   . TRP A 1 215 ? 192.402 182.371 146.908 1.00 42.40  ? 208 TRP B O   1 
ATOM   1387 C CB  . TRP A 1 215 ? 192.446 179.906 148.258 1.00 31.22  ? 208 TRP B CB  1 
ATOM   1388 C CG  . TRP A 1 215 ? 191.115 180.258 148.857 1.00 31.05  ? 208 TRP B CG  1 
ATOM   1389 C CD1 . TRP A 1 215 ? 190.842 181.312 149.675 1.00 28.02  ? 208 TRP B CD1 1 
ATOM   1390 C CD2 . TRP A 1 215 ? 189.887 179.538 148.708 1.00 30.59  ? 208 TRP B CD2 1 
ATOM   1391 N NE1 . TRP A 1 215 ? 189.519 181.301 150.035 1.00 26.42  ? 208 TRP B NE1 1 
ATOM   1392 C CE2 . TRP A 1 215 ? 188.911 180.222 149.452 1.00 28.60  ? 208 TRP B CE2 1 
ATOM   1393 C CE3 . TRP A 1 215 ? 189.517 178.388 148.009 1.00 30.68  ? 208 TRP B CE3 1 
ATOM   1394 C CZ2 . TRP A 1 215 ? 187.591 179.790 149.523 1.00 29.26  ? 208 TRP B CZ2 1 
ATOM   1395 C CZ3 . TRP A 1 215 ? 188.207 177.963 148.079 1.00 34.42  ? 208 TRP B CZ3 1 
ATOM   1396 C CH2 . TRP A 1 215 ? 187.260 178.662 148.829 1.00 28.27  ? 208 TRP B CH2 1 
ATOM   1397 N N   . VAL A 1 216 ? 191.644 181.438 145.008 1.00 30.50  ? 209 VAL B N   1 
ATOM   1398 C CA  . VAL A 1 216 ? 191.416 182.701 144.321 1.00 28.52  ? 209 VAL B CA  1 
ATOM   1399 C C   . VAL A 1 216 ? 189.969 182.767 143.864 1.00 27.75  ? 209 VAL B C   1 
ATOM   1400 O O   . VAL A 1 216 ? 189.252 181.764 143.861 1.00 31.15  ? 209 VAL B O   1 
ATOM   1401 C CB  . VAL A 1 216 ? 192.366 182.885 143.118 1.00 28.47  ? 209 VAL B CB  1 
ATOM   1402 C CG1 . VAL A 1 216 ? 193.792 182.547 143.504 1.00 26.95  ? 209 VAL B CG1 1 
ATOM   1403 C CG2 . VAL A 1 216 ? 191.911 182.029 141.949 1.00 28.07  ? 209 VAL B CG2 1 
ATOM   1404 N N   . ALA A 1 217 ? 189.540 183.964 143.481 1.00 30.46  ? 210 ALA B N   1 
ATOM   1405 C CA  . ALA A 1 217 ? 188.223 184.190 142.904 1.00 29.49  ? 210 ALA B CA  1 
ATOM   1406 C C   . ALA A 1 217 ? 188.394 184.611 141.453 1.00 31.37  ? 210 ALA B C   1 
ATOM   1407 O O   . ALA A 1 217 ? 189.273 185.417 141.139 1.00 30.77  ? 210 ALA B O   1 
ATOM   1408 C CB  . ALA A 1 217 ? 187.452 185.256 143.681 1.00 26.39  ? 210 ALA B CB  1 
ATOM   1409 N N   . ALA A 1 218 ? 187.570 184.057 140.573 1.00 32.61  ? 211 ALA B N   1 
ATOM   1410 C CA  . ALA A 1 218 ? 187.659 184.324 139.147 1.00 32.08  ? 211 ALA B CA  1 
ATOM   1411 C C   . ALA A 1 218 ? 186.407 185.047 138.674 1.00 34.80  ? 211 ALA B C   1 
ATOM   1412 O O   . ALA A 1 218 ? 185.287 184.576 138.889 1.00 41.27  ? 211 ALA B O   1 
ATOM   1413 C CB  . ALA A 1 218 ? 187.852 183.030 138.357 1.00 29.16  ? 211 ALA B CB  1 
ATOM   1414 N N   . LEU A 1 219 ? 186.608 186.192 138.031 1.00 29.82  ? 212 LEU B N   1 
ATOM   1415 C CA  . LEU A 1 219 ? 185.525 187.006 137.507 1.00 37.11  ? 212 LEU B CA  1 
ATOM   1416 C C   . LEU A 1 219 ? 185.746 187.232 136.020 1.00 40.64  ? 212 LEU B C   1 
ATOM   1417 O O   . LEU A 1 219 ? 186.879 187.254 135.536 1.00 43.62  ? 212 LEU B O   1 
ATOM   1418 C CB  . LEU A 1 219 ? 185.431 188.356 138.229 1.00 36.22  ? 212 LEU B CB  1 
ATOM   1419 C CG  . LEU A 1 219 ? 185.252 188.334 139.747 1.00 32.72  ? 212 LEU B CG  1 
ATOM   1420 C CD1 . LEU A 1 219 ? 185.229 189.745 140.295 1.00 35.26  ? 212 LEU B CD1 1 
ATOM   1421 C CD2 . LEU A 1 219 ? 183.989 187.590 140.131 1.00 41.74  ? 212 LEU B CD2 1 
ATOM   1422 N N   . GLY A 1 220 ? 184.647 187.398 135.298 1.00 41.69  ? 213 GLY B N   1 
ATOM   1423 C CA  . GLY A 1 220 ? 184.722 187.678 133.879 1.00 41.99  ? 213 GLY B CA  1 
ATOM   1424 C C   . GLY A 1 220 ? 183.546 188.521 133.450 1.00 52.47  ? 213 GLY B C   1 
ATOM   1425 O O   . GLY A 1 220 ? 182.489 188.512 134.085 1.00 57.26  ? 213 GLY B O   1 
ATOM   1426 N N   . SER A 1 221 ? 183.747 189.259 132.365 1.00 50.66  ? 214 SER B N   1 
ATOM   1427 C CA  . SER A 1 221 ? 182.681 190.095 131.841 1.00 50.34  ? 214 SER B CA  1 
ATOM   1428 C C   . SER A 1 221 ? 181.531 189.232 131.330 1.00 55.46  ? 214 SER B C   1 
ATOM   1429 O O   . SER A 1 221 ? 181.722 188.112 130.851 1.00 60.28  ? 214 SER B O   1 
ATOM   1430 C CB  . SER A 1 221 ? 183.207 191.000 130.730 1.00 51.51  ? 214 SER B CB  1 
ATOM   1431 O OG  . SER A 1 221 ? 183.904 190.250 129.756 1.00 53.67  ? 214 SER B OG  1 
ATOM   1432 N N   . ASP A 1 222 ? 180.314 189.768 131.447 1.00 54.57  ? 215 ASP B N   1 
ATOM   1433 C CA  . ASP A 1 222 ? 179.130 189.008 131.065 1.00 57.76  ? 215 ASP B CA  1 
ATOM   1434 C C   . ASP A 1 222 ? 179.053 188.752 129.565 1.00 62.46  ? 215 ASP B C   1 
ATOM   1435 O O   . ASP A 1 222 ? 178.248 187.921 129.134 1.00 69.01  ? 215 ASP B O   1 
ATOM   1436 C CB  . ASP A 1 222 ? 177.867 189.728 131.534 1.00 64.13  ? 215 ASP B CB  1 
ATOM   1437 C CG  . ASP A 1 222 ? 176.761 188.768 131.923 1.00 67.18  ? 215 ASP B CG  1 
ATOM   1438 O OD1 . ASP A 1 222 ? 176.225 188.081 131.030 1.00 58.42  ? 215 ASP B OD1 1 
ATOM   1439 O OD2 . ASP A 1 222 ? 176.422 188.701 133.122 1.00 74.28  ? 215 ASP B OD2 1 
ATOM   1440 N N   . ASP A 1 223 ? 179.861 189.439 128.763 1.00 56.27  ? 216 ASP B N   1 
ATOM   1441 C CA  . ASP A 1 223 ? 179.889 189.169 127.336 1.00 56.76  ? 216 ASP B CA  1 
ATOM   1442 C C   . ASP A 1 223 ? 180.598 187.843 127.062 1.00 59.79  ? 216 ASP B C   1 
ATOM   1443 O O   . ASP A 1 223 ? 181.074 187.159 127.971 1.00 61.13  ? 216 ASP B O   1 
ATOM   1444 C CB  . ASP A 1 223 ? 180.568 190.314 126.586 1.00 58.65  ? 216 ASP B CB  1 
ATOM   1445 C CG  . ASP A 1 223 ? 181.906 190.694 127.185 1.00 59.07  ? 216 ASP B CG  1 
ATOM   1446 O OD1 . ASP A 1 223 ? 182.796 189.825 127.260 1.00 60.82  ? 216 ASP B OD1 1 
ATOM   1447 O OD2 . ASP A 1 223 ? 182.070 191.866 127.580 1.00 55.80  ? 216 ASP B OD2 1 
ATOM   1448 N N   . GLU A 1 224 ? 180.668 187.484 125.778 1.00 61.94  ? 217 GLU B N   1 
ATOM   1449 C CA  . GLU A 1 224 ? 181.257 186.205 125.393 1.00 68.11  ? 217 GLU B CA  1 
ATOM   1450 C C   . GLU A 1 224 ? 182.729 186.119 125.771 1.00 64.07  ? 217 GLU B C   1 
ATOM   1451 O O   . GLU A 1 224 ? 183.218 185.039 126.119 1.00 65.98  ? 217 GLU B O   1 
ATOM   1452 C CB  . GLU A 1 224 ? 181.081 185.982 123.891 1.00 73.54  ? 217 GLU B CB  1 
ATOM   1453 C CG  . GLU A 1 224 ? 181.138 184.525 123.468 1.00 73.11  ? 217 GLU B CG  1 
ATOM   1454 C CD  . GLU A 1 224 ? 180.117 183.668 124.188 1.00 79.39  ? 217 GLU B CD  1 
ATOM   1455 O OE1 . GLU A 1 224 ? 178.968 184.124 124.362 1.00 84.84  ? 217 GLU B OE1 1 
ATOM   1456 O OE2 . GLU A 1 224 ? 180.465 182.537 124.582 1.00 74.88  ? 217 GLU B OE2 1 
ATOM   1457 N N   . TYR A 1 225 ? 183.448 187.240 125.702 1.00 57.47  ? 218 TYR B N   1 
ATOM   1458 C CA  . TYR A 1 225 ? 184.871 187.248 126.025 1.00 54.21  ? 218 TYR B CA  1 
ATOM   1459 C C   . TYR A 1 225 ? 185.110 186.790 127.460 1.00 59.35  ? 218 TYR B C   1 
ATOM   1460 O O   . TYR A 1 225 ? 185.908 185.878 127.713 1.00 62.80  ? 218 TYR B O   1 
ATOM   1461 C CB  . TYR A 1 225 ? 185.421 188.656 125.783 1.00 53.84  ? 218 TYR B CB  1 
ATOM   1462 C CG  . TYR A 1 225 ? 186.803 188.947 126.317 1.00 55.66  ? 218 TYR B CG  1 
ATOM   1463 C CD1 . TYR A 1 225 ? 187.933 188.554 125.618 1.00 54.32  ? 218 TYR B CD1 1 
ATOM   1464 C CD2 . TYR A 1 225 ? 186.977 189.654 127.498 1.00 49.20  ? 218 TYR B CD2 1 
ATOM   1465 C CE1 . TYR A 1 225 ? 189.194 188.835 126.090 1.00 48.15  ? 218 TYR B CE1 1 
ATOM   1466 C CE2 . TYR A 1 225 ? 188.237 189.937 127.977 1.00 44.46  ? 218 TYR B CE2 1 
ATOM   1467 C CZ  . TYR A 1 225 ? 189.341 189.525 127.269 1.00 46.41  ? 218 TYR B CZ  1 
ATOM   1468 O OH  . TYR A 1 225 ? 190.601 189.804 127.740 1.00 55.02  ? 218 TYR B OH  1 
ATOM   1469 N N   . GLY A 1 226 ? 184.390 187.388 128.409 1.00 54.75  ? 219 GLY B N   1 
ATOM   1470 C CA  . GLY A 1 226 ? 184.561 187.013 129.801 1.00 52.16  ? 219 GLY B CA  1 
ATOM   1471 C C   . GLY A 1 226 ? 184.105 185.598 130.098 1.00 52.21  ? 219 GLY B C   1 
ATOM   1472 O O   . GLY A 1 226 ? 184.730 184.894 130.892 1.00 58.19  ? 219 GLY B O   1 
ATOM   1473 N N   . ARG A 1 227 ? 183.006 185.164 129.477 1.00 52.07  ? 220 ARG B N   1 
ATOM   1474 C CA  . ARG A 1 227 ? 182.514 183.810 129.718 1.00 55.38  ? 220 ARG B CA  1 
ATOM   1475 C C   . ARG A 1 227 ? 183.486 182.759 129.198 1.00 55.11  ? 220 ARG B C   1 
ATOM   1476 O O   . ARG A 1 227 ? 183.746 181.755 129.874 1.00 56.60  ? 220 ARG B O   1 
ATOM   1477 C CB  . ARG A 1 227 ? 181.136 183.629 129.089 1.00 61.23  ? 220 ARG B CB  1 
ATOM   1478 C CG  . ARG A 1 227 ? 180.116 184.641 129.560 1.00 59.08  ? 220 ARG B CG  1 
ATOM   1479 C CD  . ARG A 1 227 ? 178.855 184.593 128.726 1.00 62.06  ? 220 ARG B CD  1 
ATOM   1480 N NE  . ARG A 1 227 ? 177.861 183.707 129.316 1.00 72.03  ? 220 ARG B NE  1 
ATOM   1481 C CZ  . ARG A 1 227 ? 176.593 184.033 129.523 1.00 75.16  ? 220 ARG B CZ  1 
ATOM   1482 N NH1 . ARG A 1 227 ? 176.128 185.232 129.213 1.00 68.47  ? 220 ARG B NH1 1 
ATOM   1483 N NH2 . ARG A 1 227 ? 175.771 183.135 130.058 1.00 68.10  ? 220 ARG B NH2 1 
ATOM   1484 N N   . GLN A 1 228 ? 184.034 182.965 127.998 1.00 55.23  ? 221 GLN B N   1 
ATOM   1485 C CA  . GLN A 1 228 ? 185.025 182.029 127.478 1.00 55.41  ? 221 GLN B CA  1 
ATOM   1486 C C   . GLN A 1 228 ? 186.296 182.046 128.318 1.00 50.22  ? 221 GLN B C   1 
ATOM   1487 O O   . GLN A 1 228 ? 186.900 180.993 128.563 1.00 54.30  ? 221 GLN B O   1 
ATOM   1488 C CB  . GLN A 1 228 ? 185.338 182.342 126.017 1.00 55.66  ? 221 GLN B CB  1 
ATOM   1489 C CG  . GLN A 1 228 ? 184.140 182.234 125.098 1.00 67.46  ? 221 GLN B CG  1 
ATOM   1490 C CD  . GLN A 1 228 ? 183.888 180.813 124.640 1.00 77.43  ? 221 GLN B CD  1 
ATOM   1491 O OE1 . GLN A 1 228 ? 184.784 179.970 124.670 1.00 74.18  ? 221 GLN B OE1 1 
ATOM   1492 N NE2 . GLN A 1 228 ? 182.660 180.537 124.218 1.00 77.51  ? 221 GLN B NE2 1 
ATOM   1493 N N   . GLY A 1 229 ? 186.721 183.229 128.766 1.00 47.69  ? 222 GLY B N   1 
ATOM   1494 C CA  . GLY A 1 229 ? 187.875 183.291 129.646 1.00 46.95  ? 222 GLY B CA  1 
ATOM   1495 C C   . GLY A 1 229 ? 187.655 182.543 130.946 1.00 46.09  ? 222 GLY B C   1 
ATOM   1496 O O   . GLY A 1 229 ? 188.536 181.818 131.414 1.00 48.56  ? 222 GLY B O   1 
ATOM   1497 N N   . LEU A 1 230 ? 186.470 182.701 131.539 1.00 46.40  ? 223 LEU B N   1 
ATOM   1498 C CA  . LEU A 1 230 ? 186.141 181.975 132.759 1.00 46.74  ? 223 LEU B CA  1 
ATOM   1499 C C   . LEU A 1 230 ? 186.136 180.472 132.522 1.00 47.96  ? 223 LEU B C   1 
ATOM   1500 O O   . LEU A 1 230 ? 186.662 179.706 133.338 1.00 50.78  ? 223 LEU B O   1 
ATOM   1501 C CB  . LEU A 1 230 ? 184.782 182.433 133.285 1.00 45.51  ? 223 LEU B CB  1 
ATOM   1502 C CG  . LEU A 1 230 ? 184.764 183.307 134.536 1.00 43.86  ? 223 LEU B CG  1 
ATOM   1503 C CD1 . LEU A 1 230 ? 183.344 183.471 135.030 1.00 48.56  ? 223 LEU B CD1 1 
ATOM   1504 C CD2 . LEU A 1 230 ? 185.627 182.694 135.606 1.00 45.58  ? 223 LEU B CD2 1 
ATOM   1505 N N   . SER A 1 231 ? 185.547 180.032 131.408 1.00 47.50  ? 224 SER B N   1 
ATOM   1506 C CA  . SER A 1 231 ? 185.476 178.604 131.122 1.00 45.84  ? 224 SER B CA  1 
ATOM   1507 C C   . SER A 1 231 ? 186.864 178.007 130.929 1.00 44.84  ? 224 SER B C   1 
ATOM   1508 O O   . SER A 1 231 ? 187.134 176.887 131.378 1.00 45.21  ? 224 SER B O   1 
ATOM   1509 C CB  . SER A 1 231 ? 184.609 178.360 129.890 1.00 54.29  ? 224 SER B CB  1 
ATOM   1510 O OG  . SER A 1 231 ? 184.562 176.983 129.565 1.00 65.03  ? 224 SER B OG  1 
ATOM   1511 N N   . ILE A 1 232 ? 187.757 178.734 130.256 1.00 45.21  ? 225 ILE B N   1 
ATOM   1512 C CA  . ILE A 1 232 ? 189.114 178.235 130.058 1.00 45.58  ? 225 ILE B CA  1 
ATOM   1513 C C   . ILE A 1 232 ? 189.872 178.207 131.381 1.00 45.22  ? 225 ILE B C   1 
ATOM   1514 O O   . ILE A 1 232 ? 190.560 177.225 131.704 1.00 43.63  ? 225 ILE B O   1 
ATOM   1515 C CB  . ILE A 1 232 ? 189.838 179.094 129.009 1.00 47.75  ? 225 ILE B CB  1 
ATOM   1516 C CG1 . ILE A 1 232 ? 189.492 178.609 127.608 1.00 52.81  ? 225 ILE B CG1 1 
ATOM   1517 C CG2 . ILE A 1 232 ? 191.341 179.032 129.205 1.00 47.50  ? 225 ILE B CG2 1 
ATOM   1518 C CD1 . ILE A 1 232 ? 189.361 179.728 126.625 1.00 53.61  ? 225 ILE B CD1 1 
ATOM   1519 N N   . PHE A 1 233 ? 189.754 179.280 132.168 1.00 43.91  ? 226 PHE B N   1 
ATOM   1520 C CA  . PHE A 1 233 ? 190.492 179.360 133.419 1.00 40.09  ? 226 PHE B CA  1 
ATOM   1521 C C   . PHE A 1 233 ? 190.011 178.326 134.424 1.00 41.19  ? 226 PHE B C   1 
ATOM   1522 O O   . PHE A 1 233 ? 190.794 177.890 135.270 1.00 40.56  ? 226 PHE B O   1 
ATOM   1523 C CB  . PHE A 1 233 ? 190.381 180.763 134.008 1.00 35.83  ? 226 PHE B CB  1 
ATOM   1524 C CG  . PHE A 1 233 ? 191.231 180.971 135.222 1.00 37.52  ? 226 PHE B CG  1 
ATOM   1525 C CD1 . PHE A 1 233 ? 192.604 181.064 135.109 1.00 35.19  ? 226 PHE B CD1 1 
ATOM   1526 C CD2 . PHE A 1 233 ? 190.659 181.065 136.476 1.00 33.52  ? 226 PHE B CD2 1 
ATOM   1527 C CE1 . PHE A 1 233 ? 193.387 181.253 136.222 1.00 37.67  ? 226 PHE B CE1 1 
ATOM   1528 C CE2 . PHE A 1 233 ? 191.439 181.252 137.588 1.00 31.93  ? 226 PHE B CE2 1 
ATOM   1529 C CZ  . PHE A 1 233 ? 192.804 181.346 137.462 1.00 35.45  ? 226 PHE B CZ  1 
ATOM   1530 N N   . SER A 1 234 ? 188.742 177.920 134.354 1.00 42.74  ? 227 SER B N   1 
ATOM   1531 C CA  . SER A 1 234 ? 188.263 176.860 135.235 1.00 42.65  ? 227 SER B CA  1 
ATOM   1532 C C   . SER A 1 234 ? 189.066 175.581 135.034 1.00 45.23  ? 227 SER B C   1 
ATOM   1533 O O   . SER A 1 234 ? 189.577 174.993 135.995 1.00 46.92  ? 227 SER B O   1 
ATOM   1534 C CB  . SER A 1 234 ? 186.782 176.598 134.982 1.00 49.32  ? 227 SER B CB  1 
ATOM   1535 O OG  . SER A 1 234 ? 186.027 177.778 135.141 1.00 49.51  ? 227 SER B OG  1 
ATOM   1536 N N   . ALA A 1 235 ? 189.191 175.140 133.781 1.00 43.00  ? 228 ALA B N   1 
ATOM   1537 C CA  . ALA A 1 235 ? 189.953 173.934 133.486 1.00 36.96  ? 228 ALA B CA  1 
ATOM   1538 C C   . ALA A 1 235 ? 191.428 174.117 133.814 1.00 38.37  ? 228 ALA B C   1 
ATOM   1539 O O   . ALA A 1 235 ? 192.065 173.206 134.357 1.00 40.79  ? 228 ALA B O   1 
ATOM   1540 C CB  . ALA A 1 235 ? 189.772 173.547 132.020 1.00 40.67  ? 228 ALA B CB  1 
ATOM   1541 N N   . LEU A 1 236 ? 191.989 175.286 133.492 1.00 38.87  ? 229 LEU B N   1 
ATOM   1542 C CA  . LEU A 1 236 ? 193.400 175.521 133.786 1.00 38.41  ? 229 LEU B CA  1 
ATOM   1543 C C   . LEU A 1 236 ? 193.675 175.444 135.285 1.00 43.85  ? 229 LEU B C   1 
ATOM   1544 O O   . LEU A 1 236 ? 194.648 174.811 135.715 1.00 44.56  ? 229 LEU B O   1 
ATOM   1545 C CB  . LEU A 1 236 ? 193.827 176.876 133.228 1.00 40.90  ? 229 LEU B CB  1 
ATOM   1546 C CG  . LEU A 1 236 ? 194.004 176.944 131.712 1.00 42.95  ? 229 LEU B CG  1 
ATOM   1547 C CD1 . LEU A 1 236 ? 194.354 178.350 131.288 1.00 42.96  ? 229 LEU B CD1 1 
ATOM   1548 C CD2 . LEU A 1 236 ? 195.070 175.969 131.256 1.00 38.34  ? 229 LEU B CD2 1 
ATOM   1549 N N   . ALA A 1 237 ? 192.821 176.074 136.095 1.00 42.56  ? 230 ALA B N   1 
ATOM   1550 C CA  . ALA A 1 237 ? 192.988 176.043 137.542 1.00 37.69  ? 230 ALA B CA  1 
ATOM   1551 C C   . ALA A 1 237 ? 192.802 174.635 138.087 1.00 35.64  ? 230 ALA B C   1 
ATOM   1552 O O   . ALA A 1 237 ? 193.590 174.173 138.918 1.00 39.01  ? 230 ALA B O   1 
ATOM   1553 C CB  . ALA A 1 237 ? 192.002 177.008 138.198 1.00 38.86  ? 230 ALA B CB  1 
ATOM   1554 N N   . ALA A 1 238 ? 191.764 173.933 137.628 1.00 36.72  ? 231 ALA B N   1 
ATOM   1555 C CA  . ALA A 1 238 ? 191.541 172.568 138.089 1.00 37.87  ? 231 ALA B CA  1 
ATOM   1556 C C   . ALA A 1 238 ? 192.720 171.667 137.759 1.00 43.58  ? 231 ALA B C   1 
ATOM   1557 O O   . ALA A 1 238 ? 193.039 170.755 138.529 1.00 47.22  ? 231 ALA B O   1 
ATOM   1558 C CB  . ALA A 1 238 ? 190.258 172.009 137.476 1.00 37.22  ? 231 ALA B CB  1 
ATOM   1559 N N   . ALA A 1 239 ? 193.378 171.901 136.621 1.00 47.70  ? 232 ALA B N   1 
ATOM   1560 C CA  . ALA A 1 239 ? 194.551 171.110 136.277 1.00 41.58  ? 232 ALA B CA  1 
ATOM   1561 C C   . ALA A 1 239 ? 195.776 171.520 137.085 1.00 43.19  ? 232 ALA B C   1 
ATOM   1562 O O   . ALA A 1 239 ? 196.641 170.681 137.358 1.00 45.86  ? 232 ALA B O   1 
ATOM   1563 C CB  . ALA A 1 239 ? 194.842 171.226 134.781 1.00 40.85  ? 232 ALA B CB  1 
ATOM   1564 N N   . ARG A 1 240 ? 195.875 172.790 137.473 1.00 45.06  ? 233 ARG B N   1 
ATOM   1565 C CA  . ARG A 1 240 ? 197.066 173.296 138.144 1.00 42.61  ? 233 ARG B CA  1 
ATOM   1566 C C   . ARG A 1 240 ? 196.965 173.263 139.664 1.00 45.00  ? 233 ARG B C   1 
ATOM   1567 O O   . ARG A 1 240 ? 197.894 173.715 140.340 1.00 40.80  ? 233 ARG B O   1 
ATOM   1568 C CB  . ARG A 1 240 ? 197.364 174.722 137.679 1.00 46.30  ? 233 ARG B CB  1 
ATOM   1569 C CG  . ARG A 1 240 ? 198.485 174.815 136.665 1.00 53.03  ? 233 ARG B CG  1 
ATOM   1570 C CD  . ARG A 1 240 ? 198.260 175.967 135.714 1.00 56.76  ? 233 ARG B CD  1 
ATOM   1571 N NE  . ARG A 1 240 ? 198.981 175.809 134.457 1.00 56.74  ? 233 ARG B NE  1 
ATOM   1572 C CZ  . ARG A 1 240 ? 198.574 175.048 133.453 1.00 56.05  ? 233 ARG B CZ  1 
ATOM   1573 N NH1 . ARG A 1 240 ? 197.449 174.357 133.522 1.00 47.28  ? 233 ARG B NH1 1 
ATOM   1574 N NH2 . ARG A 1 240 ? 199.315 174.976 132.352 1.00 57.15  ? 233 ARG B NH2 1 
ATOM   1575 N N   . GLY A 1 241 ? 195.870 172.744 140.217 1.00 40.37  ? 234 GLY B N   1 
ATOM   1576 C CA  . GLY A 1 241 ? 195.685 172.663 141.648 1.00 34.02  ? 234 GLY B CA  1 
ATOM   1577 C C   . GLY A 1 241 ? 195.077 173.896 142.286 1.00 36.83  ? 234 GLY B C   1 
ATOM   1578 O O   . GLY A 1 241 ? 194.991 173.970 143.513 1.00 47.26  ? 234 GLY B O   1 
ATOM   1579 N N   . ILE A 1 242 ? 194.662 174.870 141.479 1.00 38.32  ? 235 ILE B N   1 
ATOM   1580 C CA  . ILE A 1 242 ? 194.004 176.056 142.006 1.00 30.68  ? 235 ILE B CA  1 
ATOM   1581 C C   . ILE A 1 242 ? 192.503 175.824 142.067 1.00 35.34  ? 235 ILE B C   1 
ATOM   1582 O O   . ILE A 1 242 ? 191.889 175.329 141.114 1.00 39.99  ? 235 ILE B O   1 
ATOM   1583 C CB  . ILE A 1 242 ? 194.340 177.268 141.123 1.00 31.22  ? 235 ILE B CB  1 
ATOM   1584 C CG1 . ILE A 1 242 ? 195.854 177.417 140.972 1.00 30.52  ? 235 ILE B CG1 1 
ATOM   1585 C CG2 . ILE A 1 242 ? 193.721 178.541 141.679 1.00 33.93  ? 235 ILE B CG2 1 
ATOM   1586 C CD1 . ILE A 1 242 ? 196.267 178.164 139.740 1.00 35.86  ? 235 ILE B CD1 1 
ATOM   1587 N N   . CYS A 1 243 ? 191.895 176.169 143.193 1.00 37.19  ? 236 CYS B N   1 
ATOM   1588 C CA  . CYS A 1 243 ? 190.445 176.126 143.294 1.00 43.81  ? 236 CYS B CA  1 
ATOM   1589 C C   . CYS A 1 243 ? 189.870 177.531 143.336 1.00 36.25  ? 236 CYS B C   1 
ATOM   1590 O O   . CYS A 1 243 ? 190.422 178.430 143.969 1.00 33.77  ? 236 CYS B O   1 
ATOM   1591 C CB  . CYS A 1 243 ? 189.965 175.341 144.526 1.00 44.42  ? 236 CYS B CB  1 
ATOM   1592 S SG  . CYS A 1 243 ? 188.236 174.783 144.323 1.00 74.63  ? 236 CYS B SG  1 
ATOM   1593 N N   . ILE A 1 244 ? 188.765 177.704 142.631 1.00 35.12  ? 237 ILE B N   1 
ATOM   1594 C CA  . ILE A 1 244 ? 188.086 178.984 142.549 1.00 34.02  ? 237 ILE B CA  1 
ATOM   1595 C C   . ILE A 1 244 ? 187.057 179.065 143.665 1.00 38.83  ? 237 ILE B C   1 
ATOM   1596 O O   . ILE A 1 244 ? 186.148 178.236 143.741 1.00 49.81  ? 237 ILE B O   1 
ATOM   1597 C CB  . ILE A 1 244 ? 187.426 179.166 141.174 1.00 36.82  ? 237 ILE B CB  1 
ATOM   1598 C CG1 . ILE A 1 244 ? 188.347 178.667 140.061 1.00 37.41  ? 237 ILE B CG1 1 
ATOM   1599 C CG2 . ILE A 1 244 ? 187.109 180.623 140.943 1.00 41.29  ? 237 ILE B CG2 1 
ATOM   1600 C CD1 . ILE A 1 244 ? 189.651 179.394 139.975 1.00 39.75  ? 237 ILE B CD1 1 
ATOM   1601 N N   . ALA A 1 245 ? 187.214 180.052 144.546 1.00 32.22  ? 238 ALA B N   1 
ATOM   1602 C CA  . ALA A 1 245 ? 186.252 180.273 145.616 1.00 31.48  ? 238 ALA B CA  1 
ATOM   1603 C C   . ALA A 1 245 ? 184.899 180.698 145.061 1.00 36.09  ? 238 ALA B C   1 
ATOM   1604 O O   . ALA A 1 245 ? 183.854 180.222 145.515 1.00 40.30  ? 238 ALA B O   1 
ATOM   1605 C CB  . ALA A 1 245 ? 186.788 181.328 146.578 1.00 27.50  ? 238 ALA B CB  1 
ATOM   1606 N N   . HIS A 1 246 ? 184.903 181.601 144.084 1.00 38.04  ? 239 HIS B N   1 
ATOM   1607 C CA  . HIS A 1 246 ? 183.675 182.115 143.496 1.00 40.70  ? 239 HIS B CA  1 
ATOM   1608 C C   . HIS A 1 246 ? 183.926 182.395 142.026 1.00 43.81  ? 239 HIS B C   1 
ATOM   1609 O O   . HIS A 1 246 ? 185.010 182.853 141.658 1.00 40.65  ? 239 HIS B O   1 
ATOM   1610 C CB  . HIS A 1 246 ? 183.200 183.386 144.209 1.00 46.95  ? 239 HIS B CB  1 
ATOM   1611 C CG  . HIS A 1 246 ? 181.947 183.967 143.632 1.00 55.70  ? 239 HIS B CG  1 
ATOM   1612 N ND1 . HIS A 1 246 ? 181.946 185.092 142.837 1.00 55.93  ? 239 HIS B ND1 1 
ATOM   1613 C CD2 . HIS A 1 246 ? 180.657 183.569 143.722 1.00 56.31  ? 239 HIS B CD2 1 
ATOM   1614 C CE1 . HIS A 1 246 ? 180.708 185.367 142.469 1.00 60.71  ? 239 HIS B CE1 1 
ATOM   1615 N NE2 . HIS A 1 246 ? 179.906 184.458 142.993 1.00 60.42  ? 239 HIS B NE2 1 
ATOM   1616 N N   . GLU A 1 247 ? 182.926 182.125 141.196 1.00 50.04  ? 240 GLU B N   1 
ATOM   1617 C CA  . GLU A 1 247 ? 183.030 182.264 139.747 1.00 46.03  ? 240 GLU B CA  1 
ATOM   1618 C C   . GLU A 1 247 ? 181.808 183.045 139.277 1.00 52.92  ? 240 GLU B C   1 
ATOM   1619 O O   . GLU A 1 247 ? 180.730 182.482 139.087 1.00 59.69  ? 240 GLU B O   1 
ATOM   1620 C CB  . GLU A 1 247 ? 183.107 180.902 139.095 1.00 48.27  ? 240 GLU B CB  1 
ATOM   1621 C CG  . GLU A 1 247 ? 184.429 180.594 138.450 1.00 49.32  ? 240 GLU B CG  1 
ATOM   1622 C CD  . GLU A 1 247 ? 184.341 179.418 137.517 1.00 59.87  ? 240 GLU B CD  1 
ATOM   1623 O OE1 . GLU A 1 247 ? 185.279 178.600 137.524 1.00 61.66  ? 240 GLU B OE1 1 
ATOM   1624 O OE2 . GLU A 1 247 ? 183.337 179.309 136.784 1.00 60.95  ? 240 GLU B OE2 1 
ATOM   1625 N N   . GLY A 1 248 ? 181.982 184.353 139.093 1.00 52.27  ? 241 GLY B N   1 
ATOM   1626 C CA  . GLY A 1 248 ? 180.893 185.234 138.747 1.00 51.55  ? 241 GLY B CA  1 
ATOM   1627 C C   . GLY A 1 248 ? 181.141 185.991 137.455 1.00 48.57  ? 241 GLY B C   1 
ATOM   1628 O O   . GLY A 1 248 ? 182.264 186.078 136.954 1.00 48.99  ? 241 GLY B O   1 
ATOM   1629 N N   . LEU A 1 249 ? 180.053 186.540 136.923 1.00 52.23  ? 242 LEU B N   1 
ATOM   1630 C CA  . LEU A 1 249 ? 180.082 187.353 135.718 1.00 52.97  ? 242 LEU B CA  1 
ATOM   1631 C C   . LEU A 1 249 ? 179.699 188.776 136.086 1.00 54.16  ? 242 LEU B C   1 
ATOM   1632 O O   . LEU A 1 249 ? 178.640 189.003 136.678 1.00 56.73  ? 242 LEU B O   1 
ATOM   1633 C CB  . LEU A 1 249 ? 179.128 186.806 134.654 1.00 53.75  ? 242 LEU B CB  1 
ATOM   1634 C CG  . LEU A 1 249 ? 179.551 185.527 133.934 1.00 54.63  ? 242 LEU B CG  1 
ATOM   1635 C CD1 . LEU A 1 249 ? 178.544 185.175 132.859 1.00 55.59  ? 242 LEU B CD1 1 
ATOM   1636 C CD2 . LEU A 1 249 ? 180.935 185.677 133.340 1.00 54.35  ? 242 LEU B CD2 1 
ATOM   1637 N N   . VAL A 1 250 ? 180.558 189.727 135.743 1.00 55.51  ? 243 VAL B N   1 
ATOM   1638 C CA  . VAL A 1 250 ? 180.347 191.136 136.057 1.00 61.50  ? 243 VAL B CA  1 
ATOM   1639 C C   . VAL A 1 250 ? 179.588 191.774 134.894 1.00 64.95  ? 243 VAL B C   1 
ATOM   1640 O O   . VAL A 1 250 ? 180.051 191.687 133.748 1.00 67.56  ? 243 VAL B O   1 
ATOM   1641 C CB  . VAL A 1 250 ? 181.673 191.860 136.332 1.00 56.68  ? 243 VAL B CB  1 
ATOM   1642 C CG1 . VAL A 1 250 ? 182.238 191.387 137.649 1.00 55.68  ? 243 VAL B CG1 1 
ATOM   1643 C CG2 . VAL A 1 250 ? 182.679 191.595 135.233 1.00 56.67  ? 243 VAL B CG2 1 
ATOM   1644 N N   . PRO A 1 251 ? 178.428 192.378 135.132 1.00 67.98  ? 244 PRO B N   1 
ATOM   1645 C CA  . PRO A 1 251 ? 177.654 192.950 134.026 1.00 71.10  ? 244 PRO B CA  1 
ATOM   1646 C C   . PRO A 1 251 ? 178.325 194.177 133.432 1.00 74.43  ? 244 PRO B C   1 
ATOM   1647 O O   . PRO A 1 251 ? 179.058 194.906 134.104 1.00 72.36  ? 244 PRO B O   1 
ATOM   1648 C CB  . PRO A 1 251 ? 176.320 193.315 134.683 1.00 72.88  ? 244 PRO B CB  1 
ATOM   1649 C CG  . PRO A 1 251 ? 176.668 193.550 136.111 1.00 76.11  ? 244 PRO B CG  1 
ATOM   1650 C CD  . PRO A 1 251 ? 177.775 192.589 136.434 1.00 68.30  ? 244 PRO B CD  1 
ATOM   1651 N N   . LEU A 1 252 ? 178.064 194.396 132.145 1.00 71.30  ? 245 LEU B N   1 
ATOM   1652 C CA  . LEU A 1 252 ? 178.523 195.601 131.475 1.00 72.30  ? 245 LEU B CA  1 
ATOM   1653 C C   . LEU A 1 252 ? 177.594 196.770 131.800 1.00 77.92  ? 245 LEU B C   1 
ATOM   1654 O O   . LEU A 1 252 ? 176.388 196.581 131.981 1.00 77.54  ? 245 LEU B O   1 
ATOM   1655 C CB  . LEU A 1 252 ? 178.579 195.390 129.965 1.00 67.40  ? 245 LEU B CB  1 
ATOM   1656 C CG  . LEU A 1 252 ? 179.237 194.110 129.445 1.00 68.33  ? 245 LEU B CG  1 
ATOM   1657 C CD1 . LEU A 1 252 ? 178.219 192.994 129.272 1.00 69.60  ? 245 LEU B CD1 1 
ATOM   1658 C CD2 . LEU A 1 252 ? 179.960 194.377 128.141 1.00 59.85  ? 245 LEU B CD2 1 
ATOM   1659 N N   . PRO A 1 253 ? 178.132 197.995 131.879 1.00 82.50  ? 246 PRO B N   1 
ATOM   1660 C CA  . PRO A 1 253 ? 177.313 199.169 132.202 1.00 87.70  ? 246 PRO B CA  1 
ATOM   1661 C C   . PRO A 1 253 ? 176.303 199.509 131.109 1.00 90.73  ? 246 PRO B C   1 
ATOM   1662 O O   . PRO A 1 253 ? 176.502 199.116 129.960 1.00 87.53  ? 246 PRO B O   1 
ATOM   1663 C CB  . PRO A 1 253 ? 178.349 200.286 132.352 1.00 84.13  ? 246 PRO B CB  1 
ATOM   1664 C CG  . PRO A 1 253 ? 179.503 199.840 131.533 1.00 83.47  ? 246 PRO B CG  1 
ATOM   1665 C CD  . PRO A 1 253 ? 179.546 198.349 131.679 1.00 74.71  ? 246 PRO B CD  1 
ATOM   1666 N N   . LYS A 1 262 ? 173.612 191.886 141.312 1.00 90.05  ? 255 LYS B N   1 
ATOM   1667 C CA  . LYS A 1 262 ? 174.387 192.492 140.237 1.00 91.24  ? 255 LYS B CA  1 
ATOM   1668 C C   . LYS A 1 262 ? 175.864 192.619 140.614 1.00 91.79  ? 255 LYS B C   1 
ATOM   1669 O O   . LYS A 1 262 ? 176.453 191.684 141.160 1.00 92.07  ? 255 LYS B O   1 
ATOM   1670 C CB  . LYS A 1 262 ? 173.801 193.859 139.868 1.00 90.29  ? 255 LYS B CB  1 
ATOM   1671 C CG  . LYS A 1 262 ? 173.633 194.823 141.036 1.00 88.91  ? 255 LYS B CG  1 
ATOM   1672 C CD  . LYS A 1 262 ? 173.212 196.197 140.540 1.00 92.25  ? 255 LYS B CD  1 
ATOM   1673 C CE  . LYS A 1 262 ? 173.165 197.208 141.670 1.00 92.85  ? 255 LYS B CE  1 
ATOM   1674 N NZ  . LYS A 1 262 ? 172.791 198.562 141.179 1.00 87.83  ? 255 LYS B NZ  1 
ATOM   1675 N N   . VAL A 1 263 ? 176.461 193.771 140.301 1.00 88.42  ? 256 VAL B N   1 
ATOM   1676 C CA  . VAL A 1 263 ? 177.854 194.017 140.662 1.00 81.40  ? 256 VAL B CA  1 
ATOM   1677 C C   . VAL A 1 263 ? 178.022 193.989 142.177 1.00 81.87  ? 256 VAL B C   1 
ATOM   1678 O O   . VAL A 1 263 ? 179.027 193.488 142.699 1.00 81.33  ? 256 VAL B O   1 
ATOM   1679 C CB  . VAL A 1 263 ? 178.329 195.349 140.051 1.00 82.07  ? 256 VAL B CB  1 
ATOM   1680 C CG1 . VAL A 1 263 ? 177.301 196.445 140.294 1.00 83.51  ? 256 VAL B CG1 1 
ATOM   1681 C CG2 . VAL A 1 263 ? 179.692 195.747 140.591 1.00 72.75  ? 256 VAL B CG2 1 
ATOM   1682 N N   . GLN A 1 264 ? 177.035 194.514 142.909 1.00 83.76  ? 257 GLN B N   1 
ATOM   1683 C CA  . GLN A 1 264 ? 177.075 194.446 144.365 1.00 77.96  ? 257 GLN B CA  1 
ATOM   1684 C C   . GLN A 1 264 ? 177.095 193.001 144.840 1.00 77.38  ? 257 GLN B C   1 
ATOM   1685 O O   . GLN A 1 264 ? 177.863 192.642 145.737 1.00 78.92  ? 257 GLN B O   1 
ATOM   1686 C CB  . GLN A 1 264 ? 175.879 195.187 144.961 1.00 82.23  ? 257 GLN B CB  1 
ATOM   1687 C CG  . GLN A 1 264 ? 175.575 196.521 144.312 1.00 87.82  ? 257 GLN B CG  1 
ATOM   1688 C CD  . GLN A 1 264 ? 174.976 197.514 145.286 1.00 91.47  ? 257 GLN B CD  1 
ATOM   1689 O OE1 . GLN A 1 264 ? 175.381 197.586 146.445 1.00 92.53  ? 257 GLN B OE1 1 
ATOM   1690 N NE2 . GLN A 1 264 ? 174.001 198.285 144.819 1.00 85.43  ? 257 GLN B NE2 1 
ATOM   1691 N N   . ASP A 1 265 ? 176.259 192.153 144.238 1.00 80.59  ? 258 ASP B N   1 
ATOM   1692 C CA  . ASP A 1 265 ? 176.242 190.742 144.610 1.00 82.41  ? 258 ASP B CA  1 
ATOM   1693 C C   . ASP A 1 265 ? 177.565 190.065 144.278 1.00 80.47  ? 258 ASP B C   1 
ATOM   1694 O O   . ASP A 1 265 ? 178.053 189.234 145.052 1.00 78.56  ? 258 ASP B O   1 
ATOM   1695 C CB  . ASP A 1 265 ? 175.084 190.029 143.913 1.00 85.42  ? 258 ASP B CB  1 
ATOM   1696 C CG  . ASP A 1 265 ? 174.278 189.160 144.859 1.00 94.36  ? 258 ASP B CG  1 
ATOM   1697 O OD1 . ASP A 1 265 ? 174.577 189.158 146.072 1.00 95.46  ? 258 ASP B OD1 1 
ATOM   1698 O OD2 . ASP A 1 265 ? 173.346 188.474 144.390 1.00 96.30  ? 258 ASP B OD2 1 
ATOM   1699 N N   . VAL A 1 266 ? 178.158 190.401 143.130 1.00 79.52  ? 259 VAL B N   1 
ATOM   1700 C CA  . VAL A 1 266 ? 179.420 189.780 142.736 1.00 78.02  ? 259 VAL B CA  1 
ATOM   1701 C C   . VAL A 1 266 ? 180.529 190.150 143.714 1.00 71.03  ? 259 VAL B C   1 
ATOM   1702 O O   . VAL A 1 266 ? 181.280 189.282 144.182 1.00 69.17  ? 259 VAL B O   1 
ATOM   1703 C CB  . VAL A 1 266 ? 179.777 190.171 141.290 1.00 73.98  ? 259 VAL B CB  1 
ATOM   1704 C CG1 . VAL A 1 266 ? 181.254 189.957 141.025 1.00 65.70  ? 259 VAL B CG1 1 
ATOM   1705 C CG2 . VAL A 1 266 ? 178.945 189.366 140.310 1.00 67.10  ? 259 VAL B CG2 1 
ATOM   1706 N N   . LEU A 1 267 ? 180.590 191.420 144.072 1.00 70.92  ? 260 LEU B N   1 
ATOM   1707 C CA  . LEU A 1 267 ? 181.640 191.871 145.010 1.00 70.68  ? 260 LEU B CA  1 
ATOM   1708 C C   . LEU A 1 267 ? 181.351 191.329 146.412 1.00 67.27  ? 260 LEU B C   1 
ATOM   1709 O O   . LEU A 1 267 ? 182.317 191.112 147.149 1.00 67.24  ? 260 LEU B O   1 
ATOM   1710 C CB  . LEU A 1 267 ? 181.694 193.392 144.972 1.00 72.51  ? 260 LEU B CB  1 
ATOM   1711 C CG  . LEU A 1 267 ? 182.753 194.001 144.051 1.00 74.87  ? 260 LEU B CG  1 
ATOM   1712 C CD1 . LEU A 1 267 ? 183.565 194.978 144.870 1.00 65.18  ? 260 LEU B CD1 1 
ATOM   1713 C CD2 . LEU A 1 267 ? 183.647 192.919 143.479 1.00 77.37  ? 260 LEU B CD2 1 
ATOM   1714 N N   . HIS A 1 268 ? 180.080 191.134 146.765 1.00 71.32  ? 261 HIS B N   1 
ATOM   1715 C CA  . HIS A 1 268 ? 179.741 190.553 148.059 1.00 69.64  ? 261 HIS B CA  1 
ATOM   1716 C C   . HIS A 1 268 ? 180.164 189.093 148.133 1.00 69.48  ? 261 HIS B C   1 
ATOM   1717 O O   . HIS A 1 268 ? 180.678 188.641 149.161 1.00 68.22  ? 261 HIS B O   1 
ATOM   1718 C CB  . HIS A 1 268 ? 178.244 190.701 148.324 1.00 72.10  ? 261 HIS B CB  1 
ATOM   1719 C CG  . HIS A 1 268 ? 177.790 190.070 149.603 1.00 74.88  ? 261 HIS B CG  1 
ATOM   1720 N ND1 . HIS A 1 268 ? 177.497 188.728 149.710 1.00 76.89  ? 261 HIS B ND1 1 
ATOM   1721 C CD2 . HIS A 1 268 ? 177.595 190.597 150.835 1.00 69.51  ? 261 HIS B CD2 1 
ATOM   1722 C CE1 . HIS A 1 268 ? 177.133 188.457 150.950 1.00 71.39  ? 261 HIS B CE1 1 
ATOM   1723 N NE2 . HIS A 1 268 ? 177.184 189.574 151.653 1.00 64.69  ? 261 HIS B NE2 1 
ATOM   1724 N N   . GLN A 1 269 ? 179.953 188.337 147.053 1.00 70.03  ? 262 GLN B N   1 
ATOM   1725 C CA  . GLN A 1 269 ? 180.402 186.949 147.031 1.00 61.47  ? 262 GLN B CA  1 
ATOM   1726 C C   . GLN A 1 269 ? 181.921 186.858 147.038 1.00 60.76  ? 262 GLN B C   1 
ATOM   1727 O O   . GLN A 1 269 ? 182.492 185.946 147.648 1.00 65.10  ? 262 GLN B O   1 
ATOM   1728 C CB  . GLN A 1 269 ? 179.826 186.221 145.818 1.00 59.46  ? 262 GLN B CB  1 
ATOM   1729 C CG  . GLN A 1 269 ? 178.314 186.234 145.747 1.00 67.92  ? 262 GLN B CG  1 
ATOM   1730 C CD  . GLN A 1 269 ? 177.686 185.118 146.552 1.00 74.49  ? 262 GLN B CD  1 
ATOM   1731 O OE1 . GLN A 1 269 ? 178.374 184.380 147.256 1.00 74.35  ? 262 GLN B OE1 1 
ATOM   1732 N NE2 . GLN A 1 269 ? 176.370 184.991 146.456 1.00 76.63  ? 262 GLN B NE2 1 
ATOM   1733 N N   . VAL A 1 270 ? 182.596 187.785 146.356 1.00 61.37  ? 263 VAL B N   1 
ATOM   1734 C CA  . VAL A 1 270 ? 184.056 187.808 146.389 1.00 57.36  ? 263 VAL B CA  1 
ATOM   1735 C C   . VAL A 1 270 ? 184.552 188.073 147.806 1.00 58.49  ? 263 VAL B C   1 
ATOM   1736 O O   . VAL A 1 270 ? 185.510 187.447 148.274 1.00 54.18  ? 263 VAL B O   1 
ATOM   1737 C CB  . VAL A 1 270 ? 184.595 188.850 145.390 1.00 55.33  ? 263 VAL B CB  1 
ATOM   1738 C CG1 . VAL A 1 270 ? 185.998 189.297 145.775 1.00 45.76  ? 263 VAL B CG1 1 
ATOM   1739 C CG2 . VAL A 1 270 ? 184.580 188.287 143.983 1.00 53.64  ? 263 VAL B CG2 1 
ATOM   1740 N N   . ASN A 1 271 ? 183.901 188.998 148.512 1.00 62.80  ? 264 ASN B N   1 
ATOM   1741 C CA  . ASN A 1 271 ? 184.297 189.322 149.878 1.00 63.18  ? 264 ASN B CA  1 
ATOM   1742 C C   . ASN A 1 271 ? 183.922 188.214 150.855 1.00 62.55  ? 264 ASN B C   1 
ATOM   1743 O O   . ASN A 1 271 ? 184.567 188.069 151.900 1.00 59.44  ? 264 ASN B O   1 
ATOM   1744 C CB  . ASN A 1 271 ? 183.650 190.639 150.301 1.00 67.14  ? 264 ASN B CB  1 
ATOM   1745 C CG  . ASN A 1 271 ? 184.269 191.221 151.552 1.00 77.61  ? 264 ASN B CG  1 
ATOM   1746 O OD1 . ASN A 1 271 ? 185.478 191.126 151.764 1.00 79.24  ? 264 ASN B OD1 1 
ATOM   1747 N ND2 . ASN A 1 271 ? 183.439 191.829 152.391 1.00 86.54  ? 264 ASN B ND2 1 
ATOM   1748 N N   . GLN A 1 272 ? 182.888 187.432 150.536 1.00 61.81  ? 265 GLN B N   1 
ATOM   1749 C CA  . GLN A 1 272 ? 182.445 186.369 151.432 1.00 63.86  ? 265 GLN B CA  1 
ATOM   1750 C C   . GLN A 1 272 ? 183.542 185.336 151.647 1.00 60.90  ? 265 GLN B C   1 
ATOM   1751 O O   . GLN A 1 272 ? 183.751 184.865 152.771 1.00 62.14  ? 265 GLN B O   1 
ATOM   1752 C CB  . GLN A 1 272 ? 181.185 185.707 150.873 1.00 67.13  ? 265 GLN B CB  1 
ATOM   1753 C CG  . GLN A 1 272 ? 179.900 186.148 151.547 1.00 67.62  ? 265 GLN B CG  1 
ATOM   1754 C CD  . GLN A 1 272 ? 180.059 186.316 153.043 1.00 81.07  ? 265 GLN B CD  1 
ATOM   1755 O OE1 . GLN A 1 272 ? 180.121 185.336 153.785 1.00 81.14  ? 265 GLN B OE1 1 
ATOM   1756 N NE2 . GLN A 1 272 ? 180.127 187.563 153.496 1.00 80.76  ? 265 GLN B NE2 1 
ATOM   1757 N N   . SER A 1 273 ? 184.244 184.965 150.584 1.00 57.97  ? 266 SER B N   1 
ATOM   1758 C CA  . SER A 1 273 ? 185.422 184.124 150.712 1.00 50.11  ? 266 SER B CA  1 
ATOM   1759 C C   . SER A 1 273 ? 186.616 184.957 151.163 1.00 53.35  ? 266 SER B C   1 
ATOM   1760 O O   . SER A 1 273 ? 186.695 186.160 150.904 1.00 57.92  ? 266 SER B O   1 
ATOM   1761 C CB  . SER A 1 273 ? 185.730 183.433 149.387 1.00 42.52  ? 266 SER B CB  1 
ATOM   1762 O OG  . SER A 1 273 ? 185.575 184.330 148.303 1.00 48.44  ? 266 SER B OG  1 
ATOM   1763 N N   . SER A 1 274 ? 187.549 184.304 151.856 1.00 53.53  ? 267 SER B N   1 
ATOM   1764 C CA  . SER A 1 274 ? 188.750 184.968 152.366 1.00 52.42  ? 267 SER B CA  1 
ATOM   1765 C C   . SER A 1 274 ? 189.806 185.021 151.262 1.00 50.40  ? 267 SER B C   1 
ATOM   1766 O O   . SER A 1 274 ? 190.955 184.604 151.418 1.00 56.40  ? 267 SER B O   1 
ATOM   1767 C CB  . SER A 1 274 ? 189.268 184.250 153.604 1.00 58.37  ? 267 SER B CB  1 
ATOM   1768 O OG  . SER A 1 274 ? 189.558 182.891 153.322 1.00 49.99  ? 267 SER B OG  1 
ATOM   1769 N N   . VAL A 1 275 ? 189.390 185.568 150.124 1.00 42.03  ? 268 VAL B N   1 
ATOM   1770 C CA  . VAL A 1 275 ? 190.181 185.574 148.901 1.00 35.93  ? 268 VAL B CA  1 
ATOM   1771 C C   . VAL A 1 275 ? 190.938 186.890 148.819 1.00 41.33  ? 268 VAL B C   1 
ATOM   1772 O O   . VAL A 1 275 ? 190.343 187.967 148.946 1.00 49.08  ? 268 VAL B O   1 
ATOM   1773 C CB  . VAL A 1 275 ? 189.291 185.357 147.665 1.00 31.51  ? 268 VAL B CB  1 
ATOM   1774 C CG1 . VAL A 1 275 ? 190.092 185.485 146.394 1.00 32.61  ? 268 VAL B CG1 1 
ATOM   1775 C CG2 . VAL A 1 275 ? 188.653 183.991 147.731 1.00 31.39  ? 268 VAL B CG2 1 
ATOM   1776 N N   . GLN A 1 276 ? 192.250 186.799 148.623 1.00 37.29  ? 269 GLN B N   1 
ATOM   1777 C CA  . GLN A 1 276 ? 193.120 187.958 148.494 1.00 35.84  ? 269 GLN B CA  1 
ATOM   1778 C C   . GLN A 1 276 ? 193.523 188.234 147.054 1.00 31.76  ? 269 GLN B C   1 
ATOM   1779 O O   . GLN A 1 276 ? 194.038 189.315 146.767 1.00 31.34  ? 269 GLN B O   1 
ATOM   1780 C CB  . GLN A 1 276 ? 194.375 187.765 149.348 1.00 34.85  ? 269 GLN B CB  1 
ATOM   1781 C CG  . GLN A 1 276 ? 194.947 189.044 149.916 1.00 45.71  ? 269 GLN B CG  1 
ATOM   1782 C CD  . GLN A 1 276 ? 194.409 189.354 151.297 1.00 58.07  ? 269 GLN B CD  1 
ATOM   1783 O OE1 . GLN A 1 276 ? 193.258 189.048 151.610 1.00 59.03  ? 269 GLN B OE1 1 
ATOM   1784 N NE2 . GLN A 1 276 ? 195.240 189.969 152.131 1.00 54.92  ? 269 GLN B NE2 1 
ATOM   1785 N N   . VAL A 1 277 ? 193.315 187.280 146.150 1.00 29.84  ? 270 VAL B N   1 
ATOM   1786 C CA  . VAL A 1 277 ? 193.689 187.406 144.747 1.00 25.09  ? 270 VAL B CA  1 
ATOM   1787 C C   . VAL A 1 277 ? 192.459 187.141 143.896 1.00 25.38  ? 270 VAL B C   1 
ATOM   1788 O O   . VAL A 1 277 ? 191.828 186.086 144.018 1.00 27.64  ? 270 VAL B O   1 
ATOM   1789 C CB  . VAL A 1 277 ? 194.825 186.438 144.371 1.00 23.85  ? 270 VAL B CB  1 
ATOM   1790 C CG1 . VAL A 1 277 ? 195.264 186.675 142.943 1.00 23.91  ? 270 VAL B CG1 1 
ATOM   1791 C CG2 . VAL A 1 277 ? 195.991 186.605 145.319 1.00 24.48  ? 270 VAL B CG2 1 
ATOM   1792 N N   . VAL A 1 278 ? 192.129 188.093 143.029 1.00 28.10  ? 271 VAL B N   1 
ATOM   1793 C CA  . VAL A 1 278 ? 190.988 187.993 142.130 1.00 25.54  ? 271 VAL B CA  1 
ATOM   1794 C C   . VAL A 1 278 ? 191.509 188.108 140.707 1.00 30.84  ? 271 VAL B C   1 
ATOM   1795 O O   . VAL A 1 278 ? 192.263 189.035 140.395 1.00 35.60  ? 271 VAL B O   1 
ATOM   1796 C CB  . VAL A 1 278 ? 189.936 189.080 142.407 1.00 24.04  ? 271 VAL B CB  1 
ATOM   1797 C CG1 . VAL A 1 278 ? 188.738 188.903 141.493 1.00 27.01  ? 271 VAL B CG1 1 
ATOM   1798 C CG2 . VAL A 1 278 ? 189.512 189.052 143.858 1.00 25.32  ? 271 VAL B CG2 1 
ATOM   1799 N N   . LEU A 1 279 ? 191.119 187.170 139.852 1.00 29.60  ? 272 LEU B N   1 
ATOM   1800 C CA  . LEU A 1 279 ? 191.419 187.231 138.427 1.00 30.49  ? 272 LEU B CA  1 
ATOM   1801 C C   . LEU A 1 279 ? 190.233 187.883 137.730 1.00 29.91  ? 272 LEU B C   1 
ATOM   1802 O O   . LEU A 1 279 ? 189.122 187.350 137.756 1.00 34.93  ? 272 LEU B O   1 
ATOM   1803 C CB  . LEU A 1 279 ? 191.695 185.841 137.859 1.00 30.60  ? 272 LEU B CB  1 
ATOM   1804 C CG  . LEU A 1 279 ? 192.207 185.805 136.418 1.00 31.74  ? 272 LEU B CG  1 
ATOM   1805 C CD1 . LEU A 1 279 ? 193.155 184.647 136.229 1.00 38.09  ? 272 LEU B CD1 1 
ATOM   1806 C CD2 . LEU A 1 279 ? 191.055 185.711 135.435 1.00 27.38  ? 272 LEU B CD2 1 
ATOM   1807 N N   . LEU A 1 280 ? 190.466 189.041 137.117 1.00 26.82  ? 273 LEU B N   1 
ATOM   1808 C CA  . LEU A 1 280 ? 189.412 189.776 136.424 1.00 31.44  ? 273 LEU B CA  1 
ATOM   1809 C C   . LEU A 1 280 ? 189.687 189.706 134.925 1.00 34.97  ? 273 LEU B C   1 
ATOM   1810 O O   . LEU A 1 280 ? 190.434 190.502 134.358 1.00 39.99  ? 273 LEU B O   1 
ATOM   1811 C CB  . LEU A 1 280 ? 189.340 191.214 136.926 1.00 35.29  ? 273 LEU B CB  1 
ATOM   1812 C CG  . LEU A 1 280 ? 188.177 192.060 136.408 1.00 33.26  ? 273 LEU B CG  1 
ATOM   1813 C CD1 . LEU A 1 280 ? 186.862 191.327 136.584 1.00 35.23  ? 273 LEU B CD1 1 
ATOM   1814 C CD2 . LEU A 1 280 ? 188.142 193.400 137.105 1.00 36.75  ? 273 LEU B CD2 1 
ATOM   1815 N N   . PHE A 1 281 ? 189.064 188.723 134.278 1.00 33.67  ? 274 PHE B N   1 
ATOM   1816 C CA  . PHE A 1 281 ? 189.156 188.567 132.828 1.00 36.93  ? 274 PHE B CA  1 
ATOM   1817 C C   . PHE A 1 281 ? 187.927 189.216 132.201 1.00 41.98  ? 274 PHE B C   1 
ATOM   1818 O O   . PHE A 1 281 ? 186.994 188.557 131.741 1.00 49.82  ? 274 PHE B O   1 
ATOM   1819 C CB  . PHE A 1 281 ? 189.281 187.097 132.452 1.00 37.55  ? 274 PHE B CB  1 
ATOM   1820 C CG  . PHE A 1 281 ? 189.783 186.872 131.059 1.00 44.20  ? 274 PHE B CG  1 
ATOM   1821 C CD1 . PHE A 1 281 ? 191.135 186.897 130.784 1.00 45.29  ? 274 PHE B CD1 1 
ATOM   1822 C CD2 . PHE A 1 281 ? 188.899 186.634 130.022 1.00 46.51  ? 274 PHE B CD2 1 
ATOM   1823 C CE1 . PHE A 1 281 ? 191.596 186.693 129.502 1.00 50.51  ? 274 PHE B CE1 1 
ATOM   1824 C CE2 . PHE A 1 281 ? 189.357 186.426 128.740 1.00 45.51  ? 274 PHE B CE2 1 
ATOM   1825 C CZ  . PHE A 1 281 ? 190.705 186.455 128.480 1.00 47.16  ? 274 PHE B CZ  1 
ATOM   1826 N N   . ALA A 1 282 ? 187.941 190.545 132.179 1.00 40.90  ? 275 ALA B N   1 
ATOM   1827 C CA  . ALA A 1 282 ? 186.807 191.331 131.724 1.00 43.04  ? 275 ALA B CA  1 
ATOM   1828 C C   . ALA A 1 282 ? 187.273 192.384 130.732 1.00 49.55  ? 275 ALA B C   1 
ATOM   1829 O O   . ALA A 1 282 ? 188.466 192.670 130.607 1.00 52.49  ? 275 ALA B O   1 
ATOM   1830 C CB  . ALA A 1 282 ? 186.083 192.003 132.897 1.00 43.60  ? 275 ALA B CB  1 
ATOM   1831 N N   . SER A 1 283 ? 186.307 192.961 130.023 1.00 51.79  ? 276 SER B N   1 
ATOM   1832 C CA  . SER A 1 283 ? 186.589 194.027 129.078 1.00 53.72  ? 276 SER B CA  1 
ATOM   1833 C C   . SER A 1 283 ? 186.823 195.339 129.825 1.00 55.60  ? 276 SER B C   1 
ATOM   1834 O O   . SER A 1 283 ? 186.763 195.409 131.055 1.00 56.41  ? 276 SER B O   1 
ATOM   1835 C CB  . SER A 1 283 ? 185.448 194.159 128.076 1.00 56.39  ? 276 SER B CB  1 
ATOM   1836 O OG  . SER A 1 283 ? 184.935 192.887 127.729 1.00 57.51  ? 276 SER B OG  1 
ATOM   1837 N N   . VAL A 1 284 ? 187.097 196.397 129.062 1.00 54.08  ? 277 VAL B N   1 
ATOM   1838 C CA  . VAL A 1 284 ? 187.453 197.678 129.664 1.00 52.40  ? 277 VAL B CA  1 
ATOM   1839 C C   . VAL A 1 284 ? 186.275 198.261 130.435 1.00 52.60  ? 277 VAL B C   1 
ATOM   1840 O O   . VAL A 1 284 ? 186.434 198.766 131.551 1.00 53.39  ? 277 VAL B O   1 
ATOM   1841 C CB  . VAL A 1 284 ? 187.956 198.652 128.585 1.00 55.51  ? 277 VAL B CB  1 
ATOM   1842 C CG1 . VAL A 1 284 ? 188.722 199.786 129.226 1.00 57.45  ? 277 VAL B CG1 1 
ATOM   1843 C CG2 . VAL A 1 284 ? 188.823 197.920 127.581 1.00 54.20  ? 277 VAL B CG2 1 
ATOM   1844 N N   . HIS A 1 285 ? 185.076 198.200 129.857 1.00 55.75  ? 278 HIS B N   1 
ATOM   1845 C CA  . HIS A 1 285 ? 183.928 198.858 130.474 1.00 55.67  ? 278 HIS B CA  1 
ATOM   1846 C C   . HIS A 1 285 ? 183.427 198.092 131.693 1.00 59.56  ? 278 HIS B C   1 
ATOM   1847 O O   . HIS A 1 285 ? 183.088 198.695 132.716 1.00 58.79  ? 278 HIS B O   1 
ATOM   1848 C CB  . HIS A 1 285 ? 182.816 199.036 129.442 1.00 63.33  ? 278 HIS B CB  1 
ATOM   1849 C CG  . HIS A 1 285 ? 183.208 199.900 128.285 1.00 67.31  ? 278 HIS B CG  1 
ATOM   1850 N ND1 . HIS A 1 285 ? 183.889 201.087 128.443 1.00 62.22  ? 278 HIS B ND1 1 
ATOM   1851 C CD2 . HIS A 1 285 ? 183.027 199.744 126.953 1.00 67.07  ? 278 HIS B CD2 1 
ATOM   1852 C CE1 . HIS A 1 285 ? 184.105 201.629 127.258 1.00 62.54  ? 278 HIS B CE1 1 
ATOM   1853 N NE2 . HIS A 1 285 ? 183.591 200.834 126.337 1.00 68.46  ? 278 HIS B NE2 1 
ATOM   1854 N N   . ALA A 1 286 ? 183.368 196.761 131.603 1.00 60.68  ? 279 ALA B N   1 
ATOM   1855 C CA  . ALA A 1 286 ? 182.951 195.964 132.754 1.00 49.73  ? 279 ALA B CA  1 
ATOM   1856 C C   . ALA A 1 286 ? 183.941 196.096 133.905 1.00 47.92  ? 279 ALA B C   1 
ATOM   1857 O O   . ALA A 1 286 ? 183.542 196.237 135.070 1.00 52.41  ? 279 ALA B O   1 
ATOM   1858 C CB  . ALA A 1 286 ? 182.790 194.502 132.347 1.00 51.84  ? 279 ALA B CB  1 
ATOM   1859 N N   . ALA A 1 287 ? 185.239 196.054 133.596 1.00 47.42  ? 280 ALA B N   1 
ATOM   1860 C CA  . ALA A 1 287 ? 186.252 196.243 134.627 1.00 48.17  ? 280 ALA B CA  1 
ATOM   1861 C C   . ALA A 1 287 ? 186.166 197.636 135.231 1.00 52.10  ? 280 ALA B C   1 
ATOM   1862 O O   . ALA A 1 287 ? 186.307 197.801 136.447 1.00 53.72  ? 280 ALA B O   1 
ATOM   1863 C CB  . ALA A 1 287 ? 187.645 195.993 134.053 1.00 45.03  ? 280 ALA B CB  1 
ATOM   1864 N N   . HIS A 1 288 ? 185.934 198.653 134.398 1.00 52.83  ? 281 HIS B N   1 
ATOM   1865 C CA  . HIS A 1 288 ? 185.799 200.012 134.908 1.00 49.82  ? 281 HIS B CA  1 
ATOM   1866 C C   . HIS A 1 288 ? 184.591 200.141 135.826 1.00 53.60  ? 281 HIS B C   1 
ATOM   1867 O O   . HIS A 1 288 ? 184.663 200.805 136.864 1.00 60.12  ? 281 HIS B O   1 
ATOM   1868 C CB  . HIS A 1 288 ? 185.696 201.002 133.750 1.00 57.26  ? 281 HIS B CB  1 
ATOM   1869 C CG  . HIS A 1 288 ? 185.136 202.333 134.145 1.00 68.90  ? 281 HIS B CG  1 
ATOM   1870 N ND1 . HIS A 1 288 ? 185.767 203.169 135.040 1.00 76.25  ? 281 HIS B ND1 1 
ATOM   1871 C CD2 . HIS A 1 288 ? 184.000 202.968 133.775 1.00 67.47  ? 281 HIS B CD2 1 
ATOM   1872 C CE1 . HIS A 1 288 ? 185.045 204.264 135.201 1.00 73.43  ? 281 HIS B CE1 1 
ATOM   1873 N NE2 . HIS A 1 288 ? 183.967 204.166 134.445 1.00 68.87  ? 281 HIS B NE2 1 
ATOM   1874 N N   . ALA A 1 289 ? 183.469 199.521 135.457 1.00 50.55  ? 282 ALA B N   1 
ATOM   1875 C CA  . ALA A 1 289 ? 182.287 199.563 136.311 1.00 49.65  ? 282 ALA B CA  1 
ATOM   1876 C C   . ALA A 1 289 ? 182.549 198.886 137.649 1.00 59.06  ? 282 ALA B C   1 
ATOM   1877 O O   . ALA A 1 289 ? 182.220 199.437 138.711 1.00 68.68  ? 282 ALA B O   1 
ATOM   1878 C CB  . ALA A 1 289 ? 181.105 198.905 135.602 1.00 46.88  ? 282 ALA B CB  1 
ATOM   1879 N N   . LEU A 1 290 ? 183.157 197.696 137.620 1.00 52.52  ? 283 LEU B N   1 
ATOM   1880 C CA  . LEU A 1 290 ? 183.466 197.000 138.864 1.00 51.77  ? 283 LEU B CA  1 
ATOM   1881 C C   . LEU A 1 290 ? 184.408 197.818 139.735 1.00 52.69  ? 283 LEU B C   1 
ATOM   1882 O O   . LEU A 1 290 ? 184.213 197.917 140.952 1.00 59.01  ? 283 LEU B O   1 
ATOM   1883 C CB  . LEU A 1 290 ? 184.074 195.629 138.566 1.00 55.76  ? 283 LEU B CB  1 
ATOM   1884 C CG  . LEU A 1 290 ? 184.640 194.868 139.768 1.00 52.93  ? 283 LEU B CG  1 
ATOM   1885 C CD1 . LEU A 1 290 ? 184.179 193.432 139.756 1.00 53.45  ? 283 LEU B CD1 1 
ATOM   1886 C CD2 . LEU A 1 290 ? 186.154 194.925 139.784 1.00 43.87  ? 283 LEU B CD2 1 
ATOM   1887 N N   . PHE A 1 291 ? 185.436 198.412 139.128 1.00 47.73  ? 284 PHE B N   1 
ATOM   1888 C CA  . PHE A 1 291 ? 186.424 199.150 139.904 1.00 47.37  ? 284 PHE B CA  1 
ATOM   1889 C C   . PHE A 1 291 ? 185.843 200.441 140.457 1.00 59.05  ? 284 PHE B C   1 
ATOM   1890 O O   . PHE A 1 291 ? 186.152 200.825 141.587 1.00 64.60  ? 284 PHE B O   1 
ATOM   1891 C CB  . PHE A 1 291 ? 187.653 199.421 139.046 1.00 44.73  ? 284 PHE B CB  1 
ATOM   1892 C CG  . PHE A 1 291 ? 188.527 198.219 138.858 1.00 50.31  ? 284 PHE B CG  1 
ATOM   1893 C CD1 . PHE A 1 291 ? 188.730 197.327 139.893 1.00 44.39  ? 284 PHE B CD1 1 
ATOM   1894 C CD2 . PHE A 1 291 ? 189.121 197.962 137.639 1.00 51.38  ? 284 PHE B CD2 1 
ATOM   1895 C CE1 . PHE A 1 291 ? 189.528 196.220 139.724 1.00 36.71  ? 284 PHE B CE1 1 
ATOM   1896 C CE2 . PHE A 1 291 ? 189.919 196.854 137.465 1.00 48.10  ? 284 PHE B CE2 1 
ATOM   1897 C CZ  . PHE A 1 291 ? 190.121 195.983 138.510 1.00 39.95  ? 284 PHE B CZ  1 
ATOM   1898 N N   . ASN A 1 292 ? 184.986 201.119 139.691 1.00 60.37  ? 285 ASN B N   1 
ATOM   1899 C CA  . ASN A 1 292 ? 184.304 202.291 140.224 1.00 64.21  ? 285 ASN B CA  1 
ATOM   1900 C C   . ASN A 1 292 ? 183.435 201.918 141.415 1.00 70.76  ? 285 ASN B C   1 
ATOM   1901 O O   . ASN A 1 292 ? 183.441 202.607 142.443 1.00 74.79  ? 285 ASN B O   1 
ATOM   1902 C CB  . ASN A 1 292 ? 183.455 202.960 139.144 1.00 64.90  ? 285 ASN B CB  1 
ATOM   1903 C CG  . ASN A 1 292 ? 182.599 204.073 139.707 1.00 77.82  ? 285 ASN B CG  1 
ATOM   1904 O OD1 . ASN A 1 292 ? 183.097 205.149 140.036 1.00 78.14  ? 285 ASN B OD1 1 
ATOM   1905 N ND2 . ASN A 1 292 ? 181.304 203.813 139.840 1.00 83.59  ? 285 ASN B ND2 1 
ATOM   1906 N N   . TYR A 1 293 ? 182.677 200.823 141.300 1.00 67.01  ? 286 TYR B N   1 
ATOM   1907 C CA  . TYR A 1 293 ? 181.828 200.420 142.416 1.00 63.41  ? 286 TYR B CA  1 
ATOM   1908 C C   . TYR A 1 293 ? 182.659 200.074 143.644 1.00 66.73  ? 286 TYR B C   1 
ATOM   1909 O O   . TYR A 1 293 ? 182.329 200.488 144.760 1.00 72.60  ? 286 TYR B O   1 
ATOM   1910 C CB  . TYR A 1 293 ? 180.948 199.235 142.028 1.00 63.32  ? 286 TYR B CB  1 
ATOM   1911 C CG  . TYR A 1 293 ? 180.254 198.616 143.219 1.00 72.21  ? 286 TYR B CG  1 
ATOM   1912 C CD1 . TYR A 1 293 ? 179.237 199.291 143.878 1.00 72.99  ? 286 TYR B CD1 1 
ATOM   1913 C CD2 . TYR A 1 293 ? 180.629 197.370 143.698 1.00 71.93  ? 286 TYR B CD2 1 
ATOM   1914 C CE1 . TYR A 1 293 ? 178.605 198.738 144.971 1.00 73.92  ? 286 TYR B CE1 1 
ATOM   1915 C CE2 . TYR A 1 293 ? 180.003 196.809 144.791 1.00 77.80  ? 286 TYR B CE2 1 
ATOM   1916 C CZ  . TYR A 1 293 ? 178.991 197.497 145.424 1.00 82.66  ? 286 TYR B CZ  1 
ATOM   1917 O OH  . TYR A 1 293 ? 178.362 196.942 146.515 1.00 90.98  ? 286 TYR B OH  1 
ATOM   1918 N N   . SER A 1 294 ? 183.746 199.322 143.461 1.00 65.48  ? 287 SER B N   1 
ATOM   1919 C CA  . SER A 1 294 ? 184.546 198.910 144.610 1.00 63.53  ? 287 SER B CA  1 
ATOM   1920 C C   . SER A 1 294 ? 185.335 200.073 145.200 1.00 63.21  ? 287 SER B C   1 
ATOM   1921 O O   . SER A 1 294 ? 185.680 200.045 146.386 1.00 66.34  ? 287 SER B O   1 
ATOM   1922 C CB  . SER A 1 294 ? 185.477 197.763 144.220 1.00 54.20  ? 287 SER B CB  1 
ATOM   1923 O OG  . SER A 1 294 ? 186.128 198.030 142.998 1.00 53.20  ? 287 SER B OG  1 
ATOM   1924 N N   . ILE A 1 295 ? 185.638 201.096 144.398 1.00 61.53  ? 288 ILE B N   1 
ATOM   1925 C CA  . ILE A 1 295 ? 186.242 202.311 144.937 1.00 67.76  ? 288 ILE B CA  1 
ATOM   1926 C C   . ILE A 1 295 ? 185.223 203.082 145.764 1.00 73.08  ? 288 ILE B C   1 
ATOM   1927 O O   . ILE A 1 295 ? 185.530 203.573 146.858 1.00 75.02  ? 288 ILE B O   1 
ATOM   1928 C CB  . ILE A 1 295 ? 186.813 203.170 143.794 1.00 66.90  ? 288 ILE B CB  1 
ATOM   1929 C CG1 . ILE A 1 295 ? 188.113 202.561 143.268 1.00 62.88  ? 288 ILE B CG1 1 
ATOM   1930 C CG2 . ILE A 1 295 ? 187.041 204.597 144.261 1.00 61.95  ? 288 ILE B CG2 1 
ATOM   1931 C CD1 . ILE A 1 295 ? 188.828 203.427 142.271 1.00 65.13  ? 288 ILE B CD1 1 
ATOM   1932 N N   . SER A 1 296 ? 183.991 203.193 145.258 1.00 71.03  ? 289 SER B N   1 
ATOM   1933 C CA  . SER A 1 296 ? 182.942 203.880 146.002 1.00 67.58  ? 289 SER B CA  1 
ATOM   1934 C C   . SER A 1 296 ? 182.560 203.126 147.270 1.00 72.26  ? 289 SER B C   1 
ATOM   1935 O O   . SER A 1 296 ? 182.139 203.743 148.254 1.00 72.91  ? 289 SER B O   1 
ATOM   1936 C CB  . SER A 1 296 ? 181.713 204.074 145.113 1.00 71.83  ? 289 SER B CB  1 
ATOM   1937 O OG  . SER A 1 296 ? 182.008 204.885 143.991 1.00 75.31  ? 289 SER B OG  1 
ATOM   1938 N N   . SER A 1 297 ? 182.705 201.804 147.272 1.00 70.06  ? 290 SER B N   1 
ATOM   1939 C CA  . SER A 1 297 ? 182.320 200.973 148.405 1.00 70.19  ? 290 SER B CA  1 
ATOM   1940 C C   . SER A 1 297 ? 183.458 200.769 149.400 1.00 73.53  ? 290 SER B C   1 
ATOM   1941 O O   . SER A 1 297 ? 183.251 200.128 150.436 1.00 75.03  ? 290 SER B O   1 
ATOM   1942 C CB  . SER A 1 297 ? 181.797 199.620 147.890 1.00 71.11  ? 290 SER B CB  1 
ATOM   1943 O OG  . SER A 1 297 ? 181.988 198.558 148.807 1.00 74.91  ? 290 SER B OG  1 
ATOM   1944 N N   . ARG A 1 298 ? 184.635 201.337 149.132 1.00 71.85  ? 291 ARG B N   1 
ATOM   1945 C CA  . ARG A 1 298 ? 185.804 201.210 150.002 1.00 75.53  ? 291 ARG B CA  1 
ATOM   1946 C C   . ARG A 1 298 ? 186.159 199.737 150.219 1.00 72.58  ? 291 ARG B C   1 
ATOM   1947 O O   . ARG A 1 298 ? 186.470 199.296 151.327 1.00 71.73  ? 291 ARG B O   1 
ATOM   1948 C CB  . ARG A 1 298 ? 185.574 201.932 151.336 1.00 83.85  ? 291 ARG B CB  1 
ATOM   1949 C CG  . ARG A 1 298 ? 186.046 203.381 151.357 1.00 83.42  ? 291 ARG B CG  1 
ATOM   1950 C CD  . ARG A 1 298 ? 186.574 203.799 152.725 1.00 93.90  ? 291 ARG B CD  1 
ATOM   1951 N NE  . ARG A 1 298 ? 187.688 202.970 153.172 1.00 102.07 ? 291 ARG B NE  1 
ATOM   1952 C CZ  . ARG A 1 298 ? 187.613 202.064 154.137 1.00 102.01 ? 291 ARG B CZ  1 
ATOM   1953 N NH1 . ARG A 1 298 ? 186.483 201.835 154.786 1.00 100.43 ? 291 ARG B NH1 1 
ATOM   1954 N NH2 . ARG A 1 298 ? 188.700 201.368 154.459 1.00 99.40  ? 291 ARG B NH2 1 
ATOM   1955 N N   . LEU A 1 299 ? 186.088 198.974 149.131 1.00 62.79  ? 292 LEU B N   1 
ATOM   1956 C CA  . LEU A 1 299 ? 186.428 197.559 149.173 1.00 54.40  ? 292 LEU B CA  1 
ATOM   1957 C C   . LEU A 1 299 ? 187.931 197.387 149.389 1.00 55.64  ? 292 LEU B C   1 
ATOM   1958 O O   . LEU A 1 299 ? 188.749 198.145 148.861 1.00 60.30  ? 292 LEU B O   1 
ATOM   1959 C CB  . LEU A 1 299 ? 185.959 196.875 147.884 1.00 63.52  ? 292 LEU B CB  1 
ATOM   1960 C CG  . LEU A 1 299 ? 186.065 195.367 147.586 1.00 68.90  ? 292 LEU B CG  1 
ATOM   1961 C CD1 . LEU A 1 299 ? 187.453 194.913 147.167 1.00 56.21  ? 292 LEU B CD1 1 
ATOM   1962 C CD2 . LEU A 1 299 ? 185.577 194.541 148.773 1.00 69.06  ? 292 LEU B CD2 1 
ATOM   1963 N N   . SER A 1 300 ? 188.286 196.383 150.190 1.00 53.26  ? 293 SER B N   1 
ATOM   1964 C CA  . SER A 1 300 ? 189.656 196.232 150.659 1.00 53.08  ? 293 SER B CA  1 
ATOM   1965 C C   . SER A 1 300 ? 190.606 195.922 149.502 1.00 53.06  ? 293 SER B C   1 
ATOM   1966 O O   . SER A 1 300 ? 190.204 195.329 148.499 1.00 52.41  ? 293 SER B O   1 
ATOM   1967 C CB  . SER A 1 300 ? 189.741 195.124 151.706 1.00 53.02  ? 293 SER B CB  1 
ATOM   1968 O OG  . SER A 1 300 ? 189.186 193.914 151.223 1.00 55.87  ? 293 SER B OG  1 
ATOM   1969 N N   . PRO A 1 301 ? 191.873 196.325 149.611 1.00 50.00  ? 294 PRO B N   1 
ATOM   1970 C CA  . PRO A 1 301 ? 192.825 196.054 148.529 1.00 45.84  ? 294 PRO B CA  1 
ATOM   1971 C C   . PRO A 1 301 ? 193.000 194.563 148.284 1.00 47.96  ? 294 PRO B C   1 
ATOM   1972 O O   . PRO A 1 301 ? 192.998 193.750 149.210 1.00 50.34  ? 294 PRO B O   1 
ATOM   1973 C CB  . PRO A 1 301 ? 194.123 196.695 149.032 1.00 44.78  ? 294 PRO B CB  1 
ATOM   1974 C CG  . PRO A 1 301 ? 193.960 196.790 150.501 1.00 43.79  ? 294 PRO B CG  1 
ATOM   1975 C CD  . PRO A 1 301 ? 192.507 197.047 150.727 1.00 45.21  ? 294 PRO B CD  1 
ATOM   1976 N N   . LYS A 1 302 ? 193.157 194.213 147.011 1.00 45.02  ? 295 LYS B N   1 
ATOM   1977 C CA  . LYS A 1 302 ? 193.352 192.834 146.592 1.00 33.27  ? 295 LYS B CA  1 
ATOM   1978 C C   . LYS A 1 302 ? 194.361 192.797 145.457 1.00 27.21  ? 295 LYS B C   1 
ATOM   1979 O O   . LYS A 1 302 ? 194.663 193.817 144.838 1.00 36.50  ? 295 LYS B O   1 
ATOM   1980 C CB  . LYS A 1 302 ? 192.035 192.186 146.149 1.00 30.51  ? 295 LYS B CB  1 
ATOM   1981 C CG  . LYS A 1 302 ? 191.066 191.929 147.281 1.00 39.06  ? 295 LYS B CG  1 
ATOM   1982 C CD  . LYS A 1 302 ? 189.877 191.126 146.814 1.00 42.66  ? 295 LYS B CD  1 
ATOM   1983 C CE  . LYS A 1 302 ? 188.910 190.868 147.955 1.00 50.97  ? 295 LYS B CE  1 
ATOM   1984 N NZ  . LYS A 1 302 ? 189.553 191.043 149.283 1.00 47.63  ? 295 LYS B NZ  1 
ATOM   1985 N N   . VAL A 1 303 ? 194.896 191.608 145.197 1.00 28.35  ? 296 VAL B N   1 
ATOM   1986 C CA  . VAL A 1 303 ? 195.744 191.380 144.034 1.00 27.47  ? 296 VAL B CA  1 
ATOM   1987 C C   . VAL A 1 303 ? 194.808 191.104 142.863 1.00 27.30  ? 296 VAL B C   1 
ATOM   1988 O O   . VAL A 1 303 ? 194.038 190.146 142.879 1.00 27.96  ? 296 VAL B O   1 
ATOM   1989 C CB  . VAL A 1 303 ? 196.730 190.233 144.255 1.00 23.68  ? 296 VAL B CB  1 
ATOM   1990 C CG1 . VAL A 1 303 ? 197.514 189.967 142.988 1.00 21.00  ? 296 VAL B CG1 1 
ATOM   1991 C CG2 . VAL A 1 303 ? 197.668 190.558 145.391 1.00 23.80  ? 296 VAL B CG2 1 
ATOM   1992 N N   . TRP A 1 304 ? 194.863 191.959 141.851 1.00 29.13  ? 297 TRP B N   1 
ATOM   1993 C CA  . TRP A 1 304 ? 194.027 191.812 140.669 1.00 26.81  ? 297 TRP B CA  1 
ATOM   1994 C C   . TRP A 1 304 ? 194.877 191.290 139.521 1.00 31.78  ? 297 TRP B C   1 
ATOM   1995 O O   . TRP A 1 304 ? 195.892 191.897 139.172 1.00 41.14  ? 297 TRP B O   1 
ATOM   1996 C CB  . TRP A 1 304 ? 193.377 193.143 140.296 1.00 26.33  ? 297 TRP B CB  1 
ATOM   1997 C CG  . TRP A 1 304 ? 192.484 193.686 141.359 1.00 27.49  ? 297 TRP B CG  1 
ATOM   1998 C CD1 . TRP A 1 304 ? 192.826 194.549 142.356 1.00 26.28  ? 297 TRP B CD1 1 
ATOM   1999 C CD2 . TRP A 1 304 ? 191.091 193.405 141.531 1.00 27.49  ? 297 TRP B CD2 1 
ATOM   2000 N NE1 . TRP A 1 304 ? 191.736 194.818 143.142 1.00 26.58  ? 297 TRP B NE1 1 
ATOM   2001 C CE2 . TRP A 1 304 ? 190.657 194.129 142.656 1.00 27.35  ? 297 TRP B CE2 1 
ATOM   2002 C CE3 . TRP A 1 304 ? 190.170 192.612 140.843 1.00 25.67  ? 297 TRP B CE3 1 
ATOM   2003 C CZ2 . TRP A 1 304 ? 189.343 194.084 143.108 1.00 25.45  ? 297 TRP B CZ2 1 
ATOM   2004 C CZ3 . TRP A 1 304 ? 188.867 192.569 141.293 1.00 26.74  ? 297 TRP B CZ3 1 
ATOM   2005 C CH2 . TRP A 1 304 ? 188.466 193.300 142.415 1.00 28.27  ? 297 TRP B CH2 1 
ATOM   2006 N N   . VAL A 1 305 ? 194.472 190.166 138.946 1.00 30.05  ? 298 VAL B N   1 
ATOM   2007 C CA  . VAL A 1 305 ? 195.112 189.648 137.745 1.00 30.68  ? 298 VAL B CA  1 
ATOM   2008 C C   . VAL A 1 305 ? 194.343 190.186 136.549 1.00 33.62  ? 298 VAL B C   1 
ATOM   2009 O O   . VAL A 1 305 ? 193.130 189.985 136.437 1.00 36.44  ? 298 VAL B O   1 
ATOM   2010 C CB  . VAL A 1 305 ? 195.164 188.116 137.744 1.00 30.88  ? 298 VAL B CB  1 
ATOM   2011 C CG1 . VAL A 1 305 ? 195.730 187.615 136.431 1.00 26.74  ? 298 VAL B CG1 1 
ATOM   2012 C CG2 . VAL A 1 305 ? 196.009 187.627 138.904 1.00 28.58  ? 298 VAL B CG2 1 
ATOM   2013 N N   . ALA A 1 306 ? 195.048 190.878 135.664 1.00 34.21  ? 299 ALA B N   1 
ATOM   2014 C CA  . ALA A 1 306 ? 194.444 191.680 134.616 1.00 34.95  ? 299 ALA B CA  1 
ATOM   2015 C C   . ALA A 1 306 ? 194.545 190.982 133.272 1.00 39.42  ? 299 ALA B C   1 
ATOM   2016 O O   . ALA A 1 306 ? 195.612 190.493 132.891 1.00 48.01  ? 299 ALA B O   1 
ATOM   2017 C CB  . ALA A 1 306 ? 195.118 193.050 134.530 1.00 38.99  ? 299 ALA B CB  1 
ATOM   2018 N N   . SER A 1 307 ? 193.430 190.944 132.554 1.00 39.05  ? 300 SER B N   1 
ATOM   2019 C CA  . SER A 1 307 ? 193.473 190.580 131.152 1.00 45.66  ? 300 SER B CA  1 
ATOM   2020 C C   . SER A 1 307 ? 194.090 191.721 130.347 1.00 52.50  ? 300 SER B C   1 
ATOM   2021 O O   . SER A 1 307 ? 194.265 192.840 130.835 1.00 53.25  ? 300 SER B O   1 
ATOM   2022 C CB  . SER A 1 307 ? 192.074 190.249 130.641 1.00 45.89  ? 300 SER B CB  1 
ATOM   2023 O OG  . SER A 1 307 ? 191.364 191.423 130.304 1.00 50.93  ? 300 SER B OG  1 
ATOM   2024 N N   . GLU A 1 308 ? 194.430 191.427 129.093 1.00 52.08  ? 301 GLU B N   1 
ATOM   2025 C CA  . GLU A 1 308 ? 195.022 192.447 128.240 1.00 53.26  ? 301 GLU B CA  1 
ATOM   2026 C C   . GLU A 1 308 ? 194.042 193.555 127.881 1.00 54.62  ? 301 GLU B C   1 
ATOM   2027 O O   . GLU A 1 308 ? 194.466 194.580 127.338 1.00 59.10  ? 301 GLU B O   1 
ATOM   2028 C CB  . GLU A 1 308 ? 195.572 191.810 126.966 1.00 54.45  ? 301 GLU B CB  1 
ATOM   2029 C CG  . GLU A 1 308 ? 197.070 191.583 126.992 1.00 57.02  ? 301 GLU B CG  1 
ATOM   2030 C CD  . GLU A 1 308 ? 197.640 191.324 125.617 1.00 63.88  ? 301 GLU B CD  1 
ATOM   2031 O OE1 . GLU A 1 308 ? 197.488 190.194 125.110 1.00 61.21  ? 301 GLU B OE1 1 
ATOM   2032 O OE2 . GLU A 1 308 ? 198.241 192.255 125.041 1.00 66.41  ? 301 GLU B OE2 1 
ATOM   2033 N N   . ALA A 1 309 ? 192.751 193.373 128.166 1.00 55.03  ? 302 ALA B N   1 
ATOM   2034 C CA  . ALA A 1 309 ? 191.758 194.381 127.813 1.00 49.31  ? 302 ALA B CA  1 
ATOM   2035 C C   . ALA A 1 309 ? 191.908 195.636 128.665 1.00 55.25  ? 302 ALA B C   1 
ATOM   2036 O O   . ALA A 1 309 ? 191.911 196.755 128.139 1.00 62.20  ? 302 ALA B O   1 
ATOM   2037 C CB  . ALA A 1 309 ? 190.353 193.799 127.953 1.00 46.63  ? 302 ALA B CB  1 
ATOM   2038 N N   . TRP A 1 310 ? 192.038 195.477 129.981 1.00 52.16  ? 303 TRP B N   1 
ATOM   2039 C CA  . TRP A 1 310 ? 192.091 196.620 130.881 1.00 50.30  ? 303 TRP B CA  1 
ATOM   2040 C C   . TRP A 1 310 ? 193.426 196.796 131.586 1.00 50.52  ? 303 TRP B C   1 
ATOM   2041 O O   . TRP A 1 310 ? 193.547 197.694 132.426 1.00 50.83  ? 303 TRP B O   1 
ATOM   2042 C CB  . TRP A 1 310 ? 190.975 196.530 131.932 1.00 51.01  ? 303 TRP B CB  1 
ATOM   2043 C CG  . TRP A 1 310 ? 191.108 195.392 132.903 1.00 50.32  ? 303 TRP B CG  1 
ATOM   2044 C CD1 . TRP A 1 310 ? 190.636 194.124 132.745 1.00 44.83  ? 303 TRP B CD1 1 
ATOM   2045 C CD2 . TRP A 1 310 ? 191.744 195.425 134.188 1.00 45.63  ? 303 TRP B CD2 1 
ATOM   2046 N NE1 . TRP A 1 310 ? 190.938 193.366 133.846 1.00 43.84  ? 303 TRP B NE1 1 
ATOM   2047 C CE2 . TRP A 1 310 ? 191.620 194.140 134.746 1.00 40.54  ? 303 TRP B CE2 1 
ATOM   2048 C CE3 . TRP A 1 310 ? 192.407 196.415 134.918 1.00 46.35  ? 303 TRP B CE3 1 
ATOM   2049 C CZ2 . TRP A 1 310 ? 192.128 193.821 136.002 1.00 38.43  ? 303 TRP B CZ2 1 
ATOM   2050 C CZ3 . TRP A 1 310 ? 192.917 196.094 136.157 1.00 45.95  ? 303 TRP B CZ3 1 
ATOM   2051 C CH2 . TRP A 1 310 ? 192.777 194.808 136.687 1.00 41.29  ? 303 TRP B CH2 1 
ATOM   2052 N N   . LEU A 1 311 ? 194.433 195.982 131.270 1.00 52.81  ? 304 LEU B N   1 
ATOM   2053 C CA  . LEU A 1 311 ? 195.724 196.128 131.932 1.00 55.73  ? 304 LEU B CA  1 
ATOM   2054 C C   . LEU A 1 311 ? 196.363 197.473 131.611 1.00 55.44  ? 304 LEU B C   1 
ATOM   2055 O O   . LEU A 1 311 ? 196.974 198.102 132.482 1.00 55.91  ? 304 LEU B O   1 
ATOM   2056 C CB  . LEU A 1 311 ? 196.650 194.979 131.533 1.00 55.75  ? 304 LEU B CB  1 
ATOM   2057 C CG  . LEU A 1 311 ? 198.098 195.059 132.018 1.00 48.84  ? 304 LEU B CG  1 
ATOM   2058 C CD1 . LEU A 1 311 ? 198.171 194.984 133.531 1.00 41.58  ? 304 LEU B CD1 1 
ATOM   2059 C CD2 . LEU A 1 311 ? 198.921 193.959 131.388 1.00 41.72  ? 304 LEU B CD2 1 
ATOM   2060 N N   . THR A 1 312 ? 196.225 197.938 130.368 1.00 62.68  ? 305 THR B N   1 
ATOM   2061 C CA  . THR A 1 312 ? 196.883 199.156 129.920 1.00 66.33  ? 305 THR B CA  1 
ATOM   2062 C C   . THR A 1 312 ? 195.931 200.301 129.608 1.00 66.48  ? 305 THR B C   1 
ATOM   2063 O O   . THR A 1 312 ? 196.397 201.430 129.424 1.00 70.41  ? 305 THR B O   1 
ATOM   2064 C CB  . THR A 1 312 ? 197.731 198.870 128.673 1.00 60.58  ? 305 THR B CB  1 
ATOM   2065 O OG1 . THR A 1 312 ? 196.891 198.360 127.631 1.00 58.98  ? 305 THR B OG1 1 
ATOM   2066 C CG2 . THR A 1 312 ? 198.806 197.852 128.989 1.00 58.80  ? 305 THR B CG2 1 
ATOM   2067 N N   . SER A 1 313 ? 194.626 200.051 129.539 1.00 65.90  ? 306 SER B N   1 
ATOM   2068 C CA  . SER A 1 313 ? 193.690 201.095 129.146 1.00 70.64  ? 306 SER B CA  1 
ATOM   2069 C C   . SER A 1 313 ? 193.669 202.221 130.172 1.00 75.21  ? 306 SER B C   1 
ATOM   2070 O O   . SER A 1 313 ? 193.470 201.992 131.366 1.00 69.21  ? 306 SER B O   1 
ATOM   2071 C CB  . SER A 1 313 ? 192.288 200.514 128.976 1.00 64.91  ? 306 SER B CB  1 
ATOM   2072 O OG  . SER A 1 313 ? 191.695 200.234 130.229 1.00 63.09  ? 306 SER B OG  1 
ATOM   2073 N N   . ASP A 1 314 ? 193.849 203.453 129.691 1.00 75.55  ? 307 ASP B N   1 
ATOM   2074 C CA  . ASP A 1 314 ? 193.929 204.618 130.563 1.00 73.62  ? 307 ASP B CA  1 
ATOM   2075 C C   . ASP A 1 314 ? 192.604 204.964 131.225 1.00 74.28  ? 307 ASP B C   1 
ATOM   2076 O O   . ASP A 1 314 ? 192.587 205.799 132.134 1.00 72.43  ? 307 ASP B O   1 
ATOM   2077 C CB  . ASP A 1 314 ? 194.439 205.829 129.778 1.00 78.66  ? 307 ASP B CB  1 
ATOM   2078 C CG  . ASP A 1 314 ? 195.939 205.793 129.559 1.00 83.96  ? 307 ASP B CG  1 
ATOM   2079 O OD1 . ASP A 1 314 ? 196.567 204.769 129.898 1.00 79.15  ? 307 ASP B OD1 1 
ATOM   2080 O OD2 . ASP A 1 314 ? 196.491 206.789 129.046 1.00 85.27  ? 307 ASP B OD2 1 
ATOM   2081 N N   . LEU A 1 315 ? 191.500 204.358 130.787 1.00 74.75  ? 308 LEU B N   1 
ATOM   2082 C CA  . LEU A 1 315 ? 190.219 204.583 131.447 1.00 74.14  ? 308 LEU B CA  1 
ATOM   2083 C C   . LEU A 1 315 ? 190.251 204.085 132.886 1.00 77.95  ? 308 LEU B C   1 
ATOM   2084 O O   . LEU A 1 315 ? 189.717 204.735 133.792 1.00 79.37  ? 308 LEU B O   1 
ATOM   2085 C CB  . LEU A 1 315 ? 189.102 203.897 130.661 1.00 67.61  ? 308 LEU B CB  1 
ATOM   2086 C CG  . LEU A 1 315 ? 187.716 203.894 131.306 1.00 73.13  ? 308 LEU B CG  1 
ATOM   2087 C CD1 . LEU A 1 315 ? 187.264 205.312 131.618 1.00 69.70  ? 308 LEU B CD1 1 
ATOM   2088 C CD2 . LEU A 1 315 ? 186.710 203.193 130.407 1.00 68.10  ? 308 LEU B CD2 1 
ATOM   2089 N N   . VAL A 1 316 ? 190.876 202.930 133.116 1.00 70.88  ? 309 VAL B N   1 
ATOM   2090 C CA  . VAL A 1 316 ? 190.911 202.366 134.459 1.00 66.27  ? 309 VAL B CA  1 
ATOM   2091 C C   . VAL A 1 316 ? 192.175 202.790 135.203 1.00 68.59  ? 309 VAL B C   1 
ATOM   2092 O O   . VAL A 1 316 ? 192.151 202.947 136.429 1.00 69.54  ? 309 VAL B O   1 
ATOM   2093 C CB  . VAL A 1 316 ? 190.771 200.835 134.385 1.00 58.53  ? 309 VAL B CB  1 
ATOM   2094 C CG1 . VAL A 1 316 ? 191.819 200.247 133.470 1.00 64.34  ? 309 VAL B CG1 1 
ATOM   2095 C CG2 . VAL A 1 316 ? 190.867 200.218 135.758 1.00 54.81  ? 309 VAL B CG2 1 
ATOM   2096 N N   . MET A 1 317 ? 193.285 203.000 134.490 1.00 67.71  ? 310 MET B N   1 
ATOM   2097 C CA  . MET A 1 317 ? 194.518 203.426 135.147 1.00 64.17  ? 310 MET B CA  1 
ATOM   2098 C C   . MET A 1 317 ? 194.348 204.783 135.814 1.00 72.16  ? 310 MET B C   1 
ATOM   2099 O O   . MET A 1 317 ? 194.853 205.007 136.920 1.00 74.41  ? 310 MET B O   1 
ATOM   2100 C CB  . MET A 1 317 ? 195.669 203.469 134.142 1.00 65.17  ? 310 MET B CB  1 
ATOM   2101 C CG  . MET A 1 317 ? 195.804 202.225 133.289 1.00 70.31  ? 310 MET B CG  1 
ATOM   2102 S SD  . MET A 1 317 ? 197.498 201.877 132.784 1.00 79.59  ? 310 MET B SD  1 
ATOM   2103 C CE  . MET A 1 317 ? 198.397 202.405 134.233 1.00 63.85  ? 310 MET B CE  1 
ATOM   2104 N N   . GLY A 1 318 ? 193.649 205.702 135.156 1.00 76.58  ? 311 GLY B N   1 
ATOM   2105 C CA  . GLY A 1 318 ? 193.427 207.040 135.657 1.00 75.54  ? 311 GLY B CA  1 
ATOM   2106 C C   . GLY A 1 318 ? 192.225 207.208 136.559 1.00 78.75  ? 311 GLY B C   1 
ATOM   2107 O O   . GLY A 1 318 ? 191.918 208.339 136.950 1.00 81.96  ? 311 GLY B O   1 
ATOM   2108 N N   . LEU A 1 319 ? 191.535 206.130 136.898 1.00 77.67  ? 312 LEU B N   1 
ATOM   2109 C CA  . LEU A 1 319 ? 190.388 206.217 137.793 1.00 77.40  ? 312 LEU B CA  1 
ATOM   2110 C C   . LEU A 1 319 ? 190.851 206.685 139.167 1.00 77.89  ? 312 LEU B C   1 
ATOM   2111 O O   . LEU A 1 319 ? 191.739 206.056 139.756 1.00 74.89  ? 312 LEU B O   1 
ATOM   2112 C CB  . LEU A 1 319 ? 189.701 204.860 137.894 1.00 74.98  ? 312 LEU B CB  1 
ATOM   2113 C CG  . LEU A 1 319 ? 188.314 204.782 138.528 1.00 73.54  ? 312 LEU B CG  1 
ATOM   2114 C CD1 . LEU A 1 319 ? 187.346 205.729 137.844 1.00 78.12  ? 312 LEU B CD1 1 
ATOM   2115 C CD2 . LEU A 1 319 ? 187.800 203.357 138.466 1.00 71.08  ? 312 LEU B CD2 1 
ATOM   2116 N N   . PRO A 1 320 ? 190.302 207.775 139.703 1.00 79.67  ? 313 PRO B N   1 
ATOM   2117 C CA  . PRO A 1 320 ? 190.775 208.272 141.001 1.00 79.27  ? 313 PRO B CA  1 
ATOM   2118 C C   . PRO A 1 320 ? 190.527 207.265 142.113 1.00 74.56  ? 313 PRO B C   1 
ATOM   2119 O O   . PRO A 1 320 ? 189.499 206.586 142.144 1.00 72.70  ? 313 PRO B O   1 
ATOM   2120 C CB  . PRO A 1 320 ? 189.958 209.553 141.211 1.00 73.54  ? 313 PRO B CB  1 
ATOM   2121 C CG  . PRO A 1 320 ? 188.752 209.383 140.347 1.00 74.16  ? 313 PRO B CG  1 
ATOM   2122 C CD  . PRO A 1 320 ? 189.210 208.597 139.157 1.00 75.50  ? 313 PRO B CD  1 
ATOM   2123 N N   . GLY A 1 321 ? 191.483 207.183 143.035 1.00 72.48  ? 314 GLY B N   1 
ATOM   2124 C CA  . GLY A 1 321 ? 191.378 206.298 144.174 1.00 70.07  ? 314 GLY B CA  1 
ATOM   2125 C C   . GLY A 1 321 ? 191.778 204.861 143.927 1.00 70.77  ? 314 GLY B C   1 
ATOM   2126 O O   . GLY A 1 321 ? 191.688 204.047 144.854 1.00 72.22  ? 314 GLY B O   1 
ATOM   2127 N N   . MET A 1 322 ? 192.220 204.515 142.716 1.00 68.24  ? 315 MET B N   1 
ATOM   2128 C CA  . MET A 1 322 ? 192.601 203.136 142.435 1.00 63.85  ? 315 MET B CA  1 
ATOM   2129 C C   . MET A 1 322 ? 193.869 202.709 143.163 1.00 65.35  ? 315 MET B C   1 
ATOM   2130 O O   . MET A 1 322 ? 194.088 201.507 143.343 1.00 61.71  ? 315 MET B O   1 
ATOM   2131 C CB  . MET A 1 322 ? 192.774 202.928 140.933 1.00 61.45  ? 315 MET B CB  1 
ATOM   2132 C CG  . MET A 1 322 ? 192.760 201.468 140.547 1.00 64.05  ? 315 MET B CG  1 
ATOM   2133 S SD  . MET A 1 322 ? 191.765 201.066 139.113 1.00 69.22  ? 315 MET B SD  1 
ATOM   2134 C CE  . MET A 1 322 ? 192.057 199.304 139.047 1.00 52.54  ? 315 MET B CE  1 
ATOM   2135 N N   . ALA A 1 323 ? 194.704 203.655 143.591 1.00 68.32  ? 316 ALA B N   1 
ATOM   2136 C CA  . ALA A 1 323 ? 195.922 203.302 144.307 1.00 69.61  ? 316 ALA B CA  1 
ATOM   2137 C C   . ALA A 1 323 ? 195.645 202.580 145.617 1.00 67.60  ? 316 ALA B C   1 
ATOM   2138 O O   . ALA A 1 323 ? 196.551 201.931 146.150 1.00 68.62  ? 316 ALA B O   1 
ATOM   2139 C CB  . ALA A 1 323 ? 196.756 204.554 144.573 1.00 68.96  ? 316 ALA B CB  1 
ATOM   2140 N N   . GLN A 1 324 ? 194.425 202.675 146.144 1.00 64.84  ? 317 GLN B N   1 
ATOM   2141 C CA  . GLN A 1 324 ? 194.054 202.053 147.405 1.00 64.77  ? 317 GLN B CA  1 
ATOM   2142 C C   . GLN A 1 324 ? 193.306 200.739 147.215 1.00 59.57  ? 317 GLN B C   1 
ATOM   2143 O O   . GLN A 1 324 ? 192.662 200.262 148.156 1.00 57.44  ? 317 GLN B O   1 
ATOM   2144 C CB  . GLN A 1 324 ? 193.211 203.021 148.239 1.00 64.97  ? 317 GLN B CB  1 
ATOM   2145 C CG  . GLN A 1 324 ? 193.319 204.478 147.812 1.00 75.28  ? 317 GLN B CG  1 
ATOM   2146 C CD  . GLN A 1 324 ? 194.699 205.064 148.053 1.00 80.70  ? 317 GLN B CD  1 
ATOM   2147 O OE1 . GLN A 1 324 ? 195.457 204.574 148.890 1.00 73.50  ? 317 GLN B OE1 1 
ATOM   2148 N NE2 . GLN A 1 324 ? 195.032 206.116 147.314 1.00 78.76  ? 317 GLN B NE2 1 
ATOM   2149 N N   . MET A 1 325 ? 193.375 200.142 146.026 1.00 55.64  ? 318 MET B N   1 
ATOM   2150 C CA  . MET A 1 325 ? 192.632 198.921 145.740 1.00 53.67  ? 318 MET B CA  1 
ATOM   2151 C C   . MET A 1 325 ? 193.560 197.761 145.398 1.00 46.62  ? 318 MET B C   1 
ATOM   2152 O O   . MET A 1 325 ? 193.171 196.842 144.675 1.00 42.01  ? 318 MET B O   1 
ATOM   2153 C CB  . MET A 1 325 ? 191.622 199.151 144.620 1.00 49.50  ? 318 MET B CB  1 
ATOM   2154 C CG  . MET A 1 325 ? 190.430 199.979 145.055 1.00 58.18  ? 318 MET B CG  1 
ATOM   2155 S SD  . MET A 1 325 ? 188.888 199.166 144.633 1.00 62.88  ? 318 MET B SD  1 
ATOM   2156 C CE  . MET A 1 325 ? 189.273 198.665 142.965 1.00 53.19  ? 318 MET B CE  1 
ATOM   2157 N N   . GLY A 1 326 ? 194.784 197.787 145.911 1.00 47.04  ? 319 GLY B N   1 
ATOM   2158 C CA  . GLY A 1 326 ? 195.701 196.682 145.755 1.00 42.54  ? 319 GLY B CA  1 
ATOM   2159 C C   . GLY A 1 326 ? 196.511 196.748 144.475 1.00 42.06  ? 319 GLY B C   1 
ATOM   2160 O O   . GLY A 1 326 ? 196.349 197.631 143.631 1.00 43.80  ? 319 GLY B O   1 
ATOM   2161 N N   . THR A 1 327 ? 197.410 195.777 144.341 1.00 42.22  ? 320 THR B N   1 
ATOM   2162 C CA  . THR A 1 327 ? 198.285 195.712 143.180 1.00 45.45  ? 320 THR B CA  1 
ATOM   2163 C C   . THR A 1 327 ? 197.565 195.090 141.994 1.00 39.64  ? 320 THR B C   1 
ATOM   2164 O O   . THR A 1 327 ? 196.809 194.127 142.142 1.00 36.98  ? 320 THR B O   1 
ATOM   2165 C CB  . THR A 1 327 ? 199.537 194.899 143.501 1.00 42.34  ? 320 THR B CB  1 
ATOM   2166 O OG1 . THR A 1 327 ? 199.173 193.535 143.737 1.00 32.51  ? 320 THR B OG1 1 
ATOM   2167 C CG2 . THR A 1 327 ? 200.226 195.455 144.726 1.00 46.49  ? 320 THR B CG2 1 
ATOM   2168 N N   . VAL A 1 328 ? 197.808 195.641 140.812 1.00 36.23  ? 321 VAL B N   1 
ATOM   2169 C CA  . VAL A 1 328 ? 197.282 195.096 139.569 1.00 33.90  ? 321 VAL B CA  1 
ATOM   2170 C C   . VAL A 1 328 ? 198.443 194.451 138.828 1.00 37.53  ? 321 VAL B C   1 
ATOM   2171 O O   . VAL A 1 328 ? 199.424 195.118 138.486 1.00 44.59  ? 321 VAL B O   1 
ATOM   2172 C CB  . VAL A 1 328 ? 196.602 196.173 138.716 1.00 38.08  ? 321 VAL B CB  1 
ATOM   2173 C CG1 . VAL A 1 328 ? 196.331 195.643 137.321 1.00 39.12  ? 321 VAL B CG1 1 
ATOM   2174 C CG2 . VAL A 1 328 ? 195.314 196.632 139.372 1.00 36.79  ? 321 VAL B CG2 1 
ATOM   2175 N N   . LEU A 1 329 ? 198.331 193.151 138.586 1.00 32.43  ? 322 LEU B N   1 
ATOM   2176 C CA  . LEU A 1 329 ? 199.334 192.360 137.879 1.00 31.39  ? 322 LEU B CA  1 
ATOM   2177 C C   . LEU A 1 329 ? 198.655 191.821 136.628 1.00 33.16  ? 322 LEU B C   1 
ATOM   2178 O O   . LEU A 1 329 ? 197.544 191.297 136.700 1.00 33.67  ? 322 LEU B O   1 
ATOM   2179 C CB  . LEU A 1 329 ? 199.856 191.232 138.763 1.00 28.59  ? 322 LEU B CB  1 
ATOM   2180 C CG  . LEU A 1 329 ? 201.201 191.402 139.461 1.00 27.96  ? 322 LEU B CG  1 
ATOM   2181 C CD1 . LEU A 1 329 ? 201.519 190.160 140.259 1.00 29.13  ? 322 LEU B CD1 1 
ATOM   2182 C CD2 . LEU A 1 329 ? 202.282 191.656 138.442 1.00 32.52  ? 322 LEU B CD2 1 
ATOM   2183 N N   . GLY A 1 330 ? 199.310 191.962 135.479 1.00 32.97  ? 323 GLY B N   1 
ATOM   2184 C CA  . GLY A 1 330 ? 198.760 191.473 134.238 1.00 32.72  ? 323 GLY B CA  1 
ATOM   2185 C C   . GLY A 1 330 ? 199.849 191.005 133.294 1.00 36.66  ? 323 GLY B C   1 
ATOM   2186 O O   . GLY A 1 330 ? 201.032 191.269 133.490 1.00 38.79  ? 323 GLY B O   1 
ATOM   2187 N N   . PHE A 1 331 ? 199.418 190.304 132.252 1.00 36.34  ? 324 PHE B N   1 
ATOM   2188 C CA  . PHE A 1 331 ? 200.308 189.820 131.209 1.00 37.19  ? 324 PHE B CA  1 
ATOM   2189 C C   . PHE A 1 331 ? 200.037 190.594 129.929 1.00 44.14  ? 324 PHE B C   1 
ATOM   2190 O O   . PHE A 1 331 ? 198.931 190.530 129.383 1.00 44.69  ? 324 PHE B O   1 
ATOM   2191 C CB  . PHE A 1 331 ? 200.117 188.321 130.979 1.00 39.56  ? 324 PHE B CB  1 
ATOM   2192 C CG  . PHE A 1 331 ? 200.823 187.467 131.984 1.00 37.42  ? 324 PHE B CG  1 
ATOM   2193 C CD1 . PHE A 1 331 ? 202.179 187.228 131.878 1.00 35.53  ? 324 PHE B CD1 1 
ATOM   2194 C CD2 . PHE A 1 331 ? 200.128 186.906 133.040 1.00 36.94  ? 324 PHE B CD2 1 
ATOM   2195 C CE1 . PHE A 1 331 ? 202.828 186.448 132.805 1.00 34.46  ? 324 PHE B CE1 1 
ATOM   2196 C CE2 . PHE A 1 331 ? 200.771 186.125 133.969 1.00 36.78  ? 324 PHE B CE2 1 
ATOM   2197 C CZ  . PHE A 1 331 ? 202.121 185.894 133.851 1.00 37.31  ? 324 PHE B CZ  1 
ATOM   2198 N N   . LEU A 1 332 ? 201.047 191.315 129.452 1.00 46.36  ? 325 LEU B N   1 
ATOM   2199 C CA  . LEU A 1 332 ? 200.937 192.145 128.264 1.00 49.38  ? 325 LEU B CA  1 
ATOM   2200 C C   . LEU A 1 332 ? 201.728 191.519 127.125 1.00 49.34  ? 325 LEU B C   1 
ATOM   2201 O O   . LEU A 1 332 ? 202.860 191.067 127.310 1.00 54.09  ? 325 LEU B O   1 
ATOM   2202 C CB  . LEU A 1 332 ? 201.441 193.567 128.526 1.00 50.29  ? 325 LEU B CB  1 
ATOM   2203 C CG  . LEU A 1 332 ? 201.135 194.589 127.432 1.00 51.94  ? 325 LEU B CG  1 
ATOM   2204 C CD1 . LEU A 1 332 ? 199.638 194.749 127.257 1.00 49.88  ? 325 LEU B CD1 1 
ATOM   2205 C CD2 . LEU A 1 332 ? 201.783 195.923 127.747 1.00 56.60  ? 325 LEU B CD2 1 
ATOM   2206 N N   . GLN A 1 333 ? 201.118 191.502 125.945 1.00 49.42  ? 326 GLN B N   1 
ATOM   2207 C CA  . GLN A 1 333 ? 201.727 190.862 124.789 1.00 50.16  ? 326 GLN B CA  1 
ATOM   2208 C C   . GLN A 1 333 ? 203.065 191.506 124.452 1.00 53.38  ? 326 GLN B C   1 
ATOM   2209 O O   . GLN A 1 333 ? 203.195 192.732 124.421 1.00 57.35  ? 326 GLN B O   1 
ATOM   2210 C CB  . GLN A 1 333 ? 200.789 190.951 123.589 1.00 55.97  ? 326 GLN B CB  1 
ATOM   2211 C CG  . GLN A 1 333 ? 201.109 189.995 122.462 1.00 56.37  ? 326 GLN B CG  1 
ATOM   2212 C CD  . GLN A 1 333 ? 200.160 190.159 121.297 1.00 64.26  ? 326 GLN B CD  1 
ATOM   2213 O OE1 . GLN A 1 333 ? 198.941 190.128 121.467 1.00 63.88  ? 326 GLN B OE1 1 
ATOM   2214 N NE2 . GLN A 1 333 ? 200.712 190.335 120.103 1.00 62.88  ? 326 GLN B NE2 1 
ATOM   2215 N N   . ARG A 1 334 ? 204.060 190.666 124.194 1.00 55.91  ? 327 ARG B N   1 
ATOM   2216 C CA  . ARG A 1 334 ? 205.402 191.106 123.827 1.00 61.58  ? 327 ARG B CA  1 
ATOM   2217 C C   . ARG A 1 334 ? 205.499 191.009 122.308 1.00 70.18  ? 327 ARG B C   1 
ATOM   2218 O O   . ARG A 1 334 ? 205.843 189.963 121.756 1.00 67.89  ? 327 ARG B O   1 
ATOM   2219 C CB  . ARG A 1 334 ? 206.467 190.262 124.517 1.00 61.76  ? 327 ARG B CB  1 
ATOM   2220 C CG  . ARG A 1 334 ? 207.839 190.897 124.561 1.00 63.33  ? 327 ARG B CG  1 
ATOM   2221 C CD  . ARG A 1 334 ? 208.633 190.384 125.745 1.00 66.94  ? 327 ARG B CD  1 
ATOM   2222 N NE  . ARG A 1 334 ? 210.054 190.264 125.441 1.00 70.01  ? 327 ARG B NE  1 
ATOM   2223 C CZ  . ARG A 1 334 ? 210.901 191.282 125.399 1.00 66.76  ? 327 ARG B CZ  1 
ATOM   2224 N NH1 . ARG A 1 334 ? 210.508 192.520 125.649 1.00 67.94  ? 327 ARG B NH1 1 
ATOM   2225 N NH2 . ARG A 1 334 ? 212.177 191.053 125.102 1.00 63.82  ? 327 ARG B NH2 1 
ATOM   2226 N N   . GLY A 1 335 ? 205.184 192.113 121.633 1.00 70.15  ? 328 GLY B N   1 
ATOM   2227 C CA  . GLY A 1 335 ? 205.221 192.153 120.191 1.00 68.68  ? 328 GLY B CA  1 
ATOM   2228 C C   . GLY A 1 335 ? 205.979 193.371 119.702 1.00 70.79  ? 328 GLY B C   1 
ATOM   2229 O O   . GLY A 1 335 ? 206.236 194.316 120.447 1.00 71.41  ? 328 GLY B O   1 
ATOM   2230 N N   . ALA A 1 336 ? 206.335 193.328 118.423 1.00 69.67  ? 329 ALA B N   1 
ATOM   2231 C CA  . ALA A 1 336 ? 207.070 194.419 117.800 1.00 69.02  ? 329 ALA B CA  1 
ATOM   2232 C C   . ALA A 1 336 ? 206.093 195.520 117.395 1.00 66.73  ? 329 ALA B C   1 
ATOM   2233 O O   . ALA A 1 336 ? 204.875 195.395 117.548 1.00 62.36  ? 329 ALA B O   1 
ATOM   2234 C CB  . ALA A 1 336 ? 207.880 193.900 116.616 1.00 63.44  ? 329 ALA B CB  1 
ATOM   2235 N N   . GLN A 1 337 ? 206.624 196.623 116.877 1.00 70.72  ? 330 GLN B N   1 
ATOM   2236 C CA  . GLN A 1 337 ? 205.798 197.720 116.401 1.00 81.48  ? 330 GLN B CA  1 
ATOM   2237 C C   . GLN A 1 337 ? 206.346 198.195 115.066 1.00 82.19  ? 330 GLN B C   1 
ATOM   2238 O O   . GLN A 1 337 ? 207.524 198.001 114.759 1.00 84.27  ? 330 GLN B O   1 
ATOM   2239 C CB  . GLN A 1 337 ? 205.753 198.878 117.403 1.00 89.37  ? 330 GLN B CB  1 
ATOM   2240 C CG  . GLN A 1 337 ? 207.083 199.178 118.069 1.00 95.60  ? 330 GLN B CG  1 
ATOM   2241 C CD  . GLN A 1 337 ? 207.024 200.408 118.949 1.00 105.94 ? 330 GLN B CD  1 
ATOM   2242 O OE1 . GLN A 1 337 ? 206.057 200.614 119.683 1.00 106.44 ? 330 GLN B OE1 1 
ATOM   2243 N NE2 . GLN A 1 337 ? 208.058 201.237 118.877 1.00 109.22 ? 330 GLN B NE2 1 
ATOM   2244 N N   . LEU A 1 338 ? 205.478 198.814 114.275 1.00 78.79  ? 331 LEU B N   1 
ATOM   2245 C CA  . LEU A 1 338 ? 205.860 199.309 112.957 1.00 76.26  ? 331 LEU B CA  1 
ATOM   2246 C C   . LEU A 1 338 ? 206.535 200.662 113.131 1.00 77.16  ? 331 LEU B C   1 
ATOM   2247 O O   . LEU A 1 338 ? 205.874 201.677 113.355 1.00 79.70  ? 331 LEU B O   1 
ATOM   2248 C CB  . LEU A 1 338 ? 204.636 199.403 112.056 1.00 74.57  ? 331 LEU B CB  1 
ATOM   2249 C CG  . LEU A 1 338 ? 204.191 198.123 111.352 1.00 62.94  ? 331 LEU B CG  1 
ATOM   2250 C CD1 . LEU A 1 338 ? 203.068 198.419 110.376 1.00 55.51  ? 331 LEU B CD1 1 
ATOM   2251 C CD2 . LEU A 1 338 ? 205.364 197.479 110.644 1.00 64.60  ? 331 LEU B CD2 1 
ATOM   2252 N N   . HIS A 1 339 ? 207.865 200.678 113.033 1.00 80.93  ? 332 HIS B N   1 
ATOM   2253 C CA  . HIS A 1 339 ? 208.614 201.895 113.332 1.00 84.14  ? 332 HIS B CA  1 
ATOM   2254 C C   . HIS A 1 339 ? 208.334 202.991 112.313 1.00 84.37  ? 332 HIS B C   1 
ATOM   2255 O O   . HIS A 1 339 ? 208.239 204.170 112.673 1.00 85.67  ? 332 HIS B O   1 
ATOM   2256 C CB  . HIS A 1 339 ? 210.108 201.587 113.397 1.00 87.70  ? 332 HIS B CB  1 
ATOM   2257 C CG  . HIS A 1 339 ? 210.499 200.748 114.573 1.00 100.35 ? 332 HIS B CG  1 
ATOM   2258 N ND1 . HIS A 1 339 ? 209.932 200.906 115.819 1.00 102.94 ? 332 HIS B ND1 1 
ATOM   2259 C CD2 . HIS A 1 339 ? 211.402 199.747 114.695 1.00 101.61 ? 332 HIS B CD2 1 
ATOM   2260 C CE1 . HIS A 1 339 ? 210.467 200.035 116.657 1.00 100.40 ? 332 HIS B CE1 1 
ATOM   2261 N NE2 . HIS A 1 339 ? 211.362 199.321 116.000 1.00 102.56 ? 332 HIS B NE2 1 
ATOM   2262 N N   . GLU A 1 340 ? 208.199 202.630 111.041 1.00 84.56  ? 333 GLU B N   1 
ATOM   2263 C CA  . GLU A 1 340 ? 207.972 203.610 109.988 1.00 78.88  ? 333 GLU B CA  1 
ATOM   2264 C C   . GLU A 1 340 ? 206.498 203.811 109.660 1.00 71.63  ? 333 GLU B C   1 
ATOM   2265 O O   . GLU A 1 340 ? 206.188 204.509 108.691 1.00 69.84  ? 333 GLU B O   1 
ATOM   2266 C CB  . GLU A 1 340 ? 208.733 203.212 108.718 1.00 82.85  ? 333 GLU B CB  1 
ATOM   2267 C CG  . GLU A 1 340 ? 210.245 203.269 108.839 1.00 89.08  ? 333 GLU B CG  1 
ATOM   2268 C CD  . GLU A 1 340 ? 210.944 202.796 107.577 1.00 97.65  ? 333 GLU B CD  1 
ATOM   2269 O OE1 . GLU A 1 340 ? 210.261 202.249 106.686 1.00 94.75  ? 333 GLU B OE1 1 
ATOM   2270 O OE2 . GLU A 1 340 ? 212.176 202.966 107.477 1.00 94.53  ? 333 GLU B OE2 1 
ATOM   2271 N N   . PHE A 1 341 ? 205.588 203.214 110.430 1.00 69.90  ? 334 PHE B N   1 
ATOM   2272 C CA  . PHE A 1 341 ? 204.164 203.398 110.159 1.00 63.51  ? 334 PHE B CA  1 
ATOM   2273 C C   . PHE A 1 341 ? 203.673 204.828 110.335 1.00 68.59  ? 334 PHE B C   1 
ATOM   2274 O O   . PHE A 1 341 ? 202.968 205.313 109.433 1.00 73.06  ? 334 PHE B O   1 
ATOM   2275 C CB  . PHE A 1 341 ? 203.330 202.447 111.024 1.00 65.56  ? 334 PHE B CB  1 
ATOM   2276 C CG  . PHE A 1 341 ? 201.857 202.524 110.749 1.00 60.87  ? 334 PHE B CG  1 
ATOM   2277 C CD1 . PHE A 1 341 ? 201.366 202.323 109.473 1.00 54.56  ? 334 PHE B CD1 1 
ATOM   2278 C CD2 . PHE A 1 341 ? 200.962 202.793 111.768 1.00 58.33  ? 334 PHE B CD2 1 
ATOM   2279 C CE1 . PHE A 1 341 ? 200.015 202.395 109.218 1.00 51.48  ? 334 PHE B CE1 1 
ATOM   2280 C CE2 . PHE A 1 341 ? 199.608 202.865 111.518 1.00 56.32  ? 334 PHE B CE2 1 
ATOM   2281 C CZ  . PHE A 1 341 ? 199.135 202.664 110.241 1.00 50.91  ? 334 PHE B CZ  1 
ATOM   2282 N N   . PRO A 1 342 ? 203.952 205.539 111.439 1.00 71.37  ? 335 PRO B N   1 
ATOM   2283 C CA  . PRO A 1 342 ? 203.447 206.921 111.543 1.00 67.62  ? 335 PRO B CA  1 
ATOM   2284 C C   . PRO A 1 342 ? 203.930 207.814 110.417 1.00 65.29  ? 335 PRO B C   1 
ATOM   2285 O O   . PRO A 1 342 ? 203.162 208.635 109.889 1.00 66.37  ? 335 PRO B O   1 
ATOM   2286 C CB  . PRO A 1 342 ? 203.977 207.385 112.908 1.00 66.59  ? 335 PRO B CB  1 
ATOM   2287 C CG  . PRO A 1 342 ? 205.079 206.444 113.241 1.00 69.50  ? 335 PRO B CG  1 
ATOM   2288 C CD  . PRO A 1 342 ? 204.670 205.139 112.661 1.00 68.85  ? 335 PRO B CD  1 
ATOM   2289 N N   . GLN A 1 343 ? 205.191 207.649 110.018 1.00 63.18  ? 336 GLN B N   1 
ATOM   2290 C CA  . GLN A 1 343 ? 205.699 208.367 108.859 1.00 67.59  ? 336 GLN B CA  1 
ATOM   2291 C C   . GLN A 1 343 ? 204.900 208.019 107.614 1.00 69.14  ? 336 GLN B C   1 
ATOM   2292 O O   . GLN A 1 343 ? 204.577 208.901 106.812 1.00 68.82  ? 336 GLN B O   1 
ATOM   2293 C CB  . GLN A 1 343 ? 207.179 208.046 108.653 1.00 70.63  ? 336 GLN B CB  1 
ATOM   2294 C CG  . GLN A 1 343 ? 207.993 209.146 107.983 1.00 71.87  ? 336 GLN B CG  1 
ATOM   2295 C CD  . GLN A 1 343 ? 207.612 210.538 108.443 1.00 76.31  ? 336 GLN B CD  1 
ATOM   2296 O OE1 . GLN A 1 343 ? 207.515 210.808 109.640 1.00 80.87  ? 336 GLN B OE1 1 
ATOM   2297 N NE2 . GLN A 1 343 ? 207.399 211.435 107.487 1.00 74.16  ? 336 GLN B NE2 1 
ATOM   2298 N N   . TYR A 1 344 ? 204.574 206.736 107.439 1.00 70.73  ? 337 TYR B N   1 
ATOM   2299 C CA  . TYR A 1 344 ? 203.827 206.311 106.260 1.00 63.58  ? 337 TYR B CA  1 
ATOM   2300 C C   . TYR A 1 344 ? 202.446 206.949 106.230 1.00 67.55  ? 337 TYR B C   1 
ATOM   2301 O O   . TYR A 1 344 ? 202.001 207.433 105.183 1.00 75.20  ? 337 TYR B O   1 
ATOM   2302 C CB  . TYR A 1 344 ? 203.718 204.784 106.227 1.00 55.32  ? 337 TYR B CB  1 
ATOM   2303 C CG  . TYR A 1 344 ? 202.838 204.259 105.115 1.00 58.60  ? 337 TYR B CG  1 
ATOM   2304 C CD1 . TYR A 1 344 ? 203.361 204.027 103.851 1.00 61.59  ? 337 TYR B CD1 1 
ATOM   2305 C CD2 . TYR A 1 344 ? 201.490 204.000 105.323 1.00 57.89  ? 337 TYR B CD2 1 
ATOM   2306 C CE1 . TYR A 1 344 ? 202.571 203.555 102.828 1.00 57.96  ? 337 TYR B CE1 1 
ATOM   2307 C CE2 . TYR A 1 344 ? 200.691 203.529 104.301 1.00 57.69  ? 337 TYR B CE2 1 
ATOM   2308 C CZ  . TYR A 1 344 ? 201.239 203.307 103.057 1.00 61.22  ? 337 TYR B CZ  1 
ATOM   2309 O OH  . TYR A 1 344 ? 200.454 202.836 102.033 1.00 62.20  ? 337 TYR B OH  1 
ATOM   2310 N N   . VAL A 1 345 ? 201.757 206.971 107.375 1.00 64.17  ? 338 VAL B N   1 
ATOM   2311 C CA  . VAL A 1 345 ? 200.432 207.585 107.436 1.00 64.17  ? 338 VAL B CA  1 
ATOM   2312 C C   . VAL A 1 345 ? 200.517 209.067 107.108 1.00 71.92  ? 338 VAL B C   1 
ATOM   2313 O O   . VAL A 1 345 ? 199.703 209.595 106.344 1.00 73.70  ? 338 VAL B O   1 
ATOM   2314 C CB  . VAL A 1 345 ? 199.781 207.363 108.812 1.00 61.74  ? 338 VAL B CB  1 
ATOM   2315 C CG1 . VAL A 1 345 ? 198.295 207.633 108.729 1.00 67.03  ? 338 VAL B CG1 1 
ATOM   2316 C CG2 . VAL A 1 345 ? 199.997 205.957 109.277 1.00 61.71  ? 338 VAL B CG2 1 
ATOM   2317 N N   . LYS A 1 346 ? 201.495 209.767 107.689 1.00 69.25  ? 339 LYS B N   1 
ATOM   2318 C CA  . LYS A 1 346 ? 201.535 211.207 107.470 1.00 67.80  ? 339 LYS B CA  1 
ATOM   2319 C C   . LYS A 1 346 ? 201.906 211.542 106.028 1.00 69.31  ? 339 LYS B C   1 
ATOM   2320 O O   . LYS A 1 346 ? 201.310 212.446 105.430 1.00 76.15  ? 339 LYS B O   1 
ATOM   2321 C CB  . LYS A 1 346 ? 202.473 211.884 108.471 1.00 71.55  ? 339 LYS B CB  1 
ATOM   2322 C CG  . LYS A 1 346 ? 203.936 211.525 108.378 1.00 77.19  ? 339 LYS B CG  1 
ATOM   2323 C CD  . LYS A 1 346 ? 204.784 212.480 109.213 1.00 77.65  ? 339 LYS B CD  1 
ATOM   2324 C CE  . LYS A 1 346 ? 204.032 212.973 110.441 1.00 80.52  ? 339 LYS B CE  1 
ATOM   2325 N NZ  . LYS A 1 346 ? 204.667 214.174 111.049 1.00 83.98  ? 339 LYS B NZ  1 
ATOM   2326 N N   . THR A 1 347 ? 202.848 210.804 105.426 1.00 69.80  ? 340 THR B N   1 
ATOM   2327 C CA  . THR A 1 347 ? 203.187 211.104 104.036 1.00 73.96  ? 340 THR B CA  1 
ATOM   2328 C C   . THR A 1 347 ? 202.048 210.720 103.102 1.00 77.53  ? 340 THR B C   1 
ATOM   2329 O O   . THR A 1 347 ? 201.808 211.402 102.101 1.00 78.65  ? 340 THR B O   1 
ATOM   2330 C CB  . THR A 1 347 ? 204.476 210.406 103.595 1.00 70.81  ? 340 THR B CB  1 
ATOM   2331 O OG1 . THR A 1 347 ? 204.635 210.579 102.182 1.00 72.60  ? 340 THR B OG1 1 
ATOM   2332 C CG2 . THR A 1 347 ? 204.408 208.925 103.848 1.00 69.15  ? 340 THR B CG2 1 
ATOM   2333 N N   . HIS A 1 348 ? 201.319 209.646 103.416 1.00 79.03  ? 341 HIS B N   1 
ATOM   2334 C CA  . HIS A 1 348 ? 200.210 209.246 102.561 1.00 82.79  ? 341 HIS B CA  1 
ATOM   2335 C C   . HIS A 1 348 ? 199.053 210.231 102.661 1.00 84.37  ? 341 HIS B C   1 
ATOM   2336 O O   . HIS A 1 348 ? 198.421 210.557 101.650 1.00 86.12  ? 341 HIS B O   1 
ATOM   2337 C CB  . HIS A 1 348 ? 199.759 207.831 102.920 1.00 80.63  ? 341 HIS B CB  1 
ATOM   2338 C CG  . HIS A 1 348 ? 198.765 207.259 101.962 1.00 89.99  ? 341 HIS B CG  1 
ATOM   2339 N ND1 . HIS A 1 348 ? 197.408 207.459 102.092 1.00 97.29  ? 341 HIS B ND1 1 
ATOM   2340 C CD2 . HIS A 1 348 ? 198.932 206.516 100.843 1.00 87.28  ? 341 HIS B CD2 1 
ATOM   2341 C CE1 . HIS A 1 348 ? 196.780 206.848 101.104 1.00 91.84  ? 341 HIS B CE1 1 
ATOM   2342 N NE2 . HIS A 1 348 ? 197.682 206.274 100.328 1.00 91.99  ? 341 HIS B NE2 1 
ATOM   2343 N N   . LEU A 1 349 ? 198.772 210.729 103.867 1.00 81.38  ? 342 LEU B N   1 
ATOM   2344 C CA  . LEU A 1 349 ? 197.745 211.752 104.025 1.00 82.46  ? 342 LEU B CA  1 
ATOM   2345 C C   . LEU A 1 349 ? 198.144 213.046 103.328 1.00 85.18  ? 342 LEU B C   1 
ATOM   2346 O O   . LEU A 1 349 ? 197.296 213.722 102.734 1.00 89.18  ? 342 LEU B O   1 
ATOM   2347 C CB  . LEU A 1 349 ? 197.475 212.001 105.508 1.00 75.13  ? 342 LEU B CB  1 
ATOM   2348 C CG  . LEU A 1 349 ? 196.763 210.883 106.271 1.00 76.62  ? 342 LEU B CG  1 
ATOM   2349 C CD1 . LEU A 1 349 ? 196.083 211.427 107.512 1.00 81.58  ? 342 LEU B CD1 1 
ATOM   2350 C CD2 . LEU A 1 349 ? 195.768 210.162 105.381 1.00 75.94  ? 342 LEU B CD2 1 
ATOM   2351 N N   . ALA A 1 350 ? 199.426 213.415 103.397 1.00 83.13  ? 343 ALA B N   1 
ATOM   2352 C CA  . ALA A 1 350 ? 199.884 214.605 102.687 1.00 84.77  ? 343 ALA B CA  1 
ATOM   2353 C C   . ALA A 1 350 ? 199.776 214.430 101.177 1.00 92.27  ? 343 ALA B C   1 
ATOM   2354 O O   . ALA A 1 350 ? 199.375 215.359 100.466 1.00 98.95  ? 343 ALA B O   1 
ATOM   2355 C CB  . ALA A 1 350 ? 201.321 214.935 103.090 1.00 75.95  ? 343 ALA B CB  1 
ATOM   2356 N N   . LEU A 1 351 ? 200.126 213.248 100.668 1.00 88.73  ? 344 LEU B N   1 
ATOM   2357 C CA  . LEU A 1 351 ? 200.110 213.006 99.230  1.00 93.07  ? 344 LEU B CA  1 
ATOM   2358 C C   . LEU A 1 351 ? 198.696 212.841 98.687  1.00 97.70  ? 344 LEU B C   1 
ATOM   2359 O O   . LEU A 1 351 ? 198.457 213.114 97.506  1.00 103.91 ? 344 LEU B O   1 
ATOM   2360 C CB  . LEU A 1 351 ? 200.967 211.775 98.915  1.00 95.84  ? 344 LEU B CB  1 
ATOM   2361 C CG  . LEU A 1 351 ? 201.289 211.380 97.474  1.00 103.61 ? 344 LEU B CG  1 
ATOM   2362 C CD1 . LEU A 1 351 ? 202.666 210.751 97.408  1.00 97.61  ? 344 LEU B CD1 1 
ATOM   2363 C CD2 . LEU A 1 351 ? 200.244 210.410 96.953  1.00 101.64 ? 344 LEU B CD2 1 
ATOM   2364 N N   . ALA A 1 352 ? 197.752 212.409 99.525  1.00 97.96  ? 345 ALA B N   1 
ATOM   2365 C CA  . ALA A 1 352 ? 196.372 212.258 99.080  1.00 103.82 ? 345 ALA B CA  1 
ATOM   2366 C C   . ALA A 1 352 ? 195.717 213.589 98.734  1.00 105.09 ? 345 ALA B C   1 
ATOM   2367 O O   . ALA A 1 352 ? 194.693 213.599 98.043  1.00 104.20 ? 345 ALA B O   1 
ATOM   2368 C CB  . ALA A 1 352 ? 195.551 211.541 100.152 1.00 97.39  ? 345 ALA B CB  1 
ATOM   2369 N N   . THR A 1 353 ? 196.276 214.708 99.198  1.00 105.74 ? 346 THR B N   1 
ATOM   2370 C CA  . THR A 1 353 ? 195.675 216.011 98.946  1.00 107.19 ? 346 THR B CA  1 
ATOM   2371 C C   . THR A 1 353 ? 195.996 216.560 97.563  1.00 110.91 ? 346 THR B C   1 
ATOM   2372 O O   . THR A 1 353 ? 195.329 217.499 97.116  1.00 112.86 ? 346 THR B O   1 
ATOM   2373 C CB  . THR A 1 353 ? 196.133 217.018 100.003 1.00 104.36 ? 346 THR B CB  1 
ATOM   2374 O OG1 . THR A 1 353 ? 197.490 217.401 99.744  1.00 104.68 ? 346 THR B OG1 1 
ATOM   2375 C CG2 . THR A 1 353 ? 196.043 216.409 101.391 1.00 96.15  ? 346 THR B CG2 1 
ATOM   2376 N N   . ASP A 1 354 ? 196.987 216.008 96.879  1.00 111.72 ? 347 ASP B N   1 
ATOM   2377 C CA  . ASP A 1 354 ? 197.375 216.528 95.573  1.00 119.25 ? 347 ASP B CA  1 
ATOM   2378 C C   . ASP A 1 354 ? 196.329 216.158 94.530  1.00 121.23 ? 347 ASP B C   1 
ATOM   2379 O O   . ASP A 1 354 ? 196.052 214.966 94.341  1.00 119.34 ? 347 ASP B O   1 
ATOM   2380 C CB  . ASP A 1 354 ? 198.743 215.986 95.171  1.00 122.90 ? 347 ASP B CB  1 
ATOM   2381 C CG  . ASP A 1 354 ? 199.431 216.851 94.132  1.00 127.55 ? 347 ASP B CG  1 
ATOM   2382 O OD1 . ASP A 1 354 ? 198.851 217.052 93.044  1.00 129.59 ? 347 ASP B OD1 1 
ATOM   2383 O OD2 . ASP A 1 354 ? 200.550 217.333 94.404  1.00 125.58 ? 347 ASP B OD2 1 
ATOM   2384 N N   . PRO A 1 355 ? 195.722 217.129 93.841  1.00 123.56 ? 348 PRO B N   1 
ATOM   2385 C CA  . PRO A 1 355 ? 194.734 216.783 92.806  1.00 125.57 ? 348 PRO B CA  1 
ATOM   2386 C C   . PRO A 1 355 ? 195.309 215.955 91.672  1.00 125.82 ? 348 PRO B C   1 
ATOM   2387 O O   . PRO A 1 355 ? 194.589 215.131 91.096  1.00 126.01 ? 348 PRO B O   1 
ATOM   2388 C CB  . PRO A 1 355 ? 194.248 218.154 92.312  1.00 122.09 ? 348 PRO B CB  1 
ATOM   2389 C CG  . PRO A 1 355 ? 194.600 219.110 93.407  1.00 123.39 ? 348 PRO B CG  1 
ATOM   2390 C CD  . PRO A 1 355 ? 195.861 218.583 94.014  1.00 120.46 ? 348 PRO B CD  1 
ATOM   2391 N N   . ALA A 1 356 ? 196.584 216.156 91.328  1.00 124.60 ? 349 ALA B N   1 
ATOM   2392 C CA  . ALA A 1 356 ? 197.184 215.392 90.239  1.00 123.84 ? 349 ALA B CA  1 
ATOM   2393 C C   . ALA A 1 356 ? 197.237 213.906 90.567  1.00 127.11 ? 349 ALA B C   1 
ATOM   2394 O O   . ALA A 1 356 ? 196.940 213.063 89.712  1.00 127.21 ? 349 ALA B O   1 
ATOM   2395 C CB  . ALA A 1 356 ? 198.584 215.924 89.932  1.00 119.53 ? 349 ALA B CB  1 
ATOM   2396 N N   . PHE A 1 357 ? 197.612 213.565 91.803  1.00 125.53 ? 350 PHE B N   1 
ATOM   2397 C CA  . PHE A 1 357 ? 197.693 212.160 92.191  1.00 122.91 ? 350 PHE B CA  1 
ATOM   2398 C C   . PHE A 1 357 ? 196.330 211.485 92.120  1.00 123.20 ? 350 PHE B C   1 
ATOM   2399 O O   . PHE A 1 357 ? 196.206 210.374 91.592  1.00 122.04 ? 350 PHE B O   1 
ATOM   2400 C CB  . PHE A 1 357 ? 198.279 212.038 93.598  1.00 117.68 ? 350 PHE B CB  1 
ATOM   2401 C CG  . PHE A 1 357 ? 198.303 210.632 94.123  1.00 116.83 ? 350 PHE B CG  1 
ATOM   2402 C CD1 . PHE A 1 357 ? 199.308 209.756 93.750  1.00 115.76 ? 350 PHE B CD1 1 
ATOM   2403 C CD2 . PHE A 1 357 ? 197.321 210.185 94.991  1.00 112.80 ? 350 PHE B CD2 1 
ATOM   2404 C CE1 . PHE A 1 357 ? 199.332 208.462 94.229  1.00 112.76 ? 350 PHE B CE1 1 
ATOM   2405 C CE2 . PHE A 1 357 ? 197.339 208.892 95.473  1.00 111.14 ? 350 PHE B CE2 1 
ATOM   2406 C CZ  . PHE A 1 357 ? 198.346 208.029 95.092  1.00 110.81 ? 350 PHE B CZ  1 
ATOM   2407 N N   . CYS A 1 358 ? 195.293 212.142 92.644  1.00 122.99 ? 351 CYS B N   1 
ATOM   2408 C CA  . CYS A 1 358 ? 193.958 211.553 92.618  1.00 122.56 ? 351 CYS B CA  1 
ATOM   2409 C C   . CYS A 1 358 ? 193.420 211.463 91.195  1.00 125.88 ? 351 CYS B C   1 
ATOM   2410 O O   . CYS A 1 358 ? 192.754 210.484 90.838  1.00 126.68 ? 351 CYS B O   1 
ATOM   2411 C CB  . CYS A 1 358 ? 193.012 212.358 93.507  1.00 118.76 ? 351 CYS B CB  1 
ATOM   2412 S SG  . CYS A 1 358 ? 193.679 212.735 95.145  1.00 127.50 ? 351 CYS B SG  1 
ATOM   2413 N N   . SER A 1 359 ? 193.692 212.477 90.370  1.00 125.64 ? 352 SER B N   1 
ATOM   2414 C CA  . SER A 1 359 ? 193.255 212.433 88.978  1.00 127.40 ? 352 SER B CA  1 
ATOM   2415 C C   . SER A 1 359 ? 193.928 211.293 88.227  1.00 126.56 ? 352 SER B C   1 
ATOM   2416 O O   . SER A 1 359 ? 193.293 210.619 87.407  1.00 123.47 ? 352 SER B O   1 
ATOM   2417 C CB  . SER A 1 359 ? 193.537 213.771 88.295  1.00 123.78 ? 352 SER B CB  1 
ATOM   2418 O OG  . SER A 1 359 ? 192.657 214.776 88.765  1.00 120.54 ? 352 SER B OG  1 
ATOM   2419 N N   . ALA A 1 360 ? 195.217 211.066 88.487  1.00 127.58 ? 353 ALA B N   1 
ATOM   2420 C CA  . ALA A 1 360 ? 195.890 209.905 87.915  1.00 127.76 ? 353 ALA B CA  1 
ATOM   2421 C C   . ALA A 1 360 ? 195.273 208.611 88.427  1.00 125.94 ? 353 ALA B C   1 
ATOM   2422 O O   . ALA A 1 360 ? 195.099 207.651 87.667  1.00 121.50 ? 353 ALA B O   1 
ATOM   2423 C CB  . ALA A 1 360 ? 197.384 209.953 88.232  1.00 125.80 ? 353 ALA B CB  1 
ATOM   2424 N N   . LEU A 1 361 ? 194.936 208.568 89.712  1.00 126.28 ? 354 LEU B N   1 
ATOM   2425 C CA  . LEU A 1 361 ? 194.296 207.405 90.313  1.00 127.65 ? 354 LEU B CA  1 
ATOM   2426 C C   . LEU A 1 361 ? 192.891 207.205 89.754  1.00 126.22 ? 354 LEU B C   1 
ATOM   2427 O O   . LEU A 1 361 ? 192.708 206.543 88.733  1.00 124.72 ? 354 LEU B O   1 
ATOM   2428 C CB  . LEU A 1 361 ? 194.239 207.554 91.835  1.00 125.22 ? 354 LEU B CB  1 
ATOM   2429 C CG  . LEU A 1 361 ? 195.279 206.782 92.650  1.00 120.10 ? 354 LEU B CG  1 
ATOM   2430 C CD1 . LEU A 1 361 ? 194.872 205.326 92.787  1.00 118.23 ? 354 LEU B CD1 1 
ATOM   2431 C CD2 . LEU A 1 361 ? 196.656 206.900 92.016  1.00 121.44 ? 354 LEU B CD2 1 
ATOM   2432 N N   . GLN A 1 375 ? 180.576 204.364 97.452  1.00 102.22 ? 368 GLN B N   1 
ATOM   2433 C CA  . GLN A 1 375 ? 181.987 204.187 97.770  1.00 105.11 ? 368 GLN B CA  1 
ATOM   2434 C C   . GLN A 1 375 ? 182.141 203.373 99.052  1.00 103.51 ? 368 GLN B C   1 
ATOM   2435 O O   . GLN A 1 375 ? 181.206 203.279 99.846  1.00 102.82 ? 368 GLN B O   1 
ATOM   2436 C CB  . GLN A 1 375 ? 182.680 205.545 97.904  1.00 107.49 ? 368 GLN B CB  1 
ATOM   2437 C CG  . GLN A 1 375 ? 184.168 205.515 97.601  1.00 109.20 ? 368 GLN B CG  1 
ATOM   2438 C CD  . GLN A 1 375 ? 184.460 205.226 96.141  1.00 114.70 ? 368 GLN B CD  1 
ATOM   2439 O OE1 . GLN A 1 375 ? 185.228 204.319 95.816  1.00 109.38 ? 368 GLN B OE1 1 
ATOM   2440 N NE2 . GLN A 1 375 ? 183.852 206.001 95.251  1.00 112.81 ? 368 GLN B NE2 1 
ATOM   2441 N N   . ARG A 1 376 ? 183.322 202.777 99.244  1.00 99.38  ? 369 ARG B N   1 
ATOM   2442 C CA  . ARG A 1 376 ? 183.540 201.924 100.409 1.00 99.24  ? 369 ARG B CA  1 
ATOM   2443 C C   . ARG A 1 376 ? 183.438 202.715 101.707 1.00 100.26 ? 369 ARG B C   1 
ATOM   2444 O O   . ARG A 1 376 ? 182.699 202.330 102.621 1.00 99.46  ? 369 ARG B O   1 
ATOM   2445 C CB  . ARG A 1 376 ? 184.907 201.245 100.320 1.00 88.84  ? 369 ARG B CB  1 
ATOM   2446 C CG  . ARG A 1 376 ? 185.222 200.612 98.982  1.00 76.97  ? 369 ARG B CG  1 
ATOM   2447 C CD  . ARG A 1 376 ? 185.076 199.110 99.054  1.00 59.72  ? 369 ARG B CD  1 
ATOM   2448 N NE  . ARG A 1 376 ? 185.221 198.488 97.745  1.00 60.28  ? 369 ARG B NE  1 
ATOM   2449 C CZ  . ARG A 1 376 ? 186.383 198.167 97.197  1.00 63.64  ? 369 ARG B CZ  1 
ATOM   2450 N NH1 . ARG A 1 376 ? 187.525 198.373 97.830  1.00 63.70  ? 369 ARG B NH1 1 
ATOM   2451 N NH2 . ARG A 1 376 ? 186.400 197.621 95.985  1.00 64.07  ? 369 ARG B NH2 1 
ATOM   2452 N N   . CYS A 1 377 ? 184.174 203.818 101.809 1.00 99.39  ? 370 CYS B N   1 
ATOM   2453 C CA  . CYS A 1 377 ? 184.212 204.634 103.022 1.00 103.10 ? 370 CYS B CA  1 
ATOM   2454 C C   . CYS A 1 377 ? 184.036 206.092 102.634 1.00 107.28 ? 370 CYS B C   1 
ATOM   2455 O O   . CYS A 1 377 ? 185.010 206.846 102.522 1.00 107.30 ? 370 CYS B O   1 
ATOM   2456 C CB  . CYS A 1 377 ? 185.518 204.421 103.792 1.00 98.54  ? 370 CYS B CB  1 
ATOM   2457 S SG  . CYS A 1 377 ? 185.574 205.261 105.391 1.00 109.85 ? 370 CYS B SG  1 
ATOM   2458 N N   . PRO A 1 378 ? 182.795 206.527 102.406 1.00 109.45 ? 371 PRO B N   1 
ATOM   2459 C CA  . PRO A 1 378 ? 182.571 207.936 102.043 1.00 108.14 ? 371 PRO B CA  1 
ATOM   2460 C C   . PRO A 1 378 ? 183.057 208.911 103.098 1.00 107.60 ? 371 PRO B C   1 
ATOM   2461 O O   . PRO A 1 378 ? 183.504 210.012 102.754 1.00 107.78 ? 371 PRO B O   1 
ATOM   2462 C CB  . PRO A 1 378 ? 181.049 208.013 101.858 1.00 103.70 ? 371 PRO B CB  1 
ATOM   2463 C CG  . PRO A 1 378 ? 180.508 206.855 102.636 1.00 100.18 ? 371 PRO B CG  1 
ATOM   2464 C CD  . PRO A 1 378 ? 181.535 205.773 102.519 1.00 106.86 ? 371 PRO B CD  1 
ATOM   2465 N N   . GLN A 1 379 ? 182.989 208.537 104.377 1.00 103.49 ? 372 GLN B N   1 
ATOM   2466 C CA  . GLN A 1 379 ? 183.433 209.427 105.442 1.00 104.14 ? 372 GLN B CA  1 
ATOM   2467 C C   . GLN A 1 379 ? 184.948 209.452 105.588 1.00 107.30 ? 372 GLN B C   1 
ATOM   2468 O O   . GLN A 1 379 ? 185.471 210.278 106.343 1.00 105.32 ? 372 GLN B O   1 
ATOM   2469 C CB  . GLN A 1 379 ? 182.782 209.021 106.763 1.00 99.83  ? 372 GLN B CB  1 
ATOM   2470 C CG  . GLN A 1 379 ? 183.525 207.932 107.514 1.00 104.81 ? 372 GLN B CG  1 
ATOM   2471 C CD  . GLN A 1 379 ? 182.938 206.555 107.276 1.00 101.58 ? 372 GLN B CD  1 
ATOM   2472 O OE1 . GLN A 1 379 ? 181.973 206.399 106.529 1.00 101.09 ? 372 GLN B OE1 1 
ATOM   2473 N NE2 . GLN A 1 379 ? 183.517 205.546 107.917 1.00 91.26  ? 372 GLN B NE2 1 
ATOM   2474 N N   . CYS A 1 380 ? 185.664 208.568 104.892 1.00 109.21 ? 373 CYS B N   1 
ATOM   2475 C CA  . CYS A 1 380 ? 187.120 208.578 104.941 1.00 109.83 ? 373 CYS B CA  1 
ATOM   2476 C C   . CYS A 1 380 ? 187.728 209.719 104.139 1.00 110.29 ? 373 CYS B C   1 
ATOM   2477 O O   . CYS A 1 380 ? 188.893 210.060 104.365 1.00 109.99 ? 373 CYS B O   1 
ATOM   2478 C CB  . CYS A 1 380 ? 187.672 207.244 104.435 1.00 105.97 ? 373 CYS B CB  1 
ATOM   2479 S SG  . CYS A 1 380 ? 187.503 205.864 105.592 1.00 110.72 ? 373 CYS B SG  1 
ATOM   2480 N N   . ASP A 1 381 ? 186.978 210.312 103.210 1.00 110.65 ? 374 ASP B N   1 
ATOM   2481 C CA  . ASP A 1 381 ? 187.508 211.415 102.418 1.00 110.13 ? 374 ASP B CA  1 
ATOM   2482 C C   . ASP A 1 381 ? 187.592 212.698 103.238 1.00 110.01 ? 374 ASP B C   1 
ATOM   2483 O O   . ASP A 1 381 ? 188.577 213.437 103.149 1.00 110.29 ? 374 ASP B O   1 
ATOM   2484 C CB  . ASP A 1 381 ? 186.643 211.628 101.172 1.00 111.60 ? 374 ASP B CB  1 
ATOM   2485 C CG  . ASP A 1 381 ? 186.944 210.627 100.070 1.00 107.85 ? 374 ASP B CG  1 
ATOM   2486 O OD1 . ASP A 1 381 ? 187.554 209.579 100.364 1.00 107.71 ? 374 ASP B OD1 1 
ATOM   2487 O OD2 . ASP A 1 381 ? 186.566 210.890 98.909  1.00 101.02 ? 374 ASP B OD2 1 
ATOM   2488 N N   . CYS A 1 382 ? 186.568 212.979 104.043 1.00 110.90 ? 375 CYS B N   1 
ATOM   2489 C CA  . CYS A 1 382 ? 186.472 214.242 104.776 1.00 107.91 ? 375 CYS B CA  1 
ATOM   2490 C C   . CYS A 1 382 ? 187.087 214.073 106.159 1.00 109.39 ? 375 CYS B C   1 
ATOM   2491 O O   . CYS A 1 382 ? 186.395 214.083 107.177 1.00 110.18 ? 375 CYS B O   1 
ATOM   2492 C CB  . CYS A 1 382 ? 185.021 214.697 104.861 1.00 109.44 ? 375 CYS B CB  1 
ATOM   2493 S SG  . CYS A 1 382 ? 183.824 213.350 105.019 1.00 110.34 ? 375 CYS B SG  1 
ATOM   2494 N N   . ILE A 1 383 ? 188.412 213.925 106.198 1.00 109.88 ? 376 ILE B N   1 
ATOM   2495 C CA  . ILE A 1 383 ? 189.142 213.797 107.454 1.00 110.67 ? 376 ILE B CA  1 
ATOM   2496 C C   . ILE A 1 383 ? 190.428 214.599 107.329 1.00 110.23 ? 376 ILE B C   1 
ATOM   2497 O O   . ILE A 1 383 ? 190.769 215.085 106.248 1.00 106.60 ? 376 ILE B O   1 
ATOM   2498 C CB  . ILE A 1 383 ? 189.437 212.315 107.800 1.00 108.65 ? 376 ILE B CB  1 
ATOM   2499 C CG1 . ILE A 1 383 ? 190.269 211.669 106.696 1.00 101.88 ? 376 ILE B CG1 1 
ATOM   2500 C CG2 . ILE A 1 383 ? 188.155 211.531 108.024 1.00 109.97 ? 376 ILE B CG2 1 
ATOM   2501 C CD1 . ILE A 1 383 ? 190.827 210.333 107.076 1.00 91.57  ? 376 ILE B CD1 1 
ATOM   2502 N N   . THR A 1 384 ? 191.137 214.743 108.443 1.00 112.66 ? 377 THR B N   1 
ATOM   2503 C CA  . THR A 1 384 ? 192.452 215.366 108.477 1.00 111.11 ? 377 THR B CA  1 
ATOM   2504 C C   . THR A 1 384 ? 193.410 214.520 109.309 1.00 106.69 ? 377 THR B C   1 
ATOM   2505 O O   . THR A 1 384 ? 193.019 213.542 109.952 1.00 104.84 ? 377 THR B O   1 
ATOM   2506 C CB  . THR A 1 384 ? 192.370 216.793 109.033 1.00 108.00 ? 377 THR B CB  1 
ATOM   2507 O OG1 . THR A 1 384 ? 191.823 216.764 110.357 1.00 112.84 ? 377 THR B OG1 1 
ATOM   2508 C CG2 . THR A 1 384 ? 191.492 217.663 108.145 1.00 102.57 ? 377 THR B CG2 1 
ATOM   2509 N N   . LEU A 1 385 ? 194.685 214.919 109.289 1.00 103.40 ? 378 LEU B N   1 
ATOM   2510 C CA  . LEU A 1 385 ? 195.717 214.162 109.993 1.00 106.06 ? 378 LEU B CA  1 
ATOM   2511 C C   . LEU A 1 385 ? 195.467 214.149 111.497 1.00 103.05 ? 378 LEU B C   1 
ATOM   2512 O O   . LEU A 1 385 ? 195.833 213.186 112.184 1.00 99.89  ? 378 LEU B O   1 
ATOM   2513 C CB  . LEU A 1 385 ? 197.094 214.752 109.672 1.00 107.21 ? 378 LEU B CB  1 
ATOM   2514 C CG  . LEU A 1 385 ? 198.289 214.498 110.595 1.00 104.79 ? 378 LEU B CG  1 
ATOM   2515 C CD1 . LEU A 1 385 ? 198.573 213.003 110.716 1.00 98.02  ? 378 LEU B CD1 1 
ATOM   2516 C CD2 . LEU A 1 385 ? 199.523 215.243 110.106 1.00 95.47  ? 378 LEU B CD2 1 
ATOM   2517 N N   . GLN A 1 386 ? 194.848 215.208 112.025 1.00 104.29 ? 379 GLN B N   1 
ATOM   2518 C CA  . GLN A 1 386 ? 194.539 215.273 113.447 1.00 103.38 ? 379 GLN B CA  1 
ATOM   2519 C C   . GLN A 1 386 ? 193.542 214.206 113.873 1.00 104.24 ? 379 GLN B C   1 
ATOM   2520 O O   . GLN A 1 386 ? 193.618 213.723 115.007 1.00 96.53  ? 379 GLN B O   1 
ATOM   2521 C CB  . GLN A 1 386 ? 193.997 216.661 113.803 1.00 107.76 ? 379 GLN B CB  1 
ATOM   2522 C CG  . GLN A 1 386 ? 192.869 217.143 112.901 1.00 109.48 ? 379 GLN B CG  1 
ATOM   2523 C CD  . GLN A 1 386 ? 192.266 218.460 113.360 1.00 115.09 ? 379 GLN B CD  1 
ATOM   2524 O OE1 . GLN A 1 386 ? 192.893 219.514 113.255 1.00 116.86 ? 379 GLN B OE1 1 
ATOM   2525 N NE2 . GLN A 1 386 ? 191.042 218.403 113.874 1.00 116.89 ? 379 GLN B NE2 1 
ATOM   2526 N N   . ASN A 1 387 ? 192.611 213.831 112.995 1.00 107.14 ? 380 ASN B N   1 
ATOM   2527 C CA  . ASN A 1 387 ? 191.613 212.824 113.326 1.00 104.91 ? 380 ASN B CA  1 
ATOM   2528 C C   . ASN A 1 387 ? 192.195 211.422 113.434 1.00 100.84 ? 380 ASN B C   1 
ATOM   2529 O O   . ASN A 1 387 ? 191.516 210.527 113.946 1.00 101.47 ? 380 ASN B O   1 
ATOM   2530 C CB  . ASN A 1 387 ? 190.494 212.826 112.282 1.00 105.85 ? 380 ASN B CB  1 
ATOM   2531 C CG  . ASN A 1 387 ? 189.321 213.690 112.690 1.00 114.05 ? 380 ASN B CG  1 
ATOM   2532 O OD1 . ASN A 1 387 ? 188.857 213.628 113.828 1.00 114.03 ? 380 ASN B OD1 1 
ATOM   2533 N ND2 . ASN A 1 387 ? 188.833 214.503 111.757 1.00 119.56 ? 380 ASN B ND2 1 
ATOM   2534 N N   . VAL A 1 388 ? 193.430 211.210 112.974 1.00 100.18 ? 381 VAL B N   1 
ATOM   2535 C CA  . VAL A 1 388 ? 194.021 209.880 112.926 1.00 94.79  ? 381 VAL B CA  1 
ATOM   2536 C C   . VAL A 1 388 ? 195.336 209.788 113.684 1.00 89.30  ? 381 VAL B C   1 
ATOM   2537 O O   . VAL A 1 388 ? 195.792 208.682 113.974 1.00 83.37  ? 381 VAL B O   1 
ATOM   2538 C CB  . VAL A 1 388 ? 194.215 209.416 111.467 1.00 89.02  ? 381 VAL B CB  1 
ATOM   2539 C CG1 . VAL A 1 388 ? 195.498 209.995 110.885 1.00 90.86  ? 381 VAL B CG1 1 
ATOM   2540 C CG2 . VAL A 1 388 ? 194.195 207.903 111.373 1.00 77.53  ? 381 VAL B CG2 1 
ATOM   2541 N N   . SER A 1 389 ? 195.964 210.916 114.026 1.00 96.67  ? 382 SER B N   1 
ATOM   2542 C CA  . SER A 1 389 ? 197.263 210.865 114.689 1.00 95.79  ? 382 SER B CA  1 
ATOM   2543 C C   . SER A 1 389 ? 197.167 210.396 116.136 1.00 90.78  ? 382 SER B C   1 
ATOM   2544 O O   . SER A 1 389 ? 198.202 210.119 116.753 1.00 83.79  ? 382 SER B O   1 
ATOM   2545 C CB  . SER A 1 389 ? 197.936 212.236 114.634 1.00 100.55 ? 382 SER B CB  1 
ATOM   2546 O OG  . SER A 1 389 ? 197.208 213.188 115.387 1.00 103.87 ? 382 SER B OG  1 
ATOM   2547 N N   . ALA A 1 390 ? 195.958 210.310 116.694 1.00 95.02  ? 383 ALA B N   1 
ATOM   2548 C CA  . ALA A 1 390 ? 195.810 209.869 118.078 1.00 93.71  ? 383 ALA B CA  1 
ATOM   2549 C C   . ALA A 1 390 ? 196.245 208.420 118.255 1.00 94.28  ? 383 ALA B C   1 
ATOM   2550 O O   . ALA A 1 390 ? 196.932 208.088 119.228 1.00 91.33  ? 383 ALA B O   1 
ATOM   2551 C CB  . ALA A 1 390 ? 194.363 210.052 118.534 1.00 87.17  ? 383 ALA B CB  1 
ATOM   2552 N N   . GLY A 1 391 ? 195.860 207.544 117.330 1.00 89.87  ? 384 GLY B N   1 
ATOM   2553 C CA  . GLY A 1 391 ? 196.162 206.131 117.448 1.00 83.16  ? 384 GLY B CA  1 
ATOM   2554 C C   . GLY A 1 391 ? 197.283 205.659 116.546 1.00 82.11  ? 384 GLY B C   1 
ATOM   2555 O O   . GLY A 1 391 ? 197.330 204.484 116.169 1.00 80.67  ? 384 GLY B O   1 
ATOM   2556 N N   . LEU A 1 392 ? 198.197 206.567 116.199 1.00 81.97  ? 385 LEU B N   1 
ATOM   2557 C CA  . LEU A 1 392 ? 199.249 206.243 115.241 1.00 76.85  ? 385 LEU B CA  1 
ATOM   2558 C C   . LEU A 1 392 ? 200.128 205.102 115.742 1.00 80.90  ? 385 LEU B C   1 
ATOM   2559 O O   . LEU A 1 392 ? 200.528 204.230 114.963 1.00 79.42  ? 385 LEU B O   1 
ATOM   2560 C CB  . LEU A 1 392 ? 200.087 207.490 114.960 1.00 76.43  ? 385 LEU B CB  1 
ATOM   2561 C CG  . LEU A 1 392 ? 199.727 208.302 113.713 1.00 80.98  ? 385 LEU B CG  1 
ATOM   2562 C CD1 . LEU A 1 392 ? 200.922 209.076 113.198 1.00 77.20  ? 385 LEU B CD1 1 
ATOM   2563 C CD2 . LEU A 1 392 ? 199.187 207.399 112.626 1.00 72.03  ? 385 LEU B CD2 1 
ATOM   2564 N N   . ASN A 1 393 ? 200.435 205.087 117.038 1.00 82.75  ? 386 ASN B N   1 
ATOM   2565 C CA  . ASN A 1 393 ? 201.291 204.053 117.622 1.00 78.96  ? 386 ASN B CA  1 
ATOM   2566 C C   . ASN A 1 393 ? 200.428 202.960 118.255 1.00 74.05  ? 386 ASN B C   1 
ATOM   2567 O O   . ASN A 1 393 ? 200.378 202.778 119.472 1.00 76.36  ? 386 ASN B O   1 
ATOM   2568 C CB  . ASN A 1 393 ? 202.247 204.668 118.634 1.00 80.41  ? 386 ASN B CB  1 
ATOM   2569 C CG  . ASN A 1 393 ? 202.962 205.887 118.091 1.00 85.96  ? 386 ASN B CG  1 
ATOM   2570 O OD1 . ASN A 1 393 ? 202.549 207.021 118.329 1.00 83.76  ? 386 ASN B OD1 1 
ATOM   2571 N ND2 . ASN A 1 393 ? 204.045 205.659 117.357 1.00 83.40  ? 386 ASN B ND2 1 
ATOM   2572 N N   . HIS A 1 394 ? 199.743 202.218 117.391 1.00 71.71  ? 387 HIS B N   1 
ATOM   2573 C CA  . HIS A 1 394 ? 198.866 201.131 117.802 1.00 67.57  ? 387 HIS B CA  1 
ATOM   2574 C C   . HIS A 1 394 ? 199.558 199.794 117.574 1.00 66.89  ? 387 HIS B C   1 
ATOM   2575 O O   . HIS A 1 394 ? 200.267 199.613 116.580 1.00 71.68  ? 387 HIS B O   1 
ATOM   2576 C CB  . HIS A 1 394 ? 197.541 201.174 117.037 1.00 69.65  ? 387 HIS B CB  1 
ATOM   2577 C CG  . HIS A 1 394 ? 196.426 200.439 117.714 1.00 70.44  ? 387 HIS B CG  1 
ATOM   2578 N ND1 . HIS A 1 394 ? 196.597 199.752 118.896 1.00 71.92  ? 387 HIS B ND1 1 
ATOM   2579 C CD2 . HIS A 1 394 ? 195.126 200.283 117.375 1.00 68.41  ? 387 HIS B CD2 1 
ATOM   2580 C CE1 . HIS A 1 394 ? 195.451 199.203 119.255 1.00 68.80  ? 387 HIS B CE1 1 
ATOM   2581 N NE2 . HIS A 1 394 ? 194.542 199.511 118.349 1.00 68.30  ? 387 HIS B NE2 1 
ATOM   2582 N N   . HIS A 1 395 ? 199.351 198.858 118.502 1.00 66.72  ? 388 HIS B N   1 
ATOM   2583 C CA  . HIS A 1 395 ? 200.024 197.567 118.410 1.00 70.47  ? 388 HIS B CA  1 
ATOM   2584 C C   . HIS A 1 395 ? 199.406 196.686 117.329 1.00 67.57  ? 388 HIS B C   1 
ATOM   2585 O O   . HIS A 1 395 ? 200.098 195.852 116.734 1.00 64.41  ? 388 HIS B O   1 
ATOM   2586 C CB  . HIS A 1 395 ? 199.987 196.857 119.763 1.00 67.50  ? 388 HIS B CB  1 
ATOM   2587 C CG  . HIS A 1 395 ? 198.726 197.092 120.535 1.00 72.98  ? 388 HIS B CG  1 
ATOM   2588 N ND1 . HIS A 1 395 ? 198.505 198.237 121.269 1.00 77.49  ? 388 HIS B ND1 1 
ATOM   2589 C CD2 . HIS A 1 395 ? 197.624 196.323 120.696 1.00 74.52  ? 388 HIS B CD2 1 
ATOM   2590 C CE1 . HIS A 1 395 ? 197.317 198.167 121.842 1.00 80.94  ? 388 HIS B CE1 1 
ATOM   2591 N NE2 . HIS A 1 395 ? 196.762 197.015 121.511 1.00 82.81  ? 388 HIS B NE2 1 
ATOM   2592 N N   . GLN A 1 396 ? 198.107 196.847 117.065 1.00 62.31  ? 389 GLN B N   1 
ATOM   2593 C CA  . GLN A 1 396 ? 197.434 195.998 116.088 1.00 55.87  ? 389 GLN B CA  1 
ATOM   2594 C C   . GLN A 1 396 ? 197.867 196.292 114.659 1.00 56.25  ? 389 GLN B C   1 
ATOM   2595 O O   . GLN A 1 396 ? 197.568 195.499 113.757 1.00 56.09  ? 389 GLN B O   1 
ATOM   2596 C CB  . GLN A 1 396 ? 195.919 196.148 116.212 1.00 59.64  ? 389 GLN B CB  1 
ATOM   2597 C CG  . GLN A 1 396 ? 195.371 195.796 117.582 1.00 63.35  ? 389 GLN B CG  1 
ATOM   2598 C CD  . GLN A 1 396 ? 195.228 194.304 117.782 1.00 67.91  ? 389 GLN B CD  1 
ATOM   2599 O OE1 . GLN A 1 396 ? 195.096 193.550 116.821 1.00 61.06  ? 389 GLN B OE1 1 
ATOM   2600 N NE2 . GLN A 1 396 ? 195.255 193.868 119.034 1.00 68.41  ? 389 GLN B NE2 1 
ATOM   2601 N N   . THR A 1 397 ? 198.548 197.414 114.423 1.00 52.32  ? 390 THR B N   1 
ATOM   2602 C CA  . THR A 1 397 ? 199.085 197.666 113.092 1.00 51.56  ? 390 THR B CA  1 
ATOM   2603 C C   . THR A 1 397 ? 200.124 196.617 112.723 1.00 51.24  ? 390 THR B C   1 
ATOM   2604 O O   . THR A 1 397 ? 200.168 196.149 111.579 1.00 51.73  ? 390 THR B O   1 
ATOM   2605 C CB  . THR A 1 397 ? 199.679 199.071 113.015 1.00 56.68  ? 390 THR B CB  1 
ATOM   2606 O OG1 . THR A 1 397 ? 200.841 199.149 113.850 1.00 66.19  ? 390 THR B OG1 1 
ATOM   2607 C CG2 . THR A 1 397 ? 198.659 200.096 113.472 1.00 55.47  ? 390 THR B CG2 1 
ATOM   2608 N N   . PHE A 1 398 ? 200.956 196.217 113.688 1.00 50.12  ? 391 PHE B N   1 
ATOM   2609 C CA  . PHE A 1 398 ? 201.898 195.134 113.433 1.00 43.86  ? 391 PHE B CA  1 
ATOM   2610 C C   . PHE A 1 398 ? 201.173 193.821 113.191 1.00 42.97  ? 391 PHE B C   1 
ATOM   2611 O O   . PHE A 1 398 ? 201.630 192.999 112.396 1.00 49.12  ? 391 PHE B O   1 
ATOM   2612 C CB  . PHE A 1 398 ? 202.886 194.987 114.587 1.00 49.48  ? 391 PHE B CB  1 
ATOM   2613 C CG  . PHE A 1 398 ? 203.863 193.860 114.396 1.00 49.27  ? 391 PHE B CG  1 
ATOM   2614 C CD1 . PHE A 1 398 ? 204.997 194.034 113.624 1.00 52.94  ? 391 PHE B CD1 1 
ATOM   2615 C CD2 . PHE A 1 398 ? 203.645 192.625 114.984 1.00 46.84  ? 391 PHE B CD2 1 
ATOM   2616 C CE1 . PHE A 1 398 ? 205.892 193.000 113.441 1.00 54.16  ? 391 PHE B CE1 1 
ATOM   2617 C CE2 . PHE A 1 398 ? 204.538 191.589 114.804 1.00 48.19  ? 391 PHE B CE2 1 
ATOM   2618 C CZ  . PHE A 1 398 ? 205.662 191.778 114.033 1.00 50.95  ? 391 PHE B CZ  1 
ATOM   2619 N N   . SER A 1 399 ? 200.048 193.596 113.872 1.00 43.65  ? 392 SER B N   1 
ATOM   2620 C CA  . SER A 1 399 ? 199.284 192.375 113.636 1.00 39.99  ? 392 SER B CA  1 
ATOM   2621 C C   . SER A 1 399 ? 198.727 192.330 112.217 1.00 39.84  ? 392 SER B C   1 
ATOM   2622 O O   . SER A 1 399 ? 198.796 191.294 111.548 1.00 45.97  ? 392 SER B O   1 
ATOM   2623 C CB  . SER A 1 399 ? 198.159 192.258 114.661 1.00 41.89  ? 392 SER B CB  1 
ATOM   2624 O OG  . SER A 1 399 ? 198.678 191.965 115.944 1.00 50.63  ? 392 SER B OG  1 
ATOM   2625 N N   . VAL A 1 400 ? 198.178 193.448 111.740 1.00 36.15  ? 393 VAL B N   1 
ATOM   2626 C CA  . VAL A 1 400 ? 197.671 193.508 110.368 1.00 33.39  ? 393 VAL B CA  1 
ATOM   2627 C C   . VAL A 1 400 ? 198.807 193.317 109.369 1.00 36.21  ? 393 VAL B C   1 
ATOM   2628 O O   . VAL A 1 400 ? 198.690 192.560 108.392 1.00 43.95  ? 393 VAL B O   1 
ATOM   2629 C CB  . VAL A 1 400 ? 196.938 194.840 110.130 1.00 28.46  ? 393 VAL B CB  1 
ATOM   2630 C CG1 . VAL A 1 400 ? 196.438 194.918 108.710 1.00 31.25  ? 393 VAL B CG1 1 
ATOM   2631 C CG2 . VAL A 1 400 ? 195.799 195.008 111.110 1.00 30.75  ? 393 VAL B CG2 1 
ATOM   2632 N N   . TYR A 1 401 ? 199.924 194.005 109.604 1.00 34.20  ? 394 TYR B N   1 
ATOM   2633 C CA  . TYR A 1 401 ? 201.090 193.918 108.735 1.00 38.32  ? 394 TYR B CA  1 
ATOM   2634 C C   . TYR A 1 401 ? 201.639 192.493 108.688 1.00 38.12  ? 394 TYR B C   1 
ATOM   2635 O O   . TYR A 1 401 ? 201.983 191.981 107.615 1.00 44.27  ? 394 TYR B O   1 
ATOM   2636 C CB  . TYR A 1 401 ? 202.111 194.936 109.254 1.00 42.97  ? 394 TYR B CB  1 
ATOM   2637 C CG  . TYR A 1 401 ? 203.503 194.945 108.685 1.00 38.63  ? 394 TYR B CG  1 
ATOM   2638 C CD1 . TYR A 1 401 ? 203.829 195.738 107.596 1.00 40.72  ? 394 TYR B CD1 1 
ATOM   2639 C CD2 . TYR A 1 401 ? 204.513 194.226 109.294 1.00 45.10  ? 394 TYR B CD2 1 
ATOM   2640 C CE1 . TYR A 1 401 ? 205.114 195.771 107.102 1.00 50.28  ? 394 TYR B CE1 1 
ATOM   2641 C CE2 . TYR A 1 401 ? 205.794 194.251 108.810 1.00 53.63  ? 394 TYR B CE2 1 
ATOM   2642 C CZ  . TYR A 1 401 ? 206.093 195.020 107.717 1.00 55.32  ? 394 TYR B CZ  1 
ATOM   2643 O OH  . TYR A 1 401 ? 207.387 195.027 107.257 1.00 53.16  ? 394 TYR B OH  1 
ATOM   2644 N N   . ALA A 1 402 ? 201.681 191.820 109.839 1.00 36.26  ? 395 ALA B N   1 
ATOM   2645 C CA  . ALA A 1 402 ? 202.156 190.445 109.908 1.00 31.21  ? 395 ALA B CA  1 
ATOM   2646 C C   . ALA A 1 402 ? 201.189 189.474 109.249 1.00 33.06  ? 395 ALA B C   1 
ATOM   2647 O O   . ALA A 1 402 ? 201.626 188.493 108.647 1.00 37.98  ? 395 ALA B O   1 
ATOM   2648 C CB  . ALA A 1 402 ? 202.389 190.045 111.363 1.00 32.43  ? 395 ALA B CB  1 
ATOM   2649 N N   . ALA A 1 403 ? 199.881 189.714 109.360 1.00 34.38  ? 396 ALA B N   1 
ATOM   2650 C CA  . ALA A 1 403 ? 198.920 188.876 108.651 1.00 29.48  ? 396 ALA B CA  1 
ATOM   2651 C C   . ALA A 1 403 ? 199.117 188.976 107.146 1.00 30.20  ? 396 ALA B C   1 
ATOM   2652 O O   . ALA A 1 403 ? 199.118 187.959 106.434 1.00 30.36  ? 396 ALA B O   1 
ATOM   2653 C CB  . ALA A 1 403 ? 197.497 189.278 109.034 1.00 24.94  ? 396 ALA B CB  1 
ATOM   2654 N N   . VAL A 1 404 ? 199.301 190.198 106.644 1.00 30.17  ? 397 VAL B N   1 
ATOM   2655 C CA  . VAL A 1 404 ? 199.533 190.377 105.215 1.00 27.41  ? 397 VAL B CA  1 
ATOM   2656 C C   . VAL A 1 404 ? 200.824 189.687 104.795 1.00 29.42  ? 397 VAL B C   1 
ATOM   2657 O O   . VAL A 1 404 ? 200.882 189.026 103.750 1.00 38.75  ? 397 VAL B O   1 
ATOM   2658 C CB  . VAL A 1 404 ? 199.546 191.874 104.859 1.00 29.91  ? 397 VAL B CB  1 
ATOM   2659 C CG1 . VAL A 1 404 ? 200.044 192.073 103.442 1.00 33.94  ? 397 VAL B CG1 1 
ATOM   2660 C CG2 . VAL A 1 404 ? 198.168 192.463 105.038 1.00 30.45  ? 397 VAL B CG2 1 
ATOM   2661 N N   . TYR A 1 405 ? 201.878 189.820 105.605 1.00 30.84  ? 398 TYR B N   1 
ATOM   2662 C CA  . TYR A 1 405 ? 203.148 189.180 105.270 1.00 32.07  ? 398 TYR B CA  1 
ATOM   2663 C C   . TYR A 1 405 ? 203.042 187.660 105.309 1.00 28.86  ? 398 TYR B C   1 
ATOM   2664 O O   . TYR A 1 405 ? 203.678 186.968 104.508 1.00 30.59  ? 398 TYR B O   1 
ATOM   2665 C CB  . TYR A 1 405 ? 204.247 189.666 106.210 1.00 34.31  ? 398 TYR B CB  1 
ATOM   2666 C CG  . TYR A 1 405 ? 205.241 190.572 105.533 1.00 36.53  ? 398 TYR B CG  1 
ATOM   2667 C CD1 . TYR A 1 405 ? 204.997 191.930 105.408 1.00 37.24  ? 398 TYR B CD1 1 
ATOM   2668 C CD2 . TYR A 1 405 ? 206.413 190.065 105.001 1.00 38.74  ? 398 TYR B CD2 1 
ATOM   2669 C CE1 . TYR A 1 405 ? 205.903 192.760 104.783 1.00 39.17  ? 398 TYR B CE1 1 
ATOM   2670 C CE2 . TYR A 1 405 ? 207.321 190.884 104.374 1.00 47.30  ? 398 TYR B CE2 1 
ATOM   2671 C CZ  . TYR A 1 405 ? 207.062 192.231 104.268 1.00 46.25  ? 398 TYR B CZ  1 
ATOM   2672 O OH  . TYR A 1 405 ? 207.972 193.046 103.641 1.00 51.09  ? 398 TYR B OH  1 
ATOM   2673 N N   . SER A 1 406 ? 202.251 187.121 106.237 1.00 31.00  ? 399 SER B N   1 
ATOM   2674 C CA  . SER A 1 406 ? 202.054 185.677 106.296 1.00 31.49  ? 399 SER B CA  1 
ATOM   2675 C C   . SER A 1 406 ? 201.342 185.168 105.053 1.00 30.75  ? 399 SER B C   1 
ATOM   2676 O O   . SER A 1 406 ? 201.723 184.134 104.492 1.00 34.89  ? 399 SER B O   1 
ATOM   2677 C CB  . SER A 1 406 ? 201.274 185.303 107.553 1.00 30.27  ? 399 SER B CB  1 
ATOM   2678 O OG  . SER A 1 406 ? 199.883 185.279 107.310 1.00 33.26  ? 399 SER B OG  1 
ATOM   2679 N N   . VAL A 1 407 ? 200.307 185.881 104.601 1.00 33.54  ? 400 VAL B N   1 
ATOM   2680 C CA  . VAL A 1 407 ? 199.630 185.466 103.373 1.00 32.85  ? 400 VAL B CA  1 
ATOM   2681 C C   . VAL A 1 407 ? 200.575 185.567 102.183 1.00 33.94  ? 400 VAL B C   1 
ATOM   2682 O O   . VAL A 1 407 ? 200.592 184.691 101.309 1.00 33.49  ? 400 VAL B O   1 
ATOM   2683 C CB  . VAL A 1 407 ? 198.352 186.290 103.144 1.00 26.96  ? 400 VAL B CB  1 
ATOM   2684 C CG1 . VAL A 1 407 ? 197.806 186.012 101.763 1.00 24.55  ? 400 VAL B CG1 1 
ATOM   2685 C CG2 . VAL A 1 407 ? 197.321 185.938 104.174 1.00 31.42  ? 400 VAL B CG2 1 
ATOM   2686 N N   . ALA A 1 408 ? 201.372 186.637 102.125 1.00 29.83  ? 401 ALA B N   1 
ATOM   2687 C CA  . ALA A 1 408 ? 202.318 186.792 101.026 1.00 27.91  ? 401 ALA B CA  1 
ATOM   2688 C C   . ALA A 1 408 ? 203.337 185.662 101.007 1.00 33.34  ? 401 ALA B C   1 
ATOM   2689 O O   . ALA A 1 408 ? 203.656 185.126 99.941  1.00 39.50  ? 401 ALA B O   1 
ATOM   2690 C CB  . ALA A 1 408 ? 203.022 188.141 101.125 1.00 30.25  ? 401 ALA B CB  1 
ATOM   2691 N N   . GLN A 1 409 ? 203.859 185.285 102.175 1.00 35.04  ? 402 GLN B N   1 
ATOM   2692 C CA  . GLN A 1 409 ? 204.828 184.196 102.236 1.00 31.10  ? 402 GLN B CA  1 
ATOM   2693 C C   . GLN A 1 409 ? 204.196 182.863 101.863 1.00 33.60  ? 402 GLN B C   1 
ATOM   2694 O O   . GLN A 1 409 ? 204.815 182.055 101.164 1.00 39.68  ? 402 GLN B O   1 
ATOM   2695 C CB  . GLN A 1 409 ? 205.449 184.115 103.627 1.00 32.26  ? 402 GLN B CB  1 
ATOM   2696 C CG  . GLN A 1 409 ? 206.625 183.169 103.698 1.00 38.42  ? 402 GLN B CG  1 
ATOM   2697 C CD  . GLN A 1 409 ? 207.776 183.616 102.824 1.00 42.70  ? 402 GLN B CD  1 
ATOM   2698 O OE1 . GLN A 1 409 ? 208.280 184.729 102.963 1.00 39.85  ? 402 GLN B OE1 1 
ATOM   2699 N NE2 . GLN A 1 409 ? 208.194 182.751 101.911 1.00 42.61  ? 402 GLN B NE2 1 
ATOM   2700 N N   . ALA A 1 410 ? 202.972 182.608 102.328 1.00 35.98  ? 403 ALA B N   1 
ATOM   2701 C CA  . ALA A 1 410 ? 202.297 181.368 101.964 1.00 29.96  ? 403 ALA B CA  1 
ATOM   2702 C C   . ALA A 1 410 ? 202.059 181.290 100.463 1.00 35.30  ? 403 ALA B C   1 
ATOM   2703 O O   . ALA A 1 410 ? 202.237 180.229 99.854  1.00 43.07  ? 403 ALA B O   1 
ATOM   2704 C CB  . ALA A 1 410 ? 200.980 181.245 102.724 1.00 34.20  ? 403 ALA B CB  1 
ATOM   2705 N N   . LEU A 1 411 ? 201.654 182.404 99.846  1.00 34.63  ? 404 LEU B N   1 
ATOM   2706 C CA  . LEU A 1 411 ? 201.484 182.428 98.397  1.00 31.91  ? 404 LEU B CA  1 
ATOM   2707 C C   . LEU A 1 411 ? 202.810 182.223 97.679  1.00 39.22  ? 404 LEU B C   1 
ATOM   2708 O O   . LEU A 1 411 ? 202.878 181.497 96.681  1.00 46.59  ? 404 LEU B O   1 
ATOM   2709 C CB  . LEU A 1 411 ? 200.843 183.744 97.964  1.00 37.39  ? 404 LEU B CB  1 
ATOM   2710 C CG  . LEU A 1 411 ? 200.787 183.998 96.457  1.00 35.59  ? 404 LEU B CG  1 
ATOM   2711 C CD1 . LEU A 1 411 ? 199.930 182.953 95.773  1.00 38.33  ? 404 LEU B CD1 1 
ATOM   2712 C CD2 . LEU A 1 411 ? 200.271 185.393 96.172  1.00 35.43  ? 404 LEU B CD2 1 
ATOM   2713 N N   . HIS A 1 412 ? 203.876 182.860 98.167  1.00 40.46  ? 405 HIS B N   1 
ATOM   2714 C CA  . HIS A 1 412 ? 205.187 182.703 97.549  1.00 42.45  ? 405 HIS B CA  1 
ATOM   2715 C C   . HIS A 1 412 ? 205.650 181.254 97.612  1.00 49.68  ? 405 HIS B C   1 
ATOM   2716 O O   . HIS A 1 412 ? 206.239 180.736 96.657  1.00 56.40  ? 405 HIS B O   1 
ATOM   2717 C CB  . HIS A 1 412 ? 206.188 183.628 98.242  1.00 40.84  ? 405 HIS B CB  1 
ATOM   2718 C CG  . HIS A 1 412 ? 207.607 183.423 97.818  1.00 43.26  ? 405 HIS B CG  1 
ATOM   2719 N ND1 . HIS A 1 412 ? 208.142 184.021 96.699  1.00 54.00  ? 405 HIS B ND1 1 
ATOM   2720 C CD2 . HIS A 1 412 ? 208.605 182.694 98.368  1.00 47.44  ? 405 HIS B CD2 1 
ATOM   2721 C CE1 . HIS A 1 412 ? 209.408 183.667 96.576  1.00 58.05  ? 405 HIS B CE1 1 
ATOM   2722 N NE2 . HIS A 1 412 ? 209.714 182.860 97.575  1.00 52.63  ? 405 HIS B NE2 1 
ATOM   2723 N N   . ASN A 1 413 ? 205.388 180.584 98.735  1.00 44.93  ? 406 ASN B N   1 
ATOM   2724 C CA  . ASN A 1 413 ? 205.739 179.175 98.867  1.00 40.90  ? 406 ASN B CA  1 
ATOM   2725 C C   . ASN A 1 413 ? 204.875 178.301 97.967  1.00 47.58  ? 406 ASN B C   1 
ATOM   2726 O O   . ASN A 1 413 ? 205.364 177.328 97.384  1.00 58.98  ? 406 ASN B O   1 
ATOM   2727 C CB  . ASN A 1 413 ? 205.596 178.744 100.324 1.00 40.83  ? 406 ASN B CB  1 
ATOM   2728 C CG  . ASN A 1 413 ? 206.748 179.208 101.183 1.00 43.54  ? 406 ASN B CG  1 
ATOM   2729 O OD1 . ASN A 1 413 ? 207.658 179.884 100.709 1.00 43.49  ? 406 ASN B OD1 1 
ATOM   2730 N ND2 . ASN A 1 413 ? 206.710 178.856 102.461 1.00 39.68  ? 406 ASN B ND2 1 
ATOM   2731 N N   . THR A 1 414 ? 203.583 178.625 97.852  1.00 47.09  ? 407 THR B N   1 
ATOM   2732 C CA  . THR A 1 414 ? 202.671 177.803 97.061  1.00 47.21  ? 407 THR B CA  1 
ATOM   2733 C C   . THR A 1 414 ? 203.063 177.798 95.589  1.00 51.37  ? 407 THR B C   1 
ATOM   2734 O O   . THR A 1 414 ? 203.097 176.740 94.951  1.00 57.75  ? 407 THR B O   1 
ATOM   2735 C CB  . THR A 1 414 ? 201.237 178.303 97.235  1.00 41.84  ? 407 THR B CB  1 
ATOM   2736 O OG1 . THR A 1 414 ? 200.729 177.865 98.498  1.00 39.50  ? 407 THR B OG1 1 
ATOM   2737 C CG2 . THR A 1 414 ? 200.342 177.771 96.135  1.00 46.94  ? 407 THR B CG2 1 
ATOM   2738 N N   . LEU A 1 415 ? 203.377 178.969 95.037  1.00 52.96  ? 408 LEU B N   1 
ATOM   2739 C CA  . LEU A 1 415 ? 203.821 179.060 93.652  1.00 61.22  ? 408 LEU B CA  1 
ATOM   2740 C C   . LEU A 1 415 ? 205.232 178.532 93.453  1.00 62.43  ? 408 LEU B C   1 
ATOM   2741 O O   . LEU A 1 415 ? 205.675 178.426 92.305  1.00 66.59  ? 408 LEU B O   1 
ATOM   2742 C CB  . LEU A 1 415 ? 203.761 180.508 93.171  1.00 55.62  ? 408 LEU B CB  1 
ATOM   2743 C CG  . LEU A 1 415 ? 202.544 181.354 93.525  1.00 46.95  ? 408 LEU B CG  1 
ATOM   2744 C CD1 . LEU A 1 415 ? 202.729 182.749 92.997  1.00 49.36  ? 408 LEU B CD1 1 
ATOM   2745 C CD2 . LEU A 1 415 ? 201.306 180.747 92.937  1.00 49.68  ? 408 LEU B CD2 1 
ATOM   2746 N N   . GLN A 1 416 ? 205.944 178.215 94.535  1.00 59.41  ? 409 GLN B N   1 
ATOM   2747 C CA  . GLN A 1 416 ? 207.329 177.751 94.468  1.00 69.65  ? 409 GLN B CA  1 
ATOM   2748 C C   . GLN A 1 416 ? 208.214 178.755 93.734  1.00 73.72  ? 409 GLN B C   1 
ATOM   2749 O O   . GLN A 1 416 ? 209.086 178.385 92.946  1.00 76.61  ? 409 GLN B O   1 
ATOM   2750 C CB  . GLN A 1 416 ? 207.419 176.365 93.824  1.00 69.39  ? 409 GLN B CB  1 
ATOM   2751 C CG  . GLN A 1 416 ? 206.576 175.312 94.519  1.00 68.00  ? 409 GLN B CG  1 
ATOM   2752 C CD  . GLN A 1 416 ? 206.742 173.939 93.906  1.00 82.26  ? 409 GLN B CD  1 
ATOM   2753 O OE1 . GLN A 1 416 ? 206.132 173.624 92.885  1.00 85.80  ? 409 GLN B OE1 1 
ATOM   2754 N NE2 . GLN A 1 416 ? 207.576 173.112 94.526  1.00 89.30  ? 409 GLN B NE2 1 
ATOM   2755 N N   . CYS A 1 417 ? 207.986 180.038 93.996  1.00 67.63  ? 410 CYS B N   1 
ATOM   2756 C CA  . CYS A 1 417 ? 208.805 181.080 93.399  1.00 72.12  ? 410 CYS B CA  1 
ATOM   2757 C C   . CYS A 1 417 ? 210.198 181.062 94.020  1.00 76.41  ? 410 CYS B C   1 
ATOM   2758 O O   . CYS A 1 417 ? 210.392 180.605 95.150  1.00 75.35  ? 410 CYS B O   1 
ATOM   2759 C CB  . CYS A 1 417 ? 208.161 182.453 93.609  1.00 67.52  ? 410 CYS B CB  1 
ATOM   2760 S SG  . CYS A 1 417 ? 206.436 182.640 93.061  1.00 76.17  ? 410 CYS B SG  1 
ATOM   2761 N N   . ASN A 1 418 ? 211.177 181.556 93.272  1.00 81.45  ? 411 ASN B N   1 
ATOM   2762 C CA  . ASN A 1 418 ? 212.539 181.701 93.770  1.00 80.35  ? 411 ASN B CA  1 
ATOM   2763 C C   . ASN A 1 418 ? 212.998 183.146 93.582  1.00 85.32  ? 411 ASN B C   1 
ATOM   2764 O O   . ASN A 1 418 ? 212.276 183.985 93.043  1.00 86.99  ? 411 ASN B O   1 
ATOM   2765 C CB  . ASN A 1 418 ? 213.481 180.697 93.094  1.00 85.47  ? 411 ASN B CB  1 
ATOM   2766 C CG  . ASN A 1 418 ? 213.839 181.074 91.667  1.00 91.91  ? 411 ASN B CG  1 
ATOM   2767 O OD1 . ASN A 1 418 ? 214.640 181.974 91.430  1.00 90.44  ? 411 ASN B OD1 1 
ATOM   2768 N ND2 . ASN A 1 418 ? 213.251 180.370 90.707  1.00 94.34  ? 411 ASN B ND2 1 
ATOM   2769 N N   . ALA A 1 419 ? 214.216 183.433 94.048  1.00 88.33  ? 412 ALA B N   1 
ATOM   2770 C CA  . ALA A 1 419 ? 214.677 184.817 94.122  1.00 91.77  ? 412 ALA B CA  1 
ATOM   2771 C C   . ALA A 1 419 ? 214.769 185.462 92.743  1.00 94.86  ? 412 ALA B C   1 
ATOM   2772 O O   . ALA A 1 419 ? 214.342 186.608 92.558  1.00 87.93  ? 412 ALA B O   1 
ATOM   2773 C CB  . ALA A 1 419 ? 216.029 184.880 94.831  1.00 88.50  ? 412 ALA B CB  1 
ATOM   2774 N N   . SER A 1 420 ? 215.332 184.749 91.766  1.00 97.18  ? 413 SER B N   1 
ATOM   2775 C CA  . SER A 1 420 ? 215.496 185.319 90.432  1.00 97.50  ? 413 SER B CA  1 
ATOM   2776 C C   . SER A 1 420 ? 214.155 185.489 89.729  1.00 92.65  ? 413 SER B C   1 
ATOM   2777 O O   . SER A 1 420 ? 213.916 186.505 89.067  1.00 95.31  ? 413 SER B O   1 
ATOM   2778 C CB  . SER A 1 420 ? 216.428 184.440 89.599  1.00 99.79  ? 413 SER B CB  1 
ATOM   2779 O OG  . SER A 1 420 ? 217.632 184.168 90.295  1.00 103.13 ? 413 SER B OG  1 
ATOM   2780 N N   . GLY A 1 421 ? 213.275 184.511 89.864  1.00 88.84  ? 414 GLY B N   1 
ATOM   2781 C CA  . GLY A 1 421 ? 211.990 184.567 89.207  1.00 88.06  ? 414 GLY B CA  1 
ATOM   2782 C C   . GLY A 1 421 ? 211.086 183.493 89.757  1.00 91.14  ? 414 GLY B C   1 
ATOM   2783 O O   . GLY A 1 421 ? 211.441 182.790 90.703  1.00 95.77  ? 414 GLY B O   1 
ATOM   2784 N N   . CYS A 1 422 ? 209.916 183.350 89.146  1.00 90.01  ? 415 CYS B N   1 
ATOM   2785 C CA  . CYS A 1 422 ? 208.931 182.450 89.704  1.00 89.74  ? 415 CYS B CA  1 
ATOM   2786 C C   . CYS A 1 422 ? 208.205 181.711 88.587  1.00 92.97  ? 415 CYS B C   1 
ATOM   2787 O O   . CYS A 1 422 ? 207.838 182.331 87.578  1.00 93.03  ? 415 CYS B O   1 
ATOM   2788 C CB  . CYS A 1 422 ? 207.944 183.241 90.567  1.00 86.27  ? 415 CYS B CB  1 
ATOM   2789 S SG  . CYS A 1 422 ? 206.447 182.398 91.043  1.00 101.45 ? 415 CYS B SG  1 
ATOM   2790 N N   . PRO A 1 423 ? 207.988 180.402 88.716  1.00 93.41  ? 416 PRO B N   1 
ATOM   2791 C CA  . PRO A 1 423 ? 207.439 179.630 87.596  1.00 92.09  ? 416 PRO B CA  1 
ATOM   2792 C C   . PRO A 1 423 ? 206.021 180.044 87.242  1.00 91.86  ? 416 PRO B C   1 
ATOM   2793 O O   . PRO A 1 423 ? 205.247 180.500 88.088  1.00 94.65  ? 416 PRO B O   1 
ATOM   2794 C CB  . PRO A 1 423 ? 207.482 178.186 88.108  1.00 88.17  ? 416 PRO B CB  1 
ATOM   2795 C CG  . PRO A 1 423 ? 207.444 178.313 89.588  1.00 86.50  ? 416 PRO B CG  1 
ATOM   2796 C CD  . PRO A 1 423 ? 208.202 179.568 89.910  1.00 86.73  ? 416 PRO B CD  1 
ATOM   2797 N N   . ALA A 1 424 ? 205.688 179.876 85.965  1.00 88.08  ? 417 ALA B N   1 
ATOM   2798 C CA  . ALA A 1 424 ? 204.381 180.247 85.442  1.00 85.81  ? 417 ALA B CA  1 
ATOM   2799 C C   . ALA A 1 424 ? 203.463 179.032 85.426  1.00 86.83  ? 417 ALA B C   1 
ATOM   2800 O O   . ALA A 1 424 ? 203.821 177.981 84.884  1.00 87.74  ? 417 ALA B O   1 
ATOM   2801 C CB  . ALA A 1 424 ? 204.511 180.832 84.036  1.00 81.60  ? 417 ALA B CB  1 
ATOM   2802 N N   . GLN A 1 425 ? 202.283 179.183 86.017  1.00 82.50  ? 418 GLN B N   1 
ATOM   2803 C CA  . GLN A 1 425 ? 201.305 178.106 86.091  1.00 86.16  ? 418 GLN B CA  1 
ATOM   2804 C C   . GLN A 1 425 ? 199.923 178.731 86.228  1.00 87.57  ? 418 GLN B C   1 
ATOM   2805 O O   . GLN A 1 425 ? 199.782 179.950 86.361  1.00 86.32  ? 418 GLN B O   1 
ATOM   2806 C CB  . GLN A 1 425 ? 201.616 177.154 87.250  1.00 86.11  ? 418 GLN B CB  1 
ATOM   2807 C CG  . GLN A 1 425 ? 201.385 177.750 88.630  1.00 81.03  ? 418 GLN B CG  1 
ATOM   2808 C CD  . GLN A 1 425 ? 202.465 178.734 89.030  1.00 77.75  ? 418 GLN B CD  1 
ATOM   2809 O OE1 . GLN A 1 425 ? 203.405 178.983 88.277  1.00 72.33  ? 418 GLN B OE1 1 
ATOM   2810 N NE2 . GLN A 1 425 ? 202.338 179.298 90.224  1.00 78.80  ? 418 GLN B NE2 1 
ATOM   2811 N N   . ASP A 1 426 ? 198.898 177.883 86.187  1.00 86.98  ? 419 ASP B N   1 
ATOM   2812 C CA  . ASP A 1 426 ? 197.536 178.360 86.344  1.00 83.88  ? 419 ASP B CA  1 
ATOM   2813 C C   . ASP A 1 426 ? 197.350 178.968 87.734  1.00 82.72  ? 419 ASP B C   1 
ATOM   2814 O O   . ASP A 1 426 ? 197.980 178.529 88.700  1.00 81.66  ? 419 ASP B O   1 
ATOM   2815 C CB  . ASP A 1 426 ? 196.540 177.223 86.133  1.00 83.88  ? 419 ASP B CB  1 
ATOM   2816 C CG  . ASP A 1 426 ? 196.546 176.221 87.271  1.00 90.05  ? 419 ASP B CG  1 
ATOM   2817 O OD1 . ASP A 1 426 ? 197.632 175.703 87.606  1.00 87.33  ? 419 ASP B OD1 1 
ATOM   2818 O OD2 . ASP A 1 426 ? 195.463 175.949 87.830  1.00 91.59  ? 419 ASP B OD2 1 
ATOM   2819 N N   . PRO A 1 427 ? 196.507 179.995 87.854  1.00 81.69  ? 420 PRO B N   1 
ATOM   2820 C CA  . PRO A 1 427 ? 196.327 180.652 89.155  1.00 71.88  ? 420 PRO B CA  1 
ATOM   2821 C C   . PRO A 1 427 ? 195.828 179.675 90.206  1.00 69.61  ? 420 PRO B C   1 
ATOM   2822 O O   . PRO A 1 427 ? 195.020 178.788 89.924  1.00 75.31  ? 420 PRO B O   1 
ATOM   2823 C CB  . PRO A 1 427 ? 195.290 181.740 88.861  1.00 68.53  ? 420 PRO B CB  1 
ATOM   2824 C CG  . PRO A 1 427 ? 195.396 181.981 87.396  1.00 74.47  ? 420 PRO B CG  1 
ATOM   2825 C CD  . PRO A 1 427 ? 195.738 180.657 86.789  1.00 81.06  ? 420 PRO B CD  1 
ATOM   2826 N N   . VAL A 1 428 ? 196.319 179.844 91.428  1.00 63.13  ? 421 VAL B N   1 
ATOM   2827 C CA  . VAL A 1 428 ? 195.981 178.933 92.513  1.00 62.06  ? 421 VAL B CA  1 
ATOM   2828 C C   . VAL A 1 428 ? 194.674 179.363 93.161  1.00 60.70  ? 421 VAL B C   1 
ATOM   2829 O O   . VAL A 1 428 ? 194.374 180.557 93.279  1.00 61.08  ? 421 VAL B O   1 
ATOM   2830 C CB  . VAL A 1 428 ? 197.127 178.853 93.537  1.00 58.53  ? 421 VAL B CB  1 
ATOM   2831 C CG1 . VAL A 1 428 ? 198.453 178.758 92.823  1.00 62.66  ? 421 VAL B CG1 1 
ATOM   2832 C CG2 . VAL A 1 428 ? 197.118 180.049 94.470  1.00 49.26  ? 421 VAL B CG2 1 
ATOM   2833 N N   . LYS A 1 429 ? 193.873 178.383 93.535  1.00 55.61  ? 422 LYS B N   1 
ATOM   2834 C CA  . LYS A 1 429 ? 192.660 178.635 94.284  1.00 57.49  ? 422 LYS B CA  1 
ATOM   2835 C C   . LYS A 1 429 ? 193.003 178.950 95.738  1.00 54.86  ? 422 LYS B C   1 
ATOM   2836 O O   . LYS A 1 429 ? 194.087 178.607 96.213  1.00 54.58  ? 422 LYS B O   1 
ATOM   2837 C CB  . LYS A 1 429 ? 191.734 177.427 94.216  1.00 66.40  ? 422 LYS B CB  1 
ATOM   2838 C CG  . LYS A 1 429 ? 190.747 177.459 93.059  1.00 74.53  ? 422 LYS B CG  1 
ATOM   2839 C CD  . LYS A 1 429 ? 191.439 177.194 91.735  1.00 79.43  ? 422 LYS B CD  1 
ATOM   2840 C CE  . LYS A 1 429 ? 191.722 175.714 91.551  1.00 77.50  ? 422 LYS B CE  1 
ATOM   2841 N NZ  . LYS A 1 429 ? 192.666 175.469 90.427  1.00 78.77  ? 422 LYS B NZ  1 
ATOM   2842 N N   . PRO A 1 430 ? 192.102 179.621 96.459  1.00 53.02  ? 423 PRO B N   1 
ATOM   2843 C CA  . PRO A 1 430 ? 192.385 179.918 97.872  1.00 43.20  ? 423 PRO B CA  1 
ATOM   2844 C C   . PRO A 1 430 ? 192.680 178.688 98.713  1.00 47.83  ? 423 PRO B C   1 
ATOM   2845 O O   . PRO A 1 430 ? 193.538 178.750 99.600  1.00 52.13  ? 423 PRO B O   1 
ATOM   2846 C CB  . PRO A 1 430 ? 191.106 180.631 98.328  1.00 39.21  ? 423 PRO B CB  1 
ATOM   2847 C CG  . PRO A 1 430 ? 190.583 181.254 97.101  1.00 44.75  ? 423 PRO B CG  1 
ATOM   2848 C CD  . PRO A 1 430 ? 190.883 180.299 95.991  1.00 49.70  ? 423 PRO B CD  1 
ATOM   2849 N N   . TRP A 1 431 ? 192.006 177.566 98.456  1.00 53.58  ? 424 TRP B N   1 
ATOM   2850 C CA  . TRP A 1 431 ? 192.234 176.371 99.261  1.00 55.59  ? 424 TRP B CA  1 
ATOM   2851 C C   . TRP A 1 431 ? 193.633 175.799 99.069  1.00 55.60  ? 424 TRP B C   1 
ATOM   2852 O O   . TRP A 1 431 ? 194.096 175.034 99.920  1.00 55.31  ? 424 TRP B O   1 
ATOM   2853 C CB  . TRP A 1 431 ? 191.175 175.311 98.946  1.00 54.20  ? 424 TRP B CB  1 
ATOM   2854 C CG  . TRP A 1 431 ? 191.200 174.804 97.537  1.00 60.06  ? 424 TRP B CG  1 
ATOM   2855 C CD1 . TRP A 1 431 ? 190.418 175.225 96.505  1.00 61.05  ? 424 TRP B CD1 1 
ATOM   2856 C CD2 . TRP A 1 431 ? 192.027 173.759 97.013  1.00 63.87  ? 424 TRP B CD2 1 
ATOM   2857 N NE1 . TRP A 1 431 ? 190.717 174.520 95.367  1.00 59.77  ? 424 TRP B NE1 1 
ATOM   2858 C CE2 . TRP A 1 431 ? 191.702 173.613 95.652  1.00 62.91  ? 424 TRP B CE2 1 
ATOM   2859 C CE3 . TRP A 1 431 ? 193.017 172.937 97.561  1.00 65.88  ? 424 TRP B CE3 1 
ATOM   2860 C CZ2 . TRP A 1 431 ? 192.330 172.680 94.831  1.00 67.72  ? 424 TRP B CZ2 1 
ATOM   2861 C CZ3 . TRP A 1 431 ? 193.641 172.013 96.744  1.00 64.49  ? 424 TRP B CZ3 1 
ATOM   2862 C CH2 . TRP A 1 431 ? 193.295 171.892 95.394  1.00 65.78  ? 424 TRP B CH2 1 
ATOM   2863 N N   . GLN A 1 432 ? 194.315 176.152 97.978  1.00 53.42  ? 425 GLN B N   1 
ATOM   2864 C CA  . GLN A 1 432 ? 195.689 175.710 97.779  1.00 52.55  ? 425 GLN B CA  1 
ATOM   2865 C C   . GLN A 1 432 ? 196.655 176.382 98.743  1.00 52.67  ? 425 GLN B C   1 
ATOM   2866 O O   . GLN A 1 432 ? 197.778 175.898 98.913  1.00 58.32  ? 425 GLN B O   1 
ATOM   2867 C CB  . GLN A 1 432 ? 196.124 175.982 96.341  1.00 52.97  ? 425 GLN B CB  1 
ATOM   2868 C CG  . GLN A 1 432 ? 195.331 175.223 95.300  1.00 55.24  ? 425 GLN B CG  1 
ATOM   2869 C CD  . GLN A 1 432 ? 195.993 175.240 93.941  1.00 63.99  ? 425 GLN B CD  1 
ATOM   2870 O OE1 . GLN A 1 432 ? 197.218 175.295 93.835  1.00 61.97  ? 425 GLN B OE1 1 
ATOM   2871 N NE2 . GLN A 1 432 ? 195.185 175.194 92.890  1.00 69.76  ? 425 GLN B NE2 1 
ATOM   2872 N N   . LEU A 1 433 ? 196.251 177.492 99.363  1.00 48.19  ? 426 LEU B N   1 
ATOM   2873 C CA  . LEU A 1 433 ? 197.115 178.168 100.322 1.00 44.28  ? 426 LEU B CA  1 
ATOM   2874 C C   . LEU A 1 433 ? 197.148 177.447 101.661 1.00 47.63  ? 426 LEU B C   1 
ATOM   2875 O O   . LEU A 1 433 ? 198.147 177.533 102.381 1.00 51.29  ? 426 LEU B O   1 
ATOM   2876 C CB  . LEU A 1 433 ? 196.651 179.607 100.529 1.00 43.32  ? 426 LEU B CB  1 
ATOM   2877 C CG  . LEU A 1 433 ? 197.128 180.678 99.557  1.00 37.89  ? 426 LEU B CG  1 
ATOM   2878 C CD1 . LEU A 1 433 ? 196.879 182.045 100.156 1.00 35.19  ? 426 LEU B CD1 1 
ATOM   2879 C CD2 . LEU A 1 433 ? 198.586 180.487 99.229  1.00 42.47  ? 426 LEU B CD2 1 
ATOM   2880 N N   . LEU A 1 434 ? 196.071 176.741 102.010 1.00 48.86  ? 427 LEU B N   1 
ATOM   2881 C CA  . LEU A 1 434 ? 195.944 176.176 103.350 1.00 51.24  ? 427 LEU B CA  1 
ATOM   2882 C C   . LEU A 1 434 ? 197.041 175.168 103.655 1.00 55.31  ? 427 LEU B C   1 
ATOM   2883 O O   . LEU A 1 434 ? 197.472 175.055 104.807 1.00 56.30  ? 427 LEU B O   1 
ATOM   2884 C CB  . LEU A 1 434 ? 194.575 175.523 103.511 1.00 53.91  ? 427 LEU B CB  1 
ATOM   2885 C CG  . LEU A 1 434 ? 193.383 176.465 103.611 1.00 45.08  ? 427 LEU B CG  1 
ATOM   2886 C CD1 . LEU A 1 434 ? 192.146 175.679 103.989 1.00 48.81  ? 427 LEU B CD1 1 
ATOM   2887 C CD2 . LEU A 1 434 ? 193.661 177.557 104.622 1.00 39.04  ? 427 LEU B CD2 1 
ATOM   2888 N N   . GLU A 1 435 ? 197.495 174.419 102.650 1.00 55.98  ? 428 GLU B N   1 
ATOM   2889 C CA  . GLU A 1 435 ? 198.568 173.458 102.875 1.00 56.81  ? 428 GLU B CA  1 
ATOM   2890 C C   . GLU A 1 435 ? 199.857 174.158 103.282 1.00 58.68  ? 428 GLU B C   1 
ATOM   2891 O O   . GLU A 1 435 ? 200.607 173.654 104.126 1.00 60.66  ? 428 GLU B O   1 
ATOM   2892 C CB  . GLU A 1 435 ? 198.788 172.613 101.622 1.00 65.35  ? 428 GLU B CB  1 
ATOM   2893 C CG  . GLU A 1 435 ? 197.510 172.055 101.019 1.00 74.24  ? 428 GLU B CG  1 
ATOM   2894 C CD  . GLU A 1 435 ? 197.518 172.078 99.503  1.00 81.67  ? 428 GLU B CD  1 
ATOM   2895 O OE1 . GLU A 1 435 ? 198.567 172.416 98.915  1.00 78.84  ? 428 GLU B OE1 1 
ATOM   2896 O OE2 . GLU A 1 435 ? 196.476 171.751 98.898  1.00 81.23  ? 428 GLU B OE2 1 
ATOM   2897 N N   . ASN A 1 436 ? 200.131 175.318 102.692 1.00 50.61  ? 429 ASN B N   1 
ATOM   2898 C CA  . ASN A 1 436 ? 201.351 176.065 102.956 1.00 43.23  ? 429 ASN B CA  1 
ATOM   2899 C C   . ASN A 1 436 ? 201.181 177.142 104.018 1.00 43.81  ? 429 ASN B C   1 
ATOM   2900 O O   . ASN A 1 436 ? 202.154 177.827 104.339 1.00 48.50  ? 429 ASN B O   1 
ATOM   2901 C CB  . ASN A 1 436 ? 201.862 176.693 101.660 1.00 47.56  ? 429 ASN B CB  1 
ATOM   2902 C CG  . ASN A 1 436 ? 202.186 175.658 100.607 1.00 52.75  ? 429 ASN B CG  1 
ATOM   2903 O OD1 . ASN A 1 436 ? 201.369 175.366 99.736  1.00 58.80  ? 429 ASN B OD1 1 
ATOM   2904 N ND2 . ASN A 1 436 ? 203.383 175.093 100.683 1.00 51.36  ? 429 ASN B ND2 1 
ATOM   2905 N N   . MET A 1 437 ? 199.979 177.312 104.568 1.00 42.64  ? 430 MET B N   1 
ATOM   2906 C CA  . MET A 1 437 ? 199.773 178.253 105.661 1.00 41.74  ? 430 MET B CA  1 
ATOM   2907 C C   . MET A 1 437 ? 200.040 177.613 107.016 1.00 45.59  ? 430 MET B C   1 
ATOM   2908 O O   . MET A 1 437 ? 200.631 178.247 107.895 1.00 49.21  ? 430 MET B O   1 
ATOM   2909 C CB  . MET A 1 437 ? 198.352 178.821 105.617 1.00 42.53  ? 430 MET B CB  1 
ATOM   2910 C CG  . MET A 1 437 ? 198.155 179.918 104.584 1.00 41.83  ? 430 MET B CG  1 
ATOM   2911 S SD  . MET A 1 437 ? 198.412 181.571 105.251 1.00 62.33  ? 430 MET B SD  1 
ATOM   2912 C CE  . MET A 1 437 ? 196.780 181.950 105.875 1.00 44.22  ? 430 MET B CE  1 
ATOM   2913 N N   . TYR A 1 438 ? 199.597 176.374 107.208 1.00 47.61  ? 431 TYR B N   1 
ATOM   2914 C CA  . TYR A 1 438 ? 200.024 175.600 108.364 1.00 47.11  ? 431 TYR B CA  1 
ATOM   2915 C C   . TYR A 1 438 ? 201.502 175.268 108.238 1.00 52.86  ? 431 TYR B C   1 
ATOM   2916 O O   . TYR A 1 438 ? 202.024 175.122 107.130 1.00 54.74  ? 431 TYR B O   1 
ATOM   2917 C CB  . TYR A 1 438 ? 199.213 174.312 108.468 1.00 46.60  ? 431 TYR B CB  1 
ATOM   2918 C CG  . TYR A 1 438 ? 197.754 174.511 108.780 1.00 45.92  ? 431 TYR B CG  1 
ATOM   2919 C CD1 . TYR A 1 438 ? 197.347 174.925 110.037 1.00 50.49  ? 431 TYR B CD1 1 
ATOM   2920 C CD2 . TYR A 1 438 ? 196.783 174.281 107.819 1.00 46.74  ? 431 TYR B CD2 1 
ATOM   2921 C CE1 . TYR A 1 438 ? 196.016 175.103 110.330 1.00 52.59  ? 431 TYR B CE1 1 
ATOM   2922 C CE2 . TYR A 1 438 ? 195.447 174.459 108.103 1.00 47.44  ? 431 TYR B CE2 1 
ATOM   2923 C CZ  . TYR A 1 438 ? 195.071 174.869 109.360 1.00 51.45  ? 431 TYR B CZ  1 
ATOM   2924 O OH  . TYR A 1 438 ? 193.744 175.050 109.651 1.00 50.95  ? 431 TYR B OH  1 
ATOM   2925 N N   . ASN A 1 439 ? 202.182 175.152 109.381 1.00 51.22  ? 432 ASN B N   1 
ATOM   2926 C CA  . ASN A 1 439 ? 203.586 174.740 109.404 1.00 61.64  ? 432 ASN B CA  1 
ATOM   2927 C C   . ASN A 1 439 ? 204.457 175.740 108.645 1.00 64.04  ? 432 ASN B C   1 
ATOM   2928 O O   . ASN A 1 439 ? 205.490 175.387 108.075 1.00 74.61  ? 432 ASN B O   1 
ATOM   2929 C CB  . ASN A 1 439 ? 203.734 173.330 108.823 1.00 73.23  ? 432 ASN B CB  1 
ATOM   2930 C CG  . ASN A 1 439 ? 204.959 172.594 109.329 1.00 80.08  ? 432 ASN B CG  1 
ATOM   2931 O OD1 . ASN A 1 439 ? 205.536 171.781 108.607 1.00 79.83  ? 432 ASN B OD1 1 
ATOM   2932 N ND2 . ASN A 1 439 ? 205.357 172.858 110.563 1.00 82.54  ? 432 ASN B ND2 1 
ATOM   2933 N N   . LEU A 1 440 ? 204.032 177.000 108.632 1.00 51.86  ? 433 LEU B N   1 
ATOM   2934 C CA  . LEU A 1 440 ? 204.651 178.035 107.816 1.00 49.80  ? 433 LEU B CA  1 
ATOM   2935 C C   . LEU A 1 440 ? 205.467 178.969 108.694 1.00 49.47  ? 433 LEU B C   1 
ATOM   2936 O O   . LEU A 1 440 ? 204.988 179.418 109.739 1.00 52.37  ? 433 LEU B O   1 
ATOM   2937 C CB  . LEU A 1 440 ? 203.592 178.832 107.051 1.00 44.42  ? 433 LEU B CB  1 
ATOM   2938 C CG  . LEU A 1 440 ? 203.975 180.220 106.539 1.00 38.60  ? 433 LEU B CG  1 
ATOM   2939 C CD1 . LEU A 1 440 ? 204.830 180.108 105.295 1.00 38.70  ? 433 LEU B CD1 1 
ATOM   2940 C CD2 . LEU A 1 440 ? 202.737 181.048 106.265 1.00 37.82  ? 433 LEU B CD2 1 
ATOM   2941 N N   . THR A 1 441 ? 206.693 179.256 108.270 1.00 49.53  ? 434 THR B N   1 
ATOM   2942 C CA  . THR A 1 441 ? 207.551 180.232 108.926 1.00 47.30  ? 434 THR B CA  1 
ATOM   2943 C C   . THR A 1 441 ? 207.664 181.453 108.026 1.00 48.51  ? 434 THR B C   1 
ATOM   2944 O O   . THR A 1 441 ? 208.117 181.346 106.882 1.00 49.22  ? 434 THR B O   1 
ATOM   2945 C CB  . THR A 1 441 ? 208.934 179.652 109.219 1.00 51.01  ? 434 THR B CB  1 
ATOM   2946 O OG1 . THR A 1 441 ? 208.844 178.718 110.301 1.00 61.46  ? 434 THR B OG1 1 
ATOM   2947 C CG2 . THR A 1 441 ? 209.902 180.757 109.600 1.00 48.01  ? 434 THR B CG2 1 
ATOM   2948 N N   . PHE A 1 442 ? 207.251 182.606 108.542 1.00 44.01  ? 435 PHE B N   1 
ATOM   2949 C CA  . PHE A 1 442 ? 207.293 183.863 107.812 1.00 43.91  ? 435 PHE B CA  1 
ATOM   2950 C C   . PHE A 1 442 ? 207.944 184.929 108.676 1.00 48.31  ? 435 PHE B C   1 
ATOM   2951 O O   . PHE A 1 442 ? 207.620 185.065 109.858 1.00 54.07  ? 435 PHE B O   1 
ATOM   2952 C CB  . PHE A 1 442 ? 205.885 184.297 107.376 1.00 40.09  ? 435 PHE B CB  1 
ATOM   2953 C CG  . PHE A 1 442 ? 204.884 184.339 108.495 1.00 34.77  ? 435 PHE B CG  1 
ATOM   2954 C CD1 . PHE A 1 442 ? 204.202 183.196 108.869 1.00 39.78  ? 435 PHE B CD1 1 
ATOM   2955 C CD2 . PHE A 1 442 ? 204.609 185.518 109.157 1.00 34.24  ? 435 PHE B CD2 1 
ATOM   2956 C CE1 . PHE A 1 442 ? 203.281 183.225 109.889 1.00 39.96  ? 435 PHE B CE1 1 
ATOM   2957 C CE2 . PHE A 1 442 ? 203.685 185.551 110.180 1.00 34.92  ? 435 PHE B CE2 1 
ATOM   2958 C CZ  . PHE A 1 442 ? 203.021 184.403 110.546 1.00 36.25  ? 435 PHE B CZ  1 
ATOM   2959 N N   . HIS A 1 443 ? 208.862 185.684 108.083 1.00 48.85  ? 436 HIS B N   1 
ATOM   2960 C CA  . HIS A 1 443 ? 209.640 186.671 108.818 1.00 52.77  ? 436 HIS B CA  1 
ATOM   2961 C C   . HIS A 1 443 ? 209.005 188.045 108.655 1.00 58.74  ? 436 HIS B C   1 
ATOM   2962 O O   . HIS A 1 443 ? 208.851 188.535 107.531 1.00 57.44  ? 436 HIS B O   1 
ATOM   2963 C CB  . HIS A 1 443 ? 211.089 186.678 108.337 1.00 56.98  ? 436 HIS B CB  1 
ATOM   2964 C CG  . HIS A 1 443 ? 211.829 185.416 108.651 1.00 68.58  ? 436 HIS B CG  1 
ATOM   2965 N ND1 . HIS A 1 443 ? 211.500 184.201 108.090 1.00 71.24  ? 436 HIS B ND1 1 
ATOM   2966 C CD2 . HIS A 1 443 ? 212.867 185.176 109.486 1.00 74.31  ? 436 HIS B CD2 1 
ATOM   2967 C CE1 . HIS A 1 443 ? 212.311 183.269 108.557 1.00 71.85  ? 436 HIS B CE1 1 
ATOM   2968 N NE2 . HIS A 1 443 ? 213.150 183.834 109.406 1.00 80.14  ? 436 HIS B NE2 1 
ATOM   2969 N N   . VAL A 1 444 ? 208.642 188.660 109.776 1.00 60.38  ? 437 VAL B N   1 
ATOM   2970 C CA  . VAL A 1 444 ? 207.978 189.957 109.801 1.00 57.79  ? 437 VAL B CA  1 
ATOM   2971 C C   . VAL A 1 444 ? 208.905 190.932 110.511 1.00 66.53  ? 437 VAL B C   1 
ATOM   2972 O O   . VAL A 1 444 ? 209.138 190.808 111.720 1.00 66.14  ? 437 VAL B O   1 
ATOM   2973 C CB  . VAL A 1 444 ? 206.617 189.891 110.504 1.00 51.55  ? 437 VAL B CB  1 
ATOM   2974 C CG1 . VAL A 1 444 ? 205.753 191.052 110.085 1.00 44.79  ? 437 VAL B CG1 1 
ATOM   2975 C CG2 . VAL A 1 444 ? 205.929 188.578 110.202 1.00 49.39  ? 437 VAL B CG2 1 
ATOM   2976 N N   . GLY A 1 445 ? 209.428 191.904 109.768 1.00 62.77  ? 438 GLY B N   1 
ATOM   2977 C CA  . GLY A 1 445 ? 210.299 192.905 110.359 1.00 63.55  ? 438 GLY B CA  1 
ATOM   2978 C C   . GLY A 1 445 ? 211.595 192.355 110.910 1.00 77.02  ? 438 GLY B C   1 
ATOM   2979 O O   . GLY A 1 445 ? 212.161 192.936 111.842 1.00 78.33  ? 438 GLY B O   1 
ATOM   2980 N N   . GLY A 1 446 ? 212.085 191.249 110.356 1.00 78.44  ? 439 GLY B N   1 
ATOM   2981 C CA  . GLY A 1 446 ? 213.310 190.635 110.818 1.00 76.37  ? 439 GLY B CA  1 
ATOM   2982 C C   . GLY A 1 446 ? 213.157 189.646 111.952 1.00 80.34  ? 439 GLY B C   1 
ATOM   2983 O O   . GLY A 1 446 ? 214.153 189.031 112.353 1.00 85.68  ? 439 GLY B O   1 
ATOM   2984 N N   . LEU A 1 447 ? 211.948 189.466 112.481 1.00 79.92  ? 440 LEU B N   1 
ATOM   2985 C CA  . LEU A 1 447 ? 211.704 188.515 113.557 1.00 76.93  ? 440 LEU B CA  1 
ATOM   2986 C C   . LEU A 1 447 ? 210.866 187.361 113.034 1.00 73.24  ? 440 LEU B C   1 
ATOM   2987 O O   . LEU A 1 447 ? 209.790 187.596 112.463 1.00 69.66  ? 440 LEU B O   1 
ATOM   2988 C CB  . LEU A 1 447 ? 211.004 189.194 114.733 1.00 76.26  ? 440 LEU B CB  1 
ATOM   2989 C CG  . LEU A 1 447 ? 211.461 190.620 115.047 1.00 84.66  ? 440 LEU B CG  1 
ATOM   2990 C CD1 . LEU A 1 447 ? 210.549 191.262 116.078 1.00 82.92  ? 440 LEU B CD1 1 
ATOM   2991 C CD2 . LEU A 1 447 ? 212.905 190.624 115.527 1.00 77.31  ? 440 LEU B CD2 1 
ATOM   2992 N N   . PRO A 1 448 ? 211.312 186.117 113.188 1.00 74.90  ? 441 PRO B N   1 
ATOM   2993 C CA  . PRO A 1 448 ? 210.553 184.987 112.644 1.00 62.07  ? 441 PRO B CA  1 
ATOM   2994 C C   . PRO A 1 448 ? 209.240 184.766 113.376 1.00 50.53  ? 441 PRO B C   1 
ATOM   2995 O O   . PRO A 1 448 ? 209.121 185.000 114.580 1.00 60.58  ? 441 PRO B O   1 
ATOM   2996 C CB  . PRO A 1 448 ? 211.500 183.800 112.842 1.00 65.78  ? 441 PRO B CB  1 
ATOM   2997 C CG  . PRO A 1 448 ? 212.336 184.194 114.009 1.00 74.00  ? 441 PRO B CG  1 
ATOM   2998 C CD  . PRO A 1 448 ? 212.520 185.679 113.906 1.00 73.85  ? 441 PRO B CD  1 
ATOM   2999 N N   . LEU A 1 449 ? 208.250 184.297 112.624 1.00 44.32  ? 442 LEU B N   1 
ATOM   3000 C CA  . LEU A 1 449 ? 206.944 183.941 113.156 1.00 38.90  ? 442 LEU B CA  1 
ATOM   3001 C C   . LEU A 1 449 ? 206.514 182.629 112.519 1.00 38.74  ? 442 LEU B C   1 
ATOM   3002 O O   . LEU A 1 449 ? 206.953 182.291 111.419 1.00 44.43  ? 442 LEU B O   1 
ATOM   3003 C CB  . LEU A 1 449 ? 205.911 185.042 112.882 1.00 42.42  ? 442 LEU B CB  1 
ATOM   3004 C CG  . LEU A 1 449 ? 205.795 186.166 113.915 1.00 44.29  ? 442 LEU B CG  1 
ATOM   3005 C CD1 . LEU A 1 449 ? 206.746 187.296 113.579 1.00 51.24  ? 442 LEU B CD1 1 
ATOM   3006 C CD2 . LEU A 1 449 ? 204.380 186.693 113.966 1.00 44.00  ? 442 LEU B CD2 1 
ATOM   3007 N N   . ARG A 1 450 ? 205.663 181.882 113.215 1.00 39.71  ? 443 ARG B N   1 
ATOM   3008 C CA  . ARG A 1 450 ? 205.210 180.590 112.722 1.00 41.87  ? 443 ARG B CA  1 
ATOM   3009 C C   . ARG A 1 450 ? 203.734 180.393 113.028 1.00 41.25  ? 443 ARG B C   1 
ATOM   3010 O O   . ARG A 1 450 ? 203.226 180.899 114.031 1.00 54.16  ? 443 ARG B O   1 
ATOM   3011 C CB  . ARG A 1 450 ? 206.018 179.440 113.334 1.00 49.48  ? 443 ARG B CB  1 
ATOM   3012 C CG  . ARG A 1 450 ? 205.825 178.114 112.621 1.00 56.33  ? 443 ARG B CG  1 
ATOM   3013 C CD  . ARG A 1 450 ? 206.725 177.030 113.172 1.00 57.17  ? 443 ARG B CD  1 
ATOM   3014 N NE  . ARG A 1 450 ? 206.094 175.719 113.087 1.00 65.23  ? 443 ARG B NE  1 
ATOM   3015 C CZ  . ARG A 1 450 ? 205.169 175.274 113.927 1.00 69.24  ? 443 ARG B CZ  1 
ATOM   3016 N NH1 . ARG A 1 450 ? 204.757 176.003 114.950 1.00 67.08  ? 443 ARG B NH1 1 
ATOM   3017 N NH2 . ARG A 1 450 ? 204.646 174.067 113.735 1.00 69.57  ? 443 ARG B NH2 1 
ATOM   3018 N N   . PHE A 1 451 ? 203.055 179.651 112.159 1.00 40.14  ? 444 PHE B N   1 
ATOM   3019 C CA  . PHE A 1 451 ? 201.663 179.273 112.352 1.00 43.75  ? 444 PHE B CA  1 
ATOM   3020 C C   . PHE A 1 451 ? 201.606 177.860 112.918 1.00 50.19  ? 444 PHE B C   1 
ATOM   3021 O O   . PHE A 1 451 ? 202.270 176.954 112.405 1.00 52.15  ? 444 PHE B O   1 
ATOM   3022 C CB  . PHE A 1 451 ? 200.886 179.345 111.036 1.00 44.23  ? 444 PHE B CB  1 
ATOM   3023 C CG  . PHE A 1 451 ? 200.277 180.688 110.760 1.00 43.99  ? 444 PHE B CG  1 
ATOM   3024 C CD1 . PHE A 1 451 ? 199.889 181.518 111.796 1.00 43.16  ? 444 PHE B CD1 1 
ATOM   3025 C CD2 . PHE A 1 451 ? 200.102 181.127 109.460 1.00 37.22  ? 444 PHE B CD2 1 
ATOM   3026 C CE1 . PHE A 1 451 ? 199.332 182.751 111.539 1.00 35.04  ? 444 PHE B CE1 1 
ATOM   3027 C CE2 . PHE A 1 451 ? 199.547 182.360 109.201 1.00 31.67  ? 444 PHE B CE2 1 
ATOM   3028 C CZ  . PHE A 1 451 ? 199.165 183.173 110.243 1.00 31.65  ? 444 PHE B CZ  1 
ATOM   3029 N N   . ASP A 1 452 ? 200.816 177.677 113.970 1.00 53.57  ? 445 ASP B N   1 
ATOM   3030 C CA  . ASP A 1 452 ? 200.688 176.380 114.612 1.00 50.88  ? 445 ASP B CA  1 
ATOM   3031 C C   . ASP A 1 452 ? 199.868 175.432 113.742 1.00 48.71  ? 445 ASP B C   1 
ATOM   3032 O O   . ASP A 1 452 ? 199.362 175.793 112.677 1.00 51.67  ? 445 ASP B O   1 
ATOM   3033 C CB  . ASP A 1 452 ? 200.021 176.523 115.978 1.00 48.19  ? 445 ASP B CB  1 
ATOM   3034 C CG  . ASP A 1 452 ? 200.988 176.937 117.059 1.00 51.56  ? 445 ASP B CG  1 
ATOM   3035 O OD1 . ASP A 1 452 ? 202.081 177.439 116.723 1.00 57.43  ? 445 ASP B OD1 1 
ATOM   3036 O OD2 . ASP A 1 452 ? 200.651 176.771 118.248 1.00 49.18  ? 445 ASP B OD2 1 
ATOM   3037 N N   . SER A 1 453 ? 199.738 174.193 114.218 1.00 51.20  ? 446 SER B N   1 
ATOM   3038 C CA  . SER A 1 453 ? 198.790 173.268 113.610 1.00 56.49  ? 446 SER B CA  1 
ATOM   3039 C C   . SER A 1 453 ? 197.357 173.733 113.822 1.00 59.02  ? 446 SER B C   1 
ATOM   3040 O O   . SER A 1 453 ? 196.454 173.328 113.082 1.00 58.81  ? 446 SER B O   1 
ATOM   3041 C CB  . SER A 1 453 ? 198.983 171.864 114.182 1.00 62.29  ? 446 SER B CB  1 
ATOM   3042 O OG  . SER A 1 453 ? 198.486 170.880 113.294 1.00 70.91  ? 446 SER B OG  1 
ATOM   3043 N N   . SER A 1 454 ? 197.131 174.571 114.828 1.00 58.15  ? 447 SER B N   1 
ATOM   3044 C CA  . SER A 1 454 ? 195.828 175.158 115.097 1.00 55.16  ? 447 SER B CA  1 
ATOM   3045 C C   . SER A 1 454 ? 195.657 176.535 114.470 1.00 53.42  ? 447 SER B C   1 
ATOM   3046 O O   . SER A 1 454 ? 194.630 177.179 114.700 1.00 54.93  ? 447 SER B O   1 
ATOM   3047 C CB  . SER A 1 454 ? 195.596 175.249 116.606 1.00 52.78  ? 447 SER B CB  1 
ATOM   3048 O OG  . SER A 1 454 ? 194.887 174.118 117.079 1.00 61.38  ? 447 SER B OG  1 
ATOM   3049 N N   . GLY A 1 455 ? 196.633 177.006 113.701 1.00 50.01  ? 448 GLY B N   1 
ATOM   3050 C CA  . GLY A 1 455 ? 196.541 178.316 113.095 1.00 43.87  ? 448 GLY B CA  1 
ATOM   3051 C C   . GLY A 1 455 ? 196.890 179.458 114.018 1.00 44.21  ? 448 GLY B C   1 
ATOM   3052 O O   . GLY A 1 455 ? 196.632 180.617 113.678 1.00 39.93  ? 448 GLY B O   1 
ATOM   3053 N N   . ASN A 1 456 ? 197.472 179.168 115.178 1.00 49.67  ? 449 ASN B N   1 
ATOM   3054 C CA  . ASN A 1 456 ? 197.794 180.171 116.179 1.00 43.49  ? 449 ASN B CA  1 
ATOM   3055 C C   . ASN A 1 456 ? 199.240 180.602 116.015 1.00 45.94  ? 449 ASN B C   1 
ATOM   3056 O O   . ASN A 1 456 ? 200.116 179.775 115.756 1.00 48.71  ? 449 ASN B O   1 
ATOM   3057 C CB  . ASN A 1 456 ? 197.588 179.637 117.598 1.00 43.91  ? 449 ASN B CB  1 
ATOM   3058 C CG  . ASN A 1 456 ? 196.141 179.346 117.910 1.00 52.99  ? 449 ASN B CG  1 
ATOM   3059 O OD1 . ASN A 1 456 ? 195.261 180.163 117.662 1.00 50.72  ? 449 ASN B OD1 1 
ATOM   3060 N ND2 . ASN A 1 456 ? 195.886 178.171 118.467 1.00 62.85  ? 449 ASN B ND2 1 
ATOM   3061 N N   . VAL A 1 457 ? 199.484 181.900 116.157 1.00 49.63  ? 450 VAL B N   1 
ATOM   3062 C CA  . VAL A 1 457 ? 200.851 182.390 116.177 1.00 50.44  ? 450 VAL B CA  1 
ATOM   3063 C C   . VAL A 1 457 ? 201.392 182.306 117.600 1.00 62.44  ? 450 VAL B C   1 
ATOM   3064 O O   . VAL A 1 457 ? 200.635 182.194 118.573 1.00 69.47  ? 450 VAL B O   1 
ATOM   3065 C CB  . VAL A 1 457 ? 200.910 183.826 115.628 1.00 46.39  ? 450 VAL B CB  1 
ATOM   3066 C CG1 . VAL A 1 457 ? 200.612 184.826 116.724 1.00 50.65  ? 450 VAL B CG1 1 
ATOM   3067 C CG2 . VAL A 1 457 ? 202.249 184.093 114.988 1.00 49.76  ? 450 VAL B CG2 1 
ATOM   3068 N N   . ASP A 1 458 ? 202.714 182.348 117.730 1.00 63.21  ? 451 ASP B N   1 
ATOM   3069 C CA  . ASP A 1 458 ? 203.376 182.217 119.021 1.00 70.56  ? 451 ASP B CA  1 
ATOM   3070 C C   . ASP A 1 458 ? 204.200 183.464 119.311 1.00 69.93  ? 451 ASP B C   1 
ATOM   3071 O O   . ASP A 1 458 ? 205.032 183.867 118.492 1.00 74.36  ? 451 ASP B O   1 
ATOM   3072 C CB  . ASP A 1 458 ? 204.272 180.978 119.049 1.00 72.54  ? 451 ASP B CB  1 
ATOM   3073 C CG  . ASP A 1 458 ? 204.522 180.469 120.453 1.00 81.67  ? 451 ASP B CG  1 
ATOM   3074 O OD1 . ASP A 1 458 ? 203.983 181.067 121.407 1.00 80.92  ? 451 ASP B OD1 1 
ATOM   3075 O OD2 . ASP A 1 458 ? 205.251 179.467 120.603 1.00 84.57  ? 451 ASP B OD2 1 
ATOM   3076 N N   . MET A 1 459 ? 203.965 184.069 120.474 1.00 62.24  ? 452 MET B N   1 
ATOM   3077 C CA  . MET A 1 459 ? 204.794 185.166 120.952 1.00 64.41  ? 452 MET B CA  1 
ATOM   3078 C C   . MET A 1 459 ? 204.832 185.143 122.470 1.00 61.01  ? 452 MET B C   1 
ATOM   3079 O O   . MET A 1 459 ? 203.936 184.612 123.129 1.00 59.07  ? 452 MET B O   1 
ATOM   3080 C CB  . MET A 1 459 ? 204.304 186.535 120.463 1.00 67.81  ? 452 MET B CB  1 
ATOM   3081 C CG  . MET A 1 459 ? 202.811 186.651 120.254 1.00 62.99  ? 452 MET B CG  1 
ATOM   3082 S SD  . MET A 1 459 ? 202.469 187.797 118.908 1.00 72.42  ? 452 MET B SD  1 
ATOM   3083 C CE  . MET A 1 459 ? 203.279 186.969 117.549 1.00 60.94  ? 452 MET B CE  1 
ATOM   3084 N N   . GLU A 1 460 ? 205.887 185.737 123.015 1.00 61.56  ? 453 GLU B N   1 
ATOM   3085 C CA  . GLU A 1 460 ? 206.084 185.794 124.451 1.00 58.29  ? 453 GLU B CA  1 
ATOM   3086 C C   . GLU A 1 460 ? 205.197 186.865 125.077 1.00 55.66  ? 453 GLU B C   1 
ATOM   3087 O O   . GLU A 1 460 ? 204.603 187.705 124.398 1.00 59.75  ? 453 GLU B O   1 
ATOM   3088 C CB  . GLU A 1 460 ? 207.551 186.057 124.777 1.00 62.02  ? 453 GLU B CB  1 
ATOM   3089 C CG  . GLU A 1 460 ? 208.519 185.404 123.813 1.00 67.52  ? 453 GLU B CG  1 
ATOM   3090 C CD  . GLU A 1 460 ? 209.916 185.286 124.382 1.00 80.57  ? 453 GLU B CD  1 
ATOM   3091 O OE1 . GLU A 1 460 ? 210.260 186.078 125.284 1.00 76.11  ? 453 GLU B OE1 1 
ATOM   3092 O OE2 . GLU A 1 460 ? 210.670 184.399 123.933 1.00 87.34  ? 453 GLU B OE2 1 
ATOM   3093 N N   . TYR A 1 461 ? 205.111 186.821 126.402 1.00 49.54  ? 454 TYR B N   1 
ATOM   3094 C CA  . TYR A 1 461 ? 204.317 187.758 127.174 1.00 43.25  ? 454 TYR B CA  1 
ATOM   3095 C C   . TYR A 1 461 ? 205.205 188.376 128.240 1.00 47.01  ? 454 TYR B C   1 
ATOM   3096 O O   . TYR A 1 461 ? 206.216 187.800 128.644 1.00 53.24  ? 454 TYR B O   1 
ATOM   3097 C CB  . TYR A 1 461 ? 203.111 187.071 127.820 1.00 46.81  ? 454 TYR B CB  1 
ATOM   3098 C CG  . TYR A 1 461 ? 201.854 187.122 126.989 1.00 47.87  ? 454 TYR B CG  1 
ATOM   3099 C CD1 . TYR A 1 461 ? 201.617 186.181 125.997 1.00 47.47  ? 454 TYR B CD1 1 
ATOM   3100 C CD2 . TYR A 1 461 ? 200.901 188.104 127.199 1.00 45.57  ? 454 TYR B CD2 1 
ATOM   3101 C CE1 . TYR A 1 461 ? 200.471 186.224 125.237 1.00 48.67  ? 454 TYR B CE1 1 
ATOM   3102 C CE2 . TYR A 1 461 ? 199.754 188.153 126.444 1.00 53.32  ? 454 TYR B CE2 1 
ATOM   3103 C CZ  . TYR A 1 461 ? 199.543 187.211 125.465 1.00 56.06  ? 454 TYR B CZ  1 
ATOM   3104 O OH  . TYR A 1 461 ? 198.393 187.261 124.714 1.00 58.35  ? 454 TYR B OH  1 
ATOM   3105 N N   . ASP A 1 462 ? 204.824 189.565 128.686 1.00 51.47  ? 455 ASP B N   1 
ATOM   3106 C CA  . ASP A 1 462 ? 205.553 190.287 129.718 1.00 50.17  ? 455 ASP B CA  1 
ATOM   3107 C C   . ASP A 1 462 ? 204.627 190.473 130.909 1.00 47.08  ? 455 ASP B C   1 
ATOM   3108 O O   . ASP A 1 462 ? 203.494 190.934 130.749 1.00 48.30  ? 455 ASP B O   1 
ATOM   3109 C CB  . ASP A 1 462 ? 206.041 191.639 129.196 1.00 59.03  ? 455 ASP B CB  1 
ATOM   3110 C CG  . ASP A 1 462 ? 207.512 191.869 129.460 1.00 67.78  ? 455 ASP B CG  1 
ATOM   3111 O OD1 . ASP A 1 462 ? 207.980 191.539 130.567 1.00 62.40  ? 455 ASP B OD1 1 
ATOM   3112 O OD2 . ASP A 1 462 ? 208.206 192.373 128.553 1.00 70.54  ? 455 ASP B OD2 1 
ATOM   3113 N N   . LEU A 1 463 ? 205.102 190.112 132.096 1.00 43.44  ? 456 LEU B N   1 
ATOM   3114 C CA  . LEU A 1 463 ? 204.324 190.309 133.310 1.00 42.92  ? 456 LEU B CA  1 
ATOM   3115 C C   . LEU A 1 463 ? 204.565 191.720 133.829 1.00 41.01  ? 456 LEU B C   1 
ATOM   3116 O O   . LEU A 1 463 ? 205.700 192.084 134.149 1.00 45.73  ? 456 LEU B O   1 
ATOM   3117 C CB  . LEU A 1 463 ? 204.692 189.266 134.362 1.00 40.55  ? 456 LEU B CB  1 
ATOM   3118 C CG  . LEU A 1 463 ? 204.031 189.416 135.733 1.00 36.55  ? 456 LEU B CG  1 
ATOM   3119 C CD1 . LEU A 1 463 ? 202.575 188.999 135.690 1.00 29.54  ? 456 LEU B CD1 1 
ATOM   3120 C CD2 . LEU A 1 463 ? 204.788 188.619 136.772 1.00 36.35  ? 456 LEU B CD2 1 
ATOM   3121 N N   . LYS A 1 464 ? 203.501 192.514 133.902 1.00 33.08  ? 457 LYS B N   1 
ATOM   3122 C CA  . LYS A 1 464 ? 203.587 193.915 134.273 1.00 45.06  ? 457 LYS B CA  1 
ATOM   3123 C C   . LYS A 1 464 ? 202.754 194.186 135.517 1.00 41.47  ? 457 LYS B C   1 
ATOM   3124 O O   . LYS A 1 464 ? 201.731 193.539 135.752 1.00 42.17  ? 457 LYS B O   1 
ATOM   3125 C CB  . LYS A 1 464 ? 203.110 194.817 133.130 1.00 49.84  ? 457 LYS B CB  1 
ATOM   3126 C CG  . LYS A 1 464 ? 203.335 194.238 131.751 1.00 53.00  ? 457 LYS B CG  1 
ATOM   3127 C CD  . LYS A 1 464 ? 203.831 195.302 130.802 1.00 55.96  ? 457 LYS B CD  1 
ATOM   3128 C CE  . LYS A 1 464 ? 205.316 195.495 130.955 1.00 55.77  ? 457 LYS B CE  1 
ATOM   3129 N NZ  . LYS A 1 464 ? 205.862 196.578 130.095 1.00 65.49  ? 457 LYS B NZ  1 
ATOM   3130 N N   . LEU A 1 465 ? 203.202 195.154 136.310 1.00 35.31  ? 458 LEU B N   1 
ATOM   3131 C CA  . LEU A 1 465 ? 202.472 195.604 137.483 1.00 38.77  ? 458 LEU B CA  1 
ATOM   3132 C C   . LEU A 1 465 ? 202.359 197.122 137.481 1.00 52.11  ? 458 LEU B C   1 
ATOM   3133 O O   . LEU A 1 465 ? 203.199 197.826 136.918 1.00 64.49  ? 458 LEU B O   1 
ATOM   3134 C CB  . LEU A 1 465 ? 203.134 195.105 138.782 1.00 41.29  ? 458 LEU B CB  1 
ATOM   3135 C CG  . LEU A 1 465 ? 204.206 195.935 139.484 1.00 43.18  ? 458 LEU B CG  1 
ATOM   3136 C CD1 . LEU A 1 465 ? 204.680 195.224 140.726 1.00 44.66  ? 458 LEU B CD1 1 
ATOM   3137 C CD2 . LEU A 1 465 ? 205.380 196.144 138.558 1.00 53.66  ? 458 LEU B CD2 1 
ATOM   3138 N N   . TRP A 1 466 ? 201.295 197.616 138.108 1.00 46.21  ? 459 TRP B N   1 
ATOM   3139 C CA  . TRP A 1 466 ? 201.067 199.049 138.243 1.00 46.92  ? 459 TRP B CA  1 
ATOM   3140 C C   . TRP A 1 466 ? 201.855 199.558 139.444 1.00 54.86  ? 459 TRP B C   1 
ATOM   3141 O O   . TRP A 1 466 ? 201.526 199.234 140.590 1.00 60.37  ? 459 TRP B O   1 
ATOM   3142 C CB  . TRP A 1 466 ? 199.576 199.331 138.408 1.00 51.02  ? 459 TRP B CB  1 
ATOM   3143 C CG  . TRP A 1 466 ? 198.749 199.065 137.183 1.00 53.32  ? 459 TRP B CG  1 
ATOM   3144 C CD1 . TRP A 1 466 ? 199.142 198.423 136.048 1.00 50.49  ? 459 TRP B CD1 1 
ATOM   3145 C CD2 . TRP A 1 466 ? 197.380 199.436 136.980 1.00 56.57  ? 459 TRP B CD2 1 
ATOM   3146 N NE1 . TRP A 1 466 ? 198.105 198.373 135.149 1.00 53.50  ? 459 TRP B NE1 1 
ATOM   3147 C CE2 . TRP A 1 466 ? 197.012 198.988 135.698 1.00 53.40  ? 459 TRP B CE2 1 
ATOM   3148 C CE3 . TRP A 1 466 ? 196.431 200.102 137.758 1.00 53.13  ? 459 TRP B CE3 1 
ATOM   3149 C CZ2 . TRP A 1 466 ? 195.738 199.185 135.178 1.00 49.49  ? 459 TRP B CZ2 1 
ATOM   3150 C CZ3 . TRP A 1 466 ? 195.170 200.297 137.241 1.00 53.22  ? 459 TRP B CZ3 1 
ATOM   3151 C CH2 . TRP A 1 466 ? 194.834 199.841 135.963 1.00 51.61  ? 459 TRP B CH2 1 
ATOM   3152 N N   . VAL A 1 467 ? 202.898 200.350 139.192 1.00 56.45  ? 460 VAL B N   1 
ATOM   3153 C CA  . VAL A 1 467 ? 203.660 201.013 140.248 1.00 61.48  ? 460 VAL B CA  1 
ATOM   3154 C C   . VAL A 1 467 ? 203.205 202.463 140.310 1.00 72.00  ? 460 VAL B C   1 
ATOM   3155 O O   . VAL A 1 467 ? 203.207 203.166 139.294 1.00 76.75  ? 460 VAL B O   1 
ATOM   3156 C CB  . VAL A 1 467 ? 205.177 200.936 140.010 1.00 63.93  ? 460 VAL B CB  1 
ATOM   3157 C CG1 . VAL A 1 467 ? 205.914 201.127 141.329 1.00 58.27  ? 460 VAL B CG1 1 
ATOM   3158 C CG2 . VAL A 1 467 ? 205.577 199.631 139.343 1.00 67.11  ? 460 VAL B CG2 1 
ATOM   3159 N N   . TRP A 1 468 ? 202.823 202.917 141.499 1.00 73.20  ? 461 TRP B N   1 
ATOM   3160 C CA  . TRP A 1 468 ? 202.232 204.236 141.670 1.00 74.65  ? 461 TRP B CA  1 
ATOM   3161 C C   . TRP A 1 468 ? 203.279 205.213 142.196 1.00 88.42  ? 461 TRP B C   1 
ATOM   3162 O O   . TRP A 1 468 ? 203.981 204.915 143.167 1.00 89.17  ? 461 TRP B O   1 
ATOM   3163 C CB  . TRP A 1 468 ? 201.050 204.157 142.634 1.00 71.05  ? 461 TRP B CB  1 
ATOM   3164 C CG  . TRP A 1 468 ? 199.915 203.305 142.146 1.00 68.61  ? 461 TRP B CG  1 
ATOM   3165 C CD1 . TRP A 1 468 ? 199.762 201.962 142.335 1.00 69.07  ? 461 TRP B CD1 1 
ATOM   3166 C CD2 . TRP A 1 468 ? 198.760 203.741 141.425 1.00 71.91  ? 461 TRP B CD2 1 
ATOM   3167 N NE1 . TRP A 1 468 ? 198.593 201.533 141.761 1.00 65.11  ? 461 TRP B NE1 1 
ATOM   3168 C CE2 . TRP A 1 468 ? 197.958 202.607 141.196 1.00 67.93  ? 461 TRP B CE2 1 
ATOM   3169 C CE3 . TRP A 1 468 ? 198.330 204.977 140.943 1.00 75.98  ? 461 TRP B CE3 1 
ATOM   3170 C CZ2 . TRP A 1 468 ? 196.753 202.674 140.509 1.00 71.53  ? 461 TRP B CZ2 1 
ATOM   3171 C CZ3 . TRP A 1 468 ? 197.132 205.042 140.265 1.00 71.20  ? 461 TRP B CZ3 1 
ATOM   3172 C CH2 . TRP A 1 468 ? 196.359 203.898 140.050 1.00 69.62  ? 461 TRP B CH2 1 
ATOM   3173 N N   . GLN A 1 469 ? 203.381 206.375 141.552 1.00 93.64  ? 462 GLN B N   1 
ATOM   3174 C CA  . GLN A 1 469 ? 204.313 207.416 141.982 1.00 99.75  ? 462 GLN B CA  1 
ATOM   3175 C C   . GLN A 1 469 ? 203.648 208.759 141.728 1.00 101.18 ? 462 GLN B C   1 
ATOM   3176 O O   . GLN A 1 469 ? 203.618 209.229 140.586 1.00 100.35 ? 462 GLN B O   1 
ATOM   3177 C CB  . GLN A 1 469 ? 205.646 207.315 141.245 1.00 100.14 ? 462 GLN B CB  1 
ATOM   3178 C CG  . GLN A 1 469 ? 206.737 208.217 141.815 1.00 103.63 ? 462 GLN B CG  1 
ATOM   3179 C CD  . GLN A 1 469 ? 206.965 209.476 140.996 1.00 107.22 ? 462 GLN B CD  1 
ATOM   3180 O OE1 . GLN A 1 469 ? 206.390 209.648 139.921 1.00 107.39 ? 462 GLN B OE1 1 
ATOM   3181 N NE2 . GLN A 1 469 ? 207.812 210.365 141.505 1.00 104.49 ? 462 GLN B NE2 1 
ATOM   3182 N N   . GLY A 1 470 ? 203.126 209.371 142.785 1.00 100.97 ? 463 GLY B N   1 
ATOM   3183 C CA  . GLY A 1 470 ? 202.406 210.626 142.641 1.00 101.17 ? 463 GLY B CA  1 
ATOM   3184 C C   . GLY A 1 470 ? 201.116 210.501 141.861 1.00 100.48 ? 463 GLY B C   1 
ATOM   3185 O O   . GLY A 1 470 ? 200.833 211.340 140.997 1.00 99.81  ? 463 GLY B O   1 
ATOM   3186 N N   . SER A 1 471 ? 200.327 209.464 142.146 1.00 97.91  ? 464 SER B N   1 
ATOM   3187 C CA  . SER A 1 471 ? 199.048 209.203 141.486 1.00 95.01  ? 464 SER B CA  1 
ATOM   3188 C C   . SER A 1 471 ? 199.201 208.967 139.987 1.00 91.28  ? 464 SER B C   1 
ATOM   3189 O O   . SER A 1 471 ? 198.263 209.205 139.221 1.00 83.70  ? 464 SER B O   1 
ATOM   3190 C CB  . SER A 1 471 ? 198.044 210.334 141.740 1.00 92.54  ? 464 SER B CB  1 
ATOM   3191 O OG  . SER A 1 471 ? 196.714 209.887 141.539 1.00 93.73  ? 464 SER B OG  1 
ATOM   3192 N N   . VAL A 1 472 ? 200.367 208.501 139.553 1.00 91.79  ? 465 VAL B N   1 
ATOM   3193 C CA  . VAL A 1 472 ? 200.610 208.189 138.146 1.00 90.62  ? 465 VAL B CA  1 
ATOM   3194 C C   . VAL A 1 472 ? 201.046 206.733 138.031 1.00 87.88  ? 465 VAL B C   1 
ATOM   3195 O O   . VAL A 1 472 ? 202.231 206.427 138.223 1.00 90.45  ? 465 VAL B O   1 
ATOM   3196 C CB  . VAL A 1 472 ? 201.661 209.129 137.535 1.00 93.17  ? 465 VAL B CB  1 
ATOM   3197 C CG1 . VAL A 1 472 ? 201.790 208.876 136.043 1.00 85.16  ? 465 VAL B CG1 1 
ATOM   3198 C CG2 . VAL A 1 472 ? 201.299 210.581 137.801 1.00 90.92  ? 465 VAL B CG2 1 
ATOM   3199 N N   . PRO A 1 473 ? 200.137 205.810 137.729 1.00 78.99  ? 466 PRO B N   1 
ATOM   3200 C CA  . PRO A 1 473 ? 200.535 204.405 137.596 1.00 74.50  ? 466 PRO B CA  1 
ATOM   3201 C C   . PRO A 1 473 ? 201.335 204.176 136.325 1.00 75.63  ? 466 PRO B C   1 
ATOM   3202 O O   . PRO A 1 473 ? 201.047 204.745 135.270 1.00 79.73  ? 466 PRO B O   1 
ATOM   3203 C CB  . PRO A 1 473 ? 199.199 203.660 137.550 1.00 70.69  ? 466 PRO B CB  1 
ATOM   3204 C CG  . PRO A 1 473 ? 198.232 204.659 137.017 1.00 71.57  ? 466 PRO B CG  1 
ATOM   3205 C CD  . PRO A 1 473 ? 198.716 206.025 137.414 1.00 77.13  ? 466 PRO B CD  1 
ATOM   3206 N N   . ARG A 1 474 ? 202.350 203.324 136.433 1.00 74.48  ? 467 ARG B N   1 
ATOM   3207 C CA  . ARG A 1 474 ? 203.192 202.994 135.295 1.00 75.85  ? 467 ARG B CA  1 
ATOM   3208 C C   . ARG A 1 474 ? 203.520 201.510 135.328 1.00 74.36  ? 467 ARG B C   1 
ATOM   3209 O O   . ARG A 1 474 ? 203.581 200.894 136.395 1.00 71.76  ? 467 ARG B O   1 
ATOM   3210 C CB  . ARG A 1 474 ? 204.482 203.829 135.282 1.00 79.10  ? 467 ARG B CB  1 
ATOM   3211 C CG  . ARG A 1 474 ? 205.469 203.473 136.378 1.00 82.21  ? 467 ARG B CG  1 
ATOM   3212 C CD  . ARG A 1 474 ? 206.267 204.685 136.833 1.00 96.14  ? 467 ARG B CD  1 
ATOM   3213 N NE  . ARG A 1 474 ? 206.769 205.476 135.716 1.00 103.82 ? 467 ARG B NE  1 
ATOM   3214 C CZ  . ARG A 1 474 ? 206.377 206.712 135.436 1.00 106.47 ? 467 ARG B CZ  1 
ATOM   3215 N NH1 . ARG A 1 474 ? 205.472 207.333 136.173 1.00 102.52 ? 467 ARG B NH1 1 
ATOM   3216 N NH2 . ARG A 1 474 ? 206.908 207.340 134.390 1.00 105.06 ? 467 ARG B NH2 1 
ATOM   3217 N N   . LEU A 1 475 ? 203.723 200.942 134.145 1.00 70.04  ? 468 LEU B N   1 
ATOM   3218 C CA  . LEU A 1 475 ? 204.006 199.521 134.023 1.00 66.47  ? 468 LEU B CA  1 
ATOM   3219 C C   . LEU A 1 475 ? 205.501 199.259 134.148 1.00 69.18  ? 468 LEU B C   1 
ATOM   3220 O O   . LEU A 1 475 ? 206.330 200.018 133.637 1.00 71.46  ? 468 LEU B O   1 
ATOM   3221 C CB  . LEU A 1 475 ? 203.504 198.995 132.681 1.00 65.66  ? 468 LEU B CB  1 
ATOM   3222 C CG  . LEU A 1 475 ? 202.014 199.163 132.385 1.00 65.39  ? 468 LEU B CG  1 
ATOM   3223 C CD1 . LEU A 1 475 ? 201.743 198.894 130.917 1.00 56.60  ? 468 LEU B CD1 1 
ATOM   3224 C CD2 . LEU A 1 475 ? 201.184 198.249 133.257 1.00 64.45  ? 468 LEU B CD2 1 
ATOM   3225 N N   . HIS A 1 476 ? 205.845 198.170 134.831 1.00 60.53  ? 469 HIS B N   1 
ATOM   3226 C CA  . HIS A 1 476 ? 207.236 197.746 134.914 1.00 64.25  ? 469 HIS B CA  1 
ATOM   3227 C C   . HIS A 1 476 ? 207.324 196.242 134.713 1.00 57.63  ? 469 HIS B C   1 
ATOM   3228 O O   . HIS A 1 476 ? 206.398 195.508 135.068 1.00 55.63  ? 469 HIS B O   1 
ATOM   3229 C CB  . HIS A 1 476 ? 207.873 198.150 136.248 1.00 65.63  ? 469 HIS B CB  1 
ATOM   3230 C CG  . HIS A 1 476 ? 208.328 199.579 136.290 1.00 80.63  ? 469 HIS B CG  1 
ATOM   3231 N ND1 . HIS A 1 476 ? 207.798 200.501 137.175 1.00 83.76  ? 469 HIS B ND1 1 
ATOM   3232 C CD2 . HIS A 1 476 ? 209.258 200.243 135.562 1.00 84.89  ? 469 HIS B CD2 1 
ATOM   3233 C CE1 . HIS A 1 476 ? 208.383 201.670 136.989 1.00 83.20  ? 469 HIS B CE1 1 
ATOM   3234 N NE2 . HIS A 1 476 ? 209.271 201.540 136.017 1.00 89.82  ? 469 HIS B NE2 1 
ATOM   3235 N N   . ASP A 1 477 ? 208.436 195.798 134.130 1.00 60.93  ? 470 ASP B N   1 
ATOM   3236 C CA  . ASP A 1 477 ? 208.658 194.387 133.830 1.00 56.07  ? 470 ASP B CA  1 
ATOM   3237 C C   . ASP A 1 477 ? 209.033 193.648 135.106 1.00 54.77  ? 470 ASP B C   1 
ATOM   3238 O O   . ASP A 1 477 ? 210.066 193.936 135.717 1.00 61.07  ? 470 ASP B O   1 
ATOM   3239 C CB  . ASP A 1 477 ? 209.763 194.244 132.788 1.00 65.62  ? 470 ASP B CB  1 
ATOM   3240 C CG  . ASP A 1 477 ? 209.231 194.225 131.375 1.00 69.84  ? 470 ASP B CG  1 
ATOM   3241 O OD1 . ASP A 1 477 ? 207.999 194.246 131.215 1.00 68.57  ? 470 ASP B OD1 1 
ATOM   3242 O OD2 . ASP A 1 477 ? 210.040 194.199 130.425 1.00 67.60  ? 470 ASP B OD2 1 
ATOM   3243 N N   . VAL A 1 478 ? 208.200 192.691 135.512 1.00 52.08  ? 471 VAL B N   1 
ATOM   3244 C CA  . VAL A 1 478 ? 208.478 191.849 136.665 1.00 47.29  ? 471 VAL B CA  1 
ATOM   3245 C C   . VAL A 1 478 ? 208.378 190.369 136.324 1.00 43.33  ? 471 VAL B C   1 
ATOM   3246 O O   . VAL A 1 478 ? 208.305 189.534 137.223 1.00 48.69  ? 471 VAL B O   1 
ATOM   3247 C CB  . VAL A 1 478 ? 207.559 192.199 137.853 1.00 44.13  ? 471 VAL B CB  1 
ATOM   3248 C CG1 . VAL A 1 478 ? 207.917 193.561 138.415 1.00 45.62  ? 471 VAL B CG1 1 
ATOM   3249 C CG2 . VAL A 1 478 ? 206.101 192.153 137.439 1.00 42.44  ? 471 VAL B CG2 1 
ATOM   3250 N N   . GLY A 1 479 ? 208.369 190.029 135.044 1.00 42.74  ? 472 GLY B N   1 
ATOM   3251 C CA  . GLY A 1 479 ? 208.272 188.641 134.641 1.00 47.12  ? 472 GLY B CA  1 
ATOM   3252 C C   . GLY A 1 479 ? 208.244 188.531 133.133 1.00 47.04  ? 472 GLY B C   1 
ATOM   3253 O O   . GLY A 1 479 ? 208.226 189.535 132.415 1.00 55.05  ? 472 GLY B O   1 
ATOM   3254 N N   . ARG A 1 480 ? 208.235 187.285 132.666 1.00 42.54  ? 473 ARG B N   1 
ATOM   3255 C CA  . ARG A 1 480 ? 208.240 186.981 131.240 1.00 47.61  ? 473 ARG B CA  1 
ATOM   3256 C C   . ARG A 1 480 ? 207.725 185.565 131.041 1.00 49.44  ? 473 ARG B C   1 
ATOM   3257 O O   . ARG A 1 480 ? 208.227 184.629 131.668 1.00 57.66  ? 473 ARG B O   1 
ATOM   3258 C CB  . ARG A 1 480 ? 209.644 187.130 130.648 1.00 50.67  ? 473 ARG B CB  1 
ATOM   3259 C CG  . ARG A 1 480 ? 209.795 186.527 129.262 1.00 59.80  ? 473 ARG B CG  1 
ATOM   3260 C CD  . ARG A 1 480 ? 209.721 187.587 128.178 1.00 61.85  ? 473 ARG B CD  1 
ATOM   3261 N NE  . ARG A 1 480 ? 210.684 188.660 128.393 1.00 66.54  ? 473 ARG B NE  1 
ATOM   3262 C CZ  . ARG A 1 480 ? 211.932 188.644 127.945 1.00 70.21  ? 473 ARG B CZ  1 
ATOM   3263 N NH1 . ARG A 1 480 ? 212.398 187.630 127.236 1.00 65.14  ? 473 ARG B NH1 1 
ATOM   3264 N NH2 . ARG A 1 480 ? 212.731 189.673 128.213 1.00 71.19  ? 473 ARG B NH2 1 
ATOM   3265 N N   . PHE A 1 481 ? 206.734 185.407 130.172 1.00 44.86  ? 474 PHE B N   1 
ATOM   3266 C CA  . PHE A 1 481 ? 206.140 184.110 129.884 1.00 45.14  ? 474 PHE B CA  1 
ATOM   3267 C C   . PHE A 1 481 ? 206.438 183.725 128.443 1.00 52.56  ? 474 PHE B C   1 
ATOM   3268 O O   . PHE A 1 481 ? 206.184 184.505 127.523 1.00 60.54  ? 474 PHE B O   1 
ATOM   3269 C CB  . PHE A 1 481 ? 204.631 184.141 130.123 1.00 44.28  ? 474 PHE B CB  1 
ATOM   3270 C CG  . PHE A 1 481 ? 203.959 182.810 129.950 1.00 47.57  ? 474 PHE B CG  1 
ATOM   3271 C CD1 . PHE A 1 481 ? 204.012 181.859 130.952 1.00 47.57  ? 474 PHE B CD1 1 
ATOM   3272 C CD2 . PHE A 1 481 ? 203.271 182.511 128.788 1.00 48.35  ? 474 PHE B CD2 1 
ATOM   3273 C CE1 . PHE A 1 481 ? 203.391 180.639 130.799 1.00 49.40  ? 474 PHE B CE1 1 
ATOM   3274 C CE2 . PHE A 1 481 ? 202.651 181.290 128.630 1.00 45.39  ? 474 PHE B CE2 1 
ATOM   3275 C CZ  . PHE A 1 481 ? 202.712 180.354 129.637 1.00 46.16  ? 474 PHE B CZ  1 
ATOM   3276 N N   . ASN A 1 482 ? 206.976 182.525 128.250 1.00 55.48  ? 475 ASN B N   1 
ATOM   3277 C CA  . ASN A 1 482 ? 207.301 182.003 126.927 1.00 54.16  ? 475 ASN B CA  1 
ATOM   3278 C C   . ASN A 1 482 ? 206.884 180.545 126.824 1.00 53.69  ? 475 ASN B C   1 
ATOM   3279 O O   . ASN A 1 482 ? 207.559 179.725 126.195 1.00 66.95  ? 475 ASN B O   1 
ATOM   3280 C CB  . ASN A 1 482 ? 208.789 182.180 126.618 1.00 66.41  ? 475 ASN B CB  1 
ATOM   3281 C CG  . ASN A 1 482 ? 209.678 181.290 127.467 1.00 70.68  ? 475 ASN B CG  1 
ATOM   3282 O OD1 . ASN A 1 482 ? 209.283 180.833 128.537 1.00 70.38  ? 475 ASN B OD1 1 
ATOM   3283 N ND2 . ASN A 1 482 ? 210.890 181.046 126.994 1.00 79.96  ? 475 ASN B ND2 1 
ATOM   3284 N N   . GLY A 1 483 ? 205.751 180.209 127.430 1.00 52.33  ? 476 GLY B N   1 
ATOM   3285 C CA  . GLY A 1 483 ? 205.357 178.843 127.667 1.00 53.64  ? 476 GLY B CA  1 
ATOM   3286 C C   . GLY A 1 483 ? 205.733 178.335 129.042 1.00 56.95  ? 476 GLY B C   1 
ATOM   3287 O O   . GLY A 1 483 ? 205.140 177.360 129.515 1.00 60.37  ? 476 GLY B O   1 
ATOM   3288 N N   . SER A 1 484 ? 206.697 178.983 129.692 1.00 54.23  ? 477 SER B N   1 
ATOM   3289 C CA  . SER A 1 484 ? 207.047 178.699 131.079 1.00 50.43  ? 477 SER B CA  1 
ATOM   3290 C C   . SER A 1 484 ? 207.287 180.042 131.749 1.00 53.57  ? 477 SER B C   1 
ATOM   3291 O O   . SER A 1 484 ? 208.054 180.860 131.235 1.00 56.76  ? 477 SER B O   1 
ATOM   3292 C CB  . SER A 1 484 ? 208.280 177.806 131.173 1.00 57.01  ? 477 SER B CB  1 
ATOM   3293 O OG  . SER A 1 484 ? 209.348 178.328 130.405 1.00 65.09  ? 477 SER B OG  1 
ATOM   3294 N N   . LEU A 1 485 ? 206.630 180.273 132.880 1.00 54.06  ? 478 LEU B N   1 
ATOM   3295 C CA  . LEU A 1 485 ? 206.699 181.575 133.525 1.00 45.68  ? 478 LEU B CA  1 
ATOM   3296 C C   . LEU A 1 485 ? 208.028 181.761 134.248 1.00 43.04  ? 478 LEU B C   1 
ATOM   3297 O O   . LEU A 1 485 ? 208.558 180.833 134.862 1.00 46.97  ? 478 LEU B O   1 
ATOM   3298 C CB  . LEU A 1 485 ? 205.537 181.739 134.500 1.00 41.55  ? 478 LEU B CB  1 
ATOM   3299 C CG  . LEU A 1 485 ? 205.599 182.931 135.447 1.00 38.23  ? 478 LEU B CG  1 
ATOM   3300 C CD1 . LEU A 1 485 ? 204.948 184.135 134.809 1.00 36.62  ? 478 LEU B CD1 1 
ATOM   3301 C CD2 . LEU A 1 485 ? 204.926 182.591 136.754 1.00 43.38  ? 478 LEU B CD2 1 
ATOM   3302 N N   . ARG A 1 486 ? 208.570 182.974 134.160 1.00 43.60  ? 479 ARG B N   1 
ATOM   3303 C CA  . ARG A 1 486 ? 209.767 183.377 134.884 1.00 44.58  ? 479 ARG B CA  1 
ATOM   3304 C C   . ARG A 1 486 ? 209.522 184.756 135.473 1.00 49.52  ? 479 ARG B C   1 
ATOM   3305 O O   . ARG A 1 486 ? 209.141 185.678 134.749 1.00 50.32  ? 479 ARG B O   1 
ATOM   3306 C CB  . ARG A 1 486 ? 210.988 183.396 133.963 1.00 44.09  ? 479 ARG B CB  1 
ATOM   3307 C CG  . ARG A 1 486 ? 212.218 184.037 134.567 1.00 50.03  ? 479 ARG B CG  1 
ATOM   3308 C CD  . ARG A 1 486 ? 212.914 184.938 133.566 1.00 54.64  ? 479 ARG B CD  1 
ATOM   3309 N NE  . ARG A 1 486 ? 212.505 186.330 133.703 1.00 62.57  ? 479 ARG B NE  1 
ATOM   3310 C CZ  . ARG A 1 486 ? 212.543 187.223 132.724 1.00 66.19  ? 479 ARG B CZ  1 
ATOM   3311 N NH1 . ARG A 1 486 ? 212.951 186.899 131.508 1.00 61.33  ? 479 ARG B NH1 1 
ATOM   3312 N NH2 . ARG A 1 486 ? 212.166 188.474 132.973 1.00 57.60  ? 479 ARG B NH2 1 
ATOM   3313 N N   . THR A 1 487 ? 209.731 184.902 136.779 1.00 50.27  ? 480 THR B N   1 
ATOM   3314 C CA  . THR A 1 487 ? 209.394 186.135 137.473 1.00 48.96  ? 480 THR B CA  1 
ATOM   3315 C C   . THR A 1 487 ? 210.553 186.588 138.347 1.00 50.82  ? 480 THR B C   1 
ATOM   3316 O O   . THR A 1 487 ? 211.416 185.798 138.735 1.00 58.67  ? 480 THR B O   1 
ATOM   3317 C CB  . THR A 1 487 ? 208.141 185.977 138.346 1.00 47.53  ? 480 THR B CB  1 
ATOM   3318 O OG1 . THR A 1 487 ? 208.312 184.866 139.232 1.00 50.78  ? 480 THR B OG1 1 
ATOM   3319 C CG2 . THR A 1 487 ? 206.913 185.744 137.490 1.00 42.24  ? 480 THR B CG2 1 
ATOM   3320 N N   . GLU A 1 488 ? 210.557 187.883 138.649 1.00 46.81  ? 481 GLU B N   1 
ATOM   3321 C CA  . GLU A 1 488 ? 211.462 188.489 139.621 1.00 57.40  ? 481 GLU B CA  1 
ATOM   3322 C C   . GLU A 1 488 ? 210.599 189.104 140.717 1.00 63.09  ? 481 GLU B C   1 
ATOM   3323 O O   . GLU A 1 488 ? 210.226 190.276 140.640 1.00 66.52  ? 481 GLU B O   1 
ATOM   3324 C CB  . GLU A 1 488 ? 212.367 189.528 138.974 1.00 57.25  ? 481 GLU B CB  1 
ATOM   3325 C CG  . GLU A 1 488 ? 212.552 189.350 137.486 1.00 59.13  ? 481 GLU B CG  1 
ATOM   3326 C CD  . GLU A 1 488 ? 213.451 188.180 137.158 1.00 63.44  ? 481 GLU B CD  1 
ATOM   3327 O OE1 . GLU A 1 488 ? 213.180 187.481 136.162 1.00 64.27  ? 481 GLU B OE1 1 
ATOM   3328 O OE2 . GLU A 1 488 ? 214.435 187.960 137.895 1.00 59.73  ? 481 GLU B OE2 1 
ATOM   3329 N N   . ARG A 1 489 ? 210.284 188.313 141.742 1.00 56.66  ? 482 ARG B N   1 
ATOM   3330 C CA  . ARG A 1 489 ? 209.406 188.786 142.802 1.00 60.05  ? 482 ARG B CA  1 
ATOM   3331 C C   . ARG A 1 489 ? 210.112 189.681 143.810 1.00 66.27  ? 482 ARG B C   1 
ATOM   3332 O O   . ARG A 1 489 ? 209.441 190.265 144.668 1.00 64.33  ? 482 ARG B O   1 
ATOM   3333 C CB  . ARG A 1 489 ? 208.766 187.606 143.531 1.00 55.38  ? 482 ARG B CB  1 
ATOM   3334 C CG  . ARG A 1 489 ? 209.739 186.532 143.960 1.00 59.05  ? 482 ARG B CG  1 
ATOM   3335 C CD  . ARG A 1 489 ? 209.047 185.521 144.854 1.00 51.21  ? 482 ARG B CD  1 
ATOM   3336 N NE  . ARG A 1 489 ? 208.514 184.399 144.093 1.00 47.98  ? 482 ARG B NE  1 
ATOM   3337 C CZ  . ARG A 1 489 ? 207.635 183.529 144.566 1.00 47.85  ? 482 ARG B CZ  1 
ATOM   3338 N NH1 . ARG A 1 489 ? 207.179 183.610 145.804 1.00 45.56  ? 482 ARG B NH1 1 
ATOM   3339 N NH2 . ARG A 1 489 ? 207.200 182.553 143.775 1.00 49.75  ? 482 ARG B NH2 1 
ATOM   3340 N N   . LEU A 1 490 ? 211.436 189.802 143.737 1.00 68.29  ? 483 LEU B N   1 
ATOM   3341 C CA  . LEU A 1 490 ? 212.149 190.718 144.616 1.00 69.19  ? 483 LEU B CA  1 
ATOM   3342 C C   . LEU A 1 490 ? 212.019 192.169 144.178 1.00 67.79  ? 483 LEU B C   1 
ATOM   3343 O O   . LEU A 1 490 ? 212.362 193.066 144.955 1.00 74.29  ? 483 LEU B O   1 
ATOM   3344 C CB  . LEU A 1 490 ? 213.632 190.340 144.704 1.00 70.72  ? 483 LEU B CB  1 
ATOM   3345 C CG  . LEU A 1 490 ? 214.009 188.970 145.285 1.00 81.16  ? 483 LEU B CG  1 
ATOM   3346 C CD1 . LEU A 1 490 ? 213.191 188.664 146.535 1.00 64.16  ? 483 LEU B CD1 1 
ATOM   3347 C CD2 . LEU A 1 490 ? 213.896 187.843 144.259 1.00 77.67  ? 483 LEU B CD2 1 
ATOM   3348 N N   . LYS A 1 491 ? 211.532 192.422 142.964 1.00 66.23  ? 484 LYS B N   1 
ATOM   3349 C CA  . LYS A 1 491 ? 211.286 193.778 142.492 1.00 65.99  ? 484 LYS B CA  1 
ATOM   3350 C C   . LYS A 1 491 ? 209.801 194.062 142.317 1.00 64.95  ? 484 LYS B C   1 
ATOM   3351 O O   . LYS A 1 491 ? 209.439 195.067 141.695 1.00 69.05  ? 484 LYS B O   1 
ATOM   3352 C CB  . LYS A 1 491 ? 212.038 194.035 141.183 1.00 65.05  ? 484 LYS B CB  1 
ATOM   3353 C CG  . LYS A 1 491 ? 211.513 193.276 139.981 1.00 65.47  ? 484 LYS B CG  1 
ATOM   3354 C CD  . LYS A 1 491 ? 211.917 193.977 138.699 1.00 64.09  ? 484 LYS B CD  1 
ATOM   3355 C CE  . LYS A 1 491 ? 212.669 193.041 137.772 1.00 62.42  ? 484 LYS B CE  1 
ATOM   3356 N NZ  . LYS A 1 491 ? 213.180 193.752 136.567 1.00 56.55  ? 484 LYS B NZ  1 
ATOM   3357 N N   . ILE A 1 492 ? 208.937 193.205 142.847 1.00 61.27  ? 485 ILE B N   1 
ATOM   3358 C CA  . ILE A 1 492 ? 207.499 193.439 142.854 1.00 53.36  ? 485 ILE B CA  1 
ATOM   3359 C C   . ILE A 1 492 ? 207.152 194.171 144.141 1.00 57.25  ? 485 ILE B C   1 
ATOM   3360 O O   . ILE A 1 492 ? 207.463 193.695 145.238 1.00 65.02  ? 485 ILE B O   1 
ATOM   3361 C CB  . ILE A 1 492 ? 206.722 192.120 142.741 1.00 52.17  ? 485 ILE B CB  1 
ATOM   3362 C CG1 . ILE A 1 492 ? 207.074 191.404 141.439 1.00 52.12  ? 485 ILE B CG1 1 
ATOM   3363 C CG2 . ILE A 1 492 ? 205.229 192.375 142.818 1.00 44.68  ? 485 ILE B CG2 1 
ATOM   3364 C CD1 . ILE A 1 492 ? 206.198 190.219 141.140 1.00 45.33  ? 485 ILE B CD1 1 
ATOM   3365 N N   . ARG A 1 493 ? 206.519 195.333 144.013 1.00 56.16  ? 486 ARG B N   1 
ATOM   3366 C CA  . ARG A 1 493 ? 206.139 196.138 145.167 1.00 57.87  ? 486 ARG B CA  1 
ATOM   3367 C C   . ARG A 1 493 ? 204.671 195.865 145.467 1.00 58.12  ? 486 ARG B C   1 
ATOM   3368 O O   . ARG A 1 493 ? 203.798 196.156 144.643 1.00 56.14  ? 486 ARG B O   1 
ATOM   3369 C CB  . ARG A 1 493 ? 206.393 197.618 144.892 1.00 57.70  ? 486 ARG B CB  1 
ATOM   3370 C CG  . ARG A 1 493 ? 205.725 198.577 145.857 1.00 65.71  ? 486 ARG B CG  1 
ATOM   3371 C CD  . ARG A 1 493 ? 206.537 198.705 147.142 1.00 69.50  ? 486 ARG B CD  1 
ATOM   3372 N NE  . ARG A 1 493 ? 206.331 199.972 147.838 1.00 80.68  ? 486 ARG B NE  1 
ATOM   3373 C CZ  . ARG A 1 493 ? 205.172 200.406 148.318 1.00 86.22  ? 486 ARG B CZ  1 
ATOM   3374 N NH1 . ARG A 1 493 ? 204.073 199.671 148.257 1.00 77.88  ? 486 ARG B NH1 1 
ATOM   3375 N NH2 . ARG A 1 493 ? 205.118 201.606 148.890 1.00 84.88  ? 486 ARG B NH2 1 
ATOM   3376 N N   . TRP A 1 494 ? 204.397 195.303 146.639 1.00 54.09  ? 487 TRP B N   1 
ATOM   3377 C CA  . TRP A 1 494 ? 203.047 194.896 146.987 1.00 47.94  ? 487 TRP B CA  1 
ATOM   3378 C C   . TRP A 1 494 ? 202.325 196.015 147.730 1.00 53.86  ? 487 TRP B C   1 
ATOM   3379 O O   . TRP A 1 494 ? 202.926 196.992 148.180 1.00 61.78  ? 487 TRP B O   1 
ATOM   3380 C CB  . TRP A 1 494 ? 203.068 193.618 147.826 1.00 48.79  ? 487 TRP B CB  1 
ATOM   3381 C CG  . TRP A 1 494 ? 203.690 192.446 147.123 1.00 44.50  ? 487 TRP B CG  1 
ATOM   3382 C CD1 . TRP A 1 494 ? 204.941 191.948 147.320 1.00 44.38  ? 487 TRP B CD1 1 
ATOM   3383 C CD2 . TRP A 1 494 ? 203.093 191.635 146.105 1.00 40.44  ? 487 TRP B CD2 1 
ATOM   3384 N NE1 . TRP A 1 494 ? 205.160 190.876 146.495 1.00 43.15  ? 487 TRP B NE1 1 
ATOM   3385 C CE2 . TRP A 1 494 ? 204.041 190.663 145.737 1.00 40.94  ? 487 TRP B CE2 1 
ATOM   3386 C CE3 . TRP A 1 494 ? 201.849 191.636 145.470 1.00 39.47  ? 487 TRP B CE3 1 
ATOM   3387 C CZ2 . TRP A 1 494 ? 203.784 189.701 144.766 1.00 34.99  ? 487 TRP B CZ2 1 
ATOM   3388 C CZ3 . TRP A 1 494 ? 201.597 190.683 144.506 1.00 36.90  ? 487 TRP B CZ3 1 
ATOM   3389 C CH2 . TRP A 1 494 ? 202.560 189.728 144.163 1.00 35.82  ? 487 TRP B CH2 1 
ATOM   3390 N N   . HIS A 1 495 ? 201.010 195.856 147.855 1.00 51.26  ? 488 HIS B N   1 
ATOM   3391 C CA  . HIS A 1 495 ? 200.143 196.859 148.455 1.00 44.63  ? 488 HIS B CA  1 
ATOM   3392 C C   . HIS A 1 495 ? 199.977 196.680 149.953 1.00 49.05  ? 488 HIS B C   1 
ATOM   3393 O O   . HIS A 1 495 ? 199.337 197.517 150.595 1.00 56.35  ? 488 HIS B O   1 
ATOM   3394 C CB  . HIS A 1 495 ? 198.767 196.818 147.795 1.00 40.05  ? 488 HIS B CB  1 
ATOM   3395 C CG  . HIS A 1 495 ? 198.054 195.516 147.978 1.00 41.52  ? 488 HIS B CG  1 
ATOM   3396 N ND1 . HIS A 1 495 ? 197.282 195.240 149.084 1.00 45.62  ? 488 HIS B ND1 1 
ATOM   3397 C CD2 . HIS A 1 495 ? 198.004 194.409 147.200 1.00 38.80  ? 488 HIS B CD2 1 
ATOM   3398 C CE1 . HIS A 1 495 ? 196.782 194.022 148.978 1.00 43.65  ? 488 HIS B CE1 1 
ATOM   3399 N NE2 . HIS A 1 495 ? 197.205 193.496 147.844 1.00 37.94  ? 488 HIS B NE2 1 
ATOM   3400 N N   . THR A 1 496 ? 200.529 195.615 150.523 1.00 52.54  ? 489 THR B N   1 
ATOM   3401 C CA  . THR A 1 496 ? 200.285 195.289 151.917 1.00 53.95  ? 489 THR B CA  1 
ATOM   3402 C C   . THR A 1 496 ? 200.999 196.289 152.826 1.00 60.44  ? 489 THR B C   1 
ATOM   3403 O O   . THR A 1 496 ? 201.643 197.237 152.369 1.00 65.07  ? 489 THR B O   1 
ATOM   3404 C CB  . THR A 1 496 ? 200.720 193.854 152.198 1.00 53.47  ? 489 THR B CB  1 
ATOM   3405 O OG1 . THR A 1 496 ? 201.885 193.552 151.424 1.00 53.33  ? 489 THR B OG1 1 
ATOM   3406 C CG2 . THR A 1 496 ? 199.616 192.888 151.812 1.00 46.18  ? 489 THR B CG2 1 
ATOM   3407 N N   . SER A 1 497 ? 200.864 196.077 154.139 1.00 61.58  ? 490 SER B N   1 
ATOM   3408 C CA  . SER A 1 497 ? 201.447 197.004 155.106 1.00 67.29  ? 490 SER B CA  1 
ATOM   3409 C C   . SER A 1 497 ? 202.948 197.146 154.896 1.00 70.77  ? 490 SER B C   1 
ATOM   3410 O O   . SER A 1 497 ? 203.482 198.261 154.894 1.00 70.11  ? 490 SER B O   1 
ATOM   3411 C CB  . SER A 1 497 ? 201.144 196.536 156.528 1.00 66.81  ? 490 SER B CB  1 
ATOM   3412 O OG  . SER A 1 497 ? 199.747 196.424 156.740 1.00 71.98  ? 490 SER B OG  1 
ATOM   3413 N N   . ASP A 1 498 ? 203.641 196.032 154.718 1.00 67.63  ? 491 ASP B N   1 
ATOM   3414 C CA  . ASP A 1 498 ? 205.023 196.016 154.272 1.00 67.94  ? 491 ASP B CA  1 
ATOM   3415 C C   . ASP A 1 498 ? 205.093 195.246 152.956 1.00 70.56  ? 491 ASP B C   1 
ATOM   3416 O O   . ASP A 1 498 ? 204.070 194.884 152.373 1.00 69.97  ? 491 ASP B O   1 
ATOM   3417 C CB  . ASP A 1 498 ? 205.936 195.418 155.345 1.00 71.18  ? 491 ASP B CB  1 
ATOM   3418 C CG  . ASP A 1 498 ? 205.675 193.951 155.582 1.00 75.31  ? 491 ASP B CG  1 
ATOM   3419 O OD1 . ASP A 1 498 ? 204.561 193.601 156.023 1.00 70.47  ? 491 ASP B OD1 1 
ATOM   3420 O OD2 . ASP A 1 498 ? 206.598 193.149 155.344 1.00 74.72  ? 491 ASP B OD2 1 
ATOM   3421 N N   . ASN A 1 499 ? 206.308 195.006 152.471 1.00 67.79  ? 492 ASN B N   1 
ATOM   3422 C CA  . ASN A 1 499 ? 206.481 194.348 151.177 1.00 63.68  ? 492 ASN B CA  1 
ATOM   3423 C C   . ASN A 1 499 ? 206.508 192.830 151.360 1.00 69.90  ? 492 ASN B C   1 
ATOM   3424 O O   . ASN A 1 499 ? 207.498 192.146 151.097 1.00 77.91  ? 492 ASN B O   1 
ATOM   3425 C CB  . ASN A 1 499 ? 207.738 194.854 150.484 1.00 67.97  ? 492 ASN B CB  1 
ATOM   3426 C CG  . ASN A 1 499 ? 207.496 195.198 149.033 1.00 69.82  ? 492 ASN B CG  1 
ATOM   3427 O OD1 . ASN A 1 499 ? 206.451 195.741 148.683 1.00 67.73  ? 492 ASN B OD1 1 
ATOM   3428 N ND2 . ASN A 1 499 ? 208.460 194.882 148.180 1.00 71.69  ? 492 ASN B ND2 1 
ATOM   3429 N N   . GLN A 1 500 ? 205.374 192.307 151.814 1.00 62.20  ? 493 GLN B N   1 
ATOM   3430 C CA  . GLN A 1 500 ? 205.141 190.873 151.891 1.00 62.98  ? 493 GLN B CA  1 
ATOM   3431 C C   . GLN A 1 500 ? 204.093 190.480 150.865 1.00 57.16  ? 493 GLN B C   1 
ATOM   3432 O O   . GLN A 1 500 ? 203.093 191.181 150.686 1.00 56.62  ? 493 GLN B O   1 
ATOM   3433 C CB  . GLN A 1 500 ? 204.685 190.442 153.291 1.00 64.05  ? 493 GLN B CB  1 
ATOM   3434 C CG  . GLN A 1 500 ? 205.797 190.309 154.322 1.00 68.92  ? 493 GLN B CG  1 
ATOM   3435 C CD  . GLN A 1 500 ? 207.167 190.112 153.701 1.00 74.15  ? 493 GLN B CD  1 
ATOM   3436 O OE1 . GLN A 1 500 ? 207.455 189.065 153.122 1.00 74.80  ? 493 GLN B OE1 1 
ATOM   3437 N NE2 . GLN A 1 500 ? 208.024 191.118 153.828 1.00 69.63  ? 493 GLN B NE2 1 
ATOM   3438 N N   . LYS A 1 501 ? 204.330 189.367 150.194 1.00 50.49  ? 494 LYS B N   1 
ATOM   3439 C CA  . LYS A 1 501 ? 203.373 188.872 149.219 1.00 40.86  ? 494 LYS B CA  1 
ATOM   3440 C C   . LYS A 1 501 ? 202.066 188.516 149.917 1.00 34.92  ? 494 LYS B C   1 
ATOM   3441 O O   . LYS A 1 501 ? 202.088 187.845 150.955 1.00 36.90  ? 494 LYS B O   1 
ATOM   3442 C CB  . LYS A 1 501 ? 203.940 187.653 148.500 1.00 42.30  ? 494 LYS B CB  1 
ATOM   3443 C CG  . LYS A 1 501 ? 202.911 186.818 147.775 1.00 33.76  ? 494 LYS B CG  1 
ATOM   3444 C CD  . LYS A 1 501 ? 203.549 185.570 147.211 1.00 36.80  ? 494 LYS B CD  1 
ATOM   3445 C CE  . LYS A 1 501 ? 203.585 184.467 148.254 1.00 35.82  ? 494 LYS B CE  1 
ATOM   3446 N NZ  . LYS A 1 501 ? 202.221 184.047 148.683 1.00 33.84  ? 494 LYS B NZ  1 
ATOM   3447 N N   . PRO A 1 502 ? 200.922 188.958 149.400 1.00 35.97  ? 495 PRO B N   1 
ATOM   3448 C CA  . PRO A 1 502 ? 199.644 188.580 150.009 1.00 38.12  ? 495 PRO B CA  1 
ATOM   3449 C C   . PRO A 1 502 ? 199.439 187.074 149.990 1.00 33.47  ? 495 PRO B C   1 
ATOM   3450 O O   . PRO A 1 502 ? 199.869 186.380 149.068 1.00 36.30  ? 495 PRO B O   1 
ATOM   3451 C CB  . PRO A 1 502 ? 198.612 189.301 149.137 1.00 33.70  ? 495 PRO B CB  1 
ATOM   3452 C CG  . PRO A 1 502 ? 199.358 190.414 148.519 1.00 30.77  ? 495 PRO B CG  1 
ATOM   3453 C CD  . PRO A 1 502 ? 200.747 189.925 148.309 1.00 33.78  ? 495 PRO B CD  1 
ATOM   3454 N N   . VAL A 1 503 ? 198.776 186.570 151.025 1.00 30.40  ? 496 VAL B N   1 
ATOM   3455 C CA  . VAL A 1 503 ? 198.531 185.143 151.187 1.00 31.10  ? 496 VAL B CA  1 
ATOM   3456 C C   . VAL A 1 503 ? 197.079 184.869 150.829 1.00 28.88  ? 496 VAL B C   1 
ATOM   3457 O O   . VAL A 1 503 ? 196.162 185.399 151.467 1.00 33.12  ? 496 VAL B O   1 
ATOM   3458 C CB  . VAL A 1 503 ? 198.845 184.670 152.614 1.00 30.08  ? 496 VAL B CB  1 
ATOM   3459 C CG1 . VAL A 1 503 ? 198.481 183.209 152.774 1.00 31.79  ? 496 VAL B CG1 1 
ATOM   3460 C CG2 . VAL A 1 503 ? 200.312 184.888 152.933 1.00 29.54  ? 496 VAL B CG2 1 
ATOM   3461 N N   . SER A 1 504 ? 196.872 184.041 149.807 1.00 25.79  ? 497 SER B N   1 
ATOM   3462 C CA  . SER A 1 504 ? 195.546 183.602 149.379 1.00 24.08  ? 497 SER B CA  1 
ATOM   3463 C C   . SER A 1 504 ? 195.646 182.094 149.179 1.00 27.48  ? 497 SER B C   1 
ATOM   3464 O O   . SER A 1 504 ? 195.919 181.628 148.072 1.00 34.48  ? 497 SER B O   1 
ATOM   3465 C CB  . SER A 1 504 ? 195.116 184.323 148.110 1.00 29.46  ? 497 SER B CB  1 
ATOM   3466 O OG  . SER A 1 504 ? 193.710 184.393 148.010 1.00 30.75  ? 497 SER B OG  1 
ATOM   3467 N N   . ARG A 1 505 ? 195.420 181.335 150.249 1.00 32.14  ? 498 ARG B N   1 
ATOM   3468 C CA  . ARG A 1 505 ? 195.686 179.903 150.255 1.00 35.11  ? 498 ARG B CA  1 
ATOM   3469 C C   . ARG A 1 505 ? 194.532 179.134 150.878 1.00 37.03  ? 498 ARG B C   1 
ATOM   3470 O O   . ARG A 1 505 ? 193.778 179.668 151.695 1.00 44.60  ? 498 ARG B O   1 
ATOM   3471 C CB  . ARG A 1 505 ? 196.977 179.579 151.016 1.00 33.18  ? 498 ARG B CB  1 
ATOM   3472 C CG  . ARG A 1 505 ? 198.098 179.067 150.135 1.00 40.63  ? 498 ARG B CG  1 
ATOM   3473 C CD  . ARG A 1 505 ? 199.309 178.654 150.950 1.00 56.32  ? 498 ARG B CD  1 
ATOM   3474 N NE  . ARG A 1 505 ? 200.547 178.793 150.191 1.00 65.30  ? 498 ARG B NE  1 
ATOM   3475 C CZ  . ARG A 1 505 ? 201.565 179.564 150.549 1.00 62.41  ? 498 ARG B CZ  1 
ATOM   3476 N NH1 . ARG A 1 505 ? 201.533 180.280 151.661 1.00 54.90  ? 498 ARG B NH1 1 
ATOM   3477 N NH2 . ARG A 1 505 ? 202.642 179.618 149.772 1.00 52.38  ? 498 ARG B NH2 1 
ATOM   3478 N N   . CYS A 1 506 ? 194.406 177.876 150.476 1.00 34.30  ? 499 CYS B N   1 
ATOM   3479 C CA  . CYS A 1 506 ? 193.472 176.926 151.055 1.00 40.31  ? 499 CYS B CA  1 
ATOM   3480 C C   . CYS A 1 506 ? 194.195 175.604 151.277 1.00 50.79  ? 499 CYS B C   1 
ATOM   3481 O O   . CYS A 1 506 ? 195.213 175.324 150.638 1.00 54.66  ? 499 CYS B O   1 
ATOM   3482 C CB  . CYS A 1 506 ? 192.253 176.718 150.150 1.00 39.78  ? 499 CYS B CB  1 
ATOM   3483 S SG  . CYS A 1 506 ? 192.539 175.547 148.811 1.00 67.37  ? 499 CYS B SG  1 
ATOM   3484 N N   . SER A 1 507 ? 193.671 174.793 152.188 1.00 48.14  ? 500 SER B N   1 
ATOM   3485 C CA  . SER A 1 507 ? 194.284 173.510 152.507 1.00 51.36  ? 500 SER B CA  1 
ATOM   3486 C C   . SER A 1 507 ? 193.584 172.410 151.722 1.00 62.35  ? 500 SER B C   1 
ATOM   3487 O O   . SER A 1 507 ? 192.370 172.227 151.847 1.00 68.09  ? 500 SER B O   1 
ATOM   3488 C CB  . SER A 1 507 ? 194.216 173.229 154.006 1.00 53.61  ? 500 SER B CB  1 
ATOM   3489 O OG  . SER A 1 507 ? 192.883 173.288 154.475 1.00 60.69  ? 500 SER B OG  1 
ATOM   3490 N N   . ARG A 1 508 ? 194.348 171.684 150.908 1.00 65.25  ? 501 ARG B N   1 
ATOM   3491 C CA  . ARG A 1 508 ? 193.798 170.568 150.153 1.00 68.83  ? 501 ARG B CA  1 
ATOM   3492 C C   . ARG A 1 508 ? 193.681 169.296 150.980 1.00 73.18  ? 501 ARG B C   1 
ATOM   3493 O O   . ARG A 1 508 ? 192.950 168.383 150.582 1.00 78.71  ? 501 ARG B O   1 
ATOM   3494 C CB  . ARG A 1 508 ? 194.656 170.305 148.914 1.00 71.66  ? 501 ARG B CB  1 
ATOM   3495 C CG  . ARG A 1 508 ? 195.059 171.567 148.169 1.00 79.29  ? 501 ARG B CG  1 
ATOM   3496 C CD  . ARG A 1 508 ? 195.711 171.242 146.834 1.00 82.28  ? 501 ARG B CD  1 
ATOM   3497 N NE  . ARG A 1 508 ? 194.785 170.614 145.899 1.00 82.09  ? 501 ARG B NE  1 
ATOM   3498 C CZ  . ARG A 1 508 ? 193.780 171.234 145.295 1.00 78.55  ? 501 ARG B CZ  1 
ATOM   3499 N NH1 . ARG A 1 508 ? 193.531 172.517 145.504 1.00 70.37  ? 501 ARG B NH1 1 
ATOM   3500 N NH2 . ARG A 1 508 ? 193.003 170.548 144.462 1.00 71.31  ? 501 ARG B NH2 1 
ATOM   3501 N N   . GLN A 1 509 ? 194.378 169.213 152.110 1.00 72.70  ? 502 GLN B N   1 
ATOM   3502 C CA  . GLN A 1 509 ? 194.294 168.073 153.008 1.00 76.40  ? 502 GLN B CA  1 
ATOM   3503 C C   . GLN A 1 509 ? 194.324 168.576 154.442 1.00 75.97  ? 502 GLN B C   1 
ATOM   3504 O O   . GLN A 1 509 ? 194.940 169.602 154.740 1.00 75.54  ? 502 GLN B O   1 
ATOM   3505 C CB  . GLN A 1 509 ? 195.444 167.077 152.782 1.00 77.32  ? 502 GLN B CB  1 
ATOM   3506 C CG  . GLN A 1 509 ? 195.538 166.522 151.367 1.00 82.43  ? 502 GLN B CG  1 
ATOM   3507 C CD  . GLN A 1 509 ? 196.899 166.751 150.736 1.00 86.40  ? 502 GLN B CD  1 
ATOM   3508 O OE1 . GLN A 1 509 ? 197.775 167.378 151.331 1.00 88.77  ? 502 GLN B OE1 1 
ATOM   3509 N NE2 . GLN A 1 509 ? 197.079 166.249 149.520 1.00 76.97  ? 502 GLN B NE2 1 
ATOM   3510 N N   . CYS A 1 510 ? 193.659 167.845 155.329 1.00 72.98  ? 503 CYS B N   1 
ATOM   3511 C CA  . CYS A 1 510 ? 193.677 168.178 156.747 1.00 72.68  ? 503 CYS B CA  1 
ATOM   3512 C C   . CYS A 1 510 ? 194.669 167.293 157.494 1.00 75.06  ? 503 CYS B C   1 
ATOM   3513 O O   . CYS A 1 510 ? 194.758 167.340 158.722 1.00 71.81  ? 503 CYS B O   1 
ATOM   3514 C CB  . CYS A 1 510 ? 192.283 168.037 157.360 1.00 71.59  ? 503 CYS B CB  1 
ATOM   3515 S SG  . CYS A 1 510 ? 191.066 169.251 156.799 1.00 72.60  ? 503 CYS B SG  1 
ATOM   3516 N N   . ARG A 1 517 ? 185.748 170.020 156.384 1.00 56.25  ? 510 ARG B N   1 
ATOM   3517 C CA  . ARG A 1 517 ? 184.657 170.805 155.750 1.00 59.28  ? 510 ARG B CA  1 
ATOM   3518 C C   . ARG A 1 517 ? 185.079 171.166 154.318 1.00 55.74  ? 510 ARG B C   1 
ATOM   3519 O O   . ARG A 1 517 ? 186.097 171.868 154.158 1.00 57.28  ? 510 ARG B O   1 
ATOM   3520 C CB  . ARG A 1 517 ? 184.359 172.064 156.572 1.00 61.19  ? 510 ARG B CB  1 
ATOM   3521 C CG  . ARG A 1 517 ? 183.707 173.194 155.786 1.00 64.45  ? 510 ARG B CG  1 
ATOM   3522 C CD  . ARG A 1 517 ? 182.384 173.625 156.396 1.00 72.72  ? 510 ARG B CD  1 
ATOM   3523 N NE  . ARG A 1 517 ? 182.337 173.379 157.842 1.00 85.62  ? 510 ARG B NE  1 
ATOM   3524 C CZ  . ARG A 1 517 ? 181.247 173.023 158.509 1.00 90.40  ? 510 ARG B CZ  1 
ATOM   3525 N NH1 . ARG A 1 517 ? 180.161 172.654 157.853 1.00 86.77  ? 510 ARG B NH1 1 
ATOM   3526 N NH2 . ARG A 1 517 ? 181.245 173.040 159.830 1.00 84.19  ? 510 ARG B NH2 1 
ATOM   3527 N N   . VAL A 1 518 ? 184.320 170.703 153.321 1.00 54.38  ? 511 VAL B N   1 
ATOM   3528 C CA  . VAL A 1 518 ? 184.681 170.973 151.897 1.00 48.39  ? 511 VAL B CA  1 
ATOM   3529 C C   . VAL A 1 518 ? 184.261 172.411 151.553 1.00 49.36  ? 511 VAL B C   1 
ATOM   3530 O O   . VAL A 1 518 ? 183.290 172.907 152.169 1.00 55.51  ? 511 VAL B O   1 
ATOM   3531 C CB  . VAL A 1 518 ? 184.068 169.948 150.921 1.00 48.44  ? 511 VAL B CB  1 
ATOM   3532 C CG1 . VAL A 1 518 ? 182.625 170.282 150.561 1.00 47.41  ? 511 VAL B CG1 1 
ATOM   3533 C CG2 . VAL A 1 518 ? 184.914 169.786 149.664 1.00 47.48  ? 511 VAL B CG2 1 
ATOM   3534 N N   . LYS A 1 519 ? 184.977 173.056 150.629 1.00 50.41  ? 512 LYS B N   1 
ATOM   3535 C CA  . LYS A 1 519 ? 184.659 174.419 150.236 1.00 45.56  ? 512 LYS B CA  1 
ATOM   3536 C C   . LYS A 1 519 ? 185.190 174.687 148.836 1.00 43.40  ? 512 LYS B C   1 
ATOM   3537 O O   . LYS A 1 519 ? 186.023 173.943 148.316 1.00 50.13  ? 512 LYS B O   1 
ATOM   3538 C CB  . LYS A 1 519 ? 185.237 175.440 151.230 1.00 39.45  ? 512 LYS B CB  1 
ATOM   3539 C CG  . LYS A 1 519 ? 186.736 175.630 151.144 1.00 36.15  ? 512 LYS B CG  1 
ATOM   3540 C CD  . LYS A 1 519 ? 187.171 176.883 151.876 1.00 35.02  ? 512 LYS B CD  1 
ATOM   3541 C CE  . LYS A 1 519 ? 188.669 177.091 151.769 1.00 39.18  ? 512 LYS B CE  1 
ATOM   3542 N NZ  . LYS A 1 519 ? 189.170 178.081 152.757 1.00 33.15  ? 512 LYS B NZ  1 
ATOM   3543 N N   . GLY A 1 520 ? 184.687 175.757 148.228 1.00 42.21  ? 513 GLY B N   1 
ATOM   3544 C CA  . GLY A 1 520 ? 185.076 176.122 146.882 1.00 39.40  ? 513 GLY B CA  1 
ATOM   3545 C C   . GLY A 1 520 ? 183.946 175.957 145.889 1.00 48.96  ? 513 GLY B C   1 
ATOM   3546 O O   . GLY A 1 520 ? 182.961 175.269 146.171 1.00 54.14  ? 513 GLY B O   1 
ATOM   3547 N N   . PHE A 1 521 ? 184.072 176.586 144.721 1.00 49.69  ? 514 PHE B N   1 
ATOM   3548 C CA  . PHE A 1 521 ? 183.042 176.453 143.697 1.00 45.87  ? 514 PHE B CA  1 
ATOM   3549 C C   . PHE A 1 521 ? 183.019 175.046 143.116 1.00 44.48  ? 514 PHE B C   1 
ATOM   3550 O O   . PHE A 1 521 ? 181.957 174.543 142.734 1.00 43.78  ? 514 PHE B O   1 
ATOM   3551 C CB  . PHE A 1 521 ? 183.261 177.489 142.594 1.00 45.63  ? 514 PHE B CB  1 
ATOM   3552 C CG  . PHE A 1 521 ? 182.119 177.596 141.630 1.00 50.69  ? 514 PHE B CG  1 
ATOM   3553 C CD1 . PHE A 1 521 ? 180.814 177.611 142.080 1.00 49.12  ? 514 PHE B CD1 1 
ATOM   3554 C CD2 . PHE A 1 521 ? 182.351 177.667 140.270 1.00 50.73  ? 514 PHE B CD2 1 
ATOM   3555 C CE1 . PHE A 1 521 ? 179.763 177.701 141.192 1.00 50.84  ? 514 PHE B CE1 1 
ATOM   3556 C CE2 . PHE A 1 521 ? 181.306 177.758 139.379 1.00 49.96  ? 514 PHE B CE2 1 
ATOM   3557 C CZ  . PHE A 1 521 ? 180.011 177.776 139.840 1.00 50.91  ? 514 PHE B CZ  1 
ATOM   3558 N N   . HIS A 1 522 ? 184.180 174.400 143.033 1.00 49.04  ? 515 HIS B N   1 
ATOM   3559 C CA  . HIS A 1 522 ? 184.297 173.051 142.499 1.00 47.42  ? 515 HIS B CA  1 
ATOM   3560 C C   . HIS A 1 522 ? 184.611 172.018 143.572 1.00 50.14  ? 515 HIS B C   1 
ATOM   3561 O O   . HIS A 1 522 ? 184.979 170.889 143.237 1.00 50.09  ? 515 HIS B O   1 
ATOM   3562 C CB  . HIS A 1 522 ? 185.367 173.009 141.409 1.00 53.51  ? 515 HIS B CB  1 
ATOM   3563 C CG  . HIS A 1 522 ? 185.196 174.058 140.356 1.00 55.88  ? 515 HIS B CG  1 
ATOM   3564 N ND1 . HIS A 1 522 ? 183.998 174.284 139.716 1.00 52.91  ? 515 HIS B ND1 1 
ATOM   3565 C CD2 . HIS A 1 522 ? 186.072 174.949 139.839 1.00 54.89  ? 515 HIS B CD2 1 
ATOM   3566 C CE1 . HIS A 1 522 ? 184.145 175.264 138.844 1.00 55.00  ? 515 HIS B CE1 1 
ATOM   3567 N NE2 . HIS A 1 522 ? 185.394 175.687 138.900 1.00 60.05  ? 515 HIS B NE2 1 
ATOM   3568 N N   . SER A 1 523 ? 184.489 172.388 144.847 1.00 49.62  ? 516 SER B N   1 
ATOM   3569 C CA  . SER A 1 523 ? 184.683 171.483 145.982 1.00 47.58  ? 516 SER B CA  1 
ATOM   3570 C C   . SER A 1 523 ? 186.084 170.869 145.980 1.00 49.63  ? 516 SER B C   1 
ATOM   3571 O O   . SER A 1 523 ? 186.262 169.653 145.925 1.00 52.01  ? 516 SER B O   1 
ATOM   3572 C CB  . SER A 1 523 ? 183.606 170.396 145.999 1.00 41.98  ? 516 SER B CB  1 
ATOM   3573 O OG  . SER A 1 523 ? 182.440 170.847 146.653 1.00 51.15  ? 516 SER B OG  1 
ATOM   3574 N N   . CYS A 1 524 ? 187.087 171.739 146.055 1.00 45.80  ? 517 CYS B N   1 
ATOM   3575 C CA  . CYS A 1 524 ? 188.480 171.310 146.047 1.00 49.58  ? 517 CYS B CA  1 
ATOM   3576 C C   . CYS A 1 524 ? 189.104 171.377 147.428 1.00 53.81  ? 517 CYS B C   1 
ATOM   3577 O O   . CYS A 1 524 ? 189.689 170.399 147.902 1.00 62.69  ? 517 CYS B O   1 
ATOM   3578 C CB  . CYS A 1 524 ? 189.312 172.194 145.116 1.00 54.12  ? 517 CYS B CB  1 
ATOM   3579 S SG  . CYS A 1 524 ? 188.439 172.861 143.723 1.00 77.83  ? 517 CYS B SG  1 
ATOM   3580 N N   . CYS A 1 525 ? 188.998 172.535 148.073 1.00 51.56  ? 518 CYS B N   1 
ATOM   3581 C CA  . CYS A 1 525 ? 189.684 172.823 149.318 1.00 48.71  ? 518 CYS B CA  1 
ATOM   3582 C C   . CYS A 1 525 ? 188.916 172.243 150.497 1.00 50.78  ? 518 CYS B C   1 
ATOM   3583 O O   . CYS A 1 525 ? 187.822 171.700 150.355 1.00 53.42  ? 518 CYS B O   1 
ATOM   3584 C CB  . CYS A 1 525 ? 189.860 174.330 149.485 1.00 44.05  ? 518 CYS B CB  1 
ATOM   3585 S SG  . CYS A 1 525 ? 190.687 175.134 148.103 1.00 77.34  ? 518 CYS B SG  1 
ATOM   3586 N N   . TYR A 1 526 ? 189.502 172.366 151.683 1.00 54.28  ? 519 TYR B N   1 
ATOM   3587 C CA  . TYR A 1 526 ? 188.833 171.993 152.919 1.00 54.50  ? 519 TYR B CA  1 
ATOM   3588 C C   . TYR A 1 526 ? 189.087 173.079 153.948 1.00 54.33  ? 519 TYR B C   1 
ATOM   3589 O O   . TYR A 1 526 ? 190.137 173.726 153.925 1.00 55.22  ? 519 TYR B O   1 
ATOM   3590 C CB  . TYR A 1 526 ? 189.323 170.637 153.435 1.00 55.02  ? 519 TYR B CB  1 
ATOM   3591 C CG  . TYR A 1 526 ? 189.036 169.489 152.498 1.00 56.71  ? 519 TYR B CG  1 
ATOM   3592 C CD1 . TYR A 1 526 ? 187.761 168.950 152.401 1.00 52.34  ? 519 TYR B CD1 1 
ATOM   3593 C CD2 . TYR A 1 526 ? 190.038 168.943 151.713 1.00 61.86  ? 519 TYR B CD2 1 
ATOM   3594 C CE1 . TYR A 1 526 ? 187.491 167.901 151.549 1.00 55.17  ? 519 TYR B CE1 1 
ATOM   3595 C CE2 . TYR A 1 526 ? 189.776 167.892 150.857 1.00 66.08  ? 519 TYR B CE2 1 
ATOM   3596 C CZ  . TYR A 1 526 ? 188.502 167.377 150.779 1.00 64.86  ? 519 TYR B CZ  1 
ATOM   3597 O OH  . TYR A 1 526 ? 188.245 166.332 149.926 1.00 67.55  ? 519 TYR B OH  1 
ATOM   3598 N N   . ASP A 1 527 ? 188.113 173.295 154.826 1.00 52.97  ? 520 ASP B N   1 
ATOM   3599 C CA  . ASP A 1 527 ? 188.270 174.217 155.946 1.00 50.63  ? 520 ASP B CA  1 
ATOM   3600 C C   . ASP A 1 527 ? 188.505 173.401 157.217 1.00 59.09  ? 520 ASP B C   1 
ATOM   3601 O O   . ASP A 1 527 ? 187.592 173.088 157.984 1.00 64.45  ? 520 ASP B O   1 
ATOM   3602 C CB  . ASP A 1 527 ? 187.054 175.126 156.061 1.00 51.88  ? 520 ASP B CB  1 
ATOM   3603 C CG  . ASP A 1 527 ? 187.430 176.591 156.087 1.00 64.02  ? 520 ASP B CG  1 
ATOM   3604 O OD1 . ASP A 1 527 ? 188.500 176.921 156.644 1.00 63.72  ? 520 ASP B OD1 1 
ATOM   3605 O OD2 . ASP A 1 527 ? 186.662 177.414 155.547 1.00 61.59  ? 520 ASP B OD2 1 
ATOM   3606 N N   . CYS A 1 528 ? 189.771 173.051 157.420 1.00 62.19  ? 521 CYS B N   1 
ATOM   3607 C CA  . CYS A 1 528 ? 190.175 172.213 158.545 1.00 59.85  ? 521 CYS B CA  1 
ATOM   3608 C C   . CYS A 1 528 ? 189.980 172.938 159.869 1.00 53.49  ? 521 CYS B C   1 
ATOM   3609 O O   . CYS A 1 528 ? 188.954 172.781 160.529 1.00 50.82  ? 521 CYS B O   1 
ATOM   3610 C CB  . CYS A 1 528 ? 191.635 171.785 158.393 1.00 68.24  ? 521 CYS B CB  1 
ATOM   3611 S SG  . CYS A 1 528 ? 192.055 171.023 156.805 1.00 77.72  ? 521 CYS B SG  1 
ATOM   3612 N N   . SER B 2 34  ? 162.212 161.168 95.951  1.00 89.61  ? 25  SER A N   1 
ATOM   3613 C CA  . SER B 2 34  ? 162.271 160.797 97.359  1.00 97.20  ? 25  SER A CA  1 
ATOM   3614 C C   . SER B 2 34  ? 161.400 161.730 98.193  1.00 92.02  ? 25  SER A C   1 
ATOM   3615 O O   . SER B 2 34  ? 160.609 162.501 97.652  1.00 80.25  ? 25  SER A O   1 
ATOM   3616 C CB  . SER B 2 34  ? 163.715 160.821 97.863  1.00 97.19  ? 25  SER A CB  1 
ATOM   3617 O OG  . SER B 2 34  ? 163.889 159.940 98.960  1.00 95.86  ? 25  SER A OG  1 
ATOM   3618 N N   . ASP B 2 35  ? 161.551 161.657 99.512  1.00 90.82  ? 26  ASP A N   1 
ATOM   3619 C CA  . ASP B 2 35  ? 160.758 162.466 100.426 1.00 81.24  ? 26  ASP A CA  1 
ATOM   3620 C C   . ASP B 2 35  ? 161.429 163.784 100.792 1.00 79.08  ? 26  ASP A C   1 
ATOM   3621 O O   . ASP B 2 35  ? 160.861 164.555 101.569 1.00 81.18  ? 26  ASP A O   1 
ATOM   3622 C CB  . ASP B 2 35  ? 160.445 161.675 101.704 1.00 84.23  ? 26  ASP A CB  1 
ATOM   3623 C CG  . ASP B 2 35  ? 161.629 160.871 102.205 1.00 88.31  ? 26  ASP A CG  1 
ATOM   3624 O OD1 . ASP B 2 35  ? 162.777 161.337 102.059 1.00 88.81  ? 26  ASP A OD1 1 
ATOM   3625 O OD2 . ASP B 2 35  ? 161.411 159.771 102.754 1.00 85.88  ? 26  ASP A OD2 1 
ATOM   3626 N N   . PHE B 2 36  ? 162.608 164.069 100.246 1.00 79.27  ? 27  PHE A N   1 
ATOM   3627 C CA  . PHE B 2 36  ? 163.326 165.302 100.539 1.00 70.71  ? 27  PHE A CA  1 
ATOM   3628 C C   . PHE B 2 36  ? 162.937 166.448 99.619  1.00 65.08  ? 27  PHE A C   1 
ATOM   3629 O O   . PHE B 2 36  ? 163.613 167.479 99.620  1.00 70.03  ? 27  PHE A O   1 
ATOM   3630 C CB  . PHE B 2 36  ? 164.838 165.074 100.454 1.00 67.61  ? 27  PHE A CB  1 
ATOM   3631 C CG  . PHE B 2 36  ? 165.405 164.319 101.619 1.00 74.79  ? 27  PHE A CG  1 
ATOM   3632 C CD1 . PHE B 2 36  ? 165.323 162.941 101.677 1.00 84.13  ? 27  PHE A CD1 1 
ATOM   3633 C CD2 . PHE B 2 36  ? 166.024 164.990 102.658 1.00 79.30  ? 27  PHE A CD2 1 
ATOM   3634 C CE1 . PHE B 2 36  ? 165.845 162.248 102.751 1.00 94.39  ? 27  PHE A CE1 1 
ATOM   3635 C CE2 . PHE B 2 36  ? 166.548 164.303 103.734 1.00 81.49  ? 27  PHE A CE2 1 
ATOM   3636 C CZ  . PHE B 2 36  ? 166.459 162.931 103.780 1.00 89.59  ? 27  PHE A CZ  1 
ATOM   3637 N N   . TYR B 2 37  ? 161.872 166.297 98.835  1.00 64.41  ? 28  TYR A N   1 
ATOM   3638 C CA  . TYR B 2 37  ? 161.491 167.322 97.874  1.00 67.95  ? 28  TYR A CA  1 
ATOM   3639 C C   . TYR B 2 37  ? 160.074 167.048 97.395  1.00 74.30  ? 28  TYR A C   1 
ATOM   3640 O O   . TYR B 2 37  ? 159.754 165.917 97.022  1.00 82.39  ? 28  TYR A O   1 
ATOM   3641 C CB  . TYR B 2 37  ? 162.465 167.336 96.689  1.00 74.38  ? 28  TYR A CB  1 
ATOM   3642 C CG  . TYR B 2 37  ? 162.184 168.387 95.638  1.00 80.07  ? 28  TYR A CG  1 
ATOM   3643 C CD1 . TYR B 2 37  ? 161.476 169.541 95.945  1.00 73.29  ? 28  TYR A CD1 1 
ATOM   3644 C CD2 . TYR B 2 37  ? 162.626 168.221 94.333  1.00 82.23  ? 28  TYR A CD2 1 
ATOM   3645 C CE1 . TYR B 2 37  ? 161.216 170.497 94.986  1.00 74.63  ? 28  TYR A CE1 1 
ATOM   3646 C CE2 . TYR B 2 37  ? 162.370 169.173 93.366  1.00 85.60  ? 28  TYR A CE2 1 
ATOM   3647 C CZ  . TYR B 2 37  ? 161.664 170.309 93.699  1.00 83.23  ? 28  TYR A CZ  1 
ATOM   3648 O OH  . TYR B 2 37  ? 161.405 171.262 92.743  1.00 80.12  ? 28  TYR A OH  1 
ATOM   3649 N N   . LEU B 2 38  ? 159.232 168.077 97.416  1.00 68.47  ? 29  LEU A N   1 
ATOM   3650 C CA  . LEU B 2 38  ? 157.929 168.023 96.767  1.00 70.43  ? 29  LEU A CA  1 
ATOM   3651 C C   . LEU B 2 38  ? 157.694 169.336 96.037  1.00 69.10  ? 29  LEU A C   1 
ATOM   3652 O O   . LEU B 2 38  ? 157.727 170.406 96.657  1.00 64.75  ? 29  LEU A O   1 
ATOM   3653 C CB  . LEU B 2 38  ? 156.801 167.763 97.770  1.00 71.95  ? 29  LEU A CB  1 
ATOM   3654 C CG  . LEU B 2 38  ? 155.422 168.280 97.335  1.00 71.26  ? 29  LEU A CG  1 
ATOM   3655 C CD1 . LEU B 2 38  ? 154.754 167.309 96.376  1.00 62.63  ? 29  LEU A CD1 1 
ATOM   3656 C CD2 . LEU B 2 38  ? 154.510 168.555 98.517  1.00 63.50  ? 29  LEU A CD2 1 
ATOM   3657 N N   . PRO B 2 39  ? 157.475 169.301 94.726  1.00 75.78  ? 30  PRO A N   1 
ATOM   3658 C CA  . PRO B 2 39  ? 157.186 170.539 93.999  1.00 70.85  ? 30  PRO A CA  1 
ATOM   3659 C C   . PRO B 2 39  ? 155.906 171.182 94.501  1.00 64.81  ? 30  PRO A C   1 
ATOM   3660 O O   . PRO B 2 39  ? 154.956 170.506 94.899  1.00 65.46  ? 30  PRO A O   1 
ATOM   3661 C CB  . PRO B 2 39  ? 157.048 170.073 92.546  1.00 71.97  ? 30  PRO A CB  1 
ATOM   3662 C CG  . PRO B 2 39  ? 156.614 168.655 92.655  1.00 77.71  ? 30  PRO A CG  1 
ATOM   3663 C CD  . PRO B 2 39  ? 157.300 168.109 93.879  1.00 78.38  ? 30  PRO A CD  1 
ATOM   3664 N N   . GLY B 2 40  ? 155.897 172.508 94.492  1.00 58.55  ? 31  GLY A N   1 
ATOM   3665 C CA  . GLY B 2 40  ? 154.735 173.230 94.970  1.00 60.02  ? 31  GLY A CA  1 
ATOM   3666 C C   . GLY B 2 40  ? 154.808 174.681 94.559  1.00 61.27  ? 31  GLY A C   1 
ATOM   3667 O O   . GLY B 2 40  ? 155.810 175.149 94.014  1.00 63.90  ? 31  GLY A O   1 
ATOM   3668 N N   . ASP B 2 41  ? 153.713 175.391 94.827  1.00 64.03  ? 32  ASP A N   1 
ATOM   3669 C CA  . ASP B 2 41  ? 153.646 176.801 94.465  1.00 63.91  ? 32  ASP A CA  1 
ATOM   3670 C C   . ASP B 2 41  ? 154.607 177.625 95.314  1.00 65.72  ? 32  ASP A C   1 
ATOM   3671 O O   . ASP B 2 41  ? 155.373 178.439 94.786  1.00 68.39  ? 32  ASP A O   1 
ATOM   3672 C CB  . ASP B 2 41  ? 152.209 177.301 94.613  1.00 59.95  ? 32  ASP A CB  1 
ATOM   3673 C CG  . ASP B 2 41  ? 151.979 178.646 93.952  1.00 67.25  ? 32  ASP A CG  1 
ATOM   3674 O OD1 . ASP B 2 41  ? 152.910 179.475 93.904  1.00 68.47  ? 32  ASP A OD1 1 
ATOM   3675 O OD2 . ASP B 2 41  ? 150.851 178.869 93.467  1.00 72.86  ? 32  ASP A OD2 1 
ATOM   3676 N N   . TYR B 2 42  ? 154.590 177.420 96.630  1.00 58.14  ? 33  TYR A N   1 
ATOM   3677 C CA  . TYR B 2 42  ? 155.486 178.112 97.544  1.00 52.68  ? 33  TYR A CA  1 
ATOM   3678 C C   . TYR B 2 42  ? 156.334 177.078 98.263  1.00 54.24  ? 33  TYR A C   1 
ATOM   3679 O O   . TYR B 2 42  ? 155.800 176.222 98.972  1.00 59.43  ? 33  TYR A O   1 
ATOM   3680 C CB  . TYR B 2 42  ? 154.702 178.944 98.558  1.00 52.42  ? 33  TYR A CB  1 
ATOM   3681 C CG  . TYR B 2 42  ? 153.940 180.085 97.938  1.00 53.34  ? 33  TYR A CG  1 
ATOM   3682 C CD1 . TYR B 2 42  ? 152.642 179.904 97.490  1.00 57.76  ? 33  TYR A CD1 1 
ATOM   3683 C CD2 . TYR B 2 42  ? 154.514 181.338 97.798  1.00 50.24  ? 33  TYR A CD2 1 
ATOM   3684 C CE1 . TYR B 2 42  ? 151.935 180.935 96.921  1.00 60.66  ? 33  TYR A CE1 1 
ATOM   3685 C CE2 . TYR B 2 42  ? 153.813 182.378 97.228  1.00 53.44  ? 33  TYR A CE2 1 
ATOM   3686 C CZ  . TYR B 2 42  ? 152.524 182.168 96.793  1.00 58.92  ? 33  TYR A CZ  1 
ATOM   3687 O OH  . TYR B 2 42  ? 151.814 183.194 96.225  1.00 70.01  ? 33  TYR A OH  1 
ATOM   3688 N N   . LEU B 2 43  ? 157.647 177.161 98.089  1.00 49.64  ? 34  LEU A N   1 
ATOM   3689 C CA  . LEU B 2 43  ? 158.544 176.179 98.672  1.00 47.45  ? 34  LEU A CA  1 
ATOM   3690 C C   . LEU B 2 43  ? 158.836 176.516 100.130 1.00 42.16  ? 34  LEU A C   1 
ATOM   3691 O O   . LEU B 2 43  ? 158.603 177.630 100.600 1.00 42.38  ? 34  LEU A O   1 
ATOM   3692 C CB  . LEU B 2 43  ? 159.840 176.088 97.868  1.00 52.77  ? 34  LEU A CB  1 
ATOM   3693 C CG  . LEU B 2 43  ? 159.755 175.493 96.460  1.00 52.10  ? 34  LEU A CG  1 
ATOM   3694 C CD1 . LEU B 2 43  ? 161.027 174.734 96.135  1.00 52.21  ? 34  LEU A CD1 1 
ATOM   3695 C CD2 . LEU B 2 43  ? 158.545 174.588 96.307  1.00 52.86  ? 34  LEU A CD2 1 
ATOM   3696 N N   . LEU B 2 44  ? 159.358 175.525 100.850 1.00 43.69  ? 35  LEU A N   1 
ATOM   3697 C CA  . LEU B 2 44  ? 159.581 175.657 102.288 1.00 41.18  ? 35  LEU A CA  1 
ATOM   3698 C C   . LEU B 2 44  ? 160.853 174.891 102.631 1.00 35.62  ? 35  LEU A C   1 
ATOM   3699 O O   . LEU B 2 44  ? 160.852 173.660 102.635 1.00 46.15  ? 35  LEU A O   1 
ATOM   3700 C CB  . LEU B 2 44  ? 158.388 175.129 103.070 1.00 43.58  ? 35  LEU A CB  1 
ATOM   3701 C CG  . LEU B 2 44  ? 158.087 175.838 104.383 1.00 38.53  ? 35  LEU A CG  1 
ATOM   3702 C CD1 . LEU B 2 44  ? 157.291 177.072 104.076 1.00 32.80  ? 35  LEU A CD1 1 
ATOM   3703 C CD2 . LEU B 2 44  ? 157.321 174.924 105.317 1.00 36.55  ? 35  LEU A CD2 1 
ATOM   3704 N N   . GLY B 2 45  ? 161.924 175.620 102.924 1.00 28.93  ? 36  GLY A N   1 
ATOM   3705 C CA  . GLY B 2 45  ? 163.157 174.962 103.309 1.00 28.65  ? 36  GLY A CA  1 
ATOM   3706 C C   . GLY B 2 45  ? 162.983 174.183 104.600 1.00 29.74  ? 36  GLY A C   1 
ATOM   3707 O O   . GLY B 2 45  ? 162.174 174.537 105.458 1.00 34.84  ? 36  GLY A O   1 
ATOM   3708 N N   . GLY B 2 46  ? 163.738 173.100 104.724 1.00 34.95  ? 37  GLY A N   1 
ATOM   3709 C CA  . GLY B 2 46  ? 163.725 172.310 105.936 1.00 32.93  ? 37  GLY A CA  1 
ATOM   3710 C C   . GLY B 2 46  ? 165.106 171.800 106.275 1.00 36.45  ? 37  GLY A C   1 
ATOM   3711 O O   . GLY B 2 46  ? 165.789 171.245 105.413 1.00 44.29  ? 37  GLY A O   1 
ATOM   3712 N N   . LEU B 2 47  ? 165.536 171.986 107.516 1.00 33.58  ? 38  LEU A N   1 
ATOM   3713 C CA  . LEU B 2 47  ? 166.854 171.554 107.962 1.00 44.15  ? 38  LEU A CA  1 
ATOM   3714 C C   . LEU B 2 47  ? 166.690 170.620 109.151 1.00 51.05  ? 38  LEU A C   1 
ATOM   3715 O O   . LEU B 2 47  ? 166.246 171.047 110.221 1.00 48.77  ? 38  LEU A O   1 
ATOM   3716 C CB  . LEU B 2 47  ? 167.725 172.754 108.329 1.00 43.20  ? 38  LEU A CB  1 
ATOM   3717 C CG  . LEU B 2 47  ? 167.922 173.768 107.204 1.00 41.77  ? 38  LEU A CG  1 
ATOM   3718 C CD1 . LEU B 2 47  ? 168.694 174.971 107.697 1.00 42.47  ? 38  LEU A CD1 1 
ATOM   3719 C CD2 . LEU B 2 47  ? 168.634 173.115 106.040 1.00 45.54  ? 38  LEU A CD2 1 
ATOM   3720 N N   . PHE B 2 48  ? 167.058 169.354 108.965 1.00 53.48  ? 39  PHE A N   1 
ATOM   3721 C CA  . PHE B 2 48  ? 166.879 168.338 109.990 1.00 57.38  ? 39  PHE A CA  1 
ATOM   3722 C C   . PHE B 2 48  ? 168.194 167.607 110.212 1.00 70.58  ? 39  PHE A C   1 
ATOM   3723 O O   . PHE B 2 48  ? 168.886 167.241 109.261 1.00 73.66  ? 39  PHE A O   1 
ATOM   3724 C CB  . PHE B 2 48  ? 165.773 167.348 109.600 1.00 49.77  ? 39  PHE A CB  1 
ATOM   3725 C CG  . PHE B 2 48  ? 164.447 168.001 109.353 1.00 43.80  ? 39  PHE A CG  1 
ATOM   3726 C CD1 . PHE B 2 48  ? 164.108 168.452 108.094 1.00 44.10  ? 39  PHE A CD1 1 
ATOM   3727 C CD2 . PHE B 2 48  ? 163.548 168.184 110.383 1.00 42.51  ? 39  PHE A CD2 1 
ATOM   3728 C CE1 . PHE B 2 48  ? 162.897 169.062 107.868 1.00 42.40  ? 39  PHE A CE1 1 
ATOM   3729 C CE2 . PHE B 2 48  ? 162.339 168.800 110.162 1.00 38.92  ? 39  PHE A CE2 1 
ATOM   3730 C CZ  . PHE B 2 48  ? 162.014 169.236 108.904 1.00 38.32  ? 39  PHE A CZ  1 
ATOM   3731 N N   . SER B 2 49  ? 168.530 167.395 111.484 1.00 75.93  ? 40  SER A N   1 
ATOM   3732 C CA  . SER B 2 49  ? 169.776 166.727 111.864 1.00 83.02  ? 40  SER A CA  1 
ATOM   3733 C C   . SER B 2 49  ? 169.547 165.224 111.809 1.00 84.44  ? 40  SER A C   1 
ATOM   3734 O O   . SER B 2 49  ? 169.123 164.600 112.781 1.00 88.83  ? 40  SER A O   1 
ATOM   3735 C CB  . SER B 2 49  ? 170.232 167.177 113.246 1.00 89.19  ? 40  SER A CB  1 
ATOM   3736 O OG  . SER B 2 49  ? 171.640 167.098 113.369 1.00 95.57  ? 40  SER A OG  1 
ATOM   3737 N N   . LEU B 2 50  ? 169.837 164.632 110.651 1.00 85.16  ? 41  LEU A N   1 
ATOM   3738 C CA  . LEU B 2 50  ? 169.629 163.203 110.465 1.00 92.55  ? 41  LEU A CA  1 
ATOM   3739 C C   . LEU B 2 50  ? 170.769 162.356 111.017 1.00 101.65 ? 41  LEU A C   1 
ATOM   3740 O O   . LEU B 2 50  ? 170.639 161.129 111.062 1.00 102.80 ? 41  LEU A O   1 
ATOM   3741 C CB  . LEU B 2 50  ? 169.443 162.888 108.980 1.00 90.86  ? 41  LEU A CB  1 
ATOM   3742 C CG  . LEU B 2 50  ? 168.185 163.428 108.303 1.00 81.16  ? 41  LEU A CG  1 
ATOM   3743 C CD1 . LEU B 2 50  ? 167.925 162.692 107.004 1.00 83.14  ? 41  LEU A CD1 1 
ATOM   3744 C CD2 . LEU B 2 50  ? 166.995 163.315 109.226 1.00 75.80  ? 41  LEU A CD2 1 
ATOM   3745 N N   . HIS B 2 51  ? 171.877 162.969 111.431 1.00 104.54 ? 42  HIS A N   1 
ATOM   3746 C CA  . HIS B 2 51  ? 173.048 162.216 111.857 1.00 105.68 ? 42  HIS A CA  1 
ATOM   3747 C C   . HIS B 2 51  ? 173.771 162.979 112.958 1.00 111.79 ? 42  HIS A C   1 
ATOM   3748 O O   . HIS B 2 51  ? 173.555 164.177 113.155 1.00 109.22 ? 42  HIS A O   1 
ATOM   3749 C CB  . HIS B 2 51  ? 173.995 161.948 110.682 1.00 103.77 ? 42  HIS A CB  1 
ATOM   3750 C CG  . HIS B 2 51  ? 173.363 161.184 109.561 1.00 104.11 ? 42  HIS A CG  1 
ATOM   3751 N ND1 . HIS B 2 51  ? 172.747 161.802 108.495 1.00 100.63 ? 42  HIS A ND1 1 
ATOM   3752 C CD2 . HIS B 2 51  ? 173.245 159.854 109.343 1.00 109.73 ? 42  HIS A CD2 1 
ATOM   3753 C CE1 . HIS B 2 51  ? 172.281 160.886 107.666 1.00 101.89 ? 42  HIS A CE1 1 
ATOM   3754 N NE2 . HIS B 2 51  ? 172.570 159.695 108.157 1.00 107.26 ? 42  HIS A NE2 1 
ATOM   3755 N N   . PHE B 2 62  ? 191.465 168.499 106.579 1.00 99.29  ? 53  PHE A N   1 
ATOM   3756 C CA  . PHE B 2 62  ? 190.460 169.459 106.146 1.00 95.86  ? 53  PHE A CA  1 
ATOM   3757 C C   . PHE B 2 62  ? 190.213 169.433 104.644 1.00 96.68  ? 53  PHE A C   1 
ATOM   3758 O O   . PHE B 2 62  ? 189.216 170.004 104.189 1.00 91.23  ? 53  PHE A O   1 
ATOM   3759 C CB  . PHE B 2 62  ? 190.871 170.876 106.560 1.00 81.49  ? 53  PHE A CB  1 
ATOM   3760 C CG  . PHE B 2 62  ? 192.267 171.249 106.144 1.00 81.25  ? 53  PHE A CG  1 
ATOM   3761 C CD1 . PHE B 2 62  ? 192.521 171.729 104.870 1.00 77.13  ? 53  PHE A CD1 1 
ATOM   3762 C CD2 . PHE B 2 62  ? 193.324 171.119 107.026 1.00 81.05  ? 53  PHE A CD2 1 
ATOM   3763 C CE1 . PHE B 2 62  ? 193.802 172.068 104.483 1.00 74.99  ? 53  PHE A CE1 1 
ATOM   3764 C CE2 . PHE B 2 62  ? 194.608 171.458 106.645 1.00 80.80  ? 53  PHE A CE2 1 
ATOM   3765 C CZ  . PHE B 2 62  ? 194.847 171.934 105.372 1.00 74.55  ? 53  PHE A CZ  1 
ATOM   3766 N N   . LEU B 2 63  ? 191.092 168.795 103.869 1.00 97.53  ? 54  LEU A N   1 
ATOM   3767 C CA  . LEU B 2 63  ? 190.962 168.833 102.416 1.00 96.63  ? 54  LEU A CA  1 
ATOM   3768 C C   . LEU B 2 63  ? 189.719 168.087 101.951 1.00 96.66  ? 54  LEU A C   1 
ATOM   3769 O O   . LEU B 2 63  ? 189.047 168.516 101.006 1.00 87.47  ? 54  LEU A O   1 
ATOM   3770 C CB  . LEU B 2 63  ? 192.218 168.257 101.762 1.00 100.33 ? 54  LEU A CB  1 
ATOM   3771 C CG  . LEU B 2 63  ? 193.302 169.266 101.374 1.00 100.77 ? 54  LEU A CG  1 
ATOM   3772 C CD1 . LEU B 2 63  ? 194.146 168.735 100.228 1.00 96.21  ? 54  LEU A CD1 1 
ATOM   3773 C CD2 . LEU B 2 63  ? 192.701 170.620 101.018 1.00 89.17  ? 54  LEU A CD2 1 
ATOM   3774 N N   . GLN B 2 64  ? 189.399 166.967 102.592 1.00 105.51 ? 55  GLN A N   1 
ATOM   3775 C CA  . GLN B 2 64  ? 188.180 166.234 102.288 1.00 111.68 ? 55  GLN A CA  1 
ATOM   3776 C C   . GLN B 2 64  ? 187.120 166.558 103.334 1.00 114.06 ? 55  GLN A C   1 
ATOM   3777 O O   . GLN B 2 64  ? 187.426 166.717 104.520 1.00 109.87 ? 55  GLN A O   1 
ATOM   3778 C CB  . GLN B 2 64  ? 188.446 164.726 102.229 1.00 112.07 ? 55  GLN A CB  1 
ATOM   3779 C CG  . GLN B 2 64  ? 187.915 163.916 103.404 1.00 118.30 ? 55  GLN A CG  1 
ATOM   3780 C CD  . GLN B 2 64  ? 188.909 163.817 104.544 1.00 120.01 ? 55  GLN A CD  1 
ATOM   3781 O OE1 . GLN B 2 64  ? 189.780 164.671 104.698 1.00 118.14 ? 55  GLN A OE1 1 
ATOM   3782 N NE2 . GLN B 2 64  ? 188.782 162.769 105.350 1.00 117.01 ? 55  GLN A NE2 1 
ATOM   3783 N N   . VAL B 2 65  ? 185.878 166.688 102.882 1.00 118.42 ? 56  VAL A N   1 
ATOM   3784 C CA  . VAL B 2 65  ? 184.761 167.065 103.738 1.00 123.83 ? 56  VAL A CA  1 
ATOM   3785 C C   . VAL B 2 65  ? 183.906 165.820 103.965 1.00 126.41 ? 56  VAL A C   1 
ATOM   3786 O O   . VAL B 2 65  ? 183.246 165.344 103.030 1.00 123.61 ? 56  VAL A O   1 
ATOM   3787 C CB  . VAL B 2 65  ? 183.935 168.204 103.126 1.00 122.32 ? 56  VAL A CB  1 
ATOM   3788 C CG1 . VAL B 2 65  ? 183.000 168.798 104.168 1.00 112.97 ? 56  VAL A CG1 1 
ATOM   3789 C CG2 . VAL B 2 65  ? 184.854 169.276 102.556 1.00 112.96 ? 56  VAL A CG2 1 
ATOM   3790 N N   . PRO B 2 66  ? 183.887 165.258 105.175 1.00 132.18 ? 57  PRO A N   1 
ATOM   3791 C CA  . PRO B 2 66  ? 183.059 164.071 105.434 1.00 131.85 ? 57  PRO A CA  1 
ATOM   3792 C C   . PRO B 2 66  ? 181.581 164.426 105.377 1.00 129.10 ? 57  PRO A C   1 
ATOM   3793 O O   . PRO B 2 66  ? 181.106 165.286 106.121 1.00 127.08 ? 57  PRO A O   1 
ATOM   3794 C CB  . PRO B 2 66  ? 183.486 163.637 106.843 1.00 128.87 ? 57  PRO A CB  1 
ATOM   3795 C CG  . PRO B 2 66  ? 184.784 164.353 107.104 1.00 126.51 ? 57  PRO A CG  1 
ATOM   3796 C CD  . PRO B 2 66  ? 184.688 165.638 106.349 1.00 127.50 ? 57  PRO A CD  1 
ATOM   3797 N N   . MET B 2 67  ? 180.856 163.760 104.484 1.00 128.15 ? 58  MET A N   1 
ATOM   3798 C CA  . MET B 2 67  ? 179.429 164.006 104.345 1.00 126.79 ? 58  MET A CA  1 
ATOM   3799 C C   . MET B 2 67  ? 178.679 163.495 105.570 1.00 125.42 ? 58  MET A C   1 
ATOM   3800 O O   . MET B 2 67  ? 179.134 162.590 106.274 1.00 124.50 ? 58  MET A O   1 
ATOM   3801 C CB  . MET B 2 67  ? 178.895 163.335 103.080 1.00 124.49 ? 58  MET A CB  1 
ATOM   3802 C CG  . MET B 2 67  ? 177.566 163.886 102.595 1.00 125.39 ? 58  MET A CG  1 
ATOM   3803 S SD  . MET B 2 67  ? 177.374 163.776 100.806 1.00 137.29 ? 58  MET A SD  1 
ATOM   3804 C CE  . MET B 2 67  ? 179.085 163.740 100.279 1.00 129.68 ? 58  MET A CE  1 
ATOM   3805 N N   . CYS B 2 68  ? 177.516 164.096 105.827 1.00 121.26 ? 59  CYS A N   1 
ATOM   3806 C CA  . CYS B 2 68  ? 176.696 163.697 106.964 1.00 118.45 ? 59  CYS A CA  1 
ATOM   3807 C C   . CYS B 2 68  ? 176.192 162.265 106.859 1.00 118.03 ? 59  CYS A C   1 
ATOM   3808 O O   . CYS B 2 68  ? 175.888 161.660 107.892 1.00 119.49 ? 59  CYS A O   1 
ATOM   3809 C CB  . CYS B 2 68  ? 175.506 164.647 107.112 1.00 109.32 ? 59  CYS A CB  1 
ATOM   3810 S SG  . CYS B 2 68  ? 175.944 166.313 107.642 1.00 113.36 ? 59  CYS A SG  1 
ATOM   3811 N N   . LYS B 2 69  ? 176.104 161.709 105.649 1.00 116.69 ? 60  LYS A N   1 
ATOM   3812 C CA  . LYS B 2 69  ? 175.545 160.374 105.477 1.00 119.05 ? 60  LYS A CA  1 
ATOM   3813 C C   . LYS B 2 69  ? 176.420 159.283 106.086 1.00 122.02 ? 60  LYS A C   1 
ATOM   3814 O O   . LYS B 2 69  ? 175.921 158.181 106.339 1.00 119.06 ? 60  LYS A O   1 
ATOM   3815 C CB  . LYS B 2 69  ? 175.310 160.098 103.991 1.00 116.63 ? 60  LYS A CB  1 
ATOM   3816 C CG  . LYS B 2 69  ? 176.429 159.336 103.307 1.00 119.01 ? 60  LYS A CG  1 
ATOM   3817 C CD  . LYS B 2 69  ? 176.220 159.291 101.803 1.00 118.65 ? 60  LYS A CD  1 
ATOM   3818 C CE  . LYS B 2 69  ? 177.292 158.456 101.125 1.00 118.15 ? 60  LYS A CE  1 
ATOM   3819 N NZ  . LYS B 2 69  ? 176.813 157.876 99.841  1.00 113.20 ? 60  LYS A NZ  1 
ATOM   3820 N N   . GLU B 2 70  ? 177.703 159.555 106.328 1.00 122.45 ? 61  GLU A N   1 
ATOM   3821 C CA  . GLU B 2 70  ? 178.589 158.555 106.909 1.00 121.21 ? 61  GLU A CA  1 
ATOM   3822 C C   . GLU B 2 70  ? 178.484 158.470 108.425 1.00 121.43 ? 61  GLU A C   1 
ATOM   3823 O O   . GLU B 2 70  ? 178.959 157.489 109.009 1.00 121.35 ? 61  GLU A O   1 
ATOM   3824 C CB  . GLU B 2 70  ? 180.043 158.841 106.516 1.00 124.14 ? 61  GLU A CB  1 
ATOM   3825 C CG  . GLU B 2 70  ? 180.676 160.018 107.245 1.00 125.18 ? 61  GLU A CG  1 
ATOM   3826 C CD  . GLU B 2 70  ? 181.511 159.594 108.440 1.00 125.73 ? 61  GLU A CD  1 
ATOM   3827 O OE1 . GLU B 2 70  ? 181.794 158.384 108.573 1.00 125.94 ? 61  GLU A OE1 1 
ATOM   3828 O OE2 . GLU B 2 70  ? 181.883 160.471 109.247 1.00 120.81 ? 61  GLU A OE2 1 
ATOM   3829 N N   . TYR B 2 71  ? 177.880 159.462 109.073 1.00 121.58 ? 62  TYR A N   1 
ATOM   3830 C CA  . TYR B 2 71  ? 177.752 159.439 110.521 1.00 123.05 ? 62  TYR A CA  1 
ATOM   3831 C C   . TYR B 2 71  ? 176.627 158.497 110.947 1.00 121.59 ? 62  TYR A C   1 
ATOM   3832 O O   . TYR B 2 71  ? 175.787 158.076 110.145 1.00 117.85 ? 62  TYR A O   1 
ATOM   3833 C CB  . TYR B 2 71  ? 177.497 160.844 111.063 1.00 123.02 ? 62  TYR A CB  1 
ATOM   3834 C CG  . TYR B 2 71  ? 178.674 161.784 110.937 1.00 124.57 ? 62  TYR A CG  1 
ATOM   3835 C CD1 . TYR B 2 71  ? 178.928 162.457 109.749 1.00 124.40 ? 62  TYR A CD1 1 
ATOM   3836 C CD2 . TYR B 2 71  ? 179.528 162.001 112.009 1.00 126.78 ? 62  TYR A CD2 1 
ATOM   3837 C CE1 . TYR B 2 71  ? 180.002 163.318 109.633 1.00 126.53 ? 62  TYR A CE1 1 
ATOM   3838 C CE2 . TYR B 2 71  ? 180.605 162.859 111.902 1.00 127.74 ? 62  TYR A CE2 1 
ATOM   3839 C CZ  . TYR B 2 71  ? 180.837 163.515 110.713 1.00 126.49 ? 62  TYR A CZ  1 
ATOM   3840 O OH  . TYR B 2 71  ? 181.908 164.371 110.603 1.00 121.97 ? 62  TYR A OH  1 
ATOM   3841 N N   . GLU B 2 72  ? 176.623 158.163 112.234 1.00 124.51 ? 63  GLU A N   1 
ATOM   3842 C CA  . GLU B 2 72  ? 175.575 157.319 112.786 1.00 126.34 ? 63  GLU A CA  1 
ATOM   3843 C C   . GLU B 2 72  ? 174.223 158.016 112.687 1.00 122.25 ? 63  GLU A C   1 
ATOM   3844 O O   . GLU B 2 72  ? 174.087 159.207 112.977 1.00 118.95 ? 63  GLU A O   1 
ATOM   3845 C CB  . GLU B 2 72  ? 175.882 156.965 114.241 1.00 127.87 ? 63  GLU A CB  1 
ATOM   3846 C CG  . GLU B 2 72  ? 177.248 156.332 114.444 1.00 130.49 ? 63  GLU A CG  1 
ATOM   3847 C CD  . GLU B 2 72  ? 177.207 154.820 114.373 1.00 130.97 ? 63  GLU A CD  1 
ATOM   3848 O OE1 . GLU B 2 72  ? 176.094 154.257 114.320 1.00 129.70 ? 63  GLU A OE1 1 
ATOM   3849 O OE2 . GLU B 2 72  ? 178.289 154.193 114.369 1.00 128.19 ? 63  GLU A OE2 1 
ATOM   3850 N N   . VAL B 2 73  ? 173.217 157.254 112.272 1.00 115.88 ? 64  VAL A N   1 
ATOM   3851 C CA  . VAL B 2 73  ? 171.896 157.803 111.994 1.00 111.90 ? 64  VAL A CA  1 
ATOM   3852 C C   . VAL B 2 73  ? 171.214 158.175 113.303 1.00 110.84 ? 64  VAL A C   1 
ATOM   3853 O O   . VAL B 2 73  ? 171.211 157.395 114.262 1.00 110.92 ? 64  VAL A O   1 
ATOM   3854 C CB  . VAL B 2 73  ? 171.050 156.800 111.195 1.00 112.81 ? 64  VAL A CB  1 
ATOM   3855 C CG1 . VAL B 2 73  ? 169.603 157.249 111.142 1.00 110.61 ? 64  VAL A CG1 1 
ATOM   3856 C CG2 . VAL B 2 73  ? 171.611 156.640 109.794 1.00 115.18 ? 64  VAL A CG2 1 
ATOM   3857 N N   . LYS B 2 74  ? 170.640 159.375 113.346 1.00 108.58 ? 65  LYS A N   1 
ATOM   3858 C CA  . LYS B 2 74  ? 169.822 159.818 114.465 1.00 100.39 ? 65  LYS A CA  1 
ATOM   3859 C C   . LYS B 2 74  ? 168.355 159.708 114.061 1.00 96.20  ? 65  LYS A C   1 
ATOM   3860 O O   . LYS B 2 74  ? 167.945 160.266 113.038 1.00 91.85  ? 65  LYS A O   1 
ATOM   3861 C CB  . LYS B 2 74  ? 170.180 161.249 114.868 1.00 92.36  ? 65  LYS A CB  1 
ATOM   3862 C CG  . LYS B 2 74  ? 170.189 161.484 116.370 1.00 94.24  ? 65  LYS A CG  1 
ATOM   3863 C CD  . LYS B 2 74  ? 170.319 162.961 116.710 1.00 94.33  ? 65  LYS A CD  1 
ATOM   3864 C CE  . LYS B 2 74  ? 169.378 163.815 115.880 1.00 91.73  ? 65  LYS A CE  1 
ATOM   3865 N NZ  . LYS B 2 74  ? 169.008 165.074 116.583 1.00 91.14  ? 65  LYS A NZ  1 
ATOM   3866 N N   . VAL B 2 75  ? 167.576 158.971 114.857 1.00 94.34  ? 66  VAL A N   1 
ATOM   3867 C CA  . VAL B 2 75  ? 166.180 158.702 114.521 1.00 90.54  ? 66  VAL A CA  1 
ATOM   3868 C C   . VAL B 2 75  ? 165.313 159.942 114.707 1.00 87.68  ? 66  VAL A C   1 
ATOM   3869 O O   . VAL B 2 75  ? 164.355 160.161 113.948 1.00 84.57  ? 66  VAL A O   1 
ATOM   3870 C CB  . VAL B 2 75  ? 165.671 157.514 115.362 1.00 97.36  ? 66  VAL A CB  1 
ATOM   3871 C CG1 . VAL B 2 75  ? 165.974 157.736 116.837 1.00 96.75  ? 66  VAL A CG1 1 
ATOM   3872 C CG2 . VAL B 2 75  ? 164.183 157.307 115.155 1.00 103.59 ? 66  VAL A CG2 1 
ATOM   3873 N N   . ILE B 2 76  ? 165.631 160.771 115.705 1.00 83.39  ? 67  ILE A N   1 
ATOM   3874 C CA  . ILE B 2 76  ? 164.791 161.920 116.029 1.00 78.43  ? 67  ILE A CA  1 
ATOM   3875 C C   . ILE B 2 76  ? 164.687 162.860 114.837 1.00 72.66  ? 67  ILE A C   1 
ATOM   3876 O O   . ILE B 2 76  ? 163.613 163.400 114.547 1.00 73.41  ? 67  ILE A O   1 
ATOM   3877 C CB  . ILE B 2 76  ? 165.336 162.642 117.274 1.00 84.62  ? 67  ILE A CB  1 
ATOM   3878 C CG1 . ILE B 2 76  ? 165.481 161.659 118.438 1.00 88.83  ? 67  ILE A CG1 1 
ATOM   3879 C CG2 . ILE B 2 76  ? 164.427 163.798 117.659 1.00 78.07  ? 67  ILE A CG2 1 
ATOM   3880 C CD1 . ILE B 2 76  ? 164.165 161.196 119.024 1.00 90.44  ? 67  ILE A CD1 1 
ATOM   3881 N N   . GLY B 2 77  ? 165.799 163.076 114.133 1.00 67.56  ? 68  GLY A N   1 
ATOM   3882 C CA  . GLY B 2 77  ? 165.770 163.961 112.981 1.00 63.93  ? 68  GLY A CA  1 
ATOM   3883 C C   . GLY B 2 77  ? 164.839 163.471 111.889 1.00 65.44  ? 68  GLY A C   1 
ATOM   3884 O O   . GLY B 2 77  ? 164.086 164.254 111.306 1.00 64.66  ? 68  GLY A O   1 
ATOM   3885 N N   . TYR B 2 78  ? 164.878 162.170 111.595 1.00 65.20  ? 69  TYR A N   1 
ATOM   3886 C CA  . TYR B 2 78  ? 163.980 161.620 110.585 1.00 65.24  ? 69  TYR A CA  1 
ATOM   3887 C C   . TYR B 2 78  ? 162.529 161.716 111.034 1.00 66.13  ? 69  TYR A C   1 
ATOM   3888 O O   . TYR B 2 78  ? 161.635 161.982 110.219 1.00 66.29  ? 69  TYR A O   1 
ATOM   3889 C CB  . TYR B 2 78  ? 164.352 160.172 110.276 1.00 74.92  ? 69  TYR A CB  1 
ATOM   3890 C CG  . TYR B 2 78  ? 163.508 159.557 109.185 1.00 79.02  ? 69  TYR A CG  1 
ATOM   3891 C CD1 . TYR B 2 78  ? 163.633 159.975 107.869 1.00 80.71  ? 69  TYR A CD1 1 
ATOM   3892 C CD2 . TYR B 2 78  ? 162.579 158.569 109.472 1.00 82.93  ? 69  TYR A CD2 1 
ATOM   3893 C CE1 . TYR B 2 78  ? 162.863 159.421 106.870 1.00 81.56  ? 69  TYR A CE1 1 
ATOM   3894 C CE2 . TYR B 2 78  ? 161.803 158.011 108.479 1.00 85.62  ? 69  TYR A CE2 1 
ATOM   3895 C CZ  . TYR B 2 78  ? 161.949 158.440 107.179 1.00 85.77  ? 69  TYR A CZ  1 
ATOM   3896 O OH  . TYR B 2 78  ? 161.179 157.887 106.184 1.00 82.14  ? 69  TYR A OH  1 
ATOM   3897 N N   . ASN B 2 79  ? 162.275 161.499 112.327 1.00 67.49  ? 70  ASN A N   1 
ATOM   3898 C CA  . ASN B 2 79  ? 160.918 161.644 112.844 1.00 66.46  ? 70  ASN A CA  1 
ATOM   3899 C C   . ASN B 2 79  ? 160.407 163.069 112.658 1.00 63.29  ? 70  ASN A C   1 
ATOM   3900 O O   . ASN B 2 79  ? 159.272 163.280 112.212 1.00 54.24  ? 70  ASN A O   1 
ATOM   3901 C CB  . ASN B 2 79  ? 160.883 161.242 114.318 1.00 68.99  ? 70  ASN A CB  1 
ATOM   3902 C CG  . ASN B 2 79  ? 159.479 161.032 114.833 1.00 73.58  ? 70  ASN A CG  1 
ATOM   3903 O OD1 . ASN B 2 79  ? 158.591 160.616 114.092 1.00 74.05  ? 70  ASN A OD1 1 
ATOM   3904 N ND2 . ASN B 2 79  ? 159.271 161.308 116.115 1.00 68.74  ? 70  ASN A ND2 1 
ATOM   3905 N N   . LEU B 2 80  ? 161.243 164.060 112.972 1.00 60.45  ? 71  LEU A N   1 
ATOM   3906 C CA  . LEU B 2 80  ? 160.841 165.456 112.817 1.00 45.98  ? 71  LEU A CA  1 
ATOM   3907 C C   . LEU B 2 80  ? 160.650 165.822 111.348 1.00 49.35  ? 71  LEU A C   1 
ATOM   3908 O O   . LEU B 2 80  ? 159.743 166.591 111.003 1.00 54.88  ? 71  LEU A O   1 
ATOM   3909 C CB  . LEU B 2 80  ? 161.878 166.365 113.471 1.00 42.49  ? 71  LEU A CB  1 
ATOM   3910 C CG  . LEU B 2 80  ? 162.102 166.077 114.955 1.00 45.36  ? 71  LEU A CG  1 
ATOM   3911 C CD1 . LEU B 2 80  ? 163.034 167.093 115.585 1.00 45.68  ? 71  LEU A CD1 1 
ATOM   3912 C CD2 . LEU B 2 80  ? 160.783 166.012 115.693 1.00 47.75  ? 71  LEU A CD2 1 
ATOM   3913 N N   . MET B 2 81  ? 161.505 165.294 110.471 1.00 46.74  ? 72  MET A N   1 
ATOM   3914 C CA  . MET B 2 81  ? 161.348 165.538 109.041 1.00 46.34  ? 72  MET A CA  1 
ATOM   3915 C C   . MET B 2 81  ? 160.029 164.975 108.528 1.00 53.46  ? 72  MET A C   1 
ATOM   3916 O O   . MET B 2 81  ? 159.325 165.626 107.741 1.00 57.28  ? 72  MET A O   1 
ATOM   3917 C CB  . MET B 2 81  ? 162.532 164.933 108.291 1.00 49.87  ? 72  MET A CB  1 
ATOM   3918 C CG  . MET B 2 81  ? 162.530 165.157 106.798 1.00 54.88  ? 72  MET A CG  1 
ATOM   3919 S SD  . MET B 2 81  ? 163.261 163.770 105.915 1.00 84.30  ? 72  MET A SD  1 
ATOM   3920 C CE  . MET B 2 81  ? 162.297 163.775 104.413 1.00 71.48  ? 72  MET A CE  1 
ATOM   3921 N N   . GLN B 2 82  ? 159.674 163.767 108.967 1.00 55.07  ? 73  GLN A N   1 
ATOM   3922 C CA  . GLN B 2 82  ? 158.384 163.202 108.591 1.00 54.48  ? 73  GLN A CA  1 
ATOM   3923 C C   . GLN B 2 82  ? 157.237 164.013 109.175 1.00 51.50  ? 73  GLN A C   1 
ATOM   3924 O O   . GLN B 2 82  ? 156.174 164.124 108.557 1.00 48.81  ? 73  GLN A O   1 
ATOM   3925 C CB  . GLN B 2 82  ? 158.303 161.742 109.029 1.00 65.94  ? 73  GLN A CB  1 
ATOM   3926 C CG  . GLN B 2 82  ? 159.084 160.807 108.127 1.00 71.15  ? 73  GLN A CG  1 
ATOM   3927 C CD  . GLN B 2 82  ? 158.718 160.985 106.668 1.00 71.42  ? 73  GLN A CD  1 
ATOM   3928 O OE1 . GLN B 2 82  ? 157.546 160.930 106.301 1.00 68.38  ? 73  GLN A OE1 1 
ATOM   3929 N NE2 . GLN B 2 82  ? 159.719 161.216 105.830 1.00 70.13  ? 73  GLN A NE2 1 
ATOM   3930 N N   . ALA B 2 83  ? 157.430 164.585 110.366 1.00 53.70  ? 74  ALA A N   1 
ATOM   3931 C CA  . ALA B 2 83  ? 156.413 165.464 110.939 1.00 49.02  ? 74  ALA A CA  1 
ATOM   3932 C C   . ALA B 2 83  ? 156.180 166.684 110.059 1.00 45.27  ? 74  ALA A C   1 
ATOM   3933 O O   . ALA B 2 83  ? 155.035 167.076 109.806 1.00 42.02  ? 74  ALA A O   1 
ATOM   3934 C CB  . ALA B 2 83  ? 156.822 165.891 112.347 1.00 44.46  ? 74  ALA A CB  1 
ATOM   3935 N N   . MET B 2 84  ? 157.263 167.300 109.582 1.00 45.36  ? 75  MET A N   1 
ATOM   3936 C CA  . MET B 2 84  ? 157.124 168.448 108.690 1.00 40.69  ? 75  MET A CA  1 
ATOM   3937 C C   . MET B 2 84  ? 156.426 168.057 107.393 1.00 45.44  ? 75  MET A C   1 
ATOM   3938 O O   . MET B 2 84  ? 155.544 168.781 106.906 1.00 42.05  ? 75  MET A O   1 
ATOM   3939 C CB  . MET B 2 84  ? 158.493 169.054 108.393 1.00 35.99  ? 75  MET A CB  1 
ATOM   3940 C CG  . MET B 2 84  ? 158.605 169.699 107.023 1.00 36.07  ? 75  MET A CG  1 
ATOM   3941 S SD  . MET B 2 84  ? 159.776 171.061 106.990 1.00 40.20  ? 75  MET A SD  1 
ATOM   3942 C CE  . MET B 2 84  ? 159.661 171.558 105.280 1.00 28.03  ? 75  MET A CE  1 
ATOM   3943 N N   . ARG B 2 85  ? 156.806 166.914 106.817 1.00 53.65  ? 76  ARG A N   1 
ATOM   3944 C CA  . ARG B 2 85  ? 156.167 166.485 105.576 1.00 53.77  ? 76  ARG A CA  1 
ATOM   3945 C C   . ARG B 2 85  ? 154.688 166.196 105.786 1.00 56.35  ? 76  ARG A C   1 
ATOM   3946 O O   . ARG B 2 85  ? 153.862 166.509 104.923 1.00 54.20  ? 76  ARG A O   1 
ATOM   3947 C CB  . ARG B 2 85  ? 156.855 165.253 105.003 1.00 54.86  ? 76  ARG A CB  1 
ATOM   3948 C CG  . ARG B 2 85  ? 158.222 165.508 104.433 1.00 55.12  ? 76  ARG A CG  1 
ATOM   3949 C CD  . ARG B 2 85  ? 158.823 164.214 103.947 1.00 67.29  ? 76  ARG A CD  1 
ATOM   3950 N NE  . ARG B 2 85  ? 158.163 163.767 102.726 1.00 70.46  ? 76  ARG A NE  1 
ATOM   3951 C CZ  . ARG B 2 85  ? 157.281 162.780 102.661 1.00 68.53  ? 76  ARG A CZ  1 
ATOM   3952 N NH1 . ARG B 2 85  ? 156.922 162.101 103.737 1.00 70.72  ? 76  ARG A NH1 1 
ATOM   3953 N NH2 . ARG B 2 85  ? 156.745 162.466 101.485 1.00 58.50  ? 76  ARG A NH2 1 
ATOM   3954 N N   . PHE B 2 86  ? 154.337 165.577 106.916 1.00 57.23  ? 77  PHE A N   1 
ATOM   3955 C CA  . PHE B 2 86  ? 152.936 165.294 107.197 1.00 56.24  ? 77  PHE A CA  1 
ATOM   3956 C C   . PHE B 2 86  ? 152.152 166.577 107.405 1.00 52.41  ? 77  PHE A C   1 
ATOM   3957 O O   . PHE B 2 86  ? 150.993 166.673 106.993 1.00 55.41  ? 77  PHE A O   1 
ATOM   3958 C CB  . PHE B 2 86  ? 152.807 164.391 108.421 1.00 61.94  ? 77  PHE A CB  1 
ATOM   3959 C CG  . PHE B 2 86  ? 151.417 164.348 108.994 1.00 60.42  ? 77  PHE A CG  1 
ATOM   3960 C CD1 . PHE B 2 86  ? 150.381 163.774 108.278 1.00 57.06  ? 77  PHE A CD1 1 
ATOM   3961 C CD2 . PHE B 2 86  ? 151.148 164.872 110.243 1.00 52.58  ? 77  PHE A CD2 1 
ATOM   3962 C CE1 . PHE B 2 86  ? 149.107 163.727 108.795 1.00 48.59  ? 77  PHE A CE1 1 
ATOM   3963 C CE2 . PHE B 2 86  ? 149.874 164.825 110.763 1.00 51.57  ? 77  PHE A CE2 1 
ATOM   3964 C CZ  . PHE B 2 86  ? 148.853 164.253 110.039 1.00 49.54  ? 77  PHE A CZ  1 
ATOM   3965 N N   . ALA B 2 87  ? 152.759 167.572 108.056 1.00 48.99  ? 78  ALA A N   1 
ATOM   3966 C CA  . ALA B 2 87  ? 152.085 168.855 108.214 1.00 47.60  ? 78  ALA A CA  1 
ATOM   3967 C C   . ALA B 2 87  ? 151.813 169.497 106.862 1.00 47.37  ? 78  ALA A C   1 
ATOM   3968 O O   . ALA B 2 87  ? 150.710 169.998 106.616 1.00 51.68  ? 78  ALA A O   1 
ATOM   3969 C CB  . ALA B 2 87  ? 152.918 169.785 109.093 1.00 40.33  ? 78  ALA A CB  1 
ATOM   3970 N N   . VAL B 2 88  ? 152.801 169.474 105.965 1.00 48.77  ? 79  VAL A N   1 
ATOM   3971 C CA  . VAL B 2 88  ? 152.604 170.048 104.636 1.00 49.38  ? 79  VAL A CA  1 
ATOM   3972 C C   . VAL B 2 88  ? 151.525 169.283 103.873 1.00 54.57  ? 79  VAL A C   1 
ATOM   3973 O O   . VAL B 2 88  ? 150.655 169.882 103.225 1.00 53.90  ? 79  VAL A O   1 
ATOM   3974 C CB  . VAL B 2 88  ? 153.937 170.073 103.869 1.00 51.25  ? 79  VAL A CB  1 
ATOM   3975 C CG1 . VAL B 2 88  ? 153.696 170.276 102.392 1.00 53.42  ? 79  VAL A CG1 1 
ATOM   3976 C CG2 . VAL B 2 88  ? 154.847 171.157 104.417 1.00 46.10  ? 79  VAL A CG2 1 
ATOM   3977 N N   . GLU B 2 89  ? 151.557 167.950 103.949 1.00 61.69  ? 80  GLU A N   1 
ATOM   3978 C CA  . GLU B 2 89  ? 150.556 167.127 103.277 1.00 61.68  ? 80  GLU A CA  1 
ATOM   3979 C C   . GLU B 2 89  ? 149.159 167.384 103.824 1.00 58.06  ? 80  GLU A C   1 
ATOM   3980 O O   . GLU B 2 89  ? 148.187 167.394 103.065 1.00 57.97  ? 80  GLU A O   1 
ATOM   3981 C CB  . GLU B 2 89  ? 150.917 165.649 103.419 1.00 71.57  ? 80  GLU A CB  1 
ATOM   3982 C CG  . GLU B 2 89  ? 150.083 164.713 102.558 1.00 77.48  ? 80  GLU A CG  1 
ATOM   3983 C CD  . GLU B 2 89  ? 150.500 163.263 102.706 1.00 96.56  ? 80  GLU A CD  1 
ATOM   3984 O OE1 . GLU B 2 89  ? 150.437 162.738 103.838 1.00 96.53  ? 80  GLU A OE1 1 
ATOM   3985 O OE2 . GLU B 2 89  ? 150.886 162.646 101.692 1.00 102.95 ? 80  GLU A OE2 1 
ATOM   3986 N N   . GLU B 2 90  ? 149.034 167.564 105.139 1.00 56.08  ? 81  GLU A N   1 
ATOM   3987 C CA  . GLU B 2 90  ? 147.727 167.805 105.739 1.00 57.36  ? 81  GLU A CA  1 
ATOM   3988 C C   . GLU B 2 90  ? 147.211 169.192 105.386 1.00 60.49  ? 81  GLU A C   1 
ATOM   3989 O O   . GLU B 2 90  ? 146.002 169.391 105.215 1.00 62.48  ? 81  GLU A O   1 
ATOM   3990 C CB  . GLU B 2 90  ? 147.811 167.621 107.254 1.00 51.35  ? 81  GLU A CB  1 
ATOM   3991 C CG  . GLU B 2 90  ? 146.580 168.068 108.015 1.00 56.25  ? 81  GLU A CG  1 
ATOM   3992 C CD  . GLU B 2 90  ? 146.205 167.110 109.124 1.00 66.16  ? 81  GLU A CD  1 
ATOM   3993 O OE1 . GLU B 2 90  ? 146.851 167.155 110.190 1.00 61.93  ? 81  GLU A OE1 1 
ATOM   3994 O OE2 . GLU B 2 90  ? 145.263 166.314 108.931 1.00 69.93  ? 81  GLU A OE2 1 
ATOM   3995 N N   . ILE B 2 91  ? 148.114 170.168 105.277 1.00 58.97  ? 82  ILE A N   1 
ATOM   3996 C CA  . ILE B 2 91  ? 147.720 171.497 104.819 1.00 53.65  ? 82  ILE A CA  1 
ATOM   3997 C C   . ILE B 2 91  ? 147.201 171.428 103.390 1.00 64.03  ? 82  ILE A C   1 
ATOM   3998 O O   . ILE B 2 91  ? 146.184 172.046 103.050 1.00 65.16  ? 82  ILE A O   1 
ATOM   3999 C CB  . ILE B 2 91  ? 148.905 172.470 104.945 1.00 43.87  ? 82  ILE A CB  1 
ATOM   4000 C CG1 . ILE B 2 91  ? 149.187 172.772 106.413 1.00 40.84  ? 82  ILE A CG1 1 
ATOM   4001 C CG2 . ILE B 2 91  ? 148.613 173.758 104.199 1.00 49.40  ? 82  ILE A CG2 1 
ATOM   4002 C CD1 . ILE B 2 91  ? 150.539 173.387 106.653 1.00 38.98  ? 82  ILE A CD1 1 
ATOM   4003 N N   . ASN B 2 92  ? 147.893 170.677 102.528 1.00 67.52  ? 83  ASN A N   1 
ATOM   4004 C CA  . ASN B 2 92  ? 147.432 170.519 101.150 1.00 66.18  ? 83  ASN A CA  1 
ATOM   4005 C C   . ASN B 2 92  ? 146.109 169.760 101.082 1.00 71.41  ? 83  ASN A C   1 
ATOM   4006 O O   . ASN B 2 92  ? 145.235 170.100 100.276 1.00 63.89  ? 83  ASN A O   1 
ATOM   4007 C CB  . ASN B 2 92  ? 148.504 169.819 100.317 1.00 63.96  ? 83  ASN A CB  1 
ATOM   4008 C CG  . ASN B 2 92  ? 149.566 170.775 99.819  1.00 61.99  ? 83  ASN A CG  1 
ATOM   4009 O OD1 . ASN B 2 92  ? 149.409 171.991 99.903  1.00 60.31  ? 83  ASN A OD1 1 
ATOM   4010 N ND2 . ASN B 2 92  ? 150.658 170.230 99.303  1.00 66.09  ? 83  ASN A ND2 1 
ATOM   4011 N N   . ASN B 2 93  ? 145.954 168.719 101.906 1.00 75.75  ? 84  ASN A N   1 
ATOM   4012 C CA  . ASN B 2 93  ? 144.696 167.979 101.967 1.00 70.17  ? 84  ASN A CA  1 
ATOM   4013 C C   . ASN B 2 93  ? 143.537 168.912 102.287 1.00 71.22  ? 84  ASN A C   1 
ATOM   4014 O O   . ASN B 2 93  ? 142.479 168.853 101.650 1.00 68.68  ? 84  ASN A O   1 
ATOM   4015 C CB  . ASN B 2 93  ? 144.781 166.877 103.029 1.00 69.15  ? 84  ASN A CB  1 
ATOM   4016 C CG  . ASN B 2 93  ? 145.400 165.582 102.514 1.00 82.03  ? 84  ASN A CG  1 
ATOM   4017 O OD1 . ASN B 2 93  ? 146.222 165.587 101.599 1.00 84.96  ? 84  ASN A OD1 1 
ATOM   4018 N ND2 . ASN B 2 93  ? 144.996 164.461 103.128 1.00 89.92  ? 84  ASN A ND2 1 
ATOM   4019 N N   . ASP B 2 94  ? 143.723 169.782 103.275 1.00 75.22  ? 85  ASP A N   1 
ATOM   4020 C CA  . ASP B 2 94  ? 142.652 170.655 103.731 1.00 78.79  ? 85  ASP A CA  1 
ATOM   4021 C C   . ASP B 2 94  ? 142.384 171.754 102.713 1.00 81.30  ? 85  ASP A C   1 
ATOM   4022 O O   . ASP B 2 94  ? 143.306 172.416 102.230 1.00 86.28  ? 85  ASP A O   1 
ATOM   4023 C CB  . ASP B 2 94  ? 143.010 171.265 105.085 1.00 75.78  ? 85  ASP A CB  1 
ATOM   4024 C CG  . ASP B 2 94  ? 143.025 170.237 106.202 1.00 83.02  ? 85  ASP A CG  1 
ATOM   4025 O OD1 . ASP B 2 94  ? 142.718 169.057 105.932 1.00 81.78  ? 85  ASP A OD1 1 
ATOM   4026 O OD2 . ASP B 2 94  ? 143.348 170.607 107.351 1.00 85.88  ? 85  ASP A OD2 1 
ATOM   4027 N N   . SER B 2 95  ? 141.109 171.950 102.393 1.00 81.94  ? 86  SER A N   1 
ATOM   4028 C CA  . SER B 2 95  ? 140.696 172.936 101.405 1.00 85.95  ? 86  SER A CA  1 
ATOM   4029 C C   . SER B 2 95  ? 140.316 174.275 102.022 1.00 87.80  ? 86  SER A C   1 
ATOM   4030 O O   . SER B 2 95  ? 139.871 175.169 101.296 1.00 88.54  ? 86  SER A O   1 
ATOM   4031 C CB  . SER B 2 95  ? 139.521 172.395 100.584 1.00 85.35  ? 86  SER A CB  1 
ATOM   4032 O OG  . SER B 2 95  ? 138.370 172.224 101.391 1.00 86.56  ? 86  SER A OG  1 
ATOM   4033 N N   . SER B 2 96  ? 140.469 174.435 103.334 1.00 86.60  ? 87  SER A N   1 
ATOM   4034 C CA  . SER B 2 96  ? 140.141 175.684 104.010 1.00 86.28  ? 87  SER A CA  1 
ATOM   4035 C C   . SER B 2 96  ? 141.344 176.599 104.185 1.00 84.45  ? 87  SER A C   1 
ATOM   4036 O O   . SER B 2 96  ? 141.227 177.811 103.985 1.00 81.98  ? 87  SER A O   1 
ATOM   4037 C CB  . SER B 2 96  ? 139.514 175.394 105.377 1.00 85.97  ? 87  SER A CB  1 
ATOM   4038 O OG  . SER B 2 96  ? 140.496 175.017 106.325 1.00 85.90  ? 87  SER A OG  1 
ATOM   4039 N N   . LEU B 2 97  ? 142.499 176.049 104.550 1.00 83.27  ? 88  LEU A N   1 
ATOM   4040 C CA  . LEU B 2 97  ? 143.725 176.817 104.714 1.00 68.30  ? 88  LEU A CA  1 
ATOM   4041 C C   . LEU B 2 97  ? 144.530 176.730 103.425 1.00 73.00  ? 88  LEU A C   1 
ATOM   4042 O O   . LEU B 2 97  ? 144.845 175.629 102.960 1.00 77.15  ? 88  LEU A O   1 
ATOM   4043 C CB  . LEU B 2 97  ? 144.541 176.298 105.898 1.00 51.73  ? 88  LEU A CB  1 
ATOM   4044 C CG  . LEU B 2 97  ? 145.880 176.982 106.167 1.00 43.53  ? 88  LEU A CG  1 
ATOM   4045 C CD1 . LEU B 2 97  ? 145.670 178.308 106.861 1.00 48.91  ? 88  LEU A CD1 1 
ATOM   4046 C CD2 . LEU B 2 97  ? 146.772 176.088 106.998 1.00 36.01  ? 88  LEU A CD2 1 
ATOM   4047 N N   . LEU B 2 98  ? 144.857 177.889 102.854 1.00 66.65  ? 89  LEU A N   1 
ATOM   4048 C CA  . LEU B 2 98  ? 145.579 177.993 101.592 1.00 68.49  ? 89  LEU A CA  1 
ATOM   4049 C C   . LEU B 2 98  ? 144.878 177.174 100.515 1.00 78.75  ? 89  LEU A C   1 
ATOM   4050 O O   . LEU B 2 98  ? 145.436 176.181 100.033 1.00 77.28  ? 89  LEU A O   1 
ATOM   4051 C CB  . LEU B 2 98  ? 147.026 177.526 101.755 1.00 58.15  ? 89  LEU A CB  1 
ATOM   4052 C CG  . LEU B 2 98  ? 148.031 178.533 102.310 1.00 50.47  ? 89  LEU A CG  1 
ATOM   4053 C CD1 . LEU B 2 98  ? 149.417 177.922 102.338 1.00 46.30  ? 89  LEU A CD1 1 
ATOM   4054 C CD2 . LEU B 2 98  ? 148.019 179.815 101.497 1.00 55.81  ? 89  LEU A CD2 1 
ATOM   4055 N N   . PRO B 2 99  ? 143.662 177.547 100.113 1.00 84.05  ? 90  PRO A N   1 
ATOM   4056 C CA  . PRO B 2 99  ? 142.939 176.745 99.117  1.00 87.55  ? 90  PRO A CA  1 
ATOM   4057 C C   . PRO B 2 99  ? 143.400 177.083 97.707  1.00 91.29  ? 90  PRO A C   1 
ATOM   4058 O O   . PRO B 2 99  ? 143.539 178.254 97.347  1.00 94.52  ? 90  PRO A O   1 
ATOM   4059 C CB  . PRO B 2 99  ? 141.476 177.138 99.341  1.00 89.25  ? 90  PRO A CB  1 
ATOM   4060 C CG  . PRO B 2 99  ? 141.536 178.504 99.921  1.00 89.87  ? 90  PRO A CG  1 
ATOM   4061 C CD  . PRO B 2 99  ? 142.887 178.722 100.544 1.00 81.57  ? 90  PRO A CD  1 
ATOM   4062 N N   . GLY B 2 100 ? 143.644 176.046 96.911  1.00 92.29  ? 91  GLY A N   1 
ATOM   4063 C CA  . GLY B 2 100 ? 144.162 176.223 95.574  1.00 92.68  ? 91  GLY A CA  1 
ATOM   4064 C C   . GLY B 2 100 ? 145.647 176.490 95.503  1.00 94.28  ? 91  GLY A C   1 
ATOM   4065 O O   . GLY B 2 100 ? 146.198 176.541 94.396  1.00 99.85  ? 91  GLY A O   1 
ATOM   4066 N N   . VAL B 2 101 ? 146.314 176.647 96.643  1.00 85.81  ? 92  VAL A N   1 
ATOM   4067 C CA  . VAL B 2 101 ? 147.741 176.932 96.704  1.00 76.88  ? 92  VAL A CA  1 
ATOM   4068 C C   . VAL B 2 101 ? 148.446 175.657 97.135  1.00 74.27  ? 92  VAL A C   1 
ATOM   4069 O O   . VAL B 2 101 ? 148.123 175.089 98.186  1.00 79.64  ? 92  VAL A O   1 
ATOM   4070 C CB  . VAL B 2 101 ? 148.056 178.079 97.676  1.00 75.51  ? 92  VAL A CB  1 
ATOM   4071 C CG1 . VAL B 2 101 ? 149.537 178.093 98.023  1.00 72.83  ? 92  VAL A CG1 1 
ATOM   4072 C CG2 . VAL B 2 101 ? 147.623 179.408 97.094  1.00 76.03  ? 92  VAL A CG2 1 
ATOM   4073 N N   . LEU B 2 102 ? 149.396 175.203 96.327  1.00 70.97  ? 93  LEU A N   1 
ATOM   4074 C CA  . LEU B 2 102 ? 150.220 174.064 96.700  1.00 72.00  ? 93  LEU A CA  1 
ATOM   4075 C C   . LEU B 2 102 ? 151.352 174.542 97.599  1.00 65.09  ? 93  LEU A C   1 
ATOM   4076 O O   . LEU B 2 102 ? 151.985 175.563 97.317  1.00 64.58  ? 93  LEU A O   1 
ATOM   4077 C CB  . LEU B 2 102 ? 150.770 173.369 95.456  1.00 72.53  ? 93  LEU A CB  1 
ATOM   4078 C CG  . LEU B 2 102 ? 149.740 172.862 94.448  1.00 74.83  ? 93  LEU A CG  1 
ATOM   4079 C CD1 . LEU B 2 102 ? 150.425 172.091 93.333  1.00 74.78  ? 93  LEU A CD1 1 
ATOM   4080 C CD2 . LEU B 2 102 ? 148.700 171.996 95.140  1.00 75.48  ? 93  LEU A CD2 1 
ATOM   4081 N N   . LEU B 2 103 ? 151.592 173.821 98.688  1.00 61.96  ? 94  LEU A N   1 
ATOM   4082 C CA  . LEU B 2 103 ? 152.711 174.110 99.576  1.00 58.44  ? 94  LEU A CA  1 
ATOM   4083 C C   . LEU B 2 103 ? 153.789 173.060 99.340  1.00 56.05  ? 94  LEU A C   1 
ATOM   4084 O O   . LEU B 2 103 ? 153.619 171.893 99.702  1.00 53.99  ? 94  LEU A O   1 
ATOM   4085 C CB  . LEU B 2 103 ? 152.258 174.127 101.033 1.00 60.57  ? 94  LEU A CB  1 
ATOM   4086 C CG  . LEU B 2 103 ? 152.985 175.101 101.960 1.00 54.82  ? 94  LEU A CG  1 
ATOM   4087 C CD1 . LEU B 2 103 ? 152.982 176.498 101.371 1.00 55.63  ? 94  LEU A CD1 1 
ATOM   4088 C CD2 . LEU B 2 103 ? 152.360 175.100 103.343 1.00 48.14  ? 94  LEU A CD2 1 
ATOM   4089 N N   . GLY B 2 104 ? 154.888 173.468 98.714  1.00 55.30  ? 95  GLY A N   1 
ATOM   4090 C CA  . GLY B 2 104 ? 156.022 172.598 98.504  1.00 53.41  ? 95  GLY A CA  1 
ATOM   4091 C C   . GLY B 2 104 ? 157.062 172.762 99.597  1.00 50.34  ? 95  GLY A C   1 
ATOM   4092 O O   . GLY B 2 104 ? 156.928 173.576 100.503 1.00 48.57  ? 95  GLY A O   1 
ATOM   4093 N N   . TYR B 2 105 ? 158.118 171.960 99.494  1.00 51.97  ? 96  TYR A N   1 
ATOM   4094 C CA  . TYR B 2 105 ? 159.230 172.079 100.422 1.00 49.98  ? 96  TYR A CA  1 
ATOM   4095 C C   . TYR B 2 105 ? 160.495 171.552 99.766  1.00 52.75  ? 96  TYR A C   1 
ATOM   4096 O O   . TYR B 2 105 ? 160.442 170.847 98.756  1.00 62.87  ? 96  TYR A O   1 
ATOM   4097 C CB  . TYR B 2 105 ? 158.984 171.326 101.737 1.00 49.39  ? 96  TYR A CB  1 
ATOM   4098 C CG  . TYR B 2 105 ? 158.433 169.930 101.592 1.00 51.63  ? 96  TYR A CG  1 
ATOM   4099 C CD1 . TYR B 2 105 ? 157.089 169.707 101.338 1.00 54.30  ? 96  TYR A CD1 1 
ATOM   4100 C CD2 . TYR B 2 105 ? 159.259 168.829 101.754 1.00 55.13  ? 96  TYR A CD2 1 
ATOM   4101 C CE1 . TYR B 2 105 ? 156.591 168.427 101.228 1.00 56.83  ? 96  TYR A CE1 1 
ATOM   4102 C CE2 . TYR B 2 105 ? 158.773 167.550 101.636 1.00 58.72  ? 96  TYR A CE2 1 
ATOM   4103 C CZ  . TYR B 2 105 ? 157.438 167.353 101.370 1.00 62.40  ? 96  TYR A CZ  1 
ATOM   4104 O OH  . TYR B 2 105 ? 156.946 166.075 101.255 1.00 67.45  ? 96  TYR A OH  1 
ATOM   4105 N N   . GLU B 2 106 ? 161.636 171.910 100.353 1.00 48.22  ? 97  GLU A N   1 
ATOM   4106 C CA  . GLU B 2 106 ? 162.943 171.371 99.979  1.00 48.51  ? 97  GLU A CA  1 
ATOM   4107 C C   . GLU B 2 106 ? 163.660 171.041 101.281 1.00 43.85  ? 97  GLU A C   1 
ATOM   4108 O O   . GLU B 2 106 ? 164.190 171.930 101.950 1.00 47.41  ? 97  GLU A O   1 
ATOM   4109 C CB  . GLU B 2 106 ? 163.745 172.348 99.127  1.00 51.33  ? 97  GLU A CB  1 
ATOM   4110 C CG  . GLU B 2 106 ? 163.325 172.395 97.673  1.00 61.43  ? 97  GLU A CG  1 
ATOM   4111 C CD  . GLU B 2 106 ? 164.340 171.750 96.754  1.00 68.84  ? 97  GLU A CD  1 
ATOM   4112 O OE1 . GLU B 2 106 ? 165.330 171.188 97.264  1.00 66.99  ? 97  GLU A OE1 1 
ATOM   4113 O OE2 . GLU B 2 106 ? 164.147 171.804 95.523  1.00 74.48  ? 97  GLU A OE2 1 
ATOM   4114 N N   . ILE B 2 107 ? 163.671 169.767 101.641 1.00 47.13  ? 98  ILE A N   1 
ATOM   4115 C CA  . ILE B 2 107 ? 164.295 169.333 102.884 1.00 50.40  ? 98  ILE A CA  1 
ATOM   4116 C C   . ILE B 2 107 ? 165.735 168.938 102.599 1.00 52.76  ? 98  ILE A C   1 
ATOM   4117 O O   . ILE B 2 107 ? 166.006 168.156 101.683 1.00 68.12  ? 98  ILE A O   1 
ATOM   4118 C CB  . ILE B 2 107 ? 163.508 168.171 103.507 1.00 52.30  ? 98  ILE A CB  1 
ATOM   4119 C CG1 . ILE B 2 107 ? 162.134 168.658 103.961 1.00 53.59  ? 98  ILE A CG1 1 
ATOM   4120 C CG2 . ILE B 2 107 ? 164.272 167.585 104.674 1.00 48.08  ? 98  ILE A CG2 1 
ATOM   4121 C CD1 . ILE B 2 107 ? 161.239 167.569 104.471 1.00 54.16  ? 98  ILE A CD1 1 
ATOM   4122 N N   . VAL B 2 108 ? 166.664 169.487 103.375 1.00 50.29  ? 99  VAL A N   1 
ATOM   4123 C CA  . VAL B 2 108 ? 168.082 169.191 103.238 1.00 56.96  ? 99  VAL A CA  1 
ATOM   4124 C C   . VAL B 2 108 ? 168.590 168.640 104.560 1.00 62.17  ? 99  VAL A C   1 
ATOM   4125 O O   . VAL B 2 108 ? 168.346 169.213 105.627 1.00 63.31  ? 99  VAL A O   1 
ATOM   4126 C CB  . VAL B 2 108 ? 168.897 170.436 102.817 1.00 53.60  ? 99  VAL A CB  1 
ATOM   4127 C CG1 . VAL B 2 108 ? 170.381 170.130 102.829 1.00 56.70  ? 99  VAL A CG1 1 
ATOM   4128 C CG2 . VAL B 2 108 ? 168.467 170.914 101.444 1.00 52.48  ? 99  VAL A CG2 1 
ATOM   4129 N N   . ASP B 2 109 ? 169.295 167.515 104.488 1.00 70.25  ? 100 ASP A N   1 
ATOM   4130 C CA  . ASP B 2 109 ? 169.900 166.907 105.665 1.00 73.31  ? 100 ASP A CA  1 
ATOM   4131 C C   . ASP B 2 109 ? 171.007 167.820 106.173 1.00 73.73  ? 100 ASP A C   1 
ATOM   4132 O O   . ASP B 2 109 ? 171.988 168.072 105.466 1.00 77.49  ? 100 ASP A O   1 
ATOM   4133 C CB  . ASP B 2 109 ? 170.446 165.517 105.344 1.00 80.55  ? 100 ASP A CB  1 
ATOM   4134 C CG  . ASP B 2 109 ? 171.364 164.978 106.431 1.00 86.92  ? 100 ASP A CG  1 
ATOM   4135 O OD1 . ASP B 2 109 ? 171.121 165.259 107.623 1.00 86.58  ? 100 ASP A OD1 1 
ATOM   4136 O OD2 . ASP B 2 109 ? 172.329 164.263 106.091 1.00 91.92  ? 100 ASP A OD2 1 
ATOM   4137 N N   . VAL B 2 110 ? 170.846 168.313 107.395 1.00 72.95  ? 101 VAL A N   1 
ATOM   4138 C CA  . VAL B 2 110 ? 171.820 169.179 108.043 1.00 75.07  ? 101 VAL A CA  1 
ATOM   4139 C C   . VAL B 2 110 ? 172.502 168.359 109.127 1.00 85.67  ? 101 VAL A C   1 
ATOM   4140 O O   . VAL B 2 110 ? 171.947 167.358 109.596 1.00 87.11  ? 101 VAL A O   1 
ATOM   4141 C CB  . VAL B 2 110 ? 171.153 170.439 108.625 1.00 71.31  ? 101 VAL A CB  1 
ATOM   4142 C CG1 . VAL B 2 110 ? 170.493 170.139 109.962 1.00 74.50  ? 101 VAL A CG1 1 
ATOM   4143 C CG2 . VAL B 2 110 ? 172.147 171.569 108.761 1.00 74.84  ? 101 VAL A CG2 1 
ATOM   4144 N N   . CYS B 2 111 ? 173.711 168.755 109.501 1.00 92.35  ? 102 CYS A N   1 
ATOM   4145 C CA  . CYS B 2 111 ? 174.381 168.091 110.604 1.00 94.17  ? 102 CYS A CA  1 
ATOM   4146 C C   . CYS B 2 111 ? 174.272 168.936 111.869 1.00 97.51  ? 102 CYS A C   1 
ATOM   4147 O O   . CYS B 2 111 ? 173.785 170.070 111.854 1.00 96.94  ? 102 CYS A O   1 
ATOM   4148 C CB  . CYS B 2 111 ? 175.842 167.817 110.263 1.00 99.96  ? 102 CYS A CB  1 
ATOM   4149 S SG  . CYS B 2 111 ? 176.148 166.148 109.654 1.00 105.86 ? 102 CYS A SG  1 
ATOM   4150 N N   . TYR B 2 112 ? 174.724 168.361 112.984 1.00 97.99  ? 103 TYR A N   1 
ATOM   4151 C CA  . TYR B 2 112 ? 174.682 169.083 114.250 1.00 101.31 ? 103 TYR A CA  1 
ATOM   4152 C C   . TYR B 2 112 ? 175.579 170.316 114.197 1.00 101.82 ? 103 TYR A C   1 
ATOM   4153 O O   . TYR B 2 112 ? 175.177 171.409 114.608 1.00 99.13  ? 103 TYR A O   1 
ATOM   4154 C CB  . TYR B 2 112 ? 175.076 168.138 115.390 1.00 102.49 ? 103 TYR A CB  1 
ATOM   4155 C CG  . TYR B 2 112 ? 175.619 168.799 116.638 1.00 103.81 ? 103 TYR A CG  1 
ATOM   4156 C CD1 . TYR B 2 112 ? 174.814 169.616 117.421 1.00 104.29 ? 103 TYR A CD1 1 
ATOM   4157 C CD2 . TYR B 2 112 ? 176.921 168.567 117.059 1.00 102.68 ? 103 TYR A CD2 1 
ATOM   4158 C CE1 . TYR B 2 112 ? 175.302 170.210 118.570 1.00 106.06 ? 103 TYR A CE1 1 
ATOM   4159 C CE2 . TYR B 2 112 ? 177.416 169.154 118.207 1.00 107.36 ? 103 TYR A CE2 1 
ATOM   4160 C CZ  . TYR B 2 112 ? 176.603 169.974 118.958 1.00 111.19 ? 103 TYR A CZ  1 
ATOM   4161 O OH  . TYR B 2 112 ? 177.094 170.560 120.102 1.00 110.63 ? 103 TYR A OH  1 
ATOM   4162 N N   . ILE B 2 113 ? 176.799 170.162 113.677 1.00 99.23  ? 104 ILE A N   1 
ATOM   4163 C CA  . ILE B 2 113 ? 177.707 171.279 113.457 1.00 102.50 ? 104 ILE A CA  1 
ATOM   4164 C C   . ILE B 2 113 ? 178.245 171.306 112.032 1.00 100.19 ? 104 ILE A C   1 
ATOM   4165 O O   . ILE B 2 113 ? 178.312 172.373 111.411 1.00 95.82  ? 104 ILE A O   1 
ATOM   4166 C CB  . ILE B 2 113 ? 178.869 171.265 114.476 1.00 111.80 ? 104 ILE A CB  1 
ATOM   4167 C CG1 . ILE B 2 113 ? 178.347 171.575 115.878 1.00 105.50 ? 104 ILE A CG1 1 
ATOM   4168 C CG2 . ILE B 2 113 ? 179.946 172.270 114.090 1.00 103.49 ? 104 ILE A CG2 1 
ATOM   4169 C CD1 . ILE B 2 113 ? 177.693 172.932 115.994 1.00 93.05  ? 104 ILE A CD1 1 
ATOM   4170 N N   . SER B 2 114 ? 178.626 170.144 111.494 1.00 104.46 ? 105 SER A N   1 
ATOM   4171 C CA  . SER B 2 114 ? 179.428 170.020 110.278 1.00 107.51 ? 105 SER A CA  1 
ATOM   4172 C C   . SER B 2 114 ? 178.967 170.896 109.117 1.00 108.57 ? 105 SER A C   1 
ATOM   4173 O O   . SER B 2 114 ? 179.711 171.775 108.670 1.00 110.53 ? 105 SER A O   1 
ATOM   4174 C CB  . SER B 2 114 ? 179.455 168.558 109.824 1.00 104.57 ? 105 SER A CB  1 
ATOM   4175 O OG  . SER B 2 114 ? 179.625 167.683 110.925 1.00 114.18 ? 105 SER A OG  1 
ATOM   4176 N N   . ASN B 2 115 ? 177.745 170.672 108.623 1.00 100.97 ? 106 ASN A N   1 
ATOM   4177 C CA  . ASN B 2 115 ? 177.294 171.423 107.416 1.00 99.10  ? 106 ASN A CA  1 
ATOM   4178 C C   . ASN B 2 115 ? 176.086 172.309 107.736 1.00 91.28  ? 106 ASN A C   1 
ATOM   4179 O O   . ASN B 2 115 ? 174.968 171.763 107.802 1.00 91.17  ? 106 ASN A O   1 
ATOM   4180 C CB  . ASN B 2 115 ? 176.989 170.478 106.258 1.00 96.63  ? 106 ASN A CB  1 
ATOM   4181 C CG  . ASN B 2 115 ? 176.491 171.212 105.035 1.00 90.91  ? 106 ASN A CG  1 
ATOM   4182 O OD1 . ASN B 2 115 ? 177.018 172.275 104.687 1.00 87.29  ? 106 ASN A OD1 1 
ATOM   4183 N ND2 . ASN B 2 115 ? 175.481 170.666 104.373 1.00 80.80  ? 106 ASN A ND2 1 
ATOM   4184 N N   . ASN B 2 116 ? 176.295 173.621 107.890 1.00 81.96  ? 107 ASN A N   1 
ATOM   4185 C CA  . ASN B 2 116 ? 175.155 174.557 108.112 1.00 77.95  ? 107 ASN A CA  1 
ATOM   4186 C C   . ASN B 2 116 ? 175.339 175.797 107.230 1.00 69.73  ? 107 ASN A C   1 
ATOM   4187 O O   . ASN B 2 116 ? 174.904 176.891 107.651 1.00 71.28  ? 107 ASN A O   1 
ATOM   4188 C CB  . ASN B 2 116 ? 174.995 174.941 109.580 1.00 83.04  ? 107 ASN A CB  1 
ATOM   4189 C CG  . ASN B 2 116 ? 175.783 174.049 110.508 1.00 84.43  ? 107 ASN A CG  1 
ATOM   4190 O OD1 . ASN B 2 116 ? 175.370 172.916 110.784 1.00 85.83  ? 107 ASN A OD1 1 
ATOM   4191 N ND2 . ASN B 2 116 ? 176.909 174.539 111.005 1.00 80.93  ? 107 ASN A ND2 1 
ATOM   4192 N N   . VAL B 2 117 ? 175.959 175.634 106.056 1.00 64.47  ? 108 VAL A N   1 
ATOM   4193 C CA  . VAL B 2 117 ? 176.228 176.795 105.152 1.00 58.42  ? 108 VAL A CA  1 
ATOM   4194 C C   . VAL B 2 117 ? 175.592 176.524 103.778 1.00 57.82  ? 108 VAL A C   1 
ATOM   4195 O O   . VAL B 2 117 ? 174.666 177.274 103.401 1.00 62.12  ? 108 VAL A O   1 
ATOM   4196 C CB  . VAL B 2 117 ? 177.737 177.076 105.013 1.00 57.59  ? 108 VAL A CB  1 
ATOM   4197 C CG1 . VAL B 2 117 ? 178.013 178.231 104.057 1.00 49.72  ? 108 VAL A CG1 1 
ATOM   4198 C CG2 . VAL B 2 117 ? 178.397 177.329 106.364 1.00 50.85  ? 108 VAL A CG2 1 
ATOM   4199 N N   . GLN B 2 118 ? 176.074 175.504 103.063 1.00 59.75  ? 109 GLN A N   1 
ATOM   4200 C CA  . GLN B 2 118 ? 175.555 175.205 101.707 1.00 60.85  ? 109 GLN A CA  1 
ATOM   4201 C C   . GLN B 2 118 ? 174.022 175.133 101.738 1.00 64.25  ? 109 GLN A C   1 
ATOM   4202 O O   . GLN B 2 118 ? 173.412 175.817 100.911 1.00 64.80  ? 109 GLN A O   1 
ATOM   4203 C CB  . GLN B 2 118 ? 176.119 173.904 101.138 1.00 68.45  ? 109 GLN A CB  1 
ATOM   4204 C CG  . GLN B 2 118 ? 175.390 173.387 99.903  1.00 75.70  ? 109 GLN A CG  1 
ATOM   4205 C CD  . GLN B 2 118 ? 174.571 172.146 100.179 1.00 80.20  ? 109 GLN A CD  1 
ATOM   4206 O OE1 . GLN B 2 118 ? 174.916 171.324 101.034 1.00 82.64  ? 109 GLN A OE1 1 
ATOM   4207 N NE2 . GLN B 2 118 ? 173.468 171.999 99.459  1.00 76.88  ? 109 GLN A NE2 1 
ATOM   4208 N N   . PRO B 2 119 ? 173.361 174.354 102.624 1.00 62.58  ? 110 PRO A N   1 
ATOM   4209 C CA  . PRO B 2 119 ? 171.884 174.326 102.718 1.00 57.10  ? 110 PRO A CA  1 
ATOM   4210 C C   . PRO B 2 119 ? 171.299 175.726 102.591 1.00 56.97  ? 110 PRO A C   1 
ATOM   4211 O O   . PRO B 2 119 ? 170.350 175.895 101.804 1.00 58.30  ? 110 PRO A O   1 
ATOM   4212 C CB  . PRO B 2 119 ? 171.665 173.727 104.087 1.00 55.26  ? 110 PRO A CB  1 
ATOM   4213 C CG  . PRO B 2 119 ? 173.008 173.614 104.767 1.00 59.27  ? 110 PRO A CG  1 
ATOM   4214 C CD  . PRO B 2 119 ? 173.940 173.423 103.635 1.00 63.86  ? 110 PRO A CD  1 
ATOM   4215 N N   . VAL B 2 120 ? 171.848 176.706 103.312 1.00 58.15  ? 111 VAL A N   1 
ATOM   4216 C CA  . VAL B 2 120 ? 171.352 178.078 103.326 1.00 52.04  ? 111 VAL A CA  1 
ATOM   4217 C C   . VAL B 2 120 ? 171.636 178.761 101.995 1.00 55.26  ? 111 VAL A C   1 
ATOM   4218 O O   . VAL B 2 120 ? 170.771 179.446 101.433 1.00 58.07  ? 111 VAL A O   1 
ATOM   4219 C CB  . VAL B 2 120 ? 171.967 178.855 104.503 1.00 53.44  ? 111 VAL A CB  1 
ATOM   4220 C CG1 . VAL B 2 120 ? 171.118 180.065 104.830 1.00 55.94  ? 111 VAL A CG1 1 
ATOM   4221 C CG2 . VAL B 2 120 ? 172.104 177.955 105.714 1.00 57.66  ? 111 VAL A CG2 1 
ATOM   4222 N N   . LEU B 2 121 ? 172.853 178.587 101.471 1.00 58.93  ? 112 LEU A N   1 
ATOM   4223 C CA  . LEU B 2 121 ? 173.187 179.137 100.161 1.00 56.17  ? 112 LEU A CA  1 
ATOM   4224 C C   . LEU B 2 121 ? 172.280 178.569 99.079  1.00 56.00  ? 112 LEU A C   1 
ATOM   4225 O O   . LEU B 2 121 ? 171.955 179.257 98.105  1.00 52.85  ? 112 LEU A O   1 
ATOM   4226 C CB  . LEU B 2 121 ? 174.651 178.846 99.836  1.00 57.49  ? 112 LEU A CB  1 
ATOM   4227 C CG  . LEU B 2 121 ? 175.646 180.001 99.892  1.00 56.10  ? 112 LEU A CG  1 
ATOM   4228 C CD1 . LEU B 2 121 ? 176.997 179.542 99.384  1.00 56.91  ? 112 LEU A CD1 1 
ATOM   4229 C CD2 . LEU B 2 121 ? 175.140 181.163 99.065  1.00 60.05  ? 112 LEU A CD2 1 
ATOM   4230 N N   . TYR B 2 122 ? 171.873 177.308 99.227  1.00 59.60  ? 113 TYR A N   1 
ATOM   4231 C CA  . TYR B 2 122 ? 171.005 176.683 98.236  1.00 57.40  ? 113 TYR A CA  1 
ATOM   4232 C C   . TYR B 2 122 ? 169.577 177.204 98.350  1.00 57.35  ? 113 TYR A C   1 
ATOM   4233 O O   . TYR B 2 122 ? 168.903 177.410 97.336  1.00 60.04  ? 113 TYR A O   1 
ATOM   4234 C CB  . TYR B 2 122 ? 171.051 175.164 98.407  1.00 62.56  ? 113 TYR A CB  1 
ATOM   4235 C CG  . TYR B 2 122 ? 170.006 174.404 97.627  1.00 70.93  ? 113 TYR A CG  1 
ATOM   4236 C CD1 . TYR B 2 122 ? 169.983 174.446 96.241  1.00 74.96  ? 113 TYR A CD1 1 
ATOM   4237 C CD2 . TYR B 2 122 ? 169.070 173.610 98.274  1.00 66.51  ? 113 TYR A CD2 1 
ATOM   4238 C CE1 . TYR B 2 122 ? 169.044 173.738 95.524  1.00 74.76  ? 113 TYR A CE1 1 
ATOM   4239 C CE2 . TYR B 2 122 ? 168.123 172.904 97.563  1.00 64.15  ? 113 TYR A CE2 1 
ATOM   4240 C CZ  . TYR B 2 122 ? 168.114 172.974 96.188  1.00 68.77  ? 113 TYR A CZ  1 
ATOM   4241 O OH  . TYR B 2 122 ? 167.177 172.272 95.469  1.00 71.08  ? 113 TYR A OH  1 
ATOM   4242 N N   . PHE B 2 123 ? 169.100 177.412 99.581  1.00 56.63  ? 114 PHE A N   1 
ATOM   4243 C CA  . PHE B 2 123 ? 167.763 177.964 99.788  1.00 52.19  ? 114 PHE A CA  1 
ATOM   4244 C C   . PHE B 2 123 ? 167.662 179.386 99.258  1.00 52.50  ? 114 PHE A C   1 
ATOM   4245 O O   . PHE B 2 123 ? 166.649 179.762 98.657  1.00 50.80  ? 114 PHE A O   1 
ATOM   4246 C CB  . PHE B 2 123 ? 167.405 177.938 101.275 1.00 42.27  ? 114 PHE A CB  1 
ATOM   4247 C CG  . PHE B 2 123 ? 167.071 176.575 101.800 1.00 42.79  ? 114 PHE A CG  1 
ATOM   4248 C CD1 . PHE B 2 123 ? 166.628 175.577 100.953 1.00 47.33  ? 114 PHE A CD1 1 
ATOM   4249 C CD2 . PHE B 2 123 ? 167.204 176.292 103.146 1.00 38.92  ? 114 PHE A CD2 1 
ATOM   4250 C CE1 . PHE B 2 123 ? 166.325 174.324 101.440 1.00 40.34  ? 114 PHE A CE1 1 
ATOM   4251 C CE2 . PHE B 2 123 ? 166.903 175.043 103.636 1.00 35.60  ? 114 PHE A CE2 1 
ATOM   4252 C CZ  . PHE B 2 123 ? 166.466 174.058 102.782 1.00 37.13  ? 114 PHE A CZ  1 
ATOM   4253 N N   . LEU B 2 124 ? 168.695 180.199 99.486  1.00 51.00  ? 115 LEU A N   1 
ATOM   4254 C CA  . LEU B 2 124 ? 168.640 181.598 99.077  1.00 53.73  ? 115 LEU A CA  1 
ATOM   4255 C C   . LEU B 2 124 ? 168.851 181.787 97.581  1.00 60.01  ? 115 LEU A C   1 
ATOM   4256 O O   . LEU B 2 124 ? 168.410 182.799 97.033  1.00 64.44  ? 115 LEU A O   1 
ATOM   4257 C CB  . LEU B 2 124 ? 169.670 182.411 99.855  1.00 52.16  ? 115 LEU A CB  1 
ATOM   4258 C CG  . LEU B 2 124 ? 169.330 182.586 101.333 1.00 48.86  ? 115 LEU A CG  1 
ATOM   4259 C CD1 . LEU B 2 124 ? 170.552 182.994 102.123 1.00 49.15  ? 115 LEU A CD1 1 
ATOM   4260 C CD2 . LEU B 2 124 ? 168.223 183.602 101.491 1.00 49.63  ? 115 LEU A CD2 1 
ATOM   4261 N N   . ALA B 2 125 ? 169.507 180.845 96.912  1.00 63.15  ? 116 ALA A N   1 
ATOM   4262 C CA  . ALA B 2 125 ? 169.798 180.995 95.497  1.00 63.14  ? 116 ALA A CA  1 
ATOM   4263 C C   . ALA B 2 125 ? 168.537 180.796 94.657  1.00 71.93  ? 116 ALA A C   1 
ATOM   4264 O O   . ALA B 2 125 ? 167.505 180.315 95.130  1.00 75.38  ? 116 ALA A O   1 
ATOM   4265 C CB  . ALA B 2 125 ? 170.881 180.006 95.069  1.00 66.80  ? 116 ALA A CB  1 
ATOM   4266 N N   . HIS B 2 126 ? 168.636 181.177 93.387  1.00 79.76  ? 117 HIS A N   1 
ATOM   4267 C CA  . HIS B 2 126 ? 167.552 180.996 92.431  1.00 82.34  ? 117 HIS A CA  1 
ATOM   4268 C C   . HIS B 2 126 ? 167.523 179.542 91.966  1.00 91.30  ? 117 HIS A C   1 
ATOM   4269 O O   . HIS B 2 126 ? 168.299 178.701 92.427  1.00 91.76  ? 117 HIS A O   1 
ATOM   4270 C CB  . HIS B 2 126 ? 167.714 181.961 91.261  1.00 80.55  ? 117 HIS A CB  1 
ATOM   4271 C CG  . HIS B 2 126 ? 167.034 183.278 91.462  1.00 85.73  ? 117 HIS A CG  1 
ATOM   4272 N ND1 . HIS B 2 126 ? 167.559 184.465 90.996  1.00 90.66  ? 117 HIS A ND1 1 
ATOM   4273 C CD2 . HIS B 2 126 ? 165.867 183.596 92.068  1.00 85.54  ? 117 HIS A CD2 1 
ATOM   4274 C CE1 . HIS B 2 126 ? 166.748 185.457 91.314  1.00 82.50  ? 117 HIS A CE1 1 
ATOM   4275 N NE2 . HIS B 2 126 ? 165.713 184.957 91.964  1.00 79.93  ? 117 HIS A NE2 1 
ATOM   4276 N N   . GLU B 2 127 ? 166.624 179.230 91.028  1.00 94.97  ? 118 GLU A N   1 
ATOM   4277 C CA  . GLU B 2 127 ? 166.519 177.877 90.491  1.00 97.16  ? 118 GLU A CA  1 
ATOM   4278 C C   . GLU B 2 127 ? 167.755 177.447 89.714  1.00 95.82  ? 118 GLU A C   1 
ATOM   4279 O O   . GLU B 2 127 ? 167.912 176.251 89.448  1.00 94.83  ? 118 GLU A O   1 
ATOM   4280 C CB  . GLU B 2 127 ? 165.286 177.759 89.594  1.00 97.17  ? 118 GLU A CB  1 
ATOM   4281 C CG  . GLU B 2 127 ? 163.981 178.154 90.263  1.00 102.99 ? 118 GLU A CG  1 
ATOM   4282 C CD  . GLU B 2 127 ? 163.338 176.994 90.998  1.00 111.76 ? 118 GLU A CD  1 
ATOM   4283 O OE1 . GLU B 2 127 ? 163.786 175.845 90.799  1.00 114.50 ? 118 GLU A OE1 1 
ATOM   4284 O OE2 . GLU B 2 127 ? 162.384 177.229 91.769  1.00 104.79 ? 118 GLU A OE2 1 
ATOM   4285 N N   . ASP B 2 128 ? 168.628 178.381 89.345  1.00 95.12  ? 119 ASP A N   1 
ATOM   4286 C CA  . ASP B 2 128 ? 169.870 178.073 88.652  1.00 97.91  ? 119 ASP A CA  1 
ATOM   4287 C C   . ASP B 2 128 ? 171.062 178.003 89.597  1.00 96.57  ? 119 ASP A C   1 
ATOM   4288 O O   . ASP B 2 128 ? 172.207 178.055 89.137  1.00 96.66  ? 119 ASP A O   1 
ATOM   4289 C CB  . ASP B 2 128 ? 170.127 179.100 87.546  1.00 99.02  ? 119 ASP A CB  1 
ATOM   4290 C CG  . ASP B 2 128 ? 170.042 180.536 88.040  1.00 97.46  ? 119 ASP A CG  1 
ATOM   4291 O OD1 . ASP B 2 128 ? 170.079 180.762 89.267  1.00 94.25  ? 119 ASP A OD1 1 
ATOM   4292 O OD2 . ASP B 2 128 ? 169.932 181.446 87.192  1.00 98.96  ? 119 ASP A OD2 1 
ATOM   4293 N N   . ASN B 2 129 ? 170.815 177.887 90.904  1.00 92.36  ? 120 ASN A N   1 
ATOM   4294 C CA  . ASN B 2 129 ? 171.869 177.816 91.917  1.00 90.81  ? 120 ASN A CA  1 
ATOM   4295 C C   . ASN B 2 129 ? 172.800 179.023 91.826  1.00 91.58  ? 120 ASN A C   1 
ATOM   4296 O O   . ASN B 2 129 ? 174.023 178.903 91.897  1.00 89.49  ? 120 ASN A O   1 
ATOM   4297 C CB  . ASN B 2 129 ? 172.653 176.506 91.811  1.00 88.21  ? 120 ASN A CB  1 
ATOM   4298 C CG  . ASN B 2 129 ? 171.812 175.293 92.151  1.00 94.66  ? 120 ASN A CG  1 
ATOM   4299 O OD1 . ASN B 2 129 ? 171.979 174.684 93.208  1.00 92.31  ? 120 ASN A OD1 1 
ATOM   4300 N ND2 . ASN B 2 129 ? 170.905 174.930 91.252  1.00 97.27  ? 120 ASN A ND2 1 
ATOM   4301 N N   . LEU B 2 130 ? 172.201 180.202 91.669  1.00 90.80  ? 121 LEU A N   1 
ATOM   4302 C CA  . LEU B 2 130 ? 172.944 181.448 91.553  1.00 84.67  ? 121 LEU A CA  1 
ATOM   4303 C C   . LEU B 2 130 ? 172.263 182.509 92.403  1.00 80.30  ? 121 LEU A C   1 
ATOM   4304 O O   . LEU B 2 130 ? 171.095 182.833 92.172  1.00 81.24  ? 121 LEU A O   1 
ATOM   4305 C CB  . LEU B 2 130 ? 173.023 181.907 90.093  1.00 88.35  ? 121 LEU A CB  1 
ATOM   4306 C CG  . LEU B 2 130 ? 174.405 182.248 89.536  1.00 88.16  ? 121 LEU A CG  1 
ATOM   4307 C CD1 . LEU B 2 130 ? 175.398 181.137 89.824  1.00 81.23  ? 121 LEU A CD1 1 
ATOM   4308 C CD2 . LEU B 2 130 ? 174.323 182.519 88.043  1.00 87.31  ? 121 LEU A CD2 1 
ATOM   4309 N N   . LEU B 2 131 ? 172.991 183.043 93.382  1.00 77.24  ? 122 LEU A N   1 
ATOM   4310 C CA  . LEU B 2 131 ? 172.465 184.051 94.290  1.00 75.98  ? 122 LEU A CA  1 
ATOM   4311 C C   . LEU B 2 131 ? 173.147 185.387 94.043  1.00 77.39  ? 122 LEU A C   1 
ATOM   4312 O O   . LEU B 2 131 ? 174.370 185.493 94.205  1.00 79.44  ? 122 LEU A O   1 
ATOM   4313 C CB  . LEU B 2 131 ? 172.663 183.621 95.748  1.00 71.31  ? 122 LEU A CB  1 
ATOM   4314 C CG  . LEU B 2 131 ? 172.679 184.739 96.790  1.00 65.71  ? 122 LEU A CG  1 
ATOM   4315 C CD1 . LEU B 2 131 ? 171.276 185.255 97.036  1.00 58.88  ? 122 LEU A CD1 1 
ATOM   4316 C CD2 . LEU B 2 131 ? 173.314 184.265 98.083  1.00 65.04  ? 122 LEU A CD2 1 
ATOM   4317 N N   . PRO B 2 132 ? 172.407 186.414 93.636  1.00 78.15  ? 123 PRO A N   1 
ATOM   4318 C CA  . PRO B 2 132 ? 173.034 187.708 93.348  1.00 77.79  ? 123 PRO A CA  1 
ATOM   4319 C C   . PRO B 2 132 ? 173.468 188.426 94.615  1.00 74.60  ? 123 PRO A C   1 
ATOM   4320 O O   . PRO B 2 132 ? 172.919 188.217 95.699  1.00 76.86  ? 123 PRO A O   1 
ATOM   4321 C CB  . PRO B 2 132 ? 171.926 188.488 92.629  1.00 74.83  ? 123 PRO A CB  1 
ATOM   4322 C CG  . PRO B 2 132 ? 170.899 187.461 92.249  1.00 80.92  ? 123 PRO A CG  1 
ATOM   4323 C CD  . PRO B 2 132 ? 170.976 186.417 93.306  1.00 75.68  ? 123 PRO A CD  1 
ATOM   4324 N N   . ILE B 2 133 ? 174.451 189.305 94.465  1.00 73.20  ? 124 ILE A N   1 
ATOM   4325 C CA  . ILE B 2 133 ? 174.946 190.124 95.564  1.00 72.34  ? 124 ILE A CA  1 
ATOM   4326 C C   . ILE B 2 133 ? 174.520 191.557 95.290  1.00 78.72  ? 124 ILE A C   1 
ATOM   4327 O O   . ILE B 2 133 ? 174.912 192.153 94.279  1.00 80.29  ? 124 ILE A O   1 
ATOM   4328 C CB  . ILE B 2 133 ? 176.466 190.016 95.722  1.00 77.30  ? 124 ILE A CB  1 
ATOM   4329 C CG1 . ILE B 2 133 ? 176.879 188.548 95.662  1.00 78.27  ? 124 ILE A CG1 1 
ATOM   4330 C CG2 . ILE B 2 133 ? 176.905 190.651 97.039  1.00 68.95  ? 124 ILE A CG2 1 
ATOM   4331 C CD1 . ILE B 2 133 ? 176.730 187.837 96.959  1.00 67.19  ? 124 ILE A CD1 1 
ATOM   4332 N N   . GLN B 2 134 ? 173.707 192.106 96.186  1.00 76.18  ? 125 GLN A N   1 
ATOM   4333 C CA  . GLN B 2 134 ? 173.138 193.432 96.008  1.00 69.27  ? 125 GLN A CA  1 
ATOM   4334 C C   . GLN B 2 134 ? 172.817 194.016 97.376  1.00 72.24  ? 125 GLN A C   1 
ATOM   4335 O O   . GLN B 2 134 ? 172.632 193.291 98.354  1.00 73.12  ? 125 GLN A O   1 
ATOM   4336 C CB  . GLN B 2 134 ? 171.909 193.374 95.096  1.00 59.91  ? 125 GLN A CB  1 
ATOM   4337 C CG  . GLN B 2 134 ? 170.744 192.566 95.665  1.00 65.16  ? 125 GLN A CG  1 
ATOM   4338 C CD  . GLN B 2 134 ? 169.541 192.525 94.741  1.00 68.65  ? 125 GLN A CD  1 
ATOM   4339 O OE1 . GLN B 2 134 ? 169.650 192.767 93.544  1.00 70.02  ? 125 GLN A OE1 1 
ATOM   4340 N NE2 . GLN B 2 134 ? 168.380 192.220 95.303  1.00 66.19  ? 125 GLN A NE2 1 
ATOM   4341 N N   . GLU B 2 135 ? 172.765 195.349 97.435  1.00 75.53  ? 126 GLU A N   1 
ATOM   4342 C CA  . GLU B 2 135 ? 172.586 196.030 98.712  1.00 74.99  ? 126 GLU A CA  1 
ATOM   4343 C C   . GLU B 2 135 ? 171.160 195.900 99.230  1.00 76.46  ? 126 GLU A C   1 
ATOM   4344 O O   . GLU B 2 135 ? 170.949 195.758 100.439 1.00 79.42  ? 126 GLU A O   1 
ATOM   4345 C CB  . GLU B 2 135 ? 172.967 197.504 98.581  1.00 75.72  ? 126 GLU A CB  1 
ATOM   4346 C CG  . GLU B 2 135 ? 174.442 197.751 98.310  1.00 86.28  ? 126 GLU A CG  1 
ATOM   4347 C CD  . GLU B 2 135 ? 175.162 198.314 99.522  1.00 96.15  ? 126 GLU A CD  1 
ATOM   4348 O OE1 . GLU B 2 135 ? 174.743 199.378 100.026 1.00 95.74  ? 126 GLU A OE1 1 
ATOM   4349 O OE2 . GLU B 2 135 ? 176.146 197.691 99.972  1.00 94.25  ? 126 GLU A OE2 1 
ATOM   4350 N N   . ASP B 2 136 ? 170.173 195.953 98.343  1.00 76.25  ? 127 ASP A N   1 
ATOM   4351 C CA  . ASP B 2 136 ? 168.776 195.843 98.732  1.00 68.82  ? 127 ASP A CA  1 
ATOM   4352 C C   . ASP B 2 136 ? 168.201 194.523 98.243  1.00 65.62  ? 127 ASP A C   1 
ATOM   4353 O O   . ASP B 2 136 ? 168.345 194.165 97.070  1.00 67.38  ? 127 ASP A O   1 
ATOM   4354 C CB  . ASP B 2 136 ? 167.949 197.005 98.179  1.00 75.39  ? 127 ASP A CB  1 
ATOM   4355 C CG  . ASP B 2 136 ? 166.895 197.481 99.156  1.00 79.94  ? 127 ASP A CG  1 
ATOM   4356 O OD1 . ASP B 2 136 ? 167.196 197.547 100.365 1.00 78.24  ? 127 ASP A OD1 1 
ATOM   4357 O OD2 . ASP B 2 136 ? 165.766 197.787 98.720  1.00 77.21  ? 127 ASP A OD2 1 
ATOM   4358 N N   . TYR B 2 137 ? 167.549 193.805 99.156  1.00 62.54  ? 128 TYR A N   1 
ATOM   4359 C CA  . TYR B 2 137 ? 166.905 192.533 98.859  1.00 64.91  ? 128 TYR A CA  1 
ATOM   4360 C C   . TYR B 2 137 ? 165.392 192.619 99.020  1.00 63.34  ? 128 TYR A C   1 
ATOM   4361 O O   . TYR B 2 137 ? 164.731 191.593 99.197  1.00 67.25  ? 128 TYR A O   1 
ATOM   4362 C CB  . TYR B 2 137 ? 167.472 191.430 99.755  1.00 62.31  ? 128 TYR A CB  1 
ATOM   4363 C CG  . TYR B 2 137 ? 168.833 190.930 99.335  1.00 58.40  ? 128 TYR A CG  1 
ATOM   4364 C CD1 . TYR B 2 137 ? 168.994 190.185 98.176  1.00 57.93  ? 128 TYR A CD1 1 
ATOM   4365 C CD2 . TYR B 2 137 ? 169.959 191.209 100.094 1.00 56.45  ? 128 TYR A CD2 1 
ATOM   4366 C CE1 . TYR B 2 137 ? 170.236 189.730 97.789  1.00 57.28  ? 128 TYR A CE1 1 
ATOM   4367 C CE2 . TYR B 2 137 ? 171.204 190.758 99.713  1.00 59.82  ? 128 TYR A CE2 1 
ATOM   4368 C CZ  . TYR B 2 137 ? 171.336 190.019 98.560  1.00 61.64  ? 128 TYR A CZ  1 
ATOM   4369 O OH  . TYR B 2 137 ? 172.574 189.564 98.175  1.00 66.41  ? 128 TYR A OH  1 
ATOM   4370 N N   . SER B 2 138 ? 164.833 193.830 98.976  1.00 62.49  ? 129 SER A N   1 
ATOM   4371 C CA  . SER B 2 138 ? 163.398 193.993 99.183  1.00 62.23  ? 129 SER A CA  1 
ATOM   4372 C C   . SER B 2 138 ? 162.600 193.406 98.028  1.00 60.97  ? 129 SER A C   1 
ATOM   4373 O O   . SER B 2 138 ? 161.452 192.986 98.207  1.00 65.72  ? 129 SER A O   1 
ATOM   4374 C CB  . SER B 2 138 ? 163.062 195.470 99.375  1.00 62.00  ? 129 SER A CB  1 
ATOM   4375 O OG  . SER B 2 138 ? 163.783 196.016 100.464 1.00 66.36  ? 129 SER A OG  1 
ATOM   4376 N N   . ASN B 2 139 ? 163.185 193.373 96.832  1.00 60.66  ? 130 ASN A N   1 
ATOM   4377 C CA  . ASN B 2 139 ? 162.524 192.823 95.656  1.00 62.97  ? 130 ASN A CA  1 
ATOM   4378 C C   . ASN B 2 139 ? 163.185 191.541 95.166  1.00 65.65  ? 130 ASN A C   1 
ATOM   4379 O O   . ASN B 2 139 ? 162.990 191.150 94.012  1.00 71.34  ? 130 ASN A O   1 
ATOM   4380 C CB  . ASN B 2 139 ? 162.488 193.862 94.536  1.00 69.49  ? 130 ASN A CB  1 
ATOM   4381 C CG  . ASN B 2 139 ? 163.692 194.780 94.555  1.00 76.66  ? 130 ASN A CG  1 
ATOM   4382 O OD1 . ASN B 2 139 ? 164.825 194.343 94.354  1.00 71.92  ? 130 ASN A OD1 1 
ATOM   4383 N ND2 . ASN B 2 139 ? 163.452 196.063 94.797  1.00 74.17  ? 130 ASN A ND2 1 
ATOM   4384 N N   . TYR B 2 140 ? 163.959 190.875 96.018  1.00 65.34  ? 131 TYR A N   1 
ATOM   4385 C CA  . TYR B 2 140 ? 164.634 189.640 95.640  1.00 63.95  ? 131 TYR A CA  1 
ATOM   4386 C C   . TYR B 2 140 ? 163.779 188.454 96.065  1.00 64.09  ? 131 TYR A C   1 
ATOM   4387 O O   . TYR B 2 140 ? 163.273 188.419 97.192  1.00 65.20  ? 131 TYR A O   1 
ATOM   4388 C CB  . TYR B 2 140 ? 166.022 189.552 96.272  1.00 63.46  ? 131 TYR A CB  1 
ATOM   4389 C CG  . TYR B 2 140 ? 166.720 188.249 95.973  1.00 59.84  ? 131 TYR A CG  1 
ATOM   4390 C CD1 . TYR B 2 140 ? 167.062 187.916 94.673  1.00 62.18  ? 131 TYR A CD1 1 
ATOM   4391 C CD2 . TYR B 2 140 ? 167.029 187.349 96.982  1.00 58.11  ? 131 TYR A CD2 1 
ATOM   4392 C CE1 . TYR B 2 140 ? 167.691 186.730 94.385  1.00 59.70  ? 131 TYR A CE1 1 
ATOM   4393 C CE2 . TYR B 2 140 ? 167.663 186.158 96.701  1.00 57.71  ? 131 TYR A CE2 1 
ATOM   4394 C CZ  . TYR B 2 140 ? 167.990 185.857 95.399  1.00 60.80  ? 131 TYR A CZ  1 
ATOM   4395 O OH  . TYR B 2 140 ? 168.621 184.677 95.097  1.00 74.61  ? 131 TYR A OH  1 
ATOM   4396 N N   . ILE B 2 141 ? 163.625 187.486 95.168  1.00 62.58  ? 132 ILE A N   1 
ATOM   4397 C CA  . ILE B 2 141 ? 162.784 186.319 95.396  1.00 58.68  ? 132 ILE A CA  1 
ATOM   4398 C C   . ILE B 2 141 ? 163.691 185.106 95.535  1.00 57.93  ? 132 ILE A C   1 
ATOM   4399 O O   . ILE B 2 141 ? 164.413 184.751 94.596  1.00 66.46  ? 132 ILE A O   1 
ATOM   4400 C CB  . ILE B 2 141 ? 161.781 186.125 94.250  1.00 64.56  ? 132 ILE A CB  1 
ATOM   4401 C CG1 . ILE B 2 141 ? 160.667 187.163 94.338  1.00 65.20  ? 132 ILE A CG1 1 
ATOM   4402 C CG2 . ILE B 2 141 ? 161.190 184.726 94.288  1.00 62.05  ? 132 ILE A CG2 1 
ATOM   4403 C CD1 . ILE B 2 141 ? 160.365 187.814 93.012  1.00 59.78  ? 132 ILE A CD1 1 
ATOM   4404 N N   . SER B 2 142 ? 163.656 184.466 96.697  1.00 51.48  ? 133 SER A N   1 
ATOM   4405 C CA  . SER B 2 142 ? 164.452 183.274 96.929  1.00 54.12  ? 133 SER A CA  1 
ATOM   4406 C C   . SER B 2 142 ? 163.662 182.025 96.548  1.00 55.44  ? 133 SER A C   1 
ATOM   4407 O O   . SER B 2 142 ? 162.457 182.072 96.291  1.00 57.93  ? 133 SER A O   1 
ATOM   4408 C CB  . SER B 2 142 ? 164.900 183.202 98.388  1.00 52.99  ? 133 SER A CB  1 
ATOM   4409 O OG  . SER B 2 142 ? 163.866 183.623 99.257  1.00 53.00  ? 133 SER A OG  1 
ATOM   4410 N N   . ARG B 2 143 ? 164.364 180.895 96.501  1.00 53.40  ? 134 ARG A N   1 
ATOM   4411 C CA  . ARG B 2 143 ? 163.736 179.625 96.159  1.00 54.08  ? 134 ARG A CA  1 
ATOM   4412 C C   . ARG B 2 143 ? 162.698 179.234 97.203  1.00 55.51  ? 134 ARG A C   1 
ATOM   4413 O O   . ARG B 2 143 ? 161.596 178.795 96.857  1.00 57.16  ? 134 ARG A O   1 
ATOM   4414 C CB  . ARG B 2 143 ? 164.790 178.528 96.011  1.00 55.49  ? 134 ARG A CB  1 
ATOM   4415 C CG  . ARG B 2 143 ? 164.224 177.125 96.065  1.00 59.18  ? 134 ARG A CG  1 
ATOM   4416 C CD  . ARG B 2 143 ? 165.305 176.101 96.347  1.00 65.22  ? 134 ARG A CD  1 
ATOM   4417 N NE  . ARG B 2 143 ? 166.561 176.452 95.700  1.00 72.43  ? 134 ARG A NE  1 
ATOM   4418 C CZ  . ARG B 2 143 ? 166.938 176.008 94.509  1.00 77.31  ? 134 ARG A CZ  1 
ATOM   4419 N NH1 . ARG B 2 143 ? 166.166 175.205 93.797  1.00 75.05  ? 134 ARG A NH1 1 
ATOM   4420 N NH2 . ARG B 2 143 ? 168.120 176.374 94.024  1.00 77.35  ? 134 ARG A NH2 1 
ATOM   4421 N N   . VAL B 2 144 ? 163.034 179.396 98.474  1.00 50.31  ? 135 VAL A N   1 
ATOM   4422 C CA  . VAL B 2 144 ? 162.119 179.091 99.565  1.00 37.91  ? 135 VAL A CA  1 
ATOM   4423 C C   . VAL B 2 144 ? 161.633 180.395 100.176 1.00 42.67  ? 135 VAL A C   1 
ATOM   4424 O O   . VAL B 2 144 ? 162.338 181.408 100.183 1.00 48.08  ? 135 VAL A O   1 
ATOM   4425 C CB  . VAL B 2 144 ? 162.788 178.185 100.619 1.00 37.08  ? 135 VAL A CB  1 
ATOM   4426 C CG1 . VAL B 2 144 ? 163.418 176.976 99.953  1.00 40.67  ? 135 VAL A CG1 1 
ATOM   4427 C CG2 . VAL B 2 144 ? 163.816 178.956 101.419 1.00 36.07  ? 135 VAL A CG2 1 
ATOM   4428 N N   . VAL B 2 145 ? 160.403 180.380 100.682 1.00 43.36  ? 136 VAL A N   1 
ATOM   4429 C CA  . VAL B 2 145 ? 159.844 181.573 101.301 1.00 35.18  ? 136 VAL A CA  1 
ATOM   4430 C C   . VAL B 2 145 ? 160.074 181.580 102.812 1.00 35.35  ? 136 VAL A C   1 
ATOM   4431 O O   . VAL B 2 145 ? 160.133 182.651 103.423 1.00 40.15  ? 136 VAL A O   1 
ATOM   4432 C CB  . VAL B 2 145 ? 158.350 181.699 100.952 1.00 34.40  ? 136 VAL A CB  1 
ATOM   4433 C CG1 . VAL B 2 145 ? 157.525 180.645 101.679 1.00 35.15  ? 136 VAL A CG1 1 
ATOM   4434 C CG2 . VAL B 2 145 ? 157.845 183.100 101.250 1.00 40.75  ? 136 VAL A CG2 1 
ATOM   4435 N N   . ALA B 2 146 ? 160.224 180.409 103.424 1.00 31.51  ? 137 ALA A N   1 
ATOM   4436 C CA  . ALA B 2 146 ? 160.583 180.280 104.827 1.00 25.09  ? 137 ALA A CA  1 
ATOM   4437 C C   . ALA B 2 146 ? 161.312 178.959 105.007 1.00 31.98  ? 137 ALA A C   1 
ATOM   4438 O O   . ALA B 2 146 ? 161.225 178.064 104.166 1.00 37.95  ? 137 ALA A O   1 
ATOM   4439 C CB  . ALA B 2 146 ? 159.354 180.350 105.739 1.00 22.39  ? 137 ALA A CB  1 
ATOM   4440 N N   . VAL B 2 147 ? 162.047 178.834 106.109 1.00 29.84  ? 138 VAL A N   1 
ATOM   4441 C CA  . VAL B 2 147 ? 162.748 177.596 106.429 1.00 32.02  ? 138 VAL A CA  1 
ATOM   4442 C C   . VAL B 2 147 ? 162.344 177.151 107.828 1.00 28.17  ? 138 VAL A C   1 
ATOM   4443 O O   . VAL B 2 147 ? 162.141 177.983 108.719 1.00 32.91  ? 138 VAL A O   1 
ATOM   4444 C CB  . VAL B 2 147 ? 164.283 177.738 106.311 1.00 32.24  ? 138 VAL A CB  1 
ATOM   4445 C CG1 . VAL B 2 147 ? 164.982 176.471 106.768 1.00 36.11  ? 138 VAL A CG1 1 
ATOM   4446 C CG2 . VAL B 2 147 ? 164.711 178.098 104.909 1.00 29.96  ? 138 VAL A CG2 1 
ATOM   4447 N N   . ILE B 2 148 ? 162.170 175.843 108.002 1.00 27.17  ? 139 ILE A N   1 
ATOM   4448 C CA  . ILE B 2 148 ? 162.001 175.238 109.320 1.00 28.50  ? 139 ILE A CA  1 
ATOM   4449 C C   . ILE B 2 148 ? 163.401 174.864 109.796 1.00 31.16  ? 139 ILE A C   1 
ATOM   4450 O O   . ILE B 2 148 ? 163.922 173.803 109.456 1.00 33.81  ? 139 ILE A O   1 
ATOM   4451 C CB  . ILE B 2 148 ? 161.063 174.029 109.284 1.00 27.11  ? 139 ILE A CB  1 
ATOM   4452 C CG1 . ILE B 2 148 ? 159.790 174.354 108.498 1.00 21.79  ? 139 ILE A CG1 1 
ATOM   4453 C CG2 . ILE B 2 148 ? 160.700 173.589 110.690 1.00 29.53  ? 139 ILE A CG2 1 
ATOM   4454 C CD1 . ILE B 2 148 ? 159.086 175.617 108.936 1.00 24.80  ? 139 ILE A CD1 1 
ATOM   4455 N N   . GLY B 2 149 ? 164.010 175.741 110.591 1.00 36.57  ? 140 GLY A N   1 
ATOM   4456 C CA  . GLY B 2 149 ? 165.436 175.718 110.812 1.00 36.79  ? 140 GLY A CA  1 
ATOM   4457 C C   . GLY B 2 149 ? 165.886 174.516 111.602 1.00 44.72  ? 140 GLY A C   1 
ATOM   4458 O O   . GLY B 2 149 ? 165.091 173.681 112.047 1.00 48.84  ? 140 GLY A O   1 
ATOM   4459 N N   . PRO B 2 150 ? 167.204 174.420 111.792 1.00 50.40  ? 141 PRO A N   1 
ATOM   4460 C CA  . PRO B 2 150 ? 167.776 173.244 112.462 1.00 49.50  ? 141 PRO A CA  1 
ATOM   4461 C C   . PRO B 2 150 ? 167.396 173.150 113.932 1.00 54.74  ? 141 PRO A C   1 
ATOM   4462 O O   . PRO B 2 150 ? 166.615 173.963 114.437 1.00 51.19  ? 141 PRO A O   1 
ATOM   4463 C CB  . PRO B 2 150 ? 169.285 173.436 112.274 1.00 53.69  ? 141 PRO A CB  1 
ATOM   4464 C CG  . PRO B 2 150 ? 169.462 174.898 112.086 1.00 48.29  ? 141 PRO A CG  1 
ATOM   4465 C CD  . PRO B 2 150 ? 168.236 175.387 111.383 1.00 46.53  ? 141 PRO A CD  1 
ATOM   4466 N N   . ASP B 2 151 ? 167.940 172.153 114.629 1.00 61.14  ? 142 ASP A N   1 
ATOM   4467 C CA  . ASP B 2 151 ? 167.484 171.816 115.969 1.00 64.21  ? 142 ASP A CA  1 
ATOM   4468 C C   . ASP B 2 151 ? 168.466 172.149 117.082 1.00 66.73  ? 142 ASP A C   1 
ATOM   4469 O O   . ASP B 2 151 ? 168.067 172.124 118.251 1.00 65.01  ? 142 ASP A O   1 
ATOM   4470 C CB  . ASP B 2 151 ? 167.134 170.320 116.061 1.00 68.82  ? 142 ASP A CB  1 
ATOM   4471 C CG  . ASP B 2 151 ? 168.148 169.422 115.365 1.00 78.18  ? 142 ASP A CG  1 
ATOM   4472 O OD1 . ASP B 2 151 ? 169.257 169.883 115.023 1.00 72.21  ? 142 ASP A OD1 1 
ATOM   4473 O OD2 . ASP B 2 151 ? 167.834 168.226 115.186 1.00 81.18  ? 142 ASP A OD2 1 
ATOM   4474 N N   . ASN B 2 152 ? 169.717 172.471 116.773 1.00 70.57  ? 143 ASN A N   1 
ATOM   4475 C CA  . ASN B 2 152 ? 170.698 172.799 117.797 1.00 71.73  ? 143 ASN A CA  1 
ATOM   4476 C C   . ASN B 2 152 ? 171.047 174.276 117.704 1.00 62.57  ? 143 ASN A C   1 
ATOM   4477 O O   . ASN B 2 152 ? 170.971 174.876 116.629 1.00 60.59  ? 143 ASN A O   1 
ATOM   4478 C CB  . ASN B 2 152 ? 171.960 171.943 117.666 1.00 76.12  ? 143 ASN A CB  1 
ATOM   4479 C CG  . ASN B 2 152 ? 172.664 172.144 116.350 1.00 81.95  ? 143 ASN A CG  1 
ATOM   4480 O OD1 . ASN B 2 152 ? 173.655 172.867 116.275 1.00 83.53  ? 143 ASN A OD1 1 
ATOM   4481 N ND2 . ASN B 2 152 ? 172.161 171.504 115.301 1.00 81.82  ? 143 ASN A ND2 1 
ATOM   4482 N N   . SER B 2 153 ? 171.433 174.852 118.840 1.00 60.09  ? 144 SER A N   1 
ATOM   4483 C CA  . SER B 2 153 ? 171.583 176.294 118.978 1.00 61.57  ? 144 SER A CA  1 
ATOM   4484 C C   . SER B 2 153 ? 172.637 176.875 118.045 1.00 62.67  ? 144 SER A C   1 
ATOM   4485 O O   . SER B 2 153 ? 172.405 177.910 117.415 1.00 64.54  ? 144 SER A O   1 
ATOM   4486 C CB  . SER B 2 153 ? 171.926 176.639 120.425 1.00 60.44  ? 144 SER A CB  1 
ATOM   4487 O OG  . SER B 2 153 ? 170.754 176.676 121.215 1.00 60.05  ? 144 SER A OG  1 
ATOM   4488 N N   . GLU B 2 154 ? 173.799 176.229 117.953 1.00 58.29  ? 145 GLU A N   1 
ATOM   4489 C CA  . GLU B 2 154 ? 174.874 176.730 117.106 1.00 62.80  ? 145 GLU A CA  1 
ATOM   4490 C C   . GLU B 2 154 ? 174.504 176.714 115.628 1.00 63.71  ? 145 GLU A C   1 
ATOM   4491 O O   . GLU B 2 154 ? 174.802 177.671 114.904 1.00 60.14  ? 145 GLU A O   1 
ATOM   4492 C CB  . GLU B 2 154 ? 176.149 175.916 117.335 1.00 65.38  ? 145 GLU A CB  1 
ATOM   4493 C CG  . GLU B 2 154 ? 177.440 176.682 117.070 1.00 67.45  ? 145 GLU A CG  1 
ATOM   4494 C CD  . GLU B 2 154 ? 177.338 178.156 117.418 1.00 69.26  ? 145 GLU A CD  1 
ATOM   4495 O OE1 . GLU B 2 154 ? 177.359 178.488 118.622 1.00 68.39  ? 145 GLU A OE1 1 
ATOM   4496 O OE2 . GLU B 2 154 ? 177.244 178.985 116.487 1.00 67.93  ? 145 GLU A OE2 1 
ATOM   4497 N N   . SER B 2 155 ? 173.857 175.645 115.166 1.00 63.34  ? 146 SER A N   1 
ATOM   4498 C CA  . SER B 2 155 ? 173.373 175.590 113.794 1.00 61.07  ? 146 SER A CA  1 
ATOM   4499 C C   . SER B 2 155 ? 172.333 176.659 113.506 1.00 58.18  ? 146 SER A C   1 
ATOM   4500 O O   . SER B 2 155 ? 172.362 177.261 112.428 1.00 55.04  ? 146 SER A O   1 
ATOM   4501 C CB  . SER B 2 155 ? 172.780 174.212 113.500 1.00 68.59  ? 146 SER A CB  1 
ATOM   4502 O OG  . SER B 2 155 ? 173.756 173.329 112.979 1.00 80.05  ? 146 SER A OG  1 
ATOM   4503 N N   . VAL B 2 156 ? 171.416 176.901 114.443 1.00 57.04  ? 147 VAL A N   1 
ATOM   4504 C CA  . VAL B 2 156 ? 170.412 177.940 114.256 1.00 46.84  ? 147 VAL A CA  1 
ATOM   4505 C C   . VAL B 2 156 ? 171.070 179.310 114.189 1.00 49.01  ? 147 VAL A C   1 
ATOM   4506 O O   . VAL B 2 156 ? 170.702 180.146 113.359 1.00 51.32  ? 147 VAL A O   1 
ATOM   4507 C CB  . VAL B 2 156 ? 169.355 177.865 115.371 1.00 42.13  ? 147 VAL A CB  1 
ATOM   4508 C CG1 . VAL B 2 156 ? 168.421 179.054 115.302 1.00 38.71  ? 147 VAL A CG1 1 
ATOM   4509 C CG2 . VAL B 2 156 ? 168.575 176.575 115.256 1.00 46.81  ? 147 VAL A CG2 1 
ATOM   4510 N N   . MET B 2 157 ? 172.057 179.561 115.052 1.00 48.68  ? 148 MET A N   1 
ATOM   4511 C CA  . MET B 2 157 ? 172.790 180.822 114.995 1.00 48.41  ? 148 MET A CA  1 
ATOM   4512 C C   . MET B 2 157 ? 173.509 180.996 113.666 1.00 48.74  ? 148 MET A C   1 
ATOM   4513 O O   . MET B 2 157 ? 173.470 182.083 113.080 1.00 49.45  ? 148 MET A O   1 
ATOM   4514 C CB  . MET B 2 157 ? 173.801 180.897 116.134 1.00 54.49  ? 148 MET A CB  1 
ATOM   4515 C CG  . MET B 2 157 ? 173.195 180.999 117.513 1.00 63.90  ? 148 MET A CG  1 
ATOM   4516 S SD  . MET B 2 157 ? 174.317 181.788 118.675 1.00 76.98  ? 148 MET A SD  1 
ATOM   4517 C CE  . MET B 2 157 ? 173.307 181.781 120.146 1.00 65.94  ? 148 MET A CE  1 
ATOM   4518 N N   . THR B 2 158 ? 174.174 179.945 113.182 1.00 52.88  ? 149 THR A N   1 
ATOM   4519 C CA  . THR B 2 158 ? 174.893 180.036 111.916 1.00 48.18  ? 149 THR A CA  1 
ATOM   4520 C C   . THR B 2 158 ? 173.939 180.290 110.755 1.00 47.67  ? 149 THR A C   1 
ATOM   4521 O O   . THR B 2 158 ? 174.223 181.109 109.874 1.00 50.99  ? 149 THR A O   1 
ATOM   4522 C CB  . THR B 2 158 ? 175.702 178.760 111.683 1.00 50.88  ? 149 THR A CB  1 
ATOM   4523 O OG1 . THR B 2 158 ? 176.744 178.672 112.661 1.00 54.07  ? 149 THR A OG1 1 
ATOM   4524 C CG2 . THR B 2 158 ? 176.325 178.766 110.301 1.00 50.11  ? 149 THR A CG2 1 
ATOM   4525 N N   . VAL B 2 159 ? 172.797 179.599 110.739 1.00 49.38  ? 150 VAL A N   1 
ATOM   4526 C CA  . VAL B 2 159 ? 171.838 179.789 109.655 1.00 47.12  ? 150 VAL A CA  1 
ATOM   4527 C C   . VAL B 2 159 ? 171.208 181.175 109.723 1.00 48.10  ? 150 VAL A C   1 
ATOM   4528 O O   . VAL B 2 159 ? 171.013 181.827 108.690 1.00 49.47  ? 150 VAL A O   1 
ATOM   4529 C CB  . VAL B 2 159 ? 170.776 178.674 109.692 1.00 49.14  ? 150 VAL A CB  1 
ATOM   4530 C CG1 . VAL B 2 159 ? 169.601 179.014 108.791 1.00 43.19  ? 150 VAL A CG1 1 
ATOM   4531 C CG2 . VAL B 2 159 ? 171.393 177.347 109.292 1.00 52.83  ? 150 VAL A CG2 1 
ATOM   4532 N N   . ALA B 2 160 ? 170.899 181.658 110.924 1.00 43.90  ? 151 ALA A N   1 
ATOM   4533 C CA  . ALA B 2 160 ? 170.263 182.952 111.104 1.00 36.91  ? 151 ALA A CA  1 
ATOM   4534 C C   . ALA B 2 160 ? 171.199 184.119 110.837 1.00 45.00  ? 151 ALA A C   1 
ATOM   4535 O O   . ALA B 2 160 ? 170.734 185.173 110.397 1.00 52.49  ? 151 ALA A O   1 
ATOM   4536 C CB  . ALA B 2 160 ? 169.696 183.062 112.522 1.00 40.07  ? 151 ALA A CB  1 
ATOM   4537 N N   . ASN B 2 161 ? 172.499 183.966 111.082 1.00 47.72  ? 152 ASN A N   1 
ATOM   4538 C CA  . ASN B 2 161 ? 173.455 185.011 110.751 1.00 41.56  ? 152 ASN A CA  1 
ATOM   4539 C C   . ASN B 2 161 ? 173.544 185.270 109.255 1.00 50.17  ? 152 ASN A C   1 
ATOM   4540 O O   . ASN B 2 161 ? 173.965 186.360 108.853 1.00 55.17  ? 152 ASN A O   1 
ATOM   4541 C CB  . ASN B 2 161 ? 174.841 184.650 111.288 1.00 38.74  ? 152 ASN A CB  1 
ATOM   4542 C CG  . ASN B 2 161 ? 175.050 185.113 112.712 1.00 50.88  ? 152 ASN A CG  1 
ATOM   4543 O OD1 . ASN B 2 161 ? 174.637 186.209 113.087 1.00 51.06  ? 152 ASN A OD1 1 
ATOM   4544 N ND2 . ASN B 2 161 ? 175.694 184.278 113.516 1.00 54.41  ? 152 ASN A ND2 1 
ATOM   4545 N N   . PHE B 2 162 ? 173.154 184.301 108.428 1.00 49.36  ? 153 PHE A N   1 
ATOM   4546 C CA  . PHE B 2 162 ? 173.146 184.460 106.984 1.00 46.45  ? 153 PHE A CA  1 
ATOM   4547 C C   . PHE B 2 162 ? 171.756 184.713 106.424 1.00 51.16  ? 153 PHE A C   1 
ATOM   4548 O O   . PHE B 2 162 ? 171.638 185.321 105.357 1.00 57.55  ? 153 PHE A O   1 
ATOM   4549 C CB  . PHE B 2 162 ? 173.744 183.213 106.315 1.00 48.71  ? 153 PHE A CB  1 
ATOM   4550 C CG  . PHE B 2 162 ? 173.954 183.353 104.837 1.00 57.35  ? 153 PHE A CG  1 
ATOM   4551 C CD1 . PHE B 2 162 ? 174.373 184.554 104.292 1.00 63.69  ? 153 PHE A CD1 1 
ATOM   4552 C CD2 . PHE B 2 162 ? 173.749 182.278 103.992 1.00 57.01  ? 153 PHE A CD2 1 
ATOM   4553 C CE1 . PHE B 2 162 ? 174.567 184.683 102.935 1.00 66.71  ? 153 PHE A CE1 1 
ATOM   4554 C CE2 . PHE B 2 162 ? 173.948 182.401 102.634 1.00 62.34  ? 153 PHE A CE2 1 
ATOM   4555 C CZ  . PHE B 2 162 ? 174.356 183.605 102.104 1.00 66.13  ? 153 PHE A CZ  1 
ATOM   4556 N N   . LEU B 2 163 ? 170.708 184.267 107.112 1.00 49.64  ? 154 LEU A N   1 
ATOM   4557 C CA  . LEU B 2 163 ? 169.339 184.577 106.724 1.00 43.58  ? 154 LEU A CA  1 
ATOM   4558 C C   . LEU B 2 163 ? 168.898 185.963 107.169 1.00 46.74  ? 154 LEU A C   1 
ATOM   4559 O O   . LEU B 2 163 ? 167.857 186.440 106.710 1.00 48.88  ? 154 LEU A O   1 
ATOM   4560 C CB  . LEU B 2 163 ? 168.376 183.532 107.294 1.00 43.21  ? 154 LEU A CB  1 
ATOM   4561 C CG  . LEU B 2 163 ? 168.321 182.168 106.614 1.00 41.68  ? 154 LEU A CG  1 
ATOM   4562 C CD1 . LEU B 2 163 ? 167.100 181.410 107.086 1.00 40.82  ? 154 LEU A CD1 1 
ATOM   4563 C CD2 . LEU B 2 163 ? 168.298 182.327 105.110 1.00 41.97  ? 154 LEU A CD2 1 
ATOM   4564 N N   . SER B 2 164 ? 169.653 186.617 108.047 1.00 47.88  ? 155 SER A N   1 
ATOM   4565 C CA  . SER B 2 164 ? 169.328 187.962 108.502 1.00 48.22  ? 155 SER A CA  1 
ATOM   4566 C C   . SER B 2 164 ? 169.544 189.013 107.425 1.00 51.93  ? 155 SER A C   1 
ATOM   4567 O O   . SER B 2 164 ? 168.953 190.093 107.508 1.00 57.49  ? 155 SER A O   1 
ATOM   4568 C CB  . SER B 2 164 ? 170.160 188.320 109.736 1.00 45.85  ? 155 SER A CB  1 
ATOM   4569 O OG  . SER B 2 164 ? 169.686 187.641 110.883 1.00 44.58  ? 155 SER A OG  1 
ATOM   4570 N N   . LEU B 2 165 ? 170.371 188.725 106.424 1.00 53.00  ? 156 LEU A N   1 
ATOM   4571 C CA  . LEU B 2 165 ? 170.590 189.640 105.315 1.00 54.20  ? 156 LEU A CA  1 
ATOM   4572 C C   . LEU B 2 165 ? 169.382 189.747 104.402 1.00 52.61  ? 156 LEU A C   1 
ATOM   4573 O O   . LEU B 2 165 ? 169.201 190.781 103.750 1.00 57.01  ? 156 LEU A O   1 
ATOM   4574 C CB  . LEU B 2 165 ? 171.796 189.189 104.489 1.00 53.12  ? 156 LEU A CB  1 
ATOM   4575 C CG  . LEU B 2 165 ? 173.185 189.566 104.992 1.00 59.61  ? 156 LEU A CG  1 
ATOM   4576 C CD1 . LEU B 2 165 ? 173.581 188.693 106.169 1.00 58.07  ? 156 LEU A CD1 1 
ATOM   4577 C CD2 . LEU B 2 165 ? 174.187 189.428 103.864 1.00 65.35  ? 156 LEU A CD2 1 
ATOM   4578 N N   . PHE B 2 166 ? 168.565 188.700 104.339 1.00 45.17  ? 157 PHE A N   1 
ATOM   4579 C CA  . PHE B 2 166 ? 167.395 188.654 103.482 1.00 44.71  ? 157 PHE A CA  1 
ATOM   4580 C C   . PHE B 2 166 ? 166.101 188.726 104.273 1.00 40.59  ? 157 PHE A C   1 
ATOM   4581 O O   . PHE B 2 166 ? 165.027 188.806 103.668 1.00 39.71  ? 157 PHE A O   1 
ATOM   4582 C CB  . PHE B 2 166 ? 167.408 187.375 102.632 1.00 45.62  ? 157 PHE A CB  1 
ATOM   4583 C CG  . PHE B 2 166 ? 168.705 187.132 101.909 1.00 48.09  ? 157 PHE A CG  1 
ATOM   4584 C CD1 . PHE B 2 166 ? 169.823 186.677 102.585 1.00 47.35  ? 157 PHE A CD1 1 
ATOM   4585 C CD2 . PHE B 2 166 ? 168.798 187.341 100.549 1.00 49.93  ? 157 PHE A CD2 1 
ATOM   4586 C CE1 . PHE B 2 166 ? 171.009 186.459 101.922 1.00 46.16  ? 157 PHE A CE1 1 
ATOM   4587 C CE2 . PHE B 2 166 ? 169.981 187.115 99.881  1.00 50.67  ? 157 PHE A CE2 1 
ATOM   4588 C CZ  . PHE B 2 166 ? 171.086 186.676 100.568 1.00 50.82  ? 157 PHE A CZ  1 
ATOM   4589 N N   . LEU B 2 167 ? 166.179 188.705 105.603 1.00 40.01  ? 158 LEU A N   1 
ATOM   4590 C CA  . LEU B 2 167 ? 165.012 188.678 106.480 1.00 39.63  ? 158 LEU A CA  1 
ATOM   4591 C C   . LEU B 2 167 ? 164.067 187.547 106.090 1.00 37.70  ? 158 LEU A C   1 
ATOM   4592 O O   . LEU B 2 167 ? 162.844 187.692 106.084 1.00 38.25  ? 158 LEU A O   1 
ATOM   4593 C CB  . LEU B 2 167 ? 164.294 190.026 106.486 1.00 42.95  ? 158 LEU A CB  1 
ATOM   4594 C CG  . LEU B 2 167 ? 164.947 191.120 107.331 1.00 42.68  ? 158 LEU A CG  1 
ATOM   4595 C CD1 . LEU B 2 167 ? 163.975 192.247 107.570 1.00 50.43  ? 158 LEU A CD1 1 
ATOM   4596 C CD2 . LEU B 2 167 ? 165.440 190.563 108.647 1.00 39.42  ? 158 LEU A CD2 1 
ATOM   4597 N N   . LEU B 2 168 ? 164.654 186.410 105.754 1.00 35.86  ? 159 LEU A N   1 
ATOM   4598 C CA  . LEU B 2 168 ? 163.914 185.194 105.451 1.00 32.52  ? 159 LEU A CA  1 
ATOM   4599 C C   . LEU B 2 168 ? 163.475 184.528 106.748 1.00 33.82  ? 159 LEU A C   1 
ATOM   4600 O O   . LEU B 2 168 ? 164.315 184.278 107.619 1.00 38.19  ? 159 LEU A O   1 
ATOM   4601 C CB  . LEU B 2 168 ? 164.766 184.235 104.630 1.00 31.81  ? 159 LEU A CB  1 
ATOM   4602 C CG  . LEU B 2 168 ? 164.023 183.247 103.730 1.00 34.76  ? 159 LEU A CG  1 
ATOM   4603 C CD1 . LEU B 2 168 ? 164.802 182.959 102.470 1.00 34.81  ? 159 LEU A CD1 1 
ATOM   4604 C CD2 . LEU B 2 168 ? 163.772 181.966 104.478 1.00 35.19  ? 159 LEU A CD2 1 
ATOM   4605 N N   . PRO B 2 169 ? 162.185 184.245 106.916 1.00 26.10  ? 160 PRO A N   1 
ATOM   4606 C CA  . PRO B 2 169 ? 161.710 183.668 108.180 1.00 22.84  ? 160 PRO A CA  1 
ATOM   4607 C C   . PRO B 2 169 ? 162.364 182.324 108.463 1.00 30.02  ? 160 PRO A C   1 
ATOM   4608 O O   . PRO B 2 169 ? 162.648 181.546 107.551 1.00 34.75  ? 160 PRO A O   1 
ATOM   4609 C CB  . PRO B 2 169 ? 160.199 183.527 107.962 1.00 27.48  ? 160 PRO A CB  1 
ATOM   4610 C CG  . PRO B 2 169 ? 159.882 184.382 106.795 1.00 28.50  ? 160 PRO A CG  1 
ATOM   4611 C CD  . PRO B 2 169 ? 161.097 184.438 105.947 1.00 26.04  ? 160 PRO A CD  1 
ATOM   4612 N N   . GLN B 2 170 ? 162.606 182.059 109.743 1.00 28.51  ? 161 GLN A N   1 
ATOM   4613 C CA  . GLN B 2 170 ? 163.243 180.825 110.189 1.00 27.60  ? 161 GLN A CA  1 
ATOM   4614 C C   . GLN B 2 170 ? 162.667 180.450 111.545 1.00 31.16  ? 161 GLN A C   1 
ATOM   4615 O O   . GLN B 2 170 ? 163.013 181.065 112.555 1.00 40.78  ? 161 GLN A O   1 
ATOM   4616 C CB  . GLN B 2 170 ? 164.758 180.992 110.278 1.00 27.74  ? 161 GLN A CB  1 
ATOM   4617 C CG  . GLN B 2 170 ? 165.493 179.759 110.753 1.00 36.03  ? 161 GLN A CG  1 
ATOM   4618 C CD  . GLN B 2 170 ? 166.900 180.071 111.199 1.00 43.34  ? 161 GLN A CD  1 
ATOM   4619 O OE1 . GLN B 2 170 ? 167.414 181.156 110.944 1.00 46.07  ? 161 GLN A OE1 1 
ATOM   4620 N NE2 . GLN B 2 170 ? 167.535 179.118 111.865 1.00 42.33  ? 161 GLN A NE2 1 
ATOM   4621 N N   . ILE B 2 171 ? 161.797 179.447 111.574 1.00 22.31  ? 162 ILE A N   1 
ATOM   4622 C CA  . ILE B 2 171 ? 161.238 178.941 112.821 1.00 28.22  ? 162 ILE A CA  1 
ATOM   4623 C C   . ILE B 2 171 ? 162.049 177.724 113.235 1.00 33.35  ? 162 ILE A C   1 
ATOM   4624 O O   . ILE B 2 171 ? 162.096 176.725 112.511 1.00 33.55  ? 162 ILE A O   1 
ATOM   4625 C CB  . ILE B 2 171 ? 159.752 178.584 112.680 1.00 28.95  ? 162 ILE A CB  1 
ATOM   4626 C CG1 . ILE B 2 171 ? 159.006 179.658 111.899 1.00 25.61  ? 162 ILE A CG1 1 
ATOM   4627 C CG2 . ILE B 2 171 ? 159.123 178.421 114.048 1.00 31.19  ? 162 ILE A CG2 1 
ATOM   4628 C CD1 . ILE B 2 171 ? 157.520 179.458 111.915 1.00 28.11  ? 162 ILE A CD1 1 
ATOM   4629 N N   . THR B 2 172 ? 162.685 177.801 114.397 1.00 36.55  ? 163 THR A N   1 
ATOM   4630 C CA  . THR B 2 172 ? 163.508 176.713 114.901 1.00 34.47  ? 163 THR A CA  1 
ATOM   4631 C C   . THR B 2 172 ? 162.739 175.939 115.963 1.00 36.17  ? 163 THR A C   1 
ATOM   4632 O O   . THR B 2 172 ? 162.057 176.529 116.806 1.00 40.01  ? 163 THR A O   1 
ATOM   4633 C CB  . THR B 2 172 ? 164.832 177.225 115.469 1.00 35.51  ? 163 THR A CB  1 
ATOM   4634 O OG1 . THR B 2 172 ? 165.527 176.139 116.090 1.00 40.30  ? 163 THR A OG1 1 
ATOM   4635 C CG2 . THR B 2 172 ? 164.603 178.315 116.498 1.00 32.70  ? 163 THR A CG2 1 
ATOM   4636 N N   . TYR B 2 173 ? 162.832 174.620 115.894 1.00 39.59  ? 164 TYR A N   1 
ATOM   4637 C CA  . TYR B 2 173 ? 162.327 173.728 116.923 1.00 39.93  ? 164 TYR A CA  1 
ATOM   4638 C C   . TYR B 2 173 ? 163.499 173.187 117.731 1.00 47.59  ? 164 TYR A C   1 
ATOM   4639 O O   . TYR B 2 173 ? 164.627 173.118 117.236 1.00 55.79  ? 164 TYR A O   1 
ATOM   4640 C CB  . TYR B 2 173 ? 161.548 172.583 116.278 1.00 38.70  ? 164 TYR A CB  1 
ATOM   4641 C CG  . TYR B 2 173 ? 162.359 171.902 115.203 1.00 43.89  ? 164 TYR A CG  1 
ATOM   4642 C CD1 . TYR B 2 173 ? 163.279 170.916 115.523 1.00 46.63  ? 164 TYR A CD1 1 
ATOM   4643 C CD2 . TYR B 2 173 ? 162.236 172.274 113.874 1.00 37.07  ? 164 TYR A CD2 1 
ATOM   4644 C CE1 . TYR B 2 173 ? 164.037 170.314 114.558 1.00 48.38  ? 164 TYR A CE1 1 
ATOM   4645 C CE2 . TYR B 2 173 ? 162.991 171.671 112.898 1.00 36.34  ? 164 TYR A CE2 1 
ATOM   4646 C CZ  . TYR B 2 173 ? 163.891 170.692 113.250 1.00 46.99  ? 164 TYR A CZ  1 
ATOM   4647 O OH  . TYR B 2 173 ? 164.657 170.078 112.296 1.00 52.62  ? 164 TYR A OH  1 
ATOM   4648 N N   . SER B 2 174 ? 163.234 172.821 118.981 1.00 45.20  ? 165 SER A N   1 
ATOM   4649 C CA  . SER B 2 174 ? 164.173 172.101 119.837 1.00 56.56  ? 165 SER A CA  1 
ATOM   4650 C C   . SER B 2 174 ? 165.450 172.878 120.144 1.00 55.54  ? 165 SER A C   1 
ATOM   4651 O O   . SER B 2 174 ? 166.370 172.321 120.751 1.00 57.96  ? 165 SER A O   1 
ATOM   4652 C CB  . SER B 2 174 ? 164.541 170.741 119.229 1.00 55.36  ? 165 SER A CB  1 
ATOM   4653 O OG  . SER B 2 174 ? 165.171 169.900 120.179 1.00 60.45  ? 165 SER A OG  1 
ATOM   4654 N N   . ALA B 2 175 ? 165.547 174.146 119.754 1.00 48.85  ? 166 ALA A N   1 
ATOM   4655 C CA  . ALA B 2 175 ? 166.680 174.990 120.107 1.00 46.37  ? 166 ALA A CA  1 
ATOM   4656 C C   . ALA B 2 175 ? 166.256 175.892 121.254 1.00 51.65  ? 166 ALA A C   1 
ATOM   4657 O O   . ALA B 2 175 ? 165.238 176.579 121.157 1.00 58.11  ? 166 ALA A O   1 
ATOM   4658 C CB  . ALA B 2 175 ? 167.153 175.820 118.914 1.00 51.74  ? 166 ALA A CB  1 
ATOM   4659 N N   . ILE B 2 176 ? 167.018 175.875 122.346 1.00 50.75  ? 167 ILE A N   1 
ATOM   4660 C CA  . ILE B 2 176 ? 166.569 176.487 123.587 1.00 52.72  ? 167 ILE A CA  1 
ATOM   4661 C C   . ILE B 2 176 ? 167.556 177.513 124.129 1.00 54.89  ? 167 ILE A C   1 
ATOM   4662 O O   . ILE B 2 176 ? 167.502 177.844 125.308 1.00 60.60  ? 167 ILE A O   1 
ATOM   4663 C CB  . ILE B 2 176 ? 166.256 175.416 124.653 1.00 55.28  ? 167 ILE A CB  1 
ATOM   4664 C CG1 . ILE B 2 176 ? 167.500 174.581 124.960 1.00 50.41  ? 167 ILE A CG1 1 
ATOM   4665 C CG2 . ILE B 2 176 ? 165.107 174.530 124.203 1.00 50.39  ? 167 ILE A CG2 1 
ATOM   4666 C CD1 . ILE B 2 176 ? 167.753 174.389 126.434 1.00 51.97  ? 167 ILE A CD1 1 
ATOM   4667 N N   . SER B 2 177 ? 168.461 178.025 123.300 1.00 50.87  ? 168 SER A N   1 
ATOM   4668 C CA  . SER B 2 177 ? 169.378 179.054 123.770 1.00 49.01  ? 168 SER A CA  1 
ATOM   4669 C C   . SER B 2 177 ? 168.623 180.330 124.112 1.00 53.64  ? 168 SER A C   1 
ATOM   4670 O O   . SER B 2 177 ? 167.774 180.791 123.346 1.00 52.94  ? 168 SER A O   1 
ATOM   4671 C CB  . SER B 2 177 ? 170.441 179.349 122.714 1.00 52.95  ? 168 SER A CB  1 
ATOM   4672 O OG  . SER B 2 177 ? 171.504 180.113 123.256 1.00 57.60  ? 168 SER A OG  1 
ATOM   4673 N N   . ASP B 2 178 ? 168.935 180.902 125.273 1.00 58.37  ? 169 ASP A N   1 
ATOM   4674 C CA  . ASP B 2 178 ? 168.403 182.211 125.626 1.00 59.85  ? 169 ASP A CA  1 
ATOM   4675 C C   . ASP B 2 178 ? 168.910 183.311 124.708 1.00 63.41  ? 169 ASP A C   1 
ATOM   4676 O O   . ASP B 2 178 ? 168.289 184.377 124.642 1.00 64.34  ? 169 ASP A O   1 
ATOM   4677 C CB  . ASP B 2 178 ? 168.752 182.558 127.075 1.00 63.58  ? 169 ASP A CB  1 
ATOM   4678 C CG  . ASP B 2 178 ? 167.563 182.448 128.002 1.00 68.20  ? 169 ASP A CG  1 
ATOM   4679 O OD1 . ASP B 2 178 ? 166.500 181.974 127.554 1.00 68.16  ? 169 ASP A OD1 1 
ATOM   4680 O OD2 . ASP B 2 178 ? 167.686 182.850 129.177 1.00 66.78  ? 169 ASP A OD2 1 
ATOM   4681 N N   . GLU B 2 179 ? 170.020 183.078 124.008 1.00 61.86  ? 170 GLU A N   1 
ATOM   4682 C CA  . GLU B 2 179 ? 170.584 184.068 123.103 1.00 57.10  ? 170 GLU A CA  1 
ATOM   4683 C C   . GLU B 2 179 ? 169.795 184.201 121.808 1.00 56.82  ? 170 GLU A C   1 
ATOM   4684 O O   . GLU B 2 179 ? 169.915 185.226 121.130 1.00 60.63  ? 170 GLU A O   1 
ATOM   4685 C CB  . GLU B 2 179 ? 172.034 183.709 122.784 1.00 63.46  ? 170 GLU A CB  1 
ATOM   4686 C CG  . GLU B 2 179 ? 173.064 184.473 123.592 1.00 73.11  ? 170 GLU A CG  1 
ATOM   4687 C CD  . GLU B 2 179 ? 174.483 184.111 123.203 1.00 81.46  ? 170 GLU A CD  1 
ATOM   4688 O OE1 . GLU B 2 179 ? 174.763 182.907 123.032 1.00 78.99  ? 170 GLU A OE1 1 
ATOM   4689 O OE2 . GLU B 2 179 ? 175.320 185.029 123.070 1.00 75.29  ? 170 GLU A OE2 1 
ATOM   4690 N N   . LEU B 2 180 ? 168.997 183.195 121.448 1.00 52.10  ? 171 LEU A N   1 
ATOM   4691 C CA  . LEU B 2 180 ? 168.164 183.286 120.257 1.00 46.95  ? 171 LEU A CA  1 
ATOM   4692 C C   . LEU B 2 180 ? 166.995 184.242 120.436 1.00 49.27  ? 171 LEU A C   1 
ATOM   4693 O O   . LEU B 2 180 ? 166.313 184.549 119.455 1.00 50.04  ? 171 LEU A O   1 
ATOM   4694 C CB  . LEU B 2 180 ? 167.637 181.904 119.870 1.00 40.60  ? 171 LEU A CB  1 
ATOM   4695 C CG  . LEU B 2 180 ? 168.673 180.827 119.556 1.00 45.14  ? 171 LEU A CG  1 
ATOM   4696 C CD1 . LEU B 2 180 ? 167.982 179.531 119.175 1.00 37.96  ? 171 LEU A CD1 1 
ATOM   4697 C CD2 . LEU B 2 180 ? 169.613 181.287 118.459 1.00 47.22  ? 171 LEU A CD2 1 
ATOM   4698 N N   . ARG B 2 181 ? 166.751 184.713 121.656 1.00 51.28  ? 172 ARG A N   1 
ATOM   4699 C CA  . ARG B 2 181 ? 165.672 185.651 121.927 1.00 52.55  ? 172 ARG A CA  1 
ATOM   4700 C C   . ARG B 2 181 ? 166.037 187.083 121.564 1.00 54.30  ? 172 ARG A C   1 
ATOM   4701 O O   . ARG B 2 181 ? 165.194 187.974 121.705 1.00 54.28  ? 172 ARG A O   1 
ATOM   4702 C CB  . ARG B 2 181 ? 165.278 185.566 123.404 1.00 60.39  ? 172 ARG A CB  1 
ATOM   4703 C CG  . ARG B 2 181 ? 164.265 184.473 123.708 1.00 61.94  ? 172 ARG A CG  1 
ATOM   4704 C CD  . ARG B 2 181 ? 163.612 184.664 125.063 1.00 65.04  ? 172 ARG A CD  1 
ATOM   4705 N NE  . ARG B 2 181 ? 164.589 184.972 126.100 1.00 75.69  ? 172 ARG A NE  1 
ATOM   4706 C CZ  . ARG B 2 181 ? 164.363 184.860 127.402 1.00 74.02  ? 172 ARG A CZ  1 
ATOM   4707 N NH1 . ARG B 2 181 ? 163.203 184.427 127.868 1.00 71.49  ? 172 ARG A NH1 1 
ATOM   4708 N NH2 . ARG B 2 181 ? 165.325 185.190 128.259 1.00 71.84  ? 172 ARG A NH2 1 
ATOM   4709 N N   . ASP B 2 182 ? 167.265 187.320 121.108 1.00 58.15  ? 173 ASP A N   1 
ATOM   4710 C CA  . ASP B 2 182 ? 167.697 188.647 120.693 1.00 52.82  ? 173 ASP A CA  1 
ATOM   4711 C C   . ASP B 2 182 ? 167.211 188.934 119.278 1.00 50.16  ? 173 ASP A C   1 
ATOM   4712 O O   . ASP B 2 182 ? 167.715 188.354 118.312 1.00 48.92  ? 173 ASP A O   1 
ATOM   4713 C CB  . ASP B 2 182 ? 169.220 188.745 120.755 1.00 48.74  ? 173 ASP A CB  1 
ATOM   4714 C CG  . ASP B 2 182 ? 169.697 190.112 121.187 1.00 64.53  ? 173 ASP A CG  1 
ATOM   4715 O OD1 . ASP B 2 182 ? 168.941 191.087 121.010 1.00 65.31  ? 173 ASP A OD1 1 
ATOM   4716 O OD2 . ASP B 2 182 ? 170.831 190.213 121.700 1.00 73.24  ? 173 ASP A OD2 1 
ATOM   4717 N N   . LYS B 2 183 ? 166.242 189.840 119.152 1.00 45.85  ? 174 LYS A N   1 
ATOM   4718 C CA  . LYS B 2 183 ? 165.589 190.108 117.877 1.00 43.72  ? 174 LYS A CA  1 
ATOM   4719 C C   . LYS B 2 183 ? 166.260 191.219 117.081 1.00 46.09  ? 174 LYS A C   1 
ATOM   4720 O O   . LYS B 2 183 ? 165.761 191.587 116.014 1.00 47.20  ? 174 LYS A O   1 
ATOM   4721 C CB  . LYS B 2 183 ? 164.113 190.442 118.095 1.00 49.04  ? 174 LYS A CB  1 
ATOM   4722 C CG  . LYS B 2 183 ? 163.260 189.248 118.480 1.00 49.10  ? 174 LYS A CG  1 
ATOM   4723 C CD  . LYS B 2 183 ? 163.484 188.083 117.537 1.00 47.13  ? 174 LYS A CD  1 
ATOM   4724 C CE  . LYS B 2 183 ? 163.959 186.855 118.292 1.00 46.00  ? 174 LYS A CE  1 
ATOM   4725 N NZ  . LYS B 2 183 ? 164.832 185.998 117.457 1.00 41.96  ? 174 LYS A NZ  1 
ATOM   4726 N N   . VAL B 2 184 ? 167.361 191.777 117.573 1.00 51.03  ? 175 VAL A N   1 
ATOM   4727 C CA  . VAL B 2 184 ? 168.206 192.649 116.771 1.00 50.52  ? 175 VAL A CA  1 
ATOM   4728 C C   . VAL B 2 184 ? 169.379 191.883 116.178 1.00 47.02  ? 175 VAL A C   1 
ATOM   4729 O O   . VAL B 2 184 ? 169.813 192.171 115.063 1.00 50.09  ? 175 VAL A O   1 
ATOM   4730 C CB  . VAL B 2 184 ? 168.693 193.861 117.597 1.00 55.70  ? 175 VAL A CB  1 
ATOM   4731 C CG1 . VAL B 2 184 ? 167.626 194.942 117.634 1.00 47.10  ? 175 VAL A CG1 1 
ATOM   4732 C CG2 . VAL B 2 184 ? 169.070 193.438 118.997 1.00 50.30  ? 175 VAL A CG2 1 
ATOM   4733 N N   . ARG B 2 185 ? 169.896 190.905 116.921 1.00 47.50  ? 176 ARG A N   1 
ATOM   4734 C CA  . ARG B 2 185 ? 170.904 189.996 116.396 1.00 47.06  ? 176 ARG A CA  1 
ATOM   4735 C C   . ARG B 2 185 ? 170.311 188.976 115.433 1.00 46.56  ? 176 ARG A C   1 
ATOM   4736 O O   . ARG B 2 185 ? 170.978 188.593 114.467 1.00 47.14  ? 176 ARG A O   1 
ATOM   4737 C CB  . ARG B 2 185 ? 171.599 189.282 117.554 1.00 48.32  ? 176 ARG A CB  1 
ATOM   4738 C CG  . ARG B 2 185 ? 172.997 188.794 117.251 1.00 54.36  ? 176 ARG A CG  1 
ATOM   4739 C CD  . ARG B 2 185 ? 173.699 188.381 118.528 1.00 58.23  ? 176 ARG A CD  1 
ATOM   4740 N NE  . ARG B 2 185 ? 174.427 187.128 118.373 1.00 63.06  ? 176 ARG A NE  1 
ATOM   4741 C CZ  . ARG B 2 185 ? 174.662 186.275 119.360 1.00 65.12  ? 176 ARG A CZ  1 
ATOM   4742 N NH1 . ARG B 2 185 ? 174.238 186.509 120.590 1.00 62.09  ? 176 ARG A NH1 1 
ATOM   4743 N NH2 . ARG B 2 185 ? 175.336 185.158 119.104 1.00 61.94  ? 176 ARG A NH2 1 
ATOM   4744 N N   . PHE B 2 186 ? 169.079 188.534 115.676 1.00 47.92  ? 177 PHE A N   1 
ATOM   4745 C CA  . PHE B 2 186 ? 168.401 187.549 114.831 1.00 40.54  ? 177 PHE A CA  1 
ATOM   4746 C C   . PHE B 2 186 ? 167.016 188.076 114.491 1.00 42.70  ? 177 PHE A C   1 
ATOM   4747 O O   . PHE B 2 186 ? 166.008 187.624 115.045 1.00 42.34  ? 177 PHE A O   1 
ATOM   4748 C CB  . PHE B 2 186 ? 168.313 186.194 115.533 1.00 41.74  ? 177 PHE A CB  1 
ATOM   4749 C CG  . PHE B 2 186 ? 169.628 185.693 116.047 1.00 46.70  ? 177 PHE A CG  1 
ATOM   4750 C CD1 . PHE B 2 186 ? 170.630 185.314 115.172 1.00 47.20  ? 177 PHE A CD1 1 
ATOM   4751 C CD2 . PHE B 2 186 ? 169.870 185.618 117.405 1.00 44.68  ? 177 PHE A CD2 1 
ATOM   4752 C CE1 . PHE B 2 186 ? 171.839 184.860 115.643 1.00 47.77  ? 177 PHE A CE1 1 
ATOM   4753 C CE2 . PHE B 2 186 ? 171.079 185.166 117.879 1.00 50.02  ? 177 PHE A CE2 1 
ATOM   4754 C CZ  . PHE B 2 186 ? 172.064 184.786 116.997 1.00 53.35  ? 177 PHE A CZ  1 
ATOM   4755 N N   . PRO B 2 187 ? 166.931 189.052 113.584 1.00 39.62  ? 178 PRO A N   1 
ATOM   4756 C CA  . PRO B 2 187 ? 165.628 189.673 113.295 1.00 33.04  ? 178 PRO A CA  1 
ATOM   4757 C C   . PRO B 2 187 ? 164.585 188.712 112.758 1.00 39.60  ? 178 PRO A C   1 
ATOM   4758 O O   . PRO B 2 187 ? 163.396 188.875 113.057 1.00 41.59  ? 178 PRO A O   1 
ATOM   4759 C CB  . PRO B 2 187 ? 165.977 190.747 112.255 1.00 37.99  ? 178 PRO A CB  1 
ATOM   4760 C CG  . PRO B 2 187 ? 167.444 190.938 112.358 1.00 41.78  ? 178 PRO A CG  1 
ATOM   4761 C CD  . PRO B 2 187 ? 168.008 189.627 112.767 1.00 39.00  ? 178 PRO A CD  1 
ATOM   4762 N N   . ALA B 2 188 ? 164.988 187.716 111.974 1.00 44.54  ? 179 ALA A N   1 
ATOM   4763 C CA  . ALA B 2 188 ? 164.062 186.843 111.269 1.00 35.28  ? 179 ALA A CA  1 
ATOM   4764 C C   . ALA B 2 188 ? 163.897 185.484 111.936 1.00 35.03  ? 179 ALA A C   1 
ATOM   4765 O O   . ALA B 2 188 ? 163.344 184.569 111.322 1.00 39.50  ? 179 ALA A O   1 
ATOM   4766 C CB  . ALA B 2 188 ? 164.518 186.661 109.822 1.00 30.28  ? 179 ALA A CB  1 
ATOM   4767 N N   . LEU B 2 189 ? 164.355 185.332 113.174 1.00 34.36  ? 180 LEU A N   1 
ATOM   4768 C CA  . LEU B 2 189 ? 164.341 184.052 113.867 1.00 32.30  ? 180 LEU A CA  1 
ATOM   4769 C C   . LEU B 2 189 ? 163.126 183.963 114.779 1.00 32.65  ? 180 LEU A C   1 
ATOM   4770 O O   . LEU B 2 189 ? 162.882 184.863 115.587 1.00 39.70  ? 180 LEU A O   1 
ATOM   4771 C CB  . LEU B 2 189 ? 165.622 183.869 114.678 1.00 36.67  ? 180 LEU A CB  1 
ATOM   4772 C CG  . LEU B 2 189 ? 165.848 182.536 115.385 1.00 31.61  ? 180 LEU A CG  1 
ATOM   4773 C CD1 . LEU B 2 189 ? 165.604 181.379 114.445 1.00 31.18  ? 180 LEU A CD1 1 
ATOM   4774 C CD2 . LEU B 2 189 ? 167.254 182.488 115.934 1.00 38.08  ? 180 LEU A CD2 1 
ATOM   4775 N N   . LEU B 2 190 ? 162.376 182.876 114.647 1.00 31.48  ? 181 LEU A N   1 
ATOM   4776 C CA  . LEU B 2 190 ? 161.229 182.561 115.484 1.00 29.95  ? 181 LEU A CA  1 
ATOM   4777 C C   . LEU B 2 190 ? 161.416 181.166 116.072 1.00 35.41  ? 181 LEU A C   1 
ATOM   4778 O O   . LEU B 2 190 ? 162.351 180.446 115.723 1.00 37.52  ? 181 LEU A O   1 
ATOM   4779 C CB  . LEU B 2 190 ? 159.934 182.676 114.683 1.00 26.92  ? 181 LEU A CB  1 
ATOM   4780 C CG  . LEU B 2 190 ? 159.686 184.036 114.044 1.00 33.38  ? 181 LEU A CG  1 
ATOM   4781 C CD1 . LEU B 2 190 ? 158.904 183.854 112.780 1.00 39.94  ? 181 LEU A CD1 1 
ATOM   4782 C CD2 . LEU B 2 190 ? 158.933 184.930 115.000 1.00 33.58  ? 181 LEU A CD2 1 
ATOM   4783 N N   . ARG B 2 191 ? 160.515 180.783 116.971 1.00 36.57  ? 182 ARG A N   1 
ATOM   4784 C CA  . ARG B 2 191 ? 160.685 179.546 117.717 1.00 34.89  ? 182 ARG A CA  1 
ATOM   4785 C C   . ARG B 2 191 ? 159.325 179.024 118.148 1.00 36.13  ? 182 ARG A C   1 
ATOM   4786 O O   . ARG B 2 191 ? 158.435 179.791 118.515 1.00 43.69  ? 182 ARG A O   1 
ATOM   4787 C CB  . ARG B 2 191 ? 161.582 179.764 118.934 1.00 38.33  ? 182 ARG A CB  1 
ATOM   4788 C CG  . ARG B 2 191 ? 162.156 178.506 119.517 1.00 40.39  ? 182 ARG A CG  1 
ATOM   4789 C CD  . ARG B 2 191 ? 163.510 178.780 120.109 1.00 43.16  ? 182 ARG A CD  1 
ATOM   4790 N NE  . ARG B 2 191 ? 163.477 179.859 121.085 1.00 42.85  ? 182 ARG A NE  1 
ATOM   4791 C CZ  . ARG B 2 191 ? 164.508 180.218 121.836 1.00 43.34  ? 182 ARG A CZ  1 
ATOM   4792 N NH1 . ARG B 2 191 ? 165.661 179.577 121.775 1.00 47.84  ? 182 ARG A NH1 1 
ATOM   4793 N NH2 . ARG B 2 191 ? 164.379 181.247 122.666 1.00 46.16  ? 182 ARG A NH2 1 
ATOM   4794 N N   . THR B 2 192 ? 159.181 177.697 118.108 1.00 32.54  ? 183 THR A N   1 
ATOM   4795 C CA  . THR B 2 192 ? 157.964 177.040 118.572 1.00 35.84  ? 183 THR A CA  1 
ATOM   4796 C C   . THR B 2 192 ? 158.205 176.238 119.844 1.00 38.24  ? 183 THR A C   1 
ATOM   4797 O O   . THR B 2 192 ? 157.436 175.323 120.148 1.00 40.96  ? 183 THR A O   1 
ATOM   4798 C CB  . THR B 2 192 ? 157.375 176.134 117.488 1.00 34.10  ? 183 THR A CB  1 
ATOM   4799 O OG1 . THR B 2 192 ? 158.434 175.507 116.758 1.00 38.02  ? 183 THR A OG1 1 
ATOM   4800 C CG2 . THR B 2 192 ? 156.514 176.941 116.534 1.00 30.96  ? 183 THR A CG2 1 
ATOM   4801 N N   . THR B 2 193 ? 159.258 176.557 120.587 1.00 39.54  ? 184 THR A N   1 
ATOM   4802 C CA  . THR B 2 193 ? 159.566 175.909 121.850 1.00 42.58  ? 184 THR A CA  1 
ATOM   4803 C C   . THR B 2 193 ? 159.948 176.972 122.866 1.00 46.58  ? 184 THR A C   1 
ATOM   4804 O O   . THR B 2 193 ? 160.439 178.043 122.490 1.00 47.64  ? 184 THR A O   1 
ATOM   4805 C CB  . THR B 2 193 ? 160.719 174.900 121.716 1.00 45.50  ? 184 THR A CB  1 
ATOM   4806 O OG1 . THR B 2 193 ? 161.686 175.395 120.784 1.00 48.84  ? 184 THR A OG1 1 
ATOM   4807 C CG2 . THR B 2 193 ? 160.203 173.562 121.237 1.00 44.20  ? 184 THR A CG2 1 
ATOM   4808 N N   . PRO B 2 194 ? 159.727 176.713 124.153 1.00 47.33  ? 185 PRO A N   1 
ATOM   4809 C CA  . PRO B 2 194 ? 160.243 177.623 125.179 1.00 48.89  ? 185 PRO A CA  1 
ATOM   4810 C C   . PRO B 2 194 ? 161.763 177.590 125.225 1.00 53.33  ? 185 PRO A C   1 
ATOM   4811 O O   . PRO B 2 194 ? 162.397 176.599 124.860 1.00 57.67  ? 185 PRO A O   1 
ATOM   4812 C CB  . PRO B 2 194 ? 159.630 177.082 126.475 1.00 45.76  ? 185 PRO A CB  1 
ATOM   4813 C CG  . PRO B 2 194 ? 158.466 176.271 126.040 1.00 41.01  ? 185 PRO A CG  1 
ATOM   4814 C CD  . PRO B 2 194 ? 158.847 175.683 124.726 1.00 41.26  ? 185 PRO A CD  1 
ATOM   4815 N N   . SER B 2 195 ? 162.345 178.696 125.680 1.00 47.11  ? 186 SER A N   1 
ATOM   4816 C CA  . SER B 2 195 ? 163.790 178.798 125.794 1.00 48.75  ? 186 SER A CA  1 
ATOM   4817 C C   . SER B 2 195 ? 164.278 178.064 127.043 1.00 54.21  ? 186 SER A C   1 
ATOM   4818 O O   . SER B 2 195 ? 163.506 177.446 127.780 1.00 53.00  ? 186 SER A O   1 
ATOM   4819 C CB  . SER B 2 195 ? 164.211 180.263 125.826 1.00 54.00  ? 186 SER A CB  1 
ATOM   4820 O OG  . SER B 2 195 ? 163.235 181.052 126.481 1.00 59.29  ? 186 SER A OG  1 
ATOM   4821 N N   . ALA B 2 196 ? 165.590 178.138 127.282 1.00 56.69  ? 187 ALA A N   1 
ATOM   4822 C CA  . ALA B 2 196 ? 166.157 177.607 128.515 1.00 51.23  ? 187 ALA A CA  1 
ATOM   4823 C C   . ALA B 2 196 ? 165.690 178.389 129.731 1.00 49.70  ? 187 ALA A C   1 
ATOM   4824 O O   . ALA B 2 196 ? 165.809 177.896 130.857 1.00 48.87  ? 187 ALA A O   1 
ATOM   4825 C CB  . ALA B 2 196 ? 167.682 177.614 128.446 1.00 51.90  ? 187 ALA A CB  1 
ATOM   4826 N N   . ASP B 2 197 ? 165.161 179.594 129.519 1.00 48.06  ? 188 ASP A N   1 
ATOM   4827 C CA  . ASP B 2 197 ? 164.529 180.346 130.594 1.00 46.17  ? 188 ASP A CA  1 
ATOM   4828 C C   . ASP B 2 197 ? 163.473 179.505 131.298 1.00 48.51  ? 188 ASP A C   1 
ATOM   4829 O O   . ASP B 2 197 ? 163.523 179.310 132.518 1.00 51.14  ? 188 ASP A O   1 
ATOM   4830 C CB  . ASP B 2 197 ? 163.911 181.615 130.002 1.00 54.45  ? 188 ASP A CB  1 
ATOM   4831 C CG  . ASP B 2 197 ? 163.484 182.609 131.048 1.00 63.29  ? 188 ASP A CG  1 
ATOM   4832 O OD1 . ASP B 2 197 ? 163.921 182.490 132.203 1.00 62.39  ? 188 ASP A OD1 1 
ATOM   4833 O OD2 . ASP B 2 197 ? 162.708 183.524 130.706 1.00 67.23  ? 188 ASP A OD2 1 
ATOM   4834 N N   . HIS B 2 198 ? 162.539 178.946 130.531 1.00 46.72  ? 189 HIS A N   1 
ATOM   4835 C CA  . HIS B 2 198 ? 161.440 178.208 131.136 1.00 38.88  ? 189 HIS A CA  1 
ATOM   4836 C C   . HIS B 2 198 ? 161.867 176.824 131.603 1.00 42.28  ? 189 HIS A C   1 
ATOM   4837 O O   . HIS B 2 198 ? 161.298 176.300 132.564 1.00 50.20  ? 189 HIS A O   1 
ATOM   4838 C CB  . HIS B 2 198 ? 160.275 178.135 130.154 1.00 42.97  ? 189 HIS A CB  1 
ATOM   4839 C CG  . HIS B 2 198 ? 159.703 179.475 129.814 1.00 46.14  ? 189 HIS A CG  1 
ATOM   4840 N ND1 . HIS B 2 198 ? 159.022 180.245 130.731 1.00 47.79  ? 189 HIS A ND1 1 
ATOM   4841 C CD2 . HIS B 2 198 ? 159.726 180.191 128.667 1.00 49.42  ? 189 HIS A CD2 1 
ATOM   4842 C CE1 . HIS B 2 198 ? 158.642 181.373 130.160 1.00 46.94  ? 189 HIS A CE1 1 
ATOM   4843 N NE2 . HIS B 2 198 ? 159.056 181.365 128.907 1.00 48.71  ? 189 HIS A NE2 1 
ATOM   4844 N N   . HIS B 2 199 ? 162.878 176.227 130.970 1.00 40.96  ? 190 HIS A N   1 
ATOM   4845 C CA  . HIS B 2 199 ? 163.405 174.957 131.462 1.00 39.61  ? 190 HIS A CA  1 
ATOM   4846 C C   . HIS B 2 199 ? 164.038 175.128 132.840 1.00 38.29  ? 190 HIS A C   1 
ATOM   4847 O O   . HIS B 2 199 ? 163.776 174.347 133.765 1.00 40.70  ? 190 HIS A O   1 
ATOM   4848 C CB  . HIS B 2 199 ? 164.418 174.398 130.465 1.00 40.62  ? 190 HIS A CB  1 
ATOM   4849 C CG  . HIS B 2 199 ? 163.796 173.788 129.248 1.00 46.86  ? 190 HIS A CG  1 
ATOM   4850 N ND1 . HIS B 2 199 ? 163.368 174.539 128.177 1.00 51.30  ? 190 HIS A ND1 1 
ATOM   4851 C CD2 . HIS B 2 199 ? 163.539 172.498 128.929 1.00 49.69  ? 190 HIS A CD2 1 
ATOM   4852 C CE1 . HIS B 2 199 ? 162.868 173.739 127.252 1.00 47.56  ? 190 HIS A CE1 1 
ATOM   4853 N NE2 . HIS B 2 199 ? 162.960 172.496 127.684 1.00 46.29  ? 190 HIS A NE2 1 
ATOM   4854 N N   . ILE B 2 200 ? 164.868 176.162 132.996 1.00 41.29  ? 191 ILE A N   1 
ATOM   4855 C CA  . ILE B 2 200 ? 165.470 176.458 134.292 1.00 38.29  ? 191 ILE A CA  1 
ATOM   4856 C C   . ILE B 2 200 ? 164.400 176.820 135.310 1.00 35.77  ? 191 ILE A C   1 
ATOM   4857 O O   . ILE B 2 200 ? 164.482 176.431 136.481 1.00 38.85  ? 191 ILE A O   1 
ATOM   4858 C CB  . ILE B 2 200 ? 166.517 177.577 134.148 1.00 43.68  ? 191 ILE A CB  1 
ATOM   4859 C CG1 . ILE B 2 200 ? 167.708 177.094 133.323 1.00 46.73  ? 191 ILE A CG1 1 
ATOM   4860 C CG2 . ILE B 2 200 ? 166.969 178.069 135.504 1.00 38.73  ? 191 ILE A CG2 1 
ATOM   4861 C CD1 . ILE B 2 200 ? 168.168 175.718 133.669 1.00 39.99  ? 191 ILE A CD1 1 
ATOM   4862 N N   . GLU B 2 201 ? 163.384 177.576 134.889 1.00 37.16  ? 192 GLU A N   1 
ATOM   4863 C CA  . GLU B 2 201 ? 162.304 177.925 135.804 1.00 37.35  ? 192 GLU A CA  1 
ATOM   4864 C C   . GLU B 2 201 ? 161.566 176.682 136.285 1.00 37.89  ? 192 GLU A C   1 
ATOM   4865 O O   . GLU B 2 201 ? 161.232 176.571 137.468 1.00 45.60  ? 192 GLU A O   1 
ATOM   4866 C CB  . GLU B 2 201 ? 161.343 178.900 135.127 1.00 41.90  ? 192 GLU A CB  1 
ATOM   4867 C CG  . GLU B 2 201 ? 160.237 179.411 136.027 1.00 47.33  ? 192 GLU A CG  1 
ATOM   4868 C CD  . GLU B 2 201 ? 160.760 180.253 137.166 1.00 55.55  ? 192 GLU A CD  1 
ATOM   4869 O OE1 . GLU B 2 201 ? 161.767 180.962 136.968 1.00 57.51  ? 192 GLU A OE1 1 
ATOM   4870 O OE2 . GLU B 2 201 ? 160.158 180.214 138.258 1.00 60.09  ? 192 GLU A OE2 1 
ATOM   4871 N N   . ALA B 2 202 ? 161.309 175.733 135.382 1.00 30.79  ? 193 ALA A N   1 
ATOM   4872 C CA  . ALA B 2 202 ? 160.661 174.488 135.777 1.00 31.77  ? 193 ALA A CA  1 
ATOM   4873 C C   . ALA B 2 202 ? 161.525 173.700 136.753 1.00 32.03  ? 193 ALA A C   1 
ATOM   4874 O O   . ALA B 2 202 ? 161.015 173.137 137.729 1.00 33.20  ? 193 ALA A O   1 
ATOM   4875 C CB  . ALA B 2 202 ? 160.346 173.651 134.539 1.00 36.95  ? 193 ALA A CB  1 
ATOM   4876 N N   . MET B 2 203 ? 162.839 173.650 136.507 1.00 33.75  ? 194 MET A N   1 
ATOM   4877 C CA  . MET B 2 203 ? 163.736 172.977 137.443 1.00 28.06  ? 194 MET A CA  1 
ATOM   4878 C C   . MET B 2 203 ? 163.678 173.618 138.823 1.00 32.28  ? 194 MET A C   1 
ATOM   4879 O O   . MET B 2 203 ? 163.612 172.919 139.842 1.00 41.30  ? 194 MET A O   1 
ATOM   4880 C CB  . MET B 2 203 ? 165.170 173.006 136.919 1.00 27.44  ? 194 MET A CB  1 
ATOM   4881 C CG  . MET B 2 203 ? 165.481 171.972 135.866 1.00 27.26  ? 194 MET A CG  1 
ATOM   4882 S SD  . MET B 2 203 ? 167.088 172.256 135.113 1.00 42.86  ? 194 MET A SD  1 
ATOM   4883 C CE  . MET B 2 203 ? 167.058 171.054 133.792 1.00 38.90  ? 194 MET A CE  1 
ATOM   4884 N N   . VAL B 2 204 ? 163.699 174.949 138.874 1.00 28.97  ? 195 VAL A N   1 
ATOM   4885 C CA  . VAL B 2 204 ? 163.708 175.647 140.155 1.00 24.63  ? 195 VAL A CA  1 
ATOM   4886 C C   . VAL B 2 204 ? 162.387 175.448 140.890 1.00 25.01  ? 195 VAL A C   1 
ATOM   4887 O O   . VAL B 2 204 ? 162.364 175.282 142.114 1.00 27.23  ? 195 VAL A O   1 
ATOM   4888 C CB  . VAL B 2 204 ? 164.034 177.134 139.939 1.00 32.63  ? 195 VAL A CB  1 
ATOM   4889 C CG1 . VAL B 2 204 ? 163.736 177.938 141.187 1.00 40.66  ? 195 VAL A CG1 1 
ATOM   4890 C CG2 . VAL B 2 204 ? 165.491 177.290 139.552 1.00 39.45  ? 195 VAL A CG2 1 
ATOM   4891 N N   . GLN B 2 205 ? 161.266 175.453 140.166 1.00 28.59  ? 196 GLN A N   1 
ATOM   4892 C CA  . GLN B 2 205 ? 159.983 175.220 140.824 1.00 27.49  ? 196 GLN A CA  1 
ATOM   4893 C C   . GLN B 2 205 ? 159.859 173.786 141.320 1.00 26.04  ? 196 GLN A C   1 
ATOM   4894 O O   . GLN B 2 205 ? 159.257 173.542 142.373 1.00 31.70  ? 196 GLN A O   1 
ATOM   4895 C CB  . GLN B 2 205 ? 158.826 175.565 139.889 1.00 34.82  ? 196 GLN A CB  1 
ATOM   4896 C CG  . GLN B 2 205 ? 158.888 176.961 139.327 1.00 37.22  ? 196 GLN A CG  1 
ATOM   4897 C CD  . GLN B 2 205 ? 157.842 177.863 139.923 1.00 46.47  ? 196 GLN A CD  1 
ATOM   4898 O OE1 . GLN B 2 205 ? 156.684 177.478 140.068 1.00 47.44  ? 196 GLN A OE1 1 
ATOM   4899 N NE2 . GLN B 2 205 ? 158.244 179.072 140.282 1.00 52.80  ? 196 GLN A NE2 1 
ATOM   4900 N N   . LEU B 2 206 ? 160.412 172.823 140.578 1.00 25.46  ? 197 LEU A N   1 
ATOM   4901 C CA  . LEU B 2 206 ? 160.428 171.446 141.061 1.00 23.92  ? 197 LEU A CA  1 
ATOM   4902 C C   . LEU B 2 206 ? 161.276 171.322 142.318 1.00 24.35  ? 197 LEU A C   1 
ATOM   4903 O O   . LEU B 2 206 ? 160.923 170.589 143.249 1.00 22.92  ? 197 LEU A O   1 
ATOM   4904 C CB  . LEU B 2 206 ? 160.939 170.511 139.966 1.00 22.80  ? 197 LEU A CB  1 
ATOM   4905 C CG  . LEU B 2 206 ? 161.205 169.055 140.347 1.00 24.33  ? 197 LEU A CG  1 
ATOM   4906 C CD1 . LEU B 2 206 ? 159.907 168.271 140.382 1.00 21.05  ? 197 LEU A CD1 1 
ATOM   4907 C CD2 . LEU B 2 206 ? 162.172 168.429 139.368 1.00 26.58  ? 197 LEU A CD2 1 
ATOM   4908 N N   . MET B 2 207 ? 162.401 172.038 142.362 1.00 25.03  ? 198 MET A N   1 
ATOM   4909 C CA  . MET B 2 207 ? 163.230 172.051 143.562 1.00 22.36  ? 198 MET A CA  1 
ATOM   4910 C C   . MET B 2 207 ? 162.483 172.651 144.747 1.00 24.96  ? 198 MET A C   1 
ATOM   4911 O O   . MET B 2 207 ? 162.524 172.109 145.856 1.00 29.19  ? 198 MET A O   1 
ATOM   4912 C CB  . MET B 2 207 ? 164.509 172.839 143.296 1.00 24.65  ? 198 MET A CB  1 
ATOM   4913 C CG  . MET B 2 207 ? 165.681 172.014 142.830 1.00 20.03  ? 198 MET A CG  1 
ATOM   4914 S SD  . MET B 2 207 ? 166.853 173.046 141.935 1.00 31.18  ? 198 MET A SD  1 
ATOM   4915 C CE  . MET B 2 207 ? 167.070 172.096 140.441 1.00 30.69  ? 198 MET A CE  1 
ATOM   4916 N N   . LEU B 2 208 ? 161.798 173.778 144.534 1.00 25.04  ? 199 LEU A N   1 
ATOM   4917 C CA  . LEU B 2 208 ? 161.104 174.443 145.635 1.00 27.01  ? 199 LEU A CA  1 
ATOM   4918 C C   . LEU B 2 208 ? 159.910 173.642 146.133 1.00 32.59  ? 199 LEU A C   1 
ATOM   4919 O O   . LEU B 2 208 ? 159.622 173.656 147.334 1.00 38.01  ? 199 LEU A O   1 
ATOM   4920 C CB  . LEU B 2 208 ? 160.642 175.841 145.227 1.00 29.73  ? 199 LEU A CB  1 
ATOM   4921 C CG  . LEU B 2 208 ? 161.680 176.898 144.855 1.00 38.45  ? 199 LEU A CG  1 
ATOM   4922 C CD1 . LEU B 2 208 ? 161.143 177.790 143.758 1.00 36.02  ? 199 LEU A CD1 1 
ATOM   4923 C CD2 . LEU B 2 208 ? 162.064 177.715 146.069 1.00 43.17  ? 199 LEU A CD2 1 
ATOM   4924 N N   . HIS B 2 209 ? 159.195 172.956 145.239 1.00 29.49  ? 200 HIS A N   1 
ATOM   4925 C CA  . HIS B 2 209 ? 158.016 172.209 145.668 1.00 27.10  ? 200 HIS A CA  1 
ATOM   4926 C C   . HIS B 2 209 ? 158.386 171.095 146.637 1.00 34.74  ? 200 HIS A C   1 
ATOM   4927 O O   . HIS B 2 209 ? 157.685 170.867 147.629 1.00 44.84  ? 200 HIS A O   1 
ATOM   4928 C CB  . HIS B 2 209 ? 157.282 171.636 144.459 1.00 28.74  ? 200 HIS A CB  1 
ATOM   4929 C CG  . HIS B 2 209 ? 156.083 170.814 144.816 1.00 26.79  ? 200 HIS A CG  1 
ATOM   4930 N ND1 . HIS B 2 209 ? 155.965 169.485 144.480 1.00 26.83  ? 200 HIS A ND1 1 
ATOM   4931 C CD2 . HIS B 2 209 ? 154.949 171.135 145.481 1.00 27.14  ? 200 HIS A CD2 1 
ATOM   4932 C CE1 . HIS B 2 209 ? 154.809 169.022 144.920 1.00 26.66  ? 200 HIS A CE1 1 
ATOM   4933 N NE2 . HIS B 2 209 ? 154.174 170.003 145.532 1.00 25.31  ? 200 HIS A NE2 1 
ATOM   4934 N N   . PHE B 2 210 ? 159.481 170.390 146.369 1.00 33.47  ? 201 PHE A N   1 
ATOM   4935 C CA  . PHE B 2 210 ? 159.920 169.291 147.216 1.00 28.29  ? 201 PHE A CA  1 
ATOM   4936 C C   . PHE B 2 210 ? 160.950 169.720 148.251 1.00 31.27  ? 201 PHE A C   1 
ATOM   4937 O O   . PHE B 2 210 ? 161.488 168.865 148.959 1.00 41.23  ? 201 PHE A O   1 
ATOM   4938 C CB  . PHE B 2 210 ? 160.473 168.159 146.355 1.00 25.34  ? 201 PHE A CB  1 
ATOM   4939 C CG  . PHE B 2 210 ? 159.427 167.462 145.534 1.00 28.82  ? 201 PHE A CG  1 
ATOM   4940 C CD1 . PHE B 2 210 ? 158.327 166.881 146.137 1.00 27.00  ? 201 PHE A CD1 1 
ATOM   4941 C CD2 . PHE B 2 210 ? 159.539 167.395 144.161 1.00 28.21  ? 201 PHE A CD2 1 
ATOM   4942 C CE1 . PHE B 2 210 ? 157.365 166.247 145.386 1.00 23.00  ? 201 PHE A CE1 1 
ATOM   4943 C CE2 . PHE B 2 210 ? 158.579 166.762 143.409 1.00 22.50  ? 201 PHE A CE2 1 
ATOM   4944 C CZ  . PHE B 2 210 ? 157.493 166.188 144.022 1.00 22.45  ? 201 PHE A CZ  1 
ATOM   4945 N N   . ARG B 2 211 ? 161.235 171.019 148.347 1.00 33.59  ? 202 ARG A N   1 
ATOM   4946 C CA  . ARG B 2 211 ? 162.063 171.592 149.407 1.00 35.25  ? 202 ARG A CA  1 
ATOM   4947 C C   . ARG B 2 211 ? 163.505 171.081 149.338 1.00 32.84  ? 202 ARG A C   1 
ATOM   4948 O O   . ARG B 2 211 ? 164.046 170.522 150.291 1.00 39.39  ? 202 ARG A O   1 
ATOM   4949 C CB  . ARG B 2 211 ? 161.439 171.329 150.781 1.00 37.18  ? 202 ARG A CB  1 
ATOM   4950 C CG  . ARG B 2 211 ? 160.172 172.122 151.034 1.00 44.31  ? 202 ARG A CG  1 
ATOM   4951 C CD  . ARG B 2 211 ? 159.222 171.389 151.959 1.00 56.73  ? 202 ARG A CD  1 
ATOM   4952 N NE  . ARG B 2 211 ? 158.642 170.217 151.315 1.00 62.28  ? 202 ARG A NE  1 
ATOM   4953 C CZ  . ARG B 2 211 ? 158.136 169.177 151.963 1.00 70.40  ? 202 ARG A CZ  1 
ATOM   4954 N NH1 . ARG B 2 211 ? 158.124 169.124 153.285 1.00 70.25  ? 202 ARG A NH1 1 
ATOM   4955 N NH2 . ARG B 2 211 ? 157.632 168.162 151.266 1.00 66.39  ? 202 ARG A NH2 1 
ATOM   4956 N N   . TRP B 2 212 ? 164.124 171.294 148.184 1.00 29.56  ? 203 TRP A N   1 
ATOM   4957 C CA  . TRP B 2 212 ? 165.544 171.038 147.989 1.00 27.92  ? 203 TRP A CA  1 
ATOM   4958 C C   . TRP B 2 212 ? 166.252 172.374 147.817 1.00 30.22  ? 203 TRP A C   1 
ATOM   4959 O O   . TRP B 2 212 ? 166.043 173.063 146.814 1.00 39.16  ? 203 TRP A O   1 
ATOM   4960 C CB  . TRP B 2 212 ? 165.787 170.153 146.767 1.00 28.12  ? 203 TRP A CB  1 
ATOM   4961 C CG  . TRP B 2 212 ? 165.009 168.883 146.743 1.00 25.64  ? 203 TRP A CG  1 
ATOM   4962 C CD1 . TRP B 2 212 ? 164.731 168.071 147.797 1.00 30.04  ? 203 TRP A CD1 1 
ATOM   4963 C CD2 . TRP B 2 212 ? 164.418 168.267 145.596 1.00 23.96  ? 203 TRP A CD2 1 
ATOM   4964 N NE1 . TRP B 2 212 ? 163.998 166.989 147.382 1.00 28.36  ? 203 TRP A NE1 1 
ATOM   4965 C CE2 . TRP B 2 212 ? 163.793 167.086 146.033 1.00 28.23  ? 203 TRP A CE2 1 
ATOM   4966 C CE3 . TRP B 2 212 ? 164.356 168.601 144.242 1.00 21.62  ? 203 TRP A CE3 1 
ATOM   4967 C CZ2 . TRP B 2 212 ? 163.116 166.238 145.165 1.00 27.10  ? 203 TRP A CZ2 1 
ATOM   4968 C CZ3 . TRP B 2 212 ? 163.684 167.762 143.384 1.00 19.55  ? 203 TRP A CZ3 1 
ATOM   4969 C CH2 . TRP B 2 212 ? 163.070 166.595 143.847 1.00 25.28  ? 203 TRP A CH2 1 
ATOM   4970 N N   . ASN B 2 213 ? 167.090 172.736 148.785 1.00 28.24  ? 204 ASN A N   1 
ATOM   4971 C CA  . ASN B 2 213 ? 167.872 173.962 148.695 1.00 32.96  ? 204 ASN A CA  1 
ATOM   4972 C C   . ASN B 2 213 ? 169.364 173.663 148.701 1.00 33.14  ? 204 ASN A C   1 
ATOM   4973 O O   . ASN B 2 213 ? 170.178 174.539 148.993 1.00 39.87  ? 204 ASN A O   1 
ATOM   4974 C CB  . ASN B 2 213 ? 167.512 174.935 149.819 1.00 42.16  ? 204 ASN A CB  1 
ATOM   4975 C CG  . ASN B 2 213 ? 167.727 174.350 151.197 1.00 44.90  ? 204 ASN A CG  1 
ATOM   4976 O OD1 . ASN B 2 213 ? 168.853 174.089 151.610 1.00 45.66  ? 204 ASN A OD1 1 
ATOM   4977 N ND2 . ASN B 2 213 ? 166.640 174.166 151.926 1.00 44.50  ? 204 ASN A ND2 1 
ATOM   4978 N N   . TRP B 2 214 ? 169.735 172.429 148.373 1.00 30.78  ? 205 TRP A N   1 
ATOM   4979 C CA  . TRP B 2 214 ? 171.132 172.006 148.391 1.00 29.65  ? 205 TRP A CA  1 
ATOM   4980 C C   . TRP B 2 214 ? 171.330 171.085 147.192 1.00 28.33  ? 205 TRP A C   1 
ATOM   4981 O O   . TRP B 2 214 ? 171.093 169.881 147.292 1.00 36.05  ? 205 TRP A O   1 
ATOM   4982 C CB  . TRP B 2 214 ? 171.461 171.311 149.706 1.00 31.87  ? 205 TRP A CB  1 
ATOM   4983 C CG  . TRP B 2 214 ? 172.916 171.221 150.049 1.00 32.58  ? 205 TRP A CG  1 
ATOM   4984 C CD1 . TRP B 2 214 ? 173.568 170.123 150.513 1.00 31.62  ? 205 TRP A CD1 1 
ATOM   4985 C CD2 . TRP B 2 214 ? 173.893 172.270 149.985 1.00 34.44  ? 205 TRP A CD2 1 
ATOM   4986 N NE1 . TRP B 2 214 ? 174.890 170.411 150.726 1.00 40.79  ? 205 TRP A NE1 1 
ATOM   4987 C CE2 . TRP B 2 214 ? 175.115 171.724 150.412 1.00 35.38  ? 205 TRP A CE2 1 
ATOM   4988 C CE3 . TRP B 2 214 ? 173.853 173.614 149.607 1.00 34.98  ? 205 TRP A CE3 1 
ATOM   4989 C CZ2 . TRP B 2 214 ? 176.285 172.471 150.469 1.00 32.54  ? 205 TRP A CZ2 1 
ATOM   4990 C CZ3 . TRP B 2 214 ? 175.015 174.350 149.663 1.00 38.88  ? 205 TRP A CZ3 1 
ATOM   4991 C CH2 . TRP B 2 214 ? 176.213 173.779 150.090 1.00 37.56  ? 205 TRP A CH2 1 
ATOM   4992 N N   . ILE B 2 215 ? 171.763 171.649 146.066 1.00 24.67  ? 206 ILE A N   1 
ATOM   4993 C CA  . ILE B 2 215 ? 171.802 170.909 144.813 1.00 25.44  ? 206 ILE A CA  1 
ATOM   4994 C C   . ILE B 2 215 ? 173.209 170.937 144.237 1.00 25.52  ? 206 ILE A C   1 
ATOM   4995 O O   . ILE B 2 215 ? 174.001 171.842 144.499 1.00 34.39  ? 206 ILE A O   1 
ATOM   4996 C CB  . ILE B 2 215 ? 170.795 171.454 143.777 1.00 28.43  ? 206 ILE A CB  1 
ATOM   4997 C CG1 . ILE B 2 215 ? 171.185 172.866 143.344 1.00 23.27  ? 206 ILE A CG1 1 
ATOM   4998 C CG2 . ILE B 2 215 ? 169.388 171.432 144.341 1.00 32.95  ? 206 ILE A CG2 1 
ATOM   4999 C CD1 . ILE B 2 215 ? 170.636 173.266 142.011 1.00 22.55  ? 206 ILE A CD1 1 
ATOM   5000 N N   . ILE B 2 216 ? 173.507 169.921 143.437 1.00 22.20  ? 207 ILE A N   1 
ATOM   5001 C CA  . ILE B 2 216 ? 174.768 169.797 142.719 1.00 24.28  ? 207 ILE A CA  1 
ATOM   5002 C C   . ILE B 2 216 ? 174.474 170.017 141.245 1.00 29.56  ? 207 ILE A C   1 
ATOM   5003 O O   . ILE B 2 216 ? 173.457 169.537 140.734 1.00 32.92  ? 207 ILE A O   1 
ATOM   5004 C CB  . ILE B 2 216 ? 175.415 168.421 142.956 1.00 26.63  ? 207 ILE A CB  1 
ATOM   5005 C CG1 . ILE B 2 216 ? 175.816 168.264 144.420 1.00 28.52  ? 207 ILE A CG1 1 
ATOM   5006 C CG2 . ILE B 2 216 ? 176.615 168.222 142.050 1.00 28.41  ? 207 ILE A CG2 1 
ATOM   5007 C CD1 . ILE B 2 216 ? 175.991 166.832 144.847 1.00 26.92  ? 207 ILE A CD1 1 
ATOM   5008 N N   . VAL B 2 217 ? 175.338 170.764 140.567 1.00 27.89  ? 208 VAL A N   1 
ATOM   5009 C CA  . VAL B 2 217 ? 175.183 171.046 139.146 1.00 30.34  ? 208 VAL A CA  1 
ATOM   5010 C C   . VAL B 2 217 ? 176.369 170.452 138.404 1.00 33.75  ? 208 VAL A C   1 
ATOM   5011 O O   . VAL B 2 217 ? 177.524 170.740 138.733 1.00 44.02  ? 208 VAL A O   1 
ATOM   5012 C CB  . VAL B 2 217 ? 175.063 172.556 138.881 1.00 31.89  ? 208 VAL A CB  1 
ATOM   5013 C CG1 . VAL B 2 217 ? 175.004 172.828 137.392 1.00 33.33  ? 208 VAL A CG1 1 
ATOM   5014 C CG2 . VAL B 2 217 ? 173.836 173.108 139.571 1.00 31.08  ? 208 VAL A CG2 1 
ATOM   5015 N N   . LEU B 2 218 ? 176.085 169.613 137.415 1.00 33.46  ? 209 LEU A N   1 
ATOM   5016 C CA  . LEU B 2 218 ? 177.098 169.045 136.539 1.00 37.60  ? 209 LEU A CA  1 
ATOM   5017 C C   . LEU B 2 218 ? 176.825 169.519 135.122 1.00 43.79  ? 209 LEU A C   1 
ATOM   5018 O O   . LEU B 2 218 ? 175.764 169.231 134.565 1.00 44.37  ? 209 LEU A O   1 
ATOM   5019 C CB  . LEU B 2 218 ? 177.089 167.518 136.597 1.00 40.82  ? 209 LEU A CB  1 
ATOM   5020 C CG  . LEU B 2 218 ? 177.399 166.869 137.945 1.00 41.97  ? 209 LEU A CG  1 
ATOM   5021 C CD1 . LEU B 2 218 ? 177.232 165.370 137.848 1.00 40.63  ? 209 LEU A CD1 1 
ATOM   5022 C CD2 . LEU B 2 218 ? 178.799 167.219 138.408 1.00 39.70  ? 209 LEU A CD2 1 
ATOM   5023 N N   . VAL B 2 219 ? 177.780 170.237 134.540 1.00 46.53  ? 210 VAL A N   1 
ATOM   5024 C CA  . VAL B 2 219 ? 177.640 170.792 133.204 1.00 45.32  ? 210 VAL A CA  1 
ATOM   5025 C C   . VAL B 2 219 ? 178.658 170.118 132.294 1.00 51.65  ? 210 VAL A C   1 
ATOM   5026 O O   . VAL B 2 219 ? 179.529 169.378 132.743 1.00 52.44  ? 210 VAL A O   1 
ATOM   5027 C CB  . VAL B 2 219 ? 177.812 172.322 133.188 1.00 45.76  ? 210 VAL A CB  1 
ATOM   5028 C CG1 . VAL B 2 219 ? 176.833 172.969 134.144 1.00 47.38  ? 210 VAL A CG1 1 
ATOM   5029 C CG2 . VAL B 2 219 ? 179.237 172.698 133.551 1.00 47.46  ? 210 VAL A CG2 1 
ATOM   5030 N N   . SER B 2 220 ? 178.527 170.371 131.000 1.00 54.48  ? 211 SER A N   1 
ATOM   5031 C CA  . SER B 2 220 ? 179.467 169.856 130.018 1.00 53.75  ? 211 SER A CA  1 
ATOM   5032 C C   . SER B 2 220 ? 180.393 170.970 129.545 1.00 62.01  ? 211 SER A C   1 
ATOM   5033 O O   . SER B 2 220 ? 180.192 172.149 129.845 1.00 66.34  ? 211 SER A O   1 
ATOM   5034 C CB  . SER B 2 220 ? 178.731 169.237 128.829 1.00 55.06  ? 211 SER A CB  1 
ATOM   5035 O OG  . SER B 2 220 ? 177.656 170.057 128.411 1.00 60.11  ? 211 SER A OG  1 
ATOM   5036 N N   . SER B 2 221 ? 181.424 170.579 128.795 1.00 63.79  ? 212 SER A N   1 
ATOM   5037 C CA  . SER B 2 221 ? 182.429 171.543 128.364 1.00 65.95  ? 212 SER A CA  1 
ATOM   5038 C C   . SER B 2 221 ? 181.948 172.425 127.218 1.00 67.66  ? 212 SER A C   1 
ATOM   5039 O O   . SER B 2 221 ? 182.522 173.495 126.998 1.00 65.97  ? 212 SER A O   1 
ATOM   5040 C CB  . SER B 2 221 ? 183.710 170.818 127.958 1.00 69.66  ? 212 SER A CB  1 
ATOM   5041 O OG  . SER B 2 221 ? 184.107 169.895 128.955 1.00 71.65  ? 212 SER A OG  1 
ATOM   5042 N N   . ASP B 2 222 ? 180.918 172.008 126.488 1.00 68.50  ? 213 ASP A N   1 
ATOM   5043 C CA  . ASP B 2 222 ? 180.424 172.807 125.378 1.00 70.18  ? 213 ASP A CA  1 
ATOM   5044 C C   . ASP B 2 222 ? 179.666 174.030 125.892 1.00 64.96  ? 213 ASP A C   1 
ATOM   5045 O O   . ASP B 2 222 ? 179.358 174.158 127.079 1.00 66.36  ? 213 ASP A O   1 
ATOM   5046 C CB  . ASP B 2 222 ? 179.529 171.975 124.457 1.00 76.04  ? 213 ASP A CB  1 
ATOM   5047 C CG  . ASP B 2 222 ? 178.619 171.029 125.214 1.00 74.23  ? 213 ASP A CG  1 
ATOM   5048 O OD1 . ASP B 2 222 ? 179.125 170.067 125.824 1.00 72.91  ? 213 ASP A OD1 1 
ATOM   5049 O OD2 . ASP B 2 222 ? 177.387 171.220 125.160 1.00 72.26  ? 213 ASP A OD2 1 
ATOM   5050 N N   . THR B 2 223 ? 179.371 174.946 124.966 1.00 65.14  ? 214 THR A N   1 
ATOM   5051 C CA  . THR B 2 223 ? 178.721 176.199 125.337 1.00 70.17  ? 214 THR A CA  1 
ATOM   5052 C C   . THR B 2 223 ? 177.323 175.962 125.894 1.00 69.02  ? 214 THR A C   1 
ATOM   5053 O O   . THR B 2 223 ? 176.834 176.752 126.710 1.00 67.45  ? 214 THR A O   1 
ATOM   5054 C CB  . THR B 2 223 ? 178.662 177.137 124.132 1.00 77.73  ? 214 THR A CB  1 
ATOM   5055 O OG1 . THR B 2 223 ? 177.740 178.202 124.395 1.00 72.54  ? 214 THR A OG1 1 
ATOM   5056 C CG2 . THR B 2 223 ? 178.215 176.383 122.889 1.00 72.24  ? 214 THR A CG2 1 
ATOM   5057 N N   . TYR B 2 224 ? 176.666 174.881 125.468 1.00 65.94  ? 215 TYR A N   1 
ATOM   5058 C CA  . TYR B 2 224 ? 175.319 174.592 125.950 1.00 60.89  ? 215 TYR A CA  1 
ATOM   5059 C C   . TYR B 2 224 ? 175.319 174.348 127.452 1.00 63.42  ? 215 TYR A C   1 
ATOM   5060 O O   . TYR B 2 224 ? 174.542 174.962 128.194 1.00 60.59  ? 215 TYR A O   1 
ATOM   5061 C CB  . TYR B 2 224 ? 174.749 173.380 125.214 1.00 60.13  ? 215 TYR A CB  1 
ATOM   5062 C CG  . TYR B 2 224 ? 173.591 172.715 125.925 1.00 65.02  ? 215 TYR A CG  1 
ATOM   5063 C CD1 . TYR B 2 224 ? 172.316 173.259 125.871 1.00 59.17  ? 215 TYR A CD1 1 
ATOM   5064 C CD2 . TYR B 2 224 ? 173.773 171.549 126.654 1.00 59.15  ? 215 TYR A CD2 1 
ATOM   5065 C CE1 . TYR B 2 224 ? 171.257 172.657 126.515 1.00 50.92  ? 215 TYR A CE1 1 
ATOM   5066 C CE2 . TYR B 2 224 ? 172.720 170.945 127.305 1.00 53.73  ? 215 TYR A CE2 1 
ATOM   5067 C CZ  . TYR B 2 224 ? 171.465 171.504 127.231 1.00 52.76  ? 215 TYR A CZ  1 
ATOM   5068 O OH  . TYR B 2 224 ? 170.409 170.907 127.876 1.00 55.64  ? 215 TYR A OH  1 
ATOM   5069 N N   . GLY B 2 225 ? 176.189 173.451 127.917 1.00 63.21  ? 216 GLY A N   1 
ATOM   5070 C CA  . GLY B 2 225 ? 176.242 173.151 129.336 1.00 53.92  ? 216 GLY A CA  1 
ATOM   5071 C C   . GLY B 2 225 ? 176.661 174.344 130.171 1.00 56.57  ? 216 GLY A C   1 
ATOM   5072 O O   . GLY B 2 225 ? 176.113 174.580 131.247 1.00 60.22  ? 216 GLY A O   1 
ATOM   5073 N N   . ARG B 2 226 ? 177.630 175.119 129.681 1.00 58.77  ? 217 ARG A N   1 
ATOM   5074 C CA  . ARG B 2 226 ? 178.086 176.289 130.424 1.00 59.40  ? 217 ARG A CA  1 
ATOM   5075 C C   . ARG B 2 226 ? 176.982 177.333 130.543 1.00 57.46  ? 217 ARG A C   1 
ATOM   5076 O O   . ARG B 2 226 ? 176.739 177.874 131.628 1.00 57.26  ? 217 ARG A O   1 
ATOM   5077 C CB  . ARG B 2 226 ? 179.324 176.884 129.753 1.00 61.42  ? 217 ARG A CB  1 
ATOM   5078 C CG  . ARG B 2 226 ? 179.453 178.385 129.919 1.00 63.71  ? 217 ARG A CG  1 
ATOM   5079 C CD  . ARG B 2 226 ? 180.761 178.896 129.351 1.00 71.06  ? 217 ARG A CD  1 
ATOM   5080 N NE  . ARG B 2 226 ? 180.714 179.023 127.900 1.00 78.82  ? 217 ARG A NE  1 
ATOM   5081 C CZ  . ARG B 2 226 ? 180.112 180.011 127.254 1.00 76.35  ? 217 ARG A CZ  1 
ATOM   5082 N NH1 . ARG B 2 226 ? 179.487 180.981 127.900 1.00 67.32  ? 217 ARG A NH1 1 
ATOM   5083 N NH2 . ARG B 2 226 ? 180.135 180.025 125.925 1.00 73.98  ? 217 ARG A NH2 1 
ATOM   5084 N N   . ASP B 2 227 ? 176.294 177.625 129.435 1.00 57.87  ? 218 ASP A N   1 
ATOM   5085 C CA  . ASP B 2 227 ? 175.210 178.600 129.476 1.00 56.00  ? 218 ASP A CA  1 
ATOM   5086 C C   . ASP B 2 227 ? 174.071 178.125 130.366 1.00 55.06  ? 218 ASP A C   1 
ATOM   5087 O O   . ASP B 2 227 ? 173.525 178.905 131.157 1.00 57.72  ? 218 ASP A O   1 
ATOM   5088 C CB  . ASP B 2 227 ? 174.697 178.881 128.064 1.00 61.60  ? 218 ASP A CB  1 
ATOM   5089 C CG  . ASP B 2 227 ? 175.649 179.733 127.256 1.00 73.25  ? 218 ASP A CG  1 
ATOM   5090 O OD1 . ASP B 2 227 ? 176.769 179.998 127.735 1.00 76.15  ? 218 ASP A OD1 1 
ATOM   5091 O OD2 . ASP B 2 227 ? 175.274 180.143 126.138 1.00 79.31  ? 218 ASP A OD2 1 
ATOM   5092 N N   . ASN B 2 228 ? 173.699 176.849 130.254 1.00 49.64  ? 219 ASN A N   1 
ATOM   5093 C CA  . ASN B 2 228 ? 172.617 176.319 131.074 1.00 46.60  ? 219 ASN A CA  1 
ATOM   5094 C C   . ASN B 2 228 ? 172.975 176.352 132.554 1.00 48.33  ? 219 ASN A C   1 
ATOM   5095 O O   . ASN B 2 228 ? 172.147 176.733 133.388 1.00 54.04  ? 219 ASN A O   1 
ATOM   5096 C CB  . ASN B 2 228 ? 172.280 174.901 130.626 1.00 49.66  ? 219 ASN A CB  1 
ATOM   5097 C CG  . ASN B 2 228 ? 171.170 174.863 129.602 1.00 51.93  ? 219 ASN A CG  1 
ATOM   5098 O OD1 . ASN B 2 228 ? 171.305 175.398 128.504 1.00 52.75  ? 219 ASN A OD1 1 
ATOM   5099 N ND2 . ASN B 2 228 ? 170.062 174.226 129.954 1.00 54.37  ? 219 ASN A ND2 1 
ATOM   5100 N N   . GLY B 2 229 ? 174.206 175.969 132.897 1.00 47.19  ? 220 GLY A N   1 
ATOM   5101 C CA  . GLY B 2 229 ? 174.619 176.004 134.287 1.00 44.75  ? 220 GLY A CA  1 
ATOM   5102 C C   . GLY B 2 229 ? 174.676 177.411 134.844 1.00 47.12  ? 220 GLY A C   1 
ATOM   5103 O O   . GLY B 2 229 ? 174.267 177.652 135.981 1.00 46.88  ? 220 GLY A O   1 
ATOM   5104 N N   . GLN B 2 230 ? 175.186 178.360 134.055 1.00 52.18  ? 221 GLN A N   1 
ATOM   5105 C CA  . GLN B 2 230 ? 175.238 179.745 134.512 1.00 52.56  ? 221 GLN A CA  1 
ATOM   5106 C C   . GLN B 2 230 ? 173.838 180.308 134.722 1.00 47.94  ? 221 GLN A C   1 
ATOM   5107 O O   . GLN B 2 230 ? 173.582 181.001 135.714 1.00 46.01  ? 221 GLN A O   1 
ATOM   5108 C CB  . GLN B 2 230 ? 176.019 180.596 133.512 1.00 54.19  ? 221 GLN A CB  1 
ATOM   5109 C CG  . GLN B 2 230 ? 176.845 181.702 134.149 1.00 61.20  ? 221 GLN A CG  1 
ATOM   5110 C CD  . GLN B 2 230 ? 176.021 182.920 134.507 1.00 68.97  ? 221 GLN A CD  1 
ATOM   5111 O OE1 . GLN B 2 230 ? 174.927 183.120 133.982 1.00 68.38  ? 221 GLN A OE1 1 
ATOM   5112 N NE2 . GLN B 2 230 ? 176.542 183.739 135.413 1.00 66.54  ? 221 GLN A NE2 1 
ATOM   5113 N N   . LEU B 2 231 ? 172.916 180.014 133.802 1.00 49.22  ? 222 LEU A N   1 
ATOM   5114 C CA  . LEU B 2 231 ? 171.549 180.502 133.948 1.00 53.50  ? 222 LEU A CA  1 
ATOM   5115 C C   . LEU B 2 231 ? 170.867 179.882 135.162 1.00 47.77  ? 222 LEU A C   1 
ATOM   5116 O O   . LEU B 2 231 ? 170.192 180.582 135.930 1.00 51.13  ? 222 LEU A O   1 
ATOM   5117 C CB  . LEU B 2 231 ? 170.762 180.218 132.670 1.00 56.97  ? 222 LEU A CB  1 
ATOM   5118 C CG  . LEU B 2 231 ? 169.463 180.993 132.454 1.00 58.32  ? 222 LEU A CG  1 
ATOM   5119 C CD1 . LEU B 2 231 ? 169.745 182.280 131.708 1.00 59.28  ? 222 LEU A CD1 1 
ATOM   5120 C CD2 . LEU B 2 231 ? 168.478 180.149 131.680 1.00 56.10  ? 222 LEU A CD2 1 
ATOM   5121 N N   . LEU B 2 232 ? 171.046 178.572 135.365 1.00 44.53  ? 223 LEU A N   1 
ATOM   5122 C CA  . LEU B 2 232 ? 170.457 177.927 136.533 1.00 43.82  ? 223 LEU A CA  1 
ATOM   5123 C C   . LEU B 2 232 ? 171.035 178.489 137.821 1.00 43.99  ? 223 LEU A C   1 
ATOM   5124 O O   . LEU B 2 232 ? 170.303 178.714 138.787 1.00 42.53  ? 223 LEU A O   1 
ATOM   5125 C CB  . LEU B 2 232 ? 170.665 176.415 136.483 1.00 45.59  ? 223 LEU A CB  1 
ATOM   5126 C CG  . LEU B 2 232 ? 170.312 175.716 137.802 1.00 42.17  ? 223 LEU A CG  1 
ATOM   5127 C CD1 . LEU B 2 232 ? 168.806 175.683 138.014 1.00 35.58  ? 223 LEU A CD1 1 
ATOM   5128 C CD2 . LEU B 2 232 ? 170.890 174.321 137.873 1.00 45.87  ? 223 LEU A CD2 1 
ATOM   5129 N N   . GLY B 2 233 ? 172.348 178.718 137.859 1.00 45.45  ? 224 GLY A N   1 
ATOM   5130 C CA  . GLY B 2 233 ? 172.950 179.285 139.052 1.00 42.82  ? 224 GLY A CA  1 
ATOM   5131 C C   . GLY B 2 233 ? 172.450 180.683 139.351 1.00 44.75  ? 224 GLY A C   1 
ATOM   5132 O O   . GLY B 2 233 ? 172.131 181.006 140.499 1.00 48.77  ? 224 GLY A O   1 
ATOM   5133 N N   . GLU B 2 234 ? 172.365 181.531 138.323 1.00 47.69  ? 225 GLU A N   1 
ATOM   5134 C CA  . GLU B 2 234 ? 171.934 182.905 138.552 1.00 47.12  ? 225 GLU A CA  1 
ATOM   5135 C C   . GLU B 2 234 ? 170.465 182.964 138.948 1.00 51.91  ? 225 GLU A C   1 
ATOM   5136 O O   . GLU B 2 234 ? 170.052 183.868 139.683 1.00 57.54  ? 225 GLU A O   1 
ATOM   5137 C CB  . GLU B 2 234 ? 172.209 183.763 137.316 1.00 49.83  ? 225 GLU A CB  1 
ATOM   5138 C CG  . GLU B 2 234 ? 171.026 183.958 136.390 1.00 56.33  ? 225 GLU A CG  1 
ATOM   5139 C CD  . GLU B 2 234 ? 171.443 184.368 134.993 1.00 64.69  ? 225 GLU A CD  1 
ATOM   5140 O OE1 . GLU B 2 234 ? 172.648 184.613 134.779 1.00 64.09  ? 225 GLU A OE1 1 
ATOM   5141 O OE2 . GLU B 2 234 ? 170.565 184.444 134.108 1.00 67.80  ? 225 GLU A OE2 1 
ATOM   5142 N N   . ARG B 2 235 ? 169.655 182.012 138.477 1.00 48.23  ? 226 ARG A N   1 
ATOM   5143 C CA  . ARG B 2 235 ? 168.264 181.979 138.919 1.00 46.78  ? 226 ARG A CA  1 
ATOM   5144 C C   . ARG B 2 235 ? 168.139 181.406 140.321 1.00 50.88  ? 226 ARG A C   1 
ATOM   5145 O O   . ARG B 2 235 ? 167.328 181.879 141.125 1.00 58.51  ? 226 ARG A O   1 
ATOM   5146 C CB  . ARG B 2 235 ? 167.417 181.165 137.951 1.00 47.93  ? 226 ARG A CB  1 
ATOM   5147 C CG  . ARG B 2 235 ? 165.995 180.965 138.431 1.00 48.27  ? 226 ARG A CG  1 
ATOM   5148 C CD  . ARG B 2 235 ? 165.075 181.004 137.256 1.00 46.76  ? 226 ARG A CD  1 
ATOM   5149 N NE  . ARG B 2 235 ? 165.656 181.849 136.223 1.00 50.65  ? 226 ARG A NE  1 
ATOM   5150 C CZ  . ARG B 2 235 ? 165.281 181.843 134.956 1.00 51.88  ? 226 ARG A CZ  1 
ATOM   5151 N NH1 . ARG B 2 235 ? 164.300 181.068 134.536 1.00 53.49  ? 226 ARG A NH1 1 
ATOM   5152 N NH2 . ARG B 2 235 ? 165.917 182.624 134.089 1.00 54.11  ? 226 ARG A NH2 1 
ATOM   5153 N N   . VAL B 2 236 ? 168.939 180.389 140.633 1.00 51.35  ? 227 VAL A N   1 
ATOM   5154 C CA  . VAL B 2 236 ? 168.817 179.685 141.897 1.00 45.75  ? 227 VAL A CA  1 
ATOM   5155 C C   . VAL B 2 236 ? 169.383 180.507 143.044 1.00 51.24  ? 227 VAL A C   1 
ATOM   5156 O O   . VAL B 2 236 ? 168.981 180.310 144.197 1.00 50.62  ? 227 VAL A O   1 
ATOM   5157 C CB  . VAL B 2 236 ? 169.517 178.320 141.765 1.00 42.33  ? 227 VAL A CB  1 
ATOM   5158 C CG1 . VAL B 2 236 ? 168.830 177.431 140.731 1.00 36.79  ? 227 VAL A CG1 1 
ATOM   5159 C CG2 . VAL B 2 236 ? 170.987 178.480 141.503 1.00 35.82  ? 227 VAL A CG2 1 
ATOM   5160 N N   . ALA B 2 237 ? 170.293 181.442 142.754 1.00 59.40  ? 228 ALA A N   1 
ATOM   5161 C CA  . ALA B 2 237 ? 170.897 182.254 143.801 1.00 58.00  ? 228 ALA A CA  1 
ATOM   5162 C C   . ALA B 2 237 ? 169.921 183.246 144.417 1.00 61.38  ? 228 ALA A C   1 
ATOM   5163 O O   . ALA B 2 237 ? 170.204 183.779 145.495 1.00 68.72  ? 228 ALA A O   1 
ATOM   5164 C CB  . ALA B 2 237 ? 172.111 183.001 143.250 1.00 50.87  ? 228 ALA A CB  1 
ATOM   5165 N N   . ARG B 2 238 ? 168.791 183.516 143.769 1.00 59.86  ? 229 ARG A N   1 
ATOM   5166 C CA  . ARG B 2 238 ? 167.833 184.485 144.282 1.00 63.77  ? 229 ARG A CA  1 
ATOM   5167 C C   . ARG B 2 238 ? 166.557 183.842 144.812 1.00 62.07  ? 229 ARG A C   1 
ATOM   5168 O O   . ARG B 2 238 ? 165.633 184.559 145.206 1.00 64.70  ? 229 ARG A O   1 
ATOM   5169 C CB  . ARG B 2 238 ? 167.500 185.523 143.206 1.00 67.27  ? 229 ARG A CB  1 
ATOM   5170 C CG  . ARG B 2 238 ? 166.383 185.142 142.247 1.00 63.41  ? 229 ARG A CG  1 
ATOM   5171 C CD  . ARG B 2 238 ? 166.726 185.535 140.821 1.00 62.05  ? 229 ARG A CD  1 
ATOM   5172 N NE  . ARG B 2 238 ? 165.624 185.265 139.907 1.00 71.21  ? 229 ARG A NE  1 
ATOM   5173 C CZ  . ARG B 2 238 ? 165.705 185.346 138.586 1.00 70.42  ? 229 ARG A CZ  1 
ATOM   5174 N NH1 . ARG B 2 238 ? 166.835 185.679 137.982 1.00 68.72  ? 229 ARG A NH1 1 
ATOM   5175 N NH2 . ARG B 2 238 ? 164.626 185.091 137.853 1.00 62.09  ? 229 ARG A NH2 1 
ATOM   5176 N N   . ARG B 2 239 ? 166.488 182.513 144.852 1.00 60.78  ? 230 ARG A N   1 
ATOM   5177 C CA  . ARG B 2 239 ? 165.324 181.814 145.383 1.00 59.29  ? 230 ARG A CA  1 
ATOM   5178 C C   . ARG B 2 239 ? 165.690 180.946 146.582 1.00 57.14  ? 230 ARG A C   1 
ATOM   5179 O O   . ARG B 2 239 ? 165.010 179.961 146.875 1.00 52.78  ? 230 ARG A O   1 
ATOM   5180 C CB  . ARG B 2 239 ? 164.647 180.983 144.296 1.00 56.61  ? 230 ARG A CB  1 
ATOM   5181 C CG  . ARG B 2 239 ? 164.166 181.817 143.122 1.00 62.62  ? 230 ARG A CG  1 
ATOM   5182 C CD  . ARG B 2 239 ? 162.751 181.455 142.727 1.00 70.67  ? 230 ARG A CD  1 
ATOM   5183 N NE  . ARG B 2 239 ? 161.810 181.724 143.806 1.00 65.52  ? 230 ARG A NE  1 
ATOM   5184 C CZ  . ARG B 2 239 ? 160.503 181.518 143.729 1.00 65.89  ? 230 ARG A CZ  1 
ATOM   5185 N NH1 . ARG B 2 239 ? 159.940 181.056 142.625 1.00 62.08  ? 230 ARG A NH1 1 
ATOM   5186 N NH2 . ARG B 2 239 ? 159.740 181.787 144.785 1.00 68.02  ? 230 ARG A NH2 1 
ATOM   5187 N N   . ASP B 2 240 ? 166.766 181.312 147.280 1.00 58.56  ? 231 ASP A N   1 
ATOM   5188 C CA  . ASP B 2 240 ? 167.173 180.667 148.530 1.00 58.85  ? 231 ASP A CA  1 
ATOM   5189 C C   . ASP B 2 240 ? 167.467 179.183 148.333 1.00 53.85  ? 231 ASP A C   1 
ATOM   5190 O O   . ASP B 2 240 ? 167.191 178.354 149.202 1.00 51.66  ? 231 ASP A O   1 
ATOM   5191 C CB  . ASP B 2 240 ? 166.121 180.870 149.622 1.00 63.58  ? 231 ASP A CB  1 
ATOM   5192 C CG  . ASP B 2 240 ? 166.397 182.090 150.472 1.00 79.16  ? 231 ASP A CG  1 
ATOM   5193 O OD1 . ASP B 2 240 ? 167.388 182.073 151.234 1.00 87.11  ? 231 ASP A OD1 1 
ATOM   5194 O OD2 . ASP B 2 240 ? 165.626 183.067 150.376 1.00 78.47  ? 231 ASP A OD2 1 
ATOM   5195 N N   . ILE B 2 241 ? 168.030 178.842 147.179 1.00 51.01  ? 232 ILE A N   1 
ATOM   5196 C CA  . ILE B 2 241 ? 168.519 177.497 146.908 1.00 41.42  ? 232 ILE A CA  1 
ATOM   5197 C C   . ILE B 2 241 ? 170.001 177.612 146.593 1.00 40.20  ? 232 ILE A C   1 
ATOM   5198 O O   . ILE B 2 241 ? 170.388 178.345 145.677 1.00 44.84  ? 232 ILE A O   1 
ATOM   5199 C CB  . ILE B 2 241 ? 167.766 176.824 145.750 1.00 35.32  ? 232 ILE A CB  1 
ATOM   5200 C CG1 . ILE B 2 241 ? 166.283 176.680 146.084 1.00 36.41  ? 232 ILE A CG1 1 
ATOM   5201 C CG2 . ILE B 2 241 ? 168.371 175.465 145.444 1.00 35.57  ? 232 ILE A CG2 1 
ATOM   5202 C CD1 . ILE B 2 241 ? 165.467 176.095 144.964 1.00 28.29  ? 232 ILE A CD1 1 
ATOM   5203 N N   . CYS B 2 242 ? 170.824 176.902 147.350 1.00 40.27  ? 233 CYS A N   1 
ATOM   5204 C CA  . CYS B 2 242 ? 172.269 176.979 147.218 1.00 39.61  ? 233 CYS A CA  1 
ATOM   5205 C C   . CYS B 2 242 ? 172.816 175.771 146.468 1.00 35.77  ? 233 CYS A C   1 
ATOM   5206 O O   . CYS B 2 242 ? 172.301 174.656 146.568 1.00 34.38  ? 233 CYS A O   1 
ATOM   5207 C CB  . CYS B 2 242 ? 172.924 177.101 148.597 1.00 39.60  ? 233 CYS A CB  1 
ATOM   5208 S SG  . CYS B 2 242 ? 172.268 178.450 149.621 1.00 69.46  ? 233 CYS A SG  1 
ATOM   5209 N N   . ILE B 2 243 ? 173.873 176.015 145.700 1.00 33.17  ? 234 ILE A N   1 
ATOM   5210 C CA  . ILE B 2 243 ? 174.540 174.989 144.911 1.00 29.48  ? 234 ILE A CA  1 
ATOM   5211 C C   . ILE B 2 243 ? 175.769 174.540 145.686 1.00 32.42  ? 234 ILE A C   1 
ATOM   5212 O O   . ILE B 2 243 ? 176.669 175.346 145.952 1.00 39.10  ? 234 ILE A O   1 
ATOM   5213 C CB  . ILE B 2 243 ? 174.922 175.504 143.515 1.00 27.87  ? 234 ILE A CB  1 
ATOM   5214 C CG1 . ILE B 2 243 ? 173.677 175.700 142.653 1.00 31.56  ? 234 ILE A CG1 1 
ATOM   5215 C CG2 . ILE B 2 243 ? 175.861 174.540 142.830 1.00 27.98  ? 234 ILE A CG2 1 
ATOM   5216 C CD1 . ILE B 2 243 ? 173.955 176.380 141.335 1.00 33.17  ? 234 ILE A CD1 1 
ATOM   5217 N N   . ALA B 2 244 ? 175.803 173.258 146.055 1.00 27.16  ? 235 ALA A N   1 
ATOM   5218 C CA  . ALA B 2 244 ? 176.937 172.726 146.802 1.00 30.93  ? 235 ALA A CA  1 
ATOM   5219 C C   . ALA B 2 244 ? 178.234 172.910 146.028 1.00 39.26  ? 235 ALA A C   1 
ATOM   5220 O O   . ALA B 2 244 ? 179.223 173.425 146.562 1.00 40.91  ? 235 ALA A O   1 
ATOM   5221 C CB  . ALA B 2 244 ? 176.704 171.251 147.122 1.00 30.74  ? 235 ALA A CB  1 
ATOM   5222 N N   . PHE B 2 245 ? 178.242 172.505 144.763 1.00 34.03  ? 236 PHE A N   1 
ATOM   5223 C CA  . PHE B 2 245 ? 179.378 172.727 143.883 1.00 32.06  ? 236 PHE A CA  1 
ATOM   5224 C C   . PHE B 2 245 ? 178.924 172.497 142.453 1.00 37.60  ? 236 PHE A C   1 
ATOM   5225 O O   . PHE B 2 245 ? 177.822 172.007 142.203 1.00 39.05  ? 236 PHE A O   1 
ATOM   5226 C CB  . PHE B 2 245 ? 180.562 171.819 144.236 1.00 36.74  ? 236 PHE A CB  1 
ATOM   5227 C CG  . PHE B 2 245 ? 180.295 170.355 144.029 1.00 36.27  ? 236 PHE A CG  1 
ATOM   5228 C CD1 . PHE B 2 245 ? 179.672 169.608 145.012 1.00 34.31  ? 236 PHE A CD1 1 
ATOM   5229 C CD2 . PHE B 2 245 ? 180.681 169.724 142.862 1.00 36.03  ? 236 PHE A CD2 1 
ATOM   5230 C CE1 . PHE B 2 245 ? 179.428 168.270 144.828 1.00 31.07  ? 236 PHE A CE1 1 
ATOM   5231 C CE2 . PHE B 2 245 ? 180.438 168.385 142.677 1.00 36.75  ? 236 PHE A CE2 1 
ATOM   5232 C CZ  . PHE B 2 245 ? 179.814 167.659 143.663 1.00 32.91  ? 236 PHE A CZ  1 
ATOM   5233 N N   . GLN B 2 246 ? 179.790 172.871 141.518 1.00 42.90  ? 237 GLN A N   1 
ATOM   5234 C CA  . GLN B 2 246 ? 179.557 172.664 140.098 1.00 35.74  ? 237 GLN A CA  1 
ATOM   5235 C C   . GLN B 2 246 ? 180.795 172.026 139.497 1.00 44.13  ? 237 GLN A C   1 
ATOM   5236 O O   . GLN B 2 246 ? 181.917 172.377 139.871 1.00 54.99  ? 237 GLN A O   1 
ATOM   5237 C CB  . GLN B 2 246 ? 179.235 173.979 139.385 1.00 36.46  ? 237 GLN A CB  1 
ATOM   5238 C CG  . GLN B 2 246 ? 178.749 173.801 137.962 1.00 42.09  ? 237 GLN A CG  1 
ATOM   5239 C CD  . GLN B 2 246 ? 179.177 174.931 137.056 1.00 49.60  ? 237 GLN A CD  1 
ATOM   5240 O OE1 . GLN B 2 246 ? 178.394 175.830 136.756 1.00 49.65  ? 237 GLN A OE1 1 
ATOM   5241 N NE2 . GLN B 2 246 ? 180.428 174.895 136.617 1.00 51.57  ? 237 GLN A NE2 1 
ATOM   5242 N N   . GLU B 2 247 ? 180.597 171.085 138.580 1.00 42.66  ? 238 GLU A N   1 
ATOM   5243 C CA  . GLU B 2 247 ? 181.701 170.430 137.901 1.00 46.59  ? 238 GLU A CA  1 
ATOM   5244 C C   . GLU B 2 247 ? 181.387 170.276 136.423 1.00 53.64  ? 238 GLU A C   1 
ATOM   5245 O O   . GLU B 2 247 ? 180.224 170.282 136.014 1.00 55.68  ? 238 GLU A O   1 
ATOM   5246 C CB  . GLU B 2 247 ? 182.018 169.065 138.516 1.00 46.73  ? 238 GLU A CB  1 
ATOM   5247 C CG  . GLU B 2 247 ? 182.795 169.159 139.813 1.00 52.07  ? 238 GLU A CG  1 
ATOM   5248 C CD  . GLU B 2 247 ? 184.267 169.452 139.592 1.00 64.99  ? 238 GLU A CD  1 
ATOM   5249 O OE1 . GLU B 2 247 ? 184.677 169.685 138.436 1.00 57.78  ? 238 GLU A OE1 1 
ATOM   5250 O OE2 . GLU B 2 247 ? 185.017 169.472 140.585 1.00 72.39  ? 238 GLU A OE2 1 
ATOM   5251 N N   . THR B 2 248 ? 182.443 170.145 135.627 1.00 51.09  ? 239 THR A N   1 
ATOM   5252 C CA  . THR B 2 248 ? 182.341 170.023 134.180 1.00 50.61  ? 239 THR A CA  1 
ATOM   5253 C C   . THR B 2 248 ? 182.728 168.607 133.778 1.00 54.07  ? 239 THR A C   1 
ATOM   5254 O O   . THR B 2 248 ? 183.805 168.127 134.143 1.00 59.32  ? 239 THR A O   1 
ATOM   5255 C CB  . THR B 2 248 ? 183.238 171.044 133.480 1.00 52.04  ? 239 THR A CB  1 
ATOM   5256 O OG1 . THR B 2 248 ? 182.672 172.352 133.615 1.00 50.23  ? 239 THR A OG1 1 
ATOM   5257 C CG2 . THR B 2 248 ? 183.375 170.714 132.009 1.00 56.87  ? 239 THR A CG2 1 
ATOM   5258 N N   . LEU B 2 249 ? 181.848 167.943 133.044 1.00 54.84  ? 240 LEU A N   1 
ATOM   5259 C CA  . LEU B 2 249 ? 182.153 166.617 132.531 1.00 57.37  ? 240 LEU A CA  1 
ATOM   5260 C C   . LEU B 2 249 ? 182.958 166.739 131.242 1.00 64.66  ? 240 LEU A C   1 
ATOM   5261 O O   . LEU B 2 249 ? 182.672 167.615 130.419 1.00 62.93  ? 240 LEU A O   1 
ATOM   5262 C CB  . LEU B 2 249 ? 180.867 165.834 132.284 1.00 55.76  ? 240 LEU A CB  1 
ATOM   5263 C CG  . LEU B 2 249 ? 179.818 165.899 133.394 1.00 53.41  ? 240 LEU A CG  1 
ATOM   5264 C CD1 . LEU B 2 249 ? 178.459 165.469 132.875 1.00 55.41  ? 240 LEU A CD1 1 
ATOM   5265 C CD2 . LEU B 2 249 ? 180.236 165.041 134.569 1.00 49.13  ? 240 LEU A CD2 1 
ATOM   5266 N N   . PRO B 2 250 ? 183.965 165.895 131.032 1.00 73.20  ? 241 PRO A N   1 
ATOM   5267 C CA  . PRO B 2 250 ? 184.754 165.987 129.800 1.00 76.95  ? 241 PRO A CA  1 
ATOM   5268 C C   . PRO B 2 250 ? 183.937 165.615 128.574 1.00 79.84  ? 241 PRO A C   1 
ATOM   5269 O O   . PRO B 2 250 ? 183.024 164.788 128.631 1.00 79.02  ? 241 PRO A O   1 
ATOM   5270 C CB  . PRO B 2 250 ? 185.887 164.985 130.034 1.00 78.40  ? 241 PRO A CB  1 
ATOM   5271 C CG  . PRO B 2 250 ? 185.318 164.000 130.991 1.00 70.78  ? 241 PRO A CG  1 
ATOM   5272 C CD  . PRO B 2 250 ? 184.383 164.766 131.878 1.00 66.58  ? 241 PRO A CD  1 
ATOM   5273 N N   . THR B 2 251 ? 184.280 166.242 127.450 1.00 88.36  ? 242 THR A N   1 
ATOM   5274 C CA  . THR B 2 251 ? 183.650 165.906 126.180 1.00 93.00  ? 242 THR A CA  1 
ATOM   5275 C C   . THR B 2 251 ? 184.062 164.499 125.771 1.00 96.42  ? 242 THR A C   1 
ATOM   5276 O O   . THR B 2 251 ? 185.239 164.243 125.499 1.00 98.29  ? 242 THR A O   1 
ATOM   5277 C CB  . THR B 2 251 ? 184.039 166.914 125.102 1.00 91.40  ? 242 THR A CB  1 
ATOM   5278 O OG1 . THR B 2 251 ? 185.466 167.012 125.028 1.00 87.03  ? 242 THR A OG1 1 
ATOM   5279 C CG2 . THR B 2 251 ? 183.452 168.280 125.409 1.00 79.24  ? 242 THR A CG2 1 
ATOM   5280 N N   . LEU B 2 252 ? 183.093 163.584 125.727 1.00 95.48  ? 243 LEU A N   1 
ATOM   5281 C CA  . LEU B 2 252 ? 183.394 162.174 125.479 1.00 101.85 ? 243 LEU A CA  1 
ATOM   5282 C C   . LEU B 2 252 ? 182.231 161.585 124.677 1.00 109.38 ? 243 LEU A C   1 
ATOM   5283 O O   . LEU B 2 252 ? 181.219 161.170 125.244 1.00 104.63 ? 243 LEU A O   1 
ATOM   5284 C CB  . LEU B 2 252 ? 183.611 161.424 126.784 1.00 94.71  ? 243 LEU A CB  1 
ATOM   5285 C CG  . LEU B 2 252 ? 185.012 161.474 127.396 1.00 90.62  ? 243 LEU A CG  1 
ATOM   5286 C CD1 . LEU B 2 252 ? 185.116 160.516 128.571 1.00 86.06  ? 243 LEU A CD1 1 
ATOM   5287 C CD2 . LEU B 2 252 ? 186.070 161.166 126.352 1.00 100.10 ? 243 LEU A CD2 1 
ATOM   5288 N N   . GLN B 2 253 ? 182.392 161.559 123.357 1.00 119.24 ? 244 GLN A N   1 
ATOM   5289 C CA  . GLN B 2 253 ? 181.411 160.902 122.513 1.00 120.77 ? 244 GLN A CA  1 
ATOM   5290 C C   . GLN B 2 253 ? 181.484 159.389 122.714 1.00 123.41 ? 244 GLN A C   1 
ATOM   5291 O O   . GLN B 2 253 ? 182.565 158.833 122.924 1.00 118.84 ? 244 GLN A O   1 
ATOM   5292 C CB  . GLN B 2 253 ? 181.636 161.248 121.043 1.00 125.76 ? 244 GLN A CB  1 
ATOM   5293 C CG  . GLN B 2 253 ? 182.209 162.635 120.800 1.00 125.50 ? 244 GLN A CG  1 
ATOM   5294 C CD  . GLN B 2 253 ? 183.718 162.630 120.665 1.00 129.07 ? 244 GLN A CD  1 
ATOM   5295 O OE1 . GLN B 2 253 ? 184.397 161.758 121.204 1.00 128.07 ? 244 GLN A OE1 1 
ATOM   5296 N NE2 . GLN B 2 253 ? 184.252 163.610 119.944 1.00 128.80 ? 244 GLN A NE2 1 
ATOM   5297 N N   . PRO B 2 254 ? 180.344 158.698 122.657 1.00 129.00 ? 245 PRO A N   1 
ATOM   5298 C CA  . PRO B 2 254 ? 180.354 157.250 122.902 1.00 125.80 ? 245 PRO A CA  1 
ATOM   5299 C C   . PRO B 2 254 ? 180.958 156.477 121.741 1.00 131.12 ? 245 PRO A C   1 
ATOM   5300 O O   . PRO B 2 254 ? 181.314 157.067 120.716 1.00 132.64 ? 245 PRO A O   1 
ATOM   5301 C CB  . PRO B 2 254 ? 178.869 156.920 123.093 1.00 118.10 ? 245 PRO A CB  1 
ATOM   5302 C CG  . PRO B 2 254 ? 178.162 157.942 122.274 1.00 119.16 ? 245 PRO A CG  1 
ATOM   5303 C CD  . PRO B 2 254 ? 178.993 159.198 122.344 1.00 120.36 ? 245 PRO A CD  1 
ATOM   5304 N N   . ASN B 2 255 ? 181.080 155.158 121.901 1.00 132.21 ? 246 ASN A N   1 
ATOM   5305 C CA  . ASN B 2 255 ? 181.630 154.279 120.867 1.00 134.63 ? 246 ASN A CA  1 
ATOM   5306 C C   . ASN B 2 255 ? 183.023 154.732 120.436 1.00 134.02 ? 246 ASN A C   1 
ATOM   5307 O O   . ASN B 2 255 ? 183.366 154.711 119.252 1.00 129.57 ? 246 ASN A O   1 
ATOM   5308 C CB  . ASN B 2 255 ? 180.688 154.188 119.665 1.00 134.96 ? 246 ASN A CB  1 
ATOM   5309 C CG  . ASN B 2 255 ? 179.362 153.539 120.013 1.00 133.34 ? 246 ASN A CG  1 
ATOM   5310 O OD1 . ASN B 2 255 ? 179.180 153.028 121.117 1.00 132.01 ? 246 ASN A OD1 1 
ATOM   5311 N ND2 . ASN B 2 255 ? 178.426 153.561 119.071 1.00 128.10 ? 246 ASN A ND2 1 
ATOM   5312 N N   . GLN B 2 256 ? 183.834 155.144 121.408 1.00 135.30 ? 247 GLN A N   1 
ATOM   5313 C CA  . GLN B 2 256 ? 185.195 155.585 121.142 1.00 132.88 ? 247 GLN A CA  1 
ATOM   5314 C C   . GLN B 2 256 ? 186.070 155.235 122.336 1.00 132.63 ? 247 GLN A C   1 
ATOM   5315 O O   . GLN B 2 256 ? 185.579 154.977 123.438 1.00 126.91 ? 247 GLN A O   1 
ATOM   5316 C CB  . GLN B 2 256 ? 185.261 157.090 120.858 1.00 132.14 ? 247 GLN A CB  1 
ATOM   5317 C CG  . GLN B 2 256 ? 185.586 157.929 122.081 1.00 135.27 ? 247 GLN A CG  1 
ATOM   5318 C CD  . GLN B 2 256 ? 186.321 159.205 121.734 1.00 133.81 ? 247 GLN A CD  1 
ATOM   5319 O OE1 . GLN B 2 256 ? 186.959 159.303 120.686 1.00 133.14 ? 247 GLN A OE1 1 
ATOM   5320 N NE2 . GLN B 2 256 ? 186.254 160.186 122.625 1.00 126.73 ? 247 GLN A NE2 1 
ATOM   5321 N N   . ASN B 2 257 ? 187.380 155.226 122.102 1.00 135.25 ? 248 ASN A N   1 
ATOM   5322 C CA  . ASN B 2 257 ? 188.358 154.902 123.135 1.00 134.29 ? 248 ASN A CA  1 
ATOM   5323 C C   . ASN B 2 257 ? 188.805 156.196 123.807 1.00 129.18 ? 248 ASN A C   1 
ATOM   5324 O O   . ASN B 2 257 ? 189.360 157.085 123.153 1.00 129.29 ? 248 ASN A O   1 
ATOM   5325 C CB  . ASN B 2 257 ? 189.540 154.145 122.532 1.00 139.62 ? 248 ASN A CB  1 
ATOM   5326 C CG  . ASN B 2 257 ? 189.199 152.702 122.204 1.00 146.78 ? 248 ASN A CG  1 
ATOM   5327 O OD1 . ASN B 2 257 ? 188.049 152.379 121.902 1.00 146.76 ? 248 ASN A OD1 1 
ATOM   5328 N ND2 . ASN B 2 257 ? 190.199 151.826 122.258 1.00 147.90 ? 248 ASN A ND2 1 
ATOM   5329 N N   . MET B 2 258 ? 188.563 156.302 125.110 1.00 124.25 ? 249 MET A N   1 
ATOM   5330 C CA  . MET B 2 258 ? 188.847 157.516 125.863 1.00 120.47 ? 249 MET A CA  1 
ATOM   5331 C C   . MET B 2 258 ? 190.121 157.373 126.691 1.00 114.69 ? 249 MET A C   1 
ATOM   5332 O O   . MET B 2 258 ? 190.495 156.276 127.113 1.00 111.76 ? 249 MET A O   1 
ATOM   5333 C CB  . MET B 2 258 ? 187.657 157.872 126.759 1.00 113.86 ? 249 MET A CB  1 
ATOM   5334 C CG  . MET B 2 258 ? 187.298 156.822 127.802 1.00 109.44 ? 249 MET A CG  1 
ATOM   5335 S SD  . MET B 2 258 ? 188.143 157.003 129.380 1.00 112.01 ? 249 MET A SD  1 
ATOM   5336 C CE  . MET B 2 258 ? 186.824 157.671 130.390 1.00 89.27  ? 249 MET A CE  1 
ATOM   5337 N N   . THR B 2 259 ? 190.784 158.506 126.917 1.00 110.52 ? 250 THR A N   1 
ATOM   5338 C CA  . THR B 2 259 ? 192.084 158.523 127.572 1.00 108.73 ? 250 THR A CA  1 
ATOM   5339 C C   . THR B 2 259 ? 191.944 158.393 129.088 1.00 105.26 ? 250 THR A C   1 
ATOM   5340 O O   . THR B 2 259 ? 190.851 158.480 129.652 1.00 106.05 ? 250 THR A O   1 
ATOM   5341 C CB  . THR B 2 259 ? 192.841 159.808 127.234 1.00 108.07 ? 250 THR A CB  1 
ATOM   5342 O OG1 . THR B 2 259 ? 192.505 160.829 128.181 1.00 99.40  ? 250 THR A OG1 1 
ATOM   5343 C CG2 . THR B 2 259 ? 192.479 160.288 125.837 1.00 108.93 ? 250 THR A CG2 1 
ATOM   5344 N N   . SER B 2 260 ? 193.087 158.187 129.749 1.00 103.86 ? 251 SER A N   1 
ATOM   5345 C CA  . SER B 2 260 ? 193.088 157.968 131.192 1.00 100.71 ? 251 SER A CA  1 
ATOM   5346 C C   . SER B 2 260 ? 192.840 159.254 131.970 1.00 96.20  ? 251 SER A C   1 
ATOM   5347 O O   . SER B 2 260 ? 192.337 159.204 133.098 1.00 90.95  ? 251 SER A O   1 
ATOM   5348 C CB  . SER B 2 260 ? 194.413 157.344 131.626 1.00 101.55 ? 251 SER A CB  1 
ATOM   5349 O OG  . SER B 2 260 ? 195.454 158.303 131.596 1.00 104.69 ? 251 SER A OG  1 
ATOM   5350 N N   . GLU B 2 261 ? 193.209 160.407 131.406 1.00 100.71 ? 252 GLU A N   1 
ATOM   5351 C CA  . GLU B 2 261 ? 192.958 161.673 132.089 1.00 98.97  ? 252 GLU A CA  1 
ATOM   5352 C C   . GLU B 2 261 ? 191.465 161.913 132.268 1.00 87.73  ? 252 GLU A C   1 
ATOM   5353 O O   . GLU B 2 261 ? 191.022 162.360 133.333 1.00 81.07  ? 252 GLU A O   1 
ATOM   5354 C CB  . GLU B 2 261 ? 193.596 162.826 131.317 1.00 102.51 ? 252 GLU A CB  1 
ATOM   5355 C CG  . GLU B 2 261 ? 195.093 162.686 131.111 1.00 101.68 ? 252 GLU A CG  1 
ATOM   5356 C CD  . GLU B 2 261 ? 195.805 164.021 131.131 1.00 102.42 ? 252 GLU A CD  1 
ATOM   5357 O OE1 . GLU B 2 261 ? 195.705 164.731 132.152 1.00 102.74 ? 252 GLU A OE1 1 
ATOM   5358 O OE2 . GLU B 2 261 ? 196.462 164.362 130.125 1.00 106.79 ? 252 GLU A OE2 1 
ATOM   5359 N N   . GLU B 2 262 ? 190.673 161.616 131.237 1.00 88.18  ? 253 GLU A N   1 
ATOM   5360 C CA  . GLU B 2 262 ? 189.226 161.715 131.366 1.00 83.93  ? 253 GLU A CA  1 
ATOM   5361 C C   . GLU B 2 262 ? 188.696 160.741 132.409 1.00 76.76  ? 253 GLU A C   1 
ATOM   5362 O O   . GLU B 2 262 ? 187.762 161.071 133.149 1.00 68.05  ? 253 GLU A O   1 
ATOM   5363 C CB  . GLU B 2 262 ? 188.560 161.460 130.013 1.00 90.80  ? 253 GLU A CB  1 
ATOM   5364 C CG  . GLU B 2 262 ? 189.303 162.037 128.810 1.00 94.71  ? 253 GLU A CG  1 
ATOM   5365 C CD  . GLU B 2 262 ? 189.154 163.543 128.657 1.00 94.25  ? 253 GLU A CD  1 
ATOM   5366 O OE1 . GLU B 2 262 ? 188.972 164.248 129.671 1.00 94.87  ? 253 GLU A OE1 1 
ATOM   5367 O OE2 . GLU B 2 262 ? 189.216 164.026 127.506 1.00 91.33  ? 253 GLU A OE2 1 
ATOM   5368 N N   . ARG B 2 263 ? 189.273 159.540 132.476 1.00 79.78  ? 254 ARG A N   1 
ATOM   5369 C CA  . ARG B 2 263 ? 188.847 158.557 133.466 1.00 78.92  ? 254 ARG A CA  1 
ATOM   5370 C C   . ARG B 2 263 ? 189.111 159.058 134.880 1.00 72.43  ? 254 ARG A C   1 
ATOM   5371 O O   . ARG B 2 263 ? 188.266 158.914 135.772 1.00 73.60  ? 254 ARG A O   1 
ATOM   5372 C CB  . ARG B 2 263 ? 189.565 157.232 133.213 1.00 86.65  ? 254 ARG A CB  1 
ATOM   5373 C CG  . ARG B 2 263 ? 189.218 156.123 134.185 1.00 88.38  ? 254 ARG A CG  1 
ATOM   5374 C CD  . ARG B 2 263 ? 189.937 154.835 133.809 1.00 97.09  ? 254 ARG A CD  1 
ATOM   5375 N NE  . ARG B 2 263 ? 189.901 154.582 132.373 1.00 106.50 ? 254 ARG A NE  1 
ATOM   5376 C CZ  . ARG B 2 263 ? 188.863 154.070 131.724 1.00 106.85 ? 254 ARG A CZ  1 
ATOM   5377 N NH1 . ARG B 2 263 ? 187.747 153.740 132.354 1.00 99.79  ? 254 ARG A NH1 1 
ATOM   5378 N NH2 . ARG B 2 263 ? 188.947 153.883 130.410 1.00 103.82 ? 254 ARG A NH2 1 
ATOM   5379 N N   . GLN B 2 264 ? 190.282 159.659 135.102 1.00 73.83  ? 255 GLN A N   1 
ATOM   5380 C CA  . GLN B 2 264 ? 190.592 160.217 136.415 1.00 70.57  ? 255 GLN A CA  1 
ATOM   5381 C C   . GLN B 2 264 ? 189.690 161.402 136.738 1.00 65.11  ? 255 GLN A C   1 
ATOM   5382 O O   . GLN B 2 264 ? 189.292 161.593 137.893 1.00 61.90  ? 255 GLN A O   1 
ATOM   5383 C CB  . GLN B 2 264 ? 192.065 160.625 136.476 1.00 74.80  ? 255 GLN A CB  1 
ATOM   5384 C CG  . GLN B 2 264 ? 192.636 160.893 137.878 1.00 73.53  ? 255 GLN A CG  1 
ATOM   5385 C CD  . GLN B 2 264 ? 192.041 160.032 138.989 1.00 77.85  ? 255 GLN A CD  1 
ATOM   5386 O OE1 . GLN B 2 264 ? 191.789 158.845 138.786 1.00 74.76  ? 255 GLN A OE1 1 
ATOM   5387 N NE2 . GLN B 2 264 ? 191.728 160.645 140.128 1.00 76.04  ? 255 GLN A NE2 1 
ATOM   5388 N N   . ARG B 2 265 ? 189.368 162.218 135.733 1.00 68.50  ? 256 ARG A N   1 
ATOM   5389 C CA  . ARG B 2 265 ? 188.436 163.320 135.942 1.00 62.23  ? 256 ARG A CA  1 
ATOM   5390 C C   . ARG B 2 265 ? 187.066 162.809 136.373 1.00 60.69  ? 256 ARG A C   1 
ATOM   5391 O O   . ARG B 2 265 ? 186.456 163.349 137.304 1.00 57.21  ? 256 ARG A O   1 
ATOM   5392 C CB  . ARG B 2 265 ? 188.330 164.149 134.665 1.00 66.43  ? 256 ARG A CB  1 
ATOM   5393 C CG  . ARG B 2 265 ? 187.244 165.204 134.674 1.00 68.71  ? 256 ARG A CG  1 
ATOM   5394 C CD  . ARG B 2 265 ? 187.765 166.528 135.210 1.00 69.84  ? 256 ARG A CD  1 
ATOM   5395 N NE  . ARG B 2 265 ? 187.041 167.675 134.671 1.00 76.26  ? 256 ARG A NE  1 
ATOM   5396 C CZ  . ARG B 2 265 ? 187.015 168.021 133.390 1.00 75.03  ? 256 ARG A CZ  1 
ATOM   5397 N NH1 . ARG B 2 265 ? 187.696 167.351 132.475 1.00 77.03  ? 256 ARG A NH1 1 
ATOM   5398 N NH2 . ARG B 2 265 ? 186.301 169.080 133.019 1.00 61.69  ? 256 ARG A NH2 1 
ATOM   5399 N N   . LEU B 2 266 ? 186.569 161.764 135.708 1.00 63.57  ? 257 LEU A N   1 
ATOM   5400 C CA  . LEU B 2 266 ? 185.293 161.171 136.097 1.00 57.99  ? 257 LEU A CA  1 
ATOM   5401 C C   . LEU B 2 266 ? 185.366 160.580 137.499 1.00 55.61  ? 257 LEU A C   1 
ATOM   5402 O O   . LEU B 2 266 ? 184.416 160.700 138.281 1.00 57.27  ? 257 LEU A O   1 
ATOM   5403 C CB  . LEU B 2 266 ? 184.881 160.105 135.085 1.00 56.43  ? 257 LEU A CB  1 
ATOM   5404 C CG  . LEU B 2 266 ? 184.359 160.629 133.749 1.00 58.66  ? 257 LEU A CG  1 
ATOM   5405 C CD1 . LEU B 2 266 ? 184.320 159.512 132.728 1.00 65.33  ? 257 LEU A CD1 1 
ATOM   5406 C CD2 . LEU B 2 266 ? 182.990 161.259 133.910 1.00 59.54  ? 257 LEU A CD2 1 
ATOM   5407 N N   . VAL B 2 267 ? 186.485 159.934 137.830 1.00 55.69  ? 258 VAL A N   1 
ATOM   5408 C CA  . VAL B 2 267 ? 186.664 159.383 139.170 1.00 51.49  ? 258 VAL A CA  1 
ATOM   5409 C C   . VAL B 2 267 ? 186.564 160.490 140.210 1.00 51.91  ? 258 VAL A C   1 
ATOM   5410 O O   . VAL B 2 267 ? 185.864 160.359 141.220 1.00 55.02  ? 258 VAL A O   1 
ATOM   5411 C CB  . VAL B 2 267 ? 188.011 158.642 139.265 1.00 59.60  ? 258 VAL A CB  1 
ATOM   5412 C CG1 . VAL B 2 267 ? 188.461 158.514 140.715 1.00 62.32  ? 258 VAL A CG1 1 
ATOM   5413 C CG2 . VAL B 2 267 ? 187.923 157.282 138.604 1.00 59.83  ? 258 VAL A CG2 1 
ATOM   5414 N N   . THR B 2 268 ? 187.253 161.607 139.965 1.00 56.19  ? 259 THR A N   1 
ATOM   5415 C CA  . THR B 2 268 ? 187.234 162.718 140.910 1.00 51.33  ? 259 THR A CA  1 
ATOM   5416 C C   . THR B 2 268 ? 185.838 163.321 141.032 1.00 50.67  ? 259 THR A C   1 
ATOM   5417 O O   . THR B 2 268 ? 185.387 163.641 142.138 1.00 51.12  ? 259 THR A O   1 
ATOM   5418 C CB  . THR B 2 268 ? 188.247 163.781 140.485 1.00 51.02  ? 259 THR A CB  1 
ATOM   5419 O OG1 . THR B 2 268 ? 189.563 163.218 140.499 1.00 52.70  ? 259 THR A OG1 1 
ATOM   5420 C CG2 . THR B 2 268 ? 188.216 164.954 141.438 1.00 49.05  ? 259 THR A CG2 1 
ATOM   5421 N N   . ILE B 2 269 ? 185.134 163.474 139.908 1.00 50.68  ? 260 ILE A N   1 
ATOM   5422 C CA  . ILE B 2 269 ? 183.793 164.055 139.941 1.00 45.69  ? 260 ILE A CA  1 
ATOM   5423 C C   . ILE B 2 269 ? 182.838 163.167 140.732 1.00 44.07  ? 260 ILE A C   1 
ATOM   5424 O O   . ILE B 2 269 ? 182.061 163.652 141.563 1.00 44.84  ? 260 ILE A O   1 
ATOM   5425 C CB  . ILE B 2 269 ? 183.283 164.303 138.509 1.00 50.45  ? 260 ILE A CB  1 
ATOM   5426 C CG1 . ILE B 2 269 ? 183.997 165.503 137.889 1.00 56.56  ? 260 ILE A CG1 1 
ATOM   5427 C CG2 . ILE B 2 269 ? 181.781 164.522 138.505 1.00 44.25  ? 260 ILE A CG2 1 
ATOM   5428 C CD1 . ILE B 2 269 ? 183.596 165.778 136.460 1.00 56.14  ? 260 ILE A CD1 1 
ATOM   5429 N N   . VAL B 2 270 ? 182.879 161.855 140.491 1.00 43.28  ? 261 VAL A N   1 
ATOM   5430 C CA  . VAL B 2 270 ? 181.976 160.952 141.200 1.00 44.01  ? 261 VAL A CA  1 
ATOM   5431 C C   . VAL B 2 270 ? 182.346 160.867 142.678 1.00 46.36  ? 261 VAL A C   1 
ATOM   5432 O O   . VAL B 2 270 ? 181.471 160.732 143.541 1.00 49.00  ? 261 VAL A O   1 
ATOM   5433 C CB  . VAL B 2 270 ? 181.957 159.569 140.526 1.00 41.82  ? 261 VAL A CB  1 
ATOM   5434 C CG1 . VAL B 2 270 ? 181.056 158.619 141.286 1.00 36.71  ? 261 VAL A CG1 1 
ATOM   5435 C CG2 . VAL B 2 270 ? 181.470 159.699 139.100 1.00 45.29  ? 261 VAL A CG2 1 
ATOM   5436 N N   . ASP B 2 271 ? 183.639 160.945 143.001 1.00 48.65  ? 262 ASP A N   1 
ATOM   5437 C CA  . ASP B 2 271 ? 184.037 160.967 144.404 1.00 46.77  ? 262 ASP A CA  1 
ATOM   5438 C C   . ASP B 2 271 ? 183.534 162.226 145.100 1.00 43.83  ? 262 ASP A C   1 
ATOM   5439 O O   . ASP B 2 271 ? 183.106 162.177 146.259 1.00 46.06  ? 262 ASP A O   1 
ATOM   5440 C CB  . ASP B 2 271 ? 185.555 160.857 144.521 1.00 49.29  ? 262 ASP A CB  1 
ATOM   5441 C CG  . ASP B 2 271 ? 185.987 159.788 145.502 1.00 62.03  ? 262 ASP A CG  1 
ATOM   5442 O OD1 . ASP B 2 271 ? 185.118 159.019 145.964 1.00 61.02  ? 262 ASP A OD1 1 
ATOM   5443 O OD2 . ASP B 2 271 ? 187.194 159.715 145.810 1.00 68.37  ? 262 ASP A OD2 1 
ATOM   5444 N N   . LYS B 2 272 ? 183.589 163.367 144.410 1.00 45.35  ? 263 LYS A N   1 
ATOM   5445 C CA  . LYS B 2 272 ? 183.042 164.600 144.968 1.00 40.71  ? 263 LYS A CA  1 
ATOM   5446 C C   . LYS B 2 272 ? 181.535 164.499 145.156 1.00 39.09  ? 263 LYS A C   1 
ATOM   5447 O O   . LYS B 2 272 ? 180.994 165.002 146.146 1.00 41.99  ? 263 LYS A O   1 
ATOM   5448 C CB  . LYS B 2 272 ? 183.399 165.780 144.069 1.00 39.32  ? 263 LYS A CB  1 
ATOM   5449 C CG  . LYS B 2 272 ? 184.718 166.423 144.425 1.00 42.71  ? 263 LYS A CG  1 
ATOM   5450 C CD  . LYS B 2 272 ? 184.938 167.694 143.648 1.00 40.96  ? 263 LYS A CD  1 
ATOM   5451 C CE  . LYS B 2 272 ? 186.083 167.528 142.674 1.00 45.32  ? 263 LYS A CE  1 
ATOM   5452 N NZ  . LYS B 2 272 ? 187.099 168.606 142.807 1.00 46.72  ? 263 LYS A NZ  1 
ATOM   5453 N N   . LEU B 2 273 ? 180.842 163.865 144.209 1.00 42.92  ? 264 LEU A N   1 
ATOM   5454 C CA  . LEU B 2 273 ? 179.412 163.622 144.374 1.00 39.95  ? 264 LEU A CA  1 
ATOM   5455 C C   . LEU B 2 273 ? 179.136 162.770 145.605 1.00 39.04  ? 264 LEU A C   1 
ATOM   5456 O O   . LEU B 2 273 ? 178.235 163.075 146.394 1.00 43.58  ? 264 LEU A O   1 
ATOM   5457 C CB  . LEU B 2 273 ? 178.849 162.937 143.131 1.00 38.34  ? 264 LEU A CB  1 
ATOM   5458 C CG  . LEU B 2 273 ? 178.025 163.757 142.140 1.00 39.01  ? 264 LEU A CG  1 
ATOM   5459 C CD1 . LEU B 2 273 ? 178.794 164.971 141.675 1.00 39.58  ? 264 LEU A CD1 1 
ATOM   5460 C CD2 . LEU B 2 273 ? 177.637 162.888 140.961 1.00 43.93  ? 264 LEU A CD2 1 
ATOM   5461 N N   . GLN B 2 274 ? 179.903 161.694 145.780 1.00 40.95  ? 265 GLN A N   1 
ATOM   5462 C CA  . GLN B 2 274 ? 179.664 160.768 146.881 1.00 41.24  ? 265 GLN A CA  1 
ATOM   5463 C C   . GLN B 2 274 ? 179.962 161.411 148.229 1.00 44.91  ? 265 GLN A C   1 
ATOM   5464 O O   . GLN B 2 274 ? 179.247 161.172 149.209 1.00 49.52  ? 265 GLN A O   1 
ATOM   5465 C CB  . GLN B 2 274 ? 180.507 159.511 146.690 1.00 44.93  ? 265 GLN A CB  1 
ATOM   5466 C CG  . GLN B 2 274 ? 180.288 158.449 147.744 1.00 51.88  ? 265 GLN A CG  1 
ATOM   5467 C CD  . GLN B 2 274 ? 179.745 157.166 147.156 1.00 60.46  ? 265 GLN A CD  1 
ATOM   5468 O OE1 . GLN B 2 274 ? 180.269 156.655 146.167 1.00 61.28  ? 265 GLN A OE1 1 
ATOM   5469 N NE2 . GLN B 2 274 ? 178.686 156.639 147.758 1.00 60.29  ? 265 GLN A NE2 1 
ATOM   5470 N N   . GLN B 2 275 ? 181.017 162.224 148.302 1.00 43.41  ? 266 GLN A N   1 
ATOM   5471 C CA  . GLN B 2 275 ? 181.368 162.871 149.562 1.00 37.41  ? 266 GLN A CA  1 
ATOM   5472 C C   . GLN B 2 275 ? 180.351 163.941 149.943 1.00 43.21  ? 266 GLN A C   1 
ATOM   5473 O O   . GLN B 2 275 ? 180.097 164.169 151.131 1.00 47.08  ? 266 GLN A O   1 
ATOM   5474 C CB  . GLN B 2 275 ? 182.773 163.462 149.460 1.00 43.07  ? 266 GLN A CB  1 
ATOM   5475 C CG  . GLN B 2 275 ? 183.038 164.658 150.359 1.00 53.96  ? 266 GLN A CG  1 
ATOM   5476 C CD  . GLN B 2 275 ? 184.057 165.609 149.767 1.00 58.13  ? 266 GLN A CD  1 
ATOM   5477 O OE1 . GLN B 2 275 ? 185.256 165.476 150.004 1.00 58.67  ? 266 GLN A OE1 1 
ATOM   5478 N NE2 . GLN B 2 275 ? 183.584 166.574 148.986 1.00 52.52  ? 266 GLN A NE2 1 
ATOM   5479 N N   . SER B 2 276 ? 179.749 164.593 148.953 1.00 43.68  ? 267 SER A N   1 
ATOM   5480 C CA  . SER B 2 276 ? 178.826 165.687 149.214 1.00 43.23  ? 267 SER A CA  1 
ATOM   5481 C C   . SER B 2 276 ? 177.571 165.200 149.928 1.00 48.32  ? 267 SER A C   1 
ATOM   5482 O O   . SER B 2 276 ? 177.157 164.047 149.795 1.00 50.25  ? 267 SER A O   1 
ATOM   5483 C CB  . SER B 2 276 ? 178.438 166.378 147.909 1.00 43.48  ? 267 SER A CB  1 
ATOM   5484 O OG  . SER B 2 276 ? 177.936 167.678 148.155 1.00 49.27  ? 267 SER A OG  1 
ATOM   5485 N N   . THR B 2 277 ? 176.968 166.101 150.699 1.00 43.95  ? 268 THR A N   1 
ATOM   5486 C CA  . THR B 2 277 ? 175.717 165.828 151.390 1.00 45.14  ? 268 THR A CA  1 
ATOM   5487 C C   . THR B 2 277 ? 174.495 166.235 150.575 1.00 49.00  ? 268 THR A C   1 
ATOM   5488 O O   . THR B 2 277 ? 173.366 165.956 150.993 1.00 48.96  ? 268 THR A O   1 
ATOM   5489 C CB  . THR B 2 277 ? 175.712 166.535 152.754 1.00 42.68  ? 268 THR A CB  1 
ATOM   5490 O OG1 . THR B 2 277 ? 174.432 166.394 153.381 1.00 56.09  ? 268 THR A OG1 1 
ATOM   5491 C CG2 . THR B 2 277 ? 176.035 168.006 152.599 1.00 39.10  ? 268 THR A CG2 1 
ATOM   5492 N N   . ALA B 2 278 ? 174.692 166.872 149.424 1.00 45.59  ? 269 ALA A N   1 
ATOM   5493 C CA  . ALA B 2 278 ? 173.581 167.198 148.541 1.00 38.08  ? 269 ALA A CA  1 
ATOM   5494 C C   . ALA B 2 278 ? 173.198 165.983 147.709 1.00 36.90  ? 269 ALA A C   1 
ATOM   5495 O O   . ALA B 2 278 ? 174.050 165.340 147.092 1.00 39.09  ? 269 ALA A O   1 
ATOM   5496 C CB  . ALA B 2 278 ? 173.950 168.362 147.626 1.00 32.87  ? 269 ALA A CB  1 
ATOM   5497 N N   . ARG B 2 279 ? 171.903 165.674 147.685 1.00 33.26  ? 270 ARG A N   1 
ATOM   5498 C CA  . ARG B 2 279 ? 171.415 164.456 147.052 1.00 32.32  ? 270 ARG A CA  1 
ATOM   5499 C C   . ARG B 2 279 ? 170.467 164.758 145.899 1.00 32.21  ? 270 ARG A C   1 
ATOM   5500 O O   . ARG B 2 279 ? 169.611 163.938 145.564 1.00 34.29  ? 270 ARG A O   1 
ATOM   5501 C CB  . ARG B 2 279 ? 170.742 163.546 148.078 1.00 32.30  ? 270 ARG A CB  1 
ATOM   5502 C CG  . ARG B 2 279 ? 171.726 162.789 148.947 1.00 39.16  ? 270 ARG A CG  1 
ATOM   5503 C CD  . ARG B 2 279 ? 172.772 162.100 148.091 1.00 39.53  ? 270 ARG A CD  1 
ATOM   5504 N NE  . ARG B 2 279 ? 173.908 161.629 148.872 1.00 50.29  ? 270 ARG A NE  1 
ATOM   5505 C CZ  . ARG B 2 279 ? 175.176 161.855 148.555 1.00 46.87  ? 270 ARG A CZ  1 
ATOM   5506 N NH1 . ARG B 2 279 ? 175.507 162.574 147.497 1.00 40.91  ? 270 ARG A NH1 1 
ATOM   5507 N NH2 . ARG B 2 279 ? 176.135 161.346 149.321 1.00 46.08  ? 270 ARG A NH2 1 
ATOM   5508 N N   . VAL B 2 280 ? 170.597 165.935 145.292 1.00 27.17  ? 271 VAL A N   1 
ATOM   5509 C CA  . VAL B 2 280 ? 169.861 166.293 144.085 1.00 22.02  ? 271 VAL A CA  1 
ATOM   5510 C C   . VAL B 2 280 ? 170.875 166.849 143.098 1.00 25.12  ? 271 VAL A C   1 
ATOM   5511 O O   . VAL B 2 280 ? 171.543 167.847 143.388 1.00 25.48  ? 271 VAL A O   1 
ATOM   5512 C CB  . VAL B 2 280 ? 168.745 167.312 144.352 1.00 24.24  ? 271 VAL A CB  1 
ATOM   5513 C CG1 . VAL B 2 280 ? 168.246 167.906 143.050 1.00 26.22  ? 271 VAL A CG1 1 
ATOM   5514 C CG2 . VAL B 2 280 ? 167.606 166.650 145.091 1.00 25.00  ? 271 VAL A CG2 1 
ATOM   5515 N N   . VAL B 2 281 ? 170.995 166.210 141.937 1.00 25.04  ? 272 VAL A N   1 
ATOM   5516 C CA  . VAL B 2 281 ? 172.013 166.538 140.946 1.00 24.99  ? 272 VAL A CA  1 
ATOM   5517 C C   . VAL B 2 281 ? 171.317 166.949 139.658 1.00 28.49  ? 272 VAL A C   1 
ATOM   5518 O O   . VAL B 2 281 ? 170.475 166.211 139.137 1.00 33.80  ? 272 VAL A O   1 
ATOM   5519 C CB  . VAL B 2 281 ? 172.965 165.358 140.701 1.00 22.54  ? 272 VAL A CB  1 
ATOM   5520 C CG1 . VAL B 2 281 ? 174.214 165.825 139.984 1.00 28.64  ? 272 VAL A CG1 1 
ATOM   5521 C CG2 . VAL B 2 281 ? 173.323 164.682 142.011 1.00 22.48  ? 272 VAL A CG2 1 
ATOM   5522 N N   . VAL B 2 282 ? 171.672 168.120 139.143 1.00 25.42  ? 273 VAL A N   1 
ATOM   5523 C CA  . VAL B 2 282 ? 171.181 168.610 137.862 1.00 28.35  ? 273 VAL A CA  1 
ATOM   5524 C C   . VAL B 2 282 ? 172.300 168.444 136.848 1.00 35.50  ? 273 VAL A C   1 
ATOM   5525 O O   . VAL B 2 282 ? 173.429 168.886 137.085 1.00 40.68  ? 273 VAL A O   1 
ATOM   5526 C CB  . VAL B 2 282 ? 170.735 170.077 137.952 1.00 30.32  ? 273 VAL A CB  1 
ATOM   5527 C CG1 . VAL B 2 282 ? 170.034 170.491 136.675 1.00 34.52  ? 273 VAL A CG1 1 
ATOM   5528 C CG2 . VAL B 2 282 ? 169.839 170.286 139.152 1.00 27.58  ? 273 VAL A CG2 1 
ATOM   5529 N N   . VAL B 2 283 ? 172.000 167.806 135.721 1.00 35.84  ? 274 VAL A N   1 
ATOM   5530 C CA  . VAL B 2 283 ? 172.993 167.520 134.692 1.00 36.59  ? 274 VAL A CA  1 
ATOM   5531 C C   . VAL B 2 283 ? 172.623 168.295 133.436 1.00 45.85  ? 274 VAL A C   1 
ATOM   5532 O O   . VAL B 2 283 ? 171.518 168.141 132.902 1.00 47.49  ? 274 VAL A O   1 
ATOM   5533 C CB  . VAL B 2 283 ? 173.097 166.015 134.407 1.00 39.76  ? 274 VAL A CB  1 
ATOM   5534 C CG1 . VAL B 2 283 ? 174.399 165.703 133.701 1.00 47.68  ? 274 VAL A CG1 1 
ATOM   5535 C CG2 . VAL B 2 283 ? 173.001 165.227 135.701 1.00 39.78  ? 274 VAL A CG2 1 
ATOM   5536 N N   . PHE B 2 284 ? 173.551 169.125 132.966 1.00 47.90  ? 275 PHE A N   1 
ATOM   5537 C CA  . PHE B 2 284 ? 173.407 169.923 131.751 1.00 45.08  ? 275 PHE A CA  1 
ATOM   5538 C C   . PHE B 2 284 ? 174.482 169.448 130.785 1.00 49.93  ? 275 PHE A C   1 
ATOM   5539 O O   . PHE B 2 284 ? 175.594 169.980 130.775 1.00 58.92  ? 275 PHE A O   1 
ATOM   5540 C CB  . PHE B 2 284 ? 173.562 171.404 132.034 1.00 45.17  ? 275 PHE A CB  1 
ATOM   5541 C CG  . PHE B 2 284 ? 172.423 171.999 132.784 1.00 47.63  ? 275 PHE A CG  1 
ATOM   5542 C CD1 . PHE B 2 284 ? 171.163 172.062 132.224 1.00 48.65  ? 275 PHE A CD1 1 
ATOM   5543 C CD2 . PHE B 2 284 ? 172.614 172.506 134.052 1.00 50.54  ? 275 PHE A CD2 1 
ATOM   5544 C CE1 . PHE B 2 284 ? 170.118 172.617 132.918 1.00 48.96  ? 275 PHE A CE1 1 
ATOM   5545 C CE2 . PHE B 2 284 ? 171.574 173.059 134.747 1.00 48.39  ? 275 PHE A CE2 1 
ATOM   5546 C CZ  . PHE B 2 284 ? 170.325 173.114 134.183 1.00 44.79  ? 275 PHE A CZ  1 
ATOM   5547 N N   . SER B 2 285 ? 174.159 168.451 129.972 1.00 49.15  ? 276 SER A N   1 
ATOM   5548 C CA  . SER B 2 285 ? 175.128 167.923 129.029 1.00 56.53  ? 276 SER A CA  1 
ATOM   5549 C C   . SER B 2 285 ? 174.387 167.362 127.831 1.00 65.72  ? 276 SER A C   1 
ATOM   5550 O O   . SER B 2 285 ? 173.203 167.021 127.942 1.00 67.01  ? 276 SER A O   1 
ATOM   5551 C CB  . SER B 2 285 ? 176.000 166.836 129.670 1.00 58.95  ? 276 SER A CB  1 
ATOM   5552 O OG  . SER B 2 285 ? 175.218 165.987 130.480 1.00 61.67  ? 276 SER A OG  1 
ATOM   5553 N N   . PRO B 2 286 ? 175.041 167.268 126.675 1.00 70.57  ? 277 PRO A N   1 
ATOM   5554 C CA  . PRO B 2 286 ? 174.404 166.635 125.520 1.00 74.31  ? 277 PRO A CA  1 
ATOM   5555 C C   . PRO B 2 286 ? 174.101 165.170 125.792 1.00 76.06  ? 277 PRO A C   1 
ATOM   5556 O O   . PRO B 2 286 ? 174.731 164.514 126.622 1.00 74.71  ? 277 PRO A O   1 
ATOM   5557 C CB  . PRO B 2 286 ? 175.446 166.792 124.408 1.00 73.02  ? 277 PRO A CB  1 
ATOM   5558 C CG  . PRO B 2 286 ? 176.272 167.954 124.831 1.00 68.27  ? 277 PRO A CG  1 
ATOM   5559 C CD  . PRO B 2 286 ? 176.334 167.877 126.323 1.00 67.24  ? 277 PRO A CD  1 
ATOM   5560 N N   . ASP B 2 287 ? 173.106 164.661 125.069 1.00 78.58  ? 278 ASP A N   1 
ATOM   5561 C CA  . ASP B 2 287 ? 172.647 163.292 125.259 1.00 83.19  ? 278 ASP A CA  1 
ATOM   5562 C C   . ASP B 2 287 ? 173.698 162.248 124.908 1.00 87.59  ? 278 ASP A C   1 
ATOM   5563 O O   . ASP B 2 287 ? 173.525 161.081 125.272 1.00 84.67  ? 278 ASP A O   1 
ATOM   5564 C CB  . ASP B 2 287 ? 171.377 163.052 124.437 1.00 88.06  ? 278 ASP A CB  1 
ATOM   5565 C CG  . ASP B 2 287 ? 171.537 163.421 122.964 1.00 95.06  ? 278 ASP A CG  1 
ATOM   5566 O OD1 . ASP B 2 287 ? 172.664 163.725 122.522 1.00 95.08  ? 278 ASP A OD1 1 
ATOM   5567 O OD2 . ASP B 2 287 ? 170.519 163.406 122.240 1.00 88.24  ? 278 ASP A OD2 1 
ATOM   5568 N N   . LEU B 2 288 ? 174.772 162.630 124.219 1.00 95.33  ? 279 LEU A N   1 
ATOM   5569 C CA  . LEU B 2 288 ? 175.783 161.674 123.783 1.00 96.34  ? 279 LEU A CA  1 
ATOM   5570 C C   . LEU B 2 288 ? 176.891 161.469 124.811 1.00 92.06  ? 279 LEU A C   1 
ATOM   5571 O O   . LEU B 2 288 ? 177.486 160.389 124.868 1.00 95.99  ? 279 LEU A O   1 
ATOM   5572 C CB  . LEU B 2 288 ? 176.388 162.130 122.453 1.00 96.18  ? 279 LEU A CB  1 
ATOM   5573 C CG  . LEU B 2 288 ? 175.376 162.452 121.350 1.00 98.84  ? 279 LEU A CG  1 
ATOM   5574 C CD1 . LEU B 2 288 ? 176.018 163.269 120.238 1.00 106.47 ? 279 LEU A CD1 1 
ATOM   5575 C CD2 . LEU B 2 288 ? 174.749 161.181 120.795 1.00 100.31 ? 279 LEU A CD2 1 
ATOM   5576 N N   . THR B 2 289 ? 177.179 162.474 125.634 1.00 89.17  ? 280 THR A N   1 
ATOM   5577 C CA  . THR B 2 289 ? 178.376 162.469 126.466 1.00 91.39  ? 280 THR A CA  1 
ATOM   5578 C C   . THR B 2 289 ? 178.152 161.926 127.874 1.00 85.63  ? 280 THR A C   1 
ATOM   5579 O O   . THR B 2 289 ? 179.078 161.976 128.689 1.00 77.64  ? 280 THR A O   1 
ATOM   5580 C CB  . THR B 2 289 ? 178.955 163.885 126.559 1.00 90.38  ? 280 THR A CB  1 
ATOM   5581 O OG1 . THR B 2 289 ? 177.978 164.770 127.116 1.00 83.01  ? 280 THR A OG1 1 
ATOM   5582 C CG2 . THR B 2 289 ? 179.353 164.388 125.181 1.00 87.34  ? 280 THR A CG2 1 
ATOM   5583 N N   . LEU B 2 290 ? 176.963 161.412 128.189 1.00 83.22  ? 281 LEU A N   1 
ATOM   5584 C CA  . LEU B 2 290 ? 176.668 160.980 129.550 1.00 75.68  ? 281 LEU A CA  1 
ATOM   5585 C C   . LEU B 2 290 ? 176.812 159.482 129.777 1.00 68.41  ? 281 LEU A C   1 
ATOM   5586 O O   . LEU B 2 290 ? 176.745 159.045 130.932 1.00 62.39  ? 281 LEU A O   1 
ATOM   5587 C CB  . LEU B 2 290 ? 175.252 161.394 129.947 1.00 70.82  ? 281 LEU A CB  1 
ATOM   5588 C CG  . LEU B 2 290 ? 175.112 162.838 130.402 1.00 65.58  ? 281 LEU A CG  1 
ATOM   5589 C CD1 . LEU B 2 290 ? 173.654 163.191 130.541 1.00 65.22  ? 281 LEU A CD1 1 
ATOM   5590 C CD2 . LEU B 2 290 ? 175.852 163.029 131.710 1.00 62.95  ? 281 LEU A CD2 1 
ATOM   5591 N N   . TYR B 2 291 ? 176.987 158.687 128.720 1.00 76.04  ? 282 TYR A N   1 
ATOM   5592 C CA  . TYR B 2 291 ? 177.078 157.241 128.900 1.00 73.34  ? 282 TYR A CA  1 
ATOM   5593 C C   . TYR B 2 291 ? 178.266 156.871 129.777 1.00 66.97  ? 282 TYR A C   1 
ATOM   5594 O O   . TYR B 2 291 ? 178.140 156.057 130.699 1.00 62.35  ? 282 TYR A O   1 
ATOM   5595 C CB  . TYR B 2 291 ? 177.173 156.536 127.545 1.00 78.57  ? 282 TYR A CB  1 
ATOM   5596 C CG  . TYR B 2 291 ? 176.012 156.791 126.605 1.00 87.11  ? 282 TYR A CG  1 
ATOM   5597 C CD1 . TYR B 2 291 ? 175.849 158.019 125.977 1.00 89.64  ? 282 TYR A CD1 1 
ATOM   5598 C CD2 . TYR B 2 291 ? 175.081 155.797 126.346 1.00 85.76  ? 282 TYR A CD2 1 
ATOM   5599 C CE1 . TYR B 2 291 ? 174.793 158.248 125.121 1.00 91.74  ? 282 TYR A CE1 1 
ATOM   5600 C CE2 . TYR B 2 291 ? 174.021 156.017 125.492 1.00 90.80  ? 282 TYR A CE2 1 
ATOM   5601 C CZ  . TYR B 2 291 ? 173.881 157.245 124.883 1.00 93.45  ? 282 TYR A CZ  1 
ATOM   5602 O OH  . TYR B 2 291 ? 172.825 157.468 124.030 1.00 91.98  ? 282 TYR A OH  1 
ATOM   5603 N N   . HIS B 2 292 ? 179.425 157.475 129.513 1.00 70.04  ? 283 HIS A N   1 
ATOM   5604 C CA  . HIS B 2 292 ? 180.622 157.148 130.279 1.00 68.07  ? 283 HIS A CA  1 
ATOM   5605 C C   . HIS B 2 292 ? 180.487 157.590 131.728 1.00 65.10  ? 283 HIS A C   1 
ATOM   5606 O O   . HIS B 2 292 ? 180.871 156.858 132.647 1.00 63.42  ? 283 HIS A O   1 
ATOM   5607 C CB  . HIS B 2 292 ? 181.844 157.794 129.633 1.00 70.39  ? 283 HIS A CB  1 
ATOM   5608 C CG  . HIS B 2 292 ? 182.387 157.022 128.473 1.00 80.89  ? 283 HIS A CG  1 
ATOM   5609 N ND1 . HIS B 2 292 ? 182.700 155.682 128.551 1.00 78.61  ? 283 HIS A ND1 1 
ATOM   5610 C CD2 . HIS B 2 292 ? 182.664 157.400 127.203 1.00 84.94  ? 283 HIS A CD2 1 
ATOM   5611 C CE1 . HIS B 2 292 ? 183.150 155.270 127.380 1.00 84.27  ? 283 HIS A CE1 1 
ATOM   5612 N NE2 . HIS B 2 292 ? 183.138 156.293 126.545 1.00 90.63  ? 283 HIS A NE2 1 
ATOM   5613 N N   . PHE B 2 293 ? 179.936 158.785 131.952 1.00 65.41  ? 284 PHE A N   1 
ATOM   5614 C CA  . PHE B 2 293 ? 179.775 159.280 133.314 1.00 54.97  ? 284 PHE A CA  1 
ATOM   5615 C C   . PHE B 2 293 ? 178.818 158.406 134.113 1.00 54.37  ? 284 PHE A C   1 
ATOM   5616 O O   . PHE B 2 293 ? 179.096 158.068 135.267 1.00 54.29  ? 284 PHE A O   1 
ATOM   5617 C CB  . PHE B 2 293 ? 179.281 160.724 133.296 1.00 53.20  ? 284 PHE A CB  1 
ATOM   5618 C CG  . PHE B 2 293 ? 178.700 161.176 134.602 1.00 52.11  ? 284 PHE A CG  1 
ATOM   5619 C CD1 . PHE B 2 293 ? 179.520 161.427 135.688 1.00 49.85  ? 284 PHE A CD1 1 
ATOM   5620 C CD2 . PHE B 2 293 ? 177.336 161.336 134.750 1.00 52.83  ? 284 PHE A CD2 1 
ATOM   5621 C CE1 . PHE B 2 293 ? 178.991 161.837 136.888 1.00 46.74  ? 284 PHE A CE1 1 
ATOM   5622 C CE2 . PHE B 2 293 ? 176.804 161.743 135.950 1.00 51.33  ? 284 PHE A CE2 1 
ATOM   5623 C CZ  . PHE B 2 293 ? 177.631 161.993 137.019 1.00 48.20  ? 284 PHE A CZ  1 
ATOM   5624 N N   . PHE B 2 294 ? 177.674 157.985 133.596 1.00 59.07  ? 285 PHE A N   1 
ATOM   5625 C CA  . PHE B 2 294 ? 176.732 157.216 134.464 1.00 52.25  ? 285 PHE A CA  1 
ATOM   5626 C C   . PHE B 2 294 ? 177.302 155.850 134.802 1.00 55.92  ? 285 PHE A C   1 
ATOM   5627 O O   . PHE B 2 294 ? 176.881 155.263 135.810 1.00 57.99  ? 285 PHE A O   1 
ATOM   5628 C CB  . PHE B 2 294 ? 175.337 157.137 133.849 1.00 51.05  ? 285 PHE A CB  1 
ATOM   5629 C CG  . PHE B 2 294 ? 174.485 158.339 134.217 1.00 50.74  ? 285 PHE A CG  1 
ATOM   5630 C CD1 . PHE B 2 294 ? 174.264 158.667 135.547 1.00 44.48  ? 285 PHE A CD1 1 
ATOM   5631 C CD2 . PHE B 2 294 ? 173.934 159.150 133.236 1.00 54.30  ? 285 PHE A CD2 1 
ATOM   5632 C CE1 . PHE B 2 294 ? 173.502 159.769 135.882 1.00 38.18  ? 285 PHE A CE1 1 
ATOM   5633 C CE2 . PHE B 2 294 ? 173.175 160.252 133.579 1.00 48.93  ? 285 PHE A CE2 1 
ATOM   5634 C CZ  . PHE B 2 294 ? 172.957 160.556 134.899 1.00 38.95  ? 285 PHE A CZ  1 
ATOM   5635 N N   . ASN B 2 295 ? 178.246 155.359 134.000 1.00 60.99  ? 286 ASN A N   1 
ATOM   5636 C CA  . ASN B 2 295 ? 178.847 154.018 134.215 1.00 61.93  ? 286 ASN A CA  1 
ATOM   5637 C C   . ASN B 2 295 ? 179.741 154.041 135.452 1.00 60.59  ? 286 ASN A C   1 
ATOM   5638 O O   . ASN B 2 295 ? 179.777 153.014 136.134 1.00 58.64  ? 286 ASN A O   1 
ATOM   5639 C CB  . ASN B 2 295 ? 179.546 153.543 132.958 1.00 62.37  ? 286 ASN A CB  1 
ATOM   5640 C CG  . ASN B 2 295 ? 178.611 152.749 132.081 1.00 70.26  ? 286 ASN A CG  1 
ATOM   5641 O OD1 . ASN B 2 295 ? 178.486 151.531 132.250 1.00 71.78  ? 286 ASN A OD1 1 
ATOM   5642 N ND2 . ASN B 2 295 ? 177.936 153.414 131.156 1.00 67.83  ? 286 ASN A ND2 1 
ATOM   5643 N N   . GLU B 2 296 ? 180.397 155.179 135.698 1.00 64.49  ? 287 GLU A N   1 
ATOM   5644 C CA  . GLU B 2 296 ? 181.227 155.332 136.915 1.00 61.52  ? 287 GLU A CA  1 
ATOM   5645 C C   . GLU B 2 296 ? 180.284 155.495 138.117 1.00 58.83  ? 287 GLU A C   1 
ATOM   5646 O O   . GLU B 2 296 ? 180.478 154.775 139.108 1.00 59.75  ? 287 GLU A O   1 
ATOM   5647 C CB  . GLU B 2 296 ? 182.166 156.530 136.775 1.00 63.51  ? 287 GLU A CB  1 
ATOM   5648 C CG  . GLU B 2 296 ? 183.070 156.735 137.987 1.00 63.17  ? 287 GLU A CG  1 
ATOM   5649 C CD  . GLU B 2 296 ? 184.053 155.606 138.232 1.00 66.08  ? 287 GLU A CD  1 
ATOM   5650 O OE1 . GLU B 2 296 ? 183.873 154.869 139.224 1.00 62.81  ? 287 GLU A OE1 1 
ATOM   5651 O OE2 . GLU B 2 296 ? 185.000 155.463 137.431 1.00 72.39  ? 287 GLU A OE2 1 
ATOM   5652 N N   . VAL B 2 297 ? 179.273 156.366 138.009 1.00 59.77  ? 288 VAL A N   1 
ATOM   5653 C CA  . VAL B 2 297 ? 178.301 156.495 139.133 1.00 57.53  ? 288 VAL A CA  1 
ATOM   5654 C C   . VAL B 2 297 ? 177.885 155.070 139.509 1.00 60.17  ? 288 VAL A C   1 
ATOM   5655 O O   . VAL B 2 297 ? 177.844 154.780 140.708 1.00 57.13  ? 288 VAL A O   1 
ATOM   5656 C CB  . VAL B 2 297 ? 177.109 157.408 138.791 1.00 49.92  ? 288 VAL A CB  1 
ATOM   5657 C CG1 . VAL B 2 297 ? 176.156 157.545 139.963 1.00 45.83  ? 288 VAL A CG1 1 
ATOM   5658 C CG2 . VAL B 2 297 ? 177.568 158.770 138.300 1.00 49.14  ? 288 VAL A CG2 1 
ATOM   5659 N N   . LEU B 2 298 ? 177.647 154.211 138.519 1.00 63.02  ? 289 LEU A N   1 
ATOM   5660 C CA  . LEU B 2 298 ? 177.243 152.800 138.758 1.00 60.02  ? 289 LEU A CA  1 
ATOM   5661 C C   . LEU B 2 298 ? 178.487 151.981 139.123 1.00 67.81  ? 289 LEU A C   1 
ATOM   5662 O O   . LEU B 2 298 ? 178.438 151.309 140.160 1.00 72.49  ? 289 LEU A O   1 
ATOM   5663 C CB  . LEU B 2 298 ? 176.544 152.188 137.547 1.00 59.01  ? 289 LEU A CB  1 
ATOM   5664 C CG  . LEU B 2 298 ? 175.053 152.466 137.368 1.00 61.48  ? 289 LEU A CG  1 
ATOM   5665 C CD1 . LEU B 2 298 ? 174.759 152.319 135.887 1.00 62.64  ? 289 LEU A CD1 1 
ATOM   5666 C CD2 . LEU B 2 298 ? 174.281 151.442 138.171 1.00 65.50  ? 289 LEU A CD2 1 
ATOM   5667 N N   . ARG B 2 299 ? 179.548 152.001 138.311 1.00 68.07  ? 290 ARG A N   1 
ATOM   5668 C CA  . ARG B 2 299 ? 180.695 151.201 138.717 1.00 71.41  ? 290 ARG A CA  1 
ATOM   5669 C C   . ARG B 2 299 ? 181.129 151.547 140.134 1.00 69.77  ? 290 ARG A C   1 
ATOM   5670 O O   . ARG B 2 299 ? 181.385 150.655 140.948 1.00 74.89  ? 290 ARG A O   1 
ATOM   5671 C CB  . ARG B 2 299 ? 181.836 151.421 137.725 1.00 75.66  ? 290 ARG A CB  1 
ATOM   5672 C CG  . ARG B 2 299 ? 183.220 151.097 138.243 1.00 74.31  ? 290 ARG A CG  1 
ATOM   5673 C CD  . ARG B 2 299 ? 184.244 151.972 137.551 1.00 81.27  ? 290 ARG A CD  1 
ATOM   5674 N NE  . ARG B 2 299 ? 183.968 152.108 136.125 1.00 87.50  ? 290 ARG A NE  1 
ATOM   5675 C CZ  . ARG B 2 299 ? 184.389 151.270 135.188 1.00 98.62  ? 290 ARG A CZ  1 
ATOM   5676 N NH1 . ARG B 2 299 ? 185.123 150.210 135.486 1.00 94.00  ? 290 ARG A NH1 1 
ATOM   5677 N NH2 . ARG B 2 299 ? 184.069 151.503 133.918 1.00 94.88  ? 290 ARG A NH2 1 
ATOM   5678 N N   . GLN B 2 300 ? 181.192 152.841 140.451 1.00 67.14  ? 291 GLN A N   1 
ATOM   5679 C CA  . GLN B 2 300 ? 181.519 153.307 141.794 1.00 69.71  ? 291 GLN A CA  1 
ATOM   5680 C C   . GLN B 2 300 ? 180.419 152.986 142.798 1.00 75.13  ? 291 GLN A C   1 
ATOM   5681 O O   . GLN B 2 300 ? 180.663 153.045 144.008 1.00 73.55  ? 291 GLN A O   1 
ATOM   5682 C CB  . GLN B 2 300 ? 181.781 154.816 141.751 1.00 62.01  ? 291 GLN A CB  1 
ATOM   5683 C CG  . GLN B 2 300 ? 182.133 155.463 143.078 1.00 60.75  ? 291 GLN A CG  1 
ATOM   5684 C CD  . GLN B 2 300 ? 183.372 156.324 142.988 1.00 64.24  ? 291 GLN A CD  1 
ATOM   5685 O OE1 . GLN B 2 300 ? 183.917 156.531 141.905 1.00 58.01  ? 291 GLN A OE1 1 
ATOM   5686 N NE2 . GLN B 2 300 ? 183.829 156.826 144.128 1.00 62.62  ? 291 GLN A NE2 1 
ATOM   5687 N N   . ASN B 2 301 ? 179.226 152.637 142.316 1.00 77.58  ? 292 ASN A N   1 
ATOM   5688 C CA  . ASN B 2 301 ? 178.092 152.262 143.159 1.00 76.53  ? 292 ASN A CA  1 
ATOM   5689 C C   . ASN B 2 301 ? 177.707 153.402 144.099 1.00 75.07  ? 292 ASN A C   1 
ATOM   5690 O O   . ASN B 2 301 ? 177.624 153.240 145.318 1.00 75.37  ? 292 ASN A O   1 
ATOM   5691 C CB  . ASN B 2 301 ? 178.379 150.968 143.925 1.00 84.91  ? 292 ASN A CB  1 
ATOM   5692 C CG  . ASN B 2 301 ? 177.870 149.742 143.189 1.00 90.97  ? 292 ASN A CG  1 
ATOM   5693 O OD1 . ASN B 2 301 ? 176.817 149.792 142.551 1.00 84.12  ? 292 ASN A OD1 1 
ATOM   5694 N ND2 . ASN B 2 301 ? 178.614 148.637 143.257 1.00 97.05  ? 292 ASN A ND2 1 
ATOM   5695 N N   . PHE B 2 302 ? 177.469 154.571 143.508 1.00 71.65  ? 293 PHE A N   1 
ATOM   5696 C CA  . PHE B 2 302 ? 176.960 155.729 144.228 1.00 62.93  ? 293 PHE A CA  1 
ATOM   5697 C C   . PHE B 2 302 ? 175.445 155.747 144.080 1.00 61.53  ? 293 PHE A C   1 
ATOM   5698 O O   . PHE B 2 302 ? 174.928 155.838 142.962 1.00 65.83  ? 293 PHE A O   1 
ATOM   5699 C CB  . PHE B 2 302 ? 177.579 157.016 143.687 1.00 57.19  ? 293 PHE A CB  1 
ATOM   5700 C CG  . PHE B 2 302 ? 176.774 158.250 143.977 1.00 52.40  ? 293 PHE A CG  1 
ATOM   5701 C CD1 . PHE B 2 302 ? 176.774 158.809 145.242 1.00 51.81  ? 293 PHE A CD1 1 
ATOM   5702 C CD2 . PHE B 2 302 ? 176.030 158.861 142.983 1.00 49.85  ? 293 PHE A CD2 1 
ATOM   5703 C CE1 . PHE B 2 302 ? 176.043 159.944 145.513 1.00 46.62  ? 293 PHE A CE1 1 
ATOM   5704 C CE2 . PHE B 2 302 ? 175.296 159.999 143.251 1.00 49.58  ? 293 PHE A CE2 1 
ATOM   5705 C CZ  . PHE B 2 302 ? 175.304 160.541 144.517 1.00 45.20  ? 293 PHE A CZ  1 
ATOM   5706 N N   . THR B 2 303 ? 174.738 155.663 145.201 1.00 63.86  ? 294 THR A N   1 
ATOM   5707 C CA  . THR B 2 303 ? 173.297 155.478 145.199 1.00 65.98  ? 294 THR A CA  1 
ATOM   5708 C C   . THR B 2 303 ? 172.623 156.540 146.053 1.00 65.65  ? 294 THR A C   1 
ATOM   5709 O O   . THR B 2 303 ? 173.249 157.158 146.919 1.00 67.10  ? 294 THR A O   1 
ATOM   5710 C CB  . THR B 2 303 ? 172.916 154.082 145.713 1.00 68.52  ? 294 THR A CB  1 
ATOM   5711 O OG1 . THR B 2 303 ? 171.633 153.711 145.196 1.00 72.03  ? 294 THR A OG1 1 
ATOM   5712 C CG2 . THR B 2 303 ? 172.881 154.055 147.235 1.00 60.89  ? 294 THR A CG2 1 
ATOM   5713 N N   . GLY B 2 304 ? 171.346 156.764 145.775 1.00 55.48  ? 295 GLY A N   1 
ATOM   5714 C CA  . GLY B 2 304 ? 170.502 157.568 146.624 1.00 54.44  ? 295 GLY A CA  1 
ATOM   5715 C C   . GLY B 2 304 ? 170.357 159.021 146.243 1.00 50.93  ? 295 GLY A C   1 
ATOM   5716 O O   . GLY B 2 304 ? 170.176 159.857 147.134 1.00 53.10  ? 295 GLY A O   1 
ATOM   5717 N N   . ALA B 2 305 ? 170.416 159.353 144.957 1.00 40.67  ? 296 ALA A N   1 
ATOM   5718 C CA  . ALA B 2 305 ? 170.318 160.732 144.512 1.00 30.58  ? 296 ALA A CA  1 
ATOM   5719 C C   . ALA B 2 305 ? 169.136 160.888 143.571 1.00 34.44  ? 296 ALA A C   1 
ATOM   5720 O O   . ALA B 2 305 ? 168.707 159.933 142.922 1.00 44.19  ? 296 ALA A O   1 
ATOM   5721 C CB  . ALA B 2 305 ? 171.599 161.193 143.810 1.00 32.53  ? 296 ALA A CB  1 
ATOM   5722 N N   . VAL B 2 306 ? 168.609 162.105 143.513 1.00 34.05  ? 297 VAL A N   1 
ATOM   5723 C CA  . VAL B 2 306 ? 167.572 162.475 142.561 1.00 25.20  ? 297 VAL A CA  1 
ATOM   5724 C C   . VAL B 2 306 ? 168.276 163.192 141.418 1.00 23.65  ? 297 VAL A C   1 
ATOM   5725 O O   . VAL B 2 306 ? 168.910 164.229 141.613 1.00 23.70  ? 297 VAL A O   1 
ATOM   5726 C CB  . VAL B 2 306 ? 166.489 163.347 143.198 1.00 25.36  ? 297 VAL A CB  1 
ATOM   5727 C CG1 . VAL B 2 306 ? 165.460 163.742 142.159 1.00 22.83  ? 297 VAL A CG1 1 
ATOM   5728 C CG2 . VAL B 2 306 ? 165.831 162.616 144.348 1.00 30.12  ? 297 VAL A CG2 1 
ATOM   5729 N N   . TRP B 2 307 ? 168.172 162.632 140.222 1.00 27.31  ? 298 TRP A N   1 
ATOM   5730 C CA  . TRP B 2 307 ? 168.814 163.210 139.054 1.00 25.79  ? 298 TRP A CA  1 
ATOM   5731 C C   . TRP B 2 307 ? 167.800 164.029 138.271 1.00 25.62  ? 298 TRP A C   1 
ATOM   5732 O O   . TRP B 2 307 ? 166.699 163.555 137.982 1.00 30.48  ? 298 TRP A O   1 
ATOM   5733 C CB  . TRP B 2 307 ? 169.404 162.109 138.179 1.00 24.55  ? 298 TRP A CB  1 
ATOM   5734 C CG  . TRP B 2 307 ? 170.353 161.217 138.912 1.00 22.30  ? 298 TRP A CG  1 
ATOM   5735 C CD1 . TRP B 2 307 ? 170.039 160.103 139.628 1.00 25.04  ? 298 TRP A CD1 1 
ATOM   5736 C CD2 . TRP B 2 307 ? 171.773 161.358 138.992 1.00 26.47  ? 298 TRP A CD2 1 
ATOM   5737 N NE1 . TRP B 2 307 ? 171.173 159.545 140.155 1.00 26.46  ? 298 TRP A NE1 1 
ATOM   5738 C CE2 . TRP B 2 307 ? 172.253 160.297 139.778 1.00 26.24  ? 298 TRP A CE2 1 
ATOM   5739 C CE3 . TRP B 2 307 ? 172.685 162.282 138.477 1.00 30.00  ? 298 TRP A CE3 1 
ATOM   5740 C CZ2 . TRP B 2 307 ? 173.603 160.134 140.061 1.00 28.90  ? 298 TRP A CZ2 1 
ATOM   5741 C CZ3 . TRP B 2 307 ? 174.022 162.117 138.760 1.00 29.94  ? 298 TRP A CZ3 1 
ATOM   5742 C CH2 . TRP B 2 307 ? 174.469 161.053 139.544 1.00 31.29  ? 298 TRP A CH2 1 
ATOM   5743 N N   . ILE B 2 308 ? 168.167 165.259 137.940 1.00 24.19  ? 299 ILE A N   1 
ATOM   5744 C CA  . ILE B 2 308 ? 167.327 166.159 137.162 1.00 26.61  ? 299 ILE A CA  1 
ATOM   5745 C C   . ILE B 2 308 ? 167.996 166.342 135.810 1.00 32.55  ? 299 ILE A C   1 
ATOM   5746 O O   . ILE B 2 308 ? 169.173 166.712 135.734 1.00 39.12  ? 299 ILE A O   1 
ATOM   5747 C CB  . ILE B 2 308 ? 167.117 167.502 137.875 1.00 26.42  ? 299 ILE A CB  1 
ATOM   5748 C CG1 . ILE B 2 308 ? 166.248 167.307 139.119 1.00 27.21  ? 299 ILE A CG1 1 
ATOM   5749 C CG2 . ILE B 2 308 ? 166.486 168.510 136.934 1.00 22.78  ? 299 ILE A CG2 1 
ATOM   5750 C CD1 . ILE B 2 308 ? 166.021 168.567 139.910 1.00 27.38  ? 299 ILE A CD1 1 
ATOM   5751 N N   . ALA B 2 309 ? 167.248 166.076 134.749 1.00 32.16  ? 300 ALA A N   1 
ATOM   5752 C CA  . ALA B 2 309 ? 167.773 166.027 133.398 1.00 32.04  ? 300 ALA A CA  1 
ATOM   5753 C C   . ALA B 2 309 ? 167.290 167.221 132.591 1.00 37.28  ? 300 ALA A C   1 
ATOM   5754 O O   . ALA B 2 309 ? 166.112 167.580 132.623 1.00 40.05  ? 300 ALA A O   1 
ATOM   5755 C CB  . ALA B 2 309 ? 167.348 164.734 132.702 1.00 37.71  ? 300 ALA A CB  1 
ATOM   5756 N N   . SER B 2 310 ? 168.217 167.833 131.864 1.00 41.49  ? 301 SER A N   1 
ATOM   5757 C CA  . SER B 2 310 ? 167.859 168.867 130.913 1.00 45.74  ? 301 SER A CA  1 
ATOM   5758 C C   . SER B 2 310 ? 167.154 168.233 129.718 1.00 49.08  ? 301 SER A C   1 
ATOM   5759 O O   . SER B 2 310 ? 167.087 167.009 129.580 1.00 54.83  ? 301 SER A O   1 
ATOM   5760 C CB  . SER B 2 310 ? 169.100 169.646 130.487 1.00 50.79  ? 301 SER A CB  1 
ATOM   5761 O OG  . SER B 2 310 ? 170.215 168.785 130.337 1.00 55.83  ? 301 SER A OG  1 
ATOM   5762 N N   . GLU B 2 311 ? 166.618 169.073 128.834 1.00 50.69  ? 302 GLU A N   1 
ATOM   5763 C CA  . GLU B 2 311 ? 165.872 168.555 127.694 1.00 54.32  ? 302 GLU A CA  1 
ATOM   5764 C C   . GLU B 2 311 ? 166.753 167.773 126.726 1.00 58.54  ? 302 GLU A C   1 
ATOM   5765 O O   . GLU B 2 311 ? 166.226 167.069 125.859 1.00 63.70  ? 302 GLU A O   1 
ATOM   5766 C CB  . GLU B 2 311 ? 165.144 169.705 126.985 1.00 48.45  ? 302 GLU A CB  1 
ATOM   5767 C CG  . GLU B 2 311 ? 165.994 170.919 126.616 1.00 55.07  ? 302 GLU A CG  1 
ATOM   5768 C CD  . GLU B 2 311 ? 167.091 170.611 125.621 1.00 63.94  ? 302 GLU A CD  1 
ATOM   5769 O OE1 . GLU B 2 311 ? 166.764 170.190 124.492 1.00 63.00  ? 302 GLU A OE1 1 
ATOM   5770 O OE2 . GLU B 2 311 ? 168.278 170.787 125.964 1.00 69.23  ? 302 GLU A OE2 1 
ATOM   5771 N N   . SER B 2 312 ? 168.078 167.878 126.856 1.00 56.86  ? 303 SER A N   1 
ATOM   5772 C CA  . SER B 2 312 ? 168.970 167.139 125.969 1.00 59.98  ? 303 SER A CA  1 
ATOM   5773 C C   . SER B 2 312 ? 168.827 165.634 126.151 1.00 64.03  ? 303 SER A C   1 
ATOM   5774 O O   . SER B 2 312 ? 168.811 164.885 125.168 1.00 71.21  ? 303 SER A O   1 
ATOM   5775 C CB  . SER B 2 312 ? 170.417 167.567 126.201 1.00 58.61  ? 303 SER A CB  1 
ATOM   5776 O OG  . SER B 2 312 ? 170.591 168.933 125.888 1.00 60.19  ? 303 SER A OG  1 
ATOM   5777 N N   . TRP B 2 313 ? 168.730 165.166 127.396 1.00 58.58  ? 304 TRP A N   1 
ATOM   5778 C CA  . TRP B 2 313 ? 168.698 163.733 127.659 1.00 63.79  ? 304 TRP A CA  1 
ATOM   5779 C C   . TRP B 2 313 ? 167.523 163.299 128.526 1.00 63.05  ? 304 TRP A C   1 
ATOM   5780 O O   . TRP B 2 313 ? 167.521 162.166 129.019 1.00 66.36  ? 304 TRP A O   1 
ATOM   5781 C CB  . TRP B 2 313 ? 170.012 163.281 128.302 1.00 60.40  ? 304 TRP A CB  1 
ATOM   5782 C CG  . TRP B 2 313 ? 170.303 163.872 129.646 1.00 49.25  ? 304 TRP A CG  1 
ATOM   5783 C CD1 . TRP B 2 313 ? 170.731 165.137 129.911 1.00 52.12  ? 304 TRP A CD1 1 
ATOM   5784 C CD2 . TRP B 2 313 ? 170.208 163.207 130.912 1.00 48.38  ? 304 TRP A CD2 1 
ATOM   5785 N NE1 . TRP B 2 313 ? 170.901 165.306 131.262 1.00 49.99  ? 304 TRP A NE1 1 
ATOM   5786 C CE2 . TRP B 2 313 ? 170.586 164.135 131.899 1.00 49.26  ? 304 TRP A CE2 1 
ATOM   5787 C CE3 . TRP B 2 313 ? 169.836 161.918 131.305 1.00 51.27  ? 304 TRP A CE3 1 
ATOM   5788 C CZ2 . TRP B 2 313 ? 170.603 163.815 133.254 1.00 42.76  ? 304 TRP A CZ2 1 
ATOM   5789 C CZ3 . TRP B 2 313 ? 169.851 161.604 132.649 1.00 44.95  ? 304 TRP A CZ3 1 
ATOM   5790 C CH2 . TRP B 2 313 ? 170.231 162.549 133.608 1.00 39.51  ? 304 TRP A CH2 1 
ATOM   5791 N N   . ALA B 2 314 ? 166.524 164.160 128.727 1.00 59.18  ? 305 ALA A N   1 
ATOM   5792 C CA  . ALA B 2 314 ? 165.367 163.768 129.520 1.00 55.79  ? 305 ALA A CA  1 
ATOM   5793 C C   . ALA B 2 314 ? 164.491 162.749 128.807 1.00 68.69  ? 305 ALA A C   1 
ATOM   5794 O O   . ALA B 2 314 ? 164.129 161.734 129.409 1.00 66.31  ? 305 ALA A O   1 
ATOM   5795 C CB  . ALA B 2 314 ? 164.542 164.999 129.881 1.00 48.09  ? 305 ALA A CB  1 
ATOM   5796 N N   . ILE B 2 315 ? 164.160 162.982 127.537 1.00 77.14  ? 306 ILE A N   1 
ATOM   5797 C CA  . ILE B 2 315 ? 163.344 162.055 126.762 1.00 73.19  ? 306 ILE A CA  1 
ATOM   5798 C C   . ILE B 2 315 ? 164.241 161.300 125.797 1.00 79.91  ? 306 ILE A C   1 
ATOM   5799 O O   . ILE B 2 315 ? 163.789 160.845 124.741 1.00 82.38  ? 306 ILE A O   1 
ATOM   5800 C CB  . ILE B 2 315 ? 162.225 162.775 125.990 1.00 71.16  ? 306 ILE A CB  1 
ATOM   5801 C CG1 . ILE B 2 315 ? 162.831 163.854 125.090 1.00 68.02  ? 306 ILE A CG1 1 
ATOM   5802 C CG2 . ILE B 2 315 ? 161.174 163.310 126.944 1.00 71.94  ? 306 ILE A CG2 1 
ATOM   5803 C CD1 . ILE B 2 315 ? 161.825 164.737 124.398 1.00 70.71  ? 306 ILE A CD1 1 
ATOM   5804 N N   . ASP B 2 316 ? 165.512 161.169 126.138 1.00 81.00  ? 307 ASP A N   1 
ATOM   5805 C CA  . ASP B 2 316 ? 166.426 160.476 125.249 1.00 86.89  ? 307 ASP A CA  1 
ATOM   5806 C C   . ASP B 2 316 ? 166.119 158.987 125.295 1.00 93.28  ? 307 ASP A C   1 
ATOM   5807 O O   . ASP B 2 316 ? 166.285 158.362 126.351 1.00 88.04  ? 307 ASP A O   1 
ATOM   5808 C CB  . ASP B 2 316 ? 167.870 160.747 125.643 1.00 87.21  ? 307 ASP A CB  1 
ATOM   5809 C CG  . ASP B 2 316 ? 168.782 160.851 124.445 1.00 86.17  ? 307 ASP A CG  1 
ATOM   5810 O OD1 . ASP B 2 316 ? 168.625 161.811 123.664 1.00 84.99  ? 307 ASP A OD1 1 
ATOM   5811 O OD2 . ASP B 2 316 ? 169.638 159.962 124.270 1.00 92.44  ? 307 ASP A OD2 1 
ATOM   5812 N N   . PRO B 2 317 ? 165.682 158.381 124.190 1.00 97.64  ? 308 PRO A N   1 
ATOM   5813 C CA  . PRO B 2 317 ? 165.219 156.989 124.250 1.00 96.18  ? 308 PRO A CA  1 
ATOM   5814 C C   . PRO B 2 317 ? 166.364 155.994 124.325 1.00 93.14  ? 308 PRO A C   1 
ATOM   5815 O O   . PRO B 2 317 ? 166.261 154.974 125.011 1.00 92.73  ? 308 PRO A O   1 
ATOM   5816 C CB  . PRO B 2 317 ? 164.413 156.836 122.954 1.00 96.96  ? 308 PRO A CB  1 
ATOM   5817 C CG  . PRO B 2 317 ? 165.020 157.822 122.012 1.00 97.48  ? 308 PRO A CG  1 
ATOM   5818 C CD  . PRO B 2 317 ? 165.544 158.965 122.844 1.00 92.03  ? 308 PRO A CD  1 
ATOM   5819 N N   . VAL B 2 318 ? 167.466 156.291 123.634 1.00 93.82  ? 309 VAL A N   1 
ATOM   5820 C CA  . VAL B 2 318 ? 168.624 155.403 123.659 1.00 99.76  ? 309 VAL A CA  1 
ATOM   5821 C C   . VAL B 2 318 ? 169.306 155.449 125.023 1.00 95.07  ? 309 VAL A C   1 
ATOM   5822 O O   . VAL B 2 318 ? 169.916 154.469 125.465 1.00 89.39  ? 309 VAL A O   1 
ATOM   5823 C CB  . VAL B 2 318 ? 169.591 155.766 122.515 1.00 99.95  ? 309 VAL A CB  1 
ATOM   5824 C CG1 . VAL B 2 318 ? 169.892 157.251 122.511 1.00 91.55  ? 309 VAL A CG1 1 
ATOM   5825 C CG2 . VAL B 2 318 ? 170.866 154.940 122.586 1.00 94.70  ? 309 VAL A CG2 1 
ATOM   5826 N N   . LEU B 2 319 ? 169.233 156.592 125.706 1.00 94.64  ? 310 LEU A N   1 
ATOM   5827 C CA  . LEU B 2 319 ? 169.854 156.690 127.023 1.00 96.15  ? 310 LEU A CA  1 
ATOM   5828 C C   . LEU B 2 319 ? 169.008 155.990 128.082 1.00 96.09  ? 310 LEU A C   1 
ATOM   5829 O O   . LEU B 2 319 ? 169.549 155.385 129.015 1.00 86.94  ? 310 LEU A O   1 
ATOM   5830 C CB  . LEU B 2 319 ? 170.087 158.160 127.377 1.00 89.78  ? 310 LEU A CB  1 
ATOM   5831 C CG  . LEU B 2 319 ? 171.329 158.540 128.193 1.00 86.57  ? 310 LEU A CG  1 
ATOM   5832 C CD1 . LEU B 2 319 ? 171.399 160.043 128.359 1.00 81.22  ? 310 LEU A CD1 1 
ATOM   5833 C CD2 . LEU B 2 319 ? 171.363 157.871 129.558 1.00 69.14  ? 310 LEU A CD2 1 
ATOM   5834 N N   . HIS B 2 320 ? 167.679 156.049 127.949 1.00 94.05  ? 311 HIS A N   1 
ATOM   5835 C CA  . HIS B 2 320 ? 166.813 155.271 128.832 1.00 89.80  ? 311 HIS A CA  1 
ATOM   5836 C C   . HIS B 2 320 ? 166.886 153.785 128.502 1.00 99.87  ? 311 HIS A C   1 
ATOM   5837 O O   . HIS B 2 320 ? 166.638 152.943 129.373 1.00 96.25  ? 311 HIS A O   1 
ATOM   5838 C CB  . HIS B 2 320 ? 165.376 155.784 128.737 1.00 84.27  ? 311 HIS A CB  1 
ATOM   5839 C CG  . HIS B 2 320 ? 164.385 154.973 129.515 1.00 90.07  ? 311 HIS A CG  1 
ATOM   5840 N ND1 . HIS B 2 320 ? 163.214 154.501 128.963 1.00 95.29  ? 311 HIS A ND1 1 
ATOM   5841 C CD2 . HIS B 2 320 ? 164.386 154.559 130.804 1.00 82.50  ? 311 HIS A CD2 1 
ATOM   5842 C CE1 . HIS B 2 320 ? 162.539 153.828 129.877 1.00 88.62  ? 311 HIS A CE1 1 
ATOM   5843 N NE2 . HIS B 2 320 ? 163.228 153.848 131.003 1.00 80.21  ? 311 HIS A NE2 1 
ATOM   5844 N N   . ASN B 2 321 ? 167.227 153.454 127.253 1.00 101.30 ? 312 ASN A N   1 
ATOM   5845 C CA  . ASN B 2 321 ? 167.541 152.100 126.810 1.00 100.31 ? 312 ASN A CA  1 
ATOM   5846 C C   . ASN B 2 321 ? 168.587 151.418 127.683 1.00 101.70 ? 312 ASN A C   1 
ATOM   5847 O O   . ASN B 2 321 ? 168.682 150.185 127.656 1.00 103.42 ? 312 ASN A O   1 
ATOM   5848 C CB  . ASN B 2 321 ? 168.040 152.155 125.362 1.00 107.93 ? 312 ASN A CB  1 
ATOM   5849 C CG  . ASN B 2 321 ? 168.215 150.789 124.735 1.00 116.88 ? 312 ASN A CG  1 
ATOM   5850 O OD1 . ASN B 2 321 ? 169.113 150.598 123.912 1.00 112.15 ? 312 ASN A OD1 1 
ATOM   5851 N ND2 . ASN B 2 321 ? 167.340 149.848 125.093 1.00 121.36 ? 312 ASN A ND2 1 
ATOM   5852 N N   . LEU B 2 322 ? 169.372 152.186 128.444 1.00 97.25  ? 313 LEU A N   1 
ATOM   5853 C CA  . LEU B 2 322 ? 170.447 151.617 129.250 1.00 97.71  ? 313 LEU A CA  1 
ATOM   5854 C C   . LEU B 2 322 ? 169.899 150.634 130.278 1.00 97.21  ? 313 LEU A C   1 
ATOM   5855 O O   . LEU B 2 322 ? 170.472 149.564 130.503 1.00 98.64  ? 313 LEU A O   1 
ATOM   5856 C CB  . LEU B 2 322 ? 171.228 152.746 129.923 1.00 98.32  ? 313 LEU A CB  1 
ATOM   5857 C CG  . LEU B 2 322 ? 172.679 152.484 130.332 1.00 93.70  ? 313 LEU A CG  1 
ATOM   5858 C CD1 . LEU B 2 322 ? 173.513 153.738 130.150 1.00 91.17  ? 313 LEU A CD1 1 
ATOM   5859 C CD2 . LEU B 2 322 ? 172.741 152.017 131.766 1.00 82.85  ? 313 LEU A CD2 1 
ATOM   5860 N N   . THR B 2 323 ? 168.792 150.996 130.923 1.00 96.29  ? 314 THR A N   1 
ATOM   5861 C CA  . THR B 2 323 ? 167.982 150.153 131.804 1.00 99.39  ? 314 THR A CA  1 
ATOM   5862 C C   . THR B 2 323 ? 168.755 149.720 133.053 1.00 92.49  ? 314 THR A C   1 
ATOM   5863 O O   . THR B 2 323 ? 168.245 148.895 133.822 1.00 90.64  ? 314 THR A O   1 
ATOM   5864 C CB  . THR B 2 323 ? 167.434 148.911 131.077 1.00 99.40  ? 314 THR A CB  1 
ATOM   5865 O OG1 . THR B 2 323 ? 167.083 149.266 129.735 1.00 97.45  ? 314 THR A OG1 1 
ATOM   5866 C CG2 . THR B 2 323 ? 166.169 148.390 131.757 1.00 96.20  ? 314 THR A CG2 1 
ATOM   5867 N N   . GLU B 2 324 ? 169.957 150.241 133.291 1.00 88.66  ? 315 GLU A N   1 
ATOM   5868 C CA  . GLU B 2 324 ? 170.732 149.886 134.472 1.00 89.10  ? 315 GLU A CA  1 
ATOM   5869 C C   . GLU B 2 324 ? 170.787 151.010 135.503 1.00 81.99  ? 315 GLU A C   1 
ATOM   5870 O O   . GLU B 2 324 ? 171.154 150.765 136.657 1.00 75.53  ? 315 GLU A O   1 
ATOM   5871 C CB  . GLU B 2 324 ? 172.146 149.463 134.062 1.00 88.22  ? 315 GLU A CB  1 
ATOM   5872 C CG  . GLU B 2 324 ? 172.982 148.857 135.179 1.00 83.54  ? 315 GLU A CG  1 
ATOM   5873 C CD  . GLU B 2 324 ? 172.420 147.546 135.695 1.00 87.00  ? 315 GLU A CD  1 
ATOM   5874 O OE1 . GLU B 2 324 ? 171.609 146.916 134.983 1.00 86.51  ? 315 GLU A OE1 1 
ATOM   5875 O OE2 . GLU B 2 324 ? 172.784 147.149 136.821 1.00 84.84  ? 315 GLU A OE2 1 
ATOM   5876 N N   . LEU B 2 325 ? 170.405 152.228 135.126 1.00 74.01  ? 316 LEU A N   1 
ATOM   5877 C CA  . LEU B 2 325 ? 170.405 153.365 136.036 1.00 63.19  ? 316 LEU A CA  1 
ATOM   5878 C C   . LEU B 2 325 ? 169.278 153.308 137.057 1.00 66.41  ? 316 LEU A C   1 
ATOM   5879 O O   . LEU B 2 325 ? 169.136 154.239 137.853 1.00 72.30  ? 316 LEU A O   1 
ATOM   5880 C CB  . LEU B 2 325 ? 170.319 154.673 135.252 1.00 57.69  ? 316 LEU A CB  1 
ATOM   5881 C CG  . LEU B 2 325 ? 171.160 154.777 133.986 1.00 59.14  ? 316 LEU A CG  1 
ATOM   5882 C CD1 . LEU B 2 325 ? 170.672 155.921 133.119 1.00 54.50  ? 316 LEU A CD1 1 
ATOM   5883 C CD2 . LEU B 2 325 ? 172.609 154.970 134.364 1.00 63.06  ? 316 LEU A CD2 1 
ATOM   5884 N N   . ARG B 2 326 ? 168.474 152.244 137.050 1.00 70.26  ? 317 ARG A N   1 
ATOM   5885 C CA  . ARG B 2 326 ? 167.319 152.167 137.937 1.00 74.02  ? 317 ARG A CA  1 
ATOM   5886 C C   . ARG B 2 326 ? 167.706 152.231 139.409 1.00 72.21  ? 317 ARG A C   1 
ATOM   5887 O O   . ARG B 2 326 ? 166.969 152.822 140.206 1.00 68.59  ? 317 ARG A O   1 
ATOM   5888 C CB  . ARG B 2 326 ? 166.533 150.890 137.638 1.00 76.88  ? 317 ARG A CB  1 
ATOM   5889 C CG  . ARG B 2 326 ? 165.651 150.392 138.767 1.00 78.18  ? 317 ARG A CG  1 
ATOM   5890 C CD  . ARG B 2 326 ? 165.428 148.876 138.725 1.00 88.94  ? 317 ARG A CD  1 
ATOM   5891 N NE  . ARG B 2 326 ? 165.116 148.359 137.396 1.00 95.61  ? 317 ARG A NE  1 
ATOM   5892 C CZ  . ARG B 2 326 ? 166.008 147.867 136.545 1.00 93.73  ? 317 ARG A CZ  1 
ATOM   5893 N NH1 . ARG B 2 326 ? 167.293 147.799 136.853 1.00 89.97  ? 317 ARG A NH1 1 
ATOM   5894 N NH2 . ARG B 2 326 ? 165.600 147.430 135.358 1.00 92.74  ? 317 ARG A NH2 1 
ATOM   5895 N N   . HIS B 2 327 ? 168.851 151.670 139.783 1.00 78.43  ? 318 HIS A N   1 
ATOM   5896 C CA  . HIS B 2 327 ? 169.297 151.658 141.169 1.00 74.24  ? 318 HIS A CA  1 
ATOM   5897 C C   . HIS B 2 327 ? 170.019 152.934 141.577 1.00 66.39  ? 318 HIS A C   1 
ATOM   5898 O O   . HIS B 2 327 ? 170.411 153.060 142.740 1.00 68.71  ? 318 HIS A O   1 
ATOM   5899 C CB  . HIS B 2 327 ? 170.209 150.453 141.416 1.00 75.91  ? 318 HIS A CB  1 
ATOM   5900 C CG  . HIS B 2 327 ? 169.637 149.154 140.941 1.00 85.88  ? 318 HIS A CG  1 
ATOM   5901 N ND1 . HIS B 2 327 ? 170.378 148.227 140.241 1.00 94.51  ? 318 HIS A ND1 1 
ATOM   5902 C CD2 . HIS B 2 327 ? 168.401 148.621 141.077 1.00 89.22  ? 318 HIS A CD2 1 
ATOM   5903 C CE1 . HIS B 2 327 ? 169.621 147.182 139.960 1.00 94.08  ? 318 HIS A CE1 1 
ATOM   5904 N NE2 . HIS B 2 327 ? 168.416 147.396 140.457 1.00 92.67  ? 318 HIS A NE2 1 
ATOM   5905 N N   . LEU B 2 328 ? 170.198 153.881 140.660 1.00 57.12  ? 319 LEU A N   1 
ATOM   5906 C CA  . LEU B 2 328 ? 170.886 155.131 140.950 1.00 54.32  ? 319 LEU A CA  1 
ATOM   5907 C C   . LEU B 2 328 ? 169.988 156.167 141.615 1.00 55.90  ? 319 LEU A C   1 
ATOM   5908 O O   . LEU B 2 328 ? 170.474 157.243 141.977 1.00 55.65  ? 319 LEU A O   1 
ATOM   5909 C CB  . LEU B 2 328 ? 171.471 155.716 139.663 1.00 52.52  ? 319 LEU A CB  1 
ATOM   5910 C CG  . LEU B 2 328 ? 172.705 155.033 139.075 1.00 53.99  ? 319 LEU A CG  1 
ATOM   5911 C CD1 . LEU B 2 328 ? 173.467 156.006 138.199 1.00 55.19  ? 319 LEU A CD1 1 
ATOM   5912 C CD2 . LEU B 2 328 ? 173.599 154.500 140.176 1.00 50.56  ? 319 LEU A CD2 1 
ATOM   5913 N N   . GLY B 2 329 ? 168.703 155.876 141.788 1.00 51.25  ? 320 GLY A N   1 
ATOM   5914 C CA  . GLY B 2 329 ? 167.789 156.825 142.388 1.00 42.87  ? 320 GLY A CA  1 
ATOM   5915 C C   . GLY B 2 329 ? 166.570 157.073 141.526 1.00 44.74  ? 320 GLY A C   1 
ATOM   5916 O O   . GLY B 2 329 ? 166.089 156.158 140.853 1.00 56.91  ? 320 GLY A O   1 
ATOM   5917 N N   . THR B 2 330 ? 166.055 158.297 141.538 1.00 33.33  ? 321 THR A N   1 
ATOM   5918 C CA  . THR B 2 330 ? 164.949 158.681 140.676 1.00 30.87  ? 321 THR A CA  1 
ATOM   5919 C C   . THR B 2 330 ? 165.456 159.633 139.607 1.00 28.24  ? 321 THR A C   1 
ATOM   5920 O O   . THR B 2 330 ? 166.292 160.497 139.878 1.00 32.11  ? 321 THR A O   1 
ATOM   5921 C CB  . THR B 2 330 ? 163.814 159.346 141.460 1.00 36.04  ? 321 THR A CB  1 
ATOM   5922 O OG1 . THR B 2 330 ? 164.127 160.723 141.689 1.00 36.98  ? 321 THR A OG1 1 
ATOM   5923 C CG2 . THR B 2 330 ? 163.624 158.658 142.787 1.00 39.42  ? 321 THR A CG2 1 
ATOM   5924 N N   . PHE B 2 331 ? 164.955 159.463 138.391 1.00 27.73  ? 322 PHE A N   1 
ATOM   5925 C CA  . PHE B 2 331 ? 165.342 160.293 137.264 1.00 27.05  ? 322 PHE A CA  1 
ATOM   5926 C C   . PHE B 2 331 ? 164.154 161.139 136.837 1.00 29.03  ? 322 PHE A C   1 
ATOM   5927 O O   . PHE B 2 331 ? 163.094 160.605 136.504 1.00 39.96  ? 322 PHE A O   1 
ATOM   5928 C CB  . PHE B 2 331 ? 165.837 159.433 136.101 1.00 34.62  ? 322 PHE A CB  1 
ATOM   5929 C CG  . PHE B 2 331 ? 167.225 158.900 136.296 1.00 31.00  ? 322 PHE A CG  1 
ATOM   5930 C CD1 . PHE B 2 331 ? 167.445 157.778 137.073 1.00 31.88  ? 322 PHE A CD1 1 
ATOM   5931 C CD2 . PHE B 2 331 ? 168.307 159.520 135.708 1.00 31.94  ? 322 PHE A CD2 1 
ATOM   5932 C CE1 . PHE B 2 331 ? 168.716 157.290 137.260 1.00 32.77  ? 322 PHE A CE1 1 
ATOM   5933 C CE2 . PHE B 2 331 ? 169.582 159.032 135.891 1.00 31.30  ? 322 PHE A CE2 1 
ATOM   5934 C CZ  . PHE B 2 331 ? 169.786 157.918 136.667 1.00 31.84  ? 322 PHE A CZ  1 
ATOM   5935 N N   . LEU B 2 332 ? 164.332 162.452 136.868 1.00 23.11  ? 323 LEU A N   1 
ATOM   5936 C CA  . LEU B 2 332 ? 163.355 163.406 136.377 1.00 25.26  ? 323 LEU A CA  1 
ATOM   5937 C C   . LEU B 2 332 ? 163.990 164.207 135.252 1.00 27.47  ? 323 LEU A C   1 
ATOM   5938 O O   . LEU B 2 332 ? 165.211 164.294 135.141 1.00 37.24  ? 323 LEU A O   1 
ATOM   5939 C CB  . LEU B 2 332 ? 162.867 164.332 137.499 1.00 27.36  ? 323 LEU A CB  1 
ATOM   5940 C CG  . LEU B 2 332 ? 162.504 163.678 138.834 1.00 23.24  ? 323 LEU A CG  1 
ATOM   5941 C CD1 . LEU B 2 332 ? 162.489 164.707 139.945 1.00 22.38  ? 323 LEU A CD1 1 
ATOM   5942 C CD2 . LEU B 2 332 ? 161.172 162.962 138.750 1.00 19.84  ? 323 LEU A CD2 1 
ATOM   5943 N N   . GLY B 2 333 ? 163.155 164.780 134.398 1.00 27.57  ? 324 GLY A N   1 
ATOM   5944 C CA  . GLY B 2 333 ? 163.669 165.541 133.279 1.00 29.30  ? 324 GLY A CA  1 
ATOM   5945 C C   . GLY B 2 333 ? 162.656 166.546 132.790 1.00 34.48  ? 324 GLY A C   1 
ATOM   5946 O O   . GLY B 2 333 ? 161.445 166.326 132.871 1.00 34.58  ? 324 GLY A O   1 
ATOM   5947 N N   . ILE B 2 334 ? 163.173 167.657 132.274 1.00 37.38  ? 325 ILE A N   1 
ATOM   5948 C CA  . ILE B 2 334 ? 162.356 168.744 131.751 1.00 40.88  ? 325 ILE A CA  1 
ATOM   5949 C C   . ILE B 2 334 ? 162.299 168.591 130.240 1.00 45.28  ? 325 ILE A C   1 
ATOM   5950 O O   . ILE B 2 334 ? 163.343 168.520 129.583 1.00 54.68  ? 325 ILE A O   1 
ATOM   5951 C CB  . ILE B 2 334 ? 162.934 170.119 132.128 1.00 42.82  ? 325 ILE A CB  1 
ATOM   5952 C CG1 . ILE B 2 334 ? 163.545 170.090 133.529 1.00 37.57  ? 325 ILE A CG1 1 
ATOM   5953 C CG2 . ILE B 2 334 ? 161.855 171.179 132.053 1.00 44.26  ? 325 ILE A CG2 1 
ATOM   5954 C CD1 . ILE B 2 334 ? 162.571 169.833 134.630 1.00 32.56  ? 325 ILE A CD1 1 
ATOM   5955 N N   . THR B 2 335 ? 161.087 168.567 129.688 1.00 45.51  ? 326 THR A N   1 
ATOM   5956 C CA  . THR B 2 335 ? 160.874 168.436 128.251 1.00 53.64  ? 326 THR A CA  1 
ATOM   5957 C C   . THR B 2 335 ? 159.534 169.059 127.896 1.00 51.00  ? 326 THR A C   1 
ATOM   5958 O O   . THR B 2 335 ? 158.918 169.753 128.704 1.00 55.13  ? 326 THR A O   1 
ATOM   5959 C CB  . THR B 2 335 ? 160.926 166.976 127.783 1.00 54.14  ? 326 THR A CB  1 
ATOM   5960 O OG1 . THR B 2 335 ? 160.351 166.121 128.779 1.00 48.23  ? 326 THR A OG1 1 
ATOM   5961 C CG2 . THR B 2 335 ? 162.349 166.555 127.473 1.00 57.49  ? 326 THR A CG2 1 
ATOM   5962 N N   . ILE B 2 336 ? 159.101 168.819 126.659 1.00 50.14  ? 327 ILE A N   1 
ATOM   5963 C CA  . ILE B 2 336 ? 157.879 169.435 126.160 1.00 54.30  ? 327 ILE A CA  1 
ATOM   5964 C C   . ILE B 2 336 ? 156.696 168.516 126.433 1.00 56.55  ? 327 ILE A C   1 
ATOM   5965 O O   . ILE B 2 336 ? 156.834 167.287 126.470 1.00 59.63  ? 327 ILE A O   1 
ATOM   5966 C CB  . ILE B 2 336 ? 158.004 169.762 124.659 1.00 53.56  ? 327 ILE A CB  1 
ATOM   5967 C CG1 . ILE B 2 336 ? 159.310 170.502 124.355 1.00 51.56  ? 327 ILE A CG1 1 
ATOM   5968 C CG2 . ILE B 2 336 ? 156.849 170.634 124.195 1.00 56.94  ? 327 ILE A CG2 1 
ATOM   5969 C CD1 . ILE B 2 336 ? 160.503 169.608 124.054 1.00 54.50  ? 327 ILE A CD1 1 
ATOM   5970 N N   . GLN B 2 337 ? 155.525 169.111 126.649 1.00 58.77  ? 328 GLN A N   1 
ATOM   5971 C CA  . GLN B 2 337 ? 154.314 168.325 126.830 1.00 61.37  ? 328 GLN A CA  1 
ATOM   5972 C C   . GLN B 2 337 ? 154.004 167.537 125.566 1.00 67.44  ? 328 GLN A C   1 
ATOM   5973 O O   . GLN B 2 337 ? 154.198 168.021 124.449 1.00 70.14  ? 328 GLN A O   1 
ATOM   5974 C CB  . GLN B 2 337 ? 153.136 169.235 127.171 1.00 64.94  ? 328 GLN A CB  1 
ATOM   5975 C CG  . GLN B 2 337 ? 151.837 168.500 127.449 1.00 70.50  ? 328 GLN A CG  1 
ATOM   5976 C CD  . GLN B 2 337 ? 151.159 168.981 128.713 1.00 80.30  ? 328 GLN A CD  1 
ATOM   5977 O OE1 . GLN B 2 337 ? 151.738 168.949 129.794 1.00 69.81  ? 328 GLN A OE1 1 
ATOM   5978 N NE2 . GLN B 2 337 ? 149.925 169.449 128.576 1.00 83.24  ? 328 GLN A NE2 1 
ATOM   5979 N N   . SER B 2 338 ? 153.509 166.317 125.745 1.00 68.51  ? 329 SER A N   1 
ATOM   5980 C CA  . SER B 2 338 ? 153.117 165.502 124.606 1.00 70.21  ? 329 SER A CA  1 
ATOM   5981 C C   . SER B 2 338 ? 151.812 166.023 124.021 1.00 69.47  ? 329 SER A C   1 
ATOM   5982 O O   . SER B 2 338 ? 150.821 166.191 124.739 1.00 67.19  ? 329 SER A O   1 
ATOM   5983 C CB  . SER B 2 338 ? 152.966 164.040 125.026 1.00 80.80  ? 329 SER A CB  1 
ATOM   5984 O OG  . SER B 2 338 ? 152.159 163.321 124.109 1.00 83.21  ? 329 SER A OG  1 
ATOM   5985 N N   . VAL B 2 339 ? 151.813 166.287 122.714 1.00 67.46  ? 330 VAL A N   1 
ATOM   5986 C CA  . VAL B 2 339 ? 150.622 166.709 121.996 1.00 59.83  ? 330 VAL A CA  1 
ATOM   5987 C C   . VAL B 2 339 ? 150.341 165.648 120.940 1.00 63.03  ? 330 VAL A C   1 
ATOM   5988 O O   . VAL B 2 339 ? 151.075 165.551 119.953 1.00 61.54  ? 330 VAL A O   1 
ATOM   5989 C CB  . VAL B 2 339 ? 150.775 168.091 121.336 1.00 45.81  ? 330 VAL A CB  1 
ATOM   5990 C CG1 . VAL B 2 339 ? 149.608 168.360 120.406 1.00 44.05  ? 330 VAL A CG1 1 
ATOM   5991 C CG2 . VAL B 2 339 ? 150.890 169.179 122.384 1.00 44.42  ? 330 VAL A CG2 1 
ATOM   5992 N N   . PRO B 2 340 ? 149.308 164.824 121.101 1.00 62.51  ? 331 PRO A N   1 
ATOM   5993 C CA  . PRO B 2 340 ? 149.045 163.776 120.107 1.00 55.54  ? 331 PRO A CA  1 
ATOM   5994 C C   . PRO B 2 340 ? 148.542 164.338 118.789 1.00 57.23  ? 331 PRO A C   1 
ATOM   5995 O O   . PRO B 2 340 ? 147.490 164.983 118.740 1.00 61.81  ? 331 PRO A O   1 
ATOM   5996 C CB  . PRO B 2 340 ? 147.983 162.906 120.790 1.00 56.99  ? 331 PRO A CB  1 
ATOM   5997 C CG  . PRO B 2 340 ? 147.307 163.818 121.746 1.00 59.04  ? 331 PRO A CG  1 
ATOM   5998 C CD  . PRO B 2 340 ? 148.347 164.790 122.216 1.00 63.77  ? 331 PRO A CD  1 
ATOM   5999 N N   . ILE B 2 341 ? 149.290 164.104 117.717 1.00 54.76  ? 332 ILE A N   1 
ATOM   6000 C CA  . ILE B 2 341 ? 148.892 164.519 116.376 1.00 48.53  ? 332 ILE A CA  1 
ATOM   6001 C C   . ILE B 2 341 ? 148.104 163.372 115.749 1.00 54.82  ? 332 ILE A C   1 
ATOM   6002 O O   . ILE B 2 341 ? 148.685 162.304 115.504 1.00 62.73  ? 332 ILE A O   1 
ATOM   6003 C CB  . ILE B 2 341 ? 150.107 164.879 115.516 1.00 48.90  ? 332 ILE A CB  1 
ATOM   6004 C CG1 . ILE B 2 341 ? 150.985 165.896 116.240 1.00 52.53  ? 332 ILE A CG1 1 
ATOM   6005 C CG2 . ILE B 2 341 ? 149.661 165.422 114.178 1.00 43.68  ? 332 ILE A CG2 1 
ATOM   6006 C CD1 . ILE B 2 341 ? 152.011 166.535 115.359 1.00 47.02  ? 332 ILE A CD1 1 
ATOM   6007 N N   . PRO B 2 342 ? 146.813 163.544 115.476 1.00 55.28  ? 333 PRO A N   1 
ATOM   6008 C CA  . PRO B 2 342 ? 146.020 162.429 114.941 1.00 57.70  ? 333 PRO A CA  1 
ATOM   6009 C C   . PRO B 2 342 ? 146.405 162.119 113.502 1.00 63.31  ? 333 PRO A C   1 
ATOM   6010 O O   . PRO B 2 342 ? 146.394 162.995 112.636 1.00 62.71  ? 333 PRO A O   1 
ATOM   6011 C CB  . PRO B 2 342 ? 144.576 162.934 115.044 1.00 49.19  ? 333 PRO A CB  1 
ATOM   6012 C CG  . PRO B 2 342 ? 144.633 164.100 115.980 1.00 56.53  ? 333 PRO A CG  1 
ATOM   6013 C CD  . PRO B 2 342 ? 145.977 164.710 115.787 1.00 50.89  ? 333 PRO A CD  1 
ATOM   6014 N N   . GLY B 2 343 ? 146.734 160.855 113.254 1.00 66.21  ? 334 GLY A N   1 
ATOM   6015 C CA  . GLY B 2 343 ? 147.131 160.415 111.936 1.00 63.48  ? 334 GLY A CA  1 
ATOM   6016 C C   . GLY B 2 343 ? 148.613 160.461 111.656 1.00 66.80  ? 334 GLY A C   1 
ATOM   6017 O O   . GLY B 2 343 ? 149.031 160.051 110.569 1.00 73.30  ? 334 GLY A O   1 
ATOM   6018 N N   . PHE B 2 344 ? 149.428 160.941 112.596 1.00 60.37  ? 335 PHE A N   1 
ATOM   6019 C CA  . PHE B 2 344 ? 150.857 161.026 112.326 1.00 64.59  ? 335 PHE A CA  1 
ATOM   6020 C C   . PHE B 2 344 ? 151.578 159.720 112.627 1.00 82.46  ? 335 PHE A C   1 
ATOM   6021 O O   . PHE B 2 344 ? 152.536 159.373 111.932 1.00 91.30  ? 335 PHE A O   1 
ATOM   6022 C CB  . PHE B 2 344 ? 151.501 162.154 113.123 1.00 66.08  ? 335 PHE A CB  1 
ATOM   6023 C CG  . PHE B 2 344 ? 152.996 162.168 113.020 1.00 63.76  ? 335 PHE A CG  1 
ATOM   6024 C CD1 . PHE B 2 344 ? 153.613 162.384 111.803 1.00 56.26  ? 335 PHE A CD1 1 
ATOM   6025 C CD2 . PHE B 2 344 ? 153.784 161.936 114.131 1.00 66.82  ? 335 PHE A CD2 1 
ATOM   6026 C CE1 . PHE B 2 344 ? 154.981 162.382 111.699 1.00 58.89  ? 335 PHE A CE1 1 
ATOM   6027 C CE2 . PHE B 2 344 ? 155.157 161.935 114.030 1.00 62.12  ? 335 PHE A CE2 1 
ATOM   6028 C CZ  . PHE B 2 344 ? 155.755 162.161 112.814 1.00 60.97  ? 335 PHE A CZ  1 
ATOM   6029 N N   . SER B 2 345 ? 151.167 158.999 113.671 1.00 84.26  ? 336 SER A N   1 
ATOM   6030 C CA  . SER B 2 345 ? 151.831 157.737 113.983 1.00 89.64  ? 336 SER A CA  1 
ATOM   6031 C C   . SER B 2 345 ? 151.645 156.729 112.857 1.00 91.74  ? 336 SER A C   1 
ATOM   6032 O O   . SER B 2 345 ? 152.591 156.030 112.471 1.00 92.81  ? 336 SER A O   1 
ATOM   6033 C CB  . SER B 2 345 ? 151.304 157.177 115.303 1.00 95.16  ? 336 SER A CB  1 
ATOM   6034 O OG  . SER B 2 345 ? 152.293 156.399 115.954 1.00 101.45 ? 336 SER A OG  1 
ATOM   6035 N N   . GLU B 2 346 ? 150.434 156.654 112.305 1.00 91.00  ? 337 GLU A N   1 
ATOM   6036 C CA  . GLU B 2 346 ? 150.179 155.755 111.187 1.00 93.17  ? 337 GLU A CA  1 
ATOM   6037 C C   . GLU B 2 346 ? 150.890 156.228 109.925 1.00 94.90  ? 337 GLU A C   1 
ATOM   6038 O O   . GLU B 2 346 ? 151.338 155.409 109.116 1.00 102.91 ? 337 GLU A O   1 
ATOM   6039 C CB  . GLU B 2 346 ? 148.674 155.636 110.952 1.00 95.99  ? 337 GLU A CB  1 
ATOM   6040 C CG  . GLU B 2 346 ? 148.018 154.525 111.755 1.00 104.97 ? 337 GLU A CG  1 
ATOM   6041 C CD  . GLU B 2 346 ? 147.834 154.893 113.216 1.00 104.55 ? 337 GLU A CD  1 
ATOM   6042 O OE1 . GLU B 2 346 ? 147.831 156.101 113.532 1.00 94.47  ? 337 GLU A OE1 1 
ATOM   6043 O OE2 . GLU B 2 346 ? 147.693 153.973 114.049 1.00 104.54 ? 337 GLU A OE2 1 
ATOM   6044 N N   . PHE B 2 347 ? 150.990 157.545 109.736 1.00 92.41  ? 338 PHE A N   1 
ATOM   6045 C CA  . PHE B 2 347 ? 151.719 158.088 108.593 1.00 90.63  ? 338 PHE A CA  1 
ATOM   6046 C C   . PHE B 2 347 ? 153.201 157.740 108.675 1.00 93.49  ? 338 PHE A C   1 
ATOM   6047 O O   . PHE B 2 347 ? 153.818 157.365 107.671 1.00 93.82  ? 338 PHE A O   1 
ATOM   6048 C CB  . PHE B 2 347 ? 151.510 159.604 108.536 1.00 77.95  ? 338 PHE A CB  1 
ATOM   6049 C CG  . PHE B 2 347 ? 152.368 160.315 107.526 1.00 79.46  ? 338 PHE A CG  1 
ATOM   6050 C CD1 . PHE B 2 347 ? 151.935 160.470 106.221 1.00 80.59  ? 338 PHE A CD1 1 
ATOM   6051 C CD2 . PHE B 2 347 ? 153.592 160.854 107.888 1.00 78.90  ? 338 PHE A CD2 1 
ATOM   6052 C CE1 . PHE B 2 347 ? 152.714 161.136 105.293 1.00 75.97  ? 338 PHE A CE1 1 
ATOM   6053 C CE2 . PHE B 2 347 ? 154.374 161.514 106.963 1.00 76.26  ? 338 PHE A CE2 1 
ATOM   6054 C CZ  . PHE B 2 347 ? 153.934 161.657 105.665 1.00 72.96  ? 338 PHE A CZ  1 
ATOM   6055 N N   . ARG B 2 348 ? 153.786 157.859 109.869 1.00 90.41  ? 339 ARG A N   1 
ATOM   6056 C CA  . ARG B 2 348 ? 155.189 157.514 110.065 1.00 95.19  ? 339 ARG A CA  1 
ATOM   6057 C C   . ARG B 2 348 ? 155.423 156.018 109.896 1.00 106.72 ? 339 ARG A C   1 
ATOM   6058 O O   . ARG B 2 348 ? 156.394 155.606 109.251 1.00 108.77 ? 339 ARG A O   1 
ATOM   6059 C CB  . ARG B 2 348 ? 155.646 157.972 111.449 1.00 88.10  ? 339 ARG A CB  1 
ATOM   6060 C CG  . ARG B 2 348 ? 157.106 157.690 111.747 1.00 92.79  ? 339 ARG A CG  1 
ATOM   6061 C CD  . ARG B 2 348 ? 157.291 157.151 113.157 1.00 94.17  ? 339 ARG A CD  1 
ATOM   6062 N NE  . ARG B 2 348 ? 157.101 158.177 114.175 1.00 95.03  ? 339 ARG A NE  1 
ATOM   6063 C CZ  . ARG B 2 348 ? 156.041 158.263 114.966 1.00 90.88  ? 339 ARG A CZ  1 
ATOM   6064 N NH1 . ARG B 2 348 ? 155.045 157.398 114.883 1.00 94.61  ? 339 ARG A NH1 1 
ATOM   6065 N NH2 . ARG B 2 348 ? 155.981 159.241 115.866 1.00 81.49  ? 339 ARG A NH2 1 
ATOM   6066 N N   . GLU B 2 349 ? 154.548 155.190 110.473 1.00 106.94 ? 340 GLU A N   1 
ATOM   6067 C CA  . GLU B 2 349 ? 154.700 153.744 110.339 1.00 108.77 ? 340 GLU A CA  1 
ATOM   6068 C C   . GLU B 2 349 ? 154.517 153.297 108.894 1.00 111.00 ? 340 GLU A C   1 
ATOM   6069 O O   . GLU B 2 349 ? 155.191 152.368 108.435 1.00 110.78 ? 340 GLU A O   1 
ATOM   6070 C CB  . GLU B 2 349 ? 153.709 153.022 111.251 1.00 110.48 ? 340 GLU A CB  1 
ATOM   6071 C CG  . GLU B 2 349 ? 154.086 153.044 112.723 1.00 116.73 ? 340 GLU A CG  1 
ATOM   6072 C CD  . GLU B 2 349 ? 153.279 152.056 113.542 1.00 118.80 ? 340 GLU A CD  1 
ATOM   6073 O OE1 . GLU B 2 349 ? 152.230 151.592 113.049 1.00 115.52 ? 340 GLU A OE1 1 
ATOM   6074 O OE2 . GLU B 2 349 ? 153.694 151.745 114.678 1.00 116.19 ? 340 GLU A OE2 1 
ATOM   6075 N N   . TRP B 2 350 ? 153.600 153.941 108.167 1.00 109.94 ? 341 TRP A N   1 
ATOM   6076 C CA  . TRP B 2 350 ? 153.351 153.567 106.778 1.00 114.91 ? 341 TRP A CA  1 
ATOM   6077 C C   . TRP B 2 350 ? 154.581 153.800 105.910 1.00 120.62 ? 341 TRP A C   1 
ATOM   6078 O O   . TRP B 2 350 ? 154.910 152.974 105.051 1.00 124.15 ? 341 TRP A O   1 
ATOM   6079 C CB  . TRP B 2 350 ? 152.156 154.348 106.234 1.00 113.93 ? 341 TRP A CB  1 
ATOM   6080 C CG  . TRP B 2 350 ? 151.801 153.998 104.827 1.00 122.66 ? 341 TRP A CG  1 
ATOM   6081 C CD1 . TRP B 2 350 ? 152.085 154.721 103.706 1.00 122.92 ? 341 TRP A CD1 1 
ATOM   6082 C CD2 . TRP B 2 350 ? 151.088 152.837 104.386 1.00 128.95 ? 341 TRP A CD2 1 
ATOM   6083 N NE1 . TRP B 2 350 ? 151.596 154.081 102.594 1.00 126.80 ? 341 TRP A NE1 1 
ATOM   6084 C CE2 . TRP B 2 350 ? 150.979 152.921 102.984 1.00 128.92 ? 341 TRP A CE2 1 
ATOM   6085 C CE3 . TRP B 2 350 ? 150.533 151.733 105.041 1.00 126.91 ? 341 TRP A CE3 1 
ATOM   6086 C CZ2 . TRP B 2 350 ? 150.338 151.944 102.225 1.00 125.83 ? 341 TRP A CZ2 1 
ATOM   6087 C CZ3 . TRP B 2 350 ? 149.897 150.764 104.285 1.00 125.89 ? 341 TRP A CZ3 1 
ATOM   6088 C CH2 . TRP B 2 350 ? 149.804 150.876 102.893 1.00 126.48 ? 341 TRP A CH2 1 
ATOM   6089 N N   . GLY B 2 351 ? 155.271 154.917 106.117 1.00 116.87 ? 342 GLY A N   1 
ATOM   6090 C CA  . GLY B 2 351 ? 156.445 155.243 105.330 1.00 120.82 ? 342 GLY A CA  1 
ATOM   6091 C C   . GLY B 2 351 ? 157.612 154.300 105.552 1.00 125.03 ? 342 GLY A C   1 
ATOM   6092 O O   . GLY B 2 351 ? 158.106 153.676 104.613 1.00 121.66 ? 342 GLY A O   1 
ATOM   6093 N N   . THR B 2 367 ? 170.520 167.158 95.789  1.00 100.65 ? 358 THR A N   1 
ATOM   6094 C CA  . THR B 2 367 ? 171.702 167.929 95.348  1.00 108.34 ? 358 THR A CA  1 
ATOM   6095 C C   . THR B 2 367 ? 172.882 167.505 96.191  1.00 105.38 ? 358 THR A C   1 
ATOM   6096 O O   . THR B 2 367 ? 173.833 166.932 95.620  1.00 103.88 ? 358 THR A O   1 
ATOM   6097 C CB  . THR B 2 367 ? 171.419 169.429 95.443  1.00 107.98 ? 358 THR A CB  1 
ATOM   6098 O OG1 . THR B 2 367 ? 171.289 169.737 96.828  1.00 93.74  ? 358 THR A OG1 1 
ATOM   6099 C CG2 . THR B 2 367 ? 170.146 169.826 94.716  1.00 98.12  ? 358 THR A CG2 1 
ATOM   6100 N N   . CYS B 2 368 ? 172.842 167.777 97.497  1.00 103.54 ? 359 CYS A N   1 
ATOM   6101 C CA  . CYS B 2 368 ? 173.913 167.298 98.408  1.00 111.77 ? 359 CYS A CA  1 
ATOM   6102 C C   . CYS B 2 368 ? 173.326 167.136 99.813  1.00 108.79 ? 359 CYS A C   1 
ATOM   6103 O O   . CYS B 2 368 ? 172.254 167.713 100.072 1.00 100.56 ? 359 CYS A O   1 
ATOM   6104 C CB  . CYS B 2 368 ? 175.114 168.238 98.456  1.00 116.88 ? 359 CYS A CB  1 
ATOM   6105 S SG  . CYS B 2 368 ? 174.852 169.831 97.638  1.00 124.32 ? 359 CYS A SG  1 
ATOM   6106 N N   . ASN B 2 369 ? 174.018 166.395 100.674 1.00 106.74 ? 360 ASN A N   1 
ATOM   6107 C CA  . ASN B 2 369 ? 173.521 166.148 102.051 1.00 100.45 ? 360 ASN A CA  1 
ATOM   6108 C C   . ASN B 2 369 ? 171.998 166.061 102.015 1.00 95.13  ? 360 ASN A C   1 
ATOM   6109 O O   . ASN B 2 369 ? 171.365 166.766 102.804 1.00 93.89  ? 360 ASN A O   1 
ATOM   6110 C CB  . ASN B 2 369 ? 173.989 167.241 102.997 1.00 99.51  ? 360 ASN A CB  1 
ATOM   6111 C CG  . ASN B 2 369 ? 175.332 166.940 103.612 1.00 106.96 ? 360 ASN A CG  1 
ATOM   6112 O OD1 . ASN B 2 369 ? 175.406 166.607 104.799 1.00 105.55 ? 360 ASN A OD1 1 
ATOM   6113 N ND2 . ASN B 2 369 ? 176.397 167.062 102.835 1.00 113.88 ? 360 ASN A ND2 1 
ATOM   6114 N N   . GLN B 2 370 ? 171.432 165.221 101.146 1.00 96.69  ? 361 GLN A N   1 
ATOM   6115 C CA  . GLN B 2 370 ? 169.978 165.203 101.046 1.00 91.37  ? 361 GLN A CA  1 
ATOM   6116 C C   . GLN B 2 370 ? 169.404 163.789 101.006 1.00 101.20 ? 361 GLN A C   1 
ATOM   6117 O O   . GLN B 2 370 ? 168.273 163.607 100.540 1.00 101.75 ? 361 GLN A O   1 
ATOM   6118 C CB  . GLN B 2 370 ? 169.519 165.976 99.803  1.00 85.79  ? 361 GLN A CB  1 
ATOM   6119 C CG  . GLN B 2 370 ? 168.246 166.778 99.998  1.00 72.52  ? 361 GLN A CG  1 
ATOM   6120 C CD  . GLN B 2 370 ? 168.078 167.871 98.960  1.00 76.70  ? 361 GLN A CD  1 
ATOM   6121 O OE1 . GLN B 2 370 ? 169.053 168.342 98.378  1.00 87.43  ? 361 GLN A OE1 1 
ATOM   6122 N NE2 . GLN B 2 370 ? 166.838 168.284 98.728  1.00 63.69  ? 361 GLN A NE2 1 
ATOM   6123 N N   . GLU B 2 371 ? 170.140 162.784 101.477 1.00 104.95 ? 362 GLU A N   1 
ATOM   6124 C CA  . GLU B 2 371 ? 169.655 161.410 101.435 1.00 111.71 ? 362 GLU A CA  1 
ATOM   6125 C C   . GLU B 2 371 ? 170.244 160.609 102.586 1.00 115.39 ? 362 GLU A C   1 
ATOM   6126 O O   . GLU B 2 371 ? 171.426 160.759 102.910 1.00 117.10 ? 362 GLU A O   1 
ATOM   6127 C CB  . GLU B 2 371 ? 170.005 160.739 100.101 1.00 116.07 ? 362 GLU A CB  1 
ATOM   6128 C CG  . GLU B 2 371 ? 168.955 160.913 99.016  1.00 121.05 ? 362 GLU A CG  1 
ATOM   6129 C CD  . GLU B 2 371 ? 167.906 159.817 99.041  1.00 121.96 ? 362 GLU A CD  1 
ATOM   6130 O OE1 . GLU B 2 371 ? 167.995 158.926 99.911  1.00 120.07 ? 362 GLU A OE1 1 
ATOM   6131 O OE2 . GLU B 2 371 ? 166.993 159.845 98.190  1.00 119.39 ? 362 GLU A OE2 1 
ATOM   6132 N N   . CYS B 2 372 ? 169.414 159.766 103.196 1.00 120.34 ? 363 CYS A N   1 
ATOM   6133 C CA  . CYS B 2 372 ? 169.850 158.794 104.187 1.00 128.01 ? 363 CYS A CA  1 
ATOM   6134 C C   . CYS B 2 372 ? 169.163 157.466 103.907 1.00 132.37 ? 363 CYS A C   1 
ATOM   6135 O O   . CYS B 2 372 ? 168.028 157.437 103.422 1.00 133.18 ? 363 CYS A O   1 
ATOM   6136 C CB  . CYS B 2 372 ? 169.544 159.264 105.614 1.00 123.60 ? 363 CYS A CB  1 
ATOM   6137 S SG  . CYS B 2 372 ? 167.841 158.996 106.153 1.00 130.79 ? 363 CYS A SG  1 
ATOM   6138 N N   . ASP B 2 373 ? 169.856 156.369 104.204 1.00 132.40 ? 364 ASP A N   1 
ATOM   6139 C CA  . ASP B 2 373 ? 169.350 155.027 103.934 1.00 134.65 ? 364 ASP A CA  1 
ATOM   6140 C C   . ASP B 2 373 ? 169.071 154.215 105.187 1.00 133.59 ? 364 ASP A C   1 
ATOM   6141 O O   . ASP B 2 373 ? 168.106 153.450 105.216 1.00 130.82 ? 364 ASP A O   1 
ATOM   6142 C CB  . ASP B 2 373 ? 170.339 154.259 103.050 1.00 134.59 ? 364 ASP A CB  1 
ATOM   6143 C CG  . ASP B 2 373 ? 171.034 155.151 102.041 1.00 136.94 ? 364 ASP A CG  1 
ATOM   6144 O OD1 . ASP B 2 373 ? 170.332 155.772 101.216 1.00 136.25 ? 364 ASP A OD1 1 
ATOM   6145 O OD2 . ASP B 2 373 ? 172.279 155.231 102.073 1.00 134.69 ? 364 ASP A OD2 1 
ATOM   6146 N N   . ASN B 2 374 ? 169.892 154.360 106.229 1.00 133.80 ? 365 ASN A N   1 
ATOM   6147 C CA  . ASN B 2 374 ? 169.711 153.573 107.442 1.00 133.34 ? 365 ASN A CA  1 
ATOM   6148 C C   . ASN B 2 374 ? 168.665 154.160 108.381 1.00 131.94 ? 365 ASN A C   1 
ATOM   6149 O O   . ASN B 2 374 ? 168.417 153.573 109.439 1.00 131.71 ? 365 ASN A O   1 
ATOM   6150 C CB  . ASN B 2 374 ? 171.043 153.432 108.183 1.00 132.33 ? 365 ASN A CB  1 
ATOM   6151 C CG  . ASN B 2 374 ? 172.235 153.398 107.244 1.00 130.32 ? 365 ASN A CG  1 
ATOM   6152 O OD1 . ASN B 2 374 ? 172.245 152.659 106.260 1.00 129.99 ? 365 ASN A OD1 1 
ATOM   6153 N ND2 . ASN B 2 374 ? 173.249 154.201 107.547 1.00 125.04 ? 365 ASN A ND2 1 
ATOM   6154 N N   . CYS B 2 375 ? 168.059 155.298 108.032 1.00 131.01 ? 366 CYS A N   1 
ATOM   6155 C CA  . CYS B 2 375 ? 167.094 155.933 108.926 1.00 129.68 ? 366 CYS A CA  1 
ATOM   6156 C C   . CYS B 2 375 ? 165.875 155.049 109.157 1.00 127.06 ? 366 CYS A C   1 
ATOM   6157 O O   . CYS B 2 375 ? 165.392 154.929 110.289 1.00 125.48 ? 366 CYS A O   1 
ATOM   6158 C CB  . CYS B 2 375 ? 166.670 157.290 108.365 1.00 120.94 ? 366 CYS A CB  1 
ATOM   6159 S SG  . CYS B 2 375 ? 168.028 158.448 108.099 1.00 127.75 ? 366 CYS A SG  1 
ATOM   6160 N N   . LEU B 2 376 ? 165.360 154.424 108.096 1.00 126.69 ? 367 LEU A N   1 
ATOM   6161 C CA  . LEU B 2 376 ? 164.182 153.573 108.236 1.00 128.35 ? 367 LEU A CA  1 
ATOM   6162 C C   . LEU B 2 376 ? 164.479 152.360 109.111 1.00 128.46 ? 367 LEU A C   1 
ATOM   6163 O O   . LEU B 2 376 ? 163.715 152.037 110.029 1.00 126.01 ? 367 LEU A O   1 
ATOM   6164 C CB  . LEU B 2 376 ? 163.691 153.135 106.856 1.00 125.87 ? 367 LEU A CB  1 
ATOM   6165 C CG  . LEU B 2 376 ? 162.210 152.777 106.728 1.00 127.74 ? 367 LEU A CG  1 
ATOM   6166 C CD1 . LEU B 2 376 ? 161.348 153.737 107.534 1.00 122.45 ? 367 LEU A CD1 1 
ATOM   6167 C CD2 . LEU B 2 376 ? 161.788 152.768 105.268 1.00 124.77 ? 367 LEU A CD2 1 
ATOM   6168 N N   . ASN B 2 377 ? 165.591 151.674 108.840 1.00 128.54 ? 368 ASN A N   1 
ATOM   6169 C CA  . ASN B 2 377 ? 165.929 150.489 109.620 1.00 128.54 ? 368 ASN A CA  1 
ATOM   6170 C C   . ASN B 2 377 ? 166.311 150.848 111.050 1.00 127.85 ? 368 ASN A C   1 
ATOM   6171 O O   . ASN B 2 377 ? 166.149 150.024 111.958 1.00 125.86 ? 368 ASN A O   1 
ATOM   6172 C CB  . ASN B 2 377 ? 167.057 149.715 108.937 1.00 128.14 ? 368 ASN A CB  1 
ATOM   6173 C CG  . ASN B 2 377 ? 166.539 148.606 108.042 1.00 128.61 ? 368 ASN A CG  1 
ATOM   6174 O OD1 . ASN B 2 377 ? 165.415 148.673 107.545 1.00 125.55 ? 368 ASN A OD1 1 
ATOM   6175 N ND2 . ASN B 2 377 ? 167.353 147.579 107.834 1.00 131.53 ? 368 ASN A ND2 1 
ATOM   6176 N N   . ALA B 2 378 ? 166.820 152.061 111.273 1.00 127.84 ? 369 ALA A N   1 
ATOM   6177 C CA  . ALA B 2 378 ? 167.133 152.488 112.632 1.00 126.64 ? 369 ALA A CA  1 
ATOM   6178 C C   . ALA B 2 378 ? 165.868 152.833 113.408 1.00 125.84 ? 369 ALA A C   1 
ATOM   6179 O O   . ALA B 2 378 ? 165.764 152.528 114.601 1.00 125.25 ? 369 ALA A O   1 
ATOM   6180 C CB  . ALA B 2 378 ? 168.090 153.678 112.608 1.00 125.70 ? 369 ALA A CB  1 
ATOM   6181 N N   . THR B 2 379 ? 164.897 153.470 112.751 1.00 124.53 ? 370 THR A N   1 
ATOM   6182 C CA  . THR B 2 379 ? 163.659 153.843 113.423 1.00 125.52 ? 370 THR A CA  1 
ATOM   6183 C C   . THR B 2 379 ? 162.678 152.686 113.548 1.00 123.68 ? 370 THR A C   1 
ATOM   6184 O O   . THR B 2 379 ? 161.726 152.788 114.328 1.00 120.23 ? 370 THR A O   1 
ATOM   6185 C CB  . THR B 2 379 ? 162.980 155.009 112.692 1.00 122.43 ? 370 THR A CB  1 
ATOM   6186 O OG1 . THR B 2 379 ? 161.965 155.573 113.532 1.00 115.36 ? 370 THR A OG1 1 
ATOM   6187 C CG2 . THR B 2 379 ? 162.341 154.539 111.397 1.00 122.32 ? 370 THR A CG2 1 
ATOM   6188 N N   . LEU B 2 380 ? 162.881 151.596 112.803 1.00 125.68 ? 371 LEU A N   1 
ATOM   6189 C CA  . LEU B 2 380 ? 162.009 150.435 112.959 1.00 125.97 ? 371 LEU A CA  1 
ATOM   6190 C C   . LEU B 2 380 ? 162.128 149.836 114.356 1.00 123.69 ? 371 LEU A C   1 
ATOM   6191 O O   . LEU B 2 380 ? 161.126 149.415 114.945 1.00 121.03 ? 371 LEU A O   1 
ATOM   6192 C CB  . LEU B 2 380 ? 162.332 149.387 111.894 1.00 126.58 ? 371 LEU A CB  1 
ATOM   6193 C CG  . LEU B 2 380 ? 161.674 149.607 110.529 1.00 128.33 ? 371 LEU A CG  1 
ATOM   6194 C CD1 . LEU B 2 380 ? 162.336 148.749 109.462 1.00 126.28 ? 371 LEU A CD1 1 
ATOM   6195 C CD2 . LEU B 2 380 ? 160.181 149.330 110.598 1.00 121.40 ? 371 LEU A CD2 1 
ATOM   6196 N N   . SER B 2 381 ? 163.346 149.787 114.902 1.00 127.03 ? 372 SER A N   1 
ATOM   6197 C CA  . SER B 2 381 ? 163.547 149.223 116.233 1.00 125.74 ? 372 SER A CA  1 
ATOM   6198 C C   . SER B 2 381 ? 163.088 150.161 117.343 1.00 125.09 ? 372 SER A C   1 
ATOM   6199 O O   . SER B 2 381 ? 162.853 149.702 118.465 1.00 119.95 ? 372 SER A O   1 
ATOM   6200 C CB  . SER B 2 381 ? 165.020 148.865 116.433 1.00 119.83 ? 372 SER A CB  1 
ATOM   6201 O OG  . SER B 2 381 ? 165.819 150.031 116.535 1.00 120.39 ? 372 SER A OG  1 
ATOM   6202 N N   . PHE B 2 382 ? 162.963 151.456 117.061 1.00 124.94 ? 373 PHE A N   1 
ATOM   6203 C CA  . PHE B 2 382 ? 162.504 152.436 118.036 1.00 120.73 ? 373 PHE A CA  1 
ATOM   6204 C C   . PHE B 2 382 ? 161.042 152.815 117.840 1.00 118.77 ? 373 PHE A C   1 
ATOM   6205 O O   . PHE B 2 382 ? 160.581 153.791 118.439 1.00 116.01 ? 373 PHE A O   1 
ATOM   6206 C CB  . PHE B 2 382 ? 163.377 153.692 117.973 1.00 116.57 ? 373 PHE A CB  1 
ATOM   6207 C CG  . PHE B 2 382 ? 164.558 153.660 118.900 1.00 119.26 ? 373 PHE A CG  1 
ATOM   6208 C CD1 . PHE B 2 382 ? 164.530 152.898 120.056 1.00 119.43 ? 373 PHE A CD1 1 
ATOM   6209 C CD2 . PHE B 2 382 ? 165.697 154.392 118.614 1.00 116.42 ? 373 PHE A CD2 1 
ATOM   6210 C CE1 . PHE B 2 382 ? 165.617 152.870 120.911 1.00 116.06 ? 373 PHE A CE1 1 
ATOM   6211 C CE2 . PHE B 2 382 ? 166.786 154.367 119.463 1.00 112.89 ? 373 PHE A CE2 1 
ATOM   6212 C CZ  . PHE B 2 382 ? 166.746 153.604 120.613 1.00 111.56 ? 373 PHE A CZ  1 
ATOM   6213 N N   . ASN B 2 383 ? 160.307 152.069 117.012 1.00 121.12 ? 374 ASN A N   1 
ATOM   6214 C CA  . ASN B 2 383 ? 158.948 152.468 116.660 1.00 119.40 ? 374 ASN A CA  1 
ATOM   6215 C C   . ASN B 2 383 ? 158.014 152.433 117.864 1.00 116.26 ? 374 ASN A C   1 
ATOM   6216 O O   . ASN B 2 383 ? 157.208 153.350 118.054 1.00 115.35 ? 374 ASN A O   1 
ATOM   6217 C CB  . ASN B 2 383 ? 158.413 151.574 115.542 1.00 118.49 ? 374 ASN A CB  1 
ATOM   6218 C CG  . ASN B 2 383 ? 157.903 152.367 114.357 1.00 118.06 ? 374 ASN A CG  1 
ATOM   6219 O OD1 . ASN B 2 383 ? 158.092 153.581 114.283 1.00 117.47 ? 374 ASN A OD1 1 
ATOM   6220 N ND2 . ASN B 2 383 ? 157.253 151.685 113.423 1.00 115.76 ? 374 ASN A ND2 1 
ATOM   6221 N N   . THR B 2 384 ? 158.100 151.386 118.687 1.00 114.45 ? 375 THR A N   1 
ATOM   6222 C CA  . THR B 2 384 ? 157.122 151.225 119.760 1.00 115.43 ? 375 THR A CA  1 
ATOM   6223 C C   . THR B 2 384 ? 157.369 152.216 120.897 1.00 115.24 ? 375 THR A C   1 
ATOM   6224 O O   . THR B 2 384 ? 156.419 152.770 121.465 1.00 113.06 ? 375 THR A O   1 
ATOM   6225 C CB  . THR B 2 384 ? 157.109 149.772 120.256 1.00 114.74 ? 375 THR A CB  1 
ATOM   6226 O OG1 . THR B 2 384 ? 155.834 149.475 120.841 1.00 111.68 ? 375 THR A OG1 1 
ATOM   6227 C CG2 . THR B 2 384 ? 158.215 149.487 121.268 1.00 112.67 ? 375 THR A CG2 1 
ATOM   6228 N N   . ILE B 2 385 ? 158.636 152.476 121.228 1.00 114.95 ? 376 ILE A N   1 
ATOM   6229 C CA  . ILE B 2 385 ? 158.932 153.424 122.297 1.00 112.21 ? 376 ILE A CA  1 
ATOM   6230 C C   . ILE B 2 385 ? 158.614 154.846 121.849 1.00 110.17 ? 376 ILE A C   1 
ATOM   6231 O O   . ILE B 2 385 ? 158.098 155.655 122.629 1.00 106.97 ? 376 ILE A O   1 
ATOM   6232 C CB  . ILE B 2 385 ? 160.394 153.275 122.760 1.00 110.89 ? 376 ILE A CB  1 
ATOM   6233 C CG1 . ILE B 2 385 ? 160.758 154.376 123.760 1.00 108.99 ? 376 ILE A CG1 1 
ATOM   6234 C CG2 . ILE B 2 385 ? 161.341 153.276 121.570 1.00 113.45 ? 376 ILE A CG2 1 
ATOM   6235 C CD1 . ILE B 2 385 ? 162.172 154.278 124.286 1.00 106.50 ? 376 ILE A CD1 1 
ATOM   6236 N N   . LEU B 2 386 ? 158.907 155.170 120.587 1.00 112.78 ? 377 LEU A N   1 
ATOM   6237 C CA  . LEU B 2 386 ? 158.525 156.471 120.047 1.00 111.17 ? 377 LEU A CA  1 
ATOM   6238 C C   . LEU B 2 386 ? 157.011 156.629 120.015 1.00 111.64 ? 377 LEU A C   1 
ATOM   6239 O O   . LEU B 2 386 ? 156.486 157.715 120.287 1.00 110.81 ? 377 LEU A O   1 
ATOM   6240 C CB  . LEU B 2 386 ? 159.108 156.652 118.646 1.00 106.83 ? 377 LEU A CB  1 
ATOM   6241 C CG  . LEU B 2 386 ? 160.525 157.219 118.553 1.00 103.51 ? 377 LEU A CG  1 
ATOM   6242 C CD1 . LEU B 2 386 ? 161.000 157.229 117.110 1.00 103.57 ? 377 LEU A CD1 1 
ATOM   6243 C CD2 . LEU B 2 386 ? 160.585 158.615 119.146 1.00 96.11  ? 377 LEU A CD2 1 
ATOM   6244 N N   . ARG B 2 387 ? 156.292 155.558 119.669 1.00 115.19 ? 378 ARG A N   1 
ATOM   6245 C CA  . ARG B 2 387 ? 154.834 155.618 119.650 1.00 115.21 ? 378 ARG A CA  1 
ATOM   6246 C C   . ARG B 2 387 ? 154.271 155.833 121.049 1.00 112.23 ? 378 ARG A C   1 
ATOM   6247 O O   . ARG B 2 387 ? 153.328 156.612 121.233 1.00 107.77 ? 378 ARG A O   1 
ATOM   6248 C CB  . ARG B 2 387 ? 154.265 154.341 119.032 1.00 114.56 ? 378 ARG A CB  1 
ATOM   6249 C CG  . ARG B 2 387 ? 152.749 154.259 119.059 1.00 115.04 ? 378 ARG A CG  1 
ATOM   6250 C CD  . ARG B 2 387 ? 152.269 152.824 118.913 1.00 115.49 ? 378 ARG A CD  1 
ATOM   6251 N NE  . ARG B 2 387 ? 151.931 152.499 117.532 1.00 118.45 ? 378 ARG A NE  1 
ATOM   6252 C CZ  . ARG B 2 387 ? 150.821 152.886 116.918 1.00 117.20 ? 378 ARG A CZ  1 
ATOM   6253 N NH1 . ARG B 2 387 ? 149.904 153.611 117.538 1.00 109.47 ? 378 ARG A NH1 1 
ATOM   6254 N NH2 . ARG B 2 387 ? 150.625 152.535 115.650 1.00 116.73 ? 378 ARG A NH2 1 
ATOM   6255 N N   . LEU B 2 388 ? 154.834 155.153 122.049 1.00 112.32 ? 379 LEU A N   1 
ATOM   6256 C CA  . LEU B 2 388 ? 154.324 155.296 123.408 1.00 110.59 ? 379 LEU A CA  1 
ATOM   6257 C C   . LEU B 2 388 ? 154.722 156.625 124.038 1.00 105.89 ? 379 LEU A C   1 
ATOM   6258 O O   . LEU B 2 388 ? 153.986 157.147 124.884 1.00 99.17  ? 379 LEU A O   1 
ATOM   6259 C CB  . LEU B 2 388 ? 154.809 154.138 124.281 1.00 109.11 ? 379 LEU A CB  1 
ATOM   6260 C CG  . LEU B 2 388 ? 154.208 152.768 123.962 1.00 109.87 ? 379 LEU A CG  1 
ATOM   6261 C CD1 . LEU B 2 388 ? 155.199 151.663 124.288 1.00 110.37 ? 379 LEU A CD1 1 
ATOM   6262 C CD2 . LEU B 2 388 ? 152.901 152.564 124.709 1.00 106.76 ? 379 LEU A CD2 1 
ATOM   6263 N N   . SER B 2 389 ? 155.868 157.187 123.645 1.00 107.55 ? 380 SER A N   1 
ATOM   6264 C CA  . SER B 2 389 ? 156.323 158.443 124.230 1.00 106.09 ? 380 SER A CA  1 
ATOM   6265 C C   . SER B 2 389 ? 155.546 159.645 123.711 1.00 105.18 ? 380 SER A C   1 
ATOM   6266 O O   . SER B 2 389 ? 155.579 160.707 124.343 1.00 98.50  ? 380 SER A O   1 
ATOM   6267 C CB  . SER B 2 389 ? 157.817 158.635 123.966 1.00 101.06 ? 380 SER A CB  1 
ATOM   6268 O OG  . SER B 2 389 ? 158.039 159.257 122.713 1.00 96.36  ? 380 SER A OG  1 
ATOM   6269 N N   . GLY B 2 390 ? 154.851 159.508 122.590 1.00 101.47 ? 381 GLY A N   1 
ATOM   6270 C CA  . GLY B 2 390 ? 154.050 160.594 122.064 1.00 94.53  ? 381 GLY A CA  1 
ATOM   6271 C C   . GLY B 2 390 ? 154.823 161.503 121.126 1.00 91.83  ? 381 GLY A C   1 
ATOM   6272 O O   . GLY B 2 390 ? 155.804 161.117 120.483 1.00 87.24  ? 381 GLY A O   1 
ATOM   6273 N N   . GLU B 2 391 ? 154.355 162.748 121.054 1.00 87.25  ? 382 GLU A N   1 
ATOM   6274 C CA  . GLU B 2 391 ? 154.911 163.757 120.158 1.00 80.25  ? 382 GLU A CA  1 
ATOM   6275 C C   . GLU B 2 391 ? 155.311 164.969 120.987 1.00 79.61  ? 382 GLU A C   1 
ATOM   6276 O O   . GLU B 2 391 ? 154.451 165.635 121.573 1.00 76.87  ? 382 GLU A O   1 
ATOM   6277 C CB  . GLU B 2 391 ? 153.902 164.144 119.076 1.00 70.93  ? 382 GLU A CB  1 
ATOM   6278 C CG  . GLU B 2 391 ? 153.664 163.063 118.032 1.00 77.61  ? 382 GLU A CG  1 
ATOM   6279 C CD  . GLU B 2 391 ? 152.522 162.134 118.392 1.00 80.56  ? 382 GLU A CD  1 
ATOM   6280 O OE1 . GLU B 2 391 ? 151.941 162.297 119.485 1.00 80.74  ? 382 GLU A OE1 1 
ATOM   6281 O OE2 . GLU B 2 391 ? 152.205 161.239 117.580 1.00 75.06  ? 382 GLU A OE2 1 
ATOM   6282 N N   . ARG B 2 392 ? 156.612 165.255 121.040 1.00 77.30  ? 383 ARG A N   1 
ATOM   6283 C CA  . ARG B 2 392 ? 157.132 166.374 121.816 1.00 70.65  ? 383 ARG A CA  1 
ATOM   6284 C C   . ARG B 2 392 ? 157.773 167.438 120.934 1.00 61.63  ? 383 ARG A C   1 
ATOM   6285 O O   . ARG B 2 392 ? 157.392 168.610 121.006 1.00 56.65  ? 383 ARG A O   1 
ATOM   6286 C CB  . ARG B 2 392 ? 158.121 165.856 122.870 1.00 66.79  ? 383 ARG A CB  1 
ATOM   6287 C CG  . ARG B 2 392 ? 157.718 164.517 123.485 1.00 70.74  ? 383 ARG A CG  1 
ATOM   6288 C CD  . ARG B 2 392 ? 158.412 164.280 124.817 1.00 71.41  ? 383 ARG A CD  1 
ATOM   6289 N NE  . ARG B 2 392 ? 157.538 164.477 125.968 1.00 74.32  ? 383 ARG A NE  1 
ATOM   6290 C CZ  . ARG B 2 392 ? 156.959 163.497 126.649 1.00 72.60  ? 383 ARG A CZ  1 
ATOM   6291 N NH1 . ARG B 2 392 ? 157.162 162.228 126.340 1.00 75.30  ? 383 ARG A NH1 1 
ATOM   6292 N NH2 . ARG B 2 392 ? 156.165 163.799 127.672 1.00 66.51  ? 383 ARG A NH2 1 
ATOM   6293 N N   . VAL B 2 393 ? 158.749 167.034 120.117 1.00 52.18  ? 384 VAL A N   1 
ATOM   6294 C CA  . VAL B 2 393 ? 159.374 167.996 119.160 1.00 48.08  ? 384 VAL A CA  1 
ATOM   6295 C C   . VAL B 2 393 ? 158.636 167.861 117.819 1.00 40.78  ? 384 VAL A C   1 
ATOM   6296 O O   . VAL B 2 393 ? 158.684 168.814 117.014 1.00 40.50  ? 384 VAL A O   1 
ATOM   6297 C CB  . VAL B 2 393 ? 160.888 167.766 118.995 1.00 46.23  ? 384 VAL A CB  1 
ATOM   6298 C CG1 . VAL B 2 393 ? 161.586 169.001 118.440 1.00 47.15  ? 384 VAL A CG1 1 
ATOM   6299 C CG2 . VAL B 2 393 ? 161.538 167.321 120.299 1.00 47.90  ? 384 VAL A CG2 1 
ATOM   6300 N N   . VAL B 2 394 ? 157.980 166.718 117.598 1.00 41.48  ? 385 VAL A N   1 
ATOM   6301 C CA  . VAL B 2 394 ? 157.188 166.522 116.347 1.00 42.97  ? 385 VAL A CA  1 
ATOM   6302 C C   . VAL B 2 394 ? 156.148 167.649 116.263 1.00 42.94  ? 385 VAL A C   1 
ATOM   6303 O O   . VAL B 2 394 ? 156.077 168.311 115.204 1.00 41.80  ? 385 VAL A O   1 
ATOM   6304 C CB  . VAL B 2 394 ? 156.521 165.134 116.315 1.00 44.75  ? 385 VAL A CB  1 
ATOM   6305 C CG1 . VAL B 2 394 ? 155.257 165.128 115.465 1.00 48.93  ? 385 VAL A CG1 1 
ATOM   6306 C CG2 . VAL B 2 394 ? 157.489 164.058 115.843 1.00 46.09  ? 385 VAL A CG2 1 
ATOM   6307 N N   . TYR B 2 395 ? 155.389 167.864 117.342 1.00 44.32  ? 386 TYR A N   1 
ATOM   6308 C CA  . TYR B 2 395 ? 154.392 168.926 117.343 1.00 31.54  ? 386 TYR A CA  1 
ATOM   6309 C C   . TYR B 2 395 ? 155.030 170.294 117.171 1.00 29.45  ? 386 TYR A C   1 
ATOM   6310 O O   . TYR B 2 395 ? 154.399 171.199 116.629 1.00 31.59  ? 386 TYR A O   1 
ATOM   6311 C CB  . TYR B 2 395 ? 153.568 168.894 118.624 1.00 34.06  ? 386 TYR A CB  1 
ATOM   6312 C CG  . TYR B 2 395 ? 152.538 169.991 118.673 1.00 32.06  ? 386 TYR A CG  1 
ATOM   6313 C CD1 . TYR B 2 395 ? 151.412 169.946 117.867 1.00 30.51  ? 386 TYR A CD1 1 
ATOM   6314 C CD2 . TYR B 2 395 ? 152.696 171.080 119.514 1.00 34.80  ? 386 TYR A CD2 1 
ATOM   6315 C CE1 . TYR B 2 395 ? 150.471 170.949 117.905 1.00 31.82  ? 386 TYR A CE1 1 
ATOM   6316 C CE2 . TYR B 2 395 ? 151.762 172.088 119.557 1.00 31.69  ? 386 TYR A CE2 1 
ATOM   6317 C CZ  . TYR B 2 395 ? 150.652 172.016 118.751 1.00 32.73  ? 386 TYR A CZ  1 
ATOM   6318 O OH  . TYR B 2 395 ? 149.719 173.018 118.792 1.00 35.71  ? 386 TYR A OH  1 
ATOM   6319 N N   . SER B 2 396 ? 156.271 170.471 117.624 1.00 31.59  ? 387 SER A N   1 
ATOM   6320 C CA  . SER B 2 396 ? 156.958 171.736 117.383 1.00 28.86  ? 387 SER A CA  1 
ATOM   6321 C C   . SER B 2 396 ? 157.159 171.976 115.892 1.00 31.54  ? 387 SER A C   1 
ATOM   6322 O O   . SER B 2 396 ? 156.874 173.068 115.386 1.00 35.83  ? 387 SER A O   1 
ATOM   6323 C CB  . SER B 2 396 ? 158.295 171.749 118.117 1.00 30.98  ? 387 SER A CB  1 
ATOM   6324 O OG  . SER B 2 396 ? 158.100 171.928 119.506 1.00 37.11  ? 387 SER A OG  1 
ATOM   6325 N N   . VAL B 2 397 ? 157.626 170.958 115.167 1.00 33.00  ? 388 VAL A N   1 
ATOM   6326 C CA  . VAL B 2 397 ? 157.769 171.081 113.716 1.00 30.38  ? 388 VAL A CA  1 
ATOM   6327 C C   . VAL B 2 397 ? 156.408 171.264 113.053 1.00 31.32  ? 388 VAL A C   1 
ATOM   6328 O O   . VAL B 2 397 ? 156.250 172.069 112.123 1.00 36.96  ? 388 VAL A O   1 
ATOM   6329 C CB  . VAL B 2 397 ? 158.512 169.858 113.151 1.00 32.14  ? 388 VAL A CB  1 
ATOM   6330 C CG1 . VAL B 2 397 ? 158.928 170.118 111.729 1.00 38.84  ? 388 VAL A CG1 1 
ATOM   6331 C CG2 . VAL B 2 397 ? 159.720 169.538 114.002 1.00 32.12  ? 388 VAL A CG2 1 
ATOM   6332 N N   . TYR B 2 398 ? 155.411 170.507 113.512 1.00 29.24  ? 389 TYR A N   1 
ATOM   6333 C CA  . TYR B 2 398 ? 154.048 170.625 113.006 1.00 23.97  ? 389 TYR A CA  1 
ATOM   6334 C C   . TYR B 2 398 ? 153.537 172.057 113.121 1.00 28.50  ? 389 TYR A C   1 
ATOM   6335 O O   . TYR B 2 398 ? 153.027 172.631 112.151 1.00 34.29  ? 389 TYR A O   1 
ATOM   6336 C CB  . TYR B 2 398 ? 153.160 169.658 113.792 1.00 27.81  ? 389 TYR A CB  1 
ATOM   6337 C CG  . TYR B 2 398 ? 151.742 169.491 113.315 1.00 25.92  ? 389 TYR A CG  1 
ATOM   6338 C CD1 . TYR B 2 398 ? 151.449 168.731 112.198 1.00 26.32  ? 389 TYR A CD1 1 
ATOM   6339 C CD2 . TYR B 2 398 ? 150.692 170.070 114.004 1.00 28.60  ? 389 TYR A CD2 1 
ATOM   6340 C CE1 . TYR B 2 398 ? 150.151 168.569 111.772 1.00 32.24  ? 389 TYR A CE1 1 
ATOM   6341 C CE2 . TYR B 2 398 ? 149.397 169.915 113.586 1.00 28.30  ? 389 TYR A CE2 1 
ATOM   6342 C CZ  . TYR B 2 398 ? 149.130 169.164 112.472 1.00 31.90  ? 389 TYR A CZ  1 
ATOM   6343 O OH  . TYR B 2 398 ? 147.831 169.010 112.058 1.00 38.69  ? 389 TYR A OH  1 
ATOM   6344 N N   . SER B 2 399 ? 153.682 172.656 114.305 1.00 28.08  ? 390 SER A N   1 
ATOM   6345 C CA  . SER B 2 399 ? 153.154 173.995 114.532 1.00 23.36  ? 390 SER A CA  1 
ATOM   6346 C C   . SER B 2 399 ? 153.985 175.044 113.813 1.00 26.82  ? 390 SER A C   1 
ATOM   6347 O O   . SER B 2 399 ? 153.458 176.085 113.423 1.00 40.34  ? 390 SER A O   1 
ATOM   6348 C CB  . SER B 2 399 ? 153.091 174.302 116.027 1.00 25.52  ? 390 SER A CB  1 
ATOM   6349 O OG  . SER B 2 399 ? 154.254 173.861 116.697 1.00 35.26  ? 390 SER A OG  1 
ATOM   6350 N N   . ALA B 2 400 ? 155.284 174.799 113.624 1.00 24.93  ? 391 ALA A N   1 
ATOM   6351 C CA  . ALA B 2 400 ? 156.081 175.714 112.814 1.00 23.38  ? 391 ALA A CA  1 
ATOM   6352 C C   . ALA B 2 400 ? 155.565 175.757 111.382 1.00 26.32  ? 391 ALA A C   1 
ATOM   6353 O O   . ALA B 2 400 ? 155.365 176.835 110.805 1.00 34.74  ? 391 ALA A O   1 
ATOM   6354 C CB  . ALA B 2 400 ? 157.550 175.298 112.848 1.00 19.81  ? 391 ALA A CB  1 
ATOM   6355 N N   . VAL B 2 401 ? 155.319 174.582 110.801 1.00 26.27  ? 392 VAL A N   1 
ATOM   6356 C CA  . VAL B 2 401 ? 154.801 174.523 109.438 1.00 24.17  ? 392 VAL A CA  1 
ATOM   6357 C C   . VAL B 2 401 ? 153.421 175.166 109.362 1.00 26.52  ? 392 VAL A C   1 
ATOM   6358 O O   . VAL B 2 401 ? 153.108 175.893 108.411 1.00 30.47  ? 392 VAL A O   1 
ATOM   6359 C CB  . VAL B 2 401 ? 154.785 173.067 108.938 1.00 22.16  ? 392 VAL A CB  1 
ATOM   6360 C CG1 . VAL B 2 401 ? 154.158 172.982 107.564 1.00 27.08  ? 392 VAL A CG1 1 
ATOM   6361 C CG2 . VAL B 2 401 ? 156.188 172.503 108.918 1.00 21.49  ? 392 VAL A CG2 1 
ATOM   6362 N N   . TYR B 2 402 ? 152.576 174.919 110.365 1.00 26.96  ? 393 TYR A N   1 
ATOM   6363 C CA  . TYR B 2 402 ? 151.222 175.464 110.331 1.00 28.11  ? 393 TYR A CA  1 
ATOM   6364 C C   . TYR B 2 402 ? 151.215 176.973 110.546 1.00 26.11  ? 393 TYR A C   1 
ATOM   6365 O O   . TYR B 2 402 ? 150.378 177.679 109.977 1.00 25.55  ? 393 TYR A O   1 
ATOM   6366 C CB  . TYR B 2 402 ? 150.351 174.769 111.373 1.00 28.46  ? 393 TYR A CB  1 
ATOM   6367 C CG  . TYR B 2 402 ? 149.329 173.839 110.772 1.00 27.16  ? 393 TYR A CG  1 
ATOM   6368 C CD1 . TYR B 2 402 ? 149.670 172.548 110.409 1.00 27.75  ? 393 TYR A CD1 1 
ATOM   6369 C CD2 . TYR B 2 402 ? 148.028 174.256 110.558 1.00 28.39  ? 393 TYR A CD2 1 
ATOM   6370 C CE1 . TYR B 2 402 ? 148.741 171.696 109.857 1.00 32.25  ? 393 TYR A CE1 1 
ATOM   6371 C CE2 . TYR B 2 402 ? 147.094 173.411 110.008 1.00 30.44  ? 393 TYR A CE2 1 
ATOM   6372 C CZ  . TYR B 2 402 ? 147.454 172.133 109.659 1.00 33.10  ? 393 TYR A CZ  1 
ATOM   6373 O OH  . TYR B 2 402 ? 146.523 171.287 109.109 1.00 44.51  ? 393 TYR A OH  1 
ATOM   6374 N N   . ALA B 2 403 ? 152.132 177.487 111.367 1.00 24.03  ? 394 ALA A N   1 
ATOM   6375 C CA  . ALA B 2 403 ? 152.260 178.928 111.535 1.00 23.16  ? 394 ALA A CA  1 
ATOM   6376 C C   . ALA B 2 403 ? 152.719 179.589 110.247 1.00 25.26  ? 394 ALA A C   1 
ATOM   6377 O O   . ALA B 2 403 ? 152.205 180.649 109.870 1.00 29.91  ? 394 ALA A O   1 
ATOM   6378 C CB  . ALA B 2 403 ? 153.230 179.239 112.672 1.00 22.68  ? 394 ALA A CB  1 
ATOM   6379 N N   . VAL B 2 404 ? 153.682 178.979 109.554 1.00 27.34  ? 395 VAL A N   1 
ATOM   6380 C CA  . VAL B 2 404 ? 154.099 179.521 108.264 1.00 24.91  ? 395 VAL A CA  1 
ATOM   6381 C C   . VAL B 2 404 ? 152.937 179.501 107.278 1.00 25.61  ? 395 VAL A C   1 
ATOM   6382 O O   . VAL B 2 404 ? 152.725 180.461 106.528 1.00 27.73  ? 395 VAL A O   1 
ATOM   6383 C CB  . VAL B 2 404 ? 155.315 178.752 107.719 1.00 25.19  ? 395 VAL A CB  1 
ATOM   6384 C CG1 . VAL B 2 404 ? 155.510 179.071 106.259 1.00 25.18  ? 395 VAL A CG1 1 
ATOM   6385 C CG2 . VAL B 2 404 ? 156.558 179.110 108.498 1.00 25.38  ? 395 VAL A CG2 1 
ATOM   6386 N N   . ALA B 2 405 ? 152.167 178.410 107.263 1.00 27.13  ? 396 ALA A N   1 
ATOM   6387 C CA  . ALA B 2 405 ? 151.038 178.314 106.343 1.00 27.16  ? 396 ALA A CA  1 
ATOM   6388 C C   . ALA B 2 405 ? 149.962 179.345 106.660 1.00 26.29  ? 396 ALA A C   1 
ATOM   6389 O O   . ALA B 2 405 ? 149.362 179.921 105.749 1.00 32.19  ? 396 ALA A O   1 
ATOM   6390 C CB  . ALA B 2 405 ? 150.451 176.908 106.377 1.00 30.80  ? 396 ALA A CB  1 
ATOM   6391 N N   . HIS B 2 406 ? 149.694 179.585 107.943 1.00 30.86  ? 397 HIS A N   1 
ATOM   6392 C CA  . HIS B 2 406 ? 148.693 180.582 108.311 1.00 32.40  ? 397 HIS A CA  1 
ATOM   6393 C C   . HIS B 2 406 ? 149.164 181.989 107.971 1.00 34.69  ? 397 HIS A C   1 
ATOM   6394 O O   . HIS B 2 406 ? 148.368 182.826 107.530 1.00 38.90  ? 397 HIS A O   1 
ATOM   6395 C CB  . HIS B 2 406 ? 148.354 180.465 109.796 1.00 30.29  ? 397 HIS A CB  1 
ATOM   6396 C CG  . HIS B 2 406 ? 147.123 179.659 110.067 1.00 37.74  ? 397 HIS A CG  1 
ATOM   6397 N ND1 . HIS B 2 406 ? 147.169 178.331 110.428 1.00 41.22  ? 397 HIS A ND1 1 
ATOM   6398 C CD2 . HIS B 2 406 ? 145.812 179.990 110.019 1.00 36.38  ? 397 HIS A CD2 1 
ATOM   6399 C CE1 . HIS B 2 406 ? 145.939 177.879 110.594 1.00 36.05  ? 397 HIS A CE1 1 
ATOM   6400 N NE2 . HIS B 2 406 ? 145.097 178.866 110.351 1.00 38.67  ? 397 HIS A NE2 1 
ATOM   6401 N N   . ALA B 2 407 ? 150.455 182.269 108.165 1.00 35.81  ? 398 ALA A N   1 
ATOM   6402 C CA  . ALA B 2 407 ? 151.003 183.556 107.754 1.00 30.20  ? 398 ALA A CA  1 
ATOM   6403 C C   . ALA B 2 407 ? 150.902 183.746 106.247 1.00 33.72  ? 398 ALA A C   1 
ATOM   6404 O O   . ALA B 2 407 ? 150.565 184.836 105.772 1.00 39.48  ? 398 ALA A O   1 
ATOM   6405 C CB  . ALA B 2 407 ? 152.453 183.671 108.208 1.00 31.21  ? 398 ALA A CB  1 
ATOM   6406 N N   . LEU B 2 408 ? 151.207 182.699 105.477 1.00 36.13  ? 399 LEU A N   1 
ATOM   6407 C CA  . LEU B 2 408 ? 151.061 182.767 104.027 1.00 35.85  ? 399 LEU A CA  1 
ATOM   6408 C C   . LEU B 2 408 ? 149.609 182.992 103.629 1.00 46.02  ? 399 LEU A C   1 
ATOM   6409 O O   . LEU B 2 408 ? 149.324 183.764 102.707 1.00 56.28  ? 399 LEU A O   1 
ATOM   6410 C CB  . LEU B 2 408 ? 151.596 181.486 103.390 1.00 33.60  ? 399 LEU A CB  1 
ATOM   6411 C CG  . LEU B 2 408 ? 151.911 181.503 101.894 1.00 37.54  ? 399 LEU A CG  1 
ATOM   6412 C CD1 . LEU B 2 408 ? 152.600 182.796 101.489 1.00 45.32  ? 399 LEU A CD1 1 
ATOM   6413 C CD2 . LEU B 2 408 ? 152.760 180.300 101.526 1.00 40.86  ? 399 LEU A CD2 1 
ATOM   6414 N N   . HIS B 2 409 ? 148.681 182.315 104.308 1.00 44.17  ? 400 HIS A N   1 
ATOM   6415 C CA  . HIS B 2 409 ? 147.261 182.485 104.022 1.00 41.78  ? 400 HIS A CA  1 
ATOM   6416 C C   . HIS B 2 409 ? 146.814 183.914 104.295 1.00 50.61  ? 400 HIS A C   1 
ATOM   6417 O O   . HIS B 2 409 ? 146.063 184.500 103.507 1.00 60.96  ? 400 HIS A O   1 
ATOM   6418 C CB  . HIS B 2 409 ? 146.457 181.487 104.857 1.00 44.04  ? 400 HIS A CB  1 
ATOM   6419 C CG  . HIS B 2 409 ? 144.974 181.623 104.719 1.00 50.16  ? 400 HIS A CG  1 
ATOM   6420 N ND1 . HIS B 2 409 ? 144.240 180.874 103.826 1.00 61.88  ? 400 HIS A ND1 1 
ATOM   6421 C CD2 . HIS B 2 409 ? 144.085 182.401 105.378 1.00 48.59  ? 400 HIS A CD2 1 
ATOM   6422 C CE1 . HIS B 2 409 ? 142.963 181.194 103.933 1.00 67.20  ? 400 HIS A CE1 1 
ATOM   6423 N NE2 . HIS B 2 409 ? 142.842 182.119 104.867 1.00 58.06  ? 400 HIS A NE2 1 
ATOM   6424 N N   . SER B 2 410 ? 147.269 184.493 105.406 1.00 50.35  ? 401 SER A N   1 
ATOM   6425 C CA  . SER B 2 410 ? 146.906 185.869 105.729 1.00 49.06  ? 401 SER A CA  1 
ATOM   6426 C C   . SER B 2 410 ? 147.534 186.856 104.753 1.00 52.55  ? 401 SER A C   1 
ATOM   6427 O O   . SER B 2 410 ? 146.912 187.861 104.394 1.00 62.03  ? 401 SER A O   1 
ATOM   6428 C CB  . SER B 2 410 ? 147.320 186.196 107.160 1.00 46.66  ? 401 SER A CB  1 
ATOM   6429 O OG  . SER B 2 410 ? 147.677 187.560 107.281 1.00 47.87  ? 401 SER A OG  1 
ATOM   6430 N N   . LEU B 2 411 ? 148.772 186.597 104.326 1.00 47.83  ? 402 LEU A N   1 
ATOM   6431 C CA  . LEU B 2 411 ? 149.437 187.498 103.389 1.00 50.18  ? 402 LEU A CA  1 
ATOM   6432 C C   . LEU B 2 411 ? 148.735 187.509 102.037 1.00 58.74  ? 402 LEU A C   1 
ATOM   6433 O O   . LEU B 2 411 ? 148.502 188.576 101.459 1.00 65.25  ? 402 LEU A O   1 
ATOM   6434 C CB  . LEU B 2 411 ? 150.901 187.095 103.229 1.00 47.94  ? 402 LEU A CB  1 
ATOM   6435 C CG  . LEU B 2 411 ? 151.849 188.146 102.658 1.00 46.75  ? 402 LEU A CG  1 
ATOM   6436 C CD1 . LEU B 2 411 ? 152.392 189.027 103.759 1.00 41.97  ? 402 LEU A CD1 1 
ATOM   6437 C CD2 . LEU B 2 411 ? 152.979 187.475 101.912 1.00 53.62  ? 402 LEU A CD2 1 
ATOM   6438 N N   . LEU B 2 412 ? 148.391 186.330 101.517 1.00 60.06  ? 403 LEU A N   1 
ATOM   6439 C CA  . LEU B 2 412 ? 147.684 186.249 100.245 1.00 63.18  ? 403 LEU A CA  1 
ATOM   6440 C C   . LEU B 2 412 ? 146.268 186.803 100.334 1.00 72.35  ? 403 LEU A C   1 
ATOM   6441 O O   . LEU B 2 412 ? 145.702 187.189 99.306  1.00 79.47  ? 403 LEU A O   1 
ATOM   6442 C CB  . LEU B 2 412 ? 147.655 184.801 99.754  1.00 65.33  ? 403 LEU A CB  1 
ATOM   6443 C CG  . LEU B 2 412 ? 148.980 184.177 99.312  1.00 58.31  ? 403 LEU A CG  1 
ATOM   6444 C CD1 . LEU B 2 412 ? 148.743 183.193 98.187  1.00 74.33  ? 403 LEU A CD1 1 
ATOM   6445 C CD2 . LEU B 2 412 ? 149.966 185.241 98.873  1.00 59.22  ? 403 LEU A CD2 1 
ATOM   6446 N N   . GLY B 2 413 ? 145.687 186.846 101.528 1.00 72.43  ? 404 GLY A N   1 
ATOM   6447 C CA  . GLY B 2 413 ? 144.375 187.450 101.710 1.00 79.66  ? 404 GLY A CA  1 
ATOM   6448 C C   . GLY B 2 413 ? 143.235 186.722 101.032 1.00 87.35  ? 404 GLY A C   1 
ATOM   6449 O O   . GLY B 2 413 ? 142.380 187.361 100.406 1.00 93.36  ? 404 GLY A O   1 
ATOM   6450 N N   . CYS B 2 414 ? 143.198 185.398 101.142 1.00 82.78  ? 405 CYS A N   1 
ATOM   6451 C CA  . CYS B 2 414 ? 142.120 184.597 100.585 1.00 95.44  ? 405 CYS A CA  1 
ATOM   6452 C C   . CYS B 2 414 ? 141.337 183.936 101.711 1.00 97.16  ? 405 CYS A C   1 
ATOM   6453 O O   . CYS B 2 414 ? 141.814 183.841 102.845 1.00 92.55  ? 405 CYS A O   1 
ATOM   6454 C CB  . CYS B 2 414 ? 142.655 183.536 99.614  1.00 102.67 ? 405 CYS A CB  1 
ATOM   6455 S SG  . CYS B 2 414 ? 144.267 182.840 100.046 1.00 91.50  ? 405 CYS A SG  1 
ATOM   6456 N N   . ASP B 2 415 ? 140.121 183.488 101.395 1.00 101.90 ? 406 ASP A N   1 
ATOM   6457 C CA  . ASP B 2 415 ? 139.237 182.877 102.389 1.00 102.94 ? 406 ASP A CA  1 
ATOM   6458 C C   . ASP B 2 415 ? 138.314 181.876 101.699 1.00 104.11 ? 406 ASP A C   1 
ATOM   6459 O O   . ASP B 2 415 ? 137.360 182.265 101.018 1.00 102.58 ? 406 ASP A O   1 
ATOM   6460 C CB  . ASP B 2 415 ? 138.440 183.935 103.148 1.00 106.32 ? 406 ASP A CB  1 
ATOM   6461 C CG  . ASP B 2 415 ? 137.990 185.091 102.267 1.00 108.11 ? 406 ASP A CG  1 
ATOM   6462 O OD1 . ASP B 2 415 ? 137.775 184.896 101.052 1.00 110.77 ? 406 ASP A OD1 1 
ATOM   6463 O OD2 . ASP B 2 415 ? 137.837 186.208 102.803 1.00 103.69 ? 406 ASP A OD2 1 
ATOM   6464 N N   . LYS B 2 416 ? 138.604 180.588 101.880 1.00 105.24 ? 407 LYS A N   1 
ATOM   6465 C CA  . LYS B 2 416 ? 137.756 179.486 101.425 1.00 107.35 ? 407 LYS A CA  1 
ATOM   6466 C C   . LYS B 2 416 ? 137.520 179.503 99.917  1.00 107.73 ? 407 LYS A C   1 
ATOM   6467 O O   . LYS B 2 416 ? 136.538 178.931 99.434  1.00 106.21 ? 407 LYS A O   1 
ATOM   6468 C CB  . LYS B 2 416 ? 136.409 179.477 102.161 1.00 108.41 ? 407 LYS A CB  1 
ATOM   6469 C CG  . LYS B 2 416 ? 136.487 179.738 103.661 1.00 103.98 ? 407 LYS A CG  1 
ATOM   6470 C CD  . LYS B 2 416 ? 137.529 178.870 104.344 1.00 103.14 ? 407 LYS A CD  1 
ATOM   6471 C CE  . LYS B 2 416 ? 138.229 179.638 105.453 1.00 99.33  ? 407 LYS A CE  1 
ATOM   6472 N NZ  . LYS B 2 416 ? 139.459 178.946 105.928 1.00 94.48  ? 407 LYS A NZ  1 
ATOM   6473 N N   . SER B 2 417 ? 138.402 180.145 99.159  1.00 110.14 ? 408 SER A N   1 
ATOM   6474 C CA  . SER B 2 417 ? 138.285 180.200 97.708  1.00 110.83 ? 408 SER A CA  1 
ATOM   6475 C C   . SER B 2 417 ? 139.680 180.407 97.128  1.00 113.38 ? 408 SER A C   1 
ATOM   6476 O O   . SER B 2 417 ? 140.651 180.597 97.865  1.00 108.39 ? 408 SER A O   1 
ATOM   6477 C CB  . SER B 2 417 ? 137.306 181.302 97.284  1.00 108.39 ? 408 SER A CB  1 
ATOM   6478 O OG  . SER B 2 417 ? 137.903 182.581 97.392  1.00 108.58 ? 408 SER A OG  1 
ATOM   6479 N N   . THR B 2 418 ? 139.776 180.380 95.800  1.00 117.47 ? 409 THR A N   1 
ATOM   6480 C CA  . THR B 2 418 ? 141.072 180.474 95.141  1.00 117.38 ? 409 THR A CA  1 
ATOM   6481 C C   . THR B 2 418 ? 141.793 181.755 95.543  1.00 118.27 ? 409 THR A C   1 
ATOM   6482 O O   . THR B 2 418 ? 141.194 182.832 95.614  1.00 115.54 ? 409 THR A O   1 
ATOM   6483 C CB  . THR B 2 418 ? 140.901 180.419 93.622  1.00 117.61 ? 409 THR A CB  1 
ATOM   6484 O OG1 . THR B 2 418 ? 140.379 181.668 93.149  1.00 117.63 ? 409 THR A OG1 1 
ATOM   6485 C CG2 . THR B 2 418 ? 139.950 179.296 93.233  1.00 112.01 ? 409 THR A CG2 1 
ATOM   6486 N N   . CYS B 2 419 ? 143.088 181.630 95.814  1.00 115.34 ? 410 CYS A N   1 
ATOM   6487 C CA  . CYS B 2 419 ? 143.891 182.744 96.294  1.00 109.36 ? 410 CYS A CA  1 
ATOM   6488 C C   . CYS B 2 419 ? 144.424 183.567 95.126  1.00 105.42 ? 410 CYS A C   1 
ATOM   6489 O O   . CYS B 2 419 ? 144.292 183.197 93.957  1.00 104.33 ? 410 CYS A O   1 
ATOM   6490 C CB  . CYS B 2 419 ? 145.052 182.245 97.157  1.00 104.64 ? 410 CYS A CB  1 
ATOM   6491 S SG  . CYS B 2 419 ? 144.555 181.375 98.668  1.00 120.50 ? 410 CYS A SG  1 
ATOM   6492 N N   . THR B 2 420 ? 145.034 184.705 95.466  1.00 101.17 ? 411 THR A N   1 
ATOM   6493 C CA  . THR B 2 420 ? 145.511 185.640 94.453  1.00 100.25 ? 411 THR A CA  1 
ATOM   6494 C C   . THR B 2 420 ? 146.769 185.156 93.740  1.00 97.88  ? 411 THR A C   1 
ATOM   6495 O O   . THR B 2 420 ? 147.037 185.610 92.622  1.00 94.78  ? 411 THR A O   1 
ATOM   6496 C CB  . THR B 2 420 ? 145.770 187.005 95.088  1.00 94.57  ? 411 THR A CB  1 
ATOM   6497 O OG1 . THR B 2 420 ? 147.055 186.999 95.716  1.00 89.10  ? 411 THR A OG1 1 
ATOM   6498 C CG2 . THR B 2 420 ? 144.706 187.320 96.127  1.00 87.57  ? 411 THR A CG2 1 
ATOM   6499 N N   . LYS B 2 421 ? 147.540 184.256 94.356  1.00 97.10  ? 412 LYS A N   1 
ATOM   6500 C CA  . LYS B 2 421 ? 148.760 183.708 93.752  1.00 97.00  ? 412 LYS A CA  1 
ATOM   6501 C C   . LYS B 2 421 ? 149.747 184.810 93.370  1.00 97.10  ? 412 LYS A C   1 
ATOM   6502 O O   . LYS B 2 421 ? 150.398 184.747 92.326  1.00 96.19  ? 412 LYS A O   1 
ATOM   6503 C CB  . LYS B 2 421 ? 148.440 182.835 92.534  1.00 100.34 ? 412 LYS A CB  1 
ATOM   6504 C CG  . LYS B 2 421 ? 147.250 181.903 92.692  1.00 101.82 ? 412 LYS A CG  1 
ATOM   6505 C CD  . LYS B 2 421 ? 147.467 180.916 93.819  1.00 103.27 ? 412 LYS A CD  1 
ATOM   6506 C CE  . LYS B 2 421 ? 146.607 179.676 93.634  1.00 102.56 ? 412 LYS A CE  1 
ATOM   6507 N NZ  . LYS B 2 421 ? 145.205 180.012 93.264  1.00 106.31 ? 412 LYS A NZ  1 
ATOM   6508 N N   . ARG B 2 422 ? 149.859 185.831 94.214  1.00 92.76  ? 413 ARG A N   1 
ATOM   6509 C CA  . ARG B 2 422 ? 150.790 186.914 93.941  1.00 82.60  ? 413 ARG A CA  1 
ATOM   6510 C C   . ARG B 2 422 ? 152.211 186.504 94.311  1.00 79.55  ? 413 ARG A C   1 
ATOM   6511 O O   . ARG B 2 422 ? 152.447 185.455 94.914  1.00 76.35  ? 413 ARG A O   1 
ATOM   6512 C CB  . ARG B 2 422 ? 150.406 188.176 94.710  1.00 74.26  ? 413 ARG A CB  1 
ATOM   6513 C CG  . ARG B 2 422 ? 149.977 187.922 96.138  1.00 75.73  ? 413 ARG A CG  1 
ATOM   6514 C CD  . ARG B 2 422 ? 149.901 189.216 96.920  1.00 73.63  ? 413 ARG A CD  1 
ATOM   6515 N NE  . ARG B 2 422 ? 151.177 189.563 97.532  1.00 75.00  ? 413 ARG A NE  1 
ATOM   6516 C CZ  . ARG B 2 422 ? 151.307 190.039 98.761  1.00 73.22  ? 413 ARG A CZ  1 
ATOM   6517 N NH1 . ARG B 2 422 ? 150.258 190.235 99.541  1.00 70.98  ? 413 ARG A NH1 1 
ATOM   6518 N NH2 . ARG B 2 422 ? 152.520 190.328 99.219  1.00 66.44  ? 413 ARG A NH2 1 
ATOM   6519 N N   . VAL B 2 423 ? 153.168 187.351 93.934  1.00 79.84  ? 414 VAL A N   1 
ATOM   6520 C CA  . VAL B 2 423 ? 154.556 187.105 94.299  1.00 81.22  ? 414 VAL A CA  1 
ATOM   6521 C C   . VAL B 2 423 ? 154.785 187.549 95.738  1.00 80.91  ? 414 VAL A C   1 
ATOM   6522 O O   . VAL B 2 423 ? 154.212 188.544 96.203  1.00 78.28  ? 414 VAL A O   1 
ATOM   6523 C CB  . VAL B 2 423 ? 155.506 187.814 93.318  1.00 79.81  ? 414 VAL A CB  1 
ATOM   6524 C CG1 . VAL B 2 423 ? 155.485 189.322 93.523  1.00 78.95  ? 414 VAL A CG1 1 
ATOM   6525 C CG2 . VAL B 2 423 ? 156.910 187.267 93.462  1.00 76.24  ? 414 VAL A CG2 1 
ATOM   6526 N N   . VAL B 2 424 ? 155.608 186.796 96.462  1.00 75.89  ? 415 VAL A N   1 
ATOM   6527 C CA  . VAL B 2 424 ? 155.795 186.983 97.895  1.00 64.75  ? 415 VAL A CA  1 
ATOM   6528 C C   . VAL B 2 424 ? 157.284 187.145 98.164  1.00 58.86  ? 415 VAL A C   1 
ATOM   6529 O O   . VAL B 2 424 ? 158.096 186.322 97.725  1.00 59.17  ? 415 VAL A O   1 
ATOM   6530 C CB  . VAL B 2 424 ? 155.215 185.815 98.705  1.00 60.19  ? 415 VAL A CB  1 
ATOM   6531 C CG1 . VAL B 2 424 ? 155.730 185.848 100.132 1.00 48.86  ? 415 VAL A CG1 1 
ATOM   6532 C CG2 . VAL B 2 424 ? 153.697 185.861 98.683  1.00 63.40  ? 415 VAL A CG2 1 
ATOM   6533 N N   . TYR B 2 425 ? 157.641 188.203 98.882  1.00 54.59  ? 416 TYR A N   1 
ATOM   6534 C CA  . TYR B 2 425 ? 158.999 188.398 99.355  1.00 47.75  ? 416 TYR A CA  1 
ATOM   6535 C C   . TYR B 2 425 ? 159.120 187.904 100.793 1.00 47.09  ? 416 TYR A C   1 
ATOM   6536 O O   . TYR B 2 425 ? 158.242 188.164 101.618 1.00 47.01  ? 416 TYR A O   1 
ATOM   6537 C CB  . TYR B 2 425 ? 159.384 189.870 99.277  1.00 50.76  ? 416 TYR A CB  1 
ATOM   6538 C CG  . TYR B 2 425 ? 159.225 190.464 97.899  1.00 58.71  ? 416 TYR A CG  1 
ATOM   6539 C CD1 . TYR B 2 425 ? 159.790 189.851 96.791  1.00 60.94  ? 416 TYR A CD1 1 
ATOM   6540 C CD2 . TYR B 2 425 ? 158.493 191.624 97.703  1.00 56.15  ? 416 TYR A CD2 1 
ATOM   6541 C CE1 . TYR B 2 425 ? 159.641 190.384 95.529  1.00 61.62  ? 416 TYR A CE1 1 
ATOM   6542 C CE2 . TYR B 2 425 ? 158.337 192.164 96.445  1.00 59.47  ? 416 TYR A CE2 1 
ATOM   6543 C CZ  . TYR B 2 425 ? 158.913 191.540 95.362  1.00 63.83  ? 416 TYR A CZ  1 
ATOM   6544 O OH  . TYR B 2 425 ? 158.763 192.075 94.105  1.00 71.20  ? 416 TYR A OH  1 
ATOM   6545 N N   . PRO B 2 426 ? 160.195 187.183 101.116 1.00 46.72  ? 417 PRO A N   1 
ATOM   6546 C CA  . PRO B 2 426 ? 160.284 186.571 102.454 1.00 40.56  ? 417 PRO A CA  1 
ATOM   6547 C C   . PRO B 2 426 ? 160.216 187.565 103.602 1.00 36.62  ? 417 PRO A C   1 
ATOM   6548 O O   . PRO B 2 426 ? 159.755 187.201 104.690 1.00 39.65  ? 417 PRO A O   1 
ATOM   6549 C CB  . PRO B 2 426 ? 161.630 185.831 102.408 1.00 37.08  ? 417 PRO A CB  1 
ATOM   6550 C CG  . PRO B 2 426 ? 162.366 186.408 101.243 1.00 39.23  ? 417 PRO A CG  1 
ATOM   6551 C CD  . PRO B 2 426 ? 161.322 186.793 100.256 1.00 44.59  ? 417 PRO A CD  1 
ATOM   6552 N N   . TRP B 2 427 ? 160.656 188.810 103.405 1.00 42.98  ? 418 TRP A N   1 
ATOM   6553 C CA  . TRP B 2 427 ? 160.509 189.803 104.466 1.00 43.65  ? 418 TRP A CA  1 
ATOM   6554 C C   . TRP B 2 427 ? 159.045 190.130 104.731 1.00 43.98  ? 418 TRP A C   1 
ATOM   6555 O O   . TRP B 2 427 ? 158.666 190.377 105.881 1.00 45.86  ? 418 TRP A O   1 
ATOM   6556 C CB  . TRP B 2 427 ? 161.307 191.065 104.129 1.00 44.03  ? 418 TRP A CB  1 
ATOM   6557 C CG  . TRP B 2 427 ? 160.774 191.858 102.978 1.00 46.01  ? 418 TRP A CG  1 
ATOM   6558 C CD1 . TRP B 2 427 ? 161.113 191.718 101.667 1.00 48.60  ? 418 TRP A CD1 1 
ATOM   6559 C CD2 . TRP B 2 427 ? 159.812 192.916 103.032 1.00 52.01  ? 418 TRP A CD2 1 
ATOM   6560 N NE1 . TRP B 2 427 ? 160.420 192.618 100.900 1.00 51.48  ? 418 TRP A NE1 1 
ATOM   6561 C CE2 . TRP B 2 427 ? 159.614 193.366 101.715 1.00 53.44  ? 418 TRP A CE2 1 
ATOM   6562 C CE3 . TRP B 2 427 ? 159.096 193.523 104.066 1.00 58.13  ? 418 TRP A CE3 1 
ATOM   6563 C CZ2 . TRP B 2 427 ? 158.731 194.394 101.404 1.00 54.03  ? 418 TRP A CZ2 1 
ATOM   6564 C CZ3 . TRP B 2 427 ? 158.221 194.542 103.756 1.00 57.99  ? 418 TRP A CZ3 1 
ATOM   6565 C CH2 . TRP B 2 427 ? 158.045 194.968 102.436 1.00 53.85  ? 418 TRP A CH2 1 
ATOM   6566 N N   . GLN B 2 428 ? 158.206 190.117 103.694 1.00 43.70  ? 419 GLN A N   1 
ATOM   6567 C CA  . GLN B 2 428 ? 156.772 190.309 103.894 1.00 41.04  ? 419 GLN A CA  1 
ATOM   6568 C C   . GLN B 2 428 ? 156.166 189.168 104.701 1.00 38.12  ? 419 GLN A C   1 
ATOM   6569 O O   . GLN B 2 428 ? 155.334 189.396 105.590 1.00 44.94  ? 419 GLN A O   1 
ATOM   6570 C CB  . GLN B 2 428 ? 156.076 190.437 102.541 1.00 45.86  ? 419 GLN A CB  1 
ATOM   6571 C CG  . GLN B 2 428 ? 156.390 191.719 101.808 1.00 53.48  ? 419 GLN A CG  1 
ATOM   6572 C CD  . GLN B 2 428 ? 155.733 191.784 100.452 1.00 60.08  ? 419 GLN A CD  1 
ATOM   6573 O OE1 . GLN B 2 428 ? 155.201 190.793 99.963  1.00 60.21  ? 419 GLN A OE1 1 
ATOM   6574 N NE2 . GLN B 2 428 ? 155.762 192.958 99.836  1.00 60.78  ? 419 GLN A NE2 1 
ATOM   6575 N N   . LEU B 2 429 ? 156.563 187.931 104.403 1.00 39.80  ? 420 LEU A N   1 
ATOM   6576 C CA  . LEU B 2 429 ? 156.059 186.794 105.164 1.00 39.66  ? 420 LEU A CA  1 
ATOM   6577 C C   . LEU B 2 429 ? 156.546 186.844 106.605 1.00 35.71  ? 420 LEU A C   1 
ATOM   6578 O O   . LEU B 2 429 ? 155.811 186.484 107.529 1.00 39.24  ? 420 LEU A O   1 
ATOM   6579 C CB  . LEU B 2 429 ? 156.474 185.485 104.498 1.00 37.69  ? 420 LEU A CB  1 
ATOM   6580 C CG  . LEU B 2 429 ? 155.846 184.230 105.106 1.00 40.74  ? 420 LEU A CG  1 
ATOM   6581 C CD1 . LEU B 2 429 ? 154.376 184.174 104.761 1.00 37.56  ? 420 LEU A CD1 1 
ATOM   6582 C CD2 . LEU B 2 429 ? 156.552 182.979 104.632 1.00 38.91  ? 420 LEU A CD2 1 
ATOM   6583 N N   . LEU B 2 430 ? 157.786 187.286 106.818 1.00 32.71  ? 421 LEU A N   1 
ATOM   6584 C CA  . LEU B 2 430 ? 158.273 187.466 108.180 1.00 31.84  ? 421 LEU A CA  1 
ATOM   6585 C C   . LEU B 2 430 ? 157.474 188.536 108.911 1.00 35.17  ? 421 LEU A C   1 
ATOM   6586 O O   . LEU B 2 430 ? 157.186 188.400 110.104 1.00 33.83  ? 421 LEU A O   1 
ATOM   6587 C CB  . LEU B 2 430 ? 159.758 187.815 108.170 1.00 32.41  ? 421 LEU A CB  1 
ATOM   6588 C CG  . LEU B 2 430 ? 160.317 188.219 109.531 1.00 29.41  ? 421 LEU A CG  1 
ATOM   6589 C CD1 . LEU B 2 430 ? 160.490 186.992 110.402 1.00 33.89  ? 421 LEU A CD1 1 
ATOM   6590 C CD2 . LEU B 2 430 ? 161.625 188.960 109.378 1.00 29.32  ? 421 LEU A CD2 1 
ATOM   6591 N N   . GLU B 2 431 ? 157.118 189.615 108.214 1.00 41.06  ? 422 GLU A N   1 
ATOM   6592 C CA  . GLU B 2 431 ? 156.280 190.645 108.818 1.00 40.27  ? 422 GLU A CA  1 
ATOM   6593 C C   . GLU B 2 431 ? 154.925 190.082 109.225 1.00 43.09  ? 422 GLU A C   1 
ATOM   6594 O O   . GLU B 2 431 ? 154.437 190.349 110.329 1.00 44.80  ? 422 GLU A O   1 
ATOM   6595 C CB  . GLU B 2 431 ? 156.108 191.803 107.837 1.00 45.66  ? 422 GLU A CB  1 
ATOM   6596 C CG  . GLU B 2 431 ? 155.744 193.130 108.470 1.00 59.62  ? 422 GLU A CG  1 
ATOM   6597 C CD  . GLU B 2 431 ? 156.032 194.301 107.553 1.00 74.85  ? 422 GLU A CD  1 
ATOM   6598 O OE1 . GLU B 2 431 ? 155.680 194.223 106.358 1.00 73.50  ? 422 GLU A OE1 1 
ATOM   6599 O OE2 . GLU B 2 431 ? 156.606 195.302 108.029 1.00 77.25  ? 422 GLU A OE2 1 
ATOM   6600 N N   . GLU B 2 432 ? 154.308 189.291 108.349 1.00 41.43  ? 423 GLU A N   1 
ATOM   6601 C CA  . GLU B 2 432 ? 152.982 188.742 108.608 1.00 35.08  ? 423 GLU A CA  1 
ATOM   6602 C C   . GLU B 2 432 ? 152.977 187.594 109.610 1.00 38.37  ? 423 GLU A C   1 
ATOM   6603 O O   . GLU B 2 432 ? 151.927 187.322 110.200 1.00 43.88  ? 423 GLU A O   1 
ATOM   6604 C CB  . GLU B 2 432 ? 152.350 188.266 107.301 1.00 38.79  ? 423 GLU A CB  1 
ATOM   6605 C CG  . GLU B 2 432 ? 150.836 188.374 107.253 1.00 45.27  ? 423 GLU A CG  1 
ATOM   6606 C CD  . GLU B 2 432 ? 150.333 189.779 107.511 1.00 52.61  ? 423 GLU A CD  1 
ATOM   6607 O OE1 . GLU B 2 432 ? 149.801 190.027 108.610 1.00 62.43  ? 423 GLU A OE1 1 
ATOM   6608 O OE2 . GLU B 2 432 ? 150.468 190.636 106.614 1.00 48.12  ? 423 GLU A OE2 1 
ATOM   6609 N N   . ILE B 2 433 ? 154.105 186.913 109.815 1.00 38.91  ? 424 ILE A N   1 
ATOM   6610 C CA  . ILE B 2 433 ? 154.099 185.712 110.643 1.00 31.22  ? 424 ILE A CA  1 
ATOM   6611 C C   . ILE B 2 433 ? 154.202 186.025 112.131 1.00 31.23  ? 424 ILE A C   1 
ATOM   6612 O O   . ILE B 2 433 ? 153.826 185.187 112.958 1.00 32.93  ? 424 ILE A O   1 
ATOM   6613 C CB  . ILE B 2 433 ? 155.230 184.768 110.203 1.00 34.08  ? 424 ILE A CB  1 
ATOM   6614 C CG1 . ILE B 2 433 ? 155.097 183.402 110.871 1.00 33.98  ? 424 ILE A CG1 1 
ATOM   6615 C CG2 . ILE B 2 433 ? 156.568 185.352 110.560 1.00 37.01  ? 424 ILE A CG2 1 
ATOM   6616 C CD1 . ILE B 2 433 ? 156.307 182.546 110.713 1.00 28.99  ? 424 ILE A CD1 1 
ATOM   6617 N N   . TRP B 2 434 ? 154.691 187.208 112.505 1.00 36.11  ? 425 TRP A N   1 
ATOM   6618 C CA  . TRP B 2 434 ? 154.679 187.591 113.911 1.00 33.26  ? 425 TRP A CA  1 
ATOM   6619 C C   . TRP B 2 434 ? 153.268 187.715 114.468 1.00 39.38  ? 425 TRP A C   1 
ATOM   6620 O O   . TRP B 2 434 ? 153.086 187.604 115.684 1.00 44.88  ? 425 TRP A O   1 
ATOM   6621 C CB  . TRP B 2 434 ? 155.419 188.911 114.117 1.00 33.92  ? 425 TRP A CB  1 
ATOM   6622 C CG  . TRP B 2 434 ? 156.899 188.824 113.992 1.00 34.46  ? 425 TRP A CG  1 
ATOM   6623 C CD1 . TRP B 2 434 ? 157.643 189.053 112.880 1.00 37.15  ? 425 TRP A CD1 1 
ATOM   6624 C CD2 . TRP B 2 434 ? 157.826 188.515 115.037 1.00 37.58  ? 425 TRP A CD2 1 
ATOM   6625 N NE1 . TRP B 2 434 ? 158.977 188.889 113.158 1.00 40.58  ? 425 TRP A NE1 1 
ATOM   6626 C CE2 . TRP B 2 434 ? 159.115 188.560 114.479 1.00 37.68  ? 425 TRP A CE2 1 
ATOM   6627 C CE3 . TRP B 2 434 ? 157.688 188.200 116.391 1.00 40.19  ? 425 TRP A CE3 1 
ATOM   6628 C CZ2 . TRP B 2 434 ? 160.258 188.299 115.223 1.00 42.81  ? 425 TRP A CZ2 1 
ATOM   6629 C CZ3 . TRP B 2 434 ? 158.819 187.945 117.127 1.00 45.76  ? 425 TRP A CZ3 1 
ATOM   6630 C CH2 . TRP B 2 434 ? 160.089 187.993 116.544 1.00 47.28  ? 425 TRP A CH2 1 
ATOM   6631 N N   . LYS B 2 435 ? 152.272 187.942 113.617 1.00 37.93  ? 426 LYS A N   1 
ATOM   6632 C CA  . LYS B 2 435 ? 150.915 188.215 114.063 1.00 40.02  ? 426 LYS A CA  1 
ATOM   6633 C C   . LYS B 2 435 ? 149.983 187.018 113.924 1.00 41.57  ? 426 LYS A C   1 
ATOM   6634 O O   . LYS B 2 435 ? 148.764 187.187 114.023 1.00 40.58  ? 426 LYS A O   1 
ATOM   6635 C CB  . LYS B 2 435 ? 150.343 189.413 113.302 1.00 45.14  ? 426 LYS A CB  1 
ATOM   6636 C CG  . LYS B 2 435 ? 151.163 190.683 113.445 1.00 43.04  ? 426 LYS A CG  1 
ATOM   6637 C CD  . LYS B 2 435 ? 151.689 191.173 112.112 1.00 46.03  ? 426 LYS A CD  1 
ATOM   6638 C CE  . LYS B 2 435 ? 150.631 191.970 111.373 1.00 43.50  ? 426 LYS A CE  1 
ATOM   6639 N NZ  . LYS B 2 435 ? 150.995 192.207 109.953 1.00 42.95  ? 426 LYS A NZ  1 
ATOM   6640 N N   . VAL B 2 436 ? 150.518 185.818 113.696 1.00 43.23  ? 427 VAL A N   1 
ATOM   6641 C CA  . VAL B 2 436 ? 149.669 184.637 113.617 1.00 36.79  ? 427 VAL A CA  1 
ATOM   6642 C C   . VAL B 2 436 ? 149.122 184.314 115.000 1.00 41.63  ? 427 VAL A C   1 
ATOM   6643 O O   . VAL B 2 436 ? 149.821 184.438 116.014 1.00 43.02  ? 427 VAL A O   1 
ATOM   6644 C CB  . VAL B 2 436 ? 150.434 183.438 113.028 1.00 30.59  ? 427 VAL A CB  1 
ATOM   6645 C CG1 . VAL B 2 436 ? 150.840 183.720 111.597 1.00 34.33  ? 427 VAL A CG1 1 
ATOM   6646 C CG2 . VAL B 2 436 ? 151.643 183.088 113.876 1.00 29.05  ? 427 VAL A CG2 1 
ATOM   6647 N N   . ASN B 2 437 ? 147.853 183.916 115.048 1.00 40.26  ? 428 ASN A N   1 
ATOM   6648 C CA  . ASN B 2 437 ? 147.231 183.512 116.305 1.00 38.55  ? 428 ASN A CA  1 
ATOM   6649 C C   . ASN B 2 437 ? 146.087 182.570 115.958 1.00 39.40  ? 428 ASN A C   1 
ATOM   6650 O O   . ASN B 2 437 ? 145.004 183.027 115.583 1.00 39.14  ? 428 ASN A O   1 
ATOM   6651 C CB  . ASN B 2 437 ? 146.742 184.726 117.082 1.00 39.57  ? 428 ASN A CB  1 
ATOM   6652 C CG  . ASN B 2 437 ? 146.221 184.369 118.453 1.00 47.37  ? 428 ASN A CG  1 
ATOM   6653 O OD1 . ASN B 2 437 ? 146.704 183.436 119.088 1.00 54.98  ? 428 ASN A OD1 1 
ATOM   6654 N ND2 . ASN B 2 437 ? 145.229 185.111 118.919 1.00 54.14  ? 428 ASN A ND2 1 
ATOM   6655 N N   . PHE B 2 438 ? 146.325 181.267 116.085 1.00 41.34  ? 429 PHE A N   1 
ATOM   6656 C CA  . PHE B 2 438 ? 145.353 180.269 115.664 1.00 41.16  ? 429 PHE A CA  1 
ATOM   6657 C C   . PHE B 2 438 ? 145.386 179.107 116.646 1.00 40.64  ? 429 PHE A C   1 
ATOM   6658 O O   . PHE B 2 438 ? 146.329 178.951 117.424 1.00 38.57  ? 429 PHE A O   1 
ATOM   6659 C CB  . PHE B 2 438 ? 145.628 179.793 114.234 1.00 38.61  ? 429 PHE A CB  1 
ATOM   6660 C CG  . PHE B 2 438 ? 146.991 179.191 114.045 1.00 36.42  ? 429 PHE A CG  1 
ATOM   6661 C CD1 . PHE B 2 438 ? 148.092 179.994 113.819 1.00 33.73  ? 429 PHE A CD1 1 
ATOM   6662 C CD2 . PHE B 2 438 ? 147.170 177.821 114.100 1.00 36.52  ? 429 PHE A CD2 1 
ATOM   6663 C CE1 . PHE B 2 438 ? 149.338 179.445 113.652 1.00 31.04  ? 429 PHE A CE1 1 
ATOM   6664 C CE2 . PHE B 2 438 ? 148.416 177.270 113.933 1.00 35.05  ? 429 PHE A CE2 1 
ATOM   6665 C CZ  . PHE B 2 438 ? 149.500 178.083 113.709 1.00 33.00  ? 429 PHE A CZ  1 
ATOM   6666 N N   . THR B 2 439 ? 144.334 178.295 116.604 1.00 37.62  ? 430 THR A N   1 
ATOM   6667 C CA  . THR B 2 439 ? 144.205 177.123 117.460 1.00 38.16  ? 430 THR A CA  1 
ATOM   6668 C C   . THR B 2 439 ? 144.617 175.887 116.671 1.00 40.99  ? 430 THR A C   1 
ATOM   6669 O O   . THR B 2 439 ? 144.014 175.575 115.639 1.00 49.26  ? 430 THR A O   1 
ATOM   6670 C CB  . THR B 2 439 ? 142.774 176.979 117.975 1.00 41.40  ? 430 THR A CB  1 
ATOM   6671 O OG1 . THR B 2 439 ? 142.539 177.939 119.011 1.00 49.12  ? 430 THR A OG1 1 
ATOM   6672 C CG2 . THR B 2 439 ? 142.546 175.588 118.534 1.00 44.22  ? 430 THR A CG2 1 
ATOM   6673 N N   . LEU B 2 440 ? 145.643 175.192 117.151 1.00 35.78  ? 431 LEU A N   1 
ATOM   6674 C CA  . LEU B 2 440 ? 146.150 173.983 116.514 1.00 35.96  ? 431 LEU A CA  1 
ATOM   6675 C C   . LEU B 2 440 ? 146.174 172.870 117.550 1.00 41.38  ? 431 LEU A C   1 
ATOM   6676 O O   . LEU B 2 440 ? 146.969 172.916 118.493 1.00 48.04  ? 431 LEU A O   1 
ATOM   6677 C CB  . LEU B 2 440 ? 147.542 174.215 115.931 1.00 36.67  ? 431 LEU A CB  1 
ATOM   6678 C CG  . LEU B 2 440 ? 148.118 173.067 115.107 1.00 31.97  ? 431 LEU A CG  1 
ATOM   6679 C CD1 . LEU B 2 440 ? 147.248 172.819 113.896 1.00 28.94  ? 431 LEU A CD1 1 
ATOM   6680 C CD2 . LEU B 2 440 ? 149.539 173.376 114.694 1.00 30.42  ? 431 LEU A CD2 1 
ATOM   6681 N N   . LEU B 2 441 ? 145.314 171.870 117.365 1.00 39.35  ? 432 LEU A N   1 
ATOM   6682 C CA  . LEU B 2 441 ? 145.217 170.728 118.272 1.00 36.58  ? 432 LEU A CA  1 
ATOM   6683 C C   . LEU B 2 441 ? 144.976 171.187 119.709 1.00 45.61  ? 432 LEU A C   1 
ATOM   6684 O O   . LEU B 2 441 ? 145.608 170.712 120.654 1.00 53.01  ? 432 LEU A O   1 
ATOM   6685 C CB  . LEU B 2 441 ? 146.462 169.845 118.177 1.00 39.77  ? 432 LEU A CB  1 
ATOM   6686 C CG  . LEU B 2 441 ? 146.772 169.237 116.807 1.00 39.96  ? 432 LEU A CG  1 
ATOM   6687 C CD1 . LEU B 2 441 ? 148.085 168.476 116.840 1.00 37.65  ? 432 LEU A CD1 1 
ATOM   6688 C CD2 . LEU B 2 441 ? 145.643 168.341 116.343 1.00 33.51  ? 432 LEU A CD2 1 
ATOM   6689 N N   . ASP B 2 442 ? 144.050 172.137 119.858 1.00 46.57  ? 433 ASP A N   1 
ATOM   6690 C CA  . ASP B 2 442 ? 143.626 172.660 121.161 1.00 43.41  ? 433 ASP A CA  1 
ATOM   6691 C C   . ASP B 2 442 ? 144.766 173.357 121.899 1.00 41.00  ? 433 ASP A C   1 
ATOM   6692 O O   . ASP B 2 442 ? 144.802 173.394 123.129 1.00 50.76  ? 433 ASP A O   1 
ATOM   6693 C CB  . ASP B 2 442 ? 143.010 171.563 122.033 1.00 50.32  ? 433 ASP A CB  1 
ATOM   6694 C CG  . ASP B 2 442 ? 141.916 170.798 121.319 1.00 59.69  ? 433 ASP A CG  1 
ATOM   6695 O OD1 . ASP B 2 442 ? 140.759 171.266 121.331 1.00 60.07  ? 433 ASP A OD1 1 
ATOM   6696 O OD2 . ASP B 2 442 ? 142.211 169.727 120.748 1.00 58.06  ? 433 ASP A OD2 1 
ATOM   6697 N N   . HIS B 2 443 ? 145.708 173.915 121.145 1.00 40.87  ? 434 HIS A N   1 
ATOM   6698 C CA  . HIS B 2 443 ? 146.721 174.807 121.686 1.00 40.93  ? 434 HIS A CA  1 
ATOM   6699 C C   . HIS B 2 443 ? 146.708 176.096 120.880 1.00 45.39  ? 434 HIS A C   1 
ATOM   6700 O O   . HIS B 2 443 ? 146.511 176.085 119.665 1.00 46.07  ? 434 HIS A O   1 
ATOM   6701 C CB  . HIS B 2 443 ? 148.130 174.192 121.657 1.00 38.50  ? 434 HIS A CB  1 
ATOM   6702 C CG  . HIS B 2 443 ? 148.288 172.980 122.522 1.00 50.51  ? 434 HIS A CG  1 
ATOM   6703 N ND1 . HIS B 2 443 ? 147.419 171.913 122.480 1.00 53.75  ? 434 HIS A ND1 1 
ATOM   6704 C CD2 . HIS B 2 443 ? 149.217 172.671 123.456 1.00 53.32  ? 434 HIS A CD2 1 
ATOM   6705 C CE1 . HIS B 2 443 ? 147.805 170.997 123.350 1.00 54.38  ? 434 HIS A CE1 1 
ATOM   6706 N NE2 . HIS B 2 443 ? 148.894 171.433 123.956 1.00 56.91  ? 434 HIS A NE2 1 
ATOM   6707 N N   . GLN B 2 444 ? 146.910 177.214 121.567 1.00 43.53  ? 435 GLN A N   1 
ATOM   6708 C CA  . GLN B 2 444 ? 146.959 178.516 120.921 1.00 40.07  ? 435 GLN A CA  1 
ATOM   6709 C C   . GLN B 2 444 ? 148.383 178.796 120.469 1.00 41.47  ? 435 GLN A C   1 
ATOM   6710 O O   . GLN B 2 444 ? 149.295 178.894 121.296 1.00 38.45  ? 435 GLN A O   1 
ATOM   6711 C CB  . GLN B 2 444 ? 146.470 179.620 121.858 1.00 46.86  ? 435 GLN A CB  1 
ATOM   6712 C CG  . GLN B 2 444 ? 146.026 180.882 121.138 1.00 42.52  ? 435 GLN A CG  1 
ATOM   6713 C CD  . GLN B 2 444 ? 144.762 180.675 120.337 1.00 42.79  ? 435 GLN A CD  1 
ATOM   6714 O OE1 . GLN B 2 444 ? 143.981 179.769 120.616 1.00 52.24  ? 435 GLN A OE1 1 
ATOM   6715 N NE2 . GLN B 2 444 ? 144.554 181.513 119.335 1.00 41.31  ? 435 GLN A NE2 1 
ATOM   6716 N N   . ILE B 2 445 ? 148.568 178.929 119.160 1.00 44.39  ? 436 ILE A N   1 
ATOM   6717 C CA  . ILE B 2 445 ? 149.880 179.142 118.566 1.00 43.11  ? 436 ILE A CA  1 
ATOM   6718 C C   . ILE B 2 445 ? 149.985 180.618 118.218 1.00 40.95  ? 436 ILE A C   1 
ATOM   6719 O O   . ILE B 2 445 ? 149.335 181.091 117.278 1.00 37.98  ? 436 ILE A O   1 
ATOM   6720 C CB  . ILE B 2 445 ? 150.103 178.265 117.326 1.00 35.94  ? 436 ILE A CB  1 
ATOM   6721 C CG1 . ILE B 2 445 ? 149.986 176.784 117.688 1.00 38.71  ? 436 ILE A CG1 1 
ATOM   6722 C CG2 . ILE B 2 445 ? 151.469 178.539 116.722 1.00 30.11  ? 436 ILE A CG2 1 
ATOM   6723 C CD1 . ILE B 2 445 ? 150.933 176.343 118.778 1.00 41.50  ? 436 ILE A CD1 1 
ATOM   6724 N N   . PHE B 2 446 ? 150.792 181.347 118.982 1.00 37.26  ? 437 PHE A N   1 
ATOM   6725 C CA  . PHE B 2 446 ? 151.124 182.726 118.669 1.00 32.35  ? 437 PHE A CA  1 
ATOM   6726 C C   . PHE B 2 446 ? 152.513 183.001 119.219 1.00 34.53  ? 437 PHE A C   1 
ATOM   6727 O O   . PHE B 2 446 ? 152.994 182.302 120.113 1.00 37.71  ? 437 PHE A O   1 
ATOM   6728 C CB  . PHE B 2 446 ? 150.095 183.715 119.237 1.00 38.07  ? 437 PHE A CB  1 
ATOM   6729 C CG  . PHE B 2 446 ? 149.919 183.635 120.727 1.00 40.99  ? 437 PHE A CG  1 
ATOM   6730 C CD1 . PHE B 2 446 ? 150.731 184.368 121.573 1.00 34.82  ? 437 PHE A CD1 1 
ATOM   6731 C CD2 . PHE B 2 446 ? 148.931 182.845 121.279 1.00 43.84  ? 437 PHE A CD2 1 
ATOM   6732 C CE1 . PHE B 2 446 ? 150.573 184.299 122.937 1.00 29.00  ? 437 PHE A CE1 1 
ATOM   6733 C CE2 . PHE B 2 446 ? 148.767 182.775 122.644 1.00 41.02  ? 437 PHE A CE2 1 
ATOM   6734 C CZ  . PHE B 2 446 ? 149.588 183.503 123.473 1.00 37.97  ? 437 PHE A CZ  1 
ATOM   6735 N N   . PHE B 2 447 ? 153.156 184.027 118.676 1.00 37.70  ? 438 PHE A N   1 
ATOM   6736 C CA  . PHE B 2 447 ? 154.543 184.328 119.000 1.00 37.25  ? 438 PHE A CA  1 
ATOM   6737 C C   . PHE B 2 447 ? 154.622 185.492 119.977 1.00 47.77  ? 438 PHE A C   1 
ATOM   6738 O O   . PHE B 2 447 ? 153.868 186.463 119.864 1.00 48.25  ? 438 PHE A O   1 
ATOM   6739 C CB  . PHE B 2 447 ? 155.341 184.645 117.736 1.00 35.21  ? 438 PHE A CB  1 
ATOM   6740 C CG  . PHE B 2 447 ? 155.589 183.451 116.863 1.00 36.49  ? 438 PHE A CG  1 
ATOM   6741 C CD1 . PHE B 2 447 ? 156.628 182.583 117.137 1.00 37.00  ? 438 PHE A CD1 1 
ATOM   6742 C CD2 . PHE B 2 447 ? 154.777 183.190 115.776 1.00 33.59  ? 438 PHE A CD2 1 
ATOM   6743 C CE1 . PHE B 2 447 ? 156.857 181.485 116.341 1.00 31.13  ? 438 PHE A CE1 1 
ATOM   6744 C CE2 . PHE B 2 447 ? 155.003 182.092 114.979 1.00 30.69  ? 438 PHE A CE2 1 
ATOM   6745 C CZ  . PHE B 2 447 ? 156.044 181.239 115.263 1.00 29.98  ? 438 PHE A CZ  1 
ATOM   6746 N N   . ASP B 2 448 ? 155.536 185.382 120.935 1.00 53.84  ? 439 ASP A N   1 
ATOM   6747 C CA  . ASP B 2 448 ? 155.839 186.455 121.856 1.00 52.53  ? 439 ASP A CA  1 
ATOM   6748 C C   . ASP B 2 448 ? 156.571 187.560 121.104 1.00 56.34  ? 439 ASP A C   1 
ATOM   6749 O O   . ASP B 2 448 ? 157.071 187.344 119.999 1.00 56.19  ? 439 ASP A O   1 
ATOM   6750 C CB  . ASP B 2 448 ? 156.695 185.930 123.009 1.00 57.70  ? 439 ASP A CB  1 
ATOM   6751 C CG  . ASP B 2 448 ? 155.952 184.946 123.892 1.00 68.28  ? 439 ASP A CG  1 
ATOM   6752 O OD1 . ASP B 2 448 ? 154.750 184.707 123.648 1.00 63.72  ? 439 ASP A OD1 1 
ATOM   6753 O OD2 . ASP B 2 448 ? 156.575 184.401 124.827 1.00 76.35  ? 439 ASP A OD2 1 
ATOM   6754 N N   . PRO B 2 449 ? 156.641 188.768 121.670 1.00 62.63  ? 440 PRO A N   1 
ATOM   6755 C CA  . PRO B 2 449 ? 157.473 189.815 121.055 1.00 60.91  ? 440 PRO A CA  1 
ATOM   6756 C C   . PRO B 2 449 ? 158.943 189.438 120.935 1.00 62.31  ? 440 PRO A C   1 
ATOM   6757 O O   . PRO B 2 449 ? 159.705 190.190 120.315 1.00 64.02  ? 440 PRO A O   1 
ATOM   6758 C CB  . PRO B 2 449 ? 157.276 191.015 121.990 1.00 61.22  ? 440 PRO A CB  1 
ATOM   6759 C CG  . PRO B 2 449 ? 155.958 190.766 122.635 1.00 64.69  ? 440 PRO A CG  1 
ATOM   6760 C CD  . PRO B 2 449 ? 155.878 189.285 122.820 1.00 64.23  ? 440 PRO A CD  1 
ATOM   6761 N N   . GLN B 2 450 ? 159.362 188.306 121.505 1.00 63.74  ? 441 GLN A N   1 
ATOM   6762 C CA  . GLN B 2 450 ? 160.727 187.807 121.383 1.00 57.30  ? 441 GLN A CA  1 
ATOM   6763 C C   . GLN B 2 450 ? 160.795 186.532 120.548 1.00 58.93  ? 441 GLN A C   1 
ATOM   6764 O O   . GLN B 2 450 ? 161.766 185.777 120.656 1.00 58.43  ? 441 GLN A O   1 
ATOM   6765 C CB  . GLN B 2 450 ? 161.330 187.568 122.767 1.00 61.17  ? 441 GLN A CB  1 
ATOM   6766 C CG  . GLN B 2 450 ? 160.786 188.495 123.837 1.00 71.72  ? 441 GLN A CG  1 
ATOM   6767 C CD  . GLN B 2 450 ? 160.777 187.855 125.208 1.00 88.93  ? 441 GLN A CD  1 
ATOM   6768 O OE1 . GLN B 2 450 ? 161.799 187.361 125.683 1.00 83.22  ? 441 GLN A OE1 1 
ATOM   6769 N NE2 . GLN B 2 450 ? 159.614 187.854 125.852 1.00 88.90  ? 441 GLN A NE2 1 
ATOM   6770 N N   . GLY B 2 451 ? 159.785 186.279 119.721 1.00 55.92  ? 442 GLY A N   1 
ATOM   6771 C CA  . GLY B 2 451 ? 159.777 185.128 118.832 1.00 47.86  ? 442 GLY A CA  1 
ATOM   6772 C C   . GLY B 2 451 ? 159.727 183.772 119.500 1.00 52.11  ? 442 GLY A C   1 
ATOM   6773 O O   . GLY B 2 451 ? 160.503 182.883 119.134 1.00 53.43  ? 442 GLY A O   1 
ATOM   6774 N N   . ASP B 2 452 ? 158.841 183.589 120.474 1.00 52.66  ? 443 ASP A N   1 
ATOM   6775 C CA  . ASP B 2 452 ? 158.730 182.333 121.200 1.00 48.28  ? 443 ASP A CA  1 
ATOM   6776 C C   . ASP B 2 452 ? 157.268 181.930 121.316 1.00 44.94  ? 443 ASP A C   1 
ATOM   6777 O O   . ASP B 2 452 ? 156.379 182.779 121.377 1.00 49.88  ? 443 ASP A O   1 
ATOM   6778 C CB  . ASP B 2 452 ? 159.344 182.448 122.596 1.00 55.64  ? 443 ASP A CB  1 
ATOM   6779 C CG  . ASP B 2 452 ? 160.721 181.837 122.676 1.00 56.60  ? 443 ASP A CG  1 
ATOM   6780 O OD1 . ASP B 2 452 ? 160.934 180.777 122.058 1.00 52.17  ? 443 ASP A OD1 1 
ATOM   6781 O OD2 . ASP B 2 452 ? 161.591 182.415 123.357 1.00 58.66  ? 443 ASP A OD2 1 
ATOM   6782 N N   . VAL B 2 453 ? 157.026 180.624 121.357 1.00 38.80  ? 444 VAL A N   1 
ATOM   6783 C CA  . VAL B 2 453 ? 155.687 180.075 121.539 1.00 41.66  ? 444 VAL A CA  1 
ATOM   6784 C C   . VAL B 2 453 ? 155.623 179.415 122.908 1.00 46.91  ? 444 VAL A C   1 
ATOM   6785 O O   . VAL B 2 453 ? 156.450 178.557 123.235 1.00 46.28  ? 444 VAL A O   1 
ATOM   6786 C CB  . VAL B 2 453 ? 155.318 179.073 120.429 1.00 35.74  ? 444 VAL A CB  1 
ATOM   6787 C CG1 . VAL B 2 453 ? 153.987 178.418 120.738 1.00 34.72  ? 444 VAL A CG1 1 
ATOM   6788 C CG2 . VAL B 2 453 ? 155.264 179.766 119.087 1.00 36.67  ? 444 VAL A CG2 1 
ATOM   6789 N N   . ALA B 2 454 ? 154.640 179.823 123.711 1.00 50.56  ? 445 ALA A N   1 
ATOM   6790 C CA  . ALA B 2 454 ? 154.496 179.336 125.083 1.00 42.58  ? 445 ALA A CA  1 
ATOM   6791 C C   . ALA B 2 454 ? 153.802 177.979 125.055 1.00 43.01  ? 445 ALA A C   1 
ATOM   6792 O O   . ALA B 2 454 ? 152.595 177.847 125.272 1.00 41.96  ? 445 ALA A O   1 
ATOM   6793 C CB  . ALA B 2 454 ? 153.732 180.340 125.935 1.00 39.37  ? 445 ALA A CB  1 
ATOM   6794 N N   . LEU B 2 455 ? 154.591 176.950 124.773 1.00 43.35  ? 446 LEU A N   1 
ATOM   6795 C CA  . LEU B 2 455 ? 154.129 175.571 124.773 1.00 44.03  ? 446 LEU A CA  1 
ATOM   6796 C C   . LEU B 2 455 ? 154.458 174.952 126.122 1.00 41.13  ? 446 LEU A C   1 
ATOM   6797 O O   . LEU B 2 455 ? 155.580 175.097 126.615 1.00 43.81  ? 446 LEU A O   1 
ATOM   6798 C CB  . LEU B 2 455 ? 154.778 174.776 123.640 1.00 40.28  ? 446 LEU A CB  1 
ATOM   6799 C CG  . LEU B 2 455 ? 154.095 174.909 122.279 1.00 43.97  ? 446 LEU A CG  1 
ATOM   6800 C CD1 . LEU B 2 455 ? 154.686 173.936 121.278 1.00 49.75  ? 446 LEU A CD1 1 
ATOM   6801 C CD2 . LEU B 2 455 ? 152.600 174.693 122.414 1.00 39.44  ? 446 LEU A CD2 1 
ATOM   6802 N N   . HIS B 2 456 ? 153.479 174.280 126.720 1.00 45.32  ? 447 HIS A N   1 
ATOM   6803 C CA  . HIS B 2 456 ? 153.645 173.762 128.070 1.00 48.31  ? 447 HIS A CA  1 
ATOM   6804 C C   . HIS B 2 456 ? 154.785 172.755 128.142 1.00 44.55  ? 447 HIS A C   1 
ATOM   6805 O O   . HIS B 2 456 ? 154.935 171.894 127.273 1.00 45.86  ? 447 HIS A O   1 
ATOM   6806 C CB  . HIS B 2 456 ? 152.348 173.122 128.562 1.00 49.21  ? 447 HIS A CB  1 
ATOM   6807 C CG  . HIS B 2 456 ? 151.154 174.018 128.456 1.00 57.06  ? 447 HIS A CG  1 
ATOM   6808 N ND1 . HIS B 2 456 ? 149.891 173.547 128.176 1.00 64.64  ? 447 HIS A ND1 1 
ATOM   6809 C CD2 . HIS B 2 456 ? 151.036 175.361 128.583 1.00 56.89  ? 447 HIS A CD2 1 
ATOM   6810 C CE1 . HIS B 2 456 ? 149.043 174.560 128.144 1.00 70.59  ? 447 HIS A CE1 1 
ATOM   6811 N NE2 . HIS B 2 456 ? 149.713 175.672 128.386 1.00 65.76  ? 447 HIS A NE2 1 
ATOM   6812 N N   . LEU B 2 457 ? 155.603 172.885 129.182 1.00 42.66  ? 448 LEU A N   1 
ATOM   6813 C CA  . LEU B 2 457 ? 156.668 171.937 129.451 1.00 36.68  ? 448 LEU A CA  1 
ATOM   6814 C C   . LEU B 2 457 ? 156.136 170.811 130.336 1.00 42.93  ? 448 LEU A C   1 
ATOM   6815 O O   . LEU B 2 457 ? 154.947 170.746 130.659 1.00 45.92  ? 448 LEU A O   1 
ATOM   6816 C CB  . LEU B 2 457 ? 157.855 172.646 130.097 1.00 40.30  ? 448 LEU A CB  1 
ATOM   6817 C CG  . LEU B 2 457 ? 158.622 173.654 129.237 1.00 44.11  ? 448 LEU A CG  1 
ATOM   6818 C CD1 . LEU B 2 457 ? 159.753 174.270 130.035 1.00 43.76  ? 448 LEU A CD1 1 
ATOM   6819 C CD2 . LEU B 2 457 ? 159.149 173.021 127.962 1.00 46.88  ? 448 LEU A CD2 1 
ATOM   6820 N N   . GLU B 2 458 ? 157.025 169.908 130.740 1.00 46.38  ? 449 GLU A N   1 
ATOM   6821 C CA  . GLU B 2 458 ? 156.625 168.757 131.539 1.00 40.16  ? 449 GLU A CA  1 
ATOM   6822 C C   . GLU B 2 458 ? 157.838 168.187 132.251 1.00 40.41  ? 449 GLU A C   1 
ATOM   6823 O O   . GLU B 2 458 ? 158.870 167.948 131.619 1.00 45.47  ? 449 GLU A O   1 
ATOM   6824 C CB  . GLU B 2 458 ? 155.987 167.670 130.672 1.00 40.48  ? 449 GLU A CB  1 
ATOM   6825 C CG  . GLU B 2 458 ? 154.492 167.552 130.803 1.00 54.94  ? 449 GLU A CG  1 
ATOM   6826 C CD  . GLU B 2 458 ? 153.987 166.198 130.356 1.00 71.18  ? 449 GLU A CD  1 
ATOM   6827 O OE1 . GLU B 2 458 ? 154.818 165.380 129.911 1.00 70.25  ? 449 GLU A OE1 1 
ATOM   6828 O OE2 . GLU B 2 458 ? 152.765 165.951 130.450 1.00 74.82  ? 449 GLU A OE2 1 
ATOM   6829 N N   . ILE B 2 459 ? 157.711 167.970 133.553 1.00 35.98  ? 450 ILE A N   1 
ATOM   6830 C CA  . ILE B 2 459 ? 158.669 167.163 134.294 1.00 34.23  ? 450 ILE A CA  1 
ATOM   6831 C C   . ILE B 2 459 ? 158.252 165.710 134.144 1.00 34.73  ? 450 ILE A C   1 
ATOM   6832 O O   . ILE B 2 459 ? 157.101 165.352 134.414 1.00 41.37  ? 450 ILE A O   1 
ATOM   6833 C CB  . ILE B 2 459 ? 158.729 167.580 135.772 1.00 31.14  ? 450 ILE A CB  1 
ATOM   6834 C CG1 . ILE B 2 459 ? 159.509 168.882 135.911 1.00 31.92  ? 450 ILE A CG1 1 
ATOM   6835 C CG2 . ILE B 2 459 ? 159.423 166.510 136.592 1.00 25.66  ? 450 ILE A CG2 1 
ATOM   6836 C CD1 . ILE B 2 459 ? 158.916 169.851 136.883 1.00 31.01  ? 450 ILE A CD1 1 
ATOM   6837 N N   . VAL B 2 460 ? 159.178 164.875 133.694 1.00 33.16  ? 451 VAL A N   1 
ATOM   6838 C CA  . VAL B 2 460 ? 158.884 163.499 133.324 1.00 33.99  ? 451 VAL A CA  1 
ATOM   6839 C C   . VAL B 2 460 ? 159.779 162.594 134.158 1.00 31.54  ? 451 VAL A C   1 
ATOM   6840 O O   . VAL B 2 460 ? 160.924 162.950 134.456 1.00 35.72  ? 451 VAL A O   1 
ATOM   6841 C CB  . VAL B 2 460 ? 159.083 163.280 131.810 1.00 46.09  ? 451 VAL A CB  1 
ATOM   6842 C CG1 . VAL B 2 460 ? 158.110 164.105 130.976 1.00 44.53  ? 451 VAL A CG1 1 
ATOM   6843 C CG2 . VAL B 2 460 ? 160.518 163.525 131.419 1.00 53.52  ? 451 VAL A CG2 1 
ATOM   6844 N N   . GLN B 2 461 ? 159.245 161.453 134.575 1.00 32.60  ? 452 GLN A N   1 
ATOM   6845 C CA  . GLN B 2 461 ? 159.943 160.545 135.474 1.00 33.62  ? 452 GLN A CA  1 
ATOM   6846 C C   . GLN B 2 461 ? 160.228 159.232 134.760 1.00 43.51  ? 452 GLN A C   1 
ATOM   6847 O O   . GLN B 2 461 ? 159.335 158.648 134.141 1.00 55.03  ? 452 GLN A O   1 
ATOM   6848 C CB  . GLN B 2 461 ? 159.122 160.295 136.738 1.00 36.91  ? 452 GLN A CB  1 
ATOM   6849 C CG  . GLN B 2 461 ? 159.891 159.607 137.845 1.00 38.29  ? 452 GLN A CG  1 
ATOM   6850 C CD  . GLN B 2 461 ? 159.074 158.564 138.566 1.00 40.79  ? 452 GLN A CD  1 
ATOM   6851 O OE1 . GLN B 2 461 ? 157.883 158.406 138.310 1.00 45.37  ? 452 GLN A OE1 1 
ATOM   6852 N NE2 . GLN B 2 461 ? 159.710 157.848 139.480 1.00 41.45  ? 452 GLN A NE2 1 
ATOM   6853 N N   . TRP B 2 462 ? 161.470 158.772 134.853 1.00 41.89  ? 453 TRP A N   1 
ATOM   6854 C CA  . TRP B 2 462 ? 161.877 157.565 134.150 1.00 44.10  ? 453 TRP A CA  1 
ATOM   6855 C C   . TRP B 2 462 ? 161.395 156.334 134.902 1.00 55.66  ? 453 TRP A C   1 
ATOM   6856 O O   . TRP B 2 462 ? 161.953 155.977 135.943 1.00 63.75  ? 453 TRP A O   1 
ATOM   6857 C CB  . TRP B 2 462 ? 163.392 157.522 133.998 1.00 45.07  ? 453 TRP A CB  1 
ATOM   6858 C CG  . TRP B 2 462 ? 163.946 158.568 133.102 1.00 47.64  ? 453 TRP A CG  1 
ATOM   6859 C CD1 . TRP B 2 462 ? 163.336 159.721 132.704 1.00 44.50  ? 453 TRP A CD1 1 
ATOM   6860 C CD2 . TRP B 2 462 ? 165.226 158.551 132.467 1.00 52.30  ? 453 TRP A CD2 1 
ATOM   6861 N NE1 . TRP B 2 462 ? 164.163 160.429 131.874 1.00 49.80  ? 453 TRP A NE1 1 
ATOM   6862 C CE2 . TRP B 2 462 ? 165.330 159.730 131.708 1.00 53.50  ? 453 TRP A CE2 1 
ATOM   6863 C CE3 . TRP B 2 462 ? 166.297 157.655 132.471 1.00 48.96  ? 453 TRP A CE3 1 
ATOM   6864 C CZ2 . TRP B 2 462 ? 166.460 160.034 130.961 1.00 54.35  ? 453 TRP A CZ2 1 
ATOM   6865 C CZ3 . TRP B 2 462 ? 167.415 157.961 131.730 1.00 51.72  ? 453 TRP A CZ3 1 
ATOM   6866 C CH2 . TRP B 2 462 ? 167.490 159.139 130.985 1.00 55.53  ? 453 TRP A CH2 1 
ATOM   6867 N N   . GLN B 2 463 ? 160.361 155.687 134.377 1.00 60.55  ? 454 GLN A N   1 
ATOM   6868 C CA  . GLN B 2 463 ? 159.891 154.409 134.888 1.00 64.14  ? 454 GLN A CA  1 
ATOM   6869 C C   . GLN B 2 463 ? 160.161 153.343 133.840 1.00 77.13  ? 454 GLN A C   1 
ATOM   6870 O O   . GLN B 2 463 ? 159.805 153.513 132.670 1.00 84.49  ? 454 GLN A O   1 
ATOM   6871 C CB  . GLN B 2 463 ? 158.403 154.462 135.241 1.00 59.69  ? 454 GLN A CB  1 
ATOM   6872 C CG  . GLN B 2 463 ? 158.077 155.271 136.492 1.00 67.27  ? 454 GLN A CG  1 
ATOM   6873 C CD  . GLN B 2 463 ? 158.687 154.691 137.762 1.00 71.98  ? 454 GLN A CD  1 
ATOM   6874 O OE1 . GLN B 2 463 ? 159.904 154.709 137.952 1.00 71.46  ? 454 GLN A OE1 1 
ATOM   6875 N NE2 . GLN B 2 463 ? 157.836 154.173 138.640 1.00 62.98  ? 454 GLN A NE2 1 
ATOM   6876 N N   . TRP B 2 464 ? 160.789 152.252 134.262 1.00 79.88  ? 455 TRP A N   1 
ATOM   6877 C CA  . TRP B 2 464 ? 161.278 151.217 133.356 1.00 87.04  ? 455 TRP A CA  1 
ATOM   6878 C C   . TRP B 2 464 ? 160.158 150.210 133.112 1.00 94.93  ? 455 TRP A C   1 
ATOM   6879 O O   . TRP B 2 464 ? 159.958 149.279 133.897 1.00 91.11  ? 455 TRP A O   1 
ATOM   6880 C CB  . TRP B 2 464 ? 162.531 150.571 133.936 1.00 84.93  ? 455 TRP A CB  1 
ATOM   6881 C CG  . TRP B 2 464 ? 163.731 151.460 133.788 1.00 87.52  ? 455 TRP A CG  1 
ATOM   6882 C CD1 . TRP B 2 464 ? 164.577 151.518 132.720 1.00 92.98  ? 455 TRP A CD1 1 
ATOM   6883 C CD2 . TRP B 2 464 ? 164.169 152.475 134.700 1.00 78.82  ? 455 TRP A CD2 1 
ATOM   6884 N NE1 . TRP B 2 464 ? 165.537 152.476 132.928 1.00 93.20  ? 455 TRP A NE1 1 
ATOM   6885 C CE2 . TRP B 2 464 ? 165.306 153.081 134.135 1.00 82.20  ? 455 TRP A CE2 1 
ATOM   6886 C CE3 . TRP B 2 464 ? 163.719 152.919 135.946 1.00 69.55  ? 455 TRP A CE3 1 
ATOM   6887 C CZ2 . TRP B 2 464 ? 165.999 154.105 134.772 1.00 71.12  ? 455 TRP A CZ2 1 
ATOM   6888 C CZ3 . TRP B 2 464 ? 164.409 153.933 136.575 1.00 69.04  ? 455 TRP A CZ3 1 
ATOM   6889 C CH2 . TRP B 2 464 ? 165.535 154.515 135.988 1.00 66.51  ? 455 TRP A CH2 1 
ATOM   6890 N N   . ASP B 2 465 ? 159.429 150.410 132.014 1.00 99.32  ? 456 ASP A N   1 
ATOM   6891 C CA  . ASP B 2 465 ? 158.304 149.553 131.648 1.00 105.99 ? 456 ASP A CA  1 
ATOM   6892 C C   . ASP B 2 465 ? 158.040 149.732 130.161 1.00 110.76 ? 456 ASP A C   1 
ATOM   6893 O O   . ASP B 2 465 ? 157.658 150.823 129.726 1.00 111.08 ? 456 ASP A O   1 
ATOM   6894 C CB  . ASP B 2 465 ? 157.061 149.889 132.467 1.00 105.61 ? 456 ASP A CB  1 
ATOM   6895 C CG  . ASP B 2 465 ? 155.966 148.856 132.312 1.00 109.71 ? 456 ASP A CG  1 
ATOM   6896 O OD1 . ASP B 2 465 ? 156.263 147.743 131.829 1.00 108.37 ? 456 ASP A OD1 1 
ATOM   6897 O OD2 . ASP B 2 465 ? 154.809 149.157 132.667 1.00 106.78 ? 456 ASP A OD2 1 
ATOM   6898 N N   . ARG B 2 466 ? 158.243 148.666 129.384 1.00 111.80 ? 457 ARG A N   1 
ATOM   6899 C CA  . ARG B 2 466 ? 158.017 148.739 127.946 1.00 111.87 ? 457 ARG A CA  1 
ATOM   6900 C C   . ARG B 2 466 ? 156.538 148.749 127.584 1.00 108.28 ? 457 ARG A C   1 
ATOM   6901 O O   . ARG B 2 466 ? 156.182 149.242 126.508 1.00 106.47 ? 457 ARG A O   1 
ATOM   6902 C CB  . ARG B 2 466 ? 158.714 147.570 127.249 1.00 116.19 ? 457 ARG A CB  1 
ATOM   6903 C CG  . ARG B 2 466 ? 159.893 147.006 128.023 1.00 116.09 ? 457 ARG A CG  1 
ATOM   6904 C CD  . ARG B 2 466 ? 160.957 146.462 127.086 1.00 116.18 ? 457 ARG A CD  1 
ATOM   6905 N NE  . ARG B 2 466 ? 161.591 147.521 126.310 1.00 119.78 ? 457 ARG A NE  1 
ATOM   6906 C CZ  . ARG B 2 466 ? 162.577 148.289 126.753 1.00 113.47 ? 457 ARG A CZ  1 
ATOM   6907 N NH1 . ARG B 2 466 ? 163.072 148.143 127.971 1.00 109.68 ? 457 ARG A NH1 1 
ATOM   6908 N NH2 . ARG B 2 466 ? 163.079 149.226 125.954 1.00 109.44 ? 457 ARG A NH2 1 
ATOM   6909 N N   . SER B 2 467 ? 155.670 148.220 128.449 1.00 109.71 ? 458 SER A N   1 
ATOM   6910 C CA  . SER B 2 467 ? 154.247 148.155 128.139 1.00 112.92 ? 458 SER A CA  1 
ATOM   6911 C C   . SER B 2 467 ? 153.529 149.476 128.378 1.00 113.95 ? 458 SER A C   1 
ATOM   6912 O O   . SER B 2 467 ? 152.382 149.628 127.945 1.00 112.50 ? 458 SER A O   1 
ATOM   6913 C CB  . SER B 2 467 ? 153.576 147.054 128.962 1.00 108.64 ? 458 SER A CB  1 
ATOM   6914 O OG  . SER B 2 467 ? 153.638 147.343 130.348 1.00 108.40 ? 458 SER A OG  1 
ATOM   6915 N N   . GLN B 2 468 ? 154.170 150.424 129.050 1.00 109.63 ? 459 GLN A N   1 
ATOM   6916 C CA  . GLN B 2 468 ? 153.580 151.719 129.355 1.00 104.31 ? 459 GLN A CA  1 
ATOM   6917 C C   . GLN B 2 468 ? 154.462 152.826 128.782 1.00 101.57 ? 459 GLN A C   1 
ATOM   6918 O O   . GLN B 2 468 ? 155.449 152.569 128.087 1.00 102.38 ? 459 GLN A O   1 
ATOM   6919 C CB  . GLN B 2 468 ? 153.388 151.878 130.864 1.00 105.18 ? 459 GLN A CB  1 
ATOM   6920 C CG  . GLN B 2 468 ? 152.341 150.956 131.461 1.00 109.73 ? 459 GLN A CG  1 
ATOM   6921 C CD  . GLN B 2 468 ? 152.218 151.112 132.964 1.00 109.81 ? 459 GLN A CD  1 
ATOM   6922 O OE1 . GLN B 2 468 ? 152.366 152.211 133.500 1.00 101.88 ? 459 GLN A OE1 1 
ATOM   6923 N NE2 . GLN B 2 468 ? 151.947 150.011 133.653 1.00 107.66 ? 459 GLN A NE2 1 
ATOM   6924 N N   . ASN B 2 469 ? 154.096 154.063 129.083 1.00 96.12  ? 460 ASN A N   1 
ATOM   6925 C CA  . ASN B 2 469 ? 154.877 155.214 128.650 1.00 90.02  ? 460 ASN A CA  1 
ATOM   6926 C C   . ASN B 2 469 ? 156.243 155.157 129.323 1.00 87.02  ? 460 ASN A C   1 
ATOM   6927 O O   . ASN B 2 469 ? 156.311 155.164 130.559 1.00 86.98  ? 460 ASN A O   1 
ATOM   6928 C CB  . ASN B 2 469 ? 154.127 156.498 129.011 1.00 84.29  ? 460 ASN A CB  1 
ATOM   6929 C CG  . ASN B 2 469 ? 154.811 157.756 128.507 1.00 83.43  ? 460 ASN A CG  1 
ATOM   6930 O OD1 . ASN B 2 469 ? 155.760 157.700 127.730 1.00 87.00  ? 460 ASN A OD1 1 
ATOM   6931 N ND2 . ASN B 2 469 ? 154.306 158.907 128.934 1.00 71.29  ? 460 ASN A ND2 1 
ATOM   6932 N N   . PRO B 2 470 ? 157.344 155.079 128.568 1.00 89.89  ? 461 PRO A N   1 
ATOM   6933 C CA  . PRO B 2 470 ? 158.667 154.977 129.210 1.00 86.89  ? 461 PRO A CA  1 
ATOM   6934 C C   . PRO B 2 470 ? 159.041 156.195 130.030 1.00 79.04  ? 461 PRO A C   1 
ATOM   6935 O O   . PRO B 2 470 ? 159.857 156.075 130.951 1.00 75.04  ? 461 PRO A O   1 
ATOM   6936 C CB  . PRO B 2 470 ? 159.618 154.789 128.022 1.00 86.28  ? 461 PRO A CB  1 
ATOM   6937 C CG  . PRO B 2 470 ? 158.918 155.444 126.881 1.00 92.52  ? 461 PRO A CG  1 
ATOM   6938 C CD  . PRO B 2 470 ? 157.448 155.201 127.104 1.00 92.73  ? 461 PRO A CD  1 
ATOM   6939 N N   . PHE B 2 471 ? 158.478 157.358 129.721 1.00 68.77  ? 462 PHE A N   1 
ATOM   6940 C CA  . PHE B 2 471 ? 158.724 158.603 130.439 1.00 63.32  ? 462 PHE A CA  1 
ATOM   6941 C C   . PHE B 2 471 ? 157.376 159.081 130.966 1.00 65.09  ? 462 PHE A C   1 
ATOM   6942 O O   . PHE B 2 471 ? 156.632 159.767 130.264 1.00 72.71  ? 462 PHE A O   1 
ATOM   6943 C CB  . PHE B 2 471 ? 159.378 159.623 129.520 1.00 69.51  ? 462 PHE A CB  1 
ATOM   6944 C CG  . PHE B 2 471 ? 160.647 159.135 128.890 1.00 75.00  ? 462 PHE A CG  1 
ATOM   6945 C CD1 . PHE B 2 471 ? 161.557 158.398 129.625 1.00 72.63  ? 462 PHE A CD1 1 
ATOM   6946 C CD2 . PHE B 2 471 ? 160.908 159.368 127.551 1.00 75.57  ? 462 PHE A CD2 1 
ATOM   6947 C CE1 . PHE B 2 471 ? 162.720 157.937 129.050 1.00 70.72  ? 462 PHE A CE1 1 
ATOM   6948 C CE2 . PHE B 2 471 ? 162.068 158.898 126.968 1.00 78.65  ? 462 PHE A CE2 1 
ATOM   6949 C CZ  . PHE B 2 471 ? 162.975 158.184 127.720 1.00 77.04  ? 462 PHE A CZ  1 
ATOM   6950 N N   . GLN B 2 472 ? 157.061 158.707 132.202 1.00 61.23  ? 463 GLN A N   1 
ATOM   6951 C CA  . GLN B 2 472 ? 155.772 159.033 132.793 1.00 57.71  ? 463 GLN A CA  1 
ATOM   6952 C C   . GLN B 2 472 ? 155.737 160.484 133.253 1.00 49.54  ? 463 GLN A C   1 
ATOM   6953 O O   . GLN B 2 472 ? 156.575 160.920 134.044 1.00 49.79  ? 463 GLN A O   1 
ATOM   6954 C CB  . GLN B 2 472 ? 155.483 158.103 133.970 1.00 55.31  ? 463 GLN A CB  1 
ATOM   6955 C CG  . GLN B 2 472 ? 154.056 158.158 134.480 1.00 64.04  ? 463 GLN A CG  1 
ATOM   6956 C CD  . GLN B 2 472 ? 153.036 157.855 133.402 1.00 74.46  ? 463 GLN A CD  1 
ATOM   6957 O OE1 . GLN B 2 472 ? 153.247 156.984 132.559 1.00 77.21  ? 463 GLN A OE1 1 
ATOM   6958 N NE2 . GLN B 2 472 ? 151.919 158.574 133.426 1.00 67.06  ? 463 GLN A NE2 1 
ATOM   6959 N N   . SER B 2 473 ? 154.747 161.226 132.768 1.00 45.96  ? 464 SER A N   1 
ATOM   6960 C CA  . SER B 2 473 ? 154.587 162.636 133.097 1.00 49.13  ? 464 SER A CA  1 
ATOM   6961 C C   . SER B 2 473 ? 154.123 162.783 134.539 1.00 51.08  ? 464 SER A C   1 
ATOM   6962 O O   . SER B 2 473 ? 153.166 162.123 134.957 1.00 56.12  ? 464 SER A O   1 
ATOM   6963 C CB  . SER B 2 473 ? 153.586 163.303 132.157 1.00 57.39  ? 464 SER A CB  1 
ATOM   6964 O OG  . SER B 2 473 ? 152.916 164.365 132.809 1.00 62.07  ? 464 SER A OG  1 
ATOM   6965 N N   . VAL B 2 474 ? 154.799 163.647 135.292 1.00 47.39  ? 465 VAL A N   1 
ATOM   6966 C CA  . VAL B 2 474 ? 154.471 163.858 136.694 1.00 44.82  ? 465 VAL A CA  1 
ATOM   6967 C C   . VAL B 2 474 ? 154.169 165.312 137.029 1.00 44.51  ? 465 VAL A C   1 
ATOM   6968 O O   . VAL B 2 474 ? 153.622 165.576 138.110 1.00 50.52  ? 465 VAL A O   1 
ATOM   6969 C CB  . VAL B 2 474 ? 155.585 163.323 137.618 1.00 38.13  ? 465 VAL A CB  1 
ATOM   6970 C CG1 . VAL B 2 474 ? 155.730 161.822 137.461 1.00 37.00  ? 465 VAL A CG1 1 
ATOM   6971 C CG2 . VAL B 2 474 ? 156.894 164.018 137.335 1.00 32.05  ? 465 VAL A CG2 1 
ATOM   6972 N N   . ALA B 2 475 ? 154.502 166.270 136.169 1.00 42.89  ? 466 ALA A N   1 
ATOM   6973 C CA  . ALA B 2 475 ? 154.160 167.663 136.416 1.00 40.91  ? 466 ALA A CA  1 
ATOM   6974 C C   . ALA B 2 475 ? 154.045 168.388 135.085 1.00 44.43  ? 466 ALA A C   1 
ATOM   6975 O O   . ALA B 2 475 ? 154.608 167.955 134.078 1.00 44.05  ? 466 ALA A O   1 
ATOM   6976 C CB  . ALA B 2 475 ? 155.193 168.347 137.314 1.00 35.59  ? 466 ALA A CB  1 
ATOM   6977 N N   . SER B 2 476 ? 153.306 169.496 135.090 1.00 45.59  ? 467 SER A N   1 
ATOM   6978 C CA  . SER B 2 476 ? 153.075 170.305 133.901 1.00 37.70  ? 467 SER A CA  1 
ATOM   6979 C C   . SER B 2 476 ? 153.467 171.746 134.183 1.00 37.62  ? 467 SER A C   1 
ATOM   6980 O O   . SER B 2 476 ? 152.996 172.340 135.156 1.00 50.57  ? 467 SER A O   1 
ATOM   6981 C CB  . SER B 2 476 ? 151.611 170.239 133.466 1.00 44.54  ? 467 SER A CB  1 
ATOM   6982 O OG  . SER B 2 476 ? 151.180 168.899 133.325 1.00 60.75  ? 467 SER A OG  1 
ATOM   6983 N N   . TYR B 2 477 ? 154.312 172.309 133.326 1.00 38.95  ? 468 TYR A N   1 
ATOM   6984 C CA  . TYR B 2 477 ? 154.790 173.676 133.470 1.00 38.61  ? 468 TYR A CA  1 
ATOM   6985 C C   . TYR B 2 477 ? 154.082 174.563 132.459 1.00 43.03  ? 468 TYR A C   1 
ATOM   6986 O O   . TYR B 2 477 ? 153.930 174.184 131.294 1.00 49.18  ? 468 TYR A O   1 
ATOM   6987 C CB  . TYR B 2 477 ? 156.304 173.757 133.275 1.00 36.45  ? 468 TYR A CB  1 
ATOM   6988 C CG  . TYR B 2 477 ? 156.855 175.160 133.350 1.00 40.74  ? 468 TYR A CG  1 
ATOM   6989 C CD1 . TYR B 2 477 ? 156.996 175.810 134.567 1.00 44.28  ? 468 TYR A CD1 1 
ATOM   6990 C CD2 . TYR B 2 477 ? 157.224 175.839 132.201 1.00 42.44  ? 468 TYR A CD2 1 
ATOM   6991 C CE1 . TYR B 2 477 ? 157.497 177.092 134.634 1.00 42.33  ? 468 TYR A CE1 1 
ATOM   6992 C CE2 . TYR B 2 477 ? 157.722 177.117 132.259 1.00 42.73  ? 468 TYR A CE2 1 
ATOM   6993 C CZ  . TYR B 2 477 ? 157.857 177.740 133.475 1.00 45.25  ? 468 TYR A CZ  1 
ATOM   6994 O OH  . TYR B 2 477 ? 158.354 179.018 133.527 1.00 48.28  ? 468 TYR A OH  1 
ATOM   6995 N N   . TYR B 2 478 ? 153.647 175.736 132.908 1.00 41.50  ? 469 TYR A N   1 
ATOM   6996 C CA  . TYR B 2 478 ? 152.952 176.682 132.052 1.00 45.28  ? 469 TYR A CA  1 
ATOM   6997 C C   . TYR B 2 478 ? 153.818 177.914 131.857 1.00 51.29  ? 469 TYR A C   1 
ATOM   6998 O O   . TYR B 2 478 ? 153.935 178.726 132.785 1.00 54.70  ? 469 TYR A O   1 
ATOM   6999 C CB  . TYR B 2 478 ? 151.607 177.061 132.663 1.00 44.40  ? 469 TYR A CB  1 
ATOM   7000 C CG  . TYR B 2 478 ? 150.633 175.913 132.705 1.00 46.95  ? 469 TYR A CG  1 
ATOM   7001 C CD1 . TYR B 2 478 ? 149.786 175.661 131.639 1.00 55.50  ? 469 TYR A CD1 1 
ATOM   7002 C CD2 . TYR B 2 478 ? 150.583 175.058 133.791 1.00 50.12  ? 469 TYR A CD2 1 
ATOM   7003 C CE1 . TYR B 2 478 ? 148.899 174.607 131.664 1.00 56.07  ? 469 TYR A CE1 1 
ATOM   7004 C CE2 . TYR B 2 478 ? 149.702 173.996 133.822 1.00 50.97  ? 469 TYR A CE2 1 
ATOM   7005 C CZ  . TYR B 2 478 ? 148.862 173.776 132.758 1.00 50.14  ? 469 TYR A CZ  1 
ATOM   7006 O OH  . TYR B 2 478 ? 147.981 172.721 132.787 1.00 45.01  ? 469 TYR A OH  1 
ATOM   7007 N N   . PRO B 2 479 ? 154.445 178.097 130.693 1.00 46.85  ? 470 PRO A N   1 
ATOM   7008 C CA  . PRO B 2 479 ? 155.361 179.237 130.525 1.00 41.15  ? 470 PRO A CA  1 
ATOM   7009 C C   . PRO B 2 479 ? 154.688 180.590 130.642 1.00 47.24  ? 470 PRO A C   1 
ATOM   7010 O O   . PRO B 2 479 ? 155.359 181.575 130.975 1.00 48.63  ? 470 PRO A O   1 
ATOM   7011 C CB  . PRO B 2 479 ? 155.939 179.016 129.120 1.00 38.75  ? 470 PRO A CB  1 
ATOM   7012 C CG  . PRO B 2 479 ? 155.671 177.586 128.805 1.00 40.77  ? 470 PRO A CG  1 
ATOM   7013 C CD  . PRO B 2 479 ? 154.393 177.252 129.491 1.00 42.96  ? 470 PRO A CD  1 
ATOM   7014 N N   . LEU B 2 480 ? 153.385 180.677 130.368 1.00 49.17  ? 471 LEU A N   1 
ATOM   7015 C CA  . LEU B 2 480 ? 152.714 181.972 130.386 1.00 54.55  ? 471 LEU A CA  1 
ATOM   7016 C C   . LEU B 2 480 ? 152.649 182.545 131.796 1.00 55.69  ? 471 LEU A C   1 
ATOM   7017 O O   . LEU B 2 480 ? 152.812 183.755 131.989 1.00 57.17  ? 471 LEU A O   1 
ATOM   7018 C CB  . LEU B 2 480 ? 151.315 181.848 129.785 1.00 57.87  ? 471 LEU A CB  1 
ATOM   7019 C CG  . LEU B 2 480 ? 151.254 181.914 128.258 1.00 52.23  ? 471 LEU A CG  1 
ATOM   7020 C CD1 . LEU B 2 480 ? 149.816 181.949 127.772 1.00 50.15  ? 471 LEU A CD1 1 
ATOM   7021 C CD2 . LEU B 2 480 ? 152.022 183.117 127.746 1.00 42.47  ? 471 LEU A CD2 1 
ATOM   7022 N N   . GLN B 2 481 ? 152.411 181.697 132.791 1.00 56.65  ? 472 GLN A N   1 
ATOM   7023 C CA  . GLN B 2 481 ? 152.369 182.123 134.182 1.00 58.31  ? 472 GLN A CA  1 
ATOM   7024 C C   . GLN B 2 481 ? 153.620 181.737 134.957 1.00 55.72  ? 472 GLN A C   1 
ATOM   7025 O O   . GLN B 2 481 ? 153.744 182.109 136.128 1.00 62.43  ? 472 GLN A O   1 
ATOM   7026 C CB  . GLN B 2 481 ? 151.129 181.548 134.870 1.00 57.51  ? 472 GLN A CB  1 
ATOM   7027 C CG  . GLN B 2 481 ? 150.960 180.054 134.702 1.00 55.36  ? 472 GLN A CG  1 
ATOM   7028 C CD  . GLN B 2 481 ? 149.505 179.636 134.719 1.00 59.42  ? 472 GLN A CD  1 
ATOM   7029 O OE1 . GLN B 2 481 ? 148.990 179.179 135.738 1.00 64.04  ? 472 GLN A OE1 1 
ATOM   7030 N NE2 . GLN B 2 481 ? 148.832 179.795 133.587 1.00 49.08  ? 472 GLN A NE2 1 
ATOM   7031 N N   . ARG B 2 482 ? 154.547 181.012 134.329 1.00 47.68  ? 473 ARG A N   1 
ATOM   7032 C CA  . ARG B 2 482 ? 155.814 180.617 134.944 1.00 46.95  ? 473 ARG A CA  1 
ATOM   7033 C C   . ARG B 2 482 ? 155.591 179.906 136.273 1.00 53.93  ? 473 ARG A C   1 
ATOM   7034 O O   . ARG B 2 482 ? 156.325 180.104 137.242 1.00 54.76  ? 473 ARG A O   1 
ATOM   7035 C CB  . ARG B 2 482 ? 156.739 181.820 135.118 1.00 42.63  ? 473 ARG A CB  1 
ATOM   7036 C CG  . ARG B 2 482 ? 157.309 182.326 133.817 1.00 48.31  ? 473 ARG A CG  1 
ATOM   7037 C CD  . ARG B 2 482 ? 158.211 183.518 134.027 1.00 50.29  ? 473 ARG A CD  1 
ATOM   7038 N NE  . ARG B 2 482 ? 159.480 183.124 134.623 1.00 57.75  ? 473 ARG A NE  1 
ATOM   7039 C CZ  . ARG B 2 482 ? 160.639 183.140 133.981 1.00 59.54  ? 473 ARG A CZ  1 
ATOM   7040 N NH1 . ARG B 2 482 ? 160.719 183.498 132.711 1.00 56.62  ? 473 ARG A NH1 1 
ATOM   7041 N NH2 . ARG B 2 482 ? 161.744 182.782 134.627 1.00 60.04  ? 473 ARG A NH2 1 
ATOM   7042 N N   . GLN B 2 483 ? 154.565 179.065 136.319 1.00 53.02  ? 474 GLN A N   1 
ATOM   7043 C CA  . GLN B 2 483 ? 154.197 178.361 137.536 1.00 50.16  ? 474 GLN A CA  1 
ATOM   7044 C C   . GLN B 2 483 ? 153.970 176.895 137.210 1.00 48.91  ? 474 GLN A C   1 
ATOM   7045 O O   . GLN B 2 483 ? 153.334 176.570 136.204 1.00 49.59  ? 474 GLN A O   1 
ATOM   7046 C CB  . GLN B 2 483 ? 152.950 178.982 138.172 1.00 51.73  ? 474 GLN A CB  1 
ATOM   7047 C CG  . GLN B 2 483 ? 152.538 178.356 139.485 1.00 55.08  ? 474 GLN A CG  1 
ATOM   7048 C CD  . GLN B 2 483 ? 151.122 177.845 139.451 1.00 61.86  ? 474 GLN A CD  1 
ATOM   7049 O OE1 . GLN B 2 483 ? 150.549 177.657 138.380 1.00 59.24  ? 474 GLN A OE1 1 
ATOM   7050 N NE2 . GLN B 2 483 ? 150.544 177.617 140.623 1.00 65.35  ? 474 GLN A NE2 1 
ATOM   7051 N N   . LEU B 2 484 ? 154.496 176.020 138.057 1.00 50.53  ? 475 LEU A N   1 
ATOM   7052 C CA  . LEU B 2 484 ? 154.415 174.581 137.862 1.00 43.94  ? 475 LEU A CA  1 
ATOM   7053 C C   . LEU B 2 484 ? 153.297 174.028 138.734 1.00 47.82  ? 475 LEU A C   1 
ATOM   7054 O O   . LEU B 2 484 ? 153.269 174.277 139.943 1.00 52.23  ? 475 LEU A O   1 
ATOM   7055 C CB  . LEU B 2 484 ? 155.749 173.919 138.209 1.00 41.05  ? 475 LEU A CB  1 
ATOM   7056 C CG  . LEU B 2 484 ? 155.795 172.399 138.283 1.00 37.29  ? 475 LEU A CG  1 
ATOM   7057 C CD1 . LEU B 2 484 ? 155.941 171.850 136.888 1.00 37.82  ? 475 LEU A CD1 1 
ATOM   7058 C CD2 . LEU B 2 484 ? 156.940 171.948 139.164 1.00 35.46  ? 475 LEU A CD2 1 
ATOM   7059 N N   . LYS B 2 485 ? 152.376 173.291 138.121 1.00 44.36  ? 476 LYS A N   1 
ATOM   7060 C CA  . LYS B 2 485 ? 151.190 172.822 138.819 1.00 46.98  ? 476 LYS A CA  1 
ATOM   7061 C C   . LYS B 2 485 ? 150.822 171.437 138.307 1.00 50.52  ? 476 LYS A C   1 
ATOM   7062 O O   . LYS B 2 485 ? 151.496 170.870 137.444 1.00 50.33  ? 476 LYS A O   1 
ATOM   7063 C CB  . LYS B 2 485 ? 150.025 173.800 138.646 1.00 55.34  ? 476 LYS A CB  1 
ATOM   7064 C CG  . LYS B 2 485 ? 149.933 174.419 137.263 1.00 50.09  ? 476 LYS A CG  1 
ATOM   7065 C CD  . LYS B 2 485 ? 148.510 174.842 136.940 1.00 54.68  ? 476 LYS A CD  1 
ATOM   7066 C CE  . LYS B 2 485 ? 148.024 175.938 137.868 1.00 57.53  ? 476 LYS A CE  1 
ATOM   7067 N NZ  . LYS B 2 485 ? 147.146 176.907 137.158 1.00 56.76  ? 476 LYS A NZ  1 
ATOM   7068 N N   . ASN B 2 486 ? 149.730 170.898 138.853 1.00 57.52  ? 477 ASN A N   1 
ATOM   7069 C CA  . ASN B 2 486 ? 149.247 169.556 138.523 1.00 60.64  ? 477 ASN A CA  1 
ATOM   7070 C C   . ASN B 2 486 ? 150.326 168.501 138.757 1.00 60.95  ? 477 ASN A C   1 
ATOM   7071 O O   . ASN B 2 486 ? 150.566 167.633 137.917 1.00 60.52  ? 477 ASN A O   1 
ATOM   7072 C CB  . ASN B 2 486 ? 148.724 169.492 137.088 1.00 60.72  ? 477 ASN A CB  1 
ATOM   7073 C CG  . ASN B 2 486 ? 147.420 168.732 136.981 1.00 77.39  ? 477 ASN A CG  1 
ATOM   7074 O OD1 . ASN B 2 486 ? 147.329 167.574 137.386 1.00 72.46  ? 477 ASN A OD1 1 
ATOM   7075 N ND2 . ASN B 2 486 ? 146.399 169.383 136.438 1.00 79.88  ? 477 ASN A ND2 1 
ATOM   7076 N N   . ILE B 2 487 ? 150.980 168.576 139.911 1.00 54.37  ? 478 ILE A N   1 
ATOM   7077 C CA  . ILE B 2 487 ? 152.044 167.639 140.249 1.00 47.34  ? 478 ILE A CA  1 
ATOM   7078 C C   . ILE B 2 487 ? 151.422 166.350 140.764 1.00 51.41  ? 478 ILE A C   1 
ATOM   7079 O O   . ILE B 2 487 ? 150.581 166.368 141.670 1.00 56.21  ? 478 ILE A O   1 
ATOM   7080 C CB  . ILE B 2 487 ? 152.999 168.254 141.281 1.00 42.71  ? 478 ILE A CB  1 
ATOM   7081 C CG1 . ILE B 2 487 ? 153.431 169.646 140.821 1.00 40.64  ? 478 ILE A CG1 1 
ATOM   7082 C CG2 . ILE B 2 487 ? 154.205 167.352 141.484 1.00 39.29  ? 478 ILE A CG2 1 
ATOM   7083 C CD1 . ILE B 2 487 ? 154.665 170.167 141.499 1.00 39.99  ? 478 ILE A CD1 1 
ATOM   7084 N N   . GLN B 2 488 ? 151.832 165.229 140.185 1.00 57.66  ? 479 GLN A N   1 
ATOM   7085 C CA  . GLN B 2 488 ? 151.252 163.924 140.446 1.00 58.65  ? 479 GLN A CA  1 
ATOM   7086 C C   . GLN B 2 488 ? 152.200 163.093 141.304 1.00 58.68  ? 479 GLN A C   1 
ATOM   7087 O O   . GLN B 2 488 ? 153.250 163.566 141.750 1.00 61.50  ? 479 GLN A O   1 
ATOM   7088 C CB  . GLN B 2 488 ? 150.930 163.225 139.126 1.00 52.97  ? 479 GLN A CB  1 
ATOM   7089 C CG  . GLN B 2 488 ? 150.006 164.015 138.221 1.00 58.58  ? 479 GLN A CG  1 
ATOM   7090 C CD  . GLN B 2 488 ? 150.215 163.689 136.760 1.00 69.71  ? 479 GLN A CD  1 
ATOM   7091 O OE1 . GLN B 2 488 ? 150.447 162.537 136.398 1.00 68.62  ? 479 GLN A OE1 1 
ATOM   7092 N NE2 . GLN B 2 488 ? 150.145 164.707 135.910 1.00 72.71  ? 479 GLN A NE2 1 
ATOM   7093 N N   . ASP B 2 489 ? 151.818 161.841 141.539 1.00 56.80  ? 480 ASP A N   1 
ATOM   7094 C CA  . ASP B 2 489 ? 152.621 160.959 142.369 1.00 51.93  ? 480 ASP A CA  1 
ATOM   7095 C C   . ASP B 2 489 ? 153.938 160.629 141.682 1.00 50.59  ? 480 ASP A C   1 
ATOM   7096 O O   . ASP B 2 489 ? 153.981 160.346 140.483 1.00 55.26  ? 480 ASP A O   1 
ATOM   7097 C CB  . ASP B 2 489 ? 151.852 159.675 142.674 1.00 54.06  ? 480 ASP A CB  1 
ATOM   7098 C CG  . ASP B 2 489 ? 151.219 159.690 144.051 1.00 68.39  ? 480 ASP A CG  1 
ATOM   7099 O OD1 . ASP B 2 489 ? 151.524 160.609 144.837 1.00 70.38  ? 480 ASP A OD1 1 
ATOM   7100 O OD2 . ASP B 2 489 ? 150.410 158.785 144.345 1.00 75.66  ? 480 ASP A OD2 1 
ATOM   7101 N N   . ILE B 2 490 ? 155.018 160.670 142.455 1.00 43.61  ? 481 ILE A N   1 
ATOM   7102 C CA  . ILE B 2 490 ? 156.350 160.319 141.985 1.00 34.12  ? 481 ILE A CA  1 
ATOM   7103 C C   . ILE B 2 490 ? 156.819 159.127 142.802 1.00 38.97  ? 481 ILE A C   1 
ATOM   7104 O O   . ILE B 2 490 ? 156.705 159.132 144.032 1.00 48.31  ? 481 ILE A O   1 
ATOM   7105 C CB  . ILE B 2 490 ? 157.331 161.497 142.116 1.00 31.03  ? 481 ILE A CB  1 
ATOM   7106 C CG1 . ILE B 2 490 ? 156.856 162.681 141.272 1.00 28.45  ? 481 ILE A CG1 1 
ATOM   7107 C CG2 . ILE B 2 490 ? 158.723 161.075 141.690 1.00 27.86  ? 481 ILE A CG2 1 
ATOM   7108 C CD1 . ILE B 2 490 ? 157.910 163.731 141.040 1.00 19.69  ? 481 ILE A CD1 1 
ATOM   7109 N N   . SER B 2 491 ? 157.315 158.100 142.121 1.00 41.94  ? 482 SER A N   1 
ATOM   7110 C CA  . SER B 2 491 ? 157.816 156.901 142.787 1.00 35.95  ? 482 SER A CA  1 
ATOM   7111 C C   . SER B 2 491 ? 159.255 157.159 143.209 1.00 38.21  ? 482 SER A C   1 
ATOM   7112 O O   . SER B 2 491 ? 160.164 157.194 142.379 1.00 35.88  ? 482 SER A O   1 
ATOM   7113 C CB  . SER B 2 491 ? 157.706 155.691 141.872 1.00 40.06  ? 482 SER A CB  1 
ATOM   7114 O OG  . SER B 2 491 ? 156.369 155.226 141.823 1.00 46.82  ? 482 SER A OG  1 
ATOM   7115 N N   . TRP B 2 492 ? 159.460 157.342 144.508 1.00 40.51  ? 483 TRP A N   1 
ATOM   7116 C CA  . TRP B 2 492 ? 160.758 157.729 145.027 1.00 38.27  ? 483 TRP A CA  1 
ATOM   7117 C C   . TRP B 2 492 ? 161.602 156.498 145.350 1.00 41.94  ? 483 TRP A C   1 
ATOM   7118 O O   . TRP B 2 492 ? 161.093 155.417 145.657 1.00 45.50  ? 483 TRP A O   1 
ATOM   7119 C CB  . TRP B 2 492 ? 160.595 158.599 146.269 1.00 34.22  ? 483 TRP A CB  1 
ATOM   7120 C CG  . TRP B 2 492 ? 159.951 159.925 146.006 1.00 29.00  ? 483 TRP A CG  1 
ATOM   7121 C CD1 . TRP B 2 492 ? 158.759 160.359 146.495 1.00 29.52  ? 483 TRP A CD1 1 
ATOM   7122 C CD2 . TRP B 2 492 ? 160.463 160.988 145.197 1.00 27.26  ? 483 TRP A CD2 1 
ATOM   7123 N NE1 . TRP B 2 492 ? 158.495 161.624 146.044 1.00 28.90  ? 483 TRP A NE1 1 
ATOM   7124 C CE2 . TRP B 2 492 ? 159.528 162.035 145.247 1.00 24.58  ? 483 TRP A CE2 1 
ATOM   7125 C CE3 . TRP B 2 492 ? 161.624 161.158 144.439 1.00 28.63  ? 483 TRP A CE3 1 
ATOM   7126 C CZ2 . TRP B 2 492 ? 159.714 163.232 144.568 1.00 23.10  ? 483 TRP A CZ2 1 
ATOM   7127 C CZ3 . TRP B 2 492 ? 161.807 162.347 143.768 1.00 28.32  ? 483 TRP A CZ3 1 
ATOM   7128 C CH2 . TRP B 2 492 ? 160.858 163.369 143.836 1.00 25.06  ? 483 TRP A CH2 1 
ATOM   7129 N N   . HIS B 2 493 ? 162.917 156.681 145.287 1.00 39.92  ? 484 HIS A N   1 
ATOM   7130 C CA  . HIS B 2 493 ? 163.881 155.629 145.570 1.00 43.43  ? 484 HIS A CA  1 
ATOM   7131 C C   . HIS B 2 493 ? 164.048 155.359 147.057 1.00 47.32  ? 484 HIS A C   1 
ATOM   7132 O O   . HIS B 2 493 ? 164.761 154.422 147.425 1.00 51.87  ? 484 HIS A O   1 
ATOM   7133 C CB  . HIS B 2 493 ? 165.237 155.986 144.959 1.00 49.52  ? 484 HIS A CB  1 
ATOM   7134 C CG  . HIS B 2 493 ? 165.910 157.148 145.620 1.00 48.27  ? 484 HIS A CG  1 
ATOM   7135 N ND1 . HIS B 2 493 ? 165.417 158.431 145.546 1.00 40.07  ? 484 HIS A ND1 1 
ATOM   7136 C CD2 . HIS B 2 493 ? 167.040 157.221 146.359 1.00 52.34  ? 484 HIS A CD2 1 
ATOM   7137 C CE1 . HIS B 2 493 ? 166.213 159.246 146.213 1.00 42.47  ? 484 HIS A CE1 1 
ATOM   7138 N NE2 . HIS B 2 493 ? 167.205 158.537 146.717 1.00 48.13  ? 484 HIS A NE2 1 
ATOM   7139 N N   . THR B 2 494 ? 163.415 156.152 147.914 1.00 51.66  ? 485 THR A N   1 
ATOM   7140 C CA  . THR B 2 494 ? 163.531 155.984 149.352 1.00 52.28  ? 485 THR A CA  1 
ATOM   7141 C C   . THR B 2 494 ? 162.844 154.693 149.794 1.00 59.16  ? 485 THR A C   1 
ATOM   7142 O O   . THR B 2 494 ? 162.160 154.019 149.019 1.00 58.63  ? 485 THR A O   1 
ATOM   7143 C CB  . THR B 2 494 ? 162.941 157.193 150.069 1.00 51.37  ? 485 THR A CB  1 
ATOM   7144 O OG1 . THR B 2 494 ? 161.580 157.363 149.662 1.00 47.21  ? 485 THR A OG1 1 
ATOM   7145 C CG2 . THR B 2 494 ? 163.724 158.443 149.720 1.00 43.33  ? 485 THR A CG2 1 
ATOM   7146 N N   . ILE B 2 495 ? 163.032 154.344 151.069 1.00 64.91  ? 486 ILE A N   1 
ATOM   7147 C CA  . ILE B 2 495 ? 162.544 153.065 151.575 1.00 77.40  ? 486 ILE A CA  1 
ATOM   7148 C C   . ILE B 2 495 ? 161.021 153.032 151.604 1.00 74.80  ? 486 ILE A C   1 
ATOM   7149 O O   . ILE B 2 495 ? 160.404 152.007 151.290 1.00 75.64  ? 486 ILE A O   1 
ATOM   7150 C CB  . ILE B 2 495 ? 163.142 152.777 152.964 1.00 79.30  ? 486 ILE A CB  1 
ATOM   7151 C CG1 . ILE B 2 495 ? 164.663 152.922 152.930 1.00 77.38  ? 486 ILE A CG1 1 
ATOM   7152 C CG2 . ILE B 2 495 ? 162.756 151.383 153.432 1.00 75.36  ? 486 ILE A CG2 1 
ATOM   7153 C CD1 . ILE B 2 495 ? 165.344 151.983 151.958 1.00 75.66  ? 486 ILE A CD1 1 
ATOM   7154 N N   . ASN B 2 496 ? 160.387 154.142 151.975 1.00 70.23  ? 487 ASN A N   1 
ATOM   7155 C CA  . ASN B 2 496 ? 158.941 154.173 152.156 1.00 75.72  ? 487 ASN A CA  1 
ATOM   7156 C C   . ASN B 2 496 ? 158.281 155.186 151.226 1.00 66.54  ? 487 ASN A C   1 
ATOM   7157 O O   . ASN B 2 496 ? 157.200 155.699 151.523 1.00 64.84  ? 487 ASN A O   1 
ATOM   7158 C CB  . ASN B 2 496 ? 158.593 154.473 153.611 1.00 86.57  ? 487 ASN A CB  1 
ATOM   7159 C CG  . ASN B 2 496 ? 157.599 153.489 154.181 1.00 93.35  ? 487 ASN A CG  1 
ATOM   7160 O OD1 . ASN B 2 496 ? 156.674 153.050 153.498 1.00 86.36  ? 487 ASN A OD1 1 
ATOM   7161 N ND2 . ASN B 2 496 ? 157.799 153.122 155.440 1.00 102.17 ? 487 ASN A ND2 1 
ATOM   7162 N N   . ASN B 2 497 ? 158.933 155.480 150.100 1.00 56.93  ? 488 ASN A N   1 
ATOM   7163 C CA  . ASN B 2 497 ? 158.425 156.421 149.100 1.00 51.95  ? 488 ASN A CA  1 
ATOM   7164 C C   . ASN B 2 497 ? 158.203 157.810 149.690 1.00 50.43  ? 488 ASN A C   1 
ATOM   7165 O O   . ASN B 2 497 ? 157.344 158.567 149.235 1.00 53.49  ? 488 ASN A O   1 
ATOM   7166 C CB  . ASN B 2 497 ? 157.146 155.901 148.445 1.00 48.39  ? 488 ASN A CB  1 
ATOM   7167 C CG  . ASN B 2 497 ? 157.100 156.184 146.963 1.00 48.85  ? 488 ASN A CG  1 
ATOM   7168 O OD1 . ASN B 2 497 ? 156.671 157.254 146.536 1.00 41.37  ? 488 ASN A OD1 1 
ATOM   7169 N ND2 . ASN B 2 497 ? 157.547 155.222 146.166 1.00 44.90  ? 488 ASN A ND2 1 
ATOM   7170 N N   . THR B 2 498 ? 158.982 158.150 150.708 1.00 48.48  ? 489 THR A N   1 
ATOM   7171 C CA  . THR B 2 498 ? 158.982 159.499 151.244 1.00 45.33  ? 489 THR A CA  1 
ATOM   7172 C C   . THR B 2 498 ? 159.843 160.397 150.366 1.00 42.78  ? 489 THR A C   1 
ATOM   7173 O O   . THR B 2 498 ? 160.805 159.953 149.740 1.00 50.17  ? 489 THR A O   1 
ATOM   7174 C CB  . THR B 2 498 ? 159.494 159.515 152.685 1.00 47.58  ? 489 THR A CB  1 
ATOM   7175 O OG1 . THR B 2 498 ? 160.925 159.575 152.687 1.00 50.68  ? 489 THR A OG1 1 
ATOM   7176 C CG2 . THR B 2 498 ? 159.045 158.267 153.419 1.00 48.36  ? 489 THR A CG2 1 
ATOM   7177 N N   . ILE B 2 499 ? 159.477 161.669 150.312 1.00 35.19  ? 490 ILE A N   1 
ATOM   7178 C CA  . ILE B 2 499 ? 160.201 162.598 149.439 1.00 35.08  ? 490 ILE A CA  1 
ATOM   7179 C C   . ILE B 2 499 ? 161.647 162.703 149.910 1.00 37.20  ? 490 ILE A C   1 
ATOM   7180 O O   . ILE B 2 499 ? 161.891 162.919 151.109 1.00 46.59  ? 490 ILE A O   1 
ATOM   7181 C CB  . ILE B 2 499 ? 159.520 163.966 149.438 1.00 41.08  ? 490 ILE A CB  1 
ATOM   7182 C CG1 . ILE B 2 499 ? 158.032 163.814 149.133 1.00 38.38  ? 490 ILE A CG1 1 
ATOM   7183 C CG2 . ILE B 2 499 ? 160.171 164.879 148.419 1.00 35.94  ? 490 ILE A CG2 1 
ATOM   7184 C CD1 . ILE B 2 499 ? 157.195 164.943 149.659 1.00 35.45  ? 490 ILE A CD1 1 
ATOM   7185 N N   . PRO B 2 500 ? 162.628 162.544 149.023 1.00 34.79  ? 491 PRO A N   1 
ATOM   7186 C CA  . PRO B 2 500 ? 164.028 162.659 149.441 1.00 36.00  ? 491 PRO A CA  1 
ATOM   7187 C C   . PRO B 2 500 ? 164.336 164.045 149.980 1.00 37.46  ? 491 PRO A C   1 
ATOM   7188 O O   . PRO B 2 500 ? 163.728 165.038 149.581 1.00 45.63  ? 491 PRO A O   1 
ATOM   7189 C CB  . PRO B 2 500 ? 164.804 162.371 148.152 1.00 32.52  ? 491 PRO A CB  1 
ATOM   7190 C CG  . PRO B 2 500 ? 163.865 161.587 147.319 1.00 30.79  ? 491 PRO A CG  1 
ATOM   7191 C CD  . PRO B 2 500 ? 162.510 162.122 147.622 1.00 32.93  ? 491 PRO A CD  1 
ATOM   7192 N N   . MET B 2 501 ? 165.286 164.099 150.906 1.00 33.22  ? 492 MET A N   1 
ATOM   7193 C CA  . MET B 2 501 ? 165.675 165.338 151.562 1.00 36.64  ? 492 MET A CA  1 
ATOM   7194 C C   . MET B 2 501 ? 167.006 165.806 150.992 1.00 34.24  ? 492 MET A C   1 
ATOM   7195 O O   . MET B 2 501 ? 167.944 165.013 150.870 1.00 37.74  ? 492 MET A O   1 
ATOM   7196 C CB  . MET B 2 501 ? 165.778 165.139 153.072 1.00 39.77  ? 492 MET A CB  1 
ATOM   7197 C CG  . MET B 2 501 ? 164.614 164.379 153.671 1.00 43.60  ? 492 MET A CG  1 
ATOM   7198 S SD  . MET B 2 501 ? 163.175 165.424 153.942 1.00 76.84  ? 492 MET A SD  1 
ATOM   7199 C CE  . MET B 2 501 ? 163.935 166.814 154.772 1.00 50.47  ? 492 MET A CE  1 
ATOM   7200 N N   . SER B 2 502 ? 167.085 167.088 150.636 1.00 32.32  ? 493 SER A N   1 
ATOM   7201 C CA  . SER B 2 502 ? 168.331 167.687 150.156 1.00 28.30  ? 493 SER A CA  1 
ATOM   7202 C C   . SER B 2 502 ? 168.510 169.028 150.870 1.00 35.75  ? 493 SER A C   1 
ATOM   7203 O O   . SER B 2 502 ? 168.120 170.081 150.368 1.00 41.57  ? 493 SER A O   1 
ATOM   7204 C CB  . SER B 2 502 ? 168.313 167.834 148.649 1.00 28.50  ? 493 SER A CB  1 
ATOM   7205 O OG  . SER B 2 502 ? 169.627 167.899 148.142 1.00 28.54  ? 493 SER A OG  1 
ATOM   7206 N N   . MET B 2 503 ? 169.113 168.971 152.054 1.00 41.92  ? 494 MET A N   1 
ATOM   7207 C CA  . MET B 2 503 ? 169.407 170.134 152.876 1.00 40.20  ? 494 MET A CA  1 
ATOM   7208 C C   . MET B 2 503 ? 170.840 170.013 153.364 1.00 50.44  ? 494 MET A C   1 
ATOM   7209 O O   . MET B 2 503 ? 171.330 168.900 153.576 1.00 55.99  ? 494 MET A O   1 
ATOM   7210 C CB  . MET B 2 503 ? 168.471 170.226 154.087 1.00 39.01  ? 494 MET A CB  1 
ATOM   7211 C CG  . MET B 2 503 ? 166.987 170.214 153.780 1.00 38.51  ? 494 MET A CG  1 
ATOM   7212 S SD  . MET B 2 503 ? 166.247 171.832 154.040 1.00 69.70  ? 494 MET A SD  1 
ATOM   7213 C CE  . MET B 2 503 ? 164.728 171.676 153.114 1.00 47.19  ? 494 MET A CE  1 
ATOM   7214 N N   . CYS B 2 504 ? 171.517 171.148 153.537 1.00 46.59  ? 495 CYS A N   1 
ATOM   7215 C CA  . CYS B 2 504 ? 172.819 171.085 154.186 1.00 52.45  ? 495 CYS A CA  1 
ATOM   7216 C C   . CYS B 2 504 ? 172.740 171.387 155.671 1.00 63.96  ? 495 CYS A C   1 
ATOM   7217 O O   . CYS B 2 504 ? 173.769 171.327 156.353 1.00 70.44  ? 495 CYS A O   1 
ATOM   7218 C CB  . CYS B 2 504 ? 173.820 172.042 153.534 1.00 46.80  ? 495 CYS A CB  1 
ATOM   7219 S SG  . CYS B 2 504 ? 173.485 173.806 153.670 1.00 67.13  ? 495 CYS A SG  1 
ATOM   7220 N N   . SER B 2 505 ? 171.554 171.703 156.186 1.00 62.30  ? 496 SER A N   1 
ATOM   7221 C CA  . SER B 2 505 ? 171.434 172.161 157.561 1.00 60.03  ? 496 SER A CA  1 
ATOM   7222 C C   . SER B 2 505 ? 170.041 171.847 158.078 1.00 69.12  ? 496 SER A C   1 
ATOM   7223 O O   . SER B 2 505 ? 169.054 172.384 157.568 1.00 64.47  ? 496 SER A O   1 
ATOM   7224 C CB  . SER B 2 505 ? 171.713 173.658 157.647 1.00 61.67  ? 496 SER A CB  1 
ATOM   7225 O OG  . SER B 2 505 ? 173.102 173.897 157.575 1.00 57.20  ? 496 SER A OG  1 
ATOM   7226 N N   . LYS B 2 506 ? 169.968 170.984 159.087 1.00 79.86  ? 497 LYS A N   1 
ATOM   7227 C CA  . LYS B 2 506 ? 168.698 170.698 159.736 1.00 83.54  ? 497 LYS A CA  1 
ATOM   7228 C C   . LYS B 2 506 ? 168.157 171.954 160.405 1.00 85.94  ? 497 LYS A C   1 
ATOM   7229 O O   . LYS B 2 506 ? 168.907 172.732 161.001 1.00 87.53  ? 497 LYS A O   1 
ATOM   7230 C CB  . LYS B 2 506 ? 168.867 169.579 160.762 1.00 88.75  ? 497 LYS A CB  1 
ATOM   7231 C CG  . LYS B 2 506 ? 167.596 169.234 161.521 1.00 96.63  ? 497 LYS A CG  1 
ATOM   7232 C CD  . LYS B 2 506 ? 166.764 168.207 160.771 1.00 95.07  ? 497 LYS A CD  1 
ATOM   7233 C CE  . LYS B 2 506 ? 166.194 167.163 161.717 1.00 92.04  ? 497 LYS A CE  1 
ATOM   7234 N NZ  . LYS B 2 506 ? 165.484 167.784 162.869 1.00 83.40  ? 497 LYS A NZ  1 
ATOM   7235 N N   . LYS B 2 515 ? 174.131 180.483 163.486 1.00 85.11  ? 506 LYS A N   1 
ATOM   7236 C CA  . LYS B 2 515 ? 175.295 181.142 162.912 1.00 80.21  ? 506 LYS A CA  1 
ATOM   7237 C C   . LYS B 2 515 ? 175.678 180.521 161.566 1.00 83.52  ? 506 LYS A C   1 
ATOM   7238 O O   . LYS B 2 515 ? 175.774 179.296 161.443 1.00 88.58  ? 506 LYS A O   1 
ATOM   7239 C CB  . LYS B 2 515 ? 176.466 181.058 163.897 1.00 78.61  ? 506 LYS A CB  1 
ATOM   7240 C CG  . LYS B 2 515 ? 176.914 179.634 164.205 1.00 82.62  ? 506 LYS A CG  1 
ATOM   7241 C CD  . LYS B 2 515 ? 178.287 179.563 164.841 1.00 89.88  ? 506 LYS A CD  1 
ATOM   7242 C CE  . LYS B 2 515 ? 179.391 179.727 163.815 1.00 89.17  ? 506 LYS A CE  1 
ATOM   7243 N NZ  . LYS B 2 515 ? 180.666 180.096 164.483 1.00 81.47  ? 506 LYS A NZ  1 
ATOM   7244 N N   . PRO B 2 516 ? 175.853 181.335 160.526 1.00 80.09  ? 507 PRO A N   1 
ATOM   7245 C CA  . PRO B 2 516 ? 176.197 180.788 159.211 1.00 79.67  ? 507 PRO A CA  1 
ATOM   7246 C C   . PRO B 2 516 ? 177.585 180.171 159.173 1.00 79.44  ? 507 PRO A C   1 
ATOM   7247 O O   . PRO B 2 516 ? 178.501 180.579 159.891 1.00 84.01  ? 507 PRO A O   1 
ATOM   7248 C CB  . PRO B 2 516 ? 176.125 182.012 158.292 1.00 82.33  ? 507 PRO A CB  1 
ATOM   7249 C CG  . PRO B 2 516 ? 175.199 182.950 158.976 1.00 78.67  ? 507 PRO A CG  1 
ATOM   7250 C CD  . PRO B 2 516 ? 175.470 182.757 160.440 1.00 80.15  ? 507 PRO A CD  1 
ATOM   7251 N N   . VAL B 2 517 ? 177.725 179.166 158.311 1.00 77.51  ? 508 VAL A N   1 
ATOM   7252 C CA  . VAL B 2 517 ? 179.010 178.552 158.001 1.00 81.74  ? 508 VAL A CA  1 
ATOM   7253 C C   . VAL B 2 517 ? 179.175 178.548 156.488 1.00 81.99  ? 508 VAL A C   1 
ATOM   7254 O O   . VAL B 2 517 ? 178.248 178.183 155.757 1.00 81.47  ? 508 VAL A O   1 
ATOM   7255 C CB  . VAL B 2 517 ? 179.129 177.128 158.583 1.00 83.28  ? 508 VAL A CB  1 
ATOM   7256 C CG1 . VAL B 2 517 ? 178.009 176.232 158.090 1.00 75.39  ? 508 VAL A CG1 1 
ATOM   7257 C CG2 . VAL B 2 517 ? 180.480 176.525 158.239 1.00 80.50  ? 508 VAL A CG2 1 
ATOM   7258 N N   . GLY B 2 518 ? 180.334 178.992 156.018 1.00 80.66  ? 509 GLY A N   1 
ATOM   7259 C CA  . GLY B 2 518 ? 180.620 179.012 154.602 1.00 76.10  ? 509 GLY A CA  1 
ATOM   7260 C C   . GLY B 2 518 ? 179.960 180.173 153.879 1.00 66.98  ? 509 GLY A C   1 
ATOM   7261 O O   . GLY B 2 518 ? 179.334 181.056 154.468 1.00 58.75  ? 509 GLY A O   1 
ATOM   7262 N N   . ILE B 2 519 ? 180.117 180.159 152.555 1.00 59.61  ? 510 ILE A N   1 
ATOM   7263 C CA  . ILE B 2 519 ? 179.559 181.219 151.721 1.00 60.09  ? 510 ILE A CA  1 
ATOM   7264 C C   . ILE B 2 519 ? 178.051 181.050 151.558 1.00 61.65  ? 510 ILE A C   1 
ATOM   7265 O O   . ILE B 2 519 ? 177.317 182.034 151.415 1.00 64.35  ? 510 ILE A O   1 
ATOM   7266 C CB  . ILE B 2 519 ? 180.289 181.266 150.366 1.00 63.99  ? 510 ILE A CB  1 
ATOM   7267 C CG1 . ILE B 2 519 ? 179.894 180.079 149.487 1.00 61.37  ? 510 ILE A CG1 1 
ATOM   7268 C CG2 . ILE B 2 519 ? 181.795 181.282 150.580 1.00 60.07  ? 510 ILE A CG2 1 
ATOM   7269 C CD1 . ILE B 2 519 ? 179.673 180.439 148.040 1.00 56.29  ? 510 ILE A CD1 1 
ATOM   7270 N N   . HIS B 2 520 ? 177.566 179.810 151.562 1.00 59.51  ? 511 HIS A N   1 
ATOM   7271 C CA  . HIS B 2 520 ? 176.160 179.554 151.280 1.00 58.50  ? 511 HIS A CA  1 
ATOM   7272 C C   . HIS B 2 520 ? 175.265 179.998 152.429 1.00 59.35  ? 511 HIS A C   1 
ATOM   7273 O O   . HIS B 2 520 ? 175.549 179.737 153.600 1.00 65.76  ? 511 HIS A O   1 
ATOM   7274 C CB  . HIS B 2 520 ? 175.941 178.072 150.982 1.00 55.72  ? 511 HIS A CB  1 
ATOM   7275 C CG  . HIS B 2 520 ? 176.854 177.532 149.927 1.00 49.23  ? 511 HIS A CG  1 
ATOM   7276 N ND1 . HIS B 2 520 ? 177.903 176.685 150.209 1.00 50.88  ? 511 HIS A ND1 1 
ATOM   7277 C CD2 . HIS B 2 520 ? 176.878 177.727 148.588 1.00 44.39  ? 511 HIS A CD2 1 
ATOM   7278 C CE1 . HIS B 2 520 ? 178.532 176.379 149.089 1.00 47.37  ? 511 HIS A CE1 1 
ATOM   7279 N NE2 . HIS B 2 520 ? 177.929 176.998 148.091 1.00 45.58  ? 511 HIS A NE2 1 
ATOM   7280 N N   . VAL B 2 521 ? 174.172 180.676 152.078 1.00 58.68  ? 512 VAL A N   1 
ATOM   7281 C CA  . VAL B 2 521 ? 173.210 181.125 153.080 1.00 66.81  ? 512 VAL A CA  1 
ATOM   7282 C C   . VAL B 2 521 ? 172.417 179.944 153.626 1.00 65.60  ? 512 VAL A C   1 
ATOM   7283 O O   . VAL B 2 521 ? 172.040 179.920 154.804 1.00 67.52  ? 512 VAL A O   1 
ATOM   7284 C CB  . VAL B 2 521 ? 172.295 182.210 152.483 1.00 68.15  ? 512 VAL A CB  1 
ATOM   7285 C CG1 . VAL B 2 521 ? 171.784 181.786 151.119 1.00 66.16  ? 512 VAL A CG1 1 
ATOM   7286 C CG2 . VAL B 2 521 ? 171.136 182.518 153.417 1.00 63.63  ? 512 VAL A CG2 1 
ATOM   7287 N N   . CYS B 2 522 ? 172.159 178.943 152.785 1.00 65.79  ? 513 CYS A N   1 
ATOM   7288 C CA  . CYS B 2 522 ? 171.394 177.769 153.183 1.00 63.30  ? 513 CYS A CA  1 
ATOM   7289 C C   . CYS B 2 522 ? 172.082 176.953 154.268 1.00 64.33  ? 513 CYS A C   1 
ATOM   7290 O O   . CYS B 2 522 ? 171.423 176.127 154.907 1.00 60.41  ? 513 CYS A O   1 
ATOM   7291 C CB  . CYS B 2 522 ? 171.139 176.876 151.967 1.00 55.92  ? 513 CYS A CB  1 
ATOM   7292 S SG  . CYS B 2 522 ? 170.572 177.734 150.485 1.00 74.06  ? 513 CYS A SG  1 
ATOM   7293 N N   . CYS B 2 523 ? 173.376 177.161 154.488 1.00 61.11  ? 514 CYS A N   1 
ATOM   7294 C CA  . CYS B 2 523 ? 174.171 176.326 155.374 1.00 62.15  ? 514 CYS A CA  1 
ATOM   7295 C C   . CYS B 2 523 ? 174.465 177.075 156.667 1.00 70.00  ? 514 CYS A C   1 
ATOM   7296 O O   . CYS B 2 523 ? 174.882 178.237 156.635 1.00 76.54  ? 514 CYS A O   1 
ATOM   7297 C CB  . CYS B 2 523 ? 175.477 175.924 154.691 1.00 62.59  ? 514 CYS A CB  1 
ATOM   7298 S SG  . CYS B 2 523 ? 175.335 174.620 153.442 1.00 74.76  ? 514 CYS A SG  1 
ATOM   7299 N N   . PHE B 2 524 ? 174.247 176.409 157.795 1.00 74.71  ? 515 PHE A N   1 
ATOM   7300 C CA  . PHE B 2 524 ? 174.529 176.968 159.110 1.00 75.98  ? 515 PHE A CA  1 
ATOM   7301 C C   . PHE B 2 524 ? 174.704 175.810 160.085 1.00 79.62  ? 515 PHE A C   1 
ATOM   7302 O O   . PHE B 2 524 ? 174.521 174.643 159.730 1.00 78.73  ? 515 PHE A O   1 
ATOM   7303 C CB  . PHE B 2 524 ? 173.417 177.920 159.561 1.00 72.65  ? 515 PHE A CB  1 
ATOM   7304 C CG  . PHE B 2 524 ? 172.034 177.352 159.419 1.00 72.46  ? 515 PHE A CG  1 
ATOM   7305 C CD1 . PHE B 2 524 ? 171.545 176.439 160.338 1.00 72.10  ? 515 PHE A CD1 1 
ATOM   7306 C CD2 . PHE B 2 524 ? 171.222 177.730 158.365 1.00 72.83  ? 515 PHE A CD2 1 
ATOM   7307 C CE1 . PHE B 2 524 ? 170.275 175.917 160.209 1.00 68.70  ? 515 PHE A CE1 1 
ATOM   7308 C CE2 . PHE B 2 524 ? 169.950 177.208 158.230 1.00 70.29  ? 515 PHE A CE2 1 
ATOM   7309 C CZ  . PHE B 2 524 ? 169.477 176.301 159.154 1.00 66.74  ? 515 PHE A CZ  1 
HETATM 7310 C C1  . NAG C 3 .   ? 211.817 180.219 127.722 1.00 85.62  ? 601 NAG B C1  1 
HETATM 7311 C C2  . NAG C 3 .   ? 212.905 179.667 126.795 1.00 88.89  ? 601 NAG B C2  1 
HETATM 7312 C C3  . NAG C 3 .   ? 213.913 178.848 127.595 1.00 88.50  ? 601 NAG B C3  1 
HETATM 7313 C C4  . NAG C 3 .   ? 214.436 179.654 128.777 1.00 92.11  ? 601 NAG B C4  1 
HETATM 7314 C C5  . NAG C 3 .   ? 213.246 180.152 129.602 1.00 91.40  ? 601 NAG B C5  1 
HETATM 7315 C C6  . NAG C 3 .   ? 213.636 180.967 130.816 1.00 86.20  ? 601 NAG B C6  1 
HETATM 7316 C C7  . NAG C 3 .   ? 212.213 179.256 124.467 1.00 97.20  ? 601 NAG B C7  1 
HETATM 7317 C C8  . NAG C 3 .   ? 211.556 178.253 123.552 1.00 93.53  ? 601 NAG B C8  1 
HETATM 7318 N N2  . NAG C 3 .   ? 212.316 178.872 125.752 1.00 97.13  ? 601 NAG B N2  1 
HETATM 7319 O O3  . NAG C 3 .   ? 214.945 178.469 126.726 1.00 97.27  ? 601 NAG B O3  1 
HETATM 7320 O O4  . NAG C 3 .   ? 215.276 178.804 129.523 1.00 89.29  ? 601 NAG B O4  1 
HETATM 7321 O O5  . NAG C 3 .   ? 212.419 180.939 128.770 1.00 92.23  ? 601 NAG B O5  1 
HETATM 7322 O O6  . NAG C 3 .   ? 212.485 181.511 131.415 1.00 74.16  ? 601 NAG B O6  1 
HETATM 7323 O O7  . NAG C 3 .   ? 212.614 180.333 124.051 1.00 92.26  ? 601 NAG B O7  1 
HETATM 7324 C C1  . NAG D 3 .   ? 180.398 204.788 140.393 1.00 85.70  ? 602 NAG B C1  1 
HETATM 7325 C C2  . NAG D 3 .   ? 179.680 205.628 139.331 1.00 85.74  ? 602 NAG B C2  1 
HETATM 7326 C C3  . NAG D 3 .   ? 178.739 206.617 140.016 1.00 94.03  ? 602 NAG B C3  1 
HETATM 7327 C C4  . NAG D 3 .   ? 177.831 205.912 141.020 1.00 97.00  ? 602 NAG B C4  1 
HETATM 7328 C C5  . NAG D 3 .   ? 178.689 205.084 141.981 1.00 93.47  ? 602 NAG B C5  1 
HETATM 7329 C C6  . NAG D 3 .   ? 177.903 204.329 143.031 1.00 89.36  ? 602 NAG B C6  1 
HETATM 7330 C C7  . NAG D 3 .   ? 180.694 206.257 137.175 1.00 86.34  ? 602 NAG B C7  1 
HETATM 7331 C C8  . NAG D 3 .   ? 181.785 207.083 136.539 1.00 79.16  ? 602 NAG B C8  1 
HETATM 7332 N N2  . NAG D 3 .   ? 180.634 206.330 138.517 1.00 83.93  ? 602 NAG B N2  1 
HETATM 7333 O O3  . NAG D 3 .   ? 178.007 207.273 139.016 1.00 98.26  ? 602 NAG B O3  1 
HETATM 7334 O O4  . NAG D 3 .   ? 177.102 206.906 141.700 1.00 96.58  ? 602 NAG B O4  1 
HETATM 7335 O O5  . NAG D 3 .   ? 179.444 204.165 141.222 1.00 88.45  ? 602 NAG B O5  1 
HETATM 7336 O O6  . NAG D 3 .   ? 176.948 203.500 142.414 1.00 89.43  ? 602 NAG B O6  1 
HETATM 7337 O O7  . NAG D 3 .   ? 179.929 205.582 136.504 1.00 88.97  ? 602 NAG B O7  1 
HETATM 7338 C C1  . NAG E 3 .   ? 183.903 192.431 153.614 1.00 98.02  ? 603 NAG B C1  1 
HETATM 7339 C C2  . NAG E 3 .   ? 182.751 193.056 154.412 1.00 100.51 ? 603 NAG B C2  1 
HETATM 7340 C C3  . NAG E 3 .   ? 183.312 193.750 155.651 1.00 97.14  ? 603 NAG B C3  1 
HETATM 7341 C C4  . NAG E 3 .   ? 184.186 192.787 156.449 1.00 101.55 ? 603 NAG B C4  1 
HETATM 7342 C C5  . NAG E 3 .   ? 185.234 192.151 155.528 1.00 100.01 ? 603 NAG B C5  1 
HETATM 7343 C C6  . NAG E 3 .   ? 186.124 191.139 156.214 1.00 100.98 ? 603 NAG B C6  1 
HETATM 7344 C C7  . NAG E 3 .   ? 182.377 195.045 152.938 1.00 104.86 ? 603 NAG B C7  1 
HETATM 7345 C C8  . NAG E 3 .   ? 181.290 195.772 152.186 1.00 92.15  ? 603 NAG B C8  1 
HETATM 7346 N N2  . NAG E 3 .   ? 181.955 193.953 153.608 1.00 105.27 ? 603 NAG B N2  1 
HETATM 7347 O O3  . NAG E 3 .   ? 182.232 194.227 156.408 1.00 89.01  ? 603 NAG B O3  1 
HETATM 7348 O O4  . NAG E 3 .   ? 184.785 193.528 157.486 1.00 99.23  ? 603 NAG B O4  1 
HETATM 7349 O O5  . NAG E 3 .   ? 184.581 191.519 154.446 1.00 98.42  ? 603 NAG B O5  1 
HETATM 7350 O O6  . NAG E 3 .   ? 185.340 190.090 156.728 1.00 97.56  ? 603 NAG B O6  1 
HETATM 7351 O O7  . NAG E 3 .   ? 183.531 195.449 152.917 1.00 101.48 ? 603 NAG B O7  1 
HETATM 7352 C C1  . NAG F 3 .   ? 213.531 180.631 89.317  1.00 96.43  ? 604 NAG B C1  1 
HETATM 7353 C C2  . NAG F 3 .   ? 214.267 179.436 88.691  1.00 100.62 ? 604 NAG B C2  1 
HETATM 7354 C C3  . NAG F 3 .   ? 214.518 179.669 87.202  1.00 100.31 ? 604 NAG B C3  1 
HETATM 7355 C C4  . NAG F 3 .   ? 213.220 180.055 86.508  1.00 102.73 ? 604 NAG B C4  1 
HETATM 7356 C C5  . NAG F 3 .   ? 212.610 181.255 87.237  1.00 98.10  ? 604 NAG B C5  1 
HETATM 7357 C C6  . NAG F 3 .   ? 211.332 181.768 86.613  1.00 93.24  ? 604 NAG B C6  1 
HETATM 7358 C C7  . NAG F 3 .   ? 216.573 179.930 89.516  1.00 102.08 ? 604 NAG B C7  1 
HETATM 7359 C C8  . NAG F 3 .   ? 217.696 179.328 90.324  1.00 90.70  ? 604 NAG B C8  1 
HETATM 7360 N N2  . NAG F 3 .   ? 215.489 179.137 89.398  1.00 99.88  ? 604 NAG B N2  1 
HETATM 7361 O O3  . NAG F 3 .   ? 215.073 178.496 86.668  1.00 94.56  ? 604 NAG B O3  1 
HETATM 7362 O O4  . NAG F 3 .   ? 213.532 180.353 85.167  1.00 96.58  ? 604 NAG B O4  1 
HETATM 7363 O O5  . NAG F 3 .   ? 212.359 180.892 88.581  1.00 96.81  ? 604 NAG B O5  1 
HETATM 7364 O O6  . NAG F 3 .   ? 210.379 180.734 86.560  1.00 92.78  ? 604 NAG B O6  1 
HETATM 7365 O O7  . NAG F 3 .   ? 216.675 181.045 89.023  1.00 104.65 ? 604 NAG B O7  1 
HETATM 7366 C C1  . NAG G 3 .   ? 208.548 201.649 97.080  1.00 87.84  ? 605 NAG B C1  1 
HETATM 7367 C C2  . NAG G 3 .   ? 208.330 202.586 98.275  1.00 85.77  ? 605 NAG B C2  1 
HETATM 7368 C C3  . NAG G 3 .   ? 208.245 204.039 97.813  1.00 86.48  ? 605 NAG B C3  1 
HETATM 7369 C C4  . NAG G 3 .   ? 209.391 204.396 96.874  1.00 92.48  ? 605 NAG B C4  1 
HETATM 7370 C C5  . NAG G 3 .   ? 209.443 203.370 95.741  1.00 93.94  ? 605 NAG B C5  1 
HETATM 7371 C C6  . NAG G 3 .   ? 210.532 203.628 94.722  1.00 97.95  ? 605 NAG B C6  1 
HETATM 7372 C C7  . NAG G 3 .   ? 207.049 201.548 100.137 1.00 82.10  ? 605 NAG B C7  1 
HETATM 7373 C C8  . NAG G 3 .   ? 208.364 201.126 100.743 1.00 81.85  ? 605 NAG B C8  1 
HETATM 7374 N N2  . NAG G 3 .   ? 207.126 202.228 98.977  1.00 83.91  ? 605 NAG B N2  1 
HETATM 7375 O O3  . NAG G 3 .   ? 208.231 204.854 98.954  1.00 83.40  ? 605 NAG B O3  1 
HETATM 7376 O O4  . NAG G 3 .   ? 209.143 205.695 96.389  1.00 90.77  ? 605 NAG B O4  1 
HETATM 7377 O O5  . NAG G 3 .   ? 209.642 202.093 96.311  1.00 87.88  ? 605 NAG B O5  1 
HETATM 7378 O O6  . NAG G 3 .   ? 210.540 202.601 93.759  1.00 92.59  ? 605 NAG B O6  1 
HETATM 7379 O O7  . NAG G 3 .   ? 205.989 201.279 100.681 1.00 79.49  ? 605 NAG B O7  1 
HETATM 7380 C C1  . NAG H 3 .   ? 182.584 167.587 95.914  1.00 116.38 ? 606 NAG B C1  1 
HETATM 7381 C C2  . NAG H 3 .   ? 183.240 166.249 96.278  1.00 117.67 ? 606 NAG B C2  1 
HETATM 7382 C C3  . NAG H 3 .   ? 183.356 165.369 95.037  1.00 117.68 ? 606 NAG B C3  1 
HETATM 7383 C C4  . NAG H 3 .   ? 182.010 165.263 94.329  1.00 121.88 ? 606 NAG B C4  1 
HETATM 7384 C C5  . NAG H 3 .   ? 181.458 166.670 94.069  1.00 119.16 ? 606 NAG B C5  1 
HETATM 7385 C C6  . NAG H 3 .   ? 180.119 166.691 93.365  1.00 115.33 ? 606 NAG B C6  1 
HETATM 7386 C C7  . NAG H 3 .   ? 184.859 166.194 98.154  1.00 122.69 ? 606 NAG B C7  1 
HETATM 7387 C C8  . NAG H 3 .   ? 183.760 165.594 98.998  1.00 123.65 ? 606 NAG B C8  1 
HETATM 7388 N N2  . NAG H 3 .   ? 184.530 166.472 96.877  1.00 120.51 ? 606 NAG B N2  1 
HETATM 7389 O O3  . NAG H 3 .   ? 183.836 164.115 95.443  1.00 113.94 ? 606 NAG B O3  1 
HETATM 7390 O O4  . NAG H 3 .   ? 182.224 164.551 93.131  1.00 122.56 ? 606 NAG B O4  1 
HETATM 7391 O O5  . NAG H 3 .   ? 181.338 167.349 95.304  1.00 118.85 ? 606 NAG B O5  1 
HETATM 7392 O O6  . NAG H 3 .   ? 180.280 166.301 92.022  1.00 114.70 ? 606 NAG B O6  1 
HETATM 7393 O O7  . NAG H 3 .   ? 185.969 166.403 98.620  1.00 115.79 ? 606 NAG B O7  1 
HETATM 7394 C C1  . NAG I 3 .   ? 187.726 215.397 111.995 1.00 124.99 ? 607 NAG B C1  1 
HETATM 7395 C C2  . NAG I 3 .   ? 186.363 214.688 112.031 1.00 124.44 ? 607 NAG B C2  1 
HETATM 7396 C C3  . NAG I 3 .   ? 185.266 215.718 112.291 1.00 125.89 ? 607 NAG B C3  1 
HETATM 7397 C C4  . NAG I 3 .   ? 185.582 216.532 113.538 1.00 127.35 ? 607 NAG B C4  1 
HETATM 7398 C C5  . NAG I 3 .   ? 186.971 217.156 113.385 1.00 129.62 ? 607 NAG B C5  1 
HETATM 7399 C C6  . NAG I 3 .   ? 187.399 217.976 114.581 1.00 131.10 ? 607 NAG B C6  1 
HETATM 7400 C C7  . NAG I 3 .   ? 185.602 212.743 110.705 1.00 114.11 ? 607 NAG B C7  1 
HETATM 7401 C C8  . NAG I 3 .   ? 185.329 212.047 112.017 1.00 105.08 ? 607 NAG B C8  1 
HETATM 7402 N N2  . NAG I 3 .   ? 186.093 213.994 110.800 1.00 119.87 ? 607 NAG B N2  1 
HETATM 7403 O O3  . NAG I 3 .   ? 184.044 215.039 112.406 1.00 125.40 ? 607 NAG B O3  1 
HETATM 7404 O O4  . NAG I 3 .   ? 184.579 217.513 113.660 1.00 126.91 ? 607 NAG B O4  1 
HETATM 7405 O O5  . NAG I 3 .   ? 187.915 216.126 113.188 1.00 124.82 ? 607 NAG B O5  1 
HETATM 7406 O O6  . NAG I 3 .   ? 187.264 217.204 115.750 1.00 127.85 ? 607 NAG B O6  1 
HETATM 7407 O O7  . NAG I 3 .   ? 185.382 212.191 109.637 1.00 109.86 ? 607 NAG B O7  1 
HETATM 7408 C C1  . NAG J 3 .   ? 206.509 172.144 111.061 1.00 90.19  ? 608 NAG B C1  1 
HETATM 7409 C C2  . NAG J 3 .   ? 207.848 172.851 110.819 1.00 90.02  ? 608 NAG B C2  1 
HETATM 7410 C C3  . NAG J 3 .   ? 208.971 171.919 111.267 1.00 96.80  ? 608 NAG B C3  1 
HETATM 7411 C C4  . NAG J 3 .   ? 208.745 171.432 112.697 1.00 102.88 ? 608 NAG B C4  1 
HETATM 7412 C C5  . NAG J 3 .   ? 207.327 170.867 112.846 1.00 104.11 ? 608 NAG B C5  1 
HETATM 7413 C C6  . NAG J 3 .   ? 206.976 170.430 114.251 1.00 98.73  ? 608 NAG B C6  1 
HETATM 7414 C C7  . NAG J 3 .   ? 208.270 174.442 108.969 1.00 88.58  ? 608 NAG B C7  1 
HETATM 7415 C C8  . NAG J 3 .   ? 208.385 175.520 110.019 1.00 79.91  ? 608 NAG B C8  1 
HETATM 7416 N N2  . NAG J 3 .   ? 208.014 173.203 109.433 1.00 90.37  ? 608 NAG B N2  1 
HETATM 7417 O O3  . NAG J 3 .   ? 210.186 172.607 111.129 1.00 95.13  ? 608 NAG B O3  1 
HETATM 7418 O O4  . NAG J 3 .   ? 209.720 170.448 112.956 1.00 101.43 ? 608 NAG B O4  1 
HETATM 7419 O O5  . NAG J 3 .   ? 206.394 171.843 112.432 1.00 99.58  ? 608 NAG B O5  1 
HETATM 7420 O O6  . NAG J 3 .   ? 207.038 171.533 115.125 1.00 90.58  ? 608 NAG B O6  1 
HETATM 7421 O O7  . NAG J 3 .   ? 208.405 174.699 107.782 1.00 88.61  ? 608 NAG B O7  1 
HETATM 7422 C C1  . NAG K 3 .   ? 156.949 152.178 156.117 1.00 114.41 ? 601 NAG A C1  1 
HETATM 7423 C C2  . NAG K 3 .   ? 157.431 151.960 157.555 1.00 114.19 ? 601 NAG A C2  1 
HETATM 7424 C C3  . NAG K 3 .   ? 156.555 150.910 158.231 1.00 117.34 ? 601 NAG A C3  1 
HETATM 7425 C C4  . NAG K 3 .   ? 155.081 151.275 158.095 1.00 122.60 ? 601 NAG A C4  1 
HETATM 7426 C C5  . NAG K 3 .   ? 154.749 151.539 156.621 1.00 119.66 ? 601 NAG A C5  1 
HETATM 7427 C C6  . NAG K 3 .   ? 153.310 151.931 156.370 1.00 114.82 ? 601 NAG A C6  1 
HETATM 7428 C C7  . NAG K 3 .   ? 159.842 152.377 157.862 1.00 116.45 ? 601 NAG A C7  1 
HETATM 7429 C C8  . NAG K 3 .   ? 161.204 151.730 157.806 1.00 113.49 ? 601 NAG A C8  1 
HETATM 7430 N N2  . NAG K 3 .   ? 158.813 151.562 157.564 1.00 113.90 ? 601 NAG A N2  1 
HETATM 7431 O O3  . NAG K 3 .   ? 156.953 150.810 159.573 1.00 114.02 ? 601 NAG A O3  1 
HETATM 7432 O O4  . NAG K 3 .   ? 154.338 150.194 158.609 1.00 120.85 ? 601 NAG A O4  1 
HETATM 7433 O O5  . NAG K 3 .   ? 155.594 152.563 156.131 1.00 120.64 ? 601 NAG A O5  1 
HETATM 7434 O O6  . NAG K 3 .   ? 152.973 153.046 157.160 1.00 116.44 ? 601 NAG A O6  1 
HETATM 7435 O O7  . NAG K 3 .   ? 159.707 153.555 158.156 1.00 112.71 ? 601 NAG A O7  1 
HETATM 7436 C C1  . NAG L 3 .   ? 145.379 163.071 102.924 1.00 86.93  ? 602 NAG A C1  1 
HETATM 7437 C C2  . NAG L 3 .   ? 145.607 162.607 101.472 1.00 91.87  ? 602 NAG A C2  1 
HETATM 7438 C C3  . NAG L 3 .   ? 146.026 161.134 101.429 1.00 100.57 ? 602 NAG A C3  1 
HETATM 7439 C C4  . NAG L 3 .   ? 147.122 160.820 102.440 1.00 105.62 ? 602 NAG A C4  1 
HETATM 7440 C C5  . NAG L 3 .   ? 146.698 161.337 103.814 1.00 104.10 ? 602 NAG A C5  1 
HETATM 7441 C C6  . NAG L 3 .   ? 147.700 161.026 104.905 1.00 100.67 ? 602 NAG A C6  1 
HETATM 7442 C C7  . NAG L 3 .   ? 143.239 162.207 100.779 1.00 99.23  ? 602 NAG A C7  1 
HETATM 7443 C C8  . NAG L 3 .   ? 142.217 162.625 99.752  1.00 87.45  ? 602 NAG A C8  1 
HETATM 7444 N N2  . NAG L 3 .   ? 144.441 162.808 100.647 1.00 96.94  ? 602 NAG A N2  1 
HETATM 7445 O O3  . NAG L 3 .   ? 146.426 160.833 100.118 1.00 100.52 ? 602 NAG A O3  1 
HETATM 7446 O O4  . NAG L 3 .   ? 147.300 159.422 102.450 1.00 101.75 ? 602 NAG A O4  1 
HETATM 7447 O O5  . NAG L 3 .   ? 146.499 162.735 103.715 1.00 90.42  ? 602 NAG A O5  1 
HETATM 7448 O O6  . NAG L 3 .   ? 147.047 160.939 106.149 1.00 104.02 ? 602 NAG A O6  1 
HETATM 7449 O O7  . NAG L 3 .   ? 142.956 161.391 101.645 1.00 98.07  ? 602 NAG A O7  1 
HETATM 7450 C C1  . NAG M 3 .   ? 144.653 184.844 120.210 1.00 62.91  ? 603 NAG A C1  1 
HETATM 7451 C C2  . NAG M 3 .   ? 144.814 186.031 121.170 1.00 65.52  ? 603 NAG A C2  1 
HETATM 7452 C C3  . NAG M 3 .   ? 144.025 185.805 122.458 1.00 68.68  ? 603 NAG A C3  1 
HETATM 7453 C C4  . NAG M 3 .   ? 142.599 185.360 122.163 1.00 70.05  ? 603 NAG A C4  1 
HETATM 7454 C C5  . NAG M 3 .   ? 142.655 184.134 121.254 1.00 65.79  ? 603 NAG A C5  1 
HETATM 7455 C C6  . NAG M 3 .   ? 141.308 183.535 120.921 1.00 62.78  ? 603 NAG A C6  1 
HETATM 7456 C C7  . NAG M 3 .   ? 146.883 187.374 121.144 1.00 67.29  ? 603 NAG A C7  1 
HETATM 7457 C C8  . NAG M 3 .   ? 148.323 187.401 121.590 1.00 54.06  ? 603 NAG A C8  1 
HETATM 7458 N N2  . NAG M 3 .   ? 146.199 186.266 121.486 1.00 62.38  ? 603 NAG A N2  1 
HETATM 7459 O O3  . NAG M 3 .   ? 144.049 187.006 123.182 1.00 76.78  ? 603 NAG A O3  1 
HETATM 7460 O O4  . NAG M 3 .   ? 141.983 185.075 123.398 1.00 74.22  ? 603 NAG A O4  1 
HETATM 7461 O O5  . NAG M 3 .   ? 143.289 184.525 120.057 1.00 68.19  ? 603 NAG A O5  1 
HETATM 7462 O O6  . NAG M 3 .   ? 140.523 184.483 120.239 1.00 65.18  ? 603 NAG A O6  1 
HETATM 7463 O O7  . NAG M 3 .   ? 146.393 188.302 120.517 1.00 68.89  ? 603 NAG A O7  1 
HETATM 7464 C C1  . NAG N 3 .   ? 167.276 148.462 124.669 1.00 122.97 ? 604 NAG A C1  1 
HETATM 7465 C C2  . NAG N 3 .   ? 167.751 148.116 123.233 1.00 123.39 ? 604 NAG A C2  1 
HETATM 7466 C C3  . NAG N 3 .   ? 167.728 146.602 122.985 1.00 123.11 ? 604 NAG A C3  1 
HETATM 7467 C C4  . NAG N 3 .   ? 168.430 145.868 124.121 1.00 124.83 ? 604 NAG A C4  1 
HETATM 7468 C C5  . NAG N 3 .   ? 167.795 146.295 125.446 1.00 122.64 ? 604 NAG A C5  1 
HETATM 7469 C C6  . NAG N 3 .   ? 168.362 145.595 126.660 1.00 120.10 ? 604 NAG A C6  1 
HETATM 7470 C C7  . NAG N 3 .   ? 165.858 148.990 121.695 1.00 127.90 ? 604 NAG A C7  1 
HETATM 7471 C C8  . NAG N 3 .   ? 164.749 148.178 122.327 1.00 120.89 ? 604 NAG A C8  1 
HETATM 7472 N N2  . NAG N 3 .   ? 167.127 148.888 122.169 1.00 128.03 ? 604 NAG A N2  1 
HETATM 7473 O O3  . NAG N 3 .   ? 168.332 146.351 121.744 1.00 119.74 ? 604 NAG A O3  1 
HETATM 7474 O O4  . NAG N 3 .   ? 168.284 144.485 123.895 1.00 120.83 ? 604 NAG A O4  1 
HETATM 7475 O O5  . NAG N 3 .   ? 167.996 147.682 125.594 1.00 121.44 ? 604 NAG A O5  1 
HETATM 7476 O O6  . NAG N 3 .   ? 169.765 145.713 126.662 1.00 117.31 ? 604 NAG A O6  1 
HETATM 7477 O O7  . NAG N 3 .   ? 165.595 149.732 120.759 1.00 127.54 ? 604 NAG A O7  1 
HETATM 7478 C C1  . NAG O 3 .   ? 190.014 150.422 121.973 1.00 151.75 ? 605 NAG A C1  1 
HETATM 7479 C C2  . NAG O 3 .   ? 189.293 149.708 123.128 1.00 152.58 ? 605 NAG A C2  1 
HETATM 7480 C C3  . NAG O 3 .   ? 189.064 148.233 122.797 1.00 154.14 ? 605 NAG A C3  1 
HETATM 7481 C C4  . NAG O 3 .   ? 188.409 148.088 121.428 1.00 157.21 ? 605 NAG A C4  1 
HETATM 7482 C C5  . NAG O 3 .   ? 189.241 148.847 120.390 1.00 156.37 ? 605 NAG A C5  1 
HETATM 7483 C C6  . NAG O 3 .   ? 188.699 148.753 118.981 1.00 150.15 ? 605 NAG A C6  1 
HETATM 7484 C C7  . NAG O 3 .   ? 191.263 149.460 124.648 1.00 153.01 ? 605 NAG A C7  1 
HETATM 7485 C C8  . NAG O 3 .   ? 191.730 149.776 126.047 1.00 144.93 ? 605 NAG A C8  1 
HETATM 7486 N N2  . NAG O 3 .   ? 190.006 149.868 124.373 1.00 152.75 ? 605 NAG A N2  1 
HETATM 7487 O O3  . NAG O 3 .   ? 188.279 147.676 123.818 1.00 148.02 ? 605 NAG A O3  1 
HETATM 7488 O O4  . NAG O 3 .   ? 188.342 146.710 121.138 1.00 154.76 ? 605 NAG A O4  1 
HETATM 7489 O O5  . NAG O 3 .   ? 189.314 150.209 120.767 1.00 154.45 ? 605 NAG A O5  1 
HETATM 7490 O O6  . NAG O 3 .   ? 187.353 149.166 118.960 1.00 147.76 ? 605 NAG A O6  1 
HETATM 7491 O O7  . NAG O 3 .   ? 191.994 148.877 123.860 1.00 152.09 ? 605 NAG A O7  1 
HETATM 7492 C C1  . NAG P 3 .   ? 179.856 148.490 143.977 1.00 99.27  ? 606 NAG A C1  1 
HETATM 7493 C C2  . NAG P 3 .   ? 180.209 146.996 144.059 1.00 107.32 ? 606 NAG A C2  1 
HETATM 7494 C C3  . NAG P 3 .   ? 181.534 146.778 144.788 1.00 109.16 ? 606 NAG A C3  1 
HETATM 7495 C C4  . NAG P 3 .   ? 182.619 147.641 144.159 1.00 104.66 ? 606 NAG A C4  1 
HETATM 7496 C C5  . NAG P 3 .   ? 182.138 149.094 144.121 1.00 101.31 ? 606 NAG A C5  1 
HETATM 7497 C C6  . NAG P 3 .   ? 183.159 150.043 143.537 1.00 96.86  ? 606 NAG A C6  1 
HETATM 7498 C C7  . NAG P 3 .   ? 178.636 146.363 145.891 1.00 108.93 ? 606 NAG A C7  1 
HETATM 7499 C C8  . NAG P 3 .   ? 177.510 145.410 146.213 1.00 104.16 ? 606 NAG A C8  1 
HETATM 7500 N N2  . NAG P 3 .   ? 179.138 146.229 144.647 1.00 109.25 ? 606 NAG A N2  1 
HETATM 7501 O O3  . NAG P 3 .   ? 181.848 145.412 144.723 1.00 105.97 ? 606 NAG A O3  1 
HETATM 7502 O O4  . NAG P 3 .   ? 183.781 147.497 144.943 1.00 102.18 ? 606 NAG A O4  1 
HETATM 7503 O O5  . NAG P 3 .   ? 180.934 149.173 143.376 1.00 97.57  ? 606 NAG A O5  1 
HETATM 7504 O O6  . NAG P 3 .   ? 183.690 149.490 142.355 1.00 100.02 ? 606 NAG A O6  1 
HETATM 7505 O O7  . NAG P 3 .   ? 179.035 147.172 146.715 1.00 104.84 ? 606 NAG A O7  1 
HETATM 7506 C C1  . NAG Q 3 .   ? 166.933 146.481 106.999 1.00 135.39 ? 607 NAG A C1  1 
HETATM 7507 C C2  . NAG Q 3 .   ? 167.576 146.529 105.607 1.00 135.23 ? 607 NAG A C2  1 
HETATM 7508 C C3  . NAG Q 3 .   ? 167.039 145.373 104.768 1.00 132.89 ? 607 NAG A C3  1 
HETATM 7509 C C4  . NAG Q 3 .   ? 167.232 144.049 105.500 1.00 136.89 ? 607 NAG A C4  1 
HETATM 7510 C C5  . NAG Q 3 .   ? 166.628 144.146 106.906 1.00 136.63 ? 607 NAG A C5  1 
HETATM 7511 C C6  . NAG Q 3 .   ? 166.804 142.894 107.736 1.00 131.23 ? 607 NAG A C6  1 
HETATM 7512 C C7  . NAG Q 3 .   ? 168.253 148.712 104.655 1.00 127.93 ? 607 NAG A C7  1 
HETATM 7513 C C8  . NAG Q 3 .   ? 169.670 148.356 105.034 1.00 123.09 ? 607 NAG A C8  1 
HETATM 7514 N N2  . NAG Q 3 .   ? 167.319 147.790 104.963 1.00 133.60 ? 607 NAG A N2  1 
HETATM 7515 O O3  . NAG Q 3 .   ? 167.698 145.390 103.529 1.00 126.30 ? 607 NAG A O3  1 
HETATM 7516 O O4  . NAG Q 3 .   ? 166.600 143.049 104.733 1.00 133.79 ? 607 NAG A O4  1 
HETATM 7517 O O5  . NAG Q 3 .   ? 167.216 145.234 107.592 1.00 136.52 ? 607 NAG A O5  1 
HETATM 7518 O O6  . NAG Q 3 .   ? 166.272 143.098 109.023 1.00 127.58 ? 607 NAG A O6  1 
HETATM 7519 O O7  . NAG Q 3 .   ? 167.992 149.773 104.106 1.00 124.47 ? 607 NAG A O7  1 
# 
