data_8G7Z
# 
_entry.id   8G7Z 
# 
_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   8G7Z         pdb_00008g7z 10.2210/pdb8g7z/pdb 
WWPDB D_1000272044 ?            ?                   
EMDB  EMD-29829    ?            ?                   
# 
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 'EM metadata'     1 0 2025-05-14 ? 
3 'Half map'        1 0 2025-05-14 1 
4 'Half map'        1 0 2025-05-14 2 
5 Image             1 0 2025-05-14 ? 
6 'Primary map'     1 0 2025-05-14 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 'Half map'        repository 'Initial release' ? ? 
4 4 'Half map'        repository 'Initial release' ? ? 
5 5 Image             repository 'Initial release' ? ? 
6 6 'Primary map'     repository 'Initial release' ? ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8G7Z 
_pdbx_database_status.recvd_initial_deposition_date   2023-02-17 
_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        'Cryo-EM structure of full length Neuroligin-2 from Mouse bound to two Neurexin-1 Beta K6c3' 
_pdbx_database_related.db_id          EMD-29829 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              weiwei.wang@utsouthwestern.edu 
_pdbx_contact_author.name_first         Weiwei 
_pdbx_contact_author.name_last          Wang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0215-9467 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Boyd, R.' 1 0000-0003-0912-0220 
'Wang, W.' 2 0000-0002-0215-9467 
# 
_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            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Cryo-EM structure of full length mouse Neuroligin-2 at 3.28 Angstroms resolution' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Boyd, R.' 1 0000-0003-0912-0220 
primary 'Wang, W.' 2 0000-0002-0215-9467 
# 
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 Neuroligin-2                             95226.797 2 ? ? ? ? 
2 polymer     man Neurexin-1                               50435.332 2 ? ? ? ? 
3 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   6 ? ? ? ? 
4 non-polymer syn 'CALCIUM ION'                            40.078    2 ? ? ? ? 
# 
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 
;MALPRCMWPNYVWRAMMACVVHRGSGAPLTLCLLGCLLQTFHVLSQKYPYDVPDYAQRGGGGPGGGAPGGPGLGLGSLGE
ERFPVVNTAYGRVRGVRRELNNEILGPVVQFLGVPYATPPLGARRFQPPEAPASWPGVRNATTLPPACPQNLHGALPAIM
LPVWFTDNLEAAATYVQNQSEDCLYLNLYVPTEDDIRDSGKKPVMLFLHGGSYMEGTGNMFDGSVLAAYGNVIVVTLNYR
LGVLGFLSTGDQAAKGNYGLLDQIQALRWLSENIAHFGGDPERITIFGSGAGASCVNLLILSHHSEGLFQKAIAQSGTAI
SSWSVNYQPLKYTRLLAAKVGCDREDSTEAVECLRRKSSRELVDQDVQPARYHIAFGPVVDGDVVPDDPEILMQQGEFLN
YDMLIGVNQGEGLKFVEDSAESEDGVSASAFDFTVSNFVDNLYGYPEGKDVLRETIKFMYTDWADRDNGEMRRKTLLALF
TDHQWVAPAVATAKLHADYQSPVYFYTFYHHCQAEGRPEWADAAHGDELPYVFGVPMVGATDLFPCNFSKNDVMLSAVVM
TYWTNFAKTGDPNQPVPQDTKFIHTKPNRFEEVVWSKFNSKEKQYLHIGLKPRVRDNYRANKVAFWLELVPHLHNLHTEL
FTTTTRLPPYATRWPPRTPGPGTSGTRRPPPPATLPPESDIDLGPRAYDRFPGDSRDYSTELSVTVAVGASLLFLNILAF
AALYYKRDRRQELRCRRLSPPGGSGSGVPGGGPLLPTAGRELPPEEELVSLQLKRGGGVGADPAEALRPACPPDYTLALR
RAPDDVPLLAPGALTLLPSGLGPPPPPPPPSLHPFGPFPPPPPTATSHNNTLPHPHSTTRVSNSLEVLFQ
;
;MALPRCMWPNYVWRAMMACVVHRGSGAPLTLCLLGCLLQTFHVLSQKYPYDVPDYAQRGGGGPGGGAPGGPGLGLGSLGE
ERFPVVNTAYGRVRGVRRELNNEILGPVVQFLGVPYATPPLGARRFQPPEAPASWPGVRNATTLPPACPQNLHGALPAIM
LPVWFTDNLEAAATYVQNQSEDCLYLNLYVPTEDDIRDSGKKPVMLFLHGGSYMEGTGNMFDGSVLAAYGNVIVVTLNYR
LGVLGFLSTGDQAAKGNYGLLDQIQALRWLSENIAHFGGDPERITIFGSGAGASCVNLLILSHHSEGLFQKAIAQSGTAI
SSWSVNYQPLKYTRLLAAKVGCDREDSTEAVECLRRKSSRELVDQDVQPARYHIAFGPVVDGDVVPDDPEILMQQGEFLN
YDMLIGVNQGEGLKFVEDSAESEDGVSASAFDFTVSNFVDNLYGYPEGKDVLRETIKFMYTDWADRDNGEMRRKTLLALF
TDHQWVAPAVATAKLHADYQSPVYFYTFYHHCQAEGRPEWADAAHGDELPYVFGVPMVGATDLFPCNFSKNDVMLSAVVM
TYWTNFAKTGDPNQPVPQDTKFIHTKPNRFEEVVWSKFNSKEKQYLHIGLKPRVRDNYRANKVAFWLELVPHLHNLHTEL
FTTTTRLPPYATRWPPRTPGPGTSGTRRPPPPATLPPESDIDLGPRAYDRFPGDSRDYSTELSVTVAVGASLLFLNILAF
AALYYKRDRRQELRCRRLSPPGGSGSGVPGGGPLLPTAGRELPPEEELVSLQLKRGGGVGADPAEALRPACPPDYTLALR
RAPDDVPLLAPGALTLLPSGLGPPPPPPPPSLHPFGPFPPPPPTATSHNNTLPHPHSTTRVSNSLEVLFQ
;
A,B ? 
2 'polypeptide(L)' no no 
;MYQRMLRCGADLGSPGGGSGGGAGGRLALIWIVPLTLGGLLGVAWGASSLGAHHIHHFHGSSKEFEQKLISEEDLGFEID
KVWHDFPATSPIAIYRSPASLRGGHAGTTYIFSKGGGQITYKWPPNDRPSTRADRLAIGFSTVQKEAVLVRVDSSSGLGD
YLELHIHQGKIGVKFNVGTDDIAIEESNAIINDGKYHVVRFTRSGGNATLQVDSWPVIERYPAGRQLTIFNSQATIIIGG
KEQGQPFQGQLSGLYYNGLKVLNMAAENDANIAIVGNVRLVGEVPSSMTTESTATAMQSEMSTSIMETTTTLATSTARRG
KPPTKEPISQTTDDILVASAECPSDDEDIDPCEPSSGGLANPTRVGGREPYPGSAEVIRESSSTTGMVVGIVAAAALCIL
ILLYAMYKYRNRDEGSYHVDESRNYISNSAQSNGAVVKEKQPSSAKSANKNKKNKDKEYYVSNSLEVLFQ
;
;MYQRMLRCGADLGSPGGGSGGGAGGRLALIWIVPLTLGGLLGVAWGASSLGAHHIHHFHGSSKEFEQKLISEEDLGFEID
KVWHDFPATSPIAIYRSPASLRGGHAGTTYIFSKGGGQITYKWPPNDRPSTRADRLAIGFSTVQKEAVLVRVDSSSGLGD
YLELHIHQGKIGVKFNVGTDDIAIEESNAIINDGKYHVVRFTRSGGNATLQVDSWPVIERYPAGRQLTIFNSQATIIIGG
KEQGQPFQGQLSGLYYNGLKVLNMAAENDANIAIVGNVRLVGEVPSSMTTESTATAMQSEMSTSIMETTTTLATSTARRG
KPPTKEPISQTTDDILVASAECPSDDEDIDPCEPSSGGLANPTRVGGREPYPGSAEVIRESSSTTGMVVGIVAAAALCIL
ILLYAMYKYRNRDEGSYHVDESRNYISNSAQSNGAVVKEKQPSSAKSANKNKKNKDKEYYVSNSLEVLFQ
;
C,D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 2-acetamido-2-deoxy-beta-D-glucopyranose NAG 
4 'CALCIUM ION'                            CA  
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   LEU n 
1 4   PRO n 
1 5   ARG n 
1 6   CYS n 
1 7   MET n 
1 8   TRP n 
1 9   PRO n 
1 10  ASN n 
1 11  TYR n 
1 12  VAL n 
1 13  TRP n 
1 14  ARG n 
1 15  ALA n 
1 16  MET n 
1 17  MET n 
1 18  ALA n 
1 19  CYS n 
1 20  VAL n 
1 21  VAL n 
1 22  HIS n 
1 23  ARG n 
1 24  GLY n 
1 25  SER n 
1 26  GLY n 
1 27  ALA n 
1 28  PRO n 
1 29  LEU n 
1 30  THR n 
1 31  LEU n 
1 32  CYS n 
1 33  LEU n 
1 34  LEU n 
1 35  GLY n 
1 36  CYS n 
1 37  LEU n 
1 38  LEU n 
1 39  GLN n 
1 40  THR n 
1 41  PHE n 
1 42  HIS n 
1 43  VAL n 
1 44  LEU n 
1 45  SER n 
1 46  GLN n 
1 47  LYS n 
1 48  TYR n 
1 49  PRO n 
1 50  TYR n 
1 51  ASP n 
1 52  VAL n 
1 53  PRO n 
1 54  ASP n 
1 55  TYR n 
1 56  ALA n 
1 57  GLN n 
1 58  ARG n 
1 59  GLY n 
1 60  GLY n 
1 61  GLY n 
1 62  GLY n 
1 63  PRO n 
1 64  GLY n 
1 65  GLY n 
1 66  GLY n 
1 67  ALA n 
1 68  PRO n 
1 69  GLY n 
1 70  GLY n 
1 71  PRO n 
1 72  GLY n 
1 73  LEU n 
1 74  GLY n 
1 75  LEU n 
1 76  GLY n 
1 77  SER n 
1 78  LEU n 
1 79  GLY n 
1 80  GLU n 
1 81  GLU n 
1 82  ARG n 
1 83  PHE n 
1 84  PRO n 
1 85  VAL n 
1 86  VAL n 
1 87  ASN n 
1 88  THR n 
1 89  ALA n 
1 90  TYR n 
1 91  GLY n 
1 92  ARG n 
1 93  VAL n 
1 94  ARG n 
1 95  GLY n 
1 96  VAL n 
1 97  ARG n 
1 98  ARG n 
1 99  GLU n 
1 100 LEU n 
1 101 ASN n 
1 102 ASN n 
1 103 GLU n 
1 104 ILE n 
1 105 LEU n 
1 106 GLY n 
1 107 PRO n 
1 108 VAL n 
1 109 VAL n 
1 110 GLN n 
1 111 PHE n 
1 112 LEU n 
1 113 GLY n 
1 114 VAL n 
1 115 PRO n 
1 116 TYR n 
1 117 ALA n 
1 118 THR n 
1 119 PRO n 
1 120 PRO n 
1 121 LEU n 
1 122 GLY n 
1 123 ALA n 
1 124 ARG n 
1 125 ARG n 
1 126 PHE n 
1 127 GLN n 
1 128 PRO n 
1 129 PRO n 
1 130 GLU n 
1 131 ALA n 
1 132 PRO n 
1 133 ALA n 
1 134 SER n 
1 135 TRP n 
1 136 PRO n 
1 137 GLY n 
1 138 VAL n 
1 139 ARG n 
1 140 ASN n 
1 141 ALA n 
1 142 THR n 
1 143 THR n 
1 144 LEU n 
1 145 PRO n 
1 146 PRO n 
1 147 ALA n 
1 148 CYS n 
1 149 PRO n 
1 150 GLN n 
1 151 ASN n 
1 152 LEU n 
1 153 HIS n 
1 154 GLY n 
1 155 ALA n 
1 156 LEU n 
1 157 PRO n 
1 158 ALA n 
1 159 ILE n 
1 160 MET n 
1 161 LEU n 
1 162 PRO n 
1 163 VAL n 
1 164 TRP n 
1 165 PHE n 
1 166 THR n 
1 167 ASP n 
1 168 ASN n 
1 169 LEU n 
1 170 GLU n 
1 171 ALA n 
1 172 ALA n 
1 173 ALA n 
1 174 THR n 
1 175 TYR n 
1 176 VAL n 
1 177 GLN n 
1 178 ASN n 
1 179 GLN n 
1 180 SER n 
1 181 GLU n 
1 182 ASP n 
1 183 CYS n 
1 184 LEU n 
1 185 TYR n 
1 186 LEU n 
1 187 ASN n 
1 188 LEU n 
1 189 TYR n 
1 190 VAL n 
1 191 PRO n 
1 192 THR n 
1 193 GLU n 
1 194 ASP n 
1 195 ASP n 
1 196 ILE n 
1 197 ARG n 
1 198 ASP n 
1 199 SER n 
1 200 GLY n 
1 201 LYS n 
1 202 LYS n 
1 203 PRO n 
1 204 VAL n 
1 205 MET n 
1 206 LEU n 
1 207 PHE n 
1 208 LEU n 
1 209 HIS n 
1 210 GLY n 
1 211 GLY n 
1 212 SER n 
1 213 TYR n 
1 214 MET n 
1 215 GLU n 
1 216 GLY n 
1 217 THR n 
1 218 GLY n 
1 219 ASN n 
1 220 MET n 
1 221 PHE n 
1 222 ASP n 
1 223 GLY n 
1 224 SER n 
1 225 VAL n 
1 226 LEU n 
1 227 ALA n 
1 228 ALA n 
1 229 TYR n 
1 230 GLY n 
1 231 ASN n 
1 232 VAL n 
1 233 ILE n 
1 234 VAL n 
1 235 VAL n 
1 236 THR n 
1 237 LEU n 
1 238 ASN n 
1 239 TYR n 
1 240 ARG n 
1 241 LEU n 
1 242 GLY n 
1 243 VAL n 
1 244 LEU n 
1 245 GLY n 
1 246 PHE n 
1 247 LEU n 
1 248 SER n 
1 249 THR n 
1 250 GLY n 
1 251 ASP n 
1 252 GLN n 
1 253 ALA n 
1 254 ALA n 
1 255 LYS n 
1 256 GLY n 
1 257 ASN n 
1 258 TYR n 
1 259 GLY n 
1 260 LEU n 
1 261 LEU n 
1 262 ASP n 
1 263 GLN n 
1 264 ILE n 
1 265 GLN n 
1 266 ALA n 
1 267 LEU n 
1 268 ARG n 
1 269 TRP n 
1 270 LEU n 
1 271 SER n 
1 272 GLU n 
1 273 ASN n 
1 274 ILE n 
1 275 ALA n 
1 276 HIS n 
1 277 PHE n 
1 278 GLY n 
1 279 GLY n 
1 280 ASP n 
1 281 PRO n 
1 282 GLU n 
1 283 ARG n 
1 284 ILE n 
1 285 THR n 
1 286 ILE n 
1 287 PHE n 
1 288 GLY n 
1 289 SER n 
1 290 GLY n 
1 291 ALA n 
1 292 GLY n 
1 293 ALA n 
1 294 SER n 
1 295 CYS n 
1 296 VAL n 
1 297 ASN n 
1 298 LEU n 
1 299 LEU n 
1 300 ILE n 
1 301 LEU n 
1 302 SER n 
1 303 HIS n 
1 304 HIS n 
1 305 SER n 
1 306 GLU n 
1 307 GLY n 
1 308 LEU n 
1 309 PHE n 
1 310 GLN n 
1 311 LYS n 
1 312 ALA n 
1 313 ILE n 
1 314 ALA n 
1 315 GLN n 
1 316 SER n 
1 317 GLY n 
1 318 THR n 
1 319 ALA n 
1 320 ILE n 
1 321 SER n 
1 322 SER n 
1 323 TRP n 
1 324 SER n 
1 325 VAL n 
1 326 ASN n 
1 327 TYR n 
1 328 GLN n 
1 329 PRO n 
1 330 LEU n 
1 331 LYS n 
1 332 TYR n 
1 333 THR n 
1 334 ARG n 
1 335 LEU n 
1 336 LEU n 
1 337 ALA n 
1 338 ALA n 
1 339 LYS n 
1 340 VAL n 
1 341 GLY n 
1 342 CYS n 
1 343 ASP n 
1 344 ARG n 
1 345 GLU n 
1 346 ASP n 
1 347 SER n 
1 348 THR n 
1 349 GLU n 
1 350 ALA n 
1 351 VAL n 
1 352 GLU n 
1 353 CYS n 
1 354 LEU n 
1 355 ARG n 
1 356 ARG n 
1 357 LYS n 
1 358 SER n 
1 359 SER n 
1 360 ARG n 
1 361 GLU n 
1 362 LEU n 
1 363 VAL n 
1 364 ASP n 
1 365 GLN n 
1 366 ASP n 
1 367 VAL n 
1 368 GLN n 
1 369 PRO n 
1 370 ALA n 
1 371 ARG n 
1 372 TYR n 
1 373 HIS n 
1 374 ILE n 
1 375 ALA n 
1 376 PHE n 
1 377 GLY n 
1 378 PRO n 
1 379 VAL n 
1 380 VAL n 
1 381 ASP n 
1 382 GLY n 
1 383 ASP n 
1 384 VAL n 
1 385 VAL n 
1 386 PRO n 
1 387 ASP n 
1 388 ASP n 
1 389 PRO n 
1 390 GLU n 
1 391 ILE n 
1 392 LEU n 
1 393 MET n 
1 394 GLN n 
1 395 GLN n 
1 396 GLY n 
1 397 GLU n 
1 398 PHE n 
1 399 LEU n 
1 400 ASN n 
1 401 TYR n 
1 402 ASP n 
1 403 MET n 
1 404 LEU n 
1 405 ILE n 
1 406 GLY n 
1 407 VAL n 
1 408 ASN n 
1 409 GLN n 
1 410 GLY n 
1 411 GLU n 
1 412 GLY n 
1 413 LEU n 
1 414 LYS n 
1 415 PHE n 
1 416 VAL n 
1 417 GLU n 
1 418 ASP n 
1 419 SER n 
1 420 ALA n 
1 421 GLU n 
1 422 SER n 
1 423 GLU n 
1 424 ASP n 
1 425 GLY n 
1 426 VAL n 
1 427 SER n 
1 428 ALA n 
1 429 SER n 
1 430 ALA n 
1 431 PHE n 
1 432 ASP n 
1 433 PHE n 
1 434 THR n 
1 435 VAL n 
1 436 SER n 
1 437 ASN n 
1 438 PHE n 
1 439 VAL n 
1 440 ASP n 
1 441 ASN n 
1 442 LEU n 
1 443 TYR n 
1 444 GLY n 
1 445 TYR n 
1 446 PRO n 
1 447 GLU n 
1 448 GLY n 
1 449 LYS n 
1 450 ASP n 
1 451 VAL n 
1 452 LEU n 
1 453 ARG n 
1 454 GLU n 
1 455 THR n 
1 456 ILE n 
1 457 LYS n 
1 458 PHE n 
1 459 MET n 
1 460 TYR n 
1 461 THR n 
1 462 ASP n 
1 463 TRP n 
1 464 ALA n 
1 465 ASP n 
1 466 ARG n 
1 467 ASP n 
1 468 ASN n 
1 469 GLY n 
1 470 GLU n 
1 471 MET n 
1 472 ARG n 
1 473 ARG n 
1 474 LYS n 
1 475 THR n 
1 476 LEU n 
1 477 LEU n 
1 478 ALA n 
1 479 LEU n 
1 480 PHE n 
1 481 THR n 
1 482 ASP n 
1 483 HIS n 
1 484 GLN n 
1 485 TRP n 
1 486 VAL n 
1 487 ALA n 
1 488 PRO n 
1 489 ALA n 
1 490 VAL n 
1 491 ALA n 
1 492 THR n 
1 493 ALA n 
1 494 LYS n 
1 495 LEU n 
1 496 HIS n 
1 497 ALA n 
1 498 ASP n 
1 499 TYR n 
1 500 GLN n 
1 501 SER n 
1 502 PRO n 
1 503 VAL n 
1 504 TYR n 
1 505 PHE n 
1 506 TYR n 
1 507 THR n 
1 508 PHE n 
1 509 TYR n 
1 510 HIS n 
1 511 HIS n 
1 512 CYS n 
1 513 GLN n 
1 514 ALA n 
1 515 GLU n 
1 516 GLY n 
1 517 ARG n 
1 518 PRO n 
1 519 GLU n 
1 520 TRP n 
1 521 ALA n 
1 522 ASP n 
1 523 ALA n 
1 524 ALA n 
1 525 HIS n 
1 526 GLY n 
1 527 ASP n 
1 528 GLU n 
1 529 LEU n 
1 530 PRO n 
1 531 TYR n 
1 532 VAL n 
1 533 PHE n 
1 534 GLY n 
1 535 VAL n 
1 536 PRO n 
1 537 MET n 
1 538 VAL n 
1 539 GLY n 
1 540 ALA n 
1 541 THR n 
1 542 ASP n 
1 543 LEU n 
1 544 PHE n 
1 545 PRO n 
1 546 CYS n 
1 547 ASN n 
1 548 PHE n 
1 549 SER n 
1 550 LYS n 
1 551 ASN n 
1 552 ASP n 
1 553 VAL n 
1 554 MET n 
1 555 LEU n 
1 556 SER n 
1 557 ALA n 
1 558 VAL n 
1 559 VAL n 
1 560 MET n 
1 561 THR n 
1 562 TYR n 
1 563 TRP n 
1 564 THR n 
1 565 ASN n 
1 566 PHE n 
1 567 ALA n 
1 568 LYS n 
1 569 THR n 
1 570 GLY n 
1 571 ASP n 
1 572 PRO n 
1 573 ASN n 
1 574 GLN n 
1 575 PRO n 
1 576 VAL n 
1 577 PRO n 
1 578 GLN n 
1 579 ASP n 
1 580 THR n 
1 581 LYS n 
1 582 PHE n 
1 583 ILE n 
1 584 HIS n 
1 585 THR n 
1 586 LYS n 
1 587 PRO n 
1 588 ASN n 
1 589 ARG n 
1 590 PHE n 
1 591 GLU n 
1 592 GLU n 
1 593 VAL n 
1 594 VAL n 
1 595 TRP n 
1 596 SER n 
1 597 LYS n 
1 598 PHE n 
1 599 ASN n 
1 600 SER n 
1 601 LYS n 
1 602 GLU n 
1 603 LYS n 
1 604 GLN n 
1 605 TYR n 
1 606 LEU n 
1 607 HIS n 
1 608 ILE n 
1 609 GLY n 
1 610 LEU n 
1 611 LYS n 
1 612 PRO n 
1 613 ARG n 
1 614 VAL n 
1 615 ARG n 
1 616 ASP n 
1 617 ASN n 
1 618 TYR n 
1 619 ARG n 
1 620 ALA n 
1 621 ASN n 
1 622 LYS n 
1 623 VAL n 
1 624 ALA n 
1 625 PHE n 
1 626 TRP n 
1 627 LEU n 
1 628 GLU n 
1 629 LEU n 
1 630 VAL n 
1 631 PRO n 
1 632 HIS n 
1 633 LEU n 
1 634 HIS n 
1 635 ASN n 
1 636 LEU n 
1 637 HIS n 
1 638 THR n 
1 639 GLU n 
1 640 LEU n 
1 641 PHE n 
1 642 THR n 
1 643 THR n 
1 644 THR n 
1 645 THR n 
1 646 ARG n 
1 647 LEU n 
1 648 PRO n 
1 649 PRO n 
1 650 TYR n 
1 651 ALA n 
1 652 THR n 
1 653 ARG n 
1 654 TRP n 
1 655 PRO n 
1 656 PRO n 
1 657 ARG n 
1 658 THR n 
1 659 PRO n 
1 660 GLY n 
1 661 PRO n 
1 662 GLY n 
1 663 THR n 
1 664 SER n 
1 665 GLY n 
1 666 THR n 
1 667 ARG n 
1 668 ARG n 
1 669 PRO n 
1 670 PRO n 
1 671 PRO n 
1 672 PRO n 
1 673 ALA n 
1 674 THR n 
1 675 LEU n 
1 676 PRO n 
1 677 PRO n 
1 678 GLU n 
1 679 SER n 
1 680 ASP n 
1 681 ILE n 
1 682 ASP n 
1 683 LEU n 
1 684 GLY n 
1 685 PRO n 
1 686 ARG n 
1 687 ALA n 
1 688 TYR n 
1 689 ASP n 
1 690 ARG n 
1 691 PHE n 
1 692 PRO n 
1 693 GLY n 
1 694 ASP n 
1 695 SER n 
1 696 ARG n 
1 697 ASP n 
1 698 TYR n 
1 699 SER n 
1 700 THR n 
1 701 GLU n 
1 702 LEU n 
1 703 SER n 
1 704 VAL n 
1 705 THR n 
1 706 VAL n 
1 707 ALA n 
1 708 VAL n 
1 709 GLY n 
1 710 ALA n 
1 711 SER n 
1 712 LEU n 
1 713 LEU n 
1 714 PHE n 
1 715 LEU n 
1 716 ASN n 
1 717 ILE n 
1 718 LEU n 
1 719 ALA n 
1 720 PHE n 
1 721 ALA n 
1 722 ALA n 
1 723 LEU n 
1 724 TYR n 
1 725 TYR n 
1 726 LYS n 
1 727 ARG n 
1 728 ASP n 
1 729 ARG n 
1 730 ARG n 
1 731 GLN n 
1 732 GLU n 
1 733 LEU n 
1 734 ARG n 
1 735 CYS n 
1 736 ARG n 
1 737 ARG n 
1 738 LEU n 
1 739 SER n 
1 740 PRO n 
1 741 PRO n 
1 742 GLY n 
1 743 GLY n 
1 744 SER n 
1 745 GLY n 
1 746 SER n 
1 747 GLY n 
1 748 VAL n 
1 749 PRO n 
1 750 GLY n 
1 751 GLY n 
1 752 GLY n 
1 753 PRO n 
1 754 LEU n 
1 755 LEU n 
1 756 PRO n 
1 757 THR n 
1 758 ALA n 
1 759 GLY n 
1 760 ARG n 
1 761 GLU n 
1 762 LEU n 
1 763 PRO n 
1 764 PRO n 
1 765 GLU n 
1 766 GLU n 
1 767 GLU n 
1 768 LEU n 
1 769 VAL n 
1 770 SER n 
1 771 LEU n 
1 772 GLN n 
1 773 LEU n 
1 774 LYS n 
1 775 ARG n 
1 776 GLY n 
1 777 GLY n 
1 778 GLY n 
1 779 VAL n 
1 780 GLY n 
1 781 ALA n 
1 782 ASP n 
1 783 PRO n 
1 784 ALA n 
1 785 GLU n 
1 786 ALA n 
1 787 LEU n 
1 788 ARG n 
1 789 PRO n 
1 790 ALA n 
1 791 CYS n 
1 792 PRO n 
1 793 PRO n 
1 794 ASP n 
1 795 TYR n 
1 796 THR n 
1 797 LEU n 
1 798 ALA n 
1 799 LEU n 
1 800 ARG n 
1 801 ARG n 
1 802 ALA n 
1 803 PRO n 
1 804 ASP n 
1 805 ASP n 
1 806 VAL n 
1 807 PRO n 
1 808 LEU n 
1 809 LEU n 
1 810 ALA n 
1 811 PRO n 
1 812 GLY n 
1 813 ALA n 
1 814 LEU n 
1 815 THR n 
1 816 LEU n 
1 817 LEU n 
1 818 PRO n 
1 819 SER n 
1 820 GLY n 
1 821 LEU n 
1 822 GLY n 
1 823 PRO n 
1 824 PRO n 
1 825 PRO n 
1 826 PRO n 
1 827 PRO n 
1 828 PRO n 
1 829 PRO n 
1 830 PRO n 
1 831 SER n 
1 832 LEU n 
1 833 HIS n 
1 834 PRO n 
1 835 PHE n 
1 836 GLY n 
1 837 PRO n 
1 838 PHE n 
1 839 PRO n 
1 840 PRO n 
1 841 PRO n 
1 842 PRO n 
1 843 PRO n 
1 844 THR n 
1 845 ALA n 
1 846 THR n 
1 847 SER n 
1 848 HIS n 
1 849 ASN n 
1 850 ASN n 
1 851 THR n 
1 852 LEU n 
1 853 PRO n 
1 854 HIS n 
1 855 PRO n 
1 856 HIS n 
1 857 SER n 
1 858 THR n 
1 859 THR n 
1 860 ARG n 
1 861 VAL n 
1 862 SER n 
1 863 ASN n 
1 864 SER n 
1 865 LEU n 
1 866 GLU n 
1 867 VAL n 
1 868 LEU n 
1 869 PHE n 
1 870 GLN n 
2 1   MET n 
2 2   TYR n 
2 3   GLN n 
2 4   ARG n 
2 5   MET n 
2 6   LEU n 
2 7   ARG n 
2 8   CYS n 
2 9   GLY n 
2 10  ALA n 
2 11  ASP n 
2 12  LEU n 
2 13  GLY n 
2 14  SER n 
2 15  PRO n 
2 16  GLY n 
2 17  GLY n 
2 18  GLY n 
2 19  SER n 
2 20  GLY n 
2 21  GLY n 
2 22  GLY n 
2 23  ALA n 
2 24  GLY n 
2 25  GLY n 
2 26  ARG n 
2 27  LEU n 
2 28  ALA n 
2 29  LEU n 
2 30  ILE n 
2 31  TRP n 
2 32  ILE n 
2 33  VAL n 
2 34  PRO n 
2 35  LEU n 
2 36  THR n 
2 37  LEU n 
2 38  GLY n 
2 39  GLY n 
2 40  LEU n 
2 41  LEU n 
2 42  GLY n 
2 43  VAL n 
2 44  ALA n 
2 45  TRP n 
2 46  GLY n 
2 47  ALA n 
2 48  SER n 
2 49  SER n 
2 50  LEU n 
2 51  GLY n 
2 52  ALA n 
2 53  HIS n 
2 54  HIS n 
2 55  ILE n 
2 56  HIS n 
2 57  HIS n 
2 58  PHE n 
2 59  HIS n 
2 60  GLY n 
2 61  SER n 
2 62  SER n 
2 63  LYS n 
2 64  GLU n 
2 65  PHE n 
2 66  GLU n 
2 67  GLN n 
2 68  LYS n 
2 69  LEU n 
2 70  ILE n 
2 71  SER n 
2 72  GLU n 
2 73  GLU n 
2 74  ASP n 
2 75  LEU n 
2 76  GLY n 
2 77  PHE n 
2 78  GLU n 
2 79  ILE n 
2 80  ASP n 
2 81  LYS n 
2 82  VAL n 
2 83  TRP n 
2 84  HIS n 
2 85  ASP n 
2 86  PHE n 
2 87  PRO n 
2 88  ALA n 
2 89  THR n 
2 90  SER n 
2 91  PRO n 
2 92  ILE n 
2 93  ALA n 
2 94  ILE n 
2 95  TYR n 
2 96  ARG n 
2 97  SER n 
2 98  PRO n 
2 99  ALA n 
2 100 SER n 
2 101 LEU n 
2 102 ARG n 
2 103 GLY n 
2 104 GLY n 
2 105 HIS n 
2 106 ALA n 
2 107 GLY n 
2 108 THR n 
2 109 THR n 
2 110 TYR n 
2 111 ILE n 
2 112 PHE n 
2 113 SER n 
2 114 LYS n 
2 115 GLY n 
2 116 GLY n 
2 117 GLY n 
2 118 GLN n 
2 119 ILE n 
2 120 THR n 
2 121 TYR n 
2 122 LYS n 
2 123 TRP n 
2 124 PRO n 
2 125 PRO n 
2 126 ASN n 
2 127 ASP n 
2 128 ARG n 
2 129 PRO n 
2 130 SER n 
2 131 THR n 
2 132 ARG n 
2 133 ALA n 
2 134 ASP n 
2 135 ARG n 
2 136 LEU n 
2 137 ALA n 
2 138 ILE n 
2 139 GLY n 
2 140 PHE n 
2 141 SER n 
2 142 THR n 
2 143 VAL n 
2 144 GLN n 
2 145 LYS n 
2 146 GLU n 
2 147 ALA n 
2 148 VAL n 
2 149 LEU n 
2 150 VAL n 
2 151 ARG n 
2 152 VAL n 
2 153 ASP n 
2 154 SER n 
2 155 SER n 
2 156 SER n 
2 157 GLY n 
2 158 LEU n 
2 159 GLY n 
2 160 ASP n 
2 161 TYR n 
2 162 LEU n 
2 163 GLU n 
2 164 LEU n 
2 165 HIS n 
2 166 ILE n 
2 167 HIS n 
2 168 GLN n 
2 169 GLY n 
2 170 LYS n 
2 171 ILE n 
2 172 GLY n 
2 173 VAL n 
2 174 LYS n 
2 175 PHE n 
2 176 ASN n 
2 177 VAL n 
2 178 GLY n 
2 179 THR n 
2 180 ASP n 
2 181 ASP n 
2 182 ILE n 
2 183 ALA n 
2 184 ILE n 
2 185 GLU n 
2 186 GLU n 
2 187 SER n 
2 188 ASN n 
2 189 ALA n 
2 190 ILE n 
2 191 ILE n 
2 192 ASN n 
2 193 ASP n 
2 194 GLY n 
2 195 LYS n 
2 196 TYR n 
2 197 HIS n 
2 198 VAL n 
2 199 VAL n 
2 200 ARG n 
2 201 PHE n 
2 202 THR n 
2 203 ARG n 
2 204 SER n 
2 205 GLY n 
2 206 GLY n 
2 207 ASN n 
2 208 ALA n 
2 209 THR n 
2 210 LEU n 
2 211 GLN n 
2 212 VAL n 
2 213 ASP n 
2 214 SER n 
2 215 TRP n 
2 216 PRO n 
2 217 VAL n 
2 218 ILE n 
2 219 GLU n 
2 220 ARG n 
2 221 TYR n 
2 222 PRO n 
2 223 ALA n 
2 224 GLY n 
2 225 ARG n 
2 226 GLN n 
2 227 LEU n 
2 228 THR n 
2 229 ILE n 
2 230 PHE n 
2 231 ASN n 
2 232 SER n 
2 233 GLN n 
2 234 ALA n 
2 235 THR n 
2 236 ILE n 
2 237 ILE n 
2 238 ILE n 
2 239 GLY n 
2 240 GLY n 
2 241 LYS n 
2 242 GLU n 
2 243 GLN n 
2 244 GLY n 
2 245 GLN n 
2 246 PRO n 
2 247 PHE n 
2 248 GLN n 
2 249 GLY n 
2 250 GLN n 
2 251 LEU n 
2 252 SER n 
2 253 GLY n 
2 254 LEU n 
2 255 TYR n 
2 256 TYR n 
2 257 ASN n 
2 258 GLY n 
2 259 LEU n 
2 260 LYS n 
2 261 VAL n 
2 262 LEU n 
2 263 ASN n 
2 264 MET n 
2 265 ALA n 
2 266 ALA n 
2 267 GLU n 
2 268 ASN n 
2 269 ASP n 
2 270 ALA n 
2 271 ASN n 
2 272 ILE n 
2 273 ALA n 
2 274 ILE n 
2 275 VAL n 
2 276 GLY n 
2 277 ASN n 
2 278 VAL n 
2 279 ARG n 
2 280 LEU n 
2 281 VAL n 
2 282 GLY n 
2 283 GLU n 
2 284 VAL n 
2 285 PRO n 
2 286 SER n 
2 287 SER n 
2 288 MET n 
2 289 THR n 
2 290 THR n 
2 291 GLU n 
2 292 SER n 
2 293 THR n 
2 294 ALA n 
2 295 THR n 
2 296 ALA n 
2 297 MET n 
2 298 GLN n 
2 299 SER n 
2 300 GLU n 
2 301 MET n 
2 302 SER n 
2 303 THR n 
2 304 SER n 
2 305 ILE n 
2 306 MET n 
2 307 GLU n 
2 308 THR n 
2 309 THR n 
2 310 THR n 
2 311 THR n 
2 312 LEU n 
2 313 ALA n 
2 314 THR n 
2 315 SER n 
2 316 THR n 
2 317 ALA n 
2 318 ARG n 
2 319 ARG n 
2 320 GLY n 
2 321 LYS n 
2 322 PRO n 
2 323 PRO n 
2 324 THR n 
2 325 LYS n 
2 326 GLU n 
2 327 PRO n 
2 328 ILE n 
2 329 SER n 
2 330 GLN n 
2 331 THR n 
2 332 THR n 
2 333 ASP n 
2 334 ASP n 
2 335 ILE n 
2 336 LEU n 
2 337 VAL n 
2 338 ALA n 
2 339 SER n 
2 340 ALA n 
2 341 GLU n 
2 342 CYS n 
2 343 PRO n 
2 344 SER n 
2 345 ASP n 
2 346 ASP n 
2 347 GLU n 
2 348 ASP n 
2 349 ILE n 
2 350 ASP n 
2 351 PRO n 
2 352 CYS n 
2 353 GLU n 
2 354 PRO n 
2 355 SER n 
2 356 SER n 
2 357 GLY n 
2 358 GLY n 
2 359 LEU n 
2 360 ALA n 
2 361 ASN n 
2 362 PRO n 
2 363 THR n 
2 364 ARG n 
2 365 VAL n 
2 366 GLY n 
2 367 GLY n 
2 368 ARG n 
2 369 GLU n 
2 370 PRO n 
2 371 TYR n 
2 372 PRO n 
2 373 GLY n 
2 374 SER n 
2 375 ALA n 
2 376 GLU n 
2 377 VAL n 
2 378 ILE n 
2 379 ARG n 
2 380 GLU n 
2 381 SER n 
2 382 SER n 
2 383 SER n 
2 384 THR n 
2 385 THR n 
2 386 GLY n 
2 387 MET n 
2 388 VAL n 
2 389 VAL n 
2 390 GLY n 
2 391 ILE n 
2 392 VAL n 
2 393 ALA n 
2 394 ALA n 
2 395 ALA n 
2 396 ALA n 
2 397 LEU n 
2 398 CYS n 
2 399 ILE n 
2 400 LEU n 
2 401 ILE n 
2 402 LEU n 
2 403 LEU n 
2 404 TYR n 
2 405 ALA n 
2 406 MET n 
2 407 TYR n 
2 408 LYS n 
2 409 TYR n 
2 410 ARG n 
2 411 ASN n 
2 412 ARG n 
2 413 ASP n 
2 414 GLU n 
2 415 GLY n 
2 416 SER n 
2 417 TYR n 
2 418 HIS n 
2 419 VAL n 
2 420 ASP n 
2 421 GLU n 
2 422 SER n 
2 423 ARG n 
2 424 ASN n 
2 425 TYR n 
2 426 ILE n 
2 427 SER n 
2 428 ASN n 
2 429 SER n 
2 430 ALA n 
2 431 GLN n 
2 432 SER n 
2 433 ASN n 
2 434 GLY n 
2 435 ALA n 
2 436 VAL n 
2 437 VAL n 
2 438 LYS n 
2 439 GLU n 
2 440 LYS n 
2 441 GLN n 
2 442 PRO n 
2 443 SER n 
2 444 SER n 
2 445 ALA n 
2 446 LYS n 
2 447 SER n 
2 448 ALA n 
2 449 ASN n 
2 450 LYS n 
2 451 ASN n 
2 452 LYS n 
2 453 LYS n 
2 454 ASN n 
2 455 LYS n 
2 456 ASP n 
2 457 LYS n 
2 458 GLU n 
2 459 TYR n 
2 460 TYR n 
2 461 VAL n 
2 462 SER n 
2 463 ASN n 
2 464 SER n 
2 465 LEU n 
2 466 GLU n 
2 467 VAL n 
2 468 LEU n 
2 469 PHE n 
2 470 GLN 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  870 'house mouse' ? Nlgn2 ? ? ? ? ? ? 'Mus musculus' 10090 ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1  62  'house mouse' ? Nrxn1 ? ? ? ? ? ? 'Mus musculus' 10090 ? ? ? ? ? ? ? ? 'Homo sapiens' 9606 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 2 sample 'Biological sequence' 63 470 'house mouse' ? Nrxn1 ? ? ? ? ? ? 'Mus musculus' 10090 ? ? ? ? ? ? ? ? '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 
CA  non-polymer                  . 'CALCIUM ION'                            ? 'Ca 2'           40.078  
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   -41 ?   ?   ?   A . n 
A 1 2   ALA 2   -40 ?   ?   ?   A . n 
A 1 3   LEU 3   -39 ?   ?   ?   A . n 
A 1 4   PRO 4   -38 ?   ?   ?   A . n 
A 1 5   ARG 5   -37 ?   ?   ?   A . n 
A 1 6   CYS 6   -36 ?   ?   ?   A . n 
A 1 7   MET 7   -35 ?   ?   ?   A . n 
A 1 8   TRP 8   -34 ?   ?   ?   A . n 
A 1 9   PRO 9   -33 ?   ?   ?   A . n 
A 1 10  ASN 10  -32 ?   ?   ?   A . n 
A 1 11  TYR 11  -31 ?   ?   ?   A . n 
A 1 12  VAL 12  -30 ?   ?   ?   A . n 
A 1 13  TRP 13  -29 ?   ?   ?   A . n 
A 1 14  ARG 14  -28 ?   ?   ?   A . n 
A 1 15  ALA 15  -27 ?   ?   ?   A . n 
A 1 16  MET 16  -26 ?   ?   ?   A . n 
A 1 17  MET 17  -25 ?   ?   ?   A . n 
A 1 18  ALA 18  -24 ?   ?   ?   A . n 
A 1 19  CYS 19  -23 ?   ?   ?   A . n 
A 1 20  VAL 20  -22 ?   ?   ?   A . n 
A 1 21  VAL 21  -21 ?   ?   ?   A . n 
A 1 22  HIS 22  -20 ?   ?   ?   A . n 
A 1 23  ARG 23  -19 ?   ?   ?   A . n 
A 1 24  GLY 24  -18 ?   ?   ?   A . n 
A 1 25  SER 25  -17 ?   ?   ?   A . n 
A 1 26  GLY 26  -16 ?   ?   ?   A . n 
A 1 27  ALA 27  -15 ?   ?   ?   A . n 
A 1 28  PRO 28  -14 ?   ?   ?   A . n 
A 1 29  LEU 29  -13 ?   ?   ?   A . n 
A 1 30  THR 30  -12 ?   ?   ?   A . n 
A 1 31  LEU 31  -11 ?   ?   ?   A . n 
A 1 32  CYS 32  -10 ?   ?   ?   A . n 
A 1 33  LEU 33  -9  ?   ?   ?   A . n 
A 1 34  LEU 34  -8  ?   ?   ?   A . n 
A 1 35  GLY 35  -7  ?   ?   ?   A . n 
A 1 36  CYS 36  -6  ?   ?   ?   A . n 
A 1 37  LEU 37  -5  ?   ?   ?   A . n 
A 1 38  LEU 38  -4  ?   ?   ?   A . n 
A 1 39  GLN 39  -3  ?   ?   ?   A . n 
A 1 40  THR 40  -2  ?   ?   ?   A . n 
A 1 41  PHE 41  -1  ?   ?   ?   A . n 
A 1 42  HIS 42  0   ?   ?   ?   A . n 
A 1 43  VAL 43  1   ?   ?   ?   A . n 
A 1 44  LEU 44  2   ?   ?   ?   A . n 
A 1 45  SER 45  3   ?   ?   ?   A . n 
A 1 46  GLN 46  4   ?   ?   ?   A . n 
A 1 47  LYS 47  5   ?   ?   ?   A . n 
A 1 48  TYR 48  6   ?   ?   ?   A . n 
A 1 49  PRO 49  7   ?   ?   ?   A . n 
A 1 50  TYR 50  8   ?   ?   ?   A . n 
A 1 51  ASP 51  9   ?   ?   ?   A . n 
A 1 52  VAL 52  10  ?   ?   ?   A . n 
A 1 53  PRO 53  11  ?   ?   ?   A . n 
A 1 54  ASP 54  12  ?   ?   ?   A . n 
A 1 55  TYR 55  13  ?   ?   ?   A . n 
A 1 56  ALA 56  14  ?   ?   ?   A . n 
A 1 57  GLN 57  15  ?   ?   ?   A . n 
A 1 58  ARG 58  16  ?   ?   ?   A . n 
A 1 59  GLY 59  17  ?   ?   ?   A . n 
A 1 60  GLY 60  18  ?   ?   ?   A . n 
A 1 61  GLY 61  19  ?   ?   ?   A . n 
A 1 62  GLY 62  20  ?   ?   ?   A . n 
A 1 63  PRO 63  21  ?   ?   ?   A . n 
A 1 64  GLY 64  22  ?   ?   ?   A . n 
A 1 65  GLY 65  23  ?   ?   ?   A . n 
A 1 66  GLY 66  24  ?   ?   ?   A . n 
A 1 67  ALA 67  25  ?   ?   ?   A . n 
A 1 68  PRO 68  26  ?   ?   ?   A . n 
A 1 69  GLY 69  27  ?   ?   ?   A . n 
A 1 70  GLY 70  28  ?   ?   ?   A . n 
A 1 71  PRO 71  29  ?   ?   ?   A . n 
A 1 72  GLY 72  30  ?   ?   ?   A . n 
A 1 73  LEU 73  31  ?   ?   ?   A . n 
A 1 74  GLY 74  32  ?   ?   ?   A . n 
A 1 75  LEU 75  33  ?   ?   ?   A . n 
A 1 76  GLY 76  34  ?   ?   ?   A . n 
A 1 77  SER 77  35  ?   ?   ?   A . n 
A 1 78  LEU 78  36  ?   ?   ?   A . n 
A 1 79  GLY 79  37  ?   ?   ?   A . n 
A 1 80  GLU 80  38  ?   ?   ?   A . n 
A 1 81  GLU 81  39  ?   ?   ?   A . n 
A 1 82  ARG 82  40  40  ARG ARG A . n 
A 1 83  PHE 83  41  41  PHE PHE A . n 
A 1 84  PRO 84  42  42  PRO PRO A . n 
A 1 85  VAL 85  43  43  VAL VAL A . n 
A 1 86  VAL 86  44  44  VAL VAL A . n 
A 1 87  ASN 87  45  45  ASN ASN A . n 
A 1 88  THR 88  46  46  THR THR A . n 
A 1 89  ALA 89  47  47  ALA ALA A . n 
A 1 90  TYR 90  48  48  TYR TYR A . n 
A 1 91  GLY 91  49  49  GLY GLY A . n 
A 1 92  ARG 92  50  50  ARG ARG A . n 
A 1 93  VAL 93  51  51  VAL VAL A . n 
A 1 94  ARG 94  52  52  ARG ARG A . n 
A 1 95  GLY 95  53  53  GLY GLY A . n 
A 1 96  VAL 96  54  54  VAL VAL A . n 
A 1 97  ARG 97  55  55  ARG ARG A . n 
A 1 98  ARG 98  56  56  ARG ARG A . n 
A 1 99  GLU 99  57  57  GLU GLU A . n 
A 1 100 LEU 100 58  58  LEU LEU A . n 
A 1 101 ASN 101 59  59  ASN ASN A . n 
A 1 102 ASN 102 60  60  ASN ASN A . n 
A 1 103 GLU 103 61  61  GLU GLU A . n 
A 1 104 ILE 104 62  62  ILE ILE A . n 
A 1 105 LEU 105 63  63  LEU LEU A . n 
A 1 106 GLY 106 64  64  GLY GLY A . n 
A 1 107 PRO 107 65  65  PRO PRO A . n 
A 1 108 VAL 108 66  66  VAL VAL A . n 
A 1 109 VAL 109 67  67  VAL VAL A . n 
A 1 110 GLN 110 68  68  GLN GLN A . n 
A 1 111 PHE 111 69  69  PHE PHE A . n 
A 1 112 LEU 112 70  70  LEU LEU A . n 
A 1 113 GLY 113 71  71  GLY GLY A . n 
A 1 114 VAL 114 72  72  VAL VAL A . n 
A 1 115 PRO 115 73  73  PRO PRO A . n 
A 1 116 TYR 116 74  74  TYR TYR A . n 
A 1 117 ALA 117 75  75  ALA ALA A . n 
A 1 118 THR 118 76  76  THR THR A . n 
A 1 119 PRO 119 77  77  PRO PRO A . n 
A 1 120 PRO 120 78  78  PRO PRO A . n 
A 1 121 LEU 121 79  79  LEU LEU A . n 
A 1 122 GLY 122 80  80  GLY GLY A . n 
A 1 123 ALA 123 81  81  ALA ALA A . n 
A 1 124 ARG 124 82  82  ARG ARG A . n 
A 1 125 ARG 125 83  83  ARG ARG A . n 
A 1 126 PHE 126 84  84  PHE PHE A . n 
A 1 127 GLN 127 85  85  GLN GLN A . n 
A 1 128 PRO 128 86  86  PRO PRO A . n 
A 1 129 PRO 129 87  87  PRO PRO A . n 
A 1 130 GLU 130 88  88  GLU GLU A . n 
A 1 131 ALA 131 89  89  ALA ALA A . n 
A 1 132 PRO 132 90  90  PRO PRO A . n 
A 1 133 ALA 133 91  91  ALA ALA A . n 
A 1 134 SER 134 92  92  SER SER A . n 
A 1 135 TRP 135 93  93  TRP TRP A . n 
A 1 136 PRO 136 94  94  PRO PRO A . n 
A 1 137 GLY 137 95  95  GLY GLY A . n 
A 1 138 VAL 138 96  96  VAL VAL A . n 
A 1 139 ARG 139 97  97  ARG ARG A . n 
A 1 140 ASN 140 98  98  ASN ASN A . n 
A 1 141 ALA 141 99  99  ALA ALA A . n 
A 1 142 THR 142 100 100 THR THR A . n 
A 1 143 THR 143 101 101 THR THR A . n 
A 1 144 LEU 144 102 102 LEU LEU A . n 
A 1 145 PRO 145 103 103 PRO PRO A . n 
A 1 146 PRO 146 104 104 PRO PRO A . n 
A 1 147 ALA 147 105 105 ALA ALA A . n 
A 1 148 CYS 148 106 106 CYS CYS A . n 
A 1 149 PRO 149 107 107 PRO PRO A . n 
A 1 150 GLN 150 108 108 GLN GLN A . n 
A 1 151 ASN 151 109 109 ASN ASN A . n 
A 1 152 LEU 152 110 110 LEU LEU A . n 
A 1 153 HIS 153 111 111 HIS HIS A . n 
A 1 154 GLY 154 112 112 GLY GLY A . n 
A 1 155 ALA 155 113 113 ALA ALA A . n 
A 1 156 LEU 156 114 114 LEU LEU A . n 
A 1 157 PRO 157 115 115 PRO PRO A . n 
A 1 158 ALA 158 116 116 ALA ALA A . n 
A 1 159 ILE 159 117 117 ILE ILE A . n 
A 1 160 MET 160 118 118 MET MET A . n 
A 1 161 LEU 161 119 119 LEU LEU A . n 
A 1 162 PRO 162 120 120 PRO PRO A . n 
A 1 163 VAL 163 121 121 VAL VAL A . n 
A 1 164 TRP 164 122 122 TRP TRP A . n 
A 1 165 PHE 165 123 123 PHE PHE A . n 
A 1 166 THR 166 124 124 THR THR A . n 
A 1 167 ASP 167 125 125 ASP ASP A . n 
A 1 168 ASN 168 126 126 ASN ASN A . n 
A 1 169 LEU 169 127 127 LEU LEU A . n 
A 1 170 GLU 170 128 128 GLU GLU A . n 
A 1 171 ALA 171 129 129 ALA ALA A . n 
A 1 172 ALA 172 130 130 ALA ALA A . n 
A 1 173 ALA 173 131 131 ALA ALA A . n 
A 1 174 THR 174 132 132 THR THR A . n 
A 1 175 TYR 175 133 133 TYR TYR A . n 
A 1 176 VAL 176 134 134 VAL VAL A . n 
A 1 177 GLN 177 135 135 GLN GLN A . n 
A 1 178 ASN 178 136 136 ASN ASN A . n 
A 1 179 GLN 179 137 137 GLN GLN A . n 
A 1 180 SER 180 138 138 SER SER A . n 
A 1 181 GLU 181 139 139 GLU GLU A . n 
A 1 182 ASP 182 140 140 ASP ASP A . n 
A 1 183 CYS 183 141 141 CYS CYS A . n 
A 1 184 LEU 184 142 142 LEU LEU A . n 
A 1 185 TYR 185 143 143 TYR TYR A . n 
A 1 186 LEU 186 144 144 LEU LEU A . n 
A 1 187 ASN 187 145 145 ASN ASN A . n 
A 1 188 LEU 188 146 146 LEU LEU A . n 
A 1 189 TYR 189 147 147 TYR TYR A . n 
A 1 190 VAL 190 148 148 VAL VAL A . n 
A 1 191 PRO 191 149 149 PRO PRO A . n 
A 1 192 THR 192 150 150 THR THR A . n 
A 1 193 GLU 193 168 ?   ?   ?   A . n 
A 1 194 ASP 194 169 ?   ?   ?   A . n 
A 1 195 ASP 195 170 ?   ?   ?   A . n 
A 1 196 ILE 196 171 ?   ?   ?   A . n 
A 1 197 ARG 197 172 ?   ?   ?   A . n 
A 1 198 ASP 198 173 ?   ?   ?   A . n 
A 1 199 SER 199 174 174 SER SER A . n 
A 1 200 GLY 200 175 175 GLY GLY A . n 
A 1 201 LYS 201 176 176 LYS LYS A . n 
A 1 202 LYS 202 177 177 LYS LYS A . n 
A 1 203 PRO 203 178 178 PRO PRO A . n 
A 1 204 VAL 204 179 179 VAL VAL A . n 
A 1 205 MET 205 180 180 MET MET A . n 
A 1 206 LEU 206 181 181 LEU LEU A . n 
A 1 207 PHE 207 182 182 PHE PHE A . n 
A 1 208 LEU 208 183 183 LEU LEU A . n 
A 1 209 HIS 209 184 184 HIS HIS A . n 
A 1 210 GLY 210 185 185 GLY GLY A . n 
A 1 211 GLY 211 186 186 GLY GLY A . n 
A 1 212 SER 212 187 187 SER SER A . n 
A 1 213 TYR 213 188 188 TYR TYR A . n 
A 1 214 MET 214 189 189 MET MET A . n 
A 1 215 GLU 215 190 190 GLU GLU A . n 
A 1 216 GLY 216 191 191 GLY GLY A . n 
A 1 217 THR 217 192 192 THR THR A . n 
A 1 218 GLY 218 193 193 GLY GLY A . n 
A 1 219 ASN 219 194 194 ASN ASN A . n 
A 1 220 MET 220 195 195 MET MET A . n 
A 1 221 PHE 221 196 196 PHE PHE A . n 
A 1 222 ASP 222 197 197 ASP ASP A . n 
A 1 223 GLY 223 198 198 GLY GLY A . n 
A 1 224 SER 224 199 199 SER SER A . n 
A 1 225 VAL 225 200 200 VAL VAL A . n 
A 1 226 LEU 226 201 201 LEU LEU A . n 
A 1 227 ALA 227 202 202 ALA ALA A . n 
A 1 228 ALA 228 203 203 ALA ALA A . n 
A 1 229 TYR 229 204 204 TYR TYR A . n 
A 1 230 GLY 230 205 205 GLY GLY A . n 
A 1 231 ASN 231 206 206 ASN ASN A . n 
A 1 232 VAL 232 207 207 VAL VAL A . n 
A 1 233 ILE 233 208 208 ILE ILE A . n 
A 1 234 VAL 234 209 209 VAL VAL A . n 
A 1 235 VAL 235 210 210 VAL VAL A . n 
A 1 236 THR 236 211 211 THR THR A . n 
A 1 237 LEU 237 212 212 LEU LEU A . n 
A 1 238 ASN 238 213 213 ASN ASN A . n 
A 1 239 TYR 239 214 214 TYR TYR A . n 
A 1 240 ARG 240 215 215 ARG ARG A . n 
A 1 241 LEU 241 216 216 LEU LEU A . n 
A 1 242 GLY 242 217 217 GLY GLY A . n 
A 1 243 VAL 243 218 218 VAL VAL A . n 
A 1 244 LEU 244 219 219 LEU LEU A . n 
A 1 245 GLY 245 220 220 GLY GLY A . n 
A 1 246 PHE 246 221 221 PHE PHE A . n 
A 1 247 LEU 247 222 222 LEU LEU A . n 
A 1 248 SER 248 223 223 SER SER A . n 
A 1 249 THR 249 224 224 THR THR A . n 
A 1 250 GLY 250 225 225 GLY GLY A . n 
A 1 251 ASP 251 226 226 ASP ASP A . n 
A 1 252 GLN 252 227 227 GLN GLN A . n 
A 1 253 ALA 253 228 228 ALA ALA A . n 
A 1 254 ALA 254 229 229 ALA ALA A . n 
A 1 255 LYS 255 230 230 LYS LYS A . n 
A 1 256 GLY 256 231 231 GLY GLY A . n 
A 1 257 ASN 257 232 232 ASN ASN A . n 
A 1 258 TYR 258 233 233 TYR TYR A . n 
A 1 259 GLY 259 234 234 GLY GLY A . n 
A 1 260 LEU 260 235 235 LEU LEU A . n 
A 1 261 LEU 261 236 236 LEU LEU A . n 
A 1 262 ASP 262 237 237 ASP ASP A . n 
A 1 263 GLN 263 238 238 GLN GLN A . n 
A 1 264 ILE 264 239 239 ILE ILE A . n 
A 1 265 GLN 265 240 240 GLN GLN A . n 
A 1 266 ALA 266 241 241 ALA ALA A . n 
A 1 267 LEU 267 242 242 LEU LEU A . n 
A 1 268 ARG 268 243 243 ARG ARG A . n 
A 1 269 TRP 269 244 244 TRP TRP A . n 
A 1 270 LEU 270 245 245 LEU LEU A . n 
A 1 271 SER 271 246 246 SER SER A . n 
A 1 272 GLU 272 247 247 GLU GLU A . n 
A 1 273 ASN 273 248 248 ASN ASN A . n 
A 1 274 ILE 274 249 249 ILE ILE A . n 
A 1 275 ALA 275 250 250 ALA ALA A . n 
A 1 276 HIS 276 251 251 HIS HIS A . n 
A 1 277 PHE 277 252 252 PHE PHE A . n 
A 1 278 GLY 278 253 253 GLY GLY A . n 
A 1 279 GLY 279 254 254 GLY GLY A . n 
A 1 280 ASP 280 255 255 ASP ASP A . n 
A 1 281 PRO 281 256 256 PRO PRO A . n 
A 1 282 GLU 282 257 257 GLU GLU A . n 
A 1 283 ARG 283 258 258 ARG ARG A . n 
A 1 284 ILE 284 259 259 ILE ILE A . n 
A 1 285 THR 285 260 260 THR THR A . n 
A 1 286 ILE 286 261 261 ILE ILE A . n 
A 1 287 PHE 287 262 262 PHE PHE A . n 
A 1 288 GLY 288 263 263 GLY GLY A . n 
A 1 289 SER 289 264 264 SER SER A . n 
A 1 290 GLY 290 265 265 GLY GLY A . n 
A 1 291 ALA 291 266 266 ALA ALA A . n 
A 1 292 GLY 292 267 267 GLY GLY A . n 
A 1 293 ALA 293 268 268 ALA ALA A . n 
A 1 294 SER 294 269 269 SER SER A . n 
A 1 295 CYS 295 270 270 CYS CYS A . n 
A 1 296 VAL 296 271 271 VAL VAL A . n 
A 1 297 ASN 297 272 272 ASN ASN A . n 
A 1 298 LEU 298 273 273 LEU LEU A . n 
A 1 299 LEU 299 274 274 LEU LEU A . n 
A 1 300 ILE 300 275 275 ILE ILE A . n 
A 1 301 LEU 301 276 276 LEU LEU A . n 
A 1 302 SER 302 277 277 SER SER A . n 
A 1 303 HIS 303 278 278 HIS HIS A . n 
A 1 304 HIS 304 279 279 HIS HIS A . n 
A 1 305 SER 305 280 280 SER SER A . n 
A 1 306 GLU 306 281 281 GLU GLU A . n 
A 1 307 GLY 307 282 282 GLY GLY A . n 
A 1 308 LEU 308 283 283 LEU LEU A . n 
A 1 309 PHE 309 284 284 PHE PHE A . n 
A 1 310 GLN 310 285 285 GLN GLN A . n 
A 1 311 LYS 311 286 286 LYS LYS A . n 
A 1 312 ALA 312 287 287 ALA ALA A . n 
A 1 313 ILE 313 288 288 ILE ILE A . n 
A 1 314 ALA 314 289 289 ALA ALA A . n 
A 1 315 GLN 315 290 290 GLN GLN A . n 
A 1 316 SER 316 291 291 SER SER A . n 
A 1 317 GLY 317 292 292 GLY GLY A . n 
A 1 318 THR 318 293 293 THR THR A . n 
A 1 319 ALA 319 294 294 ALA ALA A . n 
A 1 320 ILE 320 295 295 ILE ILE A . n 
A 1 321 SER 321 296 296 SER SER A . n 
A 1 322 SER 322 297 297 SER SER A . n 
A 1 323 TRP 323 298 298 TRP TRP A . n 
A 1 324 SER 324 299 299 SER SER A . n 
A 1 325 VAL 325 300 300 VAL VAL A . n 
A 1 326 ASN 326 301 301 ASN ASN A . n 
A 1 327 TYR 327 302 302 TYR TYR A . n 
A 1 328 GLN 328 303 303 GLN GLN A . n 
A 1 329 PRO 329 304 304 PRO PRO A . n 
A 1 330 LEU 330 305 305 LEU LEU A . n 
A 1 331 LYS 331 306 306 LYS LYS A . n 
A 1 332 TYR 332 307 307 TYR TYR A . n 
A 1 333 THR 333 308 308 THR THR A . n 
A 1 334 ARG 334 309 309 ARG ARG A . n 
A 1 335 LEU 335 310 310 LEU LEU A . n 
A 1 336 LEU 336 311 311 LEU LEU A . n 
A 1 337 ALA 337 312 312 ALA ALA A . n 
A 1 338 ALA 338 313 313 ALA ALA A . n 
A 1 339 LYS 339 314 314 LYS LYS A . n 
A 1 340 VAL 340 315 315 VAL VAL A . n 
A 1 341 GLY 341 316 316 GLY GLY A . n 
A 1 342 CYS 342 317 317 CYS CYS A . n 
A 1 343 ASP 343 318 318 ASP ASP A . n 
A 1 344 ARG 344 319 319 ARG ARG A . n 
A 1 345 GLU 345 320 320 GLU GLU A . n 
A 1 346 ASP 346 321 321 ASP ASP A . n 
A 1 347 SER 347 322 322 SER SER A . n 
A 1 348 THR 348 323 323 THR THR A . n 
A 1 349 GLU 349 324 324 GLU GLU A . n 
A 1 350 ALA 350 325 325 ALA ALA A . n 
A 1 351 VAL 351 326 326 VAL VAL A . n 
A 1 352 GLU 352 327 327 GLU GLU A . n 
A 1 353 CYS 353 328 328 CYS CYS A . n 
A 1 354 LEU 354 329 329 LEU LEU A . n 
A 1 355 ARG 355 330 330 ARG ARG A . n 
A 1 356 ARG 356 331 331 ARG ARG A . n 
A 1 357 LYS 357 332 332 LYS LYS A . n 
A 1 358 SER 358 333 333 SER SER A . n 
A 1 359 SER 359 334 334 SER SER A . n 
A 1 360 ARG 360 335 335 ARG ARG A . n 
A 1 361 GLU 361 336 336 GLU GLU A . n 
A 1 362 LEU 362 337 337 LEU LEU A . n 
A 1 363 VAL 363 338 338 VAL VAL A . n 
A 1 364 ASP 364 339 339 ASP ASP A . n 
A 1 365 GLN 365 340 340 GLN GLN A . n 
A 1 366 ASP 366 341 341 ASP ASP A . n 
A 1 367 VAL 367 342 342 VAL VAL A . n 
A 1 368 GLN 368 343 343 GLN GLN A . n 
A 1 369 PRO 369 344 344 PRO PRO A . n 
A 1 370 ALA 370 345 345 ALA ALA A . n 
A 1 371 ARG 371 346 346 ARG ARG A . n 
A 1 372 TYR 372 347 347 TYR TYR A . n 
A 1 373 HIS 373 348 348 HIS HIS A . n 
A 1 374 ILE 374 349 349 ILE ILE A . n 
A 1 375 ALA 375 350 350 ALA ALA A . n 
A 1 376 PHE 376 351 351 PHE PHE A . n 
A 1 377 GLY 377 352 352 GLY GLY A . n 
A 1 378 PRO 378 353 353 PRO PRO A . n 
A 1 379 VAL 379 354 354 VAL VAL A . n 
A 1 380 VAL 380 355 355 VAL VAL A . n 
A 1 381 ASP 381 356 356 ASP ASP A . n 
A 1 382 GLY 382 357 357 GLY GLY A . n 
A 1 383 ASP 383 358 358 ASP ASP A . n 
A 1 384 VAL 384 359 359 VAL VAL A . n 
A 1 385 VAL 385 360 360 VAL VAL A . n 
A 1 386 PRO 386 361 361 PRO PRO A . n 
A 1 387 ASP 387 362 362 ASP ASP A . n 
A 1 388 ASP 388 363 363 ASP ASP A . n 
A 1 389 PRO 389 364 364 PRO PRO A . n 
A 1 390 GLU 390 365 365 GLU GLU A . n 
A 1 391 ILE 391 366 366 ILE ILE A . n 
A 1 392 LEU 392 367 367 LEU LEU A . n 
A 1 393 MET 393 368 368 MET MET A . n 
A 1 394 GLN 394 369 369 GLN GLN A . n 
A 1 395 GLN 395 370 370 GLN GLN A . n 
A 1 396 GLY 396 371 371 GLY GLY A . n 
A 1 397 GLU 397 372 372 GLU GLU A . n 
A 1 398 PHE 398 373 373 PHE PHE A . n 
A 1 399 LEU 399 374 374 LEU LEU A . n 
A 1 400 ASN 400 375 375 ASN ASN A . n 
A 1 401 TYR 401 376 376 TYR TYR A . n 
A 1 402 ASP 402 377 377 ASP ASP A . n 
A 1 403 MET 403 378 378 MET MET A . n 
A 1 404 LEU 404 379 379 LEU LEU A . n 
A 1 405 ILE 405 380 380 ILE ILE A . n 
A 1 406 GLY 406 381 381 GLY GLY A . n 
A 1 407 VAL 407 382 382 VAL VAL A . n 
A 1 408 ASN 408 383 383 ASN ASN A . n 
A 1 409 GLN 409 384 384 GLN GLN A . n 
A 1 410 GLY 410 385 385 GLY GLY A . n 
A 1 411 GLU 411 386 386 GLU GLU A . n 
A 1 412 GLY 412 387 387 GLY GLY A . n 
A 1 413 LEU 413 388 388 LEU LEU A . n 
A 1 414 LYS 414 389 389 LYS LYS A . n 
A 1 415 PHE 415 390 390 PHE PHE A . n 
A 1 416 VAL 416 391 391 VAL VAL A . n 
A 1 417 GLU 417 392 392 GLU GLU A . n 
A 1 418 ASP 418 393 393 ASP ASP A . n 
A 1 419 SER 419 394 394 SER SER A . n 
A 1 420 ALA 420 395 395 ALA ALA A . n 
A 1 421 GLU 421 396 396 GLU GLU A . n 
A 1 422 SER 422 397 397 SER SER A . n 
A 1 423 GLU 423 398 398 GLU GLU A . n 
A 1 424 ASP 424 399 399 ASP ASP A . n 
A 1 425 GLY 425 400 400 GLY GLY A . n 
A 1 426 VAL 426 401 401 VAL VAL A . n 
A 1 427 SER 427 402 402 SER SER A . n 
A 1 428 ALA 428 403 403 ALA ALA A . n 
A 1 429 SER 429 404 404 SER SER A . n 
A 1 430 ALA 430 405 405 ALA ALA A . n 
A 1 431 PHE 431 406 406 PHE PHE A . n 
A 1 432 ASP 432 407 407 ASP ASP A . n 
A 1 433 PHE 433 408 408 PHE PHE A . n 
A 1 434 THR 434 409 409 THR THR A . n 
A 1 435 VAL 435 410 410 VAL VAL A . n 
A 1 436 SER 436 411 411 SER SER A . n 
A 1 437 ASN 437 412 412 ASN ASN A . n 
A 1 438 PHE 438 413 413 PHE PHE A . n 
A 1 439 VAL 439 414 414 VAL VAL A . n 
A 1 440 ASP 440 415 415 ASP ASP A . n 
A 1 441 ASN 441 416 416 ASN ASN A . n 
A 1 442 LEU 442 417 417 LEU LEU A . n 
A 1 443 TYR 443 418 418 TYR TYR A . n 
A 1 444 GLY 444 419 419 GLY GLY A . n 
A 1 445 TYR 445 420 420 TYR TYR A . n 
A 1 446 PRO 446 421 421 PRO PRO A . n 
A 1 447 GLU 447 422 422 GLU GLU A . n 
A 1 448 GLY 448 423 423 GLY GLY A . n 
A 1 449 LYS 449 424 424 LYS LYS A . n 
A 1 450 ASP 450 425 425 ASP ASP A . n 
A 1 451 VAL 451 426 426 VAL VAL A . n 
A 1 452 LEU 452 427 427 LEU LEU A . n 
A 1 453 ARG 453 428 428 ARG ARG A . n 
A 1 454 GLU 454 429 429 GLU GLU A . n 
A 1 455 THR 455 430 430 THR THR A . n 
A 1 456 ILE 456 431 431 ILE ILE A . n 
A 1 457 LYS 457 432 432 LYS LYS A . n 
A 1 458 PHE 458 433 433 PHE PHE A . n 
A 1 459 MET 459 434 434 MET MET A . n 
A 1 460 TYR 460 435 435 TYR TYR A . n 
A 1 461 THR 461 436 436 THR THR A . n 
A 1 462 ASP 462 437 437 ASP ASP A . n 
A 1 463 TRP 463 438 438 TRP TRP A . n 
A 1 464 ALA 464 439 439 ALA ALA A . n 
A 1 465 ASP 465 440 440 ASP ASP A . n 
A 1 466 ARG 466 441 441 ARG ARG A . n 
A 1 467 ASP 467 442 442 ASP ASP A . n 
A 1 468 ASN 468 443 443 ASN ASN A . n 
A 1 469 GLY 469 444 444 GLY GLY A . n 
A 1 470 GLU 470 445 445 GLU GLU A . n 
A 1 471 MET 471 446 446 MET MET A . n 
A 1 472 ARG 472 447 447 ARG ARG A . n 
A 1 473 ARG 473 448 448 ARG ARG A . n 
A 1 474 LYS 474 449 449 LYS LYS A . n 
A 1 475 THR 475 450 450 THR THR A . n 
A 1 476 LEU 476 451 451 LEU LEU A . n 
A 1 477 LEU 477 452 452 LEU LEU A . n 
A 1 478 ALA 478 453 453 ALA ALA A . n 
A 1 479 LEU 479 454 454 LEU LEU A . n 
A 1 480 PHE 480 455 455 PHE PHE A . n 
A 1 481 THR 481 456 456 THR THR A . n 
A 1 482 ASP 482 457 457 ASP ASP A . n 
A 1 483 HIS 483 458 458 HIS HIS A . n 
A 1 484 GLN 484 459 459 GLN GLN A . n 
A 1 485 TRP 485 460 460 TRP TRP A . n 
A 1 486 VAL 486 461 461 VAL VAL A . n 
A 1 487 ALA 487 462 462 ALA ALA A . n 
A 1 488 PRO 488 463 463 PRO PRO A . n 
A 1 489 ALA 489 464 464 ALA ALA A . n 
A 1 490 VAL 490 465 465 VAL VAL A . n 
A 1 491 ALA 491 466 466 ALA ALA A . n 
A 1 492 THR 492 467 467 THR THR A . n 
A 1 493 ALA 493 468 468 ALA ALA A . n 
A 1 494 LYS 494 469 469 LYS LYS A . n 
A 1 495 LEU 495 470 470 LEU LEU A . n 
A 1 496 HIS 496 471 471 HIS HIS A . n 
A 1 497 ALA 497 472 472 ALA ALA A . n 
A 1 498 ASP 498 473 473 ASP ASP A . n 
A 1 499 TYR 499 474 474 TYR TYR A . n 
A 1 500 GLN 500 475 475 GLN GLN A . n 
A 1 501 SER 501 476 476 SER SER A . n 
A 1 502 PRO 502 477 477 PRO PRO A . n 
A 1 503 VAL 503 478 478 VAL VAL A . n 
A 1 504 TYR 504 479 479 TYR TYR A . n 
A 1 505 PHE 505 480 480 PHE PHE A . n 
A 1 506 TYR 506 481 481 TYR TYR A . n 
A 1 507 THR 507 482 482 THR THR A . n 
A 1 508 PHE 508 483 483 PHE PHE A . n 
A 1 509 TYR 509 484 484 TYR TYR A . n 
A 1 510 HIS 510 485 485 HIS HIS A . n 
A 1 511 HIS 511 486 486 HIS HIS A . n 
A 1 512 CYS 512 487 487 CYS CYS A . n 
A 1 513 GLN 513 488 488 GLN GLN A . n 
A 1 514 ALA 514 489 489 ALA ALA A . n 
A 1 515 GLU 515 490 490 GLU GLU A . n 
A 1 516 GLY 516 491 491 GLY GLY A . n 
A 1 517 ARG 517 492 492 ARG ARG A . n 
A 1 518 PRO 518 493 493 PRO PRO A . n 
A 1 519 GLU 519 494 494 GLU GLU A . n 
A 1 520 TRP 520 495 495 TRP TRP A . n 
A 1 521 ALA 521 496 496 ALA ALA A . n 
A 1 522 ASP 522 497 497 ASP ASP A . n 
A 1 523 ALA 523 498 498 ALA ALA A . n 
A 1 524 ALA 524 499 499 ALA ALA A . n 
A 1 525 HIS 525 500 500 HIS HIS A . n 
A 1 526 GLY 526 501 501 GLY GLY A . n 
A 1 527 ASP 527 502 502 ASP ASP A . n 
A 1 528 GLU 528 503 503 GLU GLU A . n 
A 1 529 LEU 529 504 504 LEU LEU A . n 
A 1 530 PRO 530 505 505 PRO PRO A . n 
A 1 531 TYR 531 506 506 TYR TYR A . n 
A 1 532 VAL 532 507 507 VAL VAL A . n 
A 1 533 PHE 533 508 508 PHE PHE A . n 
A 1 534 GLY 534 509 509 GLY GLY A . n 
A 1 535 VAL 535 510 510 VAL VAL A . n 
A 1 536 PRO 536 511 511 PRO PRO A . n 
A 1 537 MET 537 512 512 MET MET A . n 
A 1 538 VAL 538 513 513 VAL VAL A . n 
A 1 539 GLY 539 514 514 GLY GLY A . n 
A 1 540 ALA 540 515 515 ALA ALA A . n 
A 1 541 THR 541 516 516 THR THR A . n 
A 1 542 ASP 542 517 517 ASP ASP A . n 
A 1 543 LEU 543 518 518 LEU LEU A . n 
A 1 544 PHE 544 519 519 PHE PHE A . n 
A 1 545 PRO 545 520 520 PRO PRO A . n 
A 1 546 CYS 546 521 521 CYS CYS A . n 
A 1 547 ASN 547 522 522 ASN ASN A . n 
A 1 548 PHE 548 523 523 PHE PHE A . n 
A 1 549 SER 549 524 524 SER SER A . n 
A 1 550 LYS 550 525 525 LYS LYS A . n 
A 1 551 ASN 551 526 526 ASN ASN A . n 
A 1 552 ASP 552 527 527 ASP ASP A . n 
A 1 553 VAL 553 528 528 VAL VAL A . n 
A 1 554 MET 554 529 529 MET MET A . n 
A 1 555 LEU 555 530 530 LEU LEU A . n 
A 1 556 SER 556 531 531 SER SER A . n 
A 1 557 ALA 557 532 532 ALA ALA A . n 
A 1 558 VAL 558 533 533 VAL VAL A . n 
A 1 559 VAL 559 534 534 VAL VAL A . n 
A 1 560 MET 560 535 535 MET MET A . n 
A 1 561 THR 561 536 536 THR THR A . n 
A 1 562 TYR 562 537 537 TYR TYR A . n 
A 1 563 TRP 563 538 538 TRP TRP A . n 
A 1 564 THR 564 539 539 THR THR A . n 
A 1 565 ASN 565 540 540 ASN ASN A . n 
A 1 566 PHE 566 541 541 PHE PHE A . n 
A 1 567 ALA 567 542 542 ALA ALA A . n 
A 1 568 LYS 568 543 543 LYS LYS A . n 
A 1 569 THR 569 544 544 THR THR A . n 
A 1 570 GLY 570 545 545 GLY GLY A . n 
A 1 571 ASP 571 546 546 ASP ASP A . n 
A 1 572 PRO 572 547 547 PRO PRO A . n 
A 1 573 ASN 573 548 548 ASN ASN A . n 
A 1 574 GLN 574 549 549 GLN GLN A . n 
A 1 575 PRO 575 550 550 PRO PRO A . n 
A 1 576 VAL 576 551 551 VAL VAL A . n 
A 1 577 PRO 577 552 552 PRO PRO A . n 
A 1 578 GLN 578 553 553 GLN GLN A . n 
A 1 579 ASP 579 554 554 ASP ASP A . n 
A 1 580 THR 580 555 ?   ?   ?   A . n 
A 1 581 LYS 581 556 ?   ?   ?   A . n 
A 1 582 PHE 582 557 ?   ?   ?   A . n 
A 1 583 ILE 583 558 ?   ?   ?   A . n 
A 1 584 HIS 584 559 ?   ?   ?   A . n 
A 1 585 THR 585 560 ?   ?   ?   A . n 
A 1 586 LYS 586 561 ?   ?   ?   A . n 
A 1 587 PRO 587 562 ?   ?   ?   A . n 
A 1 588 ASN 588 563 ?   ?   ?   A . n 
A 1 589 ARG 589 564 564 ARG ARG A . n 
A 1 590 PHE 590 565 565 PHE PHE A . n 
A 1 591 GLU 591 566 566 GLU GLU A . n 
A 1 592 GLU 592 567 567 GLU GLU A . n 
A 1 593 VAL 593 568 568 VAL VAL A . n 
A 1 594 VAL 594 569 569 VAL VAL A . n 
A 1 595 TRP 595 570 570 TRP TRP A . n 
A 1 596 SER 596 571 571 SER SER A . n 
A 1 597 LYS 597 572 572 LYS LYS A . n 
A 1 598 PHE 598 573 573 PHE PHE A . n 
A 1 599 ASN 599 574 574 ASN ASN A . n 
A 1 600 SER 600 575 575 SER SER A . n 
A 1 601 LYS 601 576 576 LYS LYS A . n 
A 1 602 GLU 602 577 577 GLU GLU A . n 
A 1 603 LYS 603 578 578 LYS LYS A . n 
A 1 604 GLN 604 579 579 GLN GLN A . n 
A 1 605 TYR 605 580 580 TYR TYR A . n 
A 1 606 LEU 606 581 581 LEU LEU A . n 
A 1 607 HIS 607 582 582 HIS HIS A . n 
A 1 608 ILE 608 583 583 ILE ILE A . n 
A 1 609 GLY 609 584 584 GLY GLY A . n 
A 1 610 LEU 610 585 585 LEU LEU A . n 
A 1 611 LYS 611 586 586 LYS LYS A . n 
A 1 612 PRO 612 587 587 PRO PRO A . n 
A 1 613 ARG 613 588 588 ARG ARG A . n 
A 1 614 VAL 614 589 589 VAL VAL A . n 
A 1 615 ARG 615 590 590 ARG ARG A . n 
A 1 616 ASP 616 591 591 ASP ASP A . n 
A 1 617 ASN 617 592 592 ASN ASN A . n 
A 1 618 TYR 618 593 593 TYR TYR A . n 
A 1 619 ARG 619 594 594 ARG ARG A . n 
A 1 620 ALA 620 595 595 ALA ALA A . n 
A 1 621 ASN 621 596 596 ASN ASN A . n 
A 1 622 LYS 622 597 597 LYS LYS A . n 
A 1 623 VAL 623 598 598 VAL VAL A . n 
A 1 624 ALA 624 599 599 ALA ALA A . n 
A 1 625 PHE 625 600 600 PHE PHE A . n 
A 1 626 TRP 626 601 601 TRP TRP A . n 
A 1 627 LEU 627 602 602 LEU LEU A . n 
A 1 628 GLU 628 603 603 GLU GLU A . n 
A 1 629 LEU 629 604 604 LEU LEU A . n 
A 1 630 VAL 630 605 605 VAL VAL A . n 
A 1 631 PRO 631 606 606 PRO PRO A . n 
A 1 632 HIS 632 607 607 HIS HIS A . n 
A 1 633 LEU 633 608 608 LEU LEU A . n 
A 1 634 HIS 634 609 ?   ?   ?   A . n 
A 1 635 ASN 635 610 ?   ?   ?   A . n 
A 1 636 LEU 636 611 ?   ?   ?   A . n 
A 1 637 HIS 637 612 ?   ?   ?   A . n 
A 1 638 THR 638 613 ?   ?   ?   A . n 
A 1 639 GLU 639 614 ?   ?   ?   A . n 
A 1 640 LEU 640 615 ?   ?   ?   A . n 
A 1 641 PHE 641 616 ?   ?   ?   A . n 
A 1 642 THR 642 617 ?   ?   ?   A . n 
A 1 643 THR 643 618 ?   ?   ?   A . n 
A 1 644 THR 644 619 ?   ?   ?   A . n 
A 1 645 THR 645 620 ?   ?   ?   A . n 
A 1 646 ARG 646 621 ?   ?   ?   A . n 
A 1 647 LEU 647 622 ?   ?   ?   A . n 
A 1 648 PRO 648 623 ?   ?   ?   A . n 
A 1 649 PRO 649 624 ?   ?   ?   A . n 
A 1 650 TYR 650 625 ?   ?   ?   A . n 
A 1 651 ALA 651 626 ?   ?   ?   A . n 
A 1 652 THR 652 627 ?   ?   ?   A . n 
A 1 653 ARG 653 628 ?   ?   ?   A . n 
A 1 654 TRP 654 629 ?   ?   ?   A . n 
A 1 655 PRO 655 630 ?   ?   ?   A . n 
A 1 656 PRO 656 631 ?   ?   ?   A . n 
A 1 657 ARG 657 632 ?   ?   ?   A . n 
A 1 658 THR 658 633 ?   ?   ?   A . n 
A 1 659 PRO 659 634 ?   ?   ?   A . n 
A 1 660 GLY 660 635 ?   ?   ?   A . n 
A 1 661 PRO 661 636 ?   ?   ?   A . n 
A 1 662 GLY 662 637 ?   ?   ?   A . n 
A 1 663 THR 663 638 ?   ?   ?   A . n 
A 1 664 SER 664 639 ?   ?   ?   A . n 
A 1 665 GLY 665 640 ?   ?   ?   A . n 
A 1 666 THR 666 641 ?   ?   ?   A . n 
A 1 667 ARG 667 642 ?   ?   ?   A . n 
A 1 668 ARG 668 643 ?   ?   ?   A . n 
A 1 669 PRO 669 644 ?   ?   ?   A . n 
A 1 670 PRO 670 645 ?   ?   ?   A . n 
A 1 671 PRO 671 646 ?   ?   ?   A . n 
A 1 672 PRO 672 647 ?   ?   ?   A . n 
A 1 673 ALA 673 648 ?   ?   ?   A . n 
A 1 674 THR 674 649 ?   ?   ?   A . n 
A 1 675 LEU 675 650 ?   ?   ?   A . n 
A 1 676 PRO 676 651 ?   ?   ?   A . n 
A 1 677 PRO 677 652 ?   ?   ?   A . n 
A 1 678 GLU 678 653 ?   ?   ?   A . n 
A 1 679 SER 679 654 ?   ?   ?   A . n 
A 1 680 ASP 680 655 ?   ?   ?   A . n 
A 1 681 ILE 681 656 ?   ?   ?   A . n 
A 1 682 ASP 682 657 ?   ?   ?   A . n 
A 1 683 LEU 683 658 ?   ?   ?   A . n 
A 1 684 GLY 684 659 ?   ?   ?   A . n 
A 1 685 PRO 685 660 ?   ?   ?   A . n 
A 1 686 ARG 686 661 ?   ?   ?   A . n 
A 1 687 ALA 687 662 ?   ?   ?   A . n 
A 1 688 TYR 688 663 ?   ?   ?   A . n 
A 1 689 ASP 689 664 ?   ?   ?   A . n 
A 1 690 ARG 690 665 ?   ?   ?   A . n 
A 1 691 PHE 691 666 ?   ?   ?   A . n 
A 1 692 PRO 692 667 ?   ?   ?   A . n 
A 1 693 GLY 693 668 ?   ?   ?   A . n 
A 1 694 ASP 694 669 ?   ?   ?   A . n 
A 1 695 SER 695 670 ?   ?   ?   A . n 
A 1 696 ARG 696 671 ?   ?   ?   A . n 
A 1 697 ASP 697 672 ?   ?   ?   A . n 
A 1 698 TYR 698 673 ?   ?   ?   A . n 
A 1 699 SER 699 674 ?   ?   ?   A . n 
A 1 700 THR 700 675 ?   ?   ?   A . n 
A 1 701 GLU 701 676 ?   ?   ?   A . n 
A 1 702 LEU 702 677 ?   ?   ?   A . n 
A 1 703 SER 703 678 ?   ?   ?   A . n 
A 1 704 VAL 704 679 ?   ?   ?   A . n 
A 1 705 THR 705 680 ?   ?   ?   A . n 
A 1 706 VAL 706 681 ?   ?   ?   A . n 
A 1 707 ALA 707 682 ?   ?   ?   A . n 
A 1 708 VAL 708 683 ?   ?   ?   A . n 
A 1 709 GLY 709 684 ?   ?   ?   A . n 
A 1 710 ALA 710 685 ?   ?   ?   A . n 
A 1 711 SER 711 686 ?   ?   ?   A . n 
A 1 712 LEU 712 687 ?   ?   ?   A . n 
A 1 713 LEU 713 688 ?   ?   ?   A . n 
A 1 714 PHE 714 689 ?   ?   ?   A . n 
A 1 715 LEU 715 690 ?   ?   ?   A . n 
A 1 716 ASN 716 691 ?   ?   ?   A . n 
A 1 717 ILE 717 692 ?   ?   ?   A . n 
A 1 718 LEU 718 693 ?   ?   ?   A . n 
A 1 719 ALA 719 694 ?   ?   ?   A . n 
A 1 720 PHE 720 695 ?   ?   ?   A . n 
A 1 721 ALA 721 696 ?   ?   ?   A . n 
A 1 722 ALA 722 697 ?   ?   ?   A . n 
A 1 723 LEU 723 698 ?   ?   ?   A . n 
A 1 724 TYR 724 699 ?   ?   ?   A . n 
A 1 725 TYR 725 700 ?   ?   ?   A . n 
A 1 726 LYS 726 701 ?   ?   ?   A . n 
A 1 727 ARG 727 702 ?   ?   ?   A . n 
A 1 728 ASP 728 703 ?   ?   ?   A . n 
A 1 729 ARG 729 704 ?   ?   ?   A . n 
A 1 730 ARG 730 705 ?   ?   ?   A . n 
A 1 731 GLN 731 706 ?   ?   ?   A . n 
A 1 732 GLU 732 707 ?   ?   ?   A . n 
A 1 733 LEU 733 708 ?   ?   ?   A . n 
A 1 734 ARG 734 709 ?   ?   ?   A . n 
A 1 735 CYS 735 710 ?   ?   ?   A . n 
A 1 736 ARG 736 711 ?   ?   ?   A . n 
A 1 737 ARG 737 712 ?   ?   ?   A . n 
A 1 738 LEU 738 713 ?   ?   ?   A . n 
A 1 739 SER 739 714 ?   ?   ?   A . n 
A 1 740 PRO 740 715 ?   ?   ?   A . n 
A 1 741 PRO 741 716 ?   ?   ?   A . n 
A 1 742 GLY 742 717 ?   ?   ?   A . n 
A 1 743 GLY 743 718 ?   ?   ?   A . n 
A 1 744 SER 744 719 ?   ?   ?   A . n 
A 1 745 GLY 745 720 ?   ?   ?   A . n 
A 1 746 SER 746 721 ?   ?   ?   A . n 
A 1 747 GLY 747 722 ?   ?   ?   A . n 
A 1 748 VAL 748 723 ?   ?   ?   A . n 
A 1 749 PRO 749 724 ?   ?   ?   A . n 
A 1 750 GLY 750 725 ?   ?   ?   A . n 
A 1 751 GLY 751 726 ?   ?   ?   A . n 
A 1 752 GLY 752 727 ?   ?   ?   A . n 
A 1 753 PRO 753 728 ?   ?   ?   A . n 
A 1 754 LEU 754 729 ?   ?   ?   A . n 
A 1 755 LEU 755 730 ?   ?   ?   A . n 
A 1 756 PRO 756 731 ?   ?   ?   A . n 
A 1 757 THR 757 732 ?   ?   ?   A . n 
A 1 758 ALA 758 733 ?   ?   ?   A . n 
A 1 759 GLY 759 734 ?   ?   ?   A . n 
A 1 760 ARG 760 735 ?   ?   ?   A . n 
A 1 761 GLU 761 736 ?   ?   ?   A . n 
A 1 762 LEU 762 737 ?   ?   ?   A . n 
A 1 763 PRO 763 738 ?   ?   ?   A . n 
A 1 764 PRO 764 739 ?   ?   ?   A . n 
A 1 765 GLU 765 740 ?   ?   ?   A . n 
A 1 766 GLU 766 741 ?   ?   ?   A . n 
A 1 767 GLU 767 742 ?   ?   ?   A . n 
A 1 768 LEU 768 743 ?   ?   ?   A . n 
A 1 769 VAL 769 744 ?   ?   ?   A . n 
A 1 770 SER 770 745 ?   ?   ?   A . n 
A 1 771 LEU 771 746 ?   ?   ?   A . n 
A 1 772 GLN 772 747 ?   ?   ?   A . n 
A 1 773 LEU 773 748 ?   ?   ?   A . n 
A 1 774 LYS 774 749 ?   ?   ?   A . n 
A 1 775 ARG 775 750 ?   ?   ?   A . n 
A 1 776 GLY 776 751 ?   ?   ?   A . n 
A 1 777 GLY 777 752 ?   ?   ?   A . n 
A 1 778 GLY 778 753 ?   ?   ?   A . n 
A 1 779 VAL 779 754 ?   ?   ?   A . n 
A 1 780 GLY 780 755 ?   ?   ?   A . n 
A 1 781 ALA 781 756 ?   ?   ?   A . n 
A 1 782 ASP 782 757 ?   ?   ?   A . n 
A 1 783 PRO 783 758 ?   ?   ?   A . n 
A 1 784 ALA 784 759 ?   ?   ?   A . n 
A 1 785 GLU 785 760 ?   ?   ?   A . n 
A 1 786 ALA 786 761 ?   ?   ?   A . n 
A 1 787 LEU 787 762 ?   ?   ?   A . n 
A 1 788 ARG 788 763 ?   ?   ?   A . n 
A 1 789 PRO 789 764 ?   ?   ?   A . n 
A 1 790 ALA 790 765 ?   ?   ?   A . n 
A 1 791 CYS 791 766 ?   ?   ?   A . n 
A 1 792 PRO 792 767 ?   ?   ?   A . n 
A 1 793 PRO 793 768 ?   ?   ?   A . n 
A 1 794 ASP 794 769 ?   ?   ?   A . n 
A 1 795 TYR 795 770 ?   ?   ?   A . n 
A 1 796 THR 796 771 ?   ?   ?   A . n 
A 1 797 LEU 797 772 ?   ?   ?   A . n 
A 1 798 ALA 798 773 ?   ?   ?   A . n 
A 1 799 LEU 799 774 ?   ?   ?   A . n 
A 1 800 ARG 800 775 ?   ?   ?   A . n 
A 1 801 ARG 801 776 ?   ?   ?   A . n 
A 1 802 ALA 802 777 ?   ?   ?   A . n 
A 1 803 PRO 803 778 ?   ?   ?   A . n 
A 1 804 ASP 804 779 ?   ?   ?   A . n 
A 1 805 ASP 805 780 ?   ?   ?   A . n 
A 1 806 VAL 806 781 ?   ?   ?   A . n 
A 1 807 PRO 807 782 ?   ?   ?   A . n 
A 1 808 LEU 808 783 ?   ?   ?   A . n 
A 1 809 LEU 809 784 ?   ?   ?   A . n 
A 1 810 ALA 810 785 ?   ?   ?   A . n 
A 1 811 PRO 811 786 ?   ?   ?   A . n 
A 1 812 GLY 812 787 ?   ?   ?   A . n 
A 1 813 ALA 813 788 ?   ?   ?   A . n 
A 1 814 LEU 814 789 ?   ?   ?   A . n 
A 1 815 THR 815 790 ?   ?   ?   A . n 
A 1 816 LEU 816 791 ?   ?   ?   A . n 
A 1 817 LEU 817 792 ?   ?   ?   A . n 
A 1 818 PRO 818 793 ?   ?   ?   A . n 
A 1 819 SER 819 794 ?   ?   ?   A . n 
A 1 820 GLY 820 795 ?   ?   ?   A . n 
A 1 821 LEU 821 796 ?   ?   ?   A . n 
A 1 822 GLY 822 797 ?   ?   ?   A . n 
A 1 823 PRO 823 798 ?   ?   ?   A . n 
A 1 824 PRO 824 799 ?   ?   ?   A . n 
A 1 825 PRO 825 800 ?   ?   ?   A . n 
A 1 826 PRO 826 801 ?   ?   ?   A . n 
A 1 827 PRO 827 802 ?   ?   ?   A . n 
A 1 828 PRO 828 803 ?   ?   ?   A . n 
A 1 829 PRO 829 804 ?   ?   ?   A . n 
A 1 830 PRO 830 805 ?   ?   ?   A . n 
A 1 831 SER 831 806 ?   ?   ?   A . n 
A 1 832 LEU 832 807 ?   ?   ?   A . n 
A 1 833 HIS 833 808 ?   ?   ?   A . n 
A 1 834 PRO 834 809 ?   ?   ?   A . n 
A 1 835 PHE 835 810 ?   ?   ?   A . n 
A 1 836 GLY 836 811 ?   ?   ?   A . n 
A 1 837 PRO 837 812 ?   ?   ?   A . n 
A 1 838 PHE 838 813 ?   ?   ?   A . n 
A 1 839 PRO 839 814 ?   ?   ?   A . n 
A 1 840 PRO 840 815 ?   ?   ?   A . n 
A 1 841 PRO 841 816 ?   ?   ?   A . n 
A 1 842 PRO 842 817 ?   ?   ?   A . n 
A 1 843 PRO 843 818 ?   ?   ?   A . n 
A 1 844 THR 844 819 ?   ?   ?   A . n 
A 1 845 ALA 845 820 ?   ?   ?   A . n 
A 1 846 THR 846 821 ?   ?   ?   A . n 
A 1 847 SER 847 822 ?   ?   ?   A . n 
A 1 848 HIS 848 823 ?   ?   ?   A . n 
A 1 849 ASN 849 824 ?   ?   ?   A . n 
A 1 850 ASN 850 825 ?   ?   ?   A . n 
A 1 851 THR 851 826 ?   ?   ?   A . n 
A 1 852 LEU 852 827 ?   ?   ?   A . n 
A 1 853 PRO 853 828 ?   ?   ?   A . n 
A 1 854 HIS 854 829 ?   ?   ?   A . n 
A 1 855 PRO 855 830 ?   ?   ?   A . n 
A 1 856 HIS 856 831 ?   ?   ?   A . n 
A 1 857 SER 857 832 ?   ?   ?   A . n 
A 1 858 THR 858 833 ?   ?   ?   A . n 
A 1 859 THR 859 834 ?   ?   ?   A . n 
A 1 860 ARG 860 835 ?   ?   ?   A . n 
A 1 861 VAL 861 836 ?   ?   ?   A . n 
A 1 862 SER 862 837 ?   ?   ?   A . n 
A 1 863 ASN 863 838 ?   ?   ?   A . n 
A 1 864 SER 864 839 ?   ?   ?   A . n 
A 1 865 LEU 865 840 ?   ?   ?   A . n 
A 1 866 GLU 866 841 ?   ?   ?   A . n 
A 1 867 VAL 867 842 ?   ?   ?   A . n 
A 1 868 LEU 868 843 ?   ?   ?   A . n 
A 1 869 PHE 869 844 ?   ?   ?   A . n 
A 1 870 GLN 870 845 ?   ?   ?   A . n 
B 1 1   MET 1   -41 ?   ?   ?   B . n 
B 1 2   ALA 2   -40 ?   ?   ?   B . n 
B 1 3   LEU 3   -39 ?   ?   ?   B . n 
B 1 4   PRO 4   -38 ?   ?   ?   B . n 
B 1 5   ARG 5   -37 ?   ?   ?   B . n 
B 1 6   CYS 6   -36 ?   ?   ?   B . n 
B 1 7   MET 7   -35 ?   ?   ?   B . n 
B 1 8   TRP 8   -34 ?   ?   ?   B . n 
B 1 9   PRO 9   -33 ?   ?   ?   B . n 
B 1 10  ASN 10  -32 ?   ?   ?   B . n 
B 1 11  TYR 11  -31 ?   ?   ?   B . n 
B 1 12  VAL 12  -30 ?   ?   ?   B . n 
B 1 13  TRP 13  -29 ?   ?   ?   B . n 
B 1 14  ARG 14  -28 ?   ?   ?   B . n 
B 1 15  ALA 15  -27 ?   ?   ?   B . n 
B 1 16  MET 16  -26 ?   ?   ?   B . n 
B 1 17  MET 17  -25 ?   ?   ?   B . n 
B 1 18  ALA 18  -24 ?   ?   ?   B . n 
B 1 19  CYS 19  -23 ?   ?   ?   B . n 
B 1 20  VAL 20  -22 ?   ?   ?   B . n 
B 1 21  VAL 21  -21 ?   ?   ?   B . n 
B 1 22  HIS 22  -20 ?   ?   ?   B . n 
B 1 23  ARG 23  -19 ?   ?   ?   B . n 
B 1 24  GLY 24  -18 ?   ?   ?   B . n 
B 1 25  SER 25  -17 ?   ?   ?   B . n 
B 1 26  GLY 26  -16 ?   ?   ?   B . n 
B 1 27  ALA 27  -15 ?   ?   ?   B . n 
B 1 28  PRO 28  -14 ?   ?   ?   B . n 
B 1 29  LEU 29  -13 ?   ?   ?   B . n 
B 1 30  THR 30  -12 ?   ?   ?   B . n 
B 1 31  LEU 31  -11 ?   ?   ?   B . n 
B 1 32  CYS 32  -10 ?   ?   ?   B . n 
B 1 33  LEU 33  -9  ?   ?   ?   B . n 
B 1 34  LEU 34  -8  ?   ?   ?   B . n 
B 1 35  GLY 35  -7  ?   ?   ?   B . n 
B 1 36  CYS 36  -6  ?   ?   ?   B . n 
B 1 37  LEU 37  -5  ?   ?   ?   B . n 
B 1 38  LEU 38  -4  ?   ?   ?   B . n 
B 1 39  GLN 39  -3  ?   ?   ?   B . n 
B 1 40  THR 40  -2  ?   ?   ?   B . n 
B 1 41  PHE 41  -1  ?   ?   ?   B . n 
B 1 42  HIS 42  0   ?   ?   ?   B . n 
B 1 43  VAL 43  1   ?   ?   ?   B . n 
B 1 44  LEU 44  2   ?   ?   ?   B . n 
B 1 45  SER 45  3   ?   ?   ?   B . n 
B 1 46  GLN 46  4   ?   ?   ?   B . n 
B 1 47  LYS 47  5   ?   ?   ?   B . n 
B 1 48  TYR 48  6   ?   ?   ?   B . n 
B 1 49  PRO 49  7   ?   ?   ?   B . n 
B 1 50  TYR 50  8   ?   ?   ?   B . n 
B 1 51  ASP 51  9   ?   ?   ?   B . n 
B 1 52  VAL 52  10  ?   ?   ?   B . n 
B 1 53  PRO 53  11  ?   ?   ?   B . n 
B 1 54  ASP 54  12  ?   ?   ?   B . n 
B 1 55  TYR 55  13  ?   ?   ?   B . n 
B 1 56  ALA 56  14  ?   ?   ?   B . n 
B 1 57  GLN 57  15  ?   ?   ?   B . n 
B 1 58  ARG 58  16  ?   ?   ?   B . n 
B 1 59  GLY 59  17  ?   ?   ?   B . n 
B 1 60  GLY 60  18  ?   ?   ?   B . n 
B 1 61  GLY 61  19  ?   ?   ?   B . n 
B 1 62  GLY 62  20  ?   ?   ?   B . n 
B 1 63  PRO 63  21  ?   ?   ?   B . n 
B 1 64  GLY 64  22  ?   ?   ?   B . n 
B 1 65  GLY 65  23  ?   ?   ?   B . n 
B 1 66  GLY 66  24  ?   ?   ?   B . n 
B 1 67  ALA 67  25  ?   ?   ?   B . n 
B 1 68  PRO 68  26  ?   ?   ?   B . n 
B 1 69  GLY 69  27  ?   ?   ?   B . n 
B 1 70  GLY 70  28  ?   ?   ?   B . n 
B 1 71  PRO 71  29  ?   ?   ?   B . n 
B 1 72  GLY 72  30  ?   ?   ?   B . n 
B 1 73  LEU 73  31  ?   ?   ?   B . n 
B 1 74  GLY 74  32  ?   ?   ?   B . n 
B 1 75  LEU 75  33  ?   ?   ?   B . n 
B 1 76  GLY 76  34  ?   ?   ?   B . n 
B 1 77  SER 77  35  ?   ?   ?   B . n 
B 1 78  LEU 78  36  ?   ?   ?   B . n 
B 1 79  GLY 79  37  ?   ?   ?   B . n 
B 1 80  GLU 80  38  ?   ?   ?   B . n 
B 1 81  GLU 81  39  ?   ?   ?   B . n 
B 1 82  ARG 82  40  40  ARG ARG B . n 
B 1 83  PHE 83  41  41  PHE PHE B . n 
B 1 84  PRO 84  42  42  PRO PRO B . n 
B 1 85  VAL 85  43  43  VAL VAL B . n 
B 1 86  VAL 86  44  44  VAL VAL B . n 
B 1 87  ASN 87  45  45  ASN ASN B . n 
B 1 88  THR 88  46  46  THR THR B . n 
B 1 89  ALA 89  47  47  ALA ALA B . n 
B 1 90  TYR 90  48  48  TYR TYR B . n 
B 1 91  GLY 91  49  49  GLY GLY B . n 
B 1 92  ARG 92  50  50  ARG ARG B . n 
B 1 93  VAL 93  51  51  VAL VAL B . n 
B 1 94  ARG 94  52  52  ARG ARG B . n 
B 1 95  GLY 95  53  53  GLY GLY B . n 
B 1 96  VAL 96  54  54  VAL VAL B . n 
B 1 97  ARG 97  55  55  ARG ARG B . n 
B 1 98  ARG 98  56  56  ARG ARG B . n 
B 1 99  GLU 99  57  57  GLU GLU B . n 
B 1 100 LEU 100 58  58  LEU LEU B . n 
B 1 101 ASN 101 59  59  ASN ASN B . n 
B 1 102 ASN 102 60  60  ASN ASN B . n 
B 1 103 GLU 103 61  61  GLU GLU B . n 
B 1 104 ILE 104 62  62  ILE ILE B . n 
B 1 105 LEU 105 63  63  LEU LEU B . n 
B 1 106 GLY 106 64  64  GLY GLY B . n 
B 1 107 PRO 107 65  65  PRO PRO B . n 
B 1 108 VAL 108 66  66  VAL VAL B . n 
B 1 109 VAL 109 67  67  VAL VAL B . n 
B 1 110 GLN 110 68  68  GLN GLN B . n 
B 1 111 PHE 111 69  69  PHE PHE B . n 
B 1 112 LEU 112 70  70  LEU LEU B . n 
B 1 113 GLY 113 71  71  GLY GLY B . n 
B 1 114 VAL 114 72  72  VAL VAL B . n 
B 1 115 PRO 115 73  73  PRO PRO B . n 
B 1 116 TYR 116 74  74  TYR TYR B . n 
B 1 117 ALA 117 75  75  ALA ALA B . n 
B 1 118 THR 118 76  76  THR THR B . n 
B 1 119 PRO 119 77  77  PRO PRO B . n 
B 1 120 PRO 120 78  78  PRO PRO B . n 
B 1 121 LEU 121 79  79  LEU LEU B . n 
B 1 122 GLY 122 80  80  GLY GLY B . n 
B 1 123 ALA 123 81  81  ALA ALA B . n 
B 1 124 ARG 124 82  82  ARG ARG B . n 
B 1 125 ARG 125 83  83  ARG ARG B . n 
B 1 126 PHE 126 84  84  PHE PHE B . n 
B 1 127 GLN 127 85  85  GLN GLN B . n 
B 1 128 PRO 128 86  86  PRO PRO B . n 
B 1 129 PRO 129 87  87  PRO PRO B . n 
B 1 130 GLU 130 88  88  GLU GLU B . n 
B 1 131 ALA 131 89  89  ALA ALA B . n 
B 1 132 PRO 132 90  90  PRO PRO B . n 
B 1 133 ALA 133 91  91  ALA ALA B . n 
B 1 134 SER 134 92  92  SER SER B . n 
B 1 135 TRP 135 93  93  TRP TRP B . n 
B 1 136 PRO 136 94  94  PRO PRO B . n 
B 1 137 GLY 137 95  95  GLY GLY B . n 
B 1 138 VAL 138 96  96  VAL VAL B . n 
B 1 139 ARG 139 97  97  ARG ARG B . n 
B 1 140 ASN 140 98  98  ASN ASN B . n 
B 1 141 ALA 141 99  99  ALA ALA B . n 
B 1 142 THR 142 100 100 THR THR B . n 
B 1 143 THR 143 101 101 THR THR B . n 
B 1 144 LEU 144 102 102 LEU LEU B . n 
B 1 145 PRO 145 103 103 PRO PRO B . n 
B 1 146 PRO 146 104 104 PRO PRO B . n 
B 1 147 ALA 147 105 105 ALA ALA B . n 
B 1 148 CYS 148 106 106 CYS CYS B . n 
B 1 149 PRO 149 107 107 PRO PRO B . n 
B 1 150 GLN 150 108 108 GLN GLN B . n 
B 1 151 ASN 151 109 109 ASN ASN B . n 
B 1 152 LEU 152 110 110 LEU LEU B . n 
B 1 153 HIS 153 111 111 HIS HIS B . n 
B 1 154 GLY 154 112 112 GLY GLY B . n 
B 1 155 ALA 155 113 113 ALA ALA B . n 
B 1 156 LEU 156 114 114 LEU LEU B . n 
B 1 157 PRO 157 115 115 PRO PRO B . n 
B 1 158 ALA 158 116 116 ALA ALA B . n 
B 1 159 ILE 159 117 117 ILE ILE B . n 
B 1 160 MET 160 118 118 MET MET B . n 
B 1 161 LEU 161 119 119 LEU LEU B . n 
B 1 162 PRO 162 120 120 PRO PRO B . n 
B 1 163 VAL 163 121 121 VAL VAL B . n 
B 1 164 TRP 164 122 122 TRP TRP B . n 
B 1 165 PHE 165 123 123 PHE PHE B . n 
B 1 166 THR 166 124 124 THR THR B . n 
B 1 167 ASP 167 125 125 ASP ASP B . n 
B 1 168 ASN 168 126 126 ASN ASN B . n 
B 1 169 LEU 169 127 127 LEU LEU B . n 
B 1 170 GLU 170 128 128 GLU GLU B . n 
B 1 171 ALA 171 129 129 ALA ALA B . n 
B 1 172 ALA 172 130 130 ALA ALA B . n 
B 1 173 ALA 173 131 131 ALA ALA B . n 
B 1 174 THR 174 132 132 THR THR B . n 
B 1 175 TYR 175 133 133 TYR TYR B . n 
B 1 176 VAL 176 134 134 VAL VAL B . n 
B 1 177 GLN 177 135 135 GLN GLN B . n 
B 1 178 ASN 178 136 136 ASN ASN B . n 
B 1 179 GLN 179 137 137 GLN GLN B . n 
B 1 180 SER 180 138 138 SER SER B . n 
B 1 181 GLU 181 139 139 GLU GLU B . n 
B 1 182 ASP 182 140 140 ASP ASP B . n 
B 1 183 CYS 183 141 141 CYS CYS B . n 
B 1 184 LEU 184 142 142 LEU LEU B . n 
B 1 185 TYR 185 143 143 TYR TYR B . n 
B 1 186 LEU 186 144 144 LEU LEU B . n 
B 1 187 ASN 187 145 145 ASN ASN B . n 
B 1 188 LEU 188 146 146 LEU LEU B . n 
B 1 189 TYR 189 147 147 TYR TYR B . n 
B 1 190 VAL 190 148 148 VAL VAL B . n 
B 1 191 PRO 191 149 149 PRO PRO B . n 
B 1 192 THR 192 150 150 THR THR B . n 
B 1 193 GLU 193 168 ?   ?   ?   B . n 
B 1 194 ASP 194 169 ?   ?   ?   B . n 
B 1 195 ASP 195 170 ?   ?   ?   B . n 
B 1 196 ILE 196 171 ?   ?   ?   B . n 
B 1 197 ARG 197 172 ?   ?   ?   B . n 
B 1 198 ASP 198 173 ?   ?   ?   B . n 
B 1 199 SER 199 174 174 SER SER B . n 
B 1 200 GLY 200 175 175 GLY GLY B . n 
B 1 201 LYS 201 176 176 LYS LYS B . n 
B 1 202 LYS 202 177 177 LYS LYS B . n 
B 1 203 PRO 203 178 178 PRO PRO B . n 
B 1 204 VAL 204 179 179 VAL VAL B . n 
B 1 205 MET 205 180 180 MET MET B . n 
B 1 206 LEU 206 181 181 LEU LEU B . n 
B 1 207 PHE 207 182 182 PHE PHE B . n 
B 1 208 LEU 208 183 183 LEU LEU B . n 
B 1 209 HIS 209 184 184 HIS HIS B . n 
B 1 210 GLY 210 185 185 GLY GLY B . n 
B 1 211 GLY 211 186 186 GLY GLY B . n 
B 1 212 SER 212 187 187 SER SER B . n 
B 1 213 TYR 213 188 188 TYR TYR B . n 
B 1 214 MET 214 189 189 MET MET B . n 
B 1 215 GLU 215 190 190 GLU GLU B . n 
B 1 216 GLY 216 191 191 GLY GLY B . n 
B 1 217 THR 217 192 192 THR THR B . n 
B 1 218 GLY 218 193 193 GLY GLY B . n 
B 1 219 ASN 219 194 194 ASN ASN B . n 
B 1 220 MET 220 195 195 MET MET B . n 
B 1 221 PHE 221 196 196 PHE PHE B . n 
B 1 222 ASP 222 197 197 ASP ASP B . n 
B 1 223 GLY 223 198 198 GLY GLY B . n 
B 1 224 SER 224 199 199 SER SER B . n 
B 1 225 VAL 225 200 200 VAL VAL B . n 
B 1 226 LEU 226 201 201 LEU LEU B . n 
B 1 227 ALA 227 202 202 ALA ALA B . n 
B 1 228 ALA 228 203 203 ALA ALA B . n 
B 1 229 TYR 229 204 204 TYR TYR B . n 
B 1 230 GLY 230 205 205 GLY GLY B . n 
B 1 231 ASN 231 206 206 ASN ASN B . n 
B 1 232 VAL 232 207 207 VAL VAL B . n 
B 1 233 ILE 233 208 208 ILE ILE B . n 
B 1 234 VAL 234 209 209 VAL VAL B . n 
B 1 235 VAL 235 210 210 VAL VAL B . n 
B 1 236 THR 236 211 211 THR THR B . n 
B 1 237 LEU 237 212 212 LEU LEU B . n 
B 1 238 ASN 238 213 213 ASN ASN B . n 
B 1 239 TYR 239 214 214 TYR TYR B . n 
B 1 240 ARG 240 215 215 ARG ARG B . n 
B 1 241 LEU 241 216 216 LEU LEU B . n 
B 1 242 GLY 242 217 217 GLY GLY B . n 
B 1 243 VAL 243 218 218 VAL VAL B . n 
B 1 244 LEU 244 219 219 LEU LEU B . n 
B 1 245 GLY 245 220 220 GLY GLY B . n 
B 1 246 PHE 246 221 221 PHE PHE B . n 
B 1 247 LEU 247 222 222 LEU LEU B . n 
B 1 248 SER 248 223 223 SER SER B . n 
B 1 249 THR 249 224 224 THR THR B . n 
B 1 250 GLY 250 225 225 GLY GLY B . n 
B 1 251 ASP 251 226 226 ASP ASP B . n 
B 1 252 GLN 252 227 227 GLN GLN B . n 
B 1 253 ALA 253 228 228 ALA ALA B . n 
B 1 254 ALA 254 229 229 ALA ALA B . n 
B 1 255 LYS 255 230 230 LYS LYS B . n 
B 1 256 GLY 256 231 231 GLY GLY B . n 
B 1 257 ASN 257 232 232 ASN ASN B . n 
B 1 258 TYR 258 233 233 TYR TYR B . n 
B 1 259 GLY 259 234 234 GLY GLY B . n 
B 1 260 LEU 260 235 235 LEU LEU B . n 
B 1 261 LEU 261 236 236 LEU LEU B . n 
B 1 262 ASP 262 237 237 ASP ASP B . n 
B 1 263 GLN 263 238 238 GLN GLN B . n 
B 1 264 ILE 264 239 239 ILE ILE B . n 
B 1 265 GLN 265 240 240 GLN GLN B . n 
B 1 266 ALA 266 241 241 ALA ALA B . n 
B 1 267 LEU 267 242 242 LEU LEU B . n 
B 1 268 ARG 268 243 243 ARG ARG B . n 
B 1 269 TRP 269 244 244 TRP TRP B . n 
B 1 270 LEU 270 245 245 LEU LEU B . n 
B 1 271 SER 271 246 246 SER SER B . n 
B 1 272 GLU 272 247 247 GLU GLU B . n 
B 1 273 ASN 273 248 248 ASN ASN B . n 
B 1 274 ILE 274 249 249 ILE ILE B . n 
B 1 275 ALA 275 250 250 ALA ALA B . n 
B 1 276 HIS 276 251 251 HIS HIS B . n 
B 1 277 PHE 277 252 252 PHE PHE B . n 
B 1 278 GLY 278 253 253 GLY GLY B . n 
B 1 279 GLY 279 254 254 GLY GLY B . n 
B 1 280 ASP 280 255 255 ASP ASP B . n 
B 1 281 PRO 281 256 256 PRO PRO B . n 
B 1 282 GLU 282 257 257 GLU GLU B . n 
B 1 283 ARG 283 258 258 ARG ARG B . n 
B 1 284 ILE 284 259 259 ILE ILE B . n 
B 1 285 THR 285 260 260 THR THR B . n 
B 1 286 ILE 286 261 261 ILE ILE B . n 
B 1 287 PHE 287 262 262 PHE PHE B . n 
B 1 288 GLY 288 263 263 GLY GLY B . n 
B 1 289 SER 289 264 264 SER SER B . n 
B 1 290 GLY 290 265 265 GLY GLY B . n 
B 1 291 ALA 291 266 266 ALA ALA B . n 
B 1 292 GLY 292 267 267 GLY GLY B . n 
B 1 293 ALA 293 268 268 ALA ALA B . n 
B 1 294 SER 294 269 269 SER SER B . n 
B 1 295 CYS 295 270 270 CYS CYS B . n 
B 1 296 VAL 296 271 271 VAL VAL B . n 
B 1 297 ASN 297 272 272 ASN ASN B . n 
B 1 298 LEU 298 273 273 LEU LEU B . n 
B 1 299 LEU 299 274 274 LEU LEU B . n 
B 1 300 ILE 300 275 275 ILE ILE B . n 
B 1 301 LEU 301 276 276 LEU LEU B . n 
B 1 302 SER 302 277 277 SER SER B . n 
B 1 303 HIS 303 278 278 HIS HIS B . n 
B 1 304 HIS 304 279 279 HIS HIS B . n 
B 1 305 SER 305 280 280 SER SER B . n 
B 1 306 GLU 306 281 281 GLU GLU B . n 
B 1 307 GLY 307 282 282 GLY GLY B . n 
B 1 308 LEU 308 283 283 LEU LEU B . n 
B 1 309 PHE 309 284 284 PHE PHE B . n 
B 1 310 GLN 310 285 285 GLN GLN B . n 
B 1 311 LYS 311 286 286 LYS LYS B . n 
B 1 312 ALA 312 287 287 ALA ALA B . n 
B 1 313 ILE 313 288 288 ILE ILE B . n 
B 1 314 ALA 314 289 289 ALA ALA B . n 
B 1 315 GLN 315 290 290 GLN GLN B . n 
B 1 316 SER 316 291 291 SER SER B . n 
B 1 317 GLY 317 292 292 GLY GLY B . n 
B 1 318 THR 318 293 293 THR THR B . n 
B 1 319 ALA 319 294 294 ALA ALA B . n 
B 1 320 ILE 320 295 295 ILE ILE B . n 
B 1 321 SER 321 296 296 SER SER B . n 
B 1 322 SER 322 297 297 SER SER B . n 
B 1 323 TRP 323 298 298 TRP TRP B . n 
B 1 324 SER 324 299 299 SER SER B . n 
B 1 325 VAL 325 300 300 VAL VAL B . n 
B 1 326 ASN 326 301 301 ASN ASN B . n 
B 1 327 TYR 327 302 302 TYR TYR B . n 
B 1 328 GLN 328 303 303 GLN GLN B . n 
B 1 329 PRO 329 304 304 PRO PRO B . n 
B 1 330 LEU 330 305 305 LEU LEU B . n 
B 1 331 LYS 331 306 306 LYS LYS B . n 
B 1 332 TYR 332 307 307 TYR TYR B . n 
B 1 333 THR 333 308 308 THR THR B . n 
B 1 334 ARG 334 309 309 ARG ARG B . n 
B 1 335 LEU 335 310 310 LEU LEU B . n 
B 1 336 LEU 336 311 311 LEU LEU B . n 
B 1 337 ALA 337 312 312 ALA ALA B . n 
B 1 338 ALA 338 313 313 ALA ALA B . n 
B 1 339 LYS 339 314 314 LYS LYS B . n 
B 1 340 VAL 340 315 315 VAL VAL B . n 
B 1 341 GLY 341 316 316 GLY GLY B . n 
B 1 342 CYS 342 317 317 CYS CYS B . n 
B 1 343 ASP 343 318 318 ASP ASP B . n 
B 1 344 ARG 344 319 319 ARG ARG B . n 
B 1 345 GLU 345 320 320 GLU GLU B . n 
B 1 346 ASP 346 321 321 ASP ASP B . n 
B 1 347 SER 347 322 322 SER SER B . n 
B 1 348 THR 348 323 323 THR THR B . n 
B 1 349 GLU 349 324 324 GLU GLU B . n 
B 1 350 ALA 350 325 325 ALA ALA B . n 
B 1 351 VAL 351 326 326 VAL VAL B . n 
B 1 352 GLU 352 327 327 GLU GLU B . n 
B 1 353 CYS 353 328 328 CYS CYS B . n 
B 1 354 LEU 354 329 329 LEU LEU B . n 
B 1 355 ARG 355 330 330 ARG ARG B . n 
B 1 356 ARG 356 331 331 ARG ARG B . n 
B 1 357 LYS 357 332 332 LYS LYS B . n 
B 1 358 SER 358 333 333 SER SER B . n 
B 1 359 SER 359 334 334 SER SER B . n 
B 1 360 ARG 360 335 335 ARG ARG B . n 
B 1 361 GLU 361 336 336 GLU GLU B . n 
B 1 362 LEU 362 337 337 LEU LEU B . n 
B 1 363 VAL 363 338 338 VAL VAL B . n 
B 1 364 ASP 364 339 339 ASP ASP B . n 
B 1 365 GLN 365 340 340 GLN GLN B . n 
B 1 366 ASP 366 341 341 ASP ASP B . n 
B 1 367 VAL 367 342 342 VAL VAL B . n 
B 1 368 GLN 368 343 343 GLN GLN B . n 
B 1 369 PRO 369 344 344 PRO PRO B . n 
B 1 370 ALA 370 345 345 ALA ALA B . n 
B 1 371 ARG 371 346 346 ARG ARG B . n 
B 1 372 TYR 372 347 347 TYR TYR B . n 
B 1 373 HIS 373 348 348 HIS HIS B . n 
B 1 374 ILE 374 349 349 ILE ILE B . n 
B 1 375 ALA 375 350 350 ALA ALA B . n 
B 1 376 PHE 376 351 351 PHE PHE B . n 
B 1 377 GLY 377 352 352 GLY GLY B . n 
B 1 378 PRO 378 353 353 PRO PRO B . n 
B 1 379 VAL 379 354 354 VAL VAL B . n 
B 1 380 VAL 380 355 355 VAL VAL B . n 
B 1 381 ASP 381 356 356 ASP ASP B . n 
B 1 382 GLY 382 357 357 GLY GLY B . n 
B 1 383 ASP 383 358 358 ASP ASP B . n 
B 1 384 VAL 384 359 359 VAL VAL B . n 
B 1 385 VAL 385 360 360 VAL VAL B . n 
B 1 386 PRO 386 361 361 PRO PRO B . n 
B 1 387 ASP 387 362 362 ASP ASP B . n 
B 1 388 ASP 388 363 363 ASP ASP B . n 
B 1 389 PRO 389 364 364 PRO PRO B . n 
B 1 390 GLU 390 365 365 GLU GLU B . n 
B 1 391 ILE 391 366 366 ILE ILE B . n 
B 1 392 LEU 392 367 367 LEU LEU B . n 
B 1 393 MET 393 368 368 MET MET B . n 
B 1 394 GLN 394 369 369 GLN GLN B . n 
B 1 395 GLN 395 370 370 GLN GLN B . n 
B 1 396 GLY 396 371 371 GLY GLY B . n 
B 1 397 GLU 397 372 372 GLU GLU B . n 
B 1 398 PHE 398 373 373 PHE PHE B . n 
B 1 399 LEU 399 374 374 LEU LEU B . n 
B 1 400 ASN 400 375 375 ASN ASN B . n 
B 1 401 TYR 401 376 376 TYR TYR B . n 
B 1 402 ASP 402 377 377 ASP ASP B . n 
B 1 403 MET 403 378 378 MET MET B . n 
B 1 404 LEU 404 379 379 LEU LEU B . n 
B 1 405 ILE 405 380 380 ILE ILE B . n 
B 1 406 GLY 406 381 381 GLY GLY B . n 
B 1 407 VAL 407 382 382 VAL VAL B . n 
B 1 408 ASN 408 383 383 ASN ASN B . n 
B 1 409 GLN 409 384 384 GLN GLN B . n 
B 1 410 GLY 410 385 385 GLY GLY B . n 
B 1 411 GLU 411 386 386 GLU GLU B . n 
B 1 412 GLY 412 387 387 GLY GLY B . n 
B 1 413 LEU 413 388 388 LEU LEU B . n 
B 1 414 LYS 414 389 389 LYS LYS B . n 
B 1 415 PHE 415 390 390 PHE PHE B . n 
B 1 416 VAL 416 391 391 VAL VAL B . n 
B 1 417 GLU 417 392 392 GLU GLU B . n 
B 1 418 ASP 418 393 393 ASP ASP B . n 
B 1 419 SER 419 394 394 SER SER B . n 
B 1 420 ALA 420 395 395 ALA ALA B . n 
B 1 421 GLU 421 396 396 GLU GLU B . n 
B 1 422 SER 422 397 397 SER SER B . n 
B 1 423 GLU 423 398 398 GLU GLU B . n 
B 1 424 ASP 424 399 399 ASP ASP B . n 
B 1 425 GLY 425 400 400 GLY GLY B . n 
B 1 426 VAL 426 401 401 VAL VAL B . n 
B 1 427 SER 427 402 402 SER SER B . n 
B 1 428 ALA 428 403 403 ALA ALA B . n 
B 1 429 SER 429 404 404 SER SER B . n 
B 1 430 ALA 430 405 405 ALA ALA B . n 
B 1 431 PHE 431 406 406 PHE PHE B . n 
B 1 432 ASP 432 407 407 ASP ASP B . n 
B 1 433 PHE 433 408 408 PHE PHE B . n 
B 1 434 THR 434 409 409 THR THR B . n 
B 1 435 VAL 435 410 410 VAL VAL B . n 
B 1 436 SER 436 411 411 SER SER B . n 
B 1 437 ASN 437 412 412 ASN ASN B . n 
B 1 438 PHE 438 413 413 PHE PHE B . n 
B 1 439 VAL 439 414 414 VAL VAL B . n 
B 1 440 ASP 440 415 415 ASP ASP B . n 
B 1 441 ASN 441 416 416 ASN ASN B . n 
B 1 442 LEU 442 417 417 LEU LEU B . n 
B 1 443 TYR 443 418 418 TYR TYR B . n 
B 1 444 GLY 444 419 419 GLY GLY B . n 
B 1 445 TYR 445 420 420 TYR TYR B . n 
B 1 446 PRO 446 421 421 PRO PRO B . n 
B 1 447 GLU 447 422 422 GLU GLU B . n 
B 1 448 GLY 448 423 423 GLY GLY B . n 
B 1 449 LYS 449 424 424 LYS LYS B . n 
B 1 450 ASP 450 425 425 ASP ASP B . n 
B 1 451 VAL 451 426 426 VAL VAL B . n 
B 1 452 LEU 452 427 427 LEU LEU B . n 
B 1 453 ARG 453 428 428 ARG ARG B . n 
B 1 454 GLU 454 429 429 GLU GLU B . n 
B 1 455 THR 455 430 430 THR THR B . n 
B 1 456 ILE 456 431 431 ILE ILE B . n 
B 1 457 LYS 457 432 432 LYS LYS B . n 
B 1 458 PHE 458 433 433 PHE PHE B . n 
B 1 459 MET 459 434 434 MET MET B . n 
B 1 460 TYR 460 435 435 TYR TYR B . n 
B 1 461 THR 461 436 436 THR THR B . n 
B 1 462 ASP 462 437 437 ASP ASP B . n 
B 1 463 TRP 463 438 438 TRP TRP B . n 
B 1 464 ALA 464 439 439 ALA ALA B . n 
B 1 465 ASP 465 440 440 ASP ASP B . n 
B 1 466 ARG 466 441 441 ARG ARG B . n 
B 1 467 ASP 467 442 442 ASP ASP B . n 
B 1 468 ASN 468 443 443 ASN ASN B . n 
B 1 469 GLY 469 444 444 GLY GLY B . n 
B 1 470 GLU 470 445 445 GLU GLU B . n 
B 1 471 MET 471 446 446 MET MET B . n 
B 1 472 ARG 472 447 447 ARG ARG B . n 
B 1 473 ARG 473 448 448 ARG ARG B . n 
B 1 474 LYS 474 449 449 LYS LYS B . n 
B 1 475 THR 475 450 450 THR THR B . n 
B 1 476 LEU 476 451 451 LEU LEU B . n 
B 1 477 LEU 477 452 452 LEU LEU B . n 
B 1 478 ALA 478 453 453 ALA ALA B . n 
B 1 479 LEU 479 454 454 LEU LEU B . n 
B 1 480 PHE 480 455 455 PHE PHE B . n 
B 1 481 THR 481 456 456 THR THR B . n 
B 1 482 ASP 482 457 457 ASP ASP B . n 
B 1 483 HIS 483 458 458 HIS HIS B . n 
B 1 484 GLN 484 459 459 GLN GLN B . n 
B 1 485 TRP 485 460 460 TRP TRP B . n 
B 1 486 VAL 486 461 461 VAL VAL B . n 
B 1 487 ALA 487 462 462 ALA ALA B . n 
B 1 488 PRO 488 463 463 PRO PRO B . n 
B 1 489 ALA 489 464 464 ALA ALA B . n 
B 1 490 VAL 490 465 465 VAL VAL B . n 
B 1 491 ALA 491 466 466 ALA ALA B . n 
B 1 492 THR 492 467 467 THR THR B . n 
B 1 493 ALA 493 468 468 ALA ALA B . n 
B 1 494 LYS 494 469 469 LYS LYS B . n 
B 1 495 LEU 495 470 470 LEU LEU B . n 
B 1 496 HIS 496 471 471 HIS HIS B . n 
B 1 497 ALA 497 472 472 ALA ALA B . n 
B 1 498 ASP 498 473 473 ASP ASP B . n 
B 1 499 TYR 499 474 474 TYR TYR B . n 
B 1 500 GLN 500 475 475 GLN GLN B . n 
B 1 501 SER 501 476 476 SER SER B . n 
B 1 502 PRO 502 477 477 PRO PRO B . n 
B 1 503 VAL 503 478 478 VAL VAL B . n 
B 1 504 TYR 504 479 479 TYR TYR B . n 
B 1 505 PHE 505 480 480 PHE PHE B . n 
B 1 506 TYR 506 481 481 TYR TYR B . n 
B 1 507 THR 507 482 482 THR THR B . n 
B 1 508 PHE 508 483 483 PHE PHE B . n 
B 1 509 TYR 509 484 484 TYR TYR B . n 
B 1 510 HIS 510 485 485 HIS HIS B . n 
B 1 511 HIS 511 486 486 HIS HIS B . n 
B 1 512 CYS 512 487 487 CYS CYS B . n 
B 1 513 GLN 513 488 488 GLN GLN B . n 
B 1 514 ALA 514 489 489 ALA ALA B . n 
B 1 515 GLU 515 490 490 GLU GLU B . n 
B 1 516 GLY 516 491 491 GLY GLY B . n 
B 1 517 ARG 517 492 492 ARG ARG B . n 
B 1 518 PRO 518 493 493 PRO PRO B . n 
B 1 519 GLU 519 494 494 GLU GLU B . n 
B 1 520 TRP 520 495 495 TRP TRP B . n 
B 1 521 ALA 521 496 496 ALA ALA B . n 
B 1 522 ASP 522 497 497 ASP ASP B . n 
B 1 523 ALA 523 498 498 ALA ALA B . n 
B 1 524 ALA 524 499 499 ALA ALA B . n 
B 1 525 HIS 525 500 500 HIS HIS B . n 
B 1 526 GLY 526 501 501 GLY GLY B . n 
B 1 527 ASP 527 502 502 ASP ASP B . n 
B 1 528 GLU 528 503 503 GLU GLU B . n 
B 1 529 LEU 529 504 504 LEU LEU B . n 
B 1 530 PRO 530 505 505 PRO PRO B . n 
B 1 531 TYR 531 506 506 TYR TYR B . n 
B 1 532 VAL 532 507 507 VAL VAL B . n 
B 1 533 PHE 533 508 508 PHE PHE B . n 
B 1 534 GLY 534 509 509 GLY GLY B . n 
B 1 535 VAL 535 510 510 VAL VAL B . n 
B 1 536 PRO 536 511 511 PRO PRO B . n 
B 1 537 MET 537 512 512 MET MET B . n 
B 1 538 VAL 538 513 513 VAL VAL B . n 
B 1 539 GLY 539 514 514 GLY GLY B . n 
B 1 540 ALA 540 515 515 ALA ALA B . n 
B 1 541 THR 541 516 516 THR THR B . n 
B 1 542 ASP 542 517 517 ASP ASP B . n 
B 1 543 LEU 543 518 518 LEU LEU B . n 
B 1 544 PHE 544 519 519 PHE PHE B . n 
B 1 545 PRO 545 520 520 PRO PRO B . n 
B 1 546 CYS 546 521 521 CYS CYS B . n 
B 1 547 ASN 547 522 522 ASN ASN B . n 
B 1 548 PHE 548 523 523 PHE PHE B . n 
B 1 549 SER 549 524 524 SER SER B . n 
B 1 550 LYS 550 525 525 LYS LYS B . n 
B 1 551 ASN 551 526 526 ASN ASN B . n 
B 1 552 ASP 552 527 527 ASP ASP B . n 
B 1 553 VAL 553 528 528 VAL VAL B . n 
B 1 554 MET 554 529 529 MET MET B . n 
B 1 555 LEU 555 530 530 LEU LEU B . n 
B 1 556 SER 556 531 531 SER SER B . n 
B 1 557 ALA 557 532 532 ALA ALA B . n 
B 1 558 VAL 558 533 533 VAL VAL B . n 
B 1 559 VAL 559 534 534 VAL VAL B . n 
B 1 560 MET 560 535 535 MET MET B . n 
B 1 561 THR 561 536 536 THR THR B . n 
B 1 562 TYR 562 537 537 TYR TYR B . n 
B 1 563 TRP 563 538 538 TRP TRP B . n 
B 1 564 THR 564 539 539 THR THR B . n 
B 1 565 ASN 565 540 540 ASN ASN B . n 
B 1 566 PHE 566 541 541 PHE PHE B . n 
B 1 567 ALA 567 542 542 ALA ALA B . n 
B 1 568 LYS 568 543 543 LYS LYS B . n 
B 1 569 THR 569 544 544 THR THR B . n 
B 1 570 GLY 570 545 545 GLY GLY B . n 
B 1 571 ASP 571 546 546 ASP ASP B . n 
B 1 572 PRO 572 547 547 PRO PRO B . n 
B 1 573 ASN 573 548 548 ASN ASN B . n 
B 1 574 GLN 574 549 549 GLN GLN B . n 
B 1 575 PRO 575 550 550 PRO PRO B . n 
B 1 576 VAL 576 551 551 VAL VAL B . n 
B 1 577 PRO 577 552 552 PRO PRO B . n 
B 1 578 GLN 578 553 553 GLN GLN B . n 
B 1 579 ASP 579 554 ?   ?   ?   B . n 
B 1 580 THR 580 555 ?   ?   ?   B . n 
B 1 581 LYS 581 556 ?   ?   ?   B . n 
B 1 582 PHE 582 557 ?   ?   ?   B . n 
B 1 583 ILE 583 558 ?   ?   ?   B . n 
B 1 584 HIS 584 559 ?   ?   ?   B . n 
B 1 585 THR 585 560 ?   ?   ?   B . n 
B 1 586 LYS 586 561 ?   ?   ?   B . n 
B 1 587 PRO 587 562 ?   ?   ?   B . n 
B 1 588 ASN 588 563 ?   ?   ?   B . n 
B 1 589 ARG 589 564 564 ARG ARG B . n 
B 1 590 PHE 590 565 565 PHE PHE B . n 
B 1 591 GLU 591 566 566 GLU GLU B . n 
B 1 592 GLU 592 567 567 GLU GLU B . n 
B 1 593 VAL 593 568 568 VAL VAL B . n 
B 1 594 VAL 594 569 569 VAL VAL B . n 
B 1 595 TRP 595 570 570 TRP TRP B . n 
B 1 596 SER 596 571 571 SER SER B . n 
B 1 597 LYS 597 572 572 LYS LYS B . n 
B 1 598 PHE 598 573 573 PHE PHE B . n 
B 1 599 ASN 599 574 574 ASN ASN B . n 
B 1 600 SER 600 575 575 SER SER B . n 
B 1 601 LYS 601 576 576 LYS LYS B . n 
B 1 602 GLU 602 577 577 GLU GLU B . n 
B 1 603 LYS 603 578 578 LYS LYS B . n 
B 1 604 GLN 604 579 579 GLN GLN B . n 
B 1 605 TYR 605 580 580 TYR TYR B . n 
B 1 606 LEU 606 581 581 LEU LEU B . n 
B 1 607 HIS 607 582 582 HIS HIS B . n 
B 1 608 ILE 608 583 583 ILE ILE B . n 
B 1 609 GLY 609 584 584 GLY GLY B . n 
B 1 610 LEU 610 585 585 LEU LEU B . n 
B 1 611 LYS 611 586 586 LYS LYS B . n 
B 1 612 PRO 612 587 587 PRO PRO B . n 
B 1 613 ARG 613 588 588 ARG ARG B . n 
B 1 614 VAL 614 589 589 VAL VAL B . n 
B 1 615 ARG 615 590 590 ARG ARG B . n 
B 1 616 ASP 616 591 591 ASP ASP B . n 
B 1 617 ASN 617 592 592 ASN ASN B . n 
B 1 618 TYR 618 593 593 TYR TYR B . n 
B 1 619 ARG 619 594 594 ARG ARG B . n 
B 1 620 ALA 620 595 595 ALA ALA B . n 
B 1 621 ASN 621 596 596 ASN ASN B . n 
B 1 622 LYS 622 597 597 LYS LYS B . n 
B 1 623 VAL 623 598 598 VAL VAL B . n 
B 1 624 ALA 624 599 599 ALA ALA B . n 
B 1 625 PHE 625 600 600 PHE PHE B . n 
B 1 626 TRP 626 601 601 TRP TRP B . n 
B 1 627 LEU 627 602 602 LEU LEU B . n 
B 1 628 GLU 628 603 603 GLU GLU B . n 
B 1 629 LEU 629 604 604 LEU LEU B . n 
B 1 630 VAL 630 605 605 VAL VAL B . n 
B 1 631 PRO 631 606 606 PRO PRO B . n 
B 1 632 HIS 632 607 607 HIS HIS B . n 
B 1 633 LEU 633 608 608 LEU LEU B . n 
B 1 634 HIS 634 609 ?   ?   ?   B . n 
B 1 635 ASN 635 610 ?   ?   ?   B . n 
B 1 636 LEU 636 611 ?   ?   ?   B . n 
B 1 637 HIS 637 612 ?   ?   ?   B . n 
B 1 638 THR 638 613 ?   ?   ?   B . n 
B 1 639 GLU 639 614 ?   ?   ?   B . n 
B 1 640 LEU 640 615 ?   ?   ?   B . n 
B 1 641 PHE 641 616 ?   ?   ?   B . n 
B 1 642 THR 642 617 ?   ?   ?   B . n 
B 1 643 THR 643 618 ?   ?   ?   B . n 
B 1 644 THR 644 619 ?   ?   ?   B . n 
B 1 645 THR 645 620 ?   ?   ?   B . n 
B 1 646 ARG 646 621 ?   ?   ?   B . n 
B 1 647 LEU 647 622 ?   ?   ?   B . n 
B 1 648 PRO 648 623 ?   ?   ?   B . n 
B 1 649 PRO 649 624 ?   ?   ?   B . n 
B 1 650 TYR 650 625 ?   ?   ?   B . n 
B 1 651 ALA 651 626 ?   ?   ?   B . n 
B 1 652 THR 652 627 ?   ?   ?   B . n 
B 1 653 ARG 653 628 ?   ?   ?   B . n 
B 1 654 TRP 654 629 ?   ?   ?   B . n 
B 1 655 PRO 655 630 ?   ?   ?   B . n 
B 1 656 PRO 656 631 ?   ?   ?   B . n 
B 1 657 ARG 657 632 ?   ?   ?   B . n 
B 1 658 THR 658 633 ?   ?   ?   B . n 
B 1 659 PRO 659 634 ?   ?   ?   B . n 
B 1 660 GLY 660 635 ?   ?   ?   B . n 
B 1 661 PRO 661 636 ?   ?   ?   B . n 
B 1 662 GLY 662 637 ?   ?   ?   B . n 
B 1 663 THR 663 638 ?   ?   ?   B . n 
B 1 664 SER 664 639 ?   ?   ?   B . n 
B 1 665 GLY 665 640 ?   ?   ?   B . n 
B 1 666 THR 666 641 ?   ?   ?   B . n 
B 1 667 ARG 667 642 ?   ?   ?   B . n 
B 1 668 ARG 668 643 ?   ?   ?   B . n 
B 1 669 PRO 669 644 ?   ?   ?   B . n 
B 1 670 PRO 670 645 ?   ?   ?   B . n 
B 1 671 PRO 671 646 ?   ?   ?   B . n 
B 1 672 PRO 672 647 ?   ?   ?   B . n 
B 1 673 ALA 673 648 ?   ?   ?   B . n 
B 1 674 THR 674 649 ?   ?   ?   B . n 
B 1 675 LEU 675 650 ?   ?   ?   B . n 
B 1 676 PRO 676 651 ?   ?   ?   B . n 
B 1 677 PRO 677 652 ?   ?   ?   B . n 
B 1 678 GLU 678 653 ?   ?   ?   B . n 
B 1 679 SER 679 654 ?   ?   ?   B . n 
B 1 680 ASP 680 655 ?   ?   ?   B . n 
B 1 681 ILE 681 656 ?   ?   ?   B . n 
B 1 682 ASP 682 657 ?   ?   ?   B . n 
B 1 683 LEU 683 658 ?   ?   ?   B . n 
B 1 684 GLY 684 659 ?   ?   ?   B . n 
B 1 685 PRO 685 660 ?   ?   ?   B . n 
B 1 686 ARG 686 661 ?   ?   ?   B . n 
B 1 687 ALA 687 662 ?   ?   ?   B . n 
B 1 688 TYR 688 663 ?   ?   ?   B . n 
B 1 689 ASP 689 664 ?   ?   ?   B . n 
B 1 690 ARG 690 665 ?   ?   ?   B . n 
B 1 691 PHE 691 666 ?   ?   ?   B . n 
B 1 692 PRO 692 667 ?   ?   ?   B . n 
B 1 693 GLY 693 668 ?   ?   ?   B . n 
B 1 694 ASP 694 669 ?   ?   ?   B . n 
B 1 695 SER 695 670 ?   ?   ?   B . n 
B 1 696 ARG 696 671 ?   ?   ?   B . n 
B 1 697 ASP 697 672 ?   ?   ?   B . n 
B 1 698 TYR 698 673 ?   ?   ?   B . n 
B 1 699 SER 699 674 ?   ?   ?   B . n 
B 1 700 THR 700 675 ?   ?   ?   B . n 
B 1 701 GLU 701 676 ?   ?   ?   B . n 
B 1 702 LEU 702 677 ?   ?   ?   B . n 
B 1 703 SER 703 678 ?   ?   ?   B . n 
B 1 704 VAL 704 679 ?   ?   ?   B . n 
B 1 705 THR 705 680 ?   ?   ?   B . n 
B 1 706 VAL 706 681 ?   ?   ?   B . n 
B 1 707 ALA 707 682 ?   ?   ?   B . n 
B 1 708 VAL 708 683 ?   ?   ?   B . n 
B 1 709 GLY 709 684 ?   ?   ?   B . n 
B 1 710 ALA 710 685 ?   ?   ?   B . n 
B 1 711 SER 711 686 ?   ?   ?   B . n 
B 1 712 LEU 712 687 ?   ?   ?   B . n 
B 1 713 LEU 713 688 ?   ?   ?   B . n 
B 1 714 PHE 714 689 ?   ?   ?   B . n 
B 1 715 LEU 715 690 ?   ?   ?   B . n 
B 1 716 ASN 716 691 ?   ?   ?   B . n 
B 1 717 ILE 717 692 ?   ?   ?   B . n 
B 1 718 LEU 718 693 ?   ?   ?   B . n 
B 1 719 ALA 719 694 ?   ?   ?   B . n 
B 1 720 PHE 720 695 ?   ?   ?   B . n 
B 1 721 ALA 721 696 ?   ?   ?   B . n 
B 1 722 ALA 722 697 ?   ?   ?   B . n 
B 1 723 LEU 723 698 ?   ?   ?   B . n 
B 1 724 TYR 724 699 ?   ?   ?   B . n 
B 1 725 TYR 725 700 ?   ?   ?   B . n 
B 1 726 LYS 726 701 ?   ?   ?   B . n 
B 1 727 ARG 727 702 ?   ?   ?   B . n 
B 1 728 ASP 728 703 ?   ?   ?   B . n 
B 1 729 ARG 729 704 ?   ?   ?   B . n 
B 1 730 ARG 730 705 ?   ?   ?   B . n 
B 1 731 GLN 731 706 ?   ?   ?   B . n 
B 1 732 GLU 732 707 ?   ?   ?   B . n 
B 1 733 LEU 733 708 ?   ?   ?   B . n 
B 1 734 ARG 734 709 ?   ?   ?   B . n 
B 1 735 CYS 735 710 ?   ?   ?   B . n 
B 1 736 ARG 736 711 ?   ?   ?   B . n 
B 1 737 ARG 737 712 ?   ?   ?   B . n 
B 1 738 LEU 738 713 ?   ?   ?   B . n 
B 1 739 SER 739 714 ?   ?   ?   B . n 
B 1 740 PRO 740 715 ?   ?   ?   B . n 
B 1 741 PRO 741 716 ?   ?   ?   B . n 
B 1 742 GLY 742 717 ?   ?   ?   B . n 
B 1 743 GLY 743 718 ?   ?   ?   B . n 
B 1 744 SER 744 719 ?   ?   ?   B . n 
B 1 745 GLY 745 720 ?   ?   ?   B . n 
B 1 746 SER 746 721 ?   ?   ?   B . n 
B 1 747 GLY 747 722 ?   ?   ?   B . n 
B 1 748 VAL 748 723 ?   ?   ?   B . n 
B 1 749 PRO 749 724 ?   ?   ?   B . n 
B 1 750 GLY 750 725 ?   ?   ?   B . n 
B 1 751 GLY 751 726 ?   ?   ?   B . n 
B 1 752 GLY 752 727 ?   ?   ?   B . n 
B 1 753 PRO 753 728 ?   ?   ?   B . n 
B 1 754 LEU 754 729 ?   ?   ?   B . n 
B 1 755 LEU 755 730 ?   ?   ?   B . n 
B 1 756 PRO 756 731 ?   ?   ?   B . n 
B 1 757 THR 757 732 ?   ?   ?   B . n 
B 1 758 ALA 758 733 ?   ?   ?   B . n 
B 1 759 GLY 759 734 ?   ?   ?   B . n 
B 1 760 ARG 760 735 ?   ?   ?   B . n 
B 1 761 GLU 761 736 ?   ?   ?   B . n 
B 1 762 LEU 762 737 ?   ?   ?   B . n 
B 1 763 PRO 763 738 ?   ?   ?   B . n 
B 1 764 PRO 764 739 ?   ?   ?   B . n 
B 1 765 GLU 765 740 ?   ?   ?   B . n 
B 1 766 GLU 766 741 ?   ?   ?   B . n 
B 1 767 GLU 767 742 ?   ?   ?   B . n 
B 1 768 LEU 768 743 ?   ?   ?   B . n 
B 1 769 VAL 769 744 ?   ?   ?   B . n 
B 1 770 SER 770 745 ?   ?   ?   B . n 
B 1 771 LEU 771 746 ?   ?   ?   B . n 
B 1 772 GLN 772 747 ?   ?   ?   B . n 
B 1 773 LEU 773 748 ?   ?   ?   B . n 
B 1 774 LYS 774 749 ?   ?   ?   B . n 
B 1 775 ARG 775 750 ?   ?   ?   B . n 
B 1 776 GLY 776 751 ?   ?   ?   B . n 
B 1 777 GLY 777 752 ?   ?   ?   B . n 
B 1 778 GLY 778 753 ?   ?   ?   B . n 
B 1 779 VAL 779 754 ?   ?   ?   B . n 
B 1 780 GLY 780 755 ?   ?   ?   B . n 
B 1 781 ALA 781 756 ?   ?   ?   B . n 
B 1 782 ASP 782 757 ?   ?   ?   B . n 
B 1 783 PRO 783 758 ?   ?   ?   B . n 
B 1 784 ALA 784 759 ?   ?   ?   B . n 
B 1 785 GLU 785 760 ?   ?   ?   B . n 
B 1 786 ALA 786 761 ?   ?   ?   B . n 
B 1 787 LEU 787 762 ?   ?   ?   B . n 
B 1 788 ARG 788 763 ?   ?   ?   B . n 
B 1 789 PRO 789 764 ?   ?   ?   B . n 
B 1 790 ALA 790 765 ?   ?   ?   B . n 
B 1 791 CYS 791 766 ?   ?   ?   B . n 
B 1 792 PRO 792 767 ?   ?   ?   B . n 
B 1 793 PRO 793 768 ?   ?   ?   B . n 
B 1 794 ASP 794 769 ?   ?   ?   B . n 
B 1 795 TYR 795 770 ?   ?   ?   B . n 
B 1 796 THR 796 771 ?   ?   ?   B . n 
B 1 797 LEU 797 772 ?   ?   ?   B . n 
B 1 798 ALA 798 773 ?   ?   ?   B . n 
B 1 799 LEU 799 774 ?   ?   ?   B . n 
B 1 800 ARG 800 775 ?   ?   ?   B . n 
B 1 801 ARG 801 776 ?   ?   ?   B . n 
B 1 802 ALA 802 777 ?   ?   ?   B . n 
B 1 803 PRO 803 778 ?   ?   ?   B . n 
B 1 804 ASP 804 779 ?   ?   ?   B . n 
B 1 805 ASP 805 780 ?   ?   ?   B . n 
B 1 806 VAL 806 781 ?   ?   ?   B . n 
B 1 807 PRO 807 782 ?   ?   ?   B . n 
B 1 808 LEU 808 783 ?   ?   ?   B . n 
B 1 809 LEU 809 784 ?   ?   ?   B . n 
B 1 810 ALA 810 785 ?   ?   ?   B . n 
B 1 811 PRO 811 786 ?   ?   ?   B . n 
B 1 812 GLY 812 787 ?   ?   ?   B . n 
B 1 813 ALA 813 788 ?   ?   ?   B . n 
B 1 814 LEU 814 789 ?   ?   ?   B . n 
B 1 815 THR 815 790 ?   ?   ?   B . n 
B 1 816 LEU 816 791 ?   ?   ?   B . n 
B 1 817 LEU 817 792 ?   ?   ?   B . n 
B 1 818 PRO 818 793 ?   ?   ?   B . n 
B 1 819 SER 819 794 ?   ?   ?   B . n 
B 1 820 GLY 820 795 ?   ?   ?   B . n 
B 1 821 LEU 821 796 ?   ?   ?   B . n 
B 1 822 GLY 822 797 ?   ?   ?   B . n 
B 1 823 PRO 823 798 ?   ?   ?   B . n 
B 1 824 PRO 824 799 ?   ?   ?   B . n 
B 1 825 PRO 825 800 ?   ?   ?   B . n 
B 1 826 PRO 826 801 ?   ?   ?   B . n 
B 1 827 PRO 827 802 ?   ?   ?   B . n 
B 1 828 PRO 828 803 ?   ?   ?   B . n 
B 1 829 PRO 829 804 ?   ?   ?   B . n 
B 1 830 PRO 830 805 ?   ?   ?   B . n 
B 1 831 SER 831 806 ?   ?   ?   B . n 
B 1 832 LEU 832 807 ?   ?   ?   B . n 
B 1 833 HIS 833 808 ?   ?   ?   B . n 
B 1 834 PRO 834 809 ?   ?   ?   B . n 
B 1 835 PHE 835 810 ?   ?   ?   B . n 
B 1 836 GLY 836 811 ?   ?   ?   B . n 
B 1 837 PRO 837 812 ?   ?   ?   B . n 
B 1 838 PHE 838 813 ?   ?   ?   B . n 
B 1 839 PRO 839 814 ?   ?   ?   B . n 
B 1 840 PRO 840 815 ?   ?   ?   B . n 
B 1 841 PRO 841 816 ?   ?   ?   B . n 
B 1 842 PRO 842 817 ?   ?   ?   B . n 
B 1 843 PRO 843 818 ?   ?   ?   B . n 
B 1 844 THR 844 819 ?   ?   ?   B . n 
B 1 845 ALA 845 820 ?   ?   ?   B . n 
B 1 846 THR 846 821 ?   ?   ?   B . n 
B 1 847 SER 847 822 ?   ?   ?   B . n 
B 1 848 HIS 848 823 ?   ?   ?   B . n 
B 1 849 ASN 849 824 ?   ?   ?   B . n 
B 1 850 ASN 850 825 ?   ?   ?   B . n 
B 1 851 THR 851 826 ?   ?   ?   B . n 
B 1 852 LEU 852 827 ?   ?   ?   B . n 
B 1 853 PRO 853 828 ?   ?   ?   B . n 
B 1 854 HIS 854 829 ?   ?   ?   B . n 
B 1 855 PRO 855 830 ?   ?   ?   B . n 
B 1 856 HIS 856 831 ?   ?   ?   B . n 
B 1 857 SER 857 832 ?   ?   ?   B . n 
B 1 858 THR 858 833 ?   ?   ?   B . n 
B 1 859 THR 859 834 ?   ?   ?   B . n 
B 1 860 ARG 860 835 ?   ?   ?   B . n 
B 1 861 VAL 861 836 ?   ?   ?   B . n 
B 1 862 SER 862 837 ?   ?   ?   B . n 
B 1 863 ASN 863 838 ?   ?   ?   B . n 
B 1 864 SER 864 839 ?   ?   ?   B . n 
B 1 865 LEU 865 840 ?   ?   ?   B . n 
B 1 866 GLU 866 841 ?   ?   ?   B . n 
B 1 867 VAL 867 842 ?   ?   ?   B . n 
B 1 868 LEU 868 843 ?   ?   ?   B . n 
B 1 869 PHE 869 844 ?   ?   ?   B . n 
B 1 870 GLN 870 845 ?   ?   ?   B . n 
C 2 1   MET 1   -22 ?   ?   ?   C . n 
C 2 2   TYR 2   -21 ?   ?   ?   C . n 
C 2 3   GLN 3   -20 ?   ?   ?   C . n 
C 2 4   ARG 4   -19 ?   ?   ?   C . n 
C 2 5   MET 5   -18 ?   ?   ?   C . n 
C 2 6   LEU 6   -17 ?   ?   ?   C . n 
C 2 7   ARG 7   -16 ?   ?   ?   C . n 
C 2 8   CYS 8   -15 ?   ?   ?   C . n 
C 2 9   GLY 9   -14 ?   ?   ?   C . n 
C 2 10  ALA 10  -13 ?   ?   ?   C . n 
C 2 11  ASP 11  -12 ?   ?   ?   C . n 
C 2 12  LEU 12  -11 ?   ?   ?   C . n 
C 2 13  GLY 13  -10 ?   ?   ?   C . n 
C 2 14  SER 14  -9  ?   ?   ?   C . n 
C 2 15  PRO 15  -8  ?   ?   ?   C . n 
C 2 16  GLY 16  -7  ?   ?   ?   C . n 
C 2 17  GLY 17  -6  ?   ?   ?   C . n 
C 2 18  GLY 18  -5  ?   ?   ?   C . n 
C 2 19  SER 19  -4  ?   ?   ?   C . n 
C 2 20  GLY 20  -3  ?   ?   ?   C . n 
C 2 21  GLY 21  -2  ?   ?   ?   C . n 
C 2 22  GLY 22  -1  ?   ?   ?   C . n 
C 2 23  ALA 23  0   ?   ?   ?   C . n 
C 2 24  GLY 24  1   ?   ?   ?   C . n 
C 2 25  GLY 25  2   ?   ?   ?   C . n 
C 2 26  ARG 26  3   ?   ?   ?   C . n 
C 2 27  LEU 27  4   ?   ?   ?   C . n 
C 2 28  ALA 28  5   ?   ?   ?   C . n 
C 2 29  LEU 29  6   ?   ?   ?   C . n 
C 2 30  ILE 30  7   ?   ?   ?   C . n 
C 2 31  TRP 31  8   ?   ?   ?   C . n 
C 2 32  ILE 32  9   ?   ?   ?   C . n 
C 2 33  VAL 33  10  ?   ?   ?   C . n 
C 2 34  PRO 34  11  ?   ?   ?   C . n 
C 2 35  LEU 35  12  ?   ?   ?   C . n 
C 2 36  THR 36  13  ?   ?   ?   C . n 
C 2 37  LEU 37  14  ?   ?   ?   C . n 
C 2 38  GLY 38  15  ?   ?   ?   C . n 
C 2 39  GLY 39  16  ?   ?   ?   C . n 
C 2 40  LEU 40  17  ?   ?   ?   C . n 
C 2 41  LEU 41  18  ?   ?   ?   C . n 
C 2 42  GLY 42  19  ?   ?   ?   C . n 
C 2 43  VAL 43  20  ?   ?   ?   C . n 
C 2 44  ALA 44  21  ?   ?   ?   C . n 
C 2 45  TRP 45  22  ?   ?   ?   C . n 
C 2 46  GLY 46  23  ?   ?   ?   C . n 
C 2 47  ALA 47  24  ?   ?   ?   C . n 
C 2 48  SER 48  25  ?   ?   ?   C . n 
C 2 49  SER 49  26  ?   ?   ?   C . n 
C 2 50  LEU 50  27  ?   ?   ?   C . n 
C 2 51  GLY 51  28  ?   ?   ?   C . n 
C 2 52  ALA 52  29  ?   ?   ?   C . n 
C 2 53  HIS 53  30  ?   ?   ?   C . n 
C 2 54  HIS 54  31  ?   ?   ?   C . n 
C 2 55  ILE 55  32  ?   ?   ?   C . n 
C 2 56  HIS 56  33  ?   ?   ?   C . n 
C 2 57  HIS 57  34  ?   ?   ?   C . n 
C 2 58  PHE 58  35  ?   ?   ?   C . n 
C 2 59  HIS 59  36  ?   ?   ?   C . n 
C 2 60  GLY 60  37  ?   ?   ?   C . n 
C 2 61  SER 61  38  ?   ?   ?   C . n 
C 2 62  SER 62  39  ?   ?   ?   C . n 
C 2 63  LYS 63  40  ?   ?   ?   C . n 
C 2 64  GLU 64  41  ?   ?   ?   C . n 
C 2 65  PHE 65  42  ?   ?   ?   C . n 
C 2 66  GLU 66  43  ?   ?   ?   C . n 
C 2 67  GLN 67  44  ?   ?   ?   C . n 
C 2 68  LYS 68  45  ?   ?   ?   C . n 
C 2 69  LEU 69  46  ?   ?   ?   C . n 
C 2 70  ILE 70  47  ?   ?   ?   C . n 
C 2 71  SER 71  48  ?   ?   ?   C . n 
C 2 72  GLU 72  49  ?   ?   ?   C . n 
C 2 73  GLU 73  50  ?   ?   ?   C . n 
C 2 74  ASP 74  51  ?   ?   ?   C . n 
C 2 75  LEU 75  52  ?   ?   ?   C . n 
C 2 76  GLY 76  53  ?   ?   ?   C . n 
C 2 77  PHE 77  54  ?   ?   ?   C . n 
C 2 78  GLU 78  55  ?   ?   ?   C . n 
C 2 79  ILE 79  56  ?   ?   ?   C . n 
C 2 80  ASP 80  57  ?   ?   ?   C . n 
C 2 81  LYS 81  58  ?   ?   ?   C . n 
C 2 82  VAL 82  59  ?   ?   ?   C . n 
C 2 83  TRP 83  60  ?   ?   ?   C . n 
C 2 84  HIS 84  61  ?   ?   ?   C . n 
C 2 85  ASP 85  62  ?   ?   ?   C . n 
C 2 86  PHE 86  63  ?   ?   ?   C . n 
C 2 87  PRO 87  64  ?   ?   ?   C . n 
C 2 88  ALA 88  65  ?   ?   ?   C . n 
C 2 89  THR 89  66  ?   ?   ?   C . n 
C 2 90  SER 90  67  ?   ?   ?   C . n 
C 2 91  PRO 91  68  ?   ?   ?   C . n 
C 2 92  ILE 92  69  ?   ?   ?   C . n 
C 2 93  ALA 93  70  ?   ?   ?   C . n 
C 2 94  ILE 94  71  ?   ?   ?   C . n 
C 2 95  TYR 95  72  ?   ?   ?   C . n 
C 2 96  ARG 96  73  ?   ?   ?   C . n 
C 2 97  SER 97  74  ?   ?   ?   C . n 
C 2 98  PRO 98  75  ?   ?   ?   C . n 
C 2 99  ALA 99  76  ?   ?   ?   C . n 
C 2 100 SER 100 77  ?   ?   ?   C . n 
C 2 101 LEU 101 78  ?   ?   ?   C . n 
C 2 102 ARG 102 79  ?   ?   ?   C . n 
C 2 103 GLY 103 80  ?   ?   ?   C . n 
C 2 104 GLY 104 81  ?   ?   ?   C . n 
C 2 105 HIS 105 82  ?   ?   ?   C . n 
C 2 106 ALA 106 83  83  ALA ALA C . n 
C 2 107 GLY 107 84  84  GLY GLY C . n 
C 2 108 THR 108 85  85  THR THR C . n 
C 2 109 THR 109 86  86  THR THR C . n 
C 2 110 TYR 110 87  87  TYR TYR C . n 
C 2 111 ILE 111 88  88  ILE ILE C . n 
C 2 112 PHE 112 89  89  PHE PHE C . n 
C 2 113 SER 113 90  90  SER SER C . n 
C 2 114 LYS 114 91  91  LYS LYS C . n 
C 2 115 GLY 115 92  92  GLY GLY C . n 
C 2 116 GLY 116 93  93  GLY GLY C . n 
C 2 117 GLY 117 94  94  GLY GLY C . n 
C 2 118 GLN 118 95  95  GLN GLN C . n 
C 2 119 ILE 119 96  96  ILE ILE C . n 
C 2 120 THR 120 97  97  THR THR C . n 
C 2 121 TYR 121 98  98  TYR TYR C . n 
C 2 122 LYS 122 99  99  LYS LYS C . n 
C 2 123 TRP 123 100 100 TRP TRP C . n 
C 2 124 PRO 124 101 101 PRO PRO C . n 
C 2 125 PRO 125 102 102 PRO PRO C . n 
C 2 126 ASN 126 103 103 ASN ASN C . n 
C 2 127 ASP 127 104 104 ASP ASP C . n 
C 2 128 ARG 128 105 105 ARG ARG C . n 
C 2 129 PRO 129 106 106 PRO PRO C . n 
C 2 130 SER 130 107 107 SER SER C . n 
C 2 131 THR 131 108 108 THR THR C . n 
C 2 132 ARG 132 109 109 ARG ARG C . n 
C 2 133 ALA 133 110 110 ALA ALA C . n 
C 2 134 ASP 134 111 111 ASP ASP C . n 
C 2 135 ARG 135 112 112 ARG ARG C . n 
C 2 136 LEU 136 113 113 LEU LEU C . n 
C 2 137 ALA 137 114 114 ALA ALA C . n 
C 2 138 ILE 138 115 115 ILE ILE C . n 
C 2 139 GLY 139 116 116 GLY GLY C . n 
C 2 140 PHE 140 117 117 PHE PHE C . n 
C 2 141 SER 141 118 118 SER SER C . n 
C 2 142 THR 142 119 119 THR THR C . n 
C 2 143 VAL 143 120 120 VAL VAL C . n 
C 2 144 GLN 144 121 121 GLN GLN C . n 
C 2 145 LYS 145 122 122 LYS LYS C . n 
C 2 146 GLU 146 123 123 GLU GLU C . n 
C 2 147 ALA 147 124 124 ALA ALA C . n 
C 2 148 VAL 148 125 125 VAL VAL C . n 
C 2 149 LEU 149 126 126 LEU LEU C . n 
C 2 150 VAL 150 127 127 VAL VAL C . n 
C 2 151 ARG 151 128 128 ARG ARG C . n 
C 2 152 VAL 152 129 129 VAL VAL C . n 
C 2 153 ASP 153 130 130 ASP ASP C . n 
C 2 154 SER 154 131 131 SER SER C . n 
C 2 155 SER 155 132 132 SER SER C . n 
C 2 156 SER 156 133 133 SER SER C . n 
C 2 157 GLY 157 134 134 GLY GLY C . n 
C 2 158 LEU 158 135 135 LEU LEU C . n 
C 2 159 GLY 159 136 136 GLY GLY C . n 
C 2 160 ASP 160 137 137 ASP ASP C . n 
C 2 161 TYR 161 138 138 TYR TYR C . n 
C 2 162 LEU 162 139 139 LEU LEU C . n 
C 2 163 GLU 163 140 140 GLU GLU C . n 
C 2 164 LEU 164 141 141 LEU LEU C . n 
C 2 165 HIS 165 142 142 HIS HIS C . n 
C 2 166 ILE 166 143 143 ILE ILE C . n 
C 2 167 HIS 167 144 144 HIS HIS C . n 
C 2 168 GLN 168 145 145 GLN GLN C . n 
C 2 169 GLY 169 146 146 GLY GLY C . n 
C 2 170 LYS 170 147 147 LYS LYS C . n 
C 2 171 ILE 171 148 148 ILE ILE C . n 
C 2 172 GLY 172 149 149 GLY GLY C . n 
C 2 173 VAL 173 150 150 VAL VAL C . n 
C 2 174 LYS 174 151 151 LYS LYS C . n 
C 2 175 PHE 175 152 152 PHE PHE C . n 
C 2 176 ASN 176 153 153 ASN ASN C . n 
C 2 177 VAL 177 154 154 VAL VAL C . n 
C 2 178 GLY 178 155 155 GLY GLY C . n 
C 2 179 THR 179 156 156 THR THR C . n 
C 2 180 ASP 180 157 157 ASP ASP C . n 
C 2 181 ASP 181 158 158 ASP ASP C . n 
C 2 182 ILE 182 159 159 ILE ILE C . n 
C 2 183 ALA 183 160 160 ALA ALA C . n 
C 2 184 ILE 184 161 161 ILE ILE C . n 
C 2 185 GLU 185 162 162 GLU GLU C . n 
C 2 186 GLU 186 163 163 GLU GLU C . n 
C 2 187 SER 187 164 164 SER SER C . n 
C 2 188 ASN 188 165 165 ASN ASN C . n 
C 2 189 ALA 189 166 166 ALA ALA C . n 
C 2 190 ILE 190 167 167 ILE ILE C . n 
C 2 191 ILE 191 168 168 ILE ILE C . n 
C 2 192 ASN 192 169 169 ASN ASN C . n 
C 2 193 ASP 193 170 170 ASP ASP C . n 
C 2 194 GLY 194 171 171 GLY GLY C . n 
C 2 195 LYS 195 172 172 LYS LYS C . n 
C 2 196 TYR 196 173 173 TYR TYR C . n 
C 2 197 HIS 197 174 174 HIS HIS C . n 
C 2 198 VAL 198 175 175 VAL VAL C . n 
C 2 199 VAL 199 176 176 VAL VAL C . n 
C 2 200 ARG 200 177 177 ARG ARG C . n 
C 2 201 PHE 201 178 178 PHE PHE C . n 
C 2 202 THR 202 179 179 THR THR C . n 
C 2 203 ARG 203 180 180 ARG ARG C . n 
C 2 204 SER 204 181 181 SER SER C . n 
C 2 205 GLY 205 182 182 GLY GLY C . n 
C 2 206 GLY 206 183 183 GLY GLY C . n 
C 2 207 ASN 207 184 184 ASN ASN C . n 
C 2 208 ALA 208 185 185 ALA ALA C . n 
C 2 209 THR 209 186 186 THR THR C . n 
C 2 210 LEU 210 187 187 LEU LEU C . n 
C 2 211 GLN 211 188 188 GLN GLN C . n 
C 2 212 VAL 212 189 189 VAL VAL C . n 
C 2 213 ASP 213 190 190 ASP ASP C . n 
C 2 214 SER 214 191 191 SER SER C . n 
C 2 215 TRP 215 192 192 TRP TRP C . n 
C 2 216 PRO 216 193 193 PRO PRO C . n 
C 2 217 VAL 217 194 194 VAL VAL C . n 
C 2 218 ILE 218 195 195 ILE ILE C . n 
C 2 219 GLU 219 196 196 GLU GLU C . n 
C 2 220 ARG 220 197 197 ARG ARG C . n 
C 2 221 TYR 221 198 198 TYR TYR C . n 
C 2 222 PRO 222 199 199 PRO PRO C . n 
C 2 223 ALA 223 200 200 ALA ALA C . n 
C 2 224 GLY 224 201 201 GLY GLY C . n 
C 2 225 ARG 225 232 232 ARG ARG C . n 
C 2 226 GLN 226 233 233 GLN GLN C . n 
C 2 227 LEU 227 234 234 LEU LEU C . n 
C 2 228 THR 228 235 235 THR THR C . n 
C 2 229 ILE 229 236 236 ILE ILE C . n 
C 2 230 PHE 230 237 237 PHE PHE C . n 
C 2 231 ASN 231 238 238 ASN ASN C . n 
C 2 232 SER 232 239 239 SER SER C . n 
C 2 233 GLN 233 240 240 GLN GLN C . n 
C 2 234 ALA 234 241 241 ALA ALA C . n 
C 2 235 THR 235 242 242 THR THR C . n 
C 2 236 ILE 236 243 243 ILE ILE C . n 
C 2 237 ILE 237 244 244 ILE ILE C . n 
C 2 238 ILE 238 245 245 ILE ILE C . n 
C 2 239 GLY 239 246 246 GLY GLY C . n 
C 2 240 GLY 240 247 247 GLY GLY C . n 
C 2 241 LYS 241 248 248 LYS LYS C . n 
C 2 242 GLU 242 249 249 GLU GLU C . n 
C 2 243 GLN 243 250 250 GLN GLN C . n 
C 2 244 GLY 244 251 251 GLY GLY C . n 
C 2 245 GLN 245 252 252 GLN GLN C . n 
C 2 246 PRO 246 253 253 PRO PRO C . n 
C 2 247 PHE 247 254 254 PHE PHE C . n 
C 2 248 GLN 248 255 255 GLN GLN C . n 
C 2 249 GLY 249 256 256 GLY GLY C . n 
C 2 250 GLN 250 257 257 GLN GLN C . n 
C 2 251 LEU 251 258 258 LEU LEU C . n 
C 2 252 SER 252 259 259 SER SER C . n 
C 2 253 GLY 253 260 260 GLY GLY C . n 
C 2 254 LEU 254 261 261 LEU LEU C . n 
C 2 255 TYR 255 262 262 TYR TYR C . n 
C 2 256 TYR 256 263 263 TYR TYR C . n 
C 2 257 ASN 257 264 264 ASN ASN C . n 
C 2 258 GLY 258 265 265 GLY GLY C . n 
C 2 259 LEU 259 266 266 LEU LEU C . n 
C 2 260 LYS 260 267 267 LYS LYS C . n 
C 2 261 VAL 261 268 268 VAL VAL C . n 
C 2 262 LEU 262 269 269 LEU LEU C . n 
C 2 263 ASN 263 270 270 ASN ASN C . n 
C 2 264 MET 264 271 271 MET MET C . n 
C 2 265 ALA 265 272 272 ALA ALA C . n 
C 2 266 ALA 266 273 273 ALA ALA C . n 
C 2 267 GLU 267 274 274 GLU GLU C . n 
C 2 268 ASN 268 275 275 ASN ASN C . n 
C 2 269 ASP 269 276 276 ASP ASP C . n 
C 2 270 ALA 270 277 277 ALA ALA C . n 
C 2 271 ASN 271 278 278 ASN ASN C . n 
C 2 272 ILE 272 279 279 ILE ILE C . n 
C 2 273 ALA 273 280 280 ALA ALA C . n 
C 2 274 ILE 274 281 281 ILE ILE C . n 
C 2 275 VAL 275 282 282 VAL VAL C . n 
C 2 276 GLY 276 283 283 GLY GLY C . n 
C 2 277 ASN 277 284 284 ASN ASN C . n 
C 2 278 VAL 278 285 285 VAL VAL C . n 
C 2 279 ARG 279 286 286 ARG ARG C . n 
C 2 280 LEU 280 287 287 LEU LEU C . n 
C 2 281 VAL 281 288 288 VAL VAL C . n 
C 2 282 GLY 282 289 289 GLY GLY C . n 
C 2 283 GLU 283 290 ?   ?   ?   C . n 
C 2 284 VAL 284 291 ?   ?   ?   C . n 
C 2 285 PRO 285 292 ?   ?   ?   C . n 
C 2 286 SER 286 293 ?   ?   ?   C . n 
C 2 287 SER 287 294 ?   ?   ?   C . n 
C 2 288 MET 288 295 ?   ?   ?   C . n 
C 2 289 THR 289 296 ?   ?   ?   C . n 
C 2 290 THR 290 297 ?   ?   ?   C . n 
C 2 291 GLU 291 298 ?   ?   ?   C . n 
C 2 292 SER 292 299 ?   ?   ?   C . n 
C 2 293 THR 293 300 ?   ?   ?   C . n 
C 2 294 ALA 294 301 ?   ?   ?   C . n 
C 2 295 THR 295 302 ?   ?   ?   C . n 
C 2 296 ALA 296 303 ?   ?   ?   C . n 
C 2 297 MET 297 304 ?   ?   ?   C . n 
C 2 298 GLN 298 305 ?   ?   ?   C . n 
C 2 299 SER 299 306 ?   ?   ?   C . n 
C 2 300 GLU 300 307 ?   ?   ?   C . n 
C 2 301 MET 301 308 ?   ?   ?   C . n 
C 2 302 SER 302 309 ?   ?   ?   C . n 
C 2 303 THR 303 310 ?   ?   ?   C . n 
C 2 304 SER 304 311 ?   ?   ?   C . n 
C 2 305 ILE 305 312 ?   ?   ?   C . n 
C 2 306 MET 306 313 ?   ?   ?   C . n 
C 2 307 GLU 307 314 ?   ?   ?   C . n 
C 2 308 THR 308 315 ?   ?   ?   C . n 
C 2 309 THR 309 316 ?   ?   ?   C . n 
C 2 310 THR 310 317 ?   ?   ?   C . n 
C 2 311 THR 311 318 ?   ?   ?   C . n 
C 2 312 LEU 312 319 ?   ?   ?   C . n 
C 2 313 ALA 313 320 ?   ?   ?   C . n 
C 2 314 THR 314 321 ?   ?   ?   C . n 
C 2 315 SER 315 322 ?   ?   ?   C . n 
C 2 316 THR 316 323 ?   ?   ?   C . n 
C 2 317 ALA 317 324 ?   ?   ?   C . n 
C 2 318 ARG 318 325 ?   ?   ?   C . n 
C 2 319 ARG 319 326 ?   ?   ?   C . n 
C 2 320 GLY 320 327 ?   ?   ?   C . n 
C 2 321 LYS 321 328 ?   ?   ?   C . n 
C 2 322 PRO 322 329 ?   ?   ?   C . n 
C 2 323 PRO 323 330 ?   ?   ?   C . n 
C 2 324 THR 324 331 ?   ?   ?   C . n 
C 2 325 LYS 325 332 ?   ?   ?   C . n 
C 2 326 GLU 326 333 ?   ?   ?   C . n 
C 2 327 PRO 327 334 ?   ?   ?   C . n 
C 2 328 ILE 328 335 ?   ?   ?   C . n 
C 2 329 SER 329 336 ?   ?   ?   C . n 
C 2 330 GLN 330 337 ?   ?   ?   C . n 
C 2 331 THR 331 338 ?   ?   ?   C . n 
C 2 332 THR 332 339 ?   ?   ?   C . n 
C 2 333 ASP 333 340 ?   ?   ?   C . n 
C 2 334 ASP 334 341 ?   ?   ?   C . n 
C 2 335 ILE 335 342 ?   ?   ?   C . n 
C 2 336 LEU 336 343 ?   ?   ?   C . n 
C 2 337 VAL 337 344 ?   ?   ?   C . n 
C 2 338 ALA 338 345 ?   ?   ?   C . n 
C 2 339 SER 339 346 ?   ?   ?   C . n 
C 2 340 ALA 340 347 ?   ?   ?   C . n 
C 2 341 GLU 341 348 ?   ?   ?   C . n 
C 2 342 CYS 342 349 ?   ?   ?   C . n 
C 2 343 PRO 343 350 ?   ?   ?   C . n 
C 2 344 SER 344 351 ?   ?   ?   C . n 
C 2 345 ASP 345 352 ?   ?   ?   C . n 
C 2 346 ASP 346 353 ?   ?   ?   C . n 
C 2 347 GLU 347 354 ?   ?   ?   C . n 
C 2 348 ASP 348 355 ?   ?   ?   C . n 
C 2 349 ILE 349 356 ?   ?   ?   C . n 
C 2 350 ASP 350 357 ?   ?   ?   C . n 
C 2 351 PRO 351 358 ?   ?   ?   C . n 
C 2 352 CYS 352 359 ?   ?   ?   C . n 
C 2 353 GLU 353 360 ?   ?   ?   C . n 
C 2 354 PRO 354 361 ?   ?   ?   C . n 
C 2 355 SER 355 362 ?   ?   ?   C . n 
C 2 356 SER 356 363 ?   ?   ?   C . n 
C 2 357 GLY 357 364 ?   ?   ?   C . n 
C 2 358 GLY 358 365 ?   ?   ?   C . n 
C 2 359 LEU 359 366 ?   ?   ?   C . n 
C 2 360 ALA 360 367 ?   ?   ?   C . n 
C 2 361 ASN 361 368 ?   ?   ?   C . n 
C 2 362 PRO 362 369 ?   ?   ?   C . n 
C 2 363 THR 363 370 ?   ?   ?   C . n 
C 2 364 ARG 364 371 ?   ?   ?   C . n 
C 2 365 VAL 365 372 ?   ?   ?   C . n 
C 2 366 GLY 366 373 ?   ?   ?   C . n 
C 2 367 GLY 367 374 ?   ?   ?   C . n 
C 2 368 ARG 368 375 ?   ?   ?   C . n 
C 2 369 GLU 369 376 ?   ?   ?   C . n 
C 2 370 PRO 370 377 ?   ?   ?   C . n 
C 2 371 TYR 371 378 ?   ?   ?   C . n 
C 2 372 PRO 372 379 ?   ?   ?   C . n 
C 2 373 GLY 373 380 ?   ?   ?   C . n 
C 2 374 SER 374 381 ?   ?   ?   C . n 
C 2 375 ALA 375 382 ?   ?   ?   C . n 
C 2 376 GLU 376 383 ?   ?   ?   C . n 
C 2 377 VAL 377 384 ?   ?   ?   C . n 
C 2 378 ILE 378 385 ?   ?   ?   C . n 
C 2 379 ARG 379 386 ?   ?   ?   C . n 
C 2 380 GLU 380 387 ?   ?   ?   C . n 
C 2 381 SER 381 388 ?   ?   ?   C . n 
C 2 382 SER 382 389 ?   ?   ?   C . n 
C 2 383 SER 383 390 ?   ?   ?   C . n 
C 2 384 THR 384 391 ?   ?   ?   C . n 
C 2 385 THR 385 392 ?   ?   ?   C . n 
C 2 386 GLY 386 393 ?   ?   ?   C . n 
C 2 387 MET 387 394 ?   ?   ?   C . n 
C 2 388 VAL 388 395 ?   ?   ?   C . n 
C 2 389 VAL 389 396 ?   ?   ?   C . n 
C 2 390 GLY 390 397 ?   ?   ?   C . n 
C 2 391 ILE 391 398 ?   ?   ?   C . n 
C 2 392 VAL 392 399 ?   ?   ?   C . n 
C 2 393 ALA 393 400 ?   ?   ?   C . n 
C 2 394 ALA 394 401 ?   ?   ?   C . n 
C 2 395 ALA 395 402 ?   ?   ?   C . n 
C 2 396 ALA 396 403 ?   ?   ?   C . n 
C 2 397 LEU 397 404 ?   ?   ?   C . n 
C 2 398 CYS 398 405 ?   ?   ?   C . n 
C 2 399 ILE 399 406 ?   ?   ?   C . n 
C 2 400 LEU 400 407 ?   ?   ?   C . n 
C 2 401 ILE 401 408 ?   ?   ?   C . n 
C 2 402 LEU 402 409 ?   ?   ?   C . n 
C 2 403 LEU 403 410 ?   ?   ?   C . n 
C 2 404 TYR 404 411 ?   ?   ?   C . n 
C 2 405 ALA 405 412 ?   ?   ?   C . n 
C 2 406 MET 406 413 ?   ?   ?   C . n 
C 2 407 TYR 407 414 ?   ?   ?   C . n 
C 2 408 LYS 408 415 ?   ?   ?   C . n 
C 2 409 TYR 409 416 ?   ?   ?   C . n 
C 2 410 ARG 410 417 ?   ?   ?   C . n 
C 2 411 ASN 411 418 ?   ?   ?   C . n 
C 2 412 ARG 412 419 ?   ?   ?   C . n 
C 2 413 ASP 413 420 ?   ?   ?   C . n 
C 2 414 GLU 414 421 ?   ?   ?   C . n 
C 2 415 GLY 415 422 ?   ?   ?   C . n 
C 2 416 SER 416 423 ?   ?   ?   C . n 
C 2 417 TYR 417 424 ?   ?   ?   C . n 
C 2 418 HIS 418 425 ?   ?   ?   C . n 
C 2 419 VAL 419 426 ?   ?   ?   C . n 
C 2 420 ASP 420 427 ?   ?   ?   C . n 
C 2 421 GLU 421 428 ?   ?   ?   C . n 
C 2 422 SER 422 429 ?   ?   ?   C . n 
C 2 423 ARG 423 430 ?   ?   ?   C . n 
C 2 424 ASN 424 431 ?   ?   ?   C . n 
C 2 425 TYR 425 432 ?   ?   ?   C . n 
C 2 426 ILE 426 433 ?   ?   ?   C . n 
C 2 427 SER 427 434 ?   ?   ?   C . n 
C 2 428 ASN 428 435 ?   ?   ?   C . n 
C 2 429 SER 429 436 ?   ?   ?   C . n 
C 2 430 ALA 430 437 ?   ?   ?   C . n 
C 2 431 GLN 431 438 ?   ?   ?   C . n 
C 2 432 SER 432 439 ?   ?   ?   C . n 
C 2 433 ASN 433 440 ?   ?   ?   C . n 
C 2 434 GLY 434 441 ?   ?   ?   C . n 
C 2 435 ALA 435 442 ?   ?   ?   C . n 
C 2 436 VAL 436 443 ?   ?   ?   C . n 
C 2 437 VAL 437 444 ?   ?   ?   C . n 
C 2 438 LYS 438 445 ?   ?   ?   C . n 
C 2 439 GLU 439 446 ?   ?   ?   C . n 
C 2 440 LYS 440 447 ?   ?   ?   C . n 
C 2 441 GLN 441 448 ?   ?   ?   C . n 
C 2 442 PRO 442 449 ?   ?   ?   C . n 
C 2 443 SER 443 450 ?   ?   ?   C . n 
C 2 444 SER 444 451 ?   ?   ?   C . n 
C 2 445 ALA 445 452 ?   ?   ?   C . n 
C 2 446 LYS 446 453 ?   ?   ?   C . n 
C 2 447 SER 447 454 ?   ?   ?   C . n 
C 2 448 ALA 448 455 ?   ?   ?   C . n 
C 2 449 ASN 449 456 ?   ?   ?   C . n 
C 2 450 LYS 450 457 ?   ?   ?   C . n 
C 2 451 ASN 451 458 ?   ?   ?   C . n 
C 2 452 LYS 452 459 ?   ?   ?   C . n 
C 2 453 LYS 453 460 ?   ?   ?   C . n 
C 2 454 ASN 454 461 ?   ?   ?   C . n 
C 2 455 LYS 455 462 ?   ?   ?   C . n 
C 2 456 ASP 456 463 ?   ?   ?   C . n 
C 2 457 LYS 457 464 ?   ?   ?   C . n 
C 2 458 GLU 458 465 ?   ?   ?   C . n 
C 2 459 TYR 459 466 ?   ?   ?   C . n 
C 2 460 TYR 460 467 ?   ?   ?   C . n 
C 2 461 VAL 461 468 ?   ?   ?   C . n 
C 2 462 SER 462 469 ?   ?   ?   C . n 
C 2 463 ASN 463 470 ?   ?   ?   C . n 
C 2 464 SER 464 471 ?   ?   ?   C . n 
C 2 465 LEU 465 472 ?   ?   ?   C . n 
C 2 466 GLU 466 473 ?   ?   ?   C . n 
C 2 467 VAL 467 474 ?   ?   ?   C . n 
C 2 468 LEU 468 475 ?   ?   ?   C . n 
C 2 469 PHE 469 476 ?   ?   ?   C . n 
C 2 470 GLN 470 477 ?   ?   ?   C . n 
D 2 1   MET 1   -22 ?   ?   ?   D . n 
D 2 2   TYR 2   -21 ?   ?   ?   D . n 
D 2 3   GLN 3   -20 ?   ?   ?   D . n 
D 2 4   ARG 4   -19 ?   ?   ?   D . n 
D 2 5   MET 5   -18 ?   ?   ?   D . n 
D 2 6   LEU 6   -17 ?   ?   ?   D . n 
D 2 7   ARG 7   -16 ?   ?   ?   D . n 
D 2 8   CYS 8   -15 ?   ?   ?   D . n 
D 2 9   GLY 9   -14 ?   ?   ?   D . n 
D 2 10  ALA 10  -13 ?   ?   ?   D . n 
D 2 11  ASP 11  -12 ?   ?   ?   D . n 
D 2 12  LEU 12  -11 ?   ?   ?   D . n 
D 2 13  GLY 13  -10 ?   ?   ?   D . n 
D 2 14  SER 14  -9  ?   ?   ?   D . n 
D 2 15  PRO 15  -8  ?   ?   ?   D . n 
D 2 16  GLY 16  -7  ?   ?   ?   D . n 
D 2 17  GLY 17  -6  ?   ?   ?   D . n 
D 2 18  GLY 18  -5  ?   ?   ?   D . n 
D 2 19  SER 19  -4  ?   ?   ?   D . n 
D 2 20  GLY 20  -3  ?   ?   ?   D . n 
D 2 21  GLY 21  -2  ?   ?   ?   D . n 
D 2 22  GLY 22  -1  ?   ?   ?   D . n 
D 2 23  ALA 23  0   ?   ?   ?   D . n 
D 2 24  GLY 24  1   ?   ?   ?   D . n 
D 2 25  GLY 25  2   ?   ?   ?   D . n 
D 2 26  ARG 26  3   ?   ?   ?   D . n 
D 2 27  LEU 27  4   ?   ?   ?   D . n 
D 2 28  ALA 28  5   ?   ?   ?   D . n 
D 2 29  LEU 29  6   ?   ?   ?   D . n 
D 2 30  ILE 30  7   ?   ?   ?   D . n 
D 2 31  TRP 31  8   ?   ?   ?   D . n 
D 2 32  ILE 32  9   ?   ?   ?   D . n 
D 2 33  VAL 33  10  ?   ?   ?   D . n 
D 2 34  PRO 34  11  ?   ?   ?   D . n 
D 2 35  LEU 35  12  ?   ?   ?   D . n 
D 2 36  THR 36  13  ?   ?   ?   D . n 
D 2 37  LEU 37  14  ?   ?   ?   D . n 
D 2 38  GLY 38  15  ?   ?   ?   D . n 
D 2 39  GLY 39  16  ?   ?   ?   D . n 
D 2 40  LEU 40  17  ?   ?   ?   D . n 
D 2 41  LEU 41  18  ?   ?   ?   D . n 
D 2 42  GLY 42  19  ?   ?   ?   D . n 
D 2 43  VAL 43  20  ?   ?   ?   D . n 
D 2 44  ALA 44  21  ?   ?   ?   D . n 
D 2 45  TRP 45  22  ?   ?   ?   D . n 
D 2 46  GLY 46  23  ?   ?   ?   D . n 
D 2 47  ALA 47  24  ?   ?   ?   D . n 
D 2 48  SER 48  25  ?   ?   ?   D . n 
D 2 49  SER 49  26  ?   ?   ?   D . n 
D 2 50  LEU 50  27  ?   ?   ?   D . n 
D 2 51  GLY 51  28  ?   ?   ?   D . n 
D 2 52  ALA 52  29  ?   ?   ?   D . n 
D 2 53  HIS 53  30  ?   ?   ?   D . n 
D 2 54  HIS 54  31  ?   ?   ?   D . n 
D 2 55  ILE 55  32  ?   ?   ?   D . n 
D 2 56  HIS 56  33  ?   ?   ?   D . n 
D 2 57  HIS 57  34  ?   ?   ?   D . n 
D 2 58  PHE 58  35  ?   ?   ?   D . n 
D 2 59  HIS 59  36  ?   ?   ?   D . n 
D 2 60  GLY 60  37  ?   ?   ?   D . n 
D 2 61  SER 61  38  ?   ?   ?   D . n 
D 2 62  SER 62  39  ?   ?   ?   D . n 
D 2 63  LYS 63  40  ?   ?   ?   D . n 
D 2 64  GLU 64  41  ?   ?   ?   D . n 
D 2 65  PHE 65  42  ?   ?   ?   D . n 
D 2 66  GLU 66  43  ?   ?   ?   D . n 
D 2 67  GLN 67  44  ?   ?   ?   D . n 
D 2 68  LYS 68  45  ?   ?   ?   D . n 
D 2 69  LEU 69  46  ?   ?   ?   D . n 
D 2 70  ILE 70  47  ?   ?   ?   D . n 
D 2 71  SER 71  48  ?   ?   ?   D . n 
D 2 72  GLU 72  49  ?   ?   ?   D . n 
D 2 73  GLU 73  50  ?   ?   ?   D . n 
D 2 74  ASP 74  51  ?   ?   ?   D . n 
D 2 75  LEU 75  52  ?   ?   ?   D . n 
D 2 76  GLY 76  53  ?   ?   ?   D . n 
D 2 77  PHE 77  54  ?   ?   ?   D . n 
D 2 78  GLU 78  55  ?   ?   ?   D . n 
D 2 79  ILE 79  56  ?   ?   ?   D . n 
D 2 80  ASP 80  57  ?   ?   ?   D . n 
D 2 81  LYS 81  58  ?   ?   ?   D . n 
D 2 82  VAL 82  59  ?   ?   ?   D . n 
D 2 83  TRP 83  60  ?   ?   ?   D . n 
D 2 84  HIS 84  61  ?   ?   ?   D . n 
D 2 85  ASP 85  62  ?   ?   ?   D . n 
D 2 86  PHE 86  63  ?   ?   ?   D . n 
D 2 87  PRO 87  64  ?   ?   ?   D . n 
D 2 88  ALA 88  65  ?   ?   ?   D . n 
D 2 89  THR 89  66  ?   ?   ?   D . n 
D 2 90  SER 90  67  ?   ?   ?   D . n 
D 2 91  PRO 91  68  ?   ?   ?   D . n 
D 2 92  ILE 92  69  ?   ?   ?   D . n 
D 2 93  ALA 93  70  ?   ?   ?   D . n 
D 2 94  ILE 94  71  ?   ?   ?   D . n 
D 2 95  TYR 95  72  ?   ?   ?   D . n 
D 2 96  ARG 96  73  ?   ?   ?   D . n 
D 2 97  SER 97  74  ?   ?   ?   D . n 
D 2 98  PRO 98  75  ?   ?   ?   D . n 
D 2 99  ALA 99  76  ?   ?   ?   D . n 
D 2 100 SER 100 77  ?   ?   ?   D . n 
D 2 101 LEU 101 78  ?   ?   ?   D . n 
D 2 102 ARG 102 79  ?   ?   ?   D . n 
D 2 103 GLY 103 80  ?   ?   ?   D . n 
D 2 104 GLY 104 81  ?   ?   ?   D . n 
D 2 105 HIS 105 82  ?   ?   ?   D . n 
D 2 106 ALA 106 83  83  ALA ALA D . n 
D 2 107 GLY 107 84  84  GLY GLY D . n 
D 2 108 THR 108 85  85  THR THR D . n 
D 2 109 THR 109 86  86  THR THR D . n 
D 2 110 TYR 110 87  87  TYR TYR D . n 
D 2 111 ILE 111 88  88  ILE ILE D . n 
D 2 112 PHE 112 89  89  PHE PHE D . n 
D 2 113 SER 113 90  90  SER SER D . n 
D 2 114 LYS 114 91  91  LYS LYS D . n 
D 2 115 GLY 115 92  92  GLY GLY D . n 
D 2 116 GLY 116 93  93  GLY GLY D . n 
D 2 117 GLY 117 94  94  GLY GLY D . n 
D 2 118 GLN 118 95  95  GLN GLN D . n 
D 2 119 ILE 119 96  96  ILE ILE D . n 
D 2 120 THR 120 97  97  THR THR D . n 
D 2 121 TYR 121 98  98  TYR TYR D . n 
D 2 122 LYS 122 99  99  LYS LYS D . n 
D 2 123 TRP 123 100 100 TRP TRP D . n 
D 2 124 PRO 124 101 101 PRO PRO D . n 
D 2 125 PRO 125 102 102 PRO PRO D . n 
D 2 126 ASN 126 103 103 ASN ASN D . n 
D 2 127 ASP 127 104 104 ASP ASP D . n 
D 2 128 ARG 128 105 105 ARG ARG D . n 
D 2 129 PRO 129 106 106 PRO PRO D . n 
D 2 130 SER 130 107 107 SER SER D . n 
D 2 131 THR 131 108 108 THR THR D . n 
D 2 132 ARG 132 109 109 ARG ARG D . n 
D 2 133 ALA 133 110 110 ALA ALA D . n 
D 2 134 ASP 134 111 111 ASP ASP D . n 
D 2 135 ARG 135 112 112 ARG ARG D . n 
D 2 136 LEU 136 113 113 LEU LEU D . n 
D 2 137 ALA 137 114 114 ALA ALA D . n 
D 2 138 ILE 138 115 115 ILE ILE D . n 
D 2 139 GLY 139 116 116 GLY GLY D . n 
D 2 140 PHE 140 117 117 PHE PHE D . n 
D 2 141 SER 141 118 118 SER SER D . n 
D 2 142 THR 142 119 119 THR THR D . n 
D 2 143 VAL 143 120 120 VAL VAL D . n 
D 2 144 GLN 144 121 121 GLN GLN D . n 
D 2 145 LYS 145 122 122 LYS LYS D . n 
D 2 146 GLU 146 123 123 GLU GLU D . n 
D 2 147 ALA 147 124 124 ALA ALA D . n 
D 2 148 VAL 148 125 125 VAL VAL D . n 
D 2 149 LEU 149 126 126 LEU LEU D . n 
D 2 150 VAL 150 127 127 VAL VAL D . n 
D 2 151 ARG 151 128 128 ARG ARG D . n 
D 2 152 VAL 152 129 129 VAL VAL D . n 
D 2 153 ASP 153 130 130 ASP ASP D . n 
D 2 154 SER 154 131 131 SER SER D . n 
D 2 155 SER 155 132 132 SER SER D . n 
D 2 156 SER 156 133 133 SER SER D . n 
D 2 157 GLY 157 134 134 GLY GLY D . n 
D 2 158 LEU 158 135 135 LEU LEU D . n 
D 2 159 GLY 159 136 136 GLY GLY D . n 
D 2 160 ASP 160 137 137 ASP ASP D . n 
D 2 161 TYR 161 138 138 TYR TYR D . n 
D 2 162 LEU 162 139 139 LEU LEU D . n 
D 2 163 GLU 163 140 140 GLU GLU D . n 
D 2 164 LEU 164 141 141 LEU LEU D . n 
D 2 165 HIS 165 142 142 HIS HIS D . n 
D 2 166 ILE 166 143 143 ILE ILE D . n 
D 2 167 HIS 167 144 144 HIS HIS D . n 
D 2 168 GLN 168 145 145 GLN GLN D . n 
D 2 169 GLY 169 146 146 GLY GLY D . n 
D 2 170 LYS 170 147 147 LYS LYS D . n 
D 2 171 ILE 171 148 148 ILE ILE D . n 
D 2 172 GLY 172 149 149 GLY GLY D . n 
D 2 173 VAL 173 150 150 VAL VAL D . n 
D 2 174 LYS 174 151 151 LYS LYS D . n 
D 2 175 PHE 175 152 152 PHE PHE D . n 
D 2 176 ASN 176 153 153 ASN ASN D . n 
D 2 177 VAL 177 154 154 VAL VAL D . n 
D 2 178 GLY 178 155 155 GLY GLY D . n 
D 2 179 THR 179 156 156 THR THR D . n 
D 2 180 ASP 180 157 157 ASP ASP D . n 
D 2 181 ASP 181 158 158 ASP ASP D . n 
D 2 182 ILE 182 159 159 ILE ILE D . n 
D 2 183 ALA 183 160 160 ALA ALA D . n 
D 2 184 ILE 184 161 161 ILE ILE D . n 
D 2 185 GLU 185 162 162 GLU GLU D . n 
D 2 186 GLU 186 163 163 GLU GLU D . n 
D 2 187 SER 187 164 164 SER SER D . n 
D 2 188 ASN 188 165 165 ASN ASN D . n 
D 2 189 ALA 189 166 166 ALA ALA D . n 
D 2 190 ILE 190 167 167 ILE ILE D . n 
D 2 191 ILE 191 168 168 ILE ILE D . n 
D 2 192 ASN 192 169 169 ASN ASN D . n 
D 2 193 ASP 193 170 170 ASP ASP D . n 
D 2 194 GLY 194 171 171 GLY GLY D . n 
D 2 195 LYS 195 172 172 LYS LYS D . n 
D 2 196 TYR 196 173 173 TYR TYR D . n 
D 2 197 HIS 197 174 174 HIS HIS D . n 
D 2 198 VAL 198 175 175 VAL VAL D . n 
D 2 199 VAL 199 176 176 VAL VAL D . n 
D 2 200 ARG 200 177 177 ARG ARG D . n 
D 2 201 PHE 201 178 178 PHE PHE D . n 
D 2 202 THR 202 179 179 THR THR D . n 
D 2 203 ARG 203 180 180 ARG ARG D . n 
D 2 204 SER 204 181 181 SER SER D . n 
D 2 205 GLY 205 182 182 GLY GLY D . n 
D 2 206 GLY 206 183 183 GLY GLY D . n 
D 2 207 ASN 207 184 184 ASN ASN D . n 
D 2 208 ALA 208 185 185 ALA ALA D . n 
D 2 209 THR 209 186 186 THR THR D . n 
D 2 210 LEU 210 187 187 LEU LEU D . n 
D 2 211 GLN 211 188 188 GLN GLN D . n 
D 2 212 VAL 212 189 189 VAL VAL D . n 
D 2 213 ASP 213 190 190 ASP ASP D . n 
D 2 214 SER 214 191 191 SER SER D . n 
D 2 215 TRP 215 192 192 TRP TRP D . n 
D 2 216 PRO 216 193 193 PRO PRO D . n 
D 2 217 VAL 217 194 194 VAL VAL D . n 
D 2 218 ILE 218 195 195 ILE ILE D . n 
D 2 219 GLU 219 196 196 GLU GLU D . n 
D 2 220 ARG 220 197 197 ARG ARG D . n 
D 2 221 TYR 221 198 198 TYR TYR D . n 
D 2 222 PRO 222 199 199 PRO PRO D . n 
D 2 223 ALA 223 200 200 ALA ALA D . n 
D 2 224 GLY 224 201 201 GLY GLY D . n 
D 2 225 ARG 225 232 232 ARG ARG D . n 
D 2 226 GLN 226 233 233 GLN GLN D . n 
D 2 227 LEU 227 234 234 LEU LEU D . n 
D 2 228 THR 228 235 235 THR THR D . n 
D 2 229 ILE 229 236 236 ILE ILE D . n 
D 2 230 PHE 230 237 237 PHE PHE D . n 
D 2 231 ASN 231 238 238 ASN ASN D . n 
D 2 232 SER 232 239 239 SER SER D . n 
D 2 233 GLN 233 240 240 GLN GLN D . n 
D 2 234 ALA 234 241 241 ALA ALA D . n 
D 2 235 THR 235 242 242 THR THR D . n 
D 2 236 ILE 236 243 243 ILE ILE D . n 
D 2 237 ILE 237 244 244 ILE ILE D . n 
D 2 238 ILE 238 245 245 ILE ILE D . n 
D 2 239 GLY 239 246 246 GLY GLY D . n 
D 2 240 GLY 240 247 247 GLY GLY D . n 
D 2 241 LYS 241 248 248 LYS LYS D . n 
D 2 242 GLU 242 249 249 GLU GLU D . n 
D 2 243 GLN 243 250 250 GLN GLN D . n 
D 2 244 GLY 244 251 251 GLY GLY D . n 
D 2 245 GLN 245 252 252 GLN GLN D . n 
D 2 246 PRO 246 253 253 PRO PRO D . n 
D 2 247 PHE 247 254 254 PHE PHE D . n 
D 2 248 GLN 248 255 255 GLN GLN D . n 
D 2 249 GLY 249 256 256 GLY GLY D . n 
D 2 250 GLN 250 257 257 GLN GLN D . n 
D 2 251 LEU 251 258 258 LEU LEU D . n 
D 2 252 SER 252 259 259 SER SER D . n 
D 2 253 GLY 253 260 260 GLY GLY D . n 
D 2 254 LEU 254 261 261 LEU LEU D . n 
D 2 255 TYR 255 262 262 TYR TYR D . n 
D 2 256 TYR 256 263 263 TYR TYR D . n 
D 2 257 ASN 257 264 264 ASN ASN D . n 
D 2 258 GLY 258 265 265 GLY GLY D . n 
D 2 259 LEU 259 266 266 LEU LEU D . n 
D 2 260 LYS 260 267 267 LYS LYS D . n 
D 2 261 VAL 261 268 268 VAL VAL D . n 
D 2 262 LEU 262 269 269 LEU LEU D . n 
D 2 263 ASN 263 270 270 ASN ASN D . n 
D 2 264 MET 264 271 271 MET MET D . n 
D 2 265 ALA 265 272 272 ALA ALA D . n 
D 2 266 ALA 266 273 273 ALA ALA D . n 
D 2 267 GLU 267 274 274 GLU GLU D . n 
D 2 268 ASN 268 275 275 ASN ASN D . n 
D 2 269 ASP 269 276 276 ASP ASP D . n 
D 2 270 ALA 270 277 277 ALA ALA D . n 
D 2 271 ASN 271 278 278 ASN ASN D . n 
D 2 272 ILE 272 279 279 ILE ILE D . n 
D 2 273 ALA 273 280 280 ALA ALA D . n 
D 2 274 ILE 274 281 281 ILE ILE D . n 
D 2 275 VAL 275 282 282 VAL VAL D . n 
D 2 276 GLY 276 283 283 GLY GLY D . n 
D 2 277 ASN 277 284 284 ASN ASN D . n 
D 2 278 VAL 278 285 285 VAL VAL D . n 
D 2 279 ARG 279 286 286 ARG ARG D . n 
D 2 280 LEU 280 287 287 LEU LEU D . n 
D 2 281 VAL 281 288 288 VAL VAL D . n 
D 2 282 GLY 282 289 289 GLY GLY D . n 
D 2 283 GLU 283 290 ?   ?   ?   D . n 
D 2 284 VAL 284 291 ?   ?   ?   D . n 
D 2 285 PRO 285 292 ?   ?   ?   D . n 
D 2 286 SER 286 293 ?   ?   ?   D . n 
D 2 287 SER 287 294 ?   ?   ?   D . n 
D 2 288 MET 288 295 ?   ?   ?   D . n 
D 2 289 THR 289 296 ?   ?   ?   D . n 
D 2 290 THR 290 297 ?   ?   ?   D . n 
D 2 291 GLU 291 298 ?   ?   ?   D . n 
D 2 292 SER 292 299 ?   ?   ?   D . n 
D 2 293 THR 293 300 ?   ?   ?   D . n 
D 2 294 ALA 294 301 ?   ?   ?   D . n 
D 2 295 THR 295 302 ?   ?   ?   D . n 
D 2 296 ALA 296 303 ?   ?   ?   D . n 
D 2 297 MET 297 304 ?   ?   ?   D . n 
D 2 298 GLN 298 305 ?   ?   ?   D . n 
D 2 299 SER 299 306 ?   ?   ?   D . n 
D 2 300 GLU 300 307 ?   ?   ?   D . n 
D 2 301 MET 301 308 ?   ?   ?   D . n 
D 2 302 SER 302 309 ?   ?   ?   D . n 
D 2 303 THR 303 310 ?   ?   ?   D . n 
D 2 304 SER 304 311 ?   ?   ?   D . n 
D 2 305 ILE 305 312 ?   ?   ?   D . n 
D 2 306 MET 306 313 ?   ?   ?   D . n 
D 2 307 GLU 307 314 ?   ?   ?   D . n 
D 2 308 THR 308 315 ?   ?   ?   D . n 
D 2 309 THR 309 316 ?   ?   ?   D . n 
D 2 310 THR 310 317 ?   ?   ?   D . n 
D 2 311 THR 311 318 ?   ?   ?   D . n 
D 2 312 LEU 312 319 ?   ?   ?   D . n 
D 2 313 ALA 313 320 ?   ?   ?   D . n 
D 2 314 THR 314 321 ?   ?   ?   D . n 
D 2 315 SER 315 322 ?   ?   ?   D . n 
D 2 316 THR 316 323 ?   ?   ?   D . n 
D 2 317 ALA 317 324 ?   ?   ?   D . n 
D 2 318 ARG 318 325 ?   ?   ?   D . n 
D 2 319 ARG 319 326 ?   ?   ?   D . n 
D 2 320 GLY 320 327 ?   ?   ?   D . n 
D 2 321 LYS 321 328 ?   ?   ?   D . n 
D 2 322 PRO 322 329 ?   ?   ?   D . n 
D 2 323 PRO 323 330 ?   ?   ?   D . n 
D 2 324 THR 324 331 ?   ?   ?   D . n 
D 2 325 LYS 325 332 ?   ?   ?   D . n 
D 2 326 GLU 326 333 ?   ?   ?   D . n 
D 2 327 PRO 327 334 ?   ?   ?   D . n 
D 2 328 ILE 328 335 ?   ?   ?   D . n 
D 2 329 SER 329 336 ?   ?   ?   D . n 
D 2 330 GLN 330 337 ?   ?   ?   D . n 
D 2 331 THR 331 338 ?   ?   ?   D . n 
D 2 332 THR 332 339 ?   ?   ?   D . n 
D 2 333 ASP 333 340 ?   ?   ?   D . n 
D 2 334 ASP 334 341 ?   ?   ?   D . n 
D 2 335 ILE 335 342 ?   ?   ?   D . n 
D 2 336 LEU 336 343 ?   ?   ?   D . n 
D 2 337 VAL 337 344 ?   ?   ?   D . n 
D 2 338 ALA 338 345 ?   ?   ?   D . n 
D 2 339 SER 339 346 ?   ?   ?   D . n 
D 2 340 ALA 340 347 ?   ?   ?   D . n 
D 2 341 GLU 341 348 ?   ?   ?   D . n 
D 2 342 CYS 342 349 ?   ?   ?   D . n 
D 2 343 PRO 343 350 ?   ?   ?   D . n 
D 2 344 SER 344 351 ?   ?   ?   D . n 
D 2 345 ASP 345 352 ?   ?   ?   D . n 
D 2 346 ASP 346 353 ?   ?   ?   D . n 
D 2 347 GLU 347 354 ?   ?   ?   D . n 
D 2 348 ASP 348 355 ?   ?   ?   D . n 
D 2 349 ILE 349 356 ?   ?   ?   D . n 
D 2 350 ASP 350 357 ?   ?   ?   D . n 
D 2 351 PRO 351 358 ?   ?   ?   D . n 
D 2 352 CYS 352 359 ?   ?   ?   D . n 
D 2 353 GLU 353 360 ?   ?   ?   D . n 
D 2 354 PRO 354 361 ?   ?   ?   D . n 
D 2 355 SER 355 362 ?   ?   ?   D . n 
D 2 356 SER 356 363 ?   ?   ?   D . n 
D 2 357 GLY 357 364 ?   ?   ?   D . n 
D 2 358 GLY 358 365 ?   ?   ?   D . n 
D 2 359 LEU 359 366 ?   ?   ?   D . n 
D 2 360 ALA 360 367 ?   ?   ?   D . n 
D 2 361 ASN 361 368 ?   ?   ?   D . n 
D 2 362 PRO 362 369 ?   ?   ?   D . n 
D 2 363 THR 363 370 ?   ?   ?   D . n 
D 2 364 ARG 364 371 ?   ?   ?   D . n 
D 2 365 VAL 365 372 ?   ?   ?   D . n 
D 2 366 GLY 366 373 ?   ?   ?   D . n 
D 2 367 GLY 367 374 ?   ?   ?   D . n 
D 2 368 ARG 368 375 ?   ?   ?   D . n 
D 2 369 GLU 369 376 ?   ?   ?   D . n 
D 2 370 PRO 370 377 ?   ?   ?   D . n 
D 2 371 TYR 371 378 ?   ?   ?   D . n 
D 2 372 PRO 372 379 ?   ?   ?   D . n 
D 2 373 GLY 373 380 ?   ?   ?   D . n 
D 2 374 SER 374 381 ?   ?   ?   D . n 
D 2 375 ALA 375 382 ?   ?   ?   D . n 
D 2 376 GLU 376 383 ?   ?   ?   D . n 
D 2 377 VAL 377 384 ?   ?   ?   D . n 
D 2 378 ILE 378 385 ?   ?   ?   D . n 
D 2 379 ARG 379 386 ?   ?   ?   D . n 
D 2 380 GLU 380 387 ?   ?   ?   D . n 
D 2 381 SER 381 388 ?   ?   ?   D . n 
D 2 382 SER 382 389 ?   ?   ?   D . n 
D 2 383 SER 383 390 ?   ?   ?   D . n 
D 2 384 THR 384 391 ?   ?   ?   D . n 
D 2 385 THR 385 392 ?   ?   ?   D . n 
D 2 386 GLY 386 393 ?   ?   ?   D . n 
D 2 387 MET 387 394 ?   ?   ?   D . n 
D 2 388 VAL 388 395 ?   ?   ?   D . n 
D 2 389 VAL 389 396 ?   ?   ?   D . n 
D 2 390 GLY 390 397 ?   ?   ?   D . n 
D 2 391 ILE 391 398 ?   ?   ?   D . n 
D 2 392 VAL 392 399 ?   ?   ?   D . n 
D 2 393 ALA 393 400 ?   ?   ?   D . n 
D 2 394 ALA 394 401 ?   ?   ?   D . n 
D 2 395 ALA 395 402 ?   ?   ?   D . n 
D 2 396 ALA 396 403 ?   ?   ?   D . n 
D 2 397 LEU 397 404 ?   ?   ?   D . n 
D 2 398 CYS 398 405 ?   ?   ?   D . n 
D 2 399 ILE 399 406 ?   ?   ?   D . n 
D 2 400 LEU 400 407 ?   ?   ?   D . n 
D 2 401 ILE 401 408 ?   ?   ?   D . n 
D 2 402 LEU 402 409 ?   ?   ?   D . n 
D 2 403 LEU 403 410 ?   ?   ?   D . n 
D 2 404 TYR 404 411 ?   ?   ?   D . n 
D 2 405 ALA 405 412 ?   ?   ?   D . n 
D 2 406 MET 406 413 ?   ?   ?   D . n 
D 2 407 TYR 407 414 ?   ?   ?   D . n 
D 2 408 LYS 408 415 ?   ?   ?   D . n 
D 2 409 TYR 409 416 ?   ?   ?   D . n 
D 2 410 ARG 410 417 ?   ?   ?   D . n 
D 2 411 ASN 411 418 ?   ?   ?   D . n 
D 2 412 ARG 412 419 ?   ?   ?   D . n 
D 2 413 ASP 413 420 ?   ?   ?   D . n 
D 2 414 GLU 414 421 ?   ?   ?   D . n 
D 2 415 GLY 415 422 ?   ?   ?   D . n 
D 2 416 SER 416 423 ?   ?   ?   D . n 
D 2 417 TYR 417 424 ?   ?   ?   D . n 
D 2 418 HIS 418 425 ?   ?   ?   D . n 
D 2 419 VAL 419 426 ?   ?   ?   D . n 
D 2 420 ASP 420 427 ?   ?   ?   D . n 
D 2 421 GLU 421 428 ?   ?   ?   D . n 
D 2 422 SER 422 429 ?   ?   ?   D . n 
D 2 423 ARG 423 430 ?   ?   ?   D . n 
D 2 424 ASN 424 431 ?   ?   ?   D . n 
D 2 425 TYR 425 432 ?   ?   ?   D . n 
D 2 426 ILE 426 433 ?   ?   ?   D . n 
D 2 427 SER 427 434 ?   ?   ?   D . n 
D 2 428 ASN 428 435 ?   ?   ?   D . n 
D 2 429 SER 429 436 ?   ?   ?   D . n 
D 2 430 ALA 430 437 ?   ?   ?   D . n 
D 2 431 GLN 431 438 ?   ?   ?   D . n 
D 2 432 SER 432 439 ?   ?   ?   D . n 
D 2 433 ASN 433 440 ?   ?   ?   D . n 
D 2 434 GLY 434 441 ?   ?   ?   D . n 
D 2 435 ALA 435 442 ?   ?   ?   D . n 
D 2 436 VAL 436 443 ?   ?   ?   D . n 
D 2 437 VAL 437 444 ?   ?   ?   D . n 
D 2 438 LYS 438 445 ?   ?   ?   D . n 
D 2 439 GLU 439 446 ?   ?   ?   D . n 
D 2 440 LYS 440 447 ?   ?   ?   D . n 
D 2 441 GLN 441 448 ?   ?   ?   D . n 
D 2 442 PRO 442 449 ?   ?   ?   D . n 
D 2 443 SER 443 450 ?   ?   ?   D . n 
D 2 444 SER 444 451 ?   ?   ?   D . n 
D 2 445 ALA 445 452 ?   ?   ?   D . n 
D 2 446 LYS 446 453 ?   ?   ?   D . n 
D 2 447 SER 447 454 ?   ?   ?   D . n 
D 2 448 ALA 448 455 ?   ?   ?   D . n 
D 2 449 ASN 449 456 ?   ?   ?   D . n 
D 2 450 LYS 450 457 ?   ?   ?   D . n 
D 2 451 ASN 451 458 ?   ?   ?   D . n 
D 2 452 LYS 452 459 ?   ?   ?   D . n 
D 2 453 LYS 453 460 ?   ?   ?   D . n 
D 2 454 ASN 454 461 ?   ?   ?   D . n 
D 2 455 LYS 455 462 ?   ?   ?   D . n 
D 2 456 ASP 456 463 ?   ?   ?   D . n 
D 2 457 LYS 457 464 ?   ?   ?   D . n 
D 2 458 GLU 458 465 ?   ?   ?   D . n 
D 2 459 TYR 459 466 ?   ?   ?   D . n 
D 2 460 TYR 460 467 ?   ?   ?   D . n 
D 2 461 VAL 461 468 ?   ?   ?   D . n 
D 2 462 SER 462 469 ?   ?   ?   D . n 
D 2 463 ASN 463 470 ?   ?   ?   D . n 
D 2 464 SER 464 471 ?   ?   ?   D . n 
D 2 465 LEU 465 472 ?   ?   ?   D . n 
D 2 466 GLU 466 473 ?   ?   ?   D . n 
D 2 467 VAL 467 474 ?   ?   ?   D . n 
D 2 468 LEU 468 475 ?   ?   ?   D . n 
D 2 469 PHE 469 476 ?   ?   ?   D . n 
D 2 470 GLN 470 477 ?   ?   ?   D . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 CA  ? ? CA  ? ? 'SUBJECT OF INVESTIGATION' ? 
2 NAG ? ? NAG ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 NAG 1 901 1017 NAG NAG A . 
F 3 NAG 1 902 1018 NAG NAG A . 
G 3 NAG 1 901 1017 NAG NAG B . 
H 3 NAG 1 902 1018 NAG NAG B . 
I 4 CA  1 501 1007 CA  CA  C . 
J 3 NAG 1 502 1008 NAG NAG C . 
K 4 CA  1 501 1007 CA  CA  D . 
L 3 NAG 1 502 1008 NAG NAG D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A ASN 59  ? CG  ? A ASN 101 CG  
2   1 Y 1 A ASN 59  ? OD1 ? A ASN 101 OD1 
3   1 Y 1 A ASN 59  ? ND2 ? A ASN 101 ND2 
4   1 Y 1 A GLU 392 ? CG  ? A GLU 417 CG  
5   1 Y 1 A GLU 392 ? CD  ? A GLU 417 CD  
6   1 Y 1 A GLU 392 ? OE1 ? A GLU 417 OE1 
7   1 Y 1 A GLU 392 ? OE2 ? A GLU 417 OE2 
8   1 Y 1 A ASP 393 ? CG  ? A ASP 418 CG  
9   1 Y 1 A ASP 393 ? OD1 ? A ASP 418 OD1 
10  1 Y 1 A ASP 393 ? OD2 ? A ASP 418 OD2 
11  1 Y 1 A GLU 396 ? CG  ? A GLU 421 CG  
12  1 Y 1 A GLU 396 ? CD  ? A GLU 421 CD  
13  1 Y 1 A GLU 396 ? OE1 ? A GLU 421 OE1 
14  1 Y 1 A GLU 396 ? OE2 ? A GLU 421 OE2 
15  1 Y 1 A GLU 398 ? CG  ? A GLU 423 CG  
16  1 Y 1 A GLU 398 ? CD  ? A GLU 423 CD  
17  1 Y 1 A GLU 398 ? OE1 ? A GLU 423 OE1 
18  1 Y 1 A GLU 398 ? OE2 ? A GLU 423 OE2 
19  1 Y 1 A GLU 422 ? CG  ? A GLU 447 CG  
20  1 Y 1 A GLU 422 ? CD  ? A GLU 447 CD  
21  1 Y 1 A GLU 422 ? OE1 ? A GLU 447 OE1 
22  1 Y 1 A GLU 422 ? OE2 ? A GLU 447 OE2 
23  1 Y 1 A LYS 424 ? CG  ? A LYS 449 CG  
24  1 Y 1 A LYS 424 ? CD  ? A LYS 449 CD  
25  1 Y 1 A LYS 424 ? CE  ? A LYS 449 CE  
26  1 Y 1 A LYS 424 ? NZ  ? A LYS 449 NZ  
27  1 Y 1 A ASP 442 ? CG  ? A ASP 467 CG  
28  1 Y 1 A ASP 442 ? OD1 ? A ASP 467 OD1 
29  1 Y 1 A ASP 442 ? OD2 ? A ASP 467 OD2 
30  1 Y 1 A GLU 490 ? CG  ? A GLU 515 CG  
31  1 Y 1 A GLU 490 ? CD  ? A GLU 515 CD  
32  1 Y 1 A GLU 490 ? OE1 ? A GLU 515 OE1 
33  1 Y 1 A GLU 490 ? OE2 ? A GLU 515 OE2 
34  1 Y 1 A GLU 494 ? CG  ? A GLU 519 CG  
35  1 Y 1 A GLU 494 ? CD  ? A GLU 519 CD  
36  1 Y 1 A GLU 494 ? OE1 ? A GLU 519 OE1 
37  1 Y 1 A GLU 494 ? OE2 ? A GLU 519 OE2 
38  1 Y 1 A LYS 525 ? CG  ? A LYS 550 CG  
39  1 Y 1 A LYS 525 ? CD  ? A LYS 550 CD  
40  1 Y 1 A LYS 525 ? CE  ? A LYS 550 CE  
41  1 Y 1 A LYS 525 ? NZ  ? A LYS 550 NZ  
42  1 Y 1 A GLN 549 ? CG  ? A GLN 574 CG  
43  1 Y 1 A GLN 549 ? CD  ? A GLN 574 CD  
44  1 Y 1 A GLN 549 ? OE1 ? A GLN 574 OE1 
45  1 Y 1 A GLN 549 ? NE2 ? A GLN 574 NE2 
46  1 Y 1 A ARG 564 ? CG  ? A ARG 589 CG  
47  1 Y 1 A ARG 564 ? CD  ? A ARG 589 CD  
48  1 Y 1 A ARG 564 ? NE  ? A ARG 589 NE  
49  1 Y 1 A ARG 564 ? CZ  ? A ARG 589 CZ  
50  1 Y 1 A ARG 564 ? NH1 ? A ARG 589 NH1 
51  1 Y 1 A ARG 564 ? NH2 ? A ARG 589 NH2 
52  1 Y 1 A ASN 574 ? CG  ? A ASN 599 CG  
53  1 Y 1 A ASN 574 ? OD1 ? A ASN 599 OD1 
54  1 Y 1 A ASN 574 ? ND2 ? A ASN 599 ND2 
55  1 Y 1 A LYS 586 ? CG  ? A LYS 611 CG  
56  1 Y 1 A LYS 586 ? CD  ? A LYS 611 CD  
57  1 Y 1 A LYS 586 ? CE  ? A LYS 611 CE  
58  1 Y 1 A LYS 586 ? NZ  ? A LYS 611 NZ  
59  1 Y 1 B ASN 59  ? CG  ? B ASN 101 CG  
60  1 Y 1 B ASN 59  ? OD1 ? B ASN 101 OD1 
61  1 Y 1 B ASN 59  ? ND2 ? B ASN 101 ND2 
62  1 Y 1 B GLU 392 ? CG  ? B GLU 417 CG  
63  1 Y 1 B GLU 392 ? CD  ? B GLU 417 CD  
64  1 Y 1 B GLU 392 ? OE1 ? B GLU 417 OE1 
65  1 Y 1 B GLU 392 ? OE2 ? B GLU 417 OE2 
66  1 Y 1 B ASP 393 ? CG  ? B ASP 418 CG  
67  1 Y 1 B ASP 393 ? OD1 ? B ASP 418 OD1 
68  1 Y 1 B ASP 393 ? OD2 ? B ASP 418 OD2 
69  1 Y 1 B GLU 396 ? CG  ? B GLU 421 CG  
70  1 Y 1 B GLU 396 ? CD  ? B GLU 421 CD  
71  1 Y 1 B GLU 396 ? OE1 ? B GLU 421 OE1 
72  1 Y 1 B GLU 396 ? OE2 ? B GLU 421 OE2 
73  1 Y 1 B GLU 398 ? CG  ? B GLU 423 CG  
74  1 Y 1 B GLU 398 ? CD  ? B GLU 423 CD  
75  1 Y 1 B GLU 398 ? OE1 ? B GLU 423 OE1 
76  1 Y 1 B GLU 398 ? OE2 ? B GLU 423 OE2 
77  1 Y 1 B TYR 420 ? CG  ? B TYR 445 CG  
78  1 Y 1 B TYR 420 ? CD1 ? B TYR 445 CD1 
79  1 Y 1 B TYR 420 ? CD2 ? B TYR 445 CD2 
80  1 Y 1 B TYR 420 ? CE1 ? B TYR 445 CE1 
81  1 Y 1 B TYR 420 ? CE2 ? B TYR 445 CE2 
82  1 Y 1 B TYR 420 ? CZ  ? B TYR 445 CZ  
83  1 Y 1 B TYR 420 ? OH  ? B TYR 445 OH  
84  1 Y 1 B GLU 422 ? CG  ? B GLU 447 CG  
85  1 Y 1 B GLU 422 ? CD  ? B GLU 447 CD  
86  1 Y 1 B GLU 422 ? OE1 ? B GLU 447 OE1 
87  1 Y 1 B GLU 422 ? OE2 ? B GLU 447 OE2 
88  1 Y 1 B LYS 424 ? CG  ? B LYS 449 CG  
89  1 Y 1 B LYS 424 ? CD  ? B LYS 449 CD  
90  1 Y 1 B LYS 424 ? CE  ? B LYS 449 CE  
91  1 Y 1 B LYS 424 ? NZ  ? B LYS 449 NZ  
92  1 Y 1 B ASP 442 ? CG  ? B ASP 467 CG  
93  1 Y 1 B ASP 442 ? OD1 ? B ASP 467 OD1 
94  1 Y 1 B ASP 442 ? OD2 ? B ASP 467 OD2 
95  1 Y 1 B GLU 490 ? CG  ? B GLU 515 CG  
96  1 Y 1 B GLU 490 ? CD  ? B GLU 515 CD  
97  1 Y 1 B GLU 490 ? OE1 ? B GLU 515 OE1 
98  1 Y 1 B GLU 490 ? OE2 ? B GLU 515 OE2 
99  1 Y 1 B GLU 494 ? CG  ? B GLU 519 CG  
100 1 Y 1 B GLU 494 ? CD  ? B GLU 519 CD  
101 1 Y 1 B GLU 494 ? OE1 ? B GLU 519 OE1 
102 1 Y 1 B GLU 494 ? OE2 ? B GLU 519 OE2 
103 1 Y 1 B LYS 525 ? CG  ? B LYS 550 CG  
104 1 Y 1 B LYS 525 ? CD  ? B LYS 550 CD  
105 1 Y 1 B LYS 525 ? CE  ? B LYS 550 CE  
106 1 Y 1 B LYS 525 ? NZ  ? B LYS 550 NZ  
107 1 Y 1 B GLN 549 ? CG  ? B GLN 574 CG  
108 1 Y 1 B GLN 549 ? CD  ? B GLN 574 CD  
109 1 Y 1 B GLN 549 ? OE1 ? B GLN 574 OE1 
110 1 Y 1 B GLN 549 ? NE2 ? B GLN 574 NE2 
111 1 Y 1 B GLU 567 ? CG  ? B GLU 592 CG  
112 1 Y 1 B GLU 567 ? CD  ? B GLU 592 CD  
113 1 Y 1 B GLU 567 ? OE1 ? B GLU 592 OE1 
114 1 Y 1 B GLU 567 ? OE2 ? B GLU 592 OE2 
115 1 Y 1 B ASN 574 ? CG  ? B ASN 599 CG  
116 1 Y 1 B ASN 574 ? OD1 ? B ASN 599 OD1 
117 1 Y 1 B ASN 574 ? ND2 ? B ASN 599 ND2 
118 1 Y 1 B LYS 586 ? CG  ? B LYS 611 CG  
119 1 Y 1 B LYS 586 ? CD  ? B LYS 611 CD  
120 1 Y 1 B LYS 586 ? CE  ? B LYS 611 CE  
121 1 Y 1 B LYS 586 ? NZ  ? B LYS 611 NZ  
122 1 Y 1 C ILE 167 ? CG1 ? C ILE 190 CG1 
123 1 Y 1 C ILE 167 ? CG2 ? C ILE 190 CG2 
124 1 Y 1 C ILE 167 ? CD1 ? C ILE 190 CD1 
# 
_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                     8G7Z 
_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                         8G7Z 
_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                   8G7Z 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 8G7Z 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.004 ? 11371 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.569 ? 15486 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 4.576 ? 1585  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.047 ? 1706  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.004 ? 2027  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     8G7Z 
_struct.title                        
'Cryo-EM structure of full length Neuroligin-2 from Mouse bound to two Neurexin-1 Beta conformation one' 
_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        8G7Z 
_struct_keywords.text            'Neuroligin-2, membrane protein, Neurexin-1 beta' 
_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 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 4 ? 
J N N 3 ? 
K N N 4 ? 
L 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 NLGN2_RAT    Q62888 Q62888-2 1 
;AQRGGGGPGGGAPGGPGLGLGSLGEERFPVVNTAYGRVRGVRRELNNEILGPVVQFLGVPYATPPLGARRFQPPEAPASW
PGVRNATTLPPACPQNLHGALPAIMLPVWFTDNLEAAATYVQNQSEDCLYLNLYVPTEDDIRDSGKKPVMLFLHGGSYME
GTGNMFDGSVLAAYGNVIVATLNYRLGVLGFLSTGDQAAKGNYGLLDQIQALRWLSENIAHFGGDPERITIFGSGAGASC
VNLLILSHHSEGLFQKAIAQSGTAISSWSVNYQPLKYTRLLAAKVGCDREDSTEAVECLRRKSSRELVDQDVQPARYHIA
FGPVVDGDVVPDDPEILMQQGEFLNYDMLIGVNQGEGLKFVEDSAESEDGVSASAFDFTVSNFVDNLYGYPEGKDVLRET
IKFMYTDWADRDNGEMRRKTLLALFTDHQWVAPAVATAKLHADYQSPVYFYTFYHHCQAEGRPEWADAAHGDELPYVFGV
PMVGATDLFPCNFSKNDVMLSAVVMTYWTNFAKTGDPNQPVPQDTKFIHTKPNRFEEVVWSKFNSKEKQYLHIGLKPRVR
DNYRANKVAFWLELVPHLHNLHTELFTTTTRLPPYATRWPPRTPGPGTSGTRRPPPPATLPPESDIDLGPRAYDRFPGDS
RDYSTELSVTVAVGASLLFLNILAFAALYYKRDRRQELRCRRLSPPGGSGSGVPGGGPLLPTAGRELPPEEELVSLQLKR
GGGVGADPAEALRPACPPDYTLALRRAPDDVPLLAPGALTLLPSGLGPPPPPPPPSLHPFGPFPPPPPTATSHNNTLPHP
HSTTRV
;
14 
2 UNP E0CZA5_MOUSE E0CZA5 ?        2 MYQRMLRCGADLGSPGGGSGGGAGGRLALIWIVPLTLSGLLGVAWGASSLGAHHIHHFHGSS 1  
3 UNP E0CZA5_MOUSE E0CZA5 ?        2 
;PIAIYRSPASLRGGHAGTTYIFSKGGGQITYKWPPNDRPSTRADRLAIGFSTVQKEAVLVRVDSSSGLGDYLELHIHQGK
IGVKFNVGTDDIAIEESNAIINDGKYHVVRFTRSGGNATLQVDSWPVIERYPAGRQLTIFNSQATIIIGGKEQGQPFQGQ
LSGLYYNGLKVLNMAAENDANIAIVGNVRLVGEVPSSMTTESTATAMQSEMSTSIMETTTTLATSTARRGKPPTKEPISQ
TTDDILVASAECPSDDEDIDPCEPSSGGLANPTRVGGREPYPGSAEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYR
NRDEGSYHVDESRNYISNSAQSNGAVVKEKQPSSAKSANKNKKNKDKEYYV
;
68 
# 
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 8G7Z A 56 ? 861 ? Q62888 14 ? 819 ? 14  836 
2 1 8G7Z B 56 ? 861 ? Q62888 14 ? 819 ? 14  836 
3 2 8G7Z C 1  ? 62  ? E0CZA5 1  ? 62  ? -22 39  
4 3 8G7Z C 91 ? 461 ? E0CZA5 68 ? 438 ? 68  468 
5 2 8G7Z D 1  ? 62  ? E0CZA5 1  ? 62  ? -22 39  
6 3 8G7Z D 91 ? 461 ? E0CZA5 68 ? 438 ? 68  468 
# 
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 8G7Z MET A 1   ? UNP Q62888 ?   ?   'initiating methionine' -41 1   
1 8G7Z ALA A 2   ? UNP Q62888 ?   ?   'expression tag'        -40 2   
1 8G7Z LEU A 3   ? UNP Q62888 ?   ?   'expression tag'        -39 3   
1 8G7Z PRO A 4   ? UNP Q62888 ?   ?   'expression tag'        -38 4   
1 8G7Z ARG A 5   ? UNP Q62888 ?   ?   'expression tag'        -37 5   
1 8G7Z CYS A 6   ? UNP Q62888 ?   ?   'expression tag'        -36 6   
1 8G7Z MET A 7   ? UNP Q62888 ?   ?   'expression tag'        -35 7   
1 8G7Z TRP A 8   ? UNP Q62888 ?   ?   'expression tag'        -34 8   
1 8G7Z PRO A 9   ? UNP Q62888 ?   ?   'expression tag'        -33 9   
1 8G7Z ASN A 10  ? UNP Q62888 ?   ?   'expression tag'        -32 10  
1 8G7Z TYR A 11  ? UNP Q62888 ?   ?   'expression tag'        -31 11  
1 8G7Z VAL A 12  ? UNP Q62888 ?   ?   'expression tag'        -30 12  
1 8G7Z TRP A 13  ? UNP Q62888 ?   ?   'expression tag'        -29 13  
1 8G7Z ARG A 14  ? UNP Q62888 ?   ?   'expression tag'        -28 14  
1 8G7Z ALA A 15  ? UNP Q62888 ?   ?   'expression tag'        -27 15  
1 8G7Z MET A 16  ? UNP Q62888 ?   ?   'expression tag'        -26 16  
1 8G7Z MET A 17  ? UNP Q62888 ?   ?   'expression tag'        -25 17  
1 8G7Z ALA A 18  ? UNP Q62888 ?   ?   'expression tag'        -24 18  
1 8G7Z CYS A 19  ? UNP Q62888 ?   ?   'expression tag'        -23 19  
1 8G7Z VAL A 20  ? UNP Q62888 ?   ?   'expression tag'        -22 20  
1 8G7Z VAL A 21  ? UNP Q62888 ?   ?   'expression tag'        -21 21  
1 8G7Z HIS A 22  ? UNP Q62888 ?   ?   'expression tag'        -20 22  
1 8G7Z ARG A 23  ? UNP Q62888 ?   ?   'expression tag'        -19 23  
1 8G7Z GLY A 24  ? UNP Q62888 ?   ?   'expression tag'        -18 24  
1 8G7Z SER A 25  ? UNP Q62888 ?   ?   'expression tag'        -17 25  
1 8G7Z GLY A 26  ? UNP Q62888 ?   ?   'expression tag'        -16 26  
1 8G7Z ALA A 27  ? UNP Q62888 ?   ?   'expression tag'        -15 27  
1 8G7Z PRO A 28  ? UNP Q62888 ?   ?   'expression tag'        -14 28  
1 8G7Z LEU A 29  ? UNP Q62888 ?   ?   'expression tag'        -13 29  
1 8G7Z THR A 30  ? UNP Q62888 ?   ?   'expression tag'        -12 30  
1 8G7Z LEU A 31  ? UNP Q62888 ?   ?   'expression tag'        -11 31  
1 8G7Z CYS A 32  ? UNP Q62888 ?   ?   'expression tag'        -10 32  
1 8G7Z LEU A 33  ? UNP Q62888 ?   ?   'expression tag'        -9  33  
1 8G7Z LEU A 34  ? UNP Q62888 ?   ?   'expression tag'        -8  34  
1 8G7Z GLY A 35  ? UNP Q62888 ?   ?   'expression tag'        -7  35  
1 8G7Z CYS A 36  ? UNP Q62888 ?   ?   'expression tag'        -6  36  
1 8G7Z LEU A 37  ? UNP Q62888 ?   ?   'expression tag'        -5  37  
1 8G7Z LEU A 38  ? UNP Q62888 ?   ?   'expression tag'        -4  38  
1 8G7Z GLN A 39  ? UNP Q62888 ?   ?   'expression tag'        -3  39  
1 8G7Z THR A 40  ? UNP Q62888 ?   ?   'expression tag'        -2  40  
1 8G7Z PHE A 41  ? UNP Q62888 ?   ?   'expression tag'        -1  41  
1 8G7Z HIS A 42  ? UNP Q62888 ?   ?   'expression tag'        0   42  
1 8G7Z VAL A 43  ? UNP Q62888 ?   ?   'expression tag'        1   43  
1 8G7Z LEU A 44  ? UNP Q62888 ?   ?   'expression tag'        2   44  
1 8G7Z SER A 45  ? UNP Q62888 ?   ?   'expression tag'        3   45  
1 8G7Z GLN A 46  ? UNP Q62888 ?   ?   'expression tag'        4   46  
1 8G7Z LYS A 47  ? UNP Q62888 ?   ?   'expression tag'        5   47  
1 8G7Z TYR A 48  ? UNP Q62888 ?   ?   'expression tag'        6   48  
1 8G7Z PRO A 49  ? UNP Q62888 ?   ?   'expression tag'        7   49  
1 8G7Z TYR A 50  ? UNP Q62888 ?   ?   'expression tag'        8   50  
1 8G7Z ASP A 51  ? UNP Q62888 ?   ?   'expression tag'        9   51  
1 8G7Z VAL A 52  ? UNP Q62888 ?   ?   'expression tag'        10  52  
1 8G7Z PRO A 53  ? UNP Q62888 ?   ?   'expression tag'        11  53  
1 8G7Z ASP A 54  ? UNP Q62888 ?   ?   'expression tag'        12  54  
1 8G7Z TYR A 55  ? UNP Q62888 ?   ?   'expression tag'        13  55  
1 8G7Z VAL A 235 ? UNP Q62888 ALA 193 conflict                210 56  
1 8G7Z SER A 862 ? UNP Q62888 ?   ?   'expression tag'        837 57  
1 8G7Z ASN A 863 ? UNP Q62888 ?   ?   'expression tag'        838 58  
1 8G7Z SER A 864 ? UNP Q62888 ?   ?   'expression tag'        839 59  
1 8G7Z LEU A 865 ? UNP Q62888 ?   ?   'expression tag'        840 60  
1 8G7Z GLU A 866 ? UNP Q62888 ?   ?   'expression tag'        841 61  
1 8G7Z VAL A 867 ? UNP Q62888 ?   ?   'expression tag'        842 62  
1 8G7Z LEU A 868 ? UNP Q62888 ?   ?   'expression tag'        843 63  
1 8G7Z PHE A 869 ? UNP Q62888 ?   ?   'expression tag'        844 64  
1 8G7Z GLN A 870 ? UNP Q62888 ?   ?   'expression tag'        845 65  
2 8G7Z MET B 1   ? UNP Q62888 ?   ?   'initiating methionine' -41 66  
2 8G7Z ALA B 2   ? UNP Q62888 ?   ?   'expression tag'        -40 67  
2 8G7Z LEU B 3   ? UNP Q62888 ?   ?   'expression tag'        -39 68  
2 8G7Z PRO B 4   ? UNP Q62888 ?   ?   'expression tag'        -38 69  
2 8G7Z ARG B 5   ? UNP Q62888 ?   ?   'expression tag'        -37 70  
2 8G7Z CYS B 6   ? UNP Q62888 ?   ?   'expression tag'        -36 71  
2 8G7Z MET B 7   ? UNP Q62888 ?   ?   'expression tag'        -35 72  
2 8G7Z TRP B 8   ? UNP Q62888 ?   ?   'expression tag'        -34 73  
2 8G7Z PRO B 9   ? UNP Q62888 ?   ?   'expression tag'        -33 74  
2 8G7Z ASN B 10  ? UNP Q62888 ?   ?   'expression tag'        -32 75  
2 8G7Z TYR B 11  ? UNP Q62888 ?   ?   'expression tag'        -31 76  
2 8G7Z VAL B 12  ? UNP Q62888 ?   ?   'expression tag'        -30 77  
2 8G7Z TRP B 13  ? UNP Q62888 ?   ?   'expression tag'        -29 78  
2 8G7Z ARG B 14  ? UNP Q62888 ?   ?   'expression tag'        -28 79  
2 8G7Z ALA B 15  ? UNP Q62888 ?   ?   'expression tag'        -27 80  
2 8G7Z MET B 16  ? UNP Q62888 ?   ?   'expression tag'        -26 81  
2 8G7Z MET B 17  ? UNP Q62888 ?   ?   'expression tag'        -25 82  
2 8G7Z ALA B 18  ? UNP Q62888 ?   ?   'expression tag'        -24 83  
2 8G7Z CYS B 19  ? UNP Q62888 ?   ?   'expression tag'        -23 84  
2 8G7Z VAL B 20  ? UNP Q62888 ?   ?   'expression tag'        -22 85  
2 8G7Z VAL B 21  ? UNP Q62888 ?   ?   'expression tag'        -21 86  
2 8G7Z HIS B 22  ? UNP Q62888 ?   ?   'expression tag'        -20 87  
2 8G7Z ARG B 23  ? UNP Q62888 ?   ?   'expression tag'        -19 88  
2 8G7Z GLY B 24  ? UNP Q62888 ?   ?   'expression tag'        -18 89  
2 8G7Z SER B 25  ? UNP Q62888 ?   ?   'expression tag'        -17 90  
2 8G7Z GLY B 26  ? UNP Q62888 ?   ?   'expression tag'        -16 91  
2 8G7Z ALA B 27  ? UNP Q62888 ?   ?   'expression tag'        -15 92  
2 8G7Z PRO B 28  ? UNP Q62888 ?   ?   'expression tag'        -14 93  
2 8G7Z LEU B 29  ? UNP Q62888 ?   ?   'expression tag'        -13 94  
2 8G7Z THR B 30  ? UNP Q62888 ?   ?   'expression tag'        -12 95  
2 8G7Z LEU B 31  ? UNP Q62888 ?   ?   'expression tag'        -11 96  
2 8G7Z CYS B 32  ? UNP Q62888 ?   ?   'expression tag'        -10 97  
2 8G7Z LEU B 33  ? UNP Q62888 ?   ?   'expression tag'        -9  98  
2 8G7Z LEU B 34  ? UNP Q62888 ?   ?   'expression tag'        -8  99  
2 8G7Z GLY B 35  ? UNP Q62888 ?   ?   'expression tag'        -7  100 
2 8G7Z CYS B 36  ? UNP Q62888 ?   ?   'expression tag'        -6  101 
2 8G7Z LEU B 37  ? UNP Q62888 ?   ?   'expression tag'        -5  102 
2 8G7Z LEU B 38  ? UNP Q62888 ?   ?   'expression tag'        -4  103 
2 8G7Z GLN B 39  ? UNP Q62888 ?   ?   'expression tag'        -3  104 
2 8G7Z THR B 40  ? UNP Q62888 ?   ?   'expression tag'        -2  105 
2 8G7Z PHE B 41  ? UNP Q62888 ?   ?   'expression tag'        -1  106 
2 8G7Z HIS B 42  ? UNP Q62888 ?   ?   'expression tag'        0   107 
2 8G7Z VAL B 43  ? UNP Q62888 ?   ?   'expression tag'        1   108 
2 8G7Z LEU B 44  ? UNP Q62888 ?   ?   'expression tag'        2   109 
2 8G7Z SER B 45  ? UNP Q62888 ?   ?   'expression tag'        3   110 
2 8G7Z GLN B 46  ? UNP Q62888 ?   ?   'expression tag'        4   111 
2 8G7Z LYS B 47  ? UNP Q62888 ?   ?   'expression tag'        5   112 
2 8G7Z TYR B 48  ? UNP Q62888 ?   ?   'expression tag'        6   113 
2 8G7Z PRO B 49  ? UNP Q62888 ?   ?   'expression tag'        7   114 
2 8G7Z TYR B 50  ? UNP Q62888 ?   ?   'expression tag'        8   115 
2 8G7Z ASP B 51  ? UNP Q62888 ?   ?   'expression tag'        9   116 
2 8G7Z VAL B 52  ? UNP Q62888 ?   ?   'expression tag'        10  117 
2 8G7Z PRO B 53  ? UNP Q62888 ?   ?   'expression tag'        11  118 
2 8G7Z ASP B 54  ? UNP Q62888 ?   ?   'expression tag'        12  119 
2 8G7Z TYR B 55  ? UNP Q62888 ?   ?   'expression tag'        13  120 
2 8G7Z VAL B 235 ? UNP Q62888 ALA 193 conflict                210 121 
2 8G7Z SER B 862 ? UNP Q62888 ?   ?   'expression tag'        837 122 
2 8G7Z ASN B 863 ? UNP Q62888 ?   ?   'expression tag'        838 123 
2 8G7Z SER B 864 ? UNP Q62888 ?   ?   'expression tag'        839 124 
2 8G7Z LEU B 865 ? UNP Q62888 ?   ?   'expression tag'        840 125 
2 8G7Z GLU B 866 ? UNP Q62888 ?   ?   'expression tag'        841 126 
2 8G7Z VAL B 867 ? UNP Q62888 ?   ?   'expression tag'        842 127 
2 8G7Z LEU B 868 ? UNP Q62888 ?   ?   'expression tag'        843 128 
2 8G7Z PHE B 869 ? UNP Q62888 ?   ?   'expression tag'        844 129 
2 8G7Z GLN B 870 ? UNP Q62888 ?   ?   'expression tag'        845 130 
3 8G7Z GLY C 38  ? UNP E0CZA5 SER 38  conflict                15  131 
3 8G7Z LYS C 63  ? UNP E0CZA5 ?   ?   insertion               40  132 
3 8G7Z GLU C 64  ? UNP E0CZA5 ?   ?   insertion               41  133 
3 8G7Z PHE C 65  ? UNP E0CZA5 ?   ?   insertion               42  134 
3 8G7Z GLU C 66  ? UNP E0CZA5 ?   ?   insertion               43  135 
3 8G7Z GLN C 67  ? UNP E0CZA5 ?   ?   insertion               44  136 
3 8G7Z LYS C 68  ? UNP E0CZA5 ?   ?   insertion               45  137 
3 8G7Z LEU C 69  ? UNP E0CZA5 ?   ?   insertion               46  138 
3 8G7Z ILE C 70  ? UNP E0CZA5 ?   ?   insertion               47  139 
3 8G7Z SER C 71  ? UNP E0CZA5 ?   ?   insertion               48  140 
3 8G7Z GLU C 72  ? UNP E0CZA5 ?   ?   insertion               49  141 
3 8G7Z GLU C 73  ? UNP E0CZA5 ?   ?   insertion               50  142 
3 8G7Z ASP C 74  ? UNP E0CZA5 ?   ?   insertion               51  143 
3 8G7Z LEU C 75  ? UNP E0CZA5 ?   ?   insertion               52  144 
3 8G7Z GLY C 76  ? UNP E0CZA5 ?   ?   insertion               53  145 
3 8G7Z PHE C 77  ? UNP E0CZA5 ?   ?   insertion               54  146 
3 8G7Z GLU C 78  ? UNP E0CZA5 ?   ?   insertion               55  147 
3 8G7Z ILE C 79  ? UNP E0CZA5 ?   ?   insertion               56  148 
3 8G7Z ASP C 80  ? UNP E0CZA5 ?   ?   insertion               57  149 
3 8G7Z LYS C 81  ? UNP E0CZA5 ?   ?   insertion               58  150 
3 8G7Z VAL C 82  ? UNP E0CZA5 ?   ?   insertion               59  151 
3 8G7Z TRP C 83  ? UNP E0CZA5 ?   ?   insertion               60  152 
3 8G7Z HIS C 84  ? UNP E0CZA5 ?   ?   insertion               61  153 
3 8G7Z ASP C 85  ? UNP E0CZA5 ?   ?   insertion               62  154 
3 8G7Z PHE C 86  ? UNP E0CZA5 ?   ?   insertion               63  155 
3 8G7Z PRO C 87  ? UNP E0CZA5 ?   ?   insertion               64  156 
3 8G7Z ALA C 88  ? UNP E0CZA5 ?   ?   insertion               65  157 
3 8G7Z THR C 89  ? UNP E0CZA5 ?   ?   insertion               66  158 
3 8G7Z SER C 90  ? UNP E0CZA5 ?   ?   insertion               67  159 
4 8G7Z SER C 462 ? UNP E0CZA5 ?   ?   'expression tag'        469 160 
4 8G7Z ASN C 463 ? UNP E0CZA5 ?   ?   'expression tag'        470 161 
4 8G7Z SER C 464 ? UNP E0CZA5 ?   ?   'expression tag'        471 162 
4 8G7Z LEU C 465 ? UNP E0CZA5 ?   ?   'expression tag'        472 163 
4 8G7Z GLU C 466 ? UNP E0CZA5 ?   ?   'expression tag'        473 164 
4 8G7Z VAL C 467 ? UNP E0CZA5 ?   ?   'expression tag'        474 165 
4 8G7Z LEU C 468 ? UNP E0CZA5 ?   ?   'expression tag'        475 166 
4 8G7Z PHE C 469 ? UNP E0CZA5 ?   ?   'expression tag'        476 167 
4 8G7Z GLN C 470 ? UNP E0CZA5 ?   ?   'expression tag'        477 168 
5 8G7Z GLY D 38  ? UNP E0CZA5 SER 38  conflict                15  169 
5 8G7Z LYS D 63  ? UNP E0CZA5 ?   ?   insertion               40  170 
5 8G7Z GLU D 64  ? UNP E0CZA5 ?   ?   insertion               41  171 
5 8G7Z PHE D 65  ? UNP E0CZA5 ?   ?   insertion               42  172 
5 8G7Z GLU D 66  ? UNP E0CZA5 ?   ?   insertion               43  173 
5 8G7Z GLN D 67  ? UNP E0CZA5 ?   ?   insertion               44  174 
5 8G7Z LYS D 68  ? UNP E0CZA5 ?   ?   insertion               45  175 
5 8G7Z LEU D 69  ? UNP E0CZA5 ?   ?   insertion               46  176 
5 8G7Z ILE D 70  ? UNP E0CZA5 ?   ?   insertion               47  177 
5 8G7Z SER D 71  ? UNP E0CZA5 ?   ?   insertion               48  178 
5 8G7Z GLU D 72  ? UNP E0CZA5 ?   ?   insertion               49  179 
5 8G7Z GLU D 73  ? UNP E0CZA5 ?   ?   insertion               50  180 
5 8G7Z ASP D 74  ? UNP E0CZA5 ?   ?   insertion               51  181 
5 8G7Z LEU D 75  ? UNP E0CZA5 ?   ?   insertion               52  182 
5 8G7Z GLY D 76  ? UNP E0CZA5 ?   ?   insertion               53  183 
5 8G7Z PHE D 77  ? UNP E0CZA5 ?   ?   insertion               54  184 
5 8G7Z GLU D 78  ? UNP E0CZA5 ?   ?   insertion               55  185 
5 8G7Z ILE D 79  ? UNP E0CZA5 ?   ?   insertion               56  186 
5 8G7Z ASP D 80  ? UNP E0CZA5 ?   ?   insertion               57  187 
5 8G7Z LYS D 81  ? UNP E0CZA5 ?   ?   insertion               58  188 
5 8G7Z VAL D 82  ? UNP E0CZA5 ?   ?   insertion               59  189 
5 8G7Z TRP D 83  ? UNP E0CZA5 ?   ?   insertion               60  190 
5 8G7Z HIS D 84  ? UNP E0CZA5 ?   ?   insertion               61  191 
5 8G7Z ASP D 85  ? UNP E0CZA5 ?   ?   insertion               62  192 
5 8G7Z PHE D 86  ? UNP E0CZA5 ?   ?   insertion               63  193 
5 8G7Z PRO D 87  ? UNP E0CZA5 ?   ?   insertion               64  194 
5 8G7Z ALA D 88  ? UNP E0CZA5 ?   ?   insertion               65  195 
5 8G7Z THR D 89  ? UNP E0CZA5 ?   ?   insertion               66  196 
5 8G7Z SER D 90  ? UNP E0CZA5 ?   ?   insertion               67  197 
6 8G7Z SER D 462 ? UNP E0CZA5 ?   ?   'expression tag'        469 198 
6 8G7Z ASN D 463 ? UNP E0CZA5 ?   ?   'expression tag'        470 199 
6 8G7Z SER D 464 ? UNP E0CZA5 ?   ?   'expression tag'        471 200 
6 8G7Z LEU D 465 ? UNP E0CZA5 ?   ?   'expression tag'        472 201 
6 8G7Z GLU D 466 ? UNP E0CZA5 ?   ?   'expression tag'        473 202 
6 8G7Z VAL D 467 ? UNP E0CZA5 ?   ?   'expression tag'        474 203 
6 8G7Z LEU D 468 ? UNP E0CZA5 ?   ?   'expression tag'        475 204 
6 8G7Z PHE D 469 ? UNP E0CZA5 ?   ?   'expression tag'        476 205 
6 8G7Z GLN D 470 ? UNP E0CZA5 ?   ?   'expression tag'        477 206 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_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 
# 
_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                ? 
# 
_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 PRO A 162 ? ASN A 168 ? PRO A 120 ASN A 126 1 ? 7  
HELX_P HELX_P2  AA2 ASN A 168 ? VAL A 176 ? ASN A 126 VAL A 134 1 ? 9  
HELX_P HELX_P3  AA3 THR A 217 ? PHE A 221 ? THR A 192 PHE A 196 5 ? 5  
HELX_P HELX_P4  AA4 SER A 224 ? ASN A 231 ? SER A 199 ASN A 206 1 ? 8  
HELX_P HELX_P5  AA5 GLY A 242 ? LEU A 247 ? GLY A 217 LEU A 222 1 ? 6  
HELX_P HELX_P6  AA6 ASN A 257 ? ILE A 274 ? ASN A 232 ILE A 249 1 ? 18 
HELX_P HELX_P7  AA7 ALA A 275 ? PHE A 277 ? ALA A 250 PHE A 252 5 ? 3  
HELX_P HELX_P8  AA8 GLY A 290 ? ILE A 300 ? GLY A 265 ILE A 275 1 ? 11 
HELX_P HELX_P9  AA9 GLN A 328 ? GLY A 341 ? GLN A 303 GLY A 316 1 ? 14 
HELX_P HELX_P10 AB1 ASP A 346 ? ARG A 356 ? ASP A 321 ARG A 331 1 ? 11 
HELX_P HELX_P11 AB2 SER A 358 ? ASP A 364 ? SER A 333 ASP A 339 1 ? 7  
HELX_P HELX_P12 AB3 ASP A 388 ? MET A 393 ? ASP A 363 MET A 368 1 ? 6  
HELX_P HELX_P13 AB4 GLU A 411 ? PHE A 415 ? GLU A 386 PHE A 390 5 ? 5  
HELX_P HELX_P14 AB5 SER A 427 ? TYR A 443 ? SER A 402 TYR A 418 1 ? 17 
HELX_P HELX_P15 AB6 ASP A 450 ? TYR A 460 ? ASP A 425 TYR A 435 1 ? 11 
HELX_P HELX_P16 AB7 ASP A 462 ? ARG A 466 ? ASP A 437 ARG A 441 5 ? 5  
HELX_P HELX_P17 AB8 GLY A 469 ? TRP A 485 ? GLY A 444 TRP A 460 1 ? 17 
HELX_P HELX_P18 AB9 TRP A 485 ? ASP A 498 ? TRP A 460 ASP A 473 1 ? 14 
HELX_P HELX_P19 AC1 GLU A 528 ? PHE A 533 ? GLU A 503 PHE A 508 1 ? 6  
HELX_P HELX_P20 AC2 GLY A 534 ? VAL A 538 ? GLY A 509 VAL A 513 5 ? 5  
HELX_P HELX_P21 AC3 SER A 549 ? GLY A 570 ? SER A 524 GLY A 545 1 ? 22 
HELX_P HELX_P22 AC4 ARG A 619 ? LEU A 629 ? ARG A 594 LEU A 604 1 ? 11 
HELX_P HELX_P23 AC5 VAL A 630 ? LEU A 633 ? VAL A 605 LEU A 608 5 ? 4  
HELX_P HELX_P24 AC6 PRO B 162 ? ASN B 168 ? PRO B 120 ASN B 126 1 ? 7  
HELX_P HELX_P25 AC7 ASN B 168 ? VAL B 176 ? ASN B 126 VAL B 134 1 ? 9  
HELX_P HELX_P26 AC8 THR B 217 ? PHE B 221 ? THR B 192 PHE B 196 5 ? 5  
HELX_P HELX_P27 AC9 SER B 224 ? ASN B 231 ? SER B 199 ASN B 206 1 ? 8  
HELX_P HELX_P28 AD1 GLY B 242 ? LEU B 247 ? GLY B 217 LEU B 222 1 ? 6  
HELX_P HELX_P29 AD2 ASN B 257 ? ILE B 274 ? ASN B 232 ILE B 249 1 ? 18 
HELX_P HELX_P30 AD3 ALA B 275 ? PHE B 277 ? ALA B 250 PHE B 252 5 ? 3  
HELX_P HELX_P31 AD4 GLY B 290 ? LEU B 301 ? GLY B 265 LEU B 276 1 ? 12 
HELX_P HELX_P32 AD5 GLN B 328 ? GLY B 341 ? GLN B 303 GLY B 316 1 ? 14 
HELX_P HELX_P33 AD6 ASP B 346 ? LYS B 357 ? ASP B 321 LYS B 332 1 ? 12 
HELX_P HELX_P34 AD7 ARG B 360 ? GLN B 365 ? ARG B 335 GLN B 340 1 ? 6  
HELX_P HELX_P35 AD8 ASP B 388 ? GLN B 395 ? ASP B 363 GLN B 370 1 ? 8  
HELX_P HELX_P36 AD9 SER B 427 ? TYR B 443 ? SER B 402 TYR B 418 1 ? 17 
HELX_P HELX_P37 AE1 LYS B 449 ? TYR B 460 ? LYS B 424 TYR B 435 1 ? 12 
HELX_P HELX_P38 AE2 ASP B 462 ? ARG B 466 ? ASP B 437 ARG B 441 5 ? 5  
HELX_P HELX_P39 AE3 GLY B 469 ? TRP B 485 ? GLY B 444 TRP B 460 1 ? 17 
HELX_P HELX_P40 AE4 TRP B 485 ? ASP B 498 ? TRP B 460 ASP B 473 1 ? 14 
HELX_P HELX_P41 AE5 GLU B 528 ? PHE B 533 ? GLU B 503 PHE B 508 1 ? 6  
HELX_P HELX_P42 AE6 SER B 549 ? GLY B 570 ? SER B 524 GLY B 545 1 ? 22 
HELX_P HELX_P43 AE7 ARG B 619 ? LEU B 629 ? ARG B 594 LEU B 604 1 ? 11 
HELX_P HELX_P44 AE8 VAL B 630 ? LEU B 633 ? VAL B 605 LEU B 608 5 ? 4  
HELX_P HELX_P45 AE9 LYS C 260 ? ALA C 266 ? LYS C 267 ALA C 273 1 ? 7  
HELX_P HELX_P46 AF1 VAL D 261 ? GLU D 267 ? VAL D 268 GLU D 274 1 ? 7  
# 
_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 148 SG  ? ? ? 1_555 A CYS 183 SG ? ? A CYS 106 A CYS 141 1_555 ? ? ? ? ? ? ? 2.029 ? ?               
disulf2 disulf ?   ? A CYS 342 SG  ? ? ? 1_555 A CYS 353 SG ? ? A CYS 317 A CYS 328 1_555 ? ? ? ? ? ? ? 2.030 ? ?               
disulf3 disulf ?   ? B CYS 148 SG  ? ? ? 1_555 B CYS 183 SG ? ? B CYS 106 B CYS 141 1_555 ? ? ? ? ? ? ? 2.029 ? ?               
disulf4 disulf ?   ? B CYS 342 SG  ? ? ? 1_555 B CYS 353 SG ? ? B CYS 317 B CYS 328 1_555 ? ? ? ? ? ? ? 2.031 ? ?               
covale1 covale one ? A ASN 140 ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 98  A NAG 901 1_555 ? ? ? ? ? ? ? 1.427 ? N-Glycosylation 
covale2 covale one ? A ASN 547 ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 522 A NAG 902 1_555 ? ? ? ? ? ? ? 1.445 ? N-Glycosylation 
covale3 covale one ? B ASN 140 ND2 ? ? ? 1_555 G NAG .   C1 ? ? B ASN 98  B NAG 901 1_555 ? ? ? ? ? ? ? 1.435 ? N-Glycosylation 
covale4 covale one ? B ASN 547 ND2 ? ? ? 1_555 H NAG .   C1 ? ? B ASN 522 B NAG 902 1_555 ? ? ? ? ? ? ? 1.441 ? N-Glycosylation 
covale5 covale one ? C ASN 207 ND2 ? ? ? 1_555 J NAG .   C1 ? ? C ASN 184 C NAG 502 1_555 ? ? ? ? ? ? ? 1.439 ? N-Glycosylation 
covale6 covale one ? D ASN 207 ND2 ? ? ? 1_555 L NAG .   C1 ? ? D ASN 184 D NAG 502 1_555 ? ? ? ? ? ? ? 1.443 ? N-Glycosylation 
metalc1 metalc ?   ? C ASP 160 OD1 ? ? ? 1_555 I CA  .   CA ? ? C ASP 137 C CA  501 1_555 ? ? ? ? ? ? ? 2.947 ? ?               
metalc2 metalc ?   ? C ASP 160 OD2 ? ? ? 1_555 I CA  .   CA ? ? C ASP 137 C CA  501 1_555 ? ? ? ? ? ? ? 2.380 ? ?               
metalc3 metalc ?   ? C VAL 177 O   ? ? ? 1_555 I CA  .   CA ? ? C VAL 154 C CA  501 1_555 ? ? ? ? ? ? ? 2.672 ? ?               
metalc4 metalc ?   ? C ILE 229 O   ? ? ? 1_555 I CA  .   CA ? ? C ILE 236 C CA  501 1_555 ? ? ? ? ? ? ? 2.946 ? ?               
metalc5 metalc ?   ? C ASN 231 OD1 ? ? ? 1_555 I CA  .   CA ? ? C ASN 238 C CA  501 1_555 ? ? ? ? ? ? ? 2.266 ? ?               
metalc6 metalc ?   ? D ASP 160 OD2 ? ? ? 1_555 K CA  .   CA ? ? D ASP 137 D CA  501 1_555 ? ? ? ? ? ? ? 2.906 ? ?               
metalc7 metalc ?   ? D VAL 177 O   ? ? ? 1_555 K CA  .   CA ? ? D VAL 154 D CA  501 1_555 ? ? ? ? ? ? ? 2.578 ? ?               
metalc8 metalc ?   ? D ILE 229 O   ? ? ? 1_555 K CA  .   CA ? ? D ILE 236 D CA  501 1_555 ? ? ? ? ? ? ? 2.825 ? ?               
metalc9 metalc ?   ? D ASN 231 OD1 ? ? ? 1_555 K CA  .   CA ? ? D ASN 238 D CA  501 1_555 ? ? ? ? ? ? ? 2.333 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? C ASP 160 ? C ASP 137 ? 1_555 CA ? I CA . ? C CA 501 ? 1_555 OD2 ? C ASP 160 ? C ASP 137 ? 1_555 46.9  ? 
2  OD1 ? C ASP 160 ? C ASP 137 ? 1_555 CA ? I CA . ? C CA 501 ? 1_555 O   ? C VAL 177 ? C VAL 154 ? 1_555 62.2  ? 
3  OD2 ? C ASP 160 ? C ASP 137 ? 1_555 CA ? I CA . ? C CA 501 ? 1_555 O   ? C VAL 177 ? C VAL 154 ? 1_555 109.1 ? 
4  OD1 ? C ASP 160 ? C ASP 137 ? 1_555 CA ? I CA . ? C CA 501 ? 1_555 O   ? C ILE 229 ? C ILE 236 ? 1_555 94.9  ? 
5  OD2 ? C ASP 160 ? C ASP 137 ? 1_555 CA ? I CA . ? C CA 501 ? 1_555 O   ? C ILE 229 ? C ILE 236 ? 1_555 98.2  ? 
6  O   ? C VAL 177 ? C VAL 154 ? 1_555 CA ? I CA . ? C CA 501 ? 1_555 O   ? C ILE 229 ? C ILE 236 ? 1_555 87.0  ? 
7  OD1 ? C ASP 160 ? C ASP 137 ? 1_555 CA ? I CA . ? C CA 501 ? 1_555 OD1 ? C ASN 231 ? C ASN 238 ? 1_555 121.4 ? 
8  OD2 ? C ASP 160 ? C ASP 137 ? 1_555 CA ? I CA . ? C CA 501 ? 1_555 OD1 ? C ASN 231 ? C ASN 238 ? 1_555 79.7  ? 
9  O   ? C VAL 177 ? C VAL 154 ? 1_555 CA ? I CA . ? C CA 501 ? 1_555 OD1 ? C ASN 231 ? C ASN 238 ? 1_555 153.4 ? 
10 O   ? C ILE 229 ? C ILE 236 ? 1_555 CA ? I CA . ? C CA 501 ? 1_555 OD1 ? C ASN 231 ? C ASN 238 ? 1_555 66.7  ? 
11 OD2 ? D ASP 160 ? D ASP 137 ? 1_555 CA ? K CA . ? D CA 501 ? 1_555 O   ? D VAL 177 ? D VAL 154 ? 1_555 98.2  ? 
12 OD2 ? D ASP 160 ? D ASP 137 ? 1_555 CA ? K CA . ? D CA 501 ? 1_555 O   ? D ILE 229 ? D ILE 236 ? 1_555 75.9  ? 
13 O   ? D VAL 177 ? D VAL 154 ? 1_555 CA ? K CA . ? D CA 501 ? 1_555 O   ? D ILE 229 ? D ILE 236 ? 1_555 87.9  ? 
14 OD2 ? D ASP 160 ? D ASP 137 ? 1_555 CA ? K CA . ? D CA 501 ? 1_555 OD1 ? D ASN 231 ? D ASN 238 ? 1_555 66.0  ? 
15 O   ? D VAL 177 ? D VAL 154 ? 1_555 CA ? K CA . ? D CA 501 ? 1_555 OD1 ? D ASN 231 ? D ASN 238 ? 1_555 151.2 ? 
16 O   ? D ILE 229 ? D ILE 236 ? 1_555 CA ? K CA . ? D CA 501 ? 1_555 OD1 ? D ASN 231 ? D ASN 238 ? 1_555 65.4  ? 
# 
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 E .   ? ASN A 140 ? NAG A 901 ? 1_555 ASN A 98  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG F .   ? ASN A 547 ? NAG A 902 ? 1_555 ASN A 522 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG G .   ? ASN B 140 ? NAG B 901 ? 1_555 ASN B 98  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG H .   ? ASN B 547 ? NAG B 902 ? 1_555 ASN B 522 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  NAG J .   ? ASN C 207 ? NAG C 502 ? 1_555 ASN C 184 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6  NAG L .   ? ASN D 207 ? NAG D 502 ? 1_555 ASN D 184 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7  CYS A 148 ? CYS A 183 ? CYS A 106 ? 1_555 CYS A 141 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
8  CYS A 342 ? CYS A 353 ? CYS A 317 ? 1_555 CYS A 328 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
9  CYS B 148 ? CYS B 183 ? CYS B 106 ? 1_555 CYS B 141 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
10 CYS B 342 ? CYS B 353 ? CYS B 317 ? 1_555 CYS B 328 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3  ? 
AA2 ? 9  ? 
AA3 ? 3  ? 
AA4 ? 3  ? 
AA5 ? 10 ? 
AA6 ? 7  ? 
AA7 ? 7  ? 
AA8 ? 8  ? 
AA9 ? 7  ? 
# 
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      
AA2 1 2  ? anti-parallel 
AA2 2 3  ? anti-parallel 
AA2 3 4  ? parallel      
AA2 4 5  ? parallel      
AA2 5 6  ? parallel      
AA2 6 7  ? parallel      
AA2 7 8  ? parallel      
AA2 8 9  ? parallel      
AA3 1 2  ? anti-parallel 
AA3 2 3  ? parallel      
AA4 1 2  ? anti-parallel 
AA4 2 3  ? anti-parallel 
AA5 1 2  ? anti-parallel 
AA5 2 3  ? anti-parallel 
AA5 3 4  ? parallel      
AA5 4 5  ? parallel      
AA5 5 6  ? parallel      
AA5 6 7  ? parallel      
AA5 7 8  ? parallel      
AA5 8 9  ? parallel      
AA5 9 10 ? anti-parallel 
AA6 1 2  ? anti-parallel 
AA6 2 3  ? anti-parallel 
AA6 3 4  ? anti-parallel 
AA6 4 5  ? anti-parallel 
AA6 5 6  ? anti-parallel 
AA6 6 7  ? anti-parallel 
AA7 1 2  ? anti-parallel 
AA7 2 3  ? anti-parallel 
AA7 3 4  ? anti-parallel 
AA7 4 5  ? anti-parallel 
AA7 5 6  ? anti-parallel 
AA7 6 7  ? anti-parallel 
AA8 1 2  ? anti-parallel 
AA8 2 3  ? anti-parallel 
AA8 3 4  ? anti-parallel 
AA8 4 5  ? anti-parallel 
AA8 5 6  ? anti-parallel 
AA8 6 7  ? anti-parallel 
AA8 7 8  ? anti-parallel 
AA9 1 2  ? anti-parallel 
AA9 2 3  ? anti-parallel 
AA9 3 4  ? anti-parallel 
AA9 4 5  ? anti-parallel 
AA9 5 6  ? anti-parallel 
AA9 6 7  ? 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  VAL A 86  ? THR A 88  ? VAL A 44  THR A 46  
AA1 2  GLY A 91  ? ARG A 94  ? GLY A 49  ARG A 52  
AA1 3  ARG A 139 ? ASN A 140 ? ARG A 97  ASN A 98  
AA2 1  VAL A 108 ? PRO A 115 ? VAL A 66  PRO A 73  
AA2 2  TYR A 185 ? PRO A 191 ? TYR A 143 PRO A 149 
AA2 3  ILE A 233 ? LEU A 237 ? ILE A 208 LEU A 212 
AA2 4  LYS A 202 ? PHE A 207 ? LYS A 177 PHE A 182 
AA2 5  GLY A 279 ? SER A 289 ? GLY A 254 SER A 264 
AA2 6  LYS A 311 ? GLN A 315 ? LYS A 286 GLN A 290 
AA2 7  ASP A 402 ? ASN A 408 ? ASP A 377 ASN A 383 
AA2 8  VAL A 503 ? PHE A 508 ? VAL A 478 PHE A 483 
AA2 9  LEU A 606 ? ILE A 608 ? LEU A 581 ILE A 583 
AA3 1  VAL B 85  ? ASN B 87  ? VAL B 43  ASN B 45  
AA3 2  ARG B 92  ? ARG B 94  ? ARG B 50  ARG B 52  
AA3 3  VAL B 138 ? ASN B 140 ? VAL B 96  ASN B 98  
AA4 1  VAL B 108 ? GLN B 110 ? VAL B 66  GLN B 68  
AA4 2  TYR B 185 ? PRO B 191 ? TYR B 143 PRO B 149 
AA4 3  VAL B 114 ? PRO B 115 ? VAL B 72  PRO B 73  
AA5 1  VAL B 108 ? GLN B 110 ? VAL B 66  GLN B 68  
AA5 2  TYR B 185 ? PRO B 191 ? TYR B 143 PRO B 149 
AA5 3  ILE B 233 ? LEU B 237 ? ILE B 208 LEU B 212 
AA5 4  LYS B 202 ? PHE B 207 ? LYS B 177 PHE B 182 
AA5 5  GLY B 279 ? SER B 289 ? GLY B 254 SER B 264 
AA5 6  LYS B 311 ? GLN B 315 ? LYS B 286 GLN B 290 
AA5 7  ASP B 402 ? ASN B 408 ? ASP B 377 ASN B 383 
AA5 8  VAL B 503 ? PHE B 508 ? VAL B 478 PHE B 483 
AA5 9  TYR B 605 ? ILE B 608 ? TYR B 580 ILE B 583 
AA5 10 VAL B 614 ? ARG B 615 ? VAL B 589 ARG B 590 
AA6 1  ILE C 218 ? ARG C 220 ? ILE C 195 ARG C 197 
AA6 2  ASN C 207 ? VAL C 212 ? ASN C 184 VAL C 189 
AA6 3  HIS C 197 ? SER C 204 ? HIS C 174 SER C 181 
AA6 4  ALA C 133 ? SER C 141 ? ALA C 110 SER C 118 
AA6 5  GLN C 250 ? TYR C 256 ? GLN C 257 TYR C 263 
AA6 6  TYR C 110 ? ILE C 111 ? TYR C 87  ILE C 88  
AA6 7  ARG C 279 ? LEU C 280 ? ARG C 286 LEU C 287 
AA7 1  ASP C 181 ? GLU C 185 ? ASP C 158 GLU C 162 
AA7 2  LYS C 170 ? ASN C 176 ? LYS C 147 ASN C 153 
AA7 3  TYR C 161 ? HIS C 167 ? TYR C 138 HIS C 144 
AA7 4  ALA C 147 ? SER C 154 ? ALA C 124 SER C 131 
AA7 5  GLN C 233 ? ILE C 238 ? GLN C 240 ILE C 245 
AA7 6  GLY C 117 ? LYS C 122 ? GLY C 94  LYS C 99  
AA7 7  ILE C 272 ? GLY C 276 ? ILE C 279 GLY C 283 
AA8 1  ASP D 181 ? GLU D 185 ? ASP D 158 GLU D 162 
AA8 2  LYS D 170 ? ASN D 176 ? LYS D 147 ASN D 153 
AA8 3  TYR D 161 ? HIS D 167 ? TYR D 138 HIS D 144 
AA8 4  ALA D 147 ? SER D 154 ? ALA D 124 SER D 131 
AA8 5  GLN D 233 ? ILE D 238 ? GLN D 240 ILE D 245 
AA8 6  THR D 109 ? LYS D 122 ? THR D 86  LYS D 99  
AA8 7  GLN D 250 ? TYR D 256 ? GLN D 257 TYR D 263 
AA8 8  LEU D 259 ? LYS D 260 ? LEU D 266 LYS D 267 
AA9 1  ILE D 218 ? ARG D 220 ? ILE D 195 ARG D 197 
AA9 2  ASN D 207 ? VAL D 212 ? ASN D 184 VAL D 189 
AA9 3  HIS D 197 ? SER D 204 ? HIS D 174 SER D 181 
AA9 4  ARG D 135 ? SER D 141 ? ARG D 112 SER D 118 
AA9 5  GLN D 250 ? TYR D 256 ? GLN D 257 TYR D 263 
AA9 6  THR D 109 ? LYS D 122 ? THR D 86  LYS D 99  
AA9 7  ILE D 272 ? LEU D 280 ? ILE D 279 LEU D 287 
# 
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 THR A 88  ? N THR A 46  O GLY A 91  ? O GLY A 49  
AA1 2 3  N ARG A 92  ? N ARG A 50  O ARG A 139 ? O ARG A 97  
AA2 1 2  N VAL A 109 ? N VAL A 67  O VAL A 190 ? O VAL A 148 
AA2 2 3  N ASN A 187 ? N ASN A 145 O THR A 236 ? O THR A 211 
AA2 3 4  O ILE A 233 ? O ILE A 208 N PRO A 203 ? N PRO A 178 
AA2 4 5  N LEU A 206 ? N LEU A 181 O PHE A 287 ? O PHE A 262 
AA2 5 6  N ILE A 286 ? N ILE A 261 O ILE A 313 ? O ILE A 288 
AA2 6 7  N ALA A 312 ? N ALA A 287 O ASP A 402 ? O ASP A 377 
AA2 7 8  N VAL A 407 ? N VAL A 382 O PHE A 508 ? O PHE A 483 
AA2 8 9  N THR A 507 ? N THR A 482 O LEU A 606 ? O LEU A 581 
AA3 1 2  N VAL B 86  ? N VAL B 44  O VAL B 93  ? O VAL B 51  
AA3 2 3  N ARG B 92  ? N ARG B 50  O ARG B 139 ? O ARG B 97  
AA4 1 2  N VAL B 109 ? N VAL B 67  O VAL B 190 ? O VAL B 148 
AA4 2 3  O LEU B 186 ? O LEU B 144 N VAL B 114 ? N VAL B 72  
AA5 1 2  N VAL B 109 ? N VAL B 67  O VAL B 190 ? O VAL B 148 
AA5 2 3  N ASN B 187 ? N ASN B 145 O THR B 236 ? O THR B 211 
AA5 3 4  O ILE B 233 ? O ILE B 208 N PRO B 203 ? N PRO B 178 
AA5 4 5  N LEU B 206 ? N LEU B 181 O THR B 285 ? O THR B 260 
AA5 5 6  N ILE B 286 ? N ILE B 261 O ILE B 313 ? O ILE B 288 
AA5 6 7  N ALA B 312 ? N ALA B 287 O ASP B 402 ? O ASP B 377 
AA5 7 8  N VAL B 407 ? N VAL B 382 O PHE B 508 ? O PHE B 483 
AA5 8 9  N PHE B 505 ? N PHE B 480 O LEU B 606 ? O LEU B 581 
AA5 9 10 N TYR B 605 ? N TYR B 580 O ARG B 615 ? O ARG B 590 
AA6 1 2  O ILE C 218 ? O ILE C 195 N LEU C 210 ? N LEU C 187 
AA6 2 3  O GLN C 211 ? O GLN C 188 N ARG C 200 ? N ARG C 177 
AA6 3 4  O VAL C 199 ? O VAL C 176 N ILE C 138 ? N ILE C 115 
AA6 4 5  N GLY C 139 ? N GLY C 116 O SER C 252 ? O SER C 259 
AA6 5 6  O LEU C 251 ? O LEU C 258 N TYR C 110 ? N TYR C 87  
AA6 6 7  N ILE C 111 ? N ILE C 88  O ARG C 279 ? O ARG C 286 
AA7 1 2  O ILE C 182 ? O ILE C 159 N PHE C 175 ? N PHE C 152 
AA7 2 3  O GLY C 172 ? O GLY C 149 N HIS C 165 ? N HIS C 142 
AA7 3 4  O LEU C 162 ? O LEU C 139 N VAL C 152 ? N VAL C 129 
AA7 4 5  N ASP C 153 ? N ASP C 130 O ALA C 234 ? O ALA C 241 
AA7 5 6  O ILE C 238 ? O ILE C 245 N ILE C 119 ? N ILE C 96  
AA7 6 7  N GLN C 118 ? N GLN C 95  O VAL C 275 ? O VAL C 282 
AA8 1 2  O ILE D 184 ? O ILE D 161 N VAL D 173 ? N VAL D 150 
AA8 2 3  O GLY D 172 ? O GLY D 149 N HIS D 165 ? N HIS D 142 
AA8 3 4  O LEU D 164 ? O LEU D 141 N LEU D 149 ? N LEU D 126 
AA8 4 5  N ARG D 151 ? N ARG D 128 O ILE D 237 ? O ILE D 244 
AA8 5 6  O ILE D 238 ? O ILE D 245 N ILE D 119 ? N ILE D 96  
AA8 6 7  N TYR D 110 ? N TYR D 87  O LEU D 251 ? O LEU D 258 
AA8 7 8  N TYR D 256 ? N TYR D 263 O LEU D 259 ? O LEU D 266 
AA9 1 2  O ILE D 218 ? O ILE D 195 N LEU D 210 ? N LEU D 187 
AA9 2 3  O GLN D 211 ? O GLN D 188 N ARG D 200 ? N ARG D 177 
AA9 3 4  O VAL D 199 ? O VAL D 176 N ILE D 138 ? N ILE D 115 
AA9 4 5  N ALA D 137 ? N ALA D 114 O TYR D 255 ? O TYR D 262 
AA9 5 6  O LEU D 251 ? O LEU D 258 N TYR D 110 ? N TYR D 87  
AA9 6 7  N THR D 120 ? N THR D 97  O ALA D 273 ? O ALA D 280 
# 
_pdbx_entry_details.entry_id                   8G7Z 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OD2 A ASP 362 ? ? NH2 C ARG 232 ? ? 1.74 
2 1 OG  A SER 277 ? ? O   A VAL 359 ? ? 2.14 
3 1 ND2 A ASN 98  ? ? O5  A NAG 901 ? ? 2.15 
4 1 OG1 D THR 179 ? ? OG1 D THR 186 ? ? 2.18 
5 1 OH  C TYR 138 ? ? OD2 C ASP 158 ? ? 2.19 
6 1 OG1 C THR 119 ? ? O   C GLN 255 ? ? 2.19 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_1              341 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_2              341 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             OD1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_3              341 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                124.09 
_pdbx_validate_rmsd_angle.angle_target_value         118.30 
_pdbx_validate_rmsd_angle.angle_deviation            5.79 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.90 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
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 ASN A 126 ? ? -93.86  59.75   
2  1 ASN A 136 ? ? -108.46 41.46   
3  1 GLU A 281 ? ? -90.84  -61.54  
4  1 ASP A 358 ? ? -93.80  -60.78  
5  1 TYR A 435 ? ? -97.78  57.44   
6  1 MET A 446 ? ? -82.68  46.06   
7  1 ARG A 447 ? ? -130.47 -37.43  
8  1 ALA A 489 ? ? -75.75  -167.53 
9  1 GLU A 490 ? ? -96.32  -60.37  
10 1 PRO A 547 ? ? -66.24  4.95    
11 1 ARG A 590 ? ? -79.33  -169.01 
12 1 PHE B 69  ? ? -98.61  57.83   
13 1 THR B 100 ? ? -131.09 -36.75  
14 1 ASN B 126 ? ? -90.92  54.93   
15 1 GLN B 135 ? ? -132.86 -31.45  
16 1 SER B 187 ? ? -124.31 -165.35 
17 1 GLN B 370 ? ? -92.94  49.38   
18 1 GLU B 372 ? ? -92.13  51.41   
19 1 ASN B 375 ? ? 60.56   66.07   
20 1 ASP B 442 ? ? -98.62  36.77   
21 1 ARG B 447 ? ? -130.68 -32.28  
22 1 SER C 90  ? ? -125.28 -168.23 
23 1 SER C 132 ? ? -78.54  -166.07 
24 1 THR C 156 ? ? -91.27  -62.36  
25 1 ASN C 165 ? ? -91.66  51.35   
26 1 ASP C 190 ? ? 54.19   -110.64 
27 1 ASN C 284 ? ? -96.48  31.05   
28 1 ASP D 190 ? ? 53.66   -114.74 
29 1 ASN D 275 ? ? 61.23   60.90   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8G7Z 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      'RIGID BODY FIT' 
# 
_em_3d_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  3BL8 
_em_3d_fitting_list.pdb_chain_id                  ? 
_em_3d_fitting_list.pdb_chain_residue_range       ? 
_em_3d_fitting_list.details                       ? 
_em_3d_fitting_list.chain_id                      ? 
_em_3d_fitting_list.chain_residue_range           ? 
_em_3d_fitting_list.source_name                   PDB 
_em_3d_fitting_list.type                          'experimental model' 
_em_3d_fitting_list.accession_code                3BL8 
_em_3d_fitting_list.initial_refinement_model_id   1 
# 
_em_3d_reconstruction.entry_id                    8G7Z 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   'BACK PROJECTION' 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.22 
_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               51041 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          1 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.4 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Neuroligin 2 Dimer with 2 Neurexin-1 Beta confirmation one' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       '1, 2' 
# 
_em_image_scans.entry_id                8G7Z 
_em_image_scans.id                      1 
_em_image_scans.number_digital_images   ? 
_em_image_scans.details                 ? 
_em_image_scans.scanner_model           ? 
_em_image_scans.sampling_size           ? 
_em_image_scans.od_range                ? 
_em_image_scans.quant_bit_size          ? 
_em_image_scans.citation_id             ? 
_em_image_scans.dimension_height        4092 
_em_image_scans.dimension_width         5760 
_em_image_scans.frames_per_image        ? 
_em_image_scans.image_recording_id      1 
_em_image_scans.used_frames_per_image   ? 
# 
_em_imaging.entry_id                        8G7Z 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_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                      0 
_em_imaging.nominal_defocus_min             1000 
_em_imaging.nominal_defocus_max             2500 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          3600 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           105000 
_em_imaging.calibrated_magnification        105000 
_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             'COMA FREE' 
_em_imaging.c2_aperture_diameter            70 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    GOLD 
_em_sample_support.grid_mesh_size   400 
_em_sample_support.grid_type        'Quantifoil R1.2/1.3' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              8G7Z 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   298 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               'Blot force 20, blot time 5s, single blot' 
# 
_em_experiment.entry_id                8G7Z 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
_em_single_particle_entity.entry_id              8G7Z 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        C1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1    1 Y 1 A MET -41 ? A MET 1   
2    1 Y 1 A ALA -40 ? A ALA 2   
3    1 Y 1 A LEU -39 ? A LEU 3   
4    1 Y 1 A PRO -38 ? A PRO 4   
5    1 Y 1 A ARG -37 ? A ARG 5   
6    1 Y 1 A CYS -36 ? A CYS 6   
7    1 Y 1 A MET -35 ? A MET 7   
8    1 Y 1 A TRP -34 ? A TRP 8   
9    1 Y 1 A PRO -33 ? A PRO 9   
10   1 Y 1 A ASN -32 ? A ASN 10  
11   1 Y 1 A TYR -31 ? A TYR 11  
12   1 Y 1 A VAL -30 ? A VAL 12  
13   1 Y 1 A TRP -29 ? A TRP 13  
14   1 Y 1 A ARG -28 ? A ARG 14  
15   1 Y 1 A ALA -27 ? A ALA 15  
16   1 Y 1 A MET -26 ? A MET 16  
17   1 Y 1 A MET -25 ? A MET 17  
18   1 Y 1 A ALA -24 ? A ALA 18  
19   1 Y 1 A CYS -23 ? A CYS 19  
20   1 Y 1 A VAL -22 ? A VAL 20  
21   1 Y 1 A VAL -21 ? A VAL 21  
22   1 Y 1 A HIS -20 ? A HIS 22  
23   1 Y 1 A ARG -19 ? A ARG 23  
24   1 Y 1 A GLY -18 ? A GLY 24  
25   1 Y 1 A SER -17 ? A SER 25  
26   1 Y 1 A GLY -16 ? A GLY 26  
27   1 Y 1 A ALA -15 ? A ALA 27  
28   1 Y 1 A PRO -14 ? A PRO 28  
29   1 Y 1 A LEU -13 ? A LEU 29  
30   1 Y 1 A THR -12 ? A THR 30  
31   1 Y 1 A LEU -11 ? A LEU 31  
32   1 Y 1 A CYS -10 ? A CYS 32  
33   1 Y 1 A LEU -9  ? A LEU 33  
34   1 Y 1 A LEU -8  ? A LEU 34  
35   1 Y 1 A GLY -7  ? A GLY 35  
36   1 Y 1 A CYS -6  ? A CYS 36  
37   1 Y 1 A LEU -5  ? A LEU 37  
38   1 Y 1 A LEU -4  ? A LEU 38  
39   1 Y 1 A GLN -3  ? A GLN 39  
40   1 Y 1 A THR -2  ? A THR 40  
41   1 Y 1 A PHE -1  ? A PHE 41  
42   1 Y 1 A HIS 0   ? A HIS 42  
43   1 Y 1 A VAL 1   ? A VAL 43  
44   1 Y 1 A LEU 2   ? A LEU 44  
45   1 Y 1 A SER 3   ? A SER 45  
46   1 Y 1 A GLN 4   ? A GLN 46  
47   1 Y 1 A LYS 5   ? A LYS 47  
48   1 Y 1 A TYR 6   ? A TYR 48  
49   1 Y 1 A PRO 7   ? A PRO 49  
50   1 Y 1 A TYR 8   ? A TYR 50  
51   1 Y 1 A ASP 9   ? A ASP 51  
52   1 Y 1 A VAL 10  ? A VAL 52  
53   1 Y 1 A PRO 11  ? A PRO 53  
54   1 Y 1 A ASP 12  ? A ASP 54  
55   1 Y 1 A TYR 13  ? A TYR 55  
56   1 Y 1 A ALA 14  ? A ALA 56  
57   1 Y 1 A GLN 15  ? A GLN 57  
58   1 Y 1 A ARG 16  ? A ARG 58  
59   1 Y 1 A GLY 17  ? A GLY 59  
60   1 Y 1 A GLY 18  ? A GLY 60  
61   1 Y 1 A GLY 19  ? A GLY 61  
62   1 Y 1 A GLY 20  ? A GLY 62  
63   1 Y 1 A PRO 21  ? A PRO 63  
64   1 Y 1 A GLY 22  ? A GLY 64  
65   1 Y 1 A GLY 23  ? A GLY 65  
66   1 Y 1 A GLY 24  ? A GLY 66  
67   1 Y 1 A ALA 25  ? A ALA 67  
68   1 Y 1 A PRO 26  ? A PRO 68  
69   1 Y 1 A GLY 27  ? A GLY 69  
70   1 Y 1 A GLY 28  ? A GLY 70  
71   1 Y 1 A PRO 29  ? A PRO 71  
72   1 Y 1 A GLY 30  ? A GLY 72  
73   1 Y 1 A LEU 31  ? A LEU 73  
74   1 Y 1 A GLY 32  ? A GLY 74  
75   1 Y 1 A LEU 33  ? A LEU 75  
76   1 Y 1 A GLY 34  ? A GLY 76  
77   1 Y 1 A SER 35  ? A SER 77  
78   1 Y 1 A LEU 36  ? A LEU 78  
79   1 Y 1 A GLY 37  ? A GLY 79  
80   1 Y 1 A GLU 38  ? A GLU 80  
81   1 Y 1 A GLU 39  ? A GLU 81  
82   1 Y 1 A GLU 168 ? A GLU 193 
83   1 Y 1 A ASP 169 ? A ASP 194 
84   1 Y 1 A ASP 170 ? A ASP 195 
85   1 Y 1 A ILE 171 ? A ILE 196 
86   1 Y 1 A ARG 172 ? A ARG 197 
87   1 Y 1 A ASP 173 ? A ASP 198 
88   1 Y 1 A THR 555 ? A THR 580 
89   1 Y 1 A LYS 556 ? A LYS 581 
90   1 Y 1 A PHE 557 ? A PHE 582 
91   1 Y 1 A ILE 558 ? A ILE 583 
92   1 Y 1 A HIS 559 ? A HIS 584 
93   1 Y 1 A THR 560 ? A THR 585 
94   1 Y 1 A LYS 561 ? A LYS 586 
95   1 Y 1 A PRO 562 ? A PRO 587 
96   1 Y 1 A ASN 563 ? A ASN 588 
97   1 Y 1 A HIS 609 ? A HIS 634 
98   1 Y 1 A ASN 610 ? A ASN 635 
99   1 Y 1 A LEU 611 ? A LEU 636 
100  1 Y 1 A HIS 612 ? A HIS 637 
101  1 Y 1 A THR 613 ? A THR 638 
102  1 Y 1 A GLU 614 ? A GLU 639 
103  1 Y 1 A LEU 615 ? A LEU 640 
104  1 Y 1 A PHE 616 ? A PHE 641 
105  1 Y 1 A THR 617 ? A THR 642 
106  1 Y 1 A THR 618 ? A THR 643 
107  1 Y 1 A THR 619 ? A THR 644 
108  1 Y 1 A THR 620 ? A THR 645 
109  1 Y 1 A ARG 621 ? A ARG 646 
110  1 Y 1 A LEU 622 ? A LEU 647 
111  1 Y 1 A PRO 623 ? A PRO 648 
112  1 Y 1 A PRO 624 ? A PRO 649 
113  1 Y 1 A TYR 625 ? A TYR 650 
114  1 Y 1 A ALA 626 ? A ALA 651 
115  1 Y 1 A THR 627 ? A THR 652 
116  1 Y 1 A ARG 628 ? A ARG 653 
117  1 Y 1 A TRP 629 ? A TRP 654 
118  1 Y 1 A PRO 630 ? A PRO 655 
119  1 Y 1 A PRO 631 ? A PRO 656 
120  1 Y 1 A ARG 632 ? A ARG 657 
121  1 Y 1 A THR 633 ? A THR 658 
122  1 Y 1 A PRO 634 ? A PRO 659 
123  1 Y 1 A GLY 635 ? A GLY 660 
124  1 Y 1 A PRO 636 ? A PRO 661 
125  1 Y 1 A GLY 637 ? A GLY 662 
126  1 Y 1 A THR 638 ? A THR 663 
127  1 Y 1 A SER 639 ? A SER 664 
128  1 Y 1 A GLY 640 ? A GLY 665 
129  1 Y 1 A THR 641 ? A THR 666 
130  1 Y 1 A ARG 642 ? A ARG 667 
131  1 Y 1 A ARG 643 ? A ARG 668 
132  1 Y 1 A PRO 644 ? A PRO 669 
133  1 Y 1 A PRO 645 ? A PRO 670 
134  1 Y 1 A PRO 646 ? A PRO 671 
135  1 Y 1 A PRO 647 ? A PRO 672 
136  1 Y 1 A ALA 648 ? A ALA 673 
137  1 Y 1 A THR 649 ? A THR 674 
138  1 Y 1 A LEU 650 ? A LEU 675 
139  1 Y 1 A PRO 651 ? A PRO 676 
140  1 Y 1 A PRO 652 ? A PRO 677 
141  1 Y 1 A GLU 653 ? A GLU 678 
142  1 Y 1 A SER 654 ? A SER 679 
143  1 Y 1 A ASP 655 ? A ASP 680 
144  1 Y 1 A ILE 656 ? A ILE 681 
145  1 Y 1 A ASP 657 ? A ASP 682 
146  1 Y 1 A LEU 658 ? A LEU 683 
147  1 Y 1 A GLY 659 ? A GLY 684 
148  1 Y 1 A PRO 660 ? A PRO 685 
149  1 Y 1 A ARG 661 ? A ARG 686 
150  1 Y 1 A ALA 662 ? A ALA 687 
151  1 Y 1 A TYR 663 ? A TYR 688 
152  1 Y 1 A ASP 664 ? A ASP 689 
153  1 Y 1 A ARG 665 ? A ARG 690 
154  1 Y 1 A PHE 666 ? A PHE 691 
155  1 Y 1 A PRO 667 ? A PRO 692 
156  1 Y 1 A GLY 668 ? A GLY 693 
157  1 Y 1 A ASP 669 ? A ASP 694 
158  1 Y 1 A SER 670 ? A SER 695 
159  1 Y 1 A ARG 671 ? A ARG 696 
160  1 Y 1 A ASP 672 ? A ASP 697 
161  1 Y 1 A TYR 673 ? A TYR 698 
162  1 Y 1 A SER 674 ? A SER 699 
163  1 Y 1 A THR 675 ? A THR 700 
164  1 Y 1 A GLU 676 ? A GLU 701 
165  1 Y 1 A LEU 677 ? A LEU 702 
166  1 Y 1 A SER 678 ? A SER 703 
167  1 Y 1 A VAL 679 ? A VAL 704 
168  1 Y 1 A THR 680 ? A THR 705 
169  1 Y 1 A VAL 681 ? A VAL 706 
170  1 Y 1 A ALA 682 ? A ALA 707 
171  1 Y 1 A VAL 683 ? A VAL 708 
172  1 Y 1 A GLY 684 ? A GLY 709 
173  1 Y 1 A ALA 685 ? A ALA 710 
174  1 Y 1 A SER 686 ? A SER 711 
175  1 Y 1 A LEU 687 ? A LEU 712 
176  1 Y 1 A LEU 688 ? A LEU 713 
177  1 Y 1 A PHE 689 ? A PHE 714 
178  1 Y 1 A LEU 690 ? A LEU 715 
179  1 Y 1 A ASN 691 ? A ASN 716 
180  1 Y 1 A ILE 692 ? A ILE 717 
181  1 Y 1 A LEU 693 ? A LEU 718 
182  1 Y 1 A ALA 694 ? A ALA 719 
183  1 Y 1 A PHE 695 ? A PHE 720 
184  1 Y 1 A ALA 696 ? A ALA 721 
185  1 Y 1 A ALA 697 ? A ALA 722 
186  1 Y 1 A LEU 698 ? A LEU 723 
187  1 Y 1 A TYR 699 ? A TYR 724 
188  1 Y 1 A TYR 700 ? A TYR 725 
189  1 Y 1 A LYS 701 ? A LYS 726 
190  1 Y 1 A ARG 702 ? A ARG 727 
191  1 Y 1 A ASP 703 ? A ASP 728 
192  1 Y 1 A ARG 704 ? A ARG 729 
193  1 Y 1 A ARG 705 ? A ARG 730 
194  1 Y 1 A GLN 706 ? A GLN 731 
195  1 Y 1 A GLU 707 ? A GLU 732 
196  1 Y 1 A LEU 708 ? A LEU 733 
197  1 Y 1 A ARG 709 ? A ARG 734 
198  1 Y 1 A CYS 710 ? A CYS 735 
199  1 Y 1 A ARG 711 ? A ARG 736 
200  1 Y 1 A ARG 712 ? A ARG 737 
201  1 Y 1 A LEU 713 ? A LEU 738 
202  1 Y 1 A SER 714 ? A SER 739 
203  1 Y 1 A PRO 715 ? A PRO 740 
204  1 Y 1 A PRO 716 ? A PRO 741 
205  1 Y 1 A GLY 717 ? A GLY 742 
206  1 Y 1 A GLY 718 ? A GLY 743 
207  1 Y 1 A SER 719 ? A SER 744 
208  1 Y 1 A GLY 720 ? A GLY 745 
209  1 Y 1 A SER 721 ? A SER 746 
210  1 Y 1 A GLY 722 ? A GLY 747 
211  1 Y 1 A VAL 723 ? A VAL 748 
212  1 Y 1 A PRO 724 ? A PRO 749 
213  1 Y 1 A GLY 725 ? A GLY 750 
214  1 Y 1 A GLY 726 ? A GLY 751 
215  1 Y 1 A GLY 727 ? A GLY 752 
216  1 Y 1 A PRO 728 ? A PRO 753 
217  1 Y 1 A LEU 729 ? A LEU 754 
218  1 Y 1 A LEU 730 ? A LEU 755 
219  1 Y 1 A PRO 731 ? A PRO 756 
220  1 Y 1 A THR 732 ? A THR 757 
221  1 Y 1 A ALA 733 ? A ALA 758 
222  1 Y 1 A GLY 734 ? A GLY 759 
223  1 Y 1 A ARG 735 ? A ARG 760 
224  1 Y 1 A GLU 736 ? A GLU 761 
225  1 Y 1 A LEU 737 ? A LEU 762 
226  1 Y 1 A PRO 738 ? A PRO 763 
227  1 Y 1 A PRO 739 ? A PRO 764 
228  1 Y 1 A GLU 740 ? A GLU 765 
229  1 Y 1 A GLU 741 ? A GLU 766 
230  1 Y 1 A GLU 742 ? A GLU 767 
231  1 Y 1 A LEU 743 ? A LEU 768 
232  1 Y 1 A VAL 744 ? A VAL 769 
233  1 Y 1 A SER 745 ? A SER 770 
234  1 Y 1 A LEU 746 ? A LEU 771 
235  1 Y 1 A GLN 747 ? A GLN 772 
236  1 Y 1 A LEU 748 ? A LEU 773 
237  1 Y 1 A LYS 749 ? A LYS 774 
238  1 Y 1 A ARG 750 ? A ARG 775 
239  1 Y 1 A GLY 751 ? A GLY 776 
240  1 Y 1 A GLY 752 ? A GLY 777 
241  1 Y 1 A GLY 753 ? A GLY 778 
242  1 Y 1 A VAL 754 ? A VAL 779 
243  1 Y 1 A GLY 755 ? A GLY 780 
244  1 Y 1 A ALA 756 ? A ALA 781 
245  1 Y 1 A ASP 757 ? A ASP 782 
246  1 Y 1 A PRO 758 ? A PRO 783 
247  1 Y 1 A ALA 759 ? A ALA 784 
248  1 Y 1 A GLU 760 ? A GLU 785 
249  1 Y 1 A ALA 761 ? A ALA 786 
250  1 Y 1 A LEU 762 ? A LEU 787 
251  1 Y 1 A ARG 763 ? A ARG 788 
252  1 Y 1 A PRO 764 ? A PRO 789 
253  1 Y 1 A ALA 765 ? A ALA 790 
254  1 Y 1 A CYS 766 ? A CYS 791 
255  1 Y 1 A PRO 767 ? A PRO 792 
256  1 Y 1 A PRO 768 ? A PRO 793 
257  1 Y 1 A ASP 769 ? A ASP 794 
258  1 Y 1 A TYR 770 ? A TYR 795 
259  1 Y 1 A THR 771 ? A THR 796 
260  1 Y 1 A LEU 772 ? A LEU 797 
261  1 Y 1 A ALA 773 ? A ALA 798 
262  1 Y 1 A LEU 774 ? A LEU 799 
263  1 Y 1 A ARG 775 ? A ARG 800 
264  1 Y 1 A ARG 776 ? A ARG 801 
265  1 Y 1 A ALA 777 ? A ALA 802 
266  1 Y 1 A PRO 778 ? A PRO 803 
267  1 Y 1 A ASP 779 ? A ASP 804 
268  1 Y 1 A ASP 780 ? A ASP 805 
269  1 Y 1 A VAL 781 ? A VAL 806 
270  1 Y 1 A PRO 782 ? A PRO 807 
271  1 Y 1 A LEU 783 ? A LEU 808 
272  1 Y 1 A LEU 784 ? A LEU 809 
273  1 Y 1 A ALA 785 ? A ALA 810 
274  1 Y 1 A PRO 786 ? A PRO 811 
275  1 Y 1 A GLY 787 ? A GLY 812 
276  1 Y 1 A ALA 788 ? A ALA 813 
277  1 Y 1 A LEU 789 ? A LEU 814 
278  1 Y 1 A THR 790 ? A THR 815 
279  1 Y 1 A LEU 791 ? A LEU 816 
280  1 Y 1 A LEU 792 ? A LEU 817 
281  1 Y 1 A PRO 793 ? A PRO 818 
282  1 Y 1 A SER 794 ? A SER 819 
283  1 Y 1 A GLY 795 ? A GLY 820 
284  1 Y 1 A LEU 796 ? A LEU 821 
285  1 Y 1 A GLY 797 ? A GLY 822 
286  1 Y 1 A PRO 798 ? A PRO 823 
287  1 Y 1 A PRO 799 ? A PRO 824 
288  1 Y 1 A PRO 800 ? A PRO 825 
289  1 Y 1 A PRO 801 ? A PRO 826 
290  1 Y 1 A PRO 802 ? A PRO 827 
291  1 Y 1 A PRO 803 ? A PRO 828 
292  1 Y 1 A PRO 804 ? A PRO 829 
293  1 Y 1 A PRO 805 ? A PRO 830 
294  1 Y 1 A SER 806 ? A SER 831 
295  1 Y 1 A LEU 807 ? A LEU 832 
296  1 Y 1 A HIS 808 ? A HIS 833 
297  1 Y 1 A PRO 809 ? A PRO 834 
298  1 Y 1 A PHE 810 ? A PHE 835 
299  1 Y 1 A GLY 811 ? A GLY 836 
300  1 Y 1 A PRO 812 ? A PRO 837 
301  1 Y 1 A PHE 813 ? A PHE 838 
302  1 Y 1 A PRO 814 ? A PRO 839 
303  1 Y 1 A PRO 815 ? A PRO 840 
304  1 Y 1 A PRO 816 ? A PRO 841 
305  1 Y 1 A PRO 817 ? A PRO 842 
306  1 Y 1 A PRO 818 ? A PRO 843 
307  1 Y 1 A THR 819 ? A THR 844 
308  1 Y 1 A ALA 820 ? A ALA 845 
309  1 Y 1 A THR 821 ? A THR 846 
310  1 Y 1 A SER 822 ? A SER 847 
311  1 Y 1 A HIS 823 ? A HIS 848 
312  1 Y 1 A ASN 824 ? A ASN 849 
313  1 Y 1 A ASN 825 ? A ASN 850 
314  1 Y 1 A THR 826 ? A THR 851 
315  1 Y 1 A LEU 827 ? A LEU 852 
316  1 Y 1 A PRO 828 ? A PRO 853 
317  1 Y 1 A HIS 829 ? A HIS 854 
318  1 Y 1 A PRO 830 ? A PRO 855 
319  1 Y 1 A HIS 831 ? A HIS 856 
320  1 Y 1 A SER 832 ? A SER 857 
321  1 Y 1 A THR 833 ? A THR 858 
322  1 Y 1 A THR 834 ? A THR 859 
323  1 Y 1 A ARG 835 ? A ARG 860 
324  1 Y 1 A VAL 836 ? A VAL 861 
325  1 Y 1 A SER 837 ? A SER 862 
326  1 Y 1 A ASN 838 ? A ASN 863 
327  1 Y 1 A SER 839 ? A SER 864 
328  1 Y 1 A LEU 840 ? A LEU 865 
329  1 Y 1 A GLU 841 ? A GLU 866 
330  1 Y 1 A VAL 842 ? A VAL 867 
331  1 Y 1 A LEU 843 ? A LEU 868 
332  1 Y 1 A PHE 844 ? A PHE 869 
333  1 Y 1 A GLN 845 ? A GLN 870 
334  1 Y 1 B MET -41 ? B MET 1   
335  1 Y 1 B ALA -40 ? B ALA 2   
336  1 Y 1 B LEU -39 ? B LEU 3   
337  1 Y 1 B PRO -38 ? B PRO 4   
338  1 Y 1 B ARG -37 ? B ARG 5   
339  1 Y 1 B CYS -36 ? B CYS 6   
340  1 Y 1 B MET -35 ? B MET 7   
341  1 Y 1 B TRP -34 ? B TRP 8   
342  1 Y 1 B PRO -33 ? B PRO 9   
343  1 Y 1 B ASN -32 ? B ASN 10  
344  1 Y 1 B TYR -31 ? B TYR 11  
345  1 Y 1 B VAL -30 ? B VAL 12  
346  1 Y 1 B TRP -29 ? B TRP 13  
347  1 Y 1 B ARG -28 ? B ARG 14  
348  1 Y 1 B ALA -27 ? B ALA 15  
349  1 Y 1 B MET -26 ? B MET 16  
350  1 Y 1 B MET -25 ? B MET 17  
351  1 Y 1 B ALA -24 ? B ALA 18  
352  1 Y 1 B CYS -23 ? B CYS 19  
353  1 Y 1 B VAL -22 ? B VAL 20  
354  1 Y 1 B VAL -21 ? B VAL 21  
355  1 Y 1 B HIS -20 ? B HIS 22  
356  1 Y 1 B ARG -19 ? B ARG 23  
357  1 Y 1 B GLY -18 ? B GLY 24  
358  1 Y 1 B SER -17 ? B SER 25  
359  1 Y 1 B GLY -16 ? B GLY 26  
360  1 Y 1 B ALA -15 ? B ALA 27  
361  1 Y 1 B PRO -14 ? B PRO 28  
362  1 Y 1 B LEU -13 ? B LEU 29  
363  1 Y 1 B THR -12 ? B THR 30  
364  1 Y 1 B LEU -11 ? B LEU 31  
365  1 Y 1 B CYS -10 ? B CYS 32  
366  1 Y 1 B LEU -9  ? B LEU 33  
367  1 Y 1 B LEU -8  ? B LEU 34  
368  1 Y 1 B GLY -7  ? B GLY 35  
369  1 Y 1 B CYS -6  ? B CYS 36  
370  1 Y 1 B LEU -5  ? B LEU 37  
371  1 Y 1 B LEU -4  ? B LEU 38  
372  1 Y 1 B GLN -3  ? B GLN 39  
373  1 Y 1 B THR -2  ? B THR 40  
374  1 Y 1 B PHE -1  ? B PHE 41  
375  1 Y 1 B HIS 0   ? B HIS 42  
376  1 Y 1 B VAL 1   ? B VAL 43  
377  1 Y 1 B LEU 2   ? B LEU 44  
378  1 Y 1 B SER 3   ? B SER 45  
379  1 Y 1 B GLN 4   ? B GLN 46  
380  1 Y 1 B LYS 5   ? B LYS 47  
381  1 Y 1 B TYR 6   ? B TYR 48  
382  1 Y 1 B PRO 7   ? B PRO 49  
383  1 Y 1 B TYR 8   ? B TYR 50  
384  1 Y 1 B ASP 9   ? B ASP 51  
385  1 Y 1 B VAL 10  ? B VAL 52  
386  1 Y 1 B PRO 11  ? B PRO 53  
387  1 Y 1 B ASP 12  ? B ASP 54  
388  1 Y 1 B TYR 13  ? B TYR 55  
389  1 Y 1 B ALA 14  ? B ALA 56  
390  1 Y 1 B GLN 15  ? B GLN 57  
391  1 Y 1 B ARG 16  ? B ARG 58  
392  1 Y 1 B GLY 17  ? B GLY 59  
393  1 Y 1 B GLY 18  ? B GLY 60  
394  1 Y 1 B GLY 19  ? B GLY 61  
395  1 Y 1 B GLY 20  ? B GLY 62  
396  1 Y 1 B PRO 21  ? B PRO 63  
397  1 Y 1 B GLY 22  ? B GLY 64  
398  1 Y 1 B GLY 23  ? B GLY 65  
399  1 Y 1 B GLY 24  ? B GLY 66  
400  1 Y 1 B ALA 25  ? B ALA 67  
401  1 Y 1 B PRO 26  ? B PRO 68  
402  1 Y 1 B GLY 27  ? B GLY 69  
403  1 Y 1 B GLY 28  ? B GLY 70  
404  1 Y 1 B PRO 29  ? B PRO 71  
405  1 Y 1 B GLY 30  ? B GLY 72  
406  1 Y 1 B LEU 31  ? B LEU 73  
407  1 Y 1 B GLY 32  ? B GLY 74  
408  1 Y 1 B LEU 33  ? B LEU 75  
409  1 Y 1 B GLY 34  ? B GLY 76  
410  1 Y 1 B SER 35  ? B SER 77  
411  1 Y 1 B LEU 36  ? B LEU 78  
412  1 Y 1 B GLY 37  ? B GLY 79  
413  1 Y 1 B GLU 38  ? B GLU 80  
414  1 Y 1 B GLU 39  ? B GLU 81  
415  1 Y 1 B GLU 168 ? B GLU 193 
416  1 Y 1 B ASP 169 ? B ASP 194 
417  1 Y 1 B ASP 170 ? B ASP 195 
418  1 Y 1 B ILE 171 ? B ILE 196 
419  1 Y 1 B ARG 172 ? B ARG 197 
420  1 Y 1 B ASP 173 ? B ASP 198 
421  1 Y 1 B ASP 554 ? B ASP 579 
422  1 Y 1 B THR 555 ? B THR 580 
423  1 Y 1 B LYS 556 ? B LYS 581 
424  1 Y 1 B PHE 557 ? B PHE 582 
425  1 Y 1 B ILE 558 ? B ILE 583 
426  1 Y 1 B HIS 559 ? B HIS 584 
427  1 Y 1 B THR 560 ? B THR 585 
428  1 Y 1 B LYS 561 ? B LYS 586 
429  1 Y 1 B PRO 562 ? B PRO 587 
430  1 Y 1 B ASN 563 ? B ASN 588 
431  1 Y 1 B HIS 609 ? B HIS 634 
432  1 Y 1 B ASN 610 ? B ASN 635 
433  1 Y 1 B LEU 611 ? B LEU 636 
434  1 Y 1 B HIS 612 ? B HIS 637 
435  1 Y 1 B THR 613 ? B THR 638 
436  1 Y 1 B GLU 614 ? B GLU 639 
437  1 Y 1 B LEU 615 ? B LEU 640 
438  1 Y 1 B PHE 616 ? B PHE 641 
439  1 Y 1 B THR 617 ? B THR 642 
440  1 Y 1 B THR 618 ? B THR 643 
441  1 Y 1 B THR 619 ? B THR 644 
442  1 Y 1 B THR 620 ? B THR 645 
443  1 Y 1 B ARG 621 ? B ARG 646 
444  1 Y 1 B LEU 622 ? B LEU 647 
445  1 Y 1 B PRO 623 ? B PRO 648 
446  1 Y 1 B PRO 624 ? B PRO 649 
447  1 Y 1 B TYR 625 ? B TYR 650 
448  1 Y 1 B ALA 626 ? B ALA 651 
449  1 Y 1 B THR 627 ? B THR 652 
450  1 Y 1 B ARG 628 ? B ARG 653 
451  1 Y 1 B TRP 629 ? B TRP 654 
452  1 Y 1 B PRO 630 ? B PRO 655 
453  1 Y 1 B PRO 631 ? B PRO 656 
454  1 Y 1 B ARG 632 ? B ARG 657 
455  1 Y 1 B THR 633 ? B THR 658 
456  1 Y 1 B PRO 634 ? B PRO 659 
457  1 Y 1 B GLY 635 ? B GLY 660 
458  1 Y 1 B PRO 636 ? B PRO 661 
459  1 Y 1 B GLY 637 ? B GLY 662 
460  1 Y 1 B THR 638 ? B THR 663 
461  1 Y 1 B SER 639 ? B SER 664 
462  1 Y 1 B GLY 640 ? B GLY 665 
463  1 Y 1 B THR 641 ? B THR 666 
464  1 Y 1 B ARG 642 ? B ARG 667 
465  1 Y 1 B ARG 643 ? B ARG 668 
466  1 Y 1 B PRO 644 ? B PRO 669 
467  1 Y 1 B PRO 645 ? B PRO 670 
468  1 Y 1 B PRO 646 ? B PRO 671 
469  1 Y 1 B PRO 647 ? B PRO 672 
470  1 Y 1 B ALA 648 ? B ALA 673 
471  1 Y 1 B THR 649 ? B THR 674 
472  1 Y 1 B LEU 650 ? B LEU 675 
473  1 Y 1 B PRO 651 ? B PRO 676 
474  1 Y 1 B PRO 652 ? B PRO 677 
475  1 Y 1 B GLU 653 ? B GLU 678 
476  1 Y 1 B SER 654 ? B SER 679 
477  1 Y 1 B ASP 655 ? B ASP 680 
478  1 Y 1 B ILE 656 ? B ILE 681 
479  1 Y 1 B ASP 657 ? B ASP 682 
480  1 Y 1 B LEU 658 ? B LEU 683 
481  1 Y 1 B GLY 659 ? B GLY 684 
482  1 Y 1 B PRO 660 ? B PRO 685 
483  1 Y 1 B ARG 661 ? B ARG 686 
484  1 Y 1 B ALA 662 ? B ALA 687 
485  1 Y 1 B TYR 663 ? B TYR 688 
486  1 Y 1 B ASP 664 ? B ASP 689 
487  1 Y 1 B ARG 665 ? B ARG 690 
488  1 Y 1 B PHE 666 ? B PHE 691 
489  1 Y 1 B PRO 667 ? B PRO 692 
490  1 Y 1 B GLY 668 ? B GLY 693 
491  1 Y 1 B ASP 669 ? B ASP 694 
492  1 Y 1 B SER 670 ? B SER 695 
493  1 Y 1 B ARG 671 ? B ARG 696 
494  1 Y 1 B ASP 672 ? B ASP 697 
495  1 Y 1 B TYR 673 ? B TYR 698 
496  1 Y 1 B SER 674 ? B SER 699 
497  1 Y 1 B THR 675 ? B THR 700 
498  1 Y 1 B GLU 676 ? B GLU 701 
499  1 Y 1 B LEU 677 ? B LEU 702 
500  1 Y 1 B SER 678 ? B SER 703 
501  1 Y 1 B VAL 679 ? B VAL 704 
502  1 Y 1 B THR 680 ? B THR 705 
503  1 Y 1 B VAL 681 ? B VAL 706 
504  1 Y 1 B ALA 682 ? B ALA 707 
505  1 Y 1 B VAL 683 ? B VAL 708 
506  1 Y 1 B GLY 684 ? B GLY 709 
507  1 Y 1 B ALA 685 ? B ALA 710 
508  1 Y 1 B SER 686 ? B SER 711 
509  1 Y 1 B LEU 687 ? B LEU 712 
510  1 Y 1 B LEU 688 ? B LEU 713 
511  1 Y 1 B PHE 689 ? B PHE 714 
512  1 Y 1 B LEU 690 ? B LEU 715 
513  1 Y 1 B ASN 691 ? B ASN 716 
514  1 Y 1 B ILE 692 ? B ILE 717 
515  1 Y 1 B LEU 693 ? B LEU 718 
516  1 Y 1 B ALA 694 ? B ALA 719 
517  1 Y 1 B PHE 695 ? B PHE 720 
518  1 Y 1 B ALA 696 ? B ALA 721 
519  1 Y 1 B ALA 697 ? B ALA 722 
520  1 Y 1 B LEU 698 ? B LEU 723 
521  1 Y 1 B TYR 699 ? B TYR 724 
522  1 Y 1 B TYR 700 ? B TYR 725 
523  1 Y 1 B LYS 701 ? B LYS 726 
524  1 Y 1 B ARG 702 ? B ARG 727 
525  1 Y 1 B ASP 703 ? B ASP 728 
526  1 Y 1 B ARG 704 ? B ARG 729 
527  1 Y 1 B ARG 705 ? B ARG 730 
528  1 Y 1 B GLN 706 ? B GLN 731 
529  1 Y 1 B GLU 707 ? B GLU 732 
530  1 Y 1 B LEU 708 ? B LEU 733 
531  1 Y 1 B ARG 709 ? B ARG 734 
532  1 Y 1 B CYS 710 ? B CYS 735 
533  1 Y 1 B ARG 711 ? B ARG 736 
534  1 Y 1 B ARG 712 ? B ARG 737 
535  1 Y 1 B LEU 713 ? B LEU 738 
536  1 Y 1 B SER 714 ? B SER 739 
537  1 Y 1 B PRO 715 ? B PRO 740 
538  1 Y 1 B PRO 716 ? B PRO 741 
539  1 Y 1 B GLY 717 ? B GLY 742 
540  1 Y 1 B GLY 718 ? B GLY 743 
541  1 Y 1 B SER 719 ? B SER 744 
542  1 Y 1 B GLY 720 ? B GLY 745 
543  1 Y 1 B SER 721 ? B SER 746 
544  1 Y 1 B GLY 722 ? B GLY 747 
545  1 Y 1 B VAL 723 ? B VAL 748 
546  1 Y 1 B PRO 724 ? B PRO 749 
547  1 Y 1 B GLY 725 ? B GLY 750 
548  1 Y 1 B GLY 726 ? B GLY 751 
549  1 Y 1 B GLY 727 ? B GLY 752 
550  1 Y 1 B PRO 728 ? B PRO 753 
551  1 Y 1 B LEU 729 ? B LEU 754 
552  1 Y 1 B LEU 730 ? B LEU 755 
553  1 Y 1 B PRO 731 ? B PRO 756 
554  1 Y 1 B THR 732 ? B THR 757 
555  1 Y 1 B ALA 733 ? B ALA 758 
556  1 Y 1 B GLY 734 ? B GLY 759 
557  1 Y 1 B ARG 735 ? B ARG 760 
558  1 Y 1 B GLU 736 ? B GLU 761 
559  1 Y 1 B LEU 737 ? B LEU 762 
560  1 Y 1 B PRO 738 ? B PRO 763 
561  1 Y 1 B PRO 739 ? B PRO 764 
562  1 Y 1 B GLU 740 ? B GLU 765 
563  1 Y 1 B GLU 741 ? B GLU 766 
564  1 Y 1 B GLU 742 ? B GLU 767 
565  1 Y 1 B LEU 743 ? B LEU 768 
566  1 Y 1 B VAL 744 ? B VAL 769 
567  1 Y 1 B SER 745 ? B SER 770 
568  1 Y 1 B LEU 746 ? B LEU 771 
569  1 Y 1 B GLN 747 ? B GLN 772 
570  1 Y 1 B LEU 748 ? B LEU 773 
571  1 Y 1 B LYS 749 ? B LYS 774 
572  1 Y 1 B ARG 750 ? B ARG 775 
573  1 Y 1 B GLY 751 ? B GLY 776 
574  1 Y 1 B GLY 752 ? B GLY 777 
575  1 Y 1 B GLY 753 ? B GLY 778 
576  1 Y 1 B VAL 754 ? B VAL 779 
577  1 Y 1 B GLY 755 ? B GLY 780 
578  1 Y 1 B ALA 756 ? B ALA 781 
579  1 Y 1 B ASP 757 ? B ASP 782 
580  1 Y 1 B PRO 758 ? B PRO 783 
581  1 Y 1 B ALA 759 ? B ALA 784 
582  1 Y 1 B GLU 760 ? B GLU 785 
583  1 Y 1 B ALA 761 ? B ALA 786 
584  1 Y 1 B LEU 762 ? B LEU 787 
585  1 Y 1 B ARG 763 ? B ARG 788 
586  1 Y 1 B PRO 764 ? B PRO 789 
587  1 Y 1 B ALA 765 ? B ALA 790 
588  1 Y 1 B CYS 766 ? B CYS 791 
589  1 Y 1 B PRO 767 ? B PRO 792 
590  1 Y 1 B PRO 768 ? B PRO 793 
591  1 Y 1 B ASP 769 ? B ASP 794 
592  1 Y 1 B TYR 770 ? B TYR 795 
593  1 Y 1 B THR 771 ? B THR 796 
594  1 Y 1 B LEU 772 ? B LEU 797 
595  1 Y 1 B ALA 773 ? B ALA 798 
596  1 Y 1 B LEU 774 ? B LEU 799 
597  1 Y 1 B ARG 775 ? B ARG 800 
598  1 Y 1 B ARG 776 ? B ARG 801 
599  1 Y 1 B ALA 777 ? B ALA 802 
600  1 Y 1 B PRO 778 ? B PRO 803 
601  1 Y 1 B ASP 779 ? B ASP 804 
602  1 Y 1 B ASP 780 ? B ASP 805 
603  1 Y 1 B VAL 781 ? B VAL 806 
604  1 Y 1 B PRO 782 ? B PRO 807 
605  1 Y 1 B LEU 783 ? B LEU 808 
606  1 Y 1 B LEU 784 ? B LEU 809 
607  1 Y 1 B ALA 785 ? B ALA 810 
608  1 Y 1 B PRO 786 ? B PRO 811 
609  1 Y 1 B GLY 787 ? B GLY 812 
610  1 Y 1 B ALA 788 ? B ALA 813 
611  1 Y 1 B LEU 789 ? B LEU 814 
612  1 Y 1 B THR 790 ? B THR 815 
613  1 Y 1 B LEU 791 ? B LEU 816 
614  1 Y 1 B LEU 792 ? B LEU 817 
615  1 Y 1 B PRO 793 ? B PRO 818 
616  1 Y 1 B SER 794 ? B SER 819 
617  1 Y 1 B GLY 795 ? B GLY 820 
618  1 Y 1 B LEU 796 ? B LEU 821 
619  1 Y 1 B GLY 797 ? B GLY 822 
620  1 Y 1 B PRO 798 ? B PRO 823 
621  1 Y 1 B PRO 799 ? B PRO 824 
622  1 Y 1 B PRO 800 ? B PRO 825 
623  1 Y 1 B PRO 801 ? B PRO 826 
624  1 Y 1 B PRO 802 ? B PRO 827 
625  1 Y 1 B PRO 803 ? B PRO 828 
626  1 Y 1 B PRO 804 ? B PRO 829 
627  1 Y 1 B PRO 805 ? B PRO 830 
628  1 Y 1 B SER 806 ? B SER 831 
629  1 Y 1 B LEU 807 ? B LEU 832 
630  1 Y 1 B HIS 808 ? B HIS 833 
631  1 Y 1 B PRO 809 ? B PRO 834 
632  1 Y 1 B PHE 810 ? B PHE 835 
633  1 Y 1 B GLY 811 ? B GLY 836 
634  1 Y 1 B PRO 812 ? B PRO 837 
635  1 Y 1 B PHE 813 ? B PHE 838 
636  1 Y 1 B PRO 814 ? B PRO 839 
637  1 Y 1 B PRO 815 ? B PRO 840 
638  1 Y 1 B PRO 816 ? B PRO 841 
639  1 Y 1 B PRO 817 ? B PRO 842 
640  1 Y 1 B PRO 818 ? B PRO 843 
641  1 Y 1 B THR 819 ? B THR 844 
642  1 Y 1 B ALA 820 ? B ALA 845 
643  1 Y 1 B THR 821 ? B THR 846 
644  1 Y 1 B SER 822 ? B SER 847 
645  1 Y 1 B HIS 823 ? B HIS 848 
646  1 Y 1 B ASN 824 ? B ASN 849 
647  1 Y 1 B ASN 825 ? B ASN 850 
648  1 Y 1 B THR 826 ? B THR 851 
649  1 Y 1 B LEU 827 ? B LEU 852 
650  1 Y 1 B PRO 828 ? B PRO 853 
651  1 Y 1 B HIS 829 ? B HIS 854 
652  1 Y 1 B PRO 830 ? B PRO 855 
653  1 Y 1 B HIS 831 ? B HIS 856 
654  1 Y 1 B SER 832 ? B SER 857 
655  1 Y 1 B THR 833 ? B THR 858 
656  1 Y 1 B THR 834 ? B THR 859 
657  1 Y 1 B ARG 835 ? B ARG 860 
658  1 Y 1 B VAL 836 ? B VAL 861 
659  1 Y 1 B SER 837 ? B SER 862 
660  1 Y 1 B ASN 838 ? B ASN 863 
661  1 Y 1 B SER 839 ? B SER 864 
662  1 Y 1 B LEU 840 ? B LEU 865 
663  1 Y 1 B GLU 841 ? B GLU 866 
664  1 Y 1 B VAL 842 ? B VAL 867 
665  1 Y 1 B LEU 843 ? B LEU 868 
666  1 Y 1 B PHE 844 ? B PHE 869 
667  1 Y 1 B GLN 845 ? B GLN 870 
668  1 Y 1 C MET -22 ? C MET 1   
669  1 Y 1 C TYR -21 ? C TYR 2   
670  1 Y 1 C GLN -20 ? C GLN 3   
671  1 Y 1 C ARG -19 ? C ARG 4   
672  1 Y 1 C MET -18 ? C MET 5   
673  1 Y 1 C LEU -17 ? C LEU 6   
674  1 Y 1 C ARG -16 ? C ARG 7   
675  1 Y 1 C CYS -15 ? C CYS 8   
676  1 Y 1 C GLY -14 ? C GLY 9   
677  1 Y 1 C ALA -13 ? C ALA 10  
678  1 Y 1 C ASP -12 ? C ASP 11  
679  1 Y 1 C LEU -11 ? C LEU 12  
680  1 Y 1 C GLY -10 ? C GLY 13  
681  1 Y 1 C SER -9  ? C SER 14  
682  1 Y 1 C PRO -8  ? C PRO 15  
683  1 Y 1 C GLY -7  ? C GLY 16  
684  1 Y 1 C GLY -6  ? C GLY 17  
685  1 Y 1 C GLY -5  ? C GLY 18  
686  1 Y 1 C SER -4  ? C SER 19  
687  1 Y 1 C GLY -3  ? C GLY 20  
688  1 Y 1 C GLY -2  ? C GLY 21  
689  1 Y 1 C GLY -1  ? C GLY 22  
690  1 Y 1 C ALA 0   ? C ALA 23  
691  1 Y 1 C GLY 1   ? C GLY 24  
692  1 Y 1 C GLY 2   ? C GLY 25  
693  1 Y 1 C ARG 3   ? C ARG 26  
694  1 Y 1 C LEU 4   ? C LEU 27  
695  1 Y 1 C ALA 5   ? C ALA 28  
696  1 Y 1 C LEU 6   ? C LEU 29  
697  1 Y 1 C ILE 7   ? C ILE 30  
698  1 Y 1 C TRP 8   ? C TRP 31  
699  1 Y 1 C ILE 9   ? C ILE 32  
700  1 Y 1 C VAL 10  ? C VAL 33  
701  1 Y 1 C PRO 11  ? C PRO 34  
702  1 Y 1 C LEU 12  ? C LEU 35  
703  1 Y 1 C THR 13  ? C THR 36  
704  1 Y 1 C LEU 14  ? C LEU 37  
705  1 Y 1 C GLY 15  ? C GLY 38  
706  1 Y 1 C GLY 16  ? C GLY 39  
707  1 Y 1 C LEU 17  ? C LEU 40  
708  1 Y 1 C LEU 18  ? C LEU 41  
709  1 Y 1 C GLY 19  ? C GLY 42  
710  1 Y 1 C VAL 20  ? C VAL 43  
711  1 Y 1 C ALA 21  ? C ALA 44  
712  1 Y 1 C TRP 22  ? C TRP 45  
713  1 Y 1 C GLY 23  ? C GLY 46  
714  1 Y 1 C ALA 24  ? C ALA 47  
715  1 Y 1 C SER 25  ? C SER 48  
716  1 Y 1 C SER 26  ? C SER 49  
717  1 Y 1 C LEU 27  ? C LEU 50  
718  1 Y 1 C GLY 28  ? C GLY 51  
719  1 Y 1 C ALA 29  ? C ALA 52  
720  1 Y 1 C HIS 30  ? C HIS 53  
721  1 Y 1 C HIS 31  ? C HIS 54  
722  1 Y 1 C ILE 32  ? C ILE 55  
723  1 Y 1 C HIS 33  ? C HIS 56  
724  1 Y 1 C HIS 34  ? C HIS 57  
725  1 Y 1 C PHE 35  ? C PHE 58  
726  1 Y 1 C HIS 36  ? C HIS 59  
727  1 Y 1 C GLY 37  ? C GLY 60  
728  1 Y 1 C SER 38  ? C SER 61  
729  1 Y 1 C SER 39  ? C SER 62  
730  1 Y 1 C LYS 40  ? C LYS 63  
731  1 Y 1 C GLU 41  ? C GLU 64  
732  1 Y 1 C PHE 42  ? C PHE 65  
733  1 Y 1 C GLU 43  ? C GLU 66  
734  1 Y 1 C GLN 44  ? C GLN 67  
735  1 Y 1 C LYS 45  ? C LYS 68  
736  1 Y 1 C LEU 46  ? C LEU 69  
737  1 Y 1 C ILE 47  ? C ILE 70  
738  1 Y 1 C SER 48  ? C SER 71  
739  1 Y 1 C GLU 49  ? C GLU 72  
740  1 Y 1 C GLU 50  ? C GLU 73  
741  1 Y 1 C ASP 51  ? C ASP 74  
742  1 Y 1 C LEU 52  ? C LEU 75  
743  1 Y 1 C GLY 53  ? C GLY 76  
744  1 Y 1 C PHE 54  ? C PHE 77  
745  1 Y 1 C GLU 55  ? C GLU 78  
746  1 Y 1 C ILE 56  ? C ILE 79  
747  1 Y 1 C ASP 57  ? C ASP 80  
748  1 Y 1 C LYS 58  ? C LYS 81  
749  1 Y 1 C VAL 59  ? C VAL 82  
750  1 Y 1 C TRP 60  ? C TRP 83  
751  1 Y 1 C HIS 61  ? C HIS 84  
752  1 Y 1 C ASP 62  ? C ASP 85  
753  1 Y 1 C PHE 63  ? C PHE 86  
754  1 Y 1 C PRO 64  ? C PRO 87  
755  1 Y 1 C ALA 65  ? C ALA 88  
756  1 Y 1 C THR 66  ? C THR 89  
757  1 Y 1 C SER 67  ? C SER 90  
758  1 Y 1 C PRO 68  ? C PRO 91  
759  1 Y 1 C ILE 69  ? C ILE 92  
760  1 Y 1 C ALA 70  ? C ALA 93  
761  1 Y 1 C ILE 71  ? C ILE 94  
762  1 Y 1 C TYR 72  ? C TYR 95  
763  1 Y 1 C ARG 73  ? C ARG 96  
764  1 Y 1 C SER 74  ? C SER 97  
765  1 Y 1 C PRO 75  ? C PRO 98  
766  1 Y 1 C ALA 76  ? C ALA 99  
767  1 Y 1 C SER 77  ? C SER 100 
768  1 Y 1 C LEU 78  ? C LEU 101 
769  1 Y 1 C ARG 79  ? C ARG 102 
770  1 Y 1 C GLY 80  ? C GLY 103 
771  1 Y 1 C GLY 81  ? C GLY 104 
772  1 Y 1 C HIS 82  ? C HIS 105 
773  1 Y 1 C GLU 290 ? C GLU 283 
774  1 Y 1 C VAL 291 ? C VAL 284 
775  1 Y 1 C PRO 292 ? C PRO 285 
776  1 Y 1 C SER 293 ? C SER 286 
777  1 Y 1 C SER 294 ? C SER 287 
778  1 Y 1 C MET 295 ? C MET 288 
779  1 Y 1 C THR 296 ? C THR 289 
780  1 Y 1 C THR 297 ? C THR 290 
781  1 Y 1 C GLU 298 ? C GLU 291 
782  1 Y 1 C SER 299 ? C SER 292 
783  1 Y 1 C THR 300 ? C THR 293 
784  1 Y 1 C ALA 301 ? C ALA 294 
785  1 Y 1 C THR 302 ? C THR 295 
786  1 Y 1 C ALA 303 ? C ALA 296 
787  1 Y 1 C MET 304 ? C MET 297 
788  1 Y 1 C GLN 305 ? C GLN 298 
789  1 Y 1 C SER 306 ? C SER 299 
790  1 Y 1 C GLU 307 ? C GLU 300 
791  1 Y 1 C MET 308 ? C MET 301 
792  1 Y 1 C SER 309 ? C SER 302 
793  1 Y 1 C THR 310 ? C THR 303 
794  1 Y 1 C SER 311 ? C SER 304 
795  1 Y 1 C ILE 312 ? C ILE 305 
796  1 Y 1 C MET 313 ? C MET 306 
797  1 Y 1 C GLU 314 ? C GLU 307 
798  1 Y 1 C THR 315 ? C THR 308 
799  1 Y 1 C THR 316 ? C THR 309 
800  1 Y 1 C THR 317 ? C THR 310 
801  1 Y 1 C THR 318 ? C THR 311 
802  1 Y 1 C LEU 319 ? C LEU 312 
803  1 Y 1 C ALA 320 ? C ALA 313 
804  1 Y 1 C THR 321 ? C THR 314 
805  1 Y 1 C SER 322 ? C SER 315 
806  1 Y 1 C THR 323 ? C THR 316 
807  1 Y 1 C ALA 324 ? C ALA 317 
808  1 Y 1 C ARG 325 ? C ARG 318 
809  1 Y 1 C ARG 326 ? C ARG 319 
810  1 Y 1 C GLY 327 ? C GLY 320 
811  1 Y 1 C LYS 328 ? C LYS 321 
812  1 Y 1 C PRO 329 ? C PRO 322 
813  1 Y 1 C PRO 330 ? C PRO 323 
814  1 Y 1 C THR 331 ? C THR 324 
815  1 Y 1 C LYS 332 ? C LYS 325 
816  1 Y 1 C GLU 333 ? C GLU 326 
817  1 Y 1 C PRO 334 ? C PRO 327 
818  1 Y 1 C ILE 335 ? C ILE 328 
819  1 Y 1 C SER 336 ? C SER 329 
820  1 Y 1 C GLN 337 ? C GLN 330 
821  1 Y 1 C THR 338 ? C THR 331 
822  1 Y 1 C THR 339 ? C THR 332 
823  1 Y 1 C ASP 340 ? C ASP 333 
824  1 Y 1 C ASP 341 ? C ASP 334 
825  1 Y 1 C ILE 342 ? C ILE 335 
826  1 Y 1 C LEU 343 ? C LEU 336 
827  1 Y 1 C VAL 344 ? C VAL 337 
828  1 Y 1 C ALA 345 ? C ALA 338 
829  1 Y 1 C SER 346 ? C SER 339 
830  1 Y 1 C ALA 347 ? C ALA 340 
831  1 Y 1 C GLU 348 ? C GLU 341 
832  1 Y 1 C CYS 349 ? C CYS 342 
833  1 Y 1 C PRO 350 ? C PRO 343 
834  1 Y 1 C SER 351 ? C SER 344 
835  1 Y 1 C ASP 352 ? C ASP 345 
836  1 Y 1 C ASP 353 ? C ASP 346 
837  1 Y 1 C GLU 354 ? C GLU 347 
838  1 Y 1 C ASP 355 ? C ASP 348 
839  1 Y 1 C ILE 356 ? C ILE 349 
840  1 Y 1 C ASP 357 ? C ASP 350 
841  1 Y 1 C PRO 358 ? C PRO 351 
842  1 Y 1 C CYS 359 ? C CYS 352 
843  1 Y 1 C GLU 360 ? C GLU 353 
844  1 Y 1 C PRO 361 ? C PRO 354 
845  1 Y 1 C SER 362 ? C SER 355 
846  1 Y 1 C SER 363 ? C SER 356 
847  1 Y 1 C GLY 364 ? C GLY 357 
848  1 Y 1 C GLY 365 ? C GLY 358 
849  1 Y 1 C LEU 366 ? C LEU 359 
850  1 Y 1 C ALA 367 ? C ALA 360 
851  1 Y 1 C ASN 368 ? C ASN 361 
852  1 Y 1 C PRO 369 ? C PRO 362 
853  1 Y 1 C THR 370 ? C THR 363 
854  1 Y 1 C ARG 371 ? C ARG 364 
855  1 Y 1 C VAL 372 ? C VAL 365 
856  1 Y 1 C GLY 373 ? C GLY 366 
857  1 Y 1 C GLY 374 ? C GLY 367 
858  1 Y 1 C ARG 375 ? C ARG 368 
859  1 Y 1 C GLU 376 ? C GLU 369 
860  1 Y 1 C PRO 377 ? C PRO 370 
861  1 Y 1 C TYR 378 ? C TYR 371 
862  1 Y 1 C PRO 379 ? C PRO 372 
863  1 Y 1 C GLY 380 ? C GLY 373 
864  1 Y 1 C SER 381 ? C SER 374 
865  1 Y 1 C ALA 382 ? C ALA 375 
866  1 Y 1 C GLU 383 ? C GLU 376 
867  1 Y 1 C VAL 384 ? C VAL 377 
868  1 Y 1 C ILE 385 ? C ILE 378 
869  1 Y 1 C ARG 386 ? C ARG 379 
870  1 Y 1 C GLU 387 ? C GLU 380 
871  1 Y 1 C SER 388 ? C SER 381 
872  1 Y 1 C SER 389 ? C SER 382 
873  1 Y 1 C SER 390 ? C SER 383 
874  1 Y 1 C THR 391 ? C THR 384 
875  1 Y 1 C THR 392 ? C THR 385 
876  1 Y 1 C GLY 393 ? C GLY 386 
877  1 Y 1 C MET 394 ? C MET 387 
878  1 Y 1 C VAL 395 ? C VAL 388 
879  1 Y 1 C VAL 396 ? C VAL 389 
880  1 Y 1 C GLY 397 ? C GLY 390 
881  1 Y 1 C ILE 398 ? C ILE 391 
882  1 Y 1 C VAL 399 ? C VAL 392 
883  1 Y 1 C ALA 400 ? C ALA 393 
884  1 Y 1 C ALA 401 ? C ALA 394 
885  1 Y 1 C ALA 402 ? C ALA 395 
886  1 Y 1 C ALA 403 ? C ALA 396 
887  1 Y 1 C LEU 404 ? C LEU 397 
888  1 Y 1 C CYS 405 ? C CYS 398 
889  1 Y 1 C ILE 406 ? C ILE 399 
890  1 Y 1 C LEU 407 ? C LEU 400 
891  1 Y 1 C ILE 408 ? C ILE 401 
892  1 Y 1 C LEU 409 ? C LEU 402 
893  1 Y 1 C LEU 410 ? C LEU 403 
894  1 Y 1 C TYR 411 ? C TYR 404 
895  1 Y 1 C ALA 412 ? C ALA 405 
896  1 Y 1 C MET 413 ? C MET 406 
897  1 Y 1 C TYR 414 ? C TYR 407 
898  1 Y 1 C LYS 415 ? C LYS 408 
899  1 Y 1 C TYR 416 ? C TYR 409 
900  1 Y 1 C ARG 417 ? C ARG 410 
901  1 Y 1 C ASN 418 ? C ASN 411 
902  1 Y 1 C ARG 419 ? C ARG 412 
903  1 Y 1 C ASP 420 ? C ASP 413 
904  1 Y 1 C GLU 421 ? C GLU 414 
905  1 Y 1 C GLY 422 ? C GLY 415 
906  1 Y 1 C SER 423 ? C SER 416 
907  1 Y 1 C TYR 424 ? C TYR 417 
908  1 Y 1 C HIS 425 ? C HIS 418 
909  1 Y 1 C VAL 426 ? C VAL 419 
910  1 Y 1 C ASP 427 ? C ASP 420 
911  1 Y 1 C GLU 428 ? C GLU 421 
912  1 Y 1 C SER 429 ? C SER 422 
913  1 Y 1 C ARG 430 ? C ARG 423 
914  1 Y 1 C ASN 431 ? C ASN 424 
915  1 Y 1 C TYR 432 ? C TYR 425 
916  1 Y 1 C ILE 433 ? C ILE 426 
917  1 Y 1 C SER 434 ? C SER 427 
918  1 Y 1 C ASN 435 ? C ASN 428 
919  1 Y 1 C SER 436 ? C SER 429 
920  1 Y 1 C ALA 437 ? C ALA 430 
921  1 Y 1 C GLN 438 ? C GLN 431 
922  1 Y 1 C SER 439 ? C SER 432 
923  1 Y 1 C ASN 440 ? C ASN 433 
924  1 Y 1 C GLY 441 ? C GLY 434 
925  1 Y 1 C ALA 442 ? C ALA 435 
926  1 Y 1 C VAL 443 ? C VAL 436 
927  1 Y 1 C VAL 444 ? C VAL 437 
928  1 Y 1 C LYS 445 ? C LYS 438 
929  1 Y 1 C GLU 446 ? C GLU 439 
930  1 Y 1 C LYS 447 ? C LYS 440 
931  1 Y 1 C GLN 448 ? C GLN 441 
932  1 Y 1 C PRO 449 ? C PRO 442 
933  1 Y 1 C SER 450 ? C SER 443 
934  1 Y 1 C SER 451 ? C SER 444 
935  1 Y 1 C ALA 452 ? C ALA 445 
936  1 Y 1 C LYS 453 ? C LYS 446 
937  1 Y 1 C SER 454 ? C SER 447 
938  1 Y 1 C ALA 455 ? C ALA 448 
939  1 Y 1 C ASN 456 ? C ASN 449 
940  1 Y 1 C LYS 457 ? C LYS 450 
941  1 Y 1 C ASN 458 ? C ASN 451 
942  1 Y 1 C LYS 459 ? C LYS 452 
943  1 Y 1 C LYS 460 ? C LYS 453 
944  1 Y 1 C ASN 461 ? C ASN 454 
945  1 Y 1 C LYS 462 ? C LYS 455 
946  1 Y 1 C ASP 463 ? C ASP 456 
947  1 Y 1 C LYS 464 ? C LYS 457 
948  1 Y 1 C GLU 465 ? C GLU 458 
949  1 Y 1 C TYR 466 ? C TYR 459 
950  1 Y 1 C TYR 467 ? C TYR 460 
951  1 Y 1 C VAL 468 ? C VAL 461 
952  1 Y 1 C SER 469 ? C SER 462 
953  1 Y 1 C ASN 470 ? C ASN 463 
954  1 Y 1 C SER 471 ? C SER 464 
955  1 Y 1 C LEU 472 ? C LEU 465 
956  1 Y 1 C GLU 473 ? C GLU 466 
957  1 Y 1 C VAL 474 ? C VAL 467 
958  1 Y 1 C LEU 475 ? C LEU 468 
959  1 Y 1 C PHE 476 ? C PHE 469 
960  1 Y 1 C GLN 477 ? C GLN 470 
961  1 Y 1 D MET -22 ? D MET 1   
962  1 Y 1 D TYR -21 ? D TYR 2   
963  1 Y 1 D GLN -20 ? D GLN 3   
964  1 Y 1 D ARG -19 ? D ARG 4   
965  1 Y 1 D MET -18 ? D MET 5   
966  1 Y 1 D LEU -17 ? D LEU 6   
967  1 Y 1 D ARG -16 ? D ARG 7   
968  1 Y 1 D CYS -15 ? D CYS 8   
969  1 Y 1 D GLY -14 ? D GLY 9   
970  1 Y 1 D ALA -13 ? D ALA 10  
971  1 Y 1 D ASP -12 ? D ASP 11  
972  1 Y 1 D LEU -11 ? D LEU 12  
973  1 Y 1 D GLY -10 ? D GLY 13  
974  1 Y 1 D SER -9  ? D SER 14  
975  1 Y 1 D PRO -8  ? D PRO 15  
976  1 Y 1 D GLY -7  ? D GLY 16  
977  1 Y 1 D GLY -6  ? D GLY 17  
978  1 Y 1 D GLY -5  ? D GLY 18  
979  1 Y 1 D SER -4  ? D SER 19  
980  1 Y 1 D GLY -3  ? D GLY 20  
981  1 Y 1 D GLY -2  ? D GLY 21  
982  1 Y 1 D GLY -1  ? D GLY 22  
983  1 Y 1 D ALA 0   ? D ALA 23  
984  1 Y 1 D GLY 1   ? D GLY 24  
985  1 Y 1 D GLY 2   ? D GLY 25  
986  1 Y 1 D ARG 3   ? D ARG 26  
987  1 Y 1 D LEU 4   ? D LEU 27  
988  1 Y 1 D ALA 5   ? D ALA 28  
989  1 Y 1 D LEU 6   ? D LEU 29  
990  1 Y 1 D ILE 7   ? D ILE 30  
991  1 Y 1 D TRP 8   ? D TRP 31  
992  1 Y 1 D ILE 9   ? D ILE 32  
993  1 Y 1 D VAL 10  ? D VAL 33  
994  1 Y 1 D PRO 11  ? D PRO 34  
995  1 Y 1 D LEU 12  ? D LEU 35  
996  1 Y 1 D THR 13  ? D THR 36  
997  1 Y 1 D LEU 14  ? D LEU 37  
998  1 Y 1 D GLY 15  ? D GLY 38  
999  1 Y 1 D GLY 16  ? D GLY 39  
1000 1 Y 1 D LEU 17  ? D LEU 40  
1001 1 Y 1 D LEU 18  ? D LEU 41  
1002 1 Y 1 D GLY 19  ? D GLY 42  
1003 1 Y 1 D VAL 20  ? D VAL 43  
1004 1 Y 1 D ALA 21  ? D ALA 44  
1005 1 Y 1 D TRP 22  ? D TRP 45  
1006 1 Y 1 D GLY 23  ? D GLY 46  
1007 1 Y 1 D ALA 24  ? D ALA 47  
1008 1 Y 1 D SER 25  ? D SER 48  
1009 1 Y 1 D SER 26  ? D SER 49  
1010 1 Y 1 D LEU 27  ? D LEU 50  
1011 1 Y 1 D GLY 28  ? D GLY 51  
1012 1 Y 1 D ALA 29  ? D ALA 52  
1013 1 Y 1 D HIS 30  ? D HIS 53  
1014 1 Y 1 D HIS 31  ? D HIS 54  
1015 1 Y 1 D ILE 32  ? D ILE 55  
1016 1 Y 1 D HIS 33  ? D HIS 56  
1017 1 Y 1 D HIS 34  ? D HIS 57  
1018 1 Y 1 D PHE 35  ? D PHE 58  
1019 1 Y 1 D HIS 36  ? D HIS 59  
1020 1 Y 1 D GLY 37  ? D GLY 60  
1021 1 Y 1 D SER 38  ? D SER 61  
1022 1 Y 1 D SER 39  ? D SER 62  
1023 1 Y 1 D LYS 40  ? D LYS 63  
1024 1 Y 1 D GLU 41  ? D GLU 64  
1025 1 Y 1 D PHE 42  ? D PHE 65  
1026 1 Y 1 D GLU 43  ? D GLU 66  
1027 1 Y 1 D GLN 44  ? D GLN 67  
1028 1 Y 1 D LYS 45  ? D LYS 68  
1029 1 Y 1 D LEU 46  ? D LEU 69  
1030 1 Y 1 D ILE 47  ? D ILE 70  
1031 1 Y 1 D SER 48  ? D SER 71  
1032 1 Y 1 D GLU 49  ? D GLU 72  
1033 1 Y 1 D GLU 50  ? D GLU 73  
1034 1 Y 1 D ASP 51  ? D ASP 74  
1035 1 Y 1 D LEU 52  ? D LEU 75  
1036 1 Y 1 D GLY 53  ? D GLY 76  
1037 1 Y 1 D PHE 54  ? D PHE 77  
1038 1 Y 1 D GLU 55  ? D GLU 78  
1039 1 Y 1 D ILE 56  ? D ILE 79  
1040 1 Y 1 D ASP 57  ? D ASP 80  
1041 1 Y 1 D LYS 58  ? D LYS 81  
1042 1 Y 1 D VAL 59  ? D VAL 82  
1043 1 Y 1 D TRP 60  ? D TRP 83  
1044 1 Y 1 D HIS 61  ? D HIS 84  
1045 1 Y 1 D ASP 62  ? D ASP 85  
1046 1 Y 1 D PHE 63  ? D PHE 86  
1047 1 Y 1 D PRO 64  ? D PRO 87  
1048 1 Y 1 D ALA 65  ? D ALA 88  
1049 1 Y 1 D THR 66  ? D THR 89  
1050 1 Y 1 D SER 67  ? D SER 90  
1051 1 Y 1 D PRO 68  ? D PRO 91  
1052 1 Y 1 D ILE 69  ? D ILE 92  
1053 1 Y 1 D ALA 70  ? D ALA 93  
1054 1 Y 1 D ILE 71  ? D ILE 94  
1055 1 Y 1 D TYR 72  ? D TYR 95  
1056 1 Y 1 D ARG 73  ? D ARG 96  
1057 1 Y 1 D SER 74  ? D SER 97  
1058 1 Y 1 D PRO 75  ? D PRO 98  
1059 1 Y 1 D ALA 76  ? D ALA 99  
1060 1 Y 1 D SER 77  ? D SER 100 
1061 1 Y 1 D LEU 78  ? D LEU 101 
1062 1 Y 1 D ARG 79  ? D ARG 102 
1063 1 Y 1 D GLY 80  ? D GLY 103 
1064 1 Y 1 D GLY 81  ? D GLY 104 
1065 1 Y 1 D HIS 82  ? D HIS 105 
1066 1 Y 1 D GLU 290 ? D GLU 283 
1067 1 Y 1 D VAL 291 ? D VAL 284 
1068 1 Y 1 D PRO 292 ? D PRO 285 
1069 1 Y 1 D SER 293 ? D SER 286 
1070 1 Y 1 D SER 294 ? D SER 287 
1071 1 Y 1 D MET 295 ? D MET 288 
1072 1 Y 1 D THR 296 ? D THR 289 
1073 1 Y 1 D THR 297 ? D THR 290 
1074 1 Y 1 D GLU 298 ? D GLU 291 
1075 1 Y 1 D SER 299 ? D SER 292 
1076 1 Y 1 D THR 300 ? D THR 293 
1077 1 Y 1 D ALA 301 ? D ALA 294 
1078 1 Y 1 D THR 302 ? D THR 295 
1079 1 Y 1 D ALA 303 ? D ALA 296 
1080 1 Y 1 D MET 304 ? D MET 297 
1081 1 Y 1 D GLN 305 ? D GLN 298 
1082 1 Y 1 D SER 306 ? D SER 299 
1083 1 Y 1 D GLU 307 ? D GLU 300 
1084 1 Y 1 D MET 308 ? D MET 301 
1085 1 Y 1 D SER 309 ? D SER 302 
1086 1 Y 1 D THR 310 ? D THR 303 
1087 1 Y 1 D SER 311 ? D SER 304 
1088 1 Y 1 D ILE 312 ? D ILE 305 
1089 1 Y 1 D MET 313 ? D MET 306 
1090 1 Y 1 D GLU 314 ? D GLU 307 
1091 1 Y 1 D THR 315 ? D THR 308 
1092 1 Y 1 D THR 316 ? D THR 309 
1093 1 Y 1 D THR 317 ? D THR 310 
1094 1 Y 1 D THR 318 ? D THR 311 
1095 1 Y 1 D LEU 319 ? D LEU 312 
1096 1 Y 1 D ALA 320 ? D ALA 313 
1097 1 Y 1 D THR 321 ? D THR 314 
1098 1 Y 1 D SER 322 ? D SER 315 
1099 1 Y 1 D THR 323 ? D THR 316 
1100 1 Y 1 D ALA 324 ? D ALA 317 
1101 1 Y 1 D ARG 325 ? D ARG 318 
1102 1 Y 1 D ARG 326 ? D ARG 319 
1103 1 Y 1 D GLY 327 ? D GLY 320 
1104 1 Y 1 D LYS 328 ? D LYS 321 
1105 1 Y 1 D PRO 329 ? D PRO 322 
1106 1 Y 1 D PRO 330 ? D PRO 323 
1107 1 Y 1 D THR 331 ? D THR 324 
1108 1 Y 1 D LYS 332 ? D LYS 325 
1109 1 Y 1 D GLU 333 ? D GLU 326 
1110 1 Y 1 D PRO 334 ? D PRO 327 
1111 1 Y 1 D ILE 335 ? D ILE 328 
1112 1 Y 1 D SER 336 ? D SER 329 
1113 1 Y 1 D GLN 337 ? D GLN 330 
1114 1 Y 1 D THR 338 ? D THR 331 
1115 1 Y 1 D THR 339 ? D THR 332 
1116 1 Y 1 D ASP 340 ? D ASP 333 
1117 1 Y 1 D ASP 341 ? D ASP 334 
1118 1 Y 1 D ILE 342 ? D ILE 335 
1119 1 Y 1 D LEU 343 ? D LEU 336 
1120 1 Y 1 D VAL 344 ? D VAL 337 
1121 1 Y 1 D ALA 345 ? D ALA 338 
1122 1 Y 1 D SER 346 ? D SER 339 
1123 1 Y 1 D ALA 347 ? D ALA 340 
1124 1 Y 1 D GLU 348 ? D GLU 341 
1125 1 Y 1 D CYS 349 ? D CYS 342 
1126 1 Y 1 D PRO 350 ? D PRO 343 
1127 1 Y 1 D SER 351 ? D SER 344 
1128 1 Y 1 D ASP 352 ? D ASP 345 
1129 1 Y 1 D ASP 353 ? D ASP 346 
1130 1 Y 1 D GLU 354 ? D GLU 347 
1131 1 Y 1 D ASP 355 ? D ASP 348 
1132 1 Y 1 D ILE 356 ? D ILE 349 
1133 1 Y 1 D ASP 357 ? D ASP 350 
1134 1 Y 1 D PRO 358 ? D PRO 351 
1135 1 Y 1 D CYS 359 ? D CYS 352 
1136 1 Y 1 D GLU 360 ? D GLU 353 
1137 1 Y 1 D PRO 361 ? D PRO 354 
1138 1 Y 1 D SER 362 ? D SER 355 
1139 1 Y 1 D SER 363 ? D SER 356 
1140 1 Y 1 D GLY 364 ? D GLY 357 
1141 1 Y 1 D GLY 365 ? D GLY 358 
1142 1 Y 1 D LEU 366 ? D LEU 359 
1143 1 Y 1 D ALA 367 ? D ALA 360 
1144 1 Y 1 D ASN 368 ? D ASN 361 
1145 1 Y 1 D PRO 369 ? D PRO 362 
1146 1 Y 1 D THR 370 ? D THR 363 
1147 1 Y 1 D ARG 371 ? D ARG 364 
1148 1 Y 1 D VAL 372 ? D VAL 365 
1149 1 Y 1 D GLY 373 ? D GLY 366 
1150 1 Y 1 D GLY 374 ? D GLY 367 
1151 1 Y 1 D ARG 375 ? D ARG 368 
1152 1 Y 1 D GLU 376 ? D GLU 369 
1153 1 Y 1 D PRO 377 ? D PRO 370 
1154 1 Y 1 D TYR 378 ? D TYR 371 
1155 1 Y 1 D PRO 379 ? D PRO 372 
1156 1 Y 1 D GLY 380 ? D GLY 373 
1157 1 Y 1 D SER 381 ? D SER 374 
1158 1 Y 1 D ALA 382 ? D ALA 375 
1159 1 Y 1 D GLU 383 ? D GLU 376 
1160 1 Y 1 D VAL 384 ? D VAL 377 
1161 1 Y 1 D ILE 385 ? D ILE 378 
1162 1 Y 1 D ARG 386 ? D ARG 379 
1163 1 Y 1 D GLU 387 ? D GLU 380 
1164 1 Y 1 D SER 388 ? D SER 381 
1165 1 Y 1 D SER 389 ? D SER 382 
1166 1 Y 1 D SER 390 ? D SER 383 
1167 1 Y 1 D THR 391 ? D THR 384 
1168 1 Y 1 D THR 392 ? D THR 385 
1169 1 Y 1 D GLY 393 ? D GLY 386 
1170 1 Y 1 D MET 394 ? D MET 387 
1171 1 Y 1 D VAL 395 ? D VAL 388 
1172 1 Y 1 D VAL 396 ? D VAL 389 
1173 1 Y 1 D GLY 397 ? D GLY 390 
1174 1 Y 1 D ILE 398 ? D ILE 391 
1175 1 Y 1 D VAL 399 ? D VAL 392 
1176 1 Y 1 D ALA 400 ? D ALA 393 
1177 1 Y 1 D ALA 401 ? D ALA 394 
1178 1 Y 1 D ALA 402 ? D ALA 395 
1179 1 Y 1 D ALA 403 ? D ALA 396 
1180 1 Y 1 D LEU 404 ? D LEU 397 
1181 1 Y 1 D CYS 405 ? D CYS 398 
1182 1 Y 1 D ILE 406 ? D ILE 399 
1183 1 Y 1 D LEU 407 ? D LEU 400 
1184 1 Y 1 D ILE 408 ? D ILE 401 
1185 1 Y 1 D LEU 409 ? D LEU 402 
1186 1 Y 1 D LEU 410 ? D LEU 403 
1187 1 Y 1 D TYR 411 ? D TYR 404 
1188 1 Y 1 D ALA 412 ? D ALA 405 
1189 1 Y 1 D MET 413 ? D MET 406 
1190 1 Y 1 D TYR 414 ? D TYR 407 
1191 1 Y 1 D LYS 415 ? D LYS 408 
1192 1 Y 1 D TYR 416 ? D TYR 409 
1193 1 Y 1 D ARG 417 ? D ARG 410 
1194 1 Y 1 D ASN 418 ? D ASN 411 
1195 1 Y 1 D ARG 419 ? D ARG 412 
1196 1 Y 1 D ASP 420 ? D ASP 413 
1197 1 Y 1 D GLU 421 ? D GLU 414 
1198 1 Y 1 D GLY 422 ? D GLY 415 
1199 1 Y 1 D SER 423 ? D SER 416 
1200 1 Y 1 D TYR 424 ? D TYR 417 
1201 1 Y 1 D HIS 425 ? D HIS 418 
1202 1 Y 1 D VAL 426 ? D VAL 419 
1203 1 Y 1 D ASP 427 ? D ASP 420 
1204 1 Y 1 D GLU 428 ? D GLU 421 
1205 1 Y 1 D SER 429 ? D SER 422 
1206 1 Y 1 D ARG 430 ? D ARG 423 
1207 1 Y 1 D ASN 431 ? D ASN 424 
1208 1 Y 1 D TYR 432 ? D TYR 425 
1209 1 Y 1 D ILE 433 ? D ILE 426 
1210 1 Y 1 D SER 434 ? D SER 427 
1211 1 Y 1 D ASN 435 ? D ASN 428 
1212 1 Y 1 D SER 436 ? D SER 429 
1213 1 Y 1 D ALA 437 ? D ALA 430 
1214 1 Y 1 D GLN 438 ? D GLN 431 
1215 1 Y 1 D SER 439 ? D SER 432 
1216 1 Y 1 D ASN 440 ? D ASN 433 
1217 1 Y 1 D GLY 441 ? D GLY 434 
1218 1 Y 1 D ALA 442 ? D ALA 435 
1219 1 Y 1 D VAL 443 ? D VAL 436 
1220 1 Y 1 D VAL 444 ? D VAL 437 
1221 1 Y 1 D LYS 445 ? D LYS 438 
1222 1 Y 1 D GLU 446 ? D GLU 439 
1223 1 Y 1 D LYS 447 ? D LYS 440 
1224 1 Y 1 D GLN 448 ? D GLN 441 
1225 1 Y 1 D PRO 449 ? D PRO 442 
1226 1 Y 1 D SER 450 ? D SER 443 
1227 1 Y 1 D SER 451 ? D SER 444 
1228 1 Y 1 D ALA 452 ? D ALA 445 
1229 1 Y 1 D LYS 453 ? D LYS 446 
1230 1 Y 1 D SER 454 ? D SER 447 
1231 1 Y 1 D ALA 455 ? D ALA 448 
1232 1 Y 1 D ASN 456 ? D ASN 449 
1233 1 Y 1 D LYS 457 ? D LYS 450 
1234 1 Y 1 D ASN 458 ? D ASN 451 
1235 1 Y 1 D LYS 459 ? D LYS 452 
1236 1 Y 1 D LYS 460 ? D LYS 453 
1237 1 Y 1 D ASN 461 ? D ASN 454 
1238 1 Y 1 D LYS 462 ? D LYS 455 
1239 1 Y 1 D ASP 463 ? D ASP 456 
1240 1 Y 1 D LYS 464 ? D LYS 457 
1241 1 Y 1 D GLU 465 ? D GLU 458 
1242 1 Y 1 D TYR 466 ? D TYR 459 
1243 1 Y 1 D TYR 467 ? D TYR 460 
1244 1 Y 1 D VAL 468 ? D VAL 461 
1245 1 Y 1 D SER 469 ? D SER 462 
1246 1 Y 1 D ASN 470 ? D ASN 463 
1247 1 Y 1 D SER 471 ? D SER 464 
1248 1 Y 1 D LEU 472 ? D LEU 465 
1249 1 Y 1 D GLU 473 ? D GLU 466 
1250 1 Y 1 D VAL 474 ? D VAL 467 
1251 1 Y 1 D LEU 475 ? D LEU 468 
1252 1 Y 1 D PHE 476 ? D PHE 469 
1253 1 Y 1 D GLN 477 ? D GLN 470 
# 
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  
CA  CA   CA N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
ILE N    N  N N 159 
ILE CA   C  N S 160 
ILE C    C  N N 161 
ILE O    O  N N 162 
ILE CB   C  N S 163 
ILE CG1  C  N N 164 
ILE CG2  C  N N 165 
ILE CD1  C  N N 166 
ILE OXT  O  N N 167 
ILE H    H  N N 168 
ILE H2   H  N N 169 
ILE HA   H  N N 170 
ILE HB   H  N N 171 
ILE HG12 H  N N 172 
ILE HG13 H  N N 173 
ILE HG21 H  N N 174 
ILE HG22 H  N N 175 
ILE HG23 H  N N 176 
ILE HD11 H  N N 177 
ILE HD12 H  N N 178 
ILE HD13 H  N N 179 
ILE HXT  H  N N 180 
LEU N    N  N N 181 
LEU CA   C  N S 182 
LEU C    C  N N 183 
LEU O    O  N N 184 
LEU CB   C  N N 185 
LEU CG   C  N N 186 
LEU CD1  C  N N 187 
LEU CD2  C  N N 188 
LEU OXT  O  N N 189 
LEU H    H  N N 190 
LEU H2   H  N N 191 
LEU HA   H  N N 192 
LEU HB2  H  N N 193 
LEU HB3  H  N N 194 
LEU HG   H  N N 195 
LEU HD11 H  N N 196 
LEU HD12 H  N N 197 
LEU HD13 H  N N 198 
LEU HD21 H  N N 199 
LEU HD22 H  N N 200 
LEU HD23 H  N N 201 
LEU HXT  H  N N 202 
LYS N    N  N N 203 
LYS CA   C  N S 204 
LYS C    C  N N 205 
LYS O    O  N N 206 
LYS CB   C  N N 207 
LYS CG   C  N N 208 
LYS CD   C  N N 209 
LYS CE   C  N N 210 
LYS NZ   N  N N 211 
LYS OXT  O  N N 212 
LYS H    H  N N 213 
LYS H2   H  N N 214 
LYS HA   H  N N 215 
LYS HB2  H  N N 216 
LYS HB3  H  N N 217 
LYS HG2  H  N N 218 
LYS HG3  H  N N 219 
LYS HD2  H  N N 220 
LYS HD3  H  N N 221 
LYS HE2  H  N N 222 
LYS HE3  H  N N 223 
LYS HZ1  H  N N 224 
LYS HZ2  H  N N 225 
LYS HZ3  H  N N 226 
LYS HXT  H  N N 227 
MET N    N  N N 228 
MET CA   C  N S 229 
MET C    C  N N 230 
MET O    O  N N 231 
MET CB   C  N N 232 
MET CG   C  N N 233 
MET SD   S  N N 234 
MET CE   C  N N 235 
MET OXT  O  N N 236 
MET H    H  N N 237 
MET H2   H  N N 238 
MET HA   H  N N 239 
MET HB2  H  N N 240 
MET HB3  H  N N 241 
MET HG2  H  N N 242 
MET HG3  H  N N 243 
MET HE1  H  N N 244 
MET HE2  H  N N 245 
MET HE3  H  N N 246 
MET HXT  H  N N 247 
NAG C1   C  N R 248 
NAG C2   C  N R 249 
NAG C3   C  N R 250 
NAG C4   C  N S 251 
NAG C5   C  N R 252 
NAG C6   C  N N 253 
NAG C7   C  N N 254 
NAG C8   C  N N 255 
NAG N2   N  N N 256 
NAG O1   O  N N 257 
NAG O3   O  N N 258 
NAG O4   O  N N 259 
NAG O5   O  N N 260 
NAG O6   O  N N 261 
NAG O7   O  N N 262 
NAG H1   H  N N 263 
NAG H2   H  N N 264 
NAG H3   H  N N 265 
NAG H4   H  N N 266 
NAG H5   H  N N 267 
NAG H61  H  N N 268 
NAG H62  H  N N 269 
NAG H81  H  N N 270 
NAG H82  H  N N 271 
NAG H83  H  N N 272 
NAG HN2  H  N N 273 
NAG HO1  H  N N 274 
NAG HO3  H  N N 275 
NAG HO4  H  N N 276 
NAG HO6  H  N N 277 
PHE N    N  N N 278 
PHE CA   C  N S 279 
PHE C    C  N N 280 
PHE O    O  N N 281 
PHE CB   C  N N 282 
PHE CG   C  Y N 283 
PHE CD1  C  Y N 284 
PHE CD2  C  Y N 285 
PHE CE1  C  Y N 286 
PHE CE2  C  Y N 287 
PHE CZ   C  Y N 288 
PHE OXT  O  N N 289 
PHE H    H  N N 290 
PHE H2   H  N N 291 
PHE HA   H  N N 292 
PHE HB2  H  N N 293 
PHE HB3  H  N N 294 
PHE HD1  H  N N 295 
PHE HD2  H  N N 296 
PHE HE1  H  N N 297 
PHE HE2  H  N N 298 
PHE HZ   H  N N 299 
PHE HXT  H  N N 300 
PRO N    N  N N 301 
PRO CA   C  N S 302 
PRO C    C  N N 303 
PRO O    O  N N 304 
PRO CB   C  N N 305 
PRO CG   C  N N 306 
PRO CD   C  N N 307 
PRO OXT  O  N N 308 
PRO H    H  N N 309 
PRO HA   H  N N 310 
PRO HB2  H  N N 311 
PRO HB3  H  N N 312 
PRO HG2  H  N N 313 
PRO HG3  H  N N 314 
PRO HD2  H  N N 315 
PRO HD3  H  N N 316 
PRO HXT  H  N N 317 
SER N    N  N N 318 
SER CA   C  N S 319 
SER C    C  N N 320 
SER O    O  N N 321 
SER CB   C  N N 322 
SER OG   O  N N 323 
SER OXT  O  N N 324 
SER H    H  N N 325 
SER H2   H  N N 326 
SER HA   H  N N 327 
SER HB2  H  N N 328 
SER HB3  H  N N 329 
SER HG   H  N N 330 
SER HXT  H  N N 331 
THR N    N  N N 332 
THR CA   C  N S 333 
THR C    C  N N 334 
THR O    O  N N 335 
THR CB   C  N R 336 
THR OG1  O  N N 337 
THR CG2  C  N N 338 
THR OXT  O  N N 339 
THR H    H  N N 340 
THR H2   H  N N 341 
THR HA   H  N N 342 
THR HB   H  N N 343 
THR HG1  H  N N 344 
THR HG21 H  N N 345 
THR HG22 H  N N 346 
THR HG23 H  N N 347 
THR HXT  H  N N 348 
TRP N    N  N N 349 
TRP CA   C  N S 350 
TRP C    C  N N 351 
TRP O    O  N N 352 
TRP CB   C  N N 353 
TRP CG   C  Y N 354 
TRP CD1  C  Y N 355 
TRP CD2  C  Y N 356 
TRP NE1  N  Y N 357 
TRP CE2  C  Y N 358 
TRP CE3  C  Y N 359 
TRP CZ2  C  Y N 360 
TRP CZ3  C  Y N 361 
TRP CH2  C  Y N 362 
TRP OXT  O  N N 363 
TRP H    H  N N 364 
TRP H2   H  N N 365 
TRP HA   H  N N 366 
TRP HB2  H  N N 367 
TRP HB3  H  N N 368 
TRP HD1  H  N N 369 
TRP HE1  H  N N 370 
TRP HE3  H  N N 371 
TRP HZ2  H  N N 372 
TRP HZ3  H  N N 373 
TRP HH2  H  N N 374 
TRP HXT  H  N N 375 
TYR N    N  N N 376 
TYR CA   C  N S 377 
TYR C    C  N N 378 
TYR O    O  N N 379 
TYR CB   C  N N 380 
TYR CG   C  Y N 381 
TYR CD1  C  Y N 382 
TYR CD2  C  Y N 383 
TYR CE1  C  Y N 384 
TYR CE2  C  Y N 385 
TYR CZ   C  Y N 386 
TYR OH   O  N N 387 
TYR OXT  O  N N 388 
TYR H    H  N N 389 
TYR H2   H  N N 390 
TYR HA   H  N N 391 
TYR HB2  H  N N 392 
TYR HB3  H  N N 393 
TYR HD1  H  N N 394 
TYR HD2  H  N N 395 
TYR HE1  H  N N 396 
TYR HE2  H  N N 397 
TYR HH   H  N N 398 
TYR HXT  H  N N 399 
VAL N    N  N N 400 
VAL CA   C  N S 401 
VAL C    C  N N 402 
VAL O    O  N N 403 
VAL CB   C  N N 404 
VAL CG1  C  N N 405 
VAL CG2  C  N N 406 
VAL OXT  O  N N 407 
VAL H    H  N N 408 
VAL H2   H  N N 409 
VAL HA   H  N N 410 
VAL HB   H  N N 411 
VAL HG11 H  N N 412 
VAL HG12 H  N N 413 
VAL HG13 H  N N 414 
VAL HG21 H  N N 415 
VAL HG22 H  N N 416 
VAL HG23 H  N N 417 
VAL HXT  H  N N 418 
# 
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    2023-02-17 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           8G7Z 
_em_admin.last_update        2025-05-14 
_em_admin.map_release_date   2025-05-14 
_em_admin.title              
'Cryo-EM structure of full length Neuroligin-2 from Mouse bound to two Neurexin-1 Beta conformation one' 
# 
loop_
_em_buffer_component.buffer_id 
_em_buffer_component.concentration 
_em_buffer_component.concentration_units 
_em_buffer_component.formula 
_em_buffer_component.id 
_em_buffer_component.name 
1 20   mM C8H18N2O4S 1 HEPES                
1 150  mM NaCl       2 'Sodium Chloride'    
1 1    mM MgCl2      3 'Magnesium Chloride' 
1 0.5  mM CaCl2      4 'Calcium Chloride'   
1 0.05 %  ?          5 LMNG                 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                0.18 
# 
_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          10090 
_em_entity_assembly_naturalsource.organism             'Mus musculus' 
_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         90 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    1 
_em_image_recording.num_real_images                     6615 
# 
_em_particle_selection.details                  ? 
_em_particle_selection.id                       1 
_em_particle_selection.image_processing_id      1 
_em_particle_selection.method                   ? 
_em_particle_selection.num_particles_selected   2964465 
_em_particle_selection.reference_model          ? 
# 
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 
'MODEL REFINEMENT'              ? 1  ? ? ? PHENIX 1.20.1_4487: 
'IMAGE ACQUISITION'             ? 2  1 1 1 ?      ?            
'PARTICLE SELECTION'            ? 3  1 1 1 ?      ?            
'VOLUME SELECTION'              ? 4  1 1 1 ?      ?            
CLASSIFICATION                  ? 5  1 1 1 ?      ?            
MASKING                         ? 6  1 1 1 ?      ?            
RECONSTRUCTION                  ? 7  1 1 1 ?      ?            
'INITIAL EULER ASSIGNMENT'      ? 8  1 1 1 ?      ?            
'FINAL EULER ASSIGNMENT'        ? 9  1 1 1 ?      ?            
'CTF CORRECTION'                ? 10 1 1 1 ?      ?            
'LAYERLINE INDEXING'            ? 11 1 1 1 ?      ?            
'DIFFRACTION INDEXING'          ? 12 1 1 1 ?      ?            
'MODEL FITTING'                 ? 13 1 1 1 ?      ?            
'SERIES ALIGNMENT'              ? 14 1 1 1 ?      ?            
'MOLECULAR REPLACEMENT'         ? 15 1 1 1 ?      ?            
'LATTICE DISTORTION CORRECTION' ? 16 1 1 1 ?      ?            
'SYMMETRY DETERMINATION'        ? 17 1 1 1 ?      ?            
'CRYSTALLOGRAPHY MERGING'       ? 18 1 1 1 ?      ?            
OTHER                           ? 19 1 1 1 ?      ?            
# 
_em_specimen.concentration           6.2 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Cancer Institute (NIH/NCI)' 'United States' 1R35Gm146860         1 
'Other private'                                                     ?               '2022 Scholar Award' 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3BL8 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8G7Z 
_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  
CA 
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   . ARG A 1 82  ? 134.643 175.130 93.504  1.00 88.65  ? 40  ARG A N   1 
ATOM   2     C  CA  . ARG A 1 82  ? 133.517 175.718 92.792  1.00 91.70  ? 40  ARG A CA  1 
ATOM   3     C  C   . ARG A 1 82  ? 132.229 175.563 93.594  1.00 94.42  ? 40  ARG A C   1 
ATOM   4     O  O   . ARG A 1 82  ? 132.196 174.841 94.587  1.00 94.09  ? 40  ARG A O   1 
ATOM   5     C  CB  . ARG A 1 82  ? 133.377 175.086 91.406  1.00 90.86  ? 40  ARG A CB  1 
ATOM   6     C  CG  . ARG A 1 82  ? 133.275 173.575 91.419  1.00 88.95  ? 40  ARG A CG  1 
ATOM   7     C  CD  . ARG A 1 82  ? 132.781 173.039 90.087  1.00 89.02  ? 40  ARG A CD  1 
ATOM   8     N  NE  . ARG A 1 82  ? 131.481 173.586 89.718  1.00 93.19  ? 40  ARG A NE  1 
ATOM   9     C  CZ  . ARG A 1 82  ? 130.640 173.006 88.872  1.00 97.10  ? 40  ARG A CZ  1 
ATOM   10    N  NH1 . ARG A 1 82  ? 130.929 171.853 88.293  1.00 95.35  ? 40  ARG A NH1 1 
ATOM   11    N  NH2 . ARG A 1 82  ? 129.480 173.597 88.604  1.00 94.51  ? 40  ARG A NH2 1 
ATOM   12    N  N   . PHE A 1 83  ? 131.172 176.256 93.166  1.00 92.95  ? 41  PHE A N   1 
ATOM   13    C  CA  . PHE A 1 83  ? 129.891 176.274 93.869  1.00 89.91  ? 41  PHE A CA  1 
ATOM   14    C  C   . PHE A 1 83  ? 128.823 175.689 92.954  1.00 88.92  ? 41  PHE A C   1 
ATOM   15    O  O   . PHE A 1 83  ? 128.168 176.425 92.204  1.00 92.28  ? 41  PHE A O   1 
ATOM   16    C  CB  . PHE A 1 83  ? 129.518 177.696 94.296  1.00 85.36  ? 41  PHE A CB  1 
ATOM   17    C  CG  . PHE A 1 83  ? 130.264 178.191 95.506  1.00 85.38  ? 41  PHE A CG  1 
ATOM   18    C  CD1 . PHE A 1 83  ? 131.623 177.982 95.640  1.00 86.97  ? 41  PHE A CD1 1 
ATOM   19    C  CD2 . PHE A 1 83  ? 129.600 178.877 96.506  1.00 86.07  ? 41  PHE A CD2 1 
ATOM   20    C  CE1 . PHE A 1 83  ? 132.305 178.441 96.746  1.00 88.94  ? 41  PHE A CE1 1 
ATOM   21    C  CE2 . PHE A 1 83  ? 130.277 179.338 97.616  1.00 89.77  ? 41  PHE A CE2 1 
ATOM   22    C  CZ  . PHE A 1 83  ? 131.631 179.121 97.735  1.00 91.24  ? 41  PHE A CZ  1 
ATOM   23    N  N   . PRO A 1 84  ? 128.596 174.383 92.993  1.00 75.99  ? 42  PRO A N   1 
ATOM   24    C  CA  . PRO A 1 84  ? 127.701 173.750 92.016  1.00 77.93  ? 42  PRO A CA  1 
ATOM   25    C  C   . PRO A 1 84  ? 126.225 173.978 92.292  1.00 79.79  ? 42  PRO A C   1 
ATOM   26    O  O   . PRO A 1 84  ? 125.591 173.165 92.970  1.00 82.58  ? 42  PRO A O   1 
ATOM   27    C  CB  . PRO A 1 84  ? 128.062 172.265 92.129  1.00 76.58  ? 42  PRO A CB  1 
ATOM   28    C  CG  . PRO A 1 84  ? 128.581 172.114 93.502  1.00 78.64  ? 42  PRO A CG  1 
ATOM   29    C  CD  . PRO A 1 84  ? 129.245 173.401 93.875  1.00 76.89  ? 42  PRO A CD  1 
ATOM   30    N  N   . VAL A 1 85  ? 125.672 175.085 91.789  1.00 89.39  ? 43  VAL A N   1 
ATOM   31    C  CA  . VAL A 1 85  ? 124.247 175.343 91.960  1.00 90.01  ? 43  VAL A CA  1 
ATOM   32    C  C   . VAL A 1 85  ? 123.437 174.210 91.343  1.00 89.82  ? 43  VAL A C   1 
ATOM   33    O  O   . VAL A 1 85  ? 123.796 173.653 90.297  1.00 89.78  ? 43  VAL A O   1 
ATOM   34    C  CB  . VAL A 1 85  ? 123.864 176.707 91.360  1.00 86.89  ? 43  VAL A CB  1 
ATOM   35    C  CG1 . VAL A 1 85  ? 124.901 177.754 91.724  1.00 84.41  ? 43  VAL A CG1 1 
ATOM   36    C  CG2 . VAL A 1 85  ? 123.696 176.626 89.852  1.00 88.38  ? 43  VAL A CG2 1 
ATOM   37    N  N   . VAL A 1 86  ? 122.355 173.832 92.021  1.00 87.43  ? 44  VAL A N   1 
ATOM   38    C  CA  . VAL A 1 86  ? 121.462 172.770 91.572  1.00 87.02  ? 44  VAL A CA  1 
ATOM   39    C  C   . VAL A 1 86  ? 120.032 173.283 91.642  1.00 87.71  ? 44  VAL A C   1 
ATOM   40    O  O   . VAL A 1 86  ? 119.675 174.032 92.558  1.00 87.74  ? 44  VAL A O   1 
ATOM   41    C  CB  . VAL A 1 86  ? 121.620 171.484 92.412  1.00 81.49  ? 44  VAL A CB  1 
ATOM   42    C  CG1 . VAL A 1 86  ? 120.776 170.368 91.833  1.00 82.56  ? 44  VAL A CG1 1 
ATOM   43    C  CG2 . VAL A 1 86  ? 123.070 171.056 92.463  1.00 81.99  ? 44  VAL A CG2 1 
ATOM   44    N  N   . ASN A 1 87  ? 119.216 172.885 90.672  1.00 92.76  ? 45  ASN A N   1 
ATOM   45    C  CA  . ASN A 1 87  ? 117.840 173.349 90.570  1.00 92.86  ? 45  ASN A CA  1 
ATOM   46    C  C   . ASN A 1 87  ? 116.895 172.354 91.230  1.00 94.75  ? 45  ASN A C   1 
ATOM   47    O  O   . ASN A 1 87  ? 116.911 171.164 90.903  1.00 94.34  ? 45  ASN A O   1 
ATOM   48    C  CB  . ASN A 1 87  ? 117.457 173.546 89.104  1.00 89.89  ? 45  ASN A CB  1 
ATOM   49    C  CG  . ASN A 1 87  ? 115.966 173.460 88.876  1.00 93.11  ? 45  ASN A CG  1 
ATOM   50    O  OD1 . ASN A 1 87  ? 115.198 174.272 89.391  1.00 91.74  ? 45  ASN A OD1 1 
ATOM   51    N  ND2 . ASN A 1 87  ? 115.544 172.469 88.100  1.00 92.82  ? 45  ASN A ND2 1 
ATOM   52    N  N   . THR A 1 88  ? 116.072 172.843 92.153  1.00 94.35  ? 46  THR A N   1 
ATOM   53    C  CA  . THR A 1 88  ? 115.036 172.052 92.800  1.00 92.37  ? 46  THR A CA  1 
ATOM   54    C  C   . THR A 1 88  ? 113.669 172.468 92.266  1.00 93.67  ? 46  THR A C   1 
ATOM   55    O  O   . THR A 1 88  ? 113.541 173.418 91.491  1.00 94.19  ? 46  THR A O   1 
ATOM   56    C  CB  . THR A 1 88  ? 115.099 172.210 94.318  1.00 88.49  ? 46  THR A CB  1 
ATOM   57    O  OG1 . THR A 1 88  ? 114.355 173.371 94.705  1.00 93.75  ? 46  THR A OG1 1 
ATOM   58    C  CG2 . THR A 1 88  ? 116.537 172.360 94.775  1.00 87.58  ? 46  THR A CG2 1 
ATOM   59    N  N   . ALA A 1 89  ? 112.632 171.745 92.694  1.00 90.64  ? 47  ALA A N   1 
ATOM   60    C  CA  . ALA A 1 89  ? 111.287 172.031 92.208  1.00 89.61  ? 47  ALA A CA  1 
ATOM   61    C  C   . ALA A 1 89  ? 110.764 173.375 92.697  1.00 92.08  ? 47  ALA A C   1 
ATOM   62    O  O   . ALA A 1 89  ? 109.761 173.864 92.167  1.00 92.82  ? 47  ALA A O   1 
ATOM   63    C  CB  . ALA A 1 89  ? 110.325 170.919 92.622  1.00 87.50  ? 47  ALA A CB  1 
ATOM   64    N  N   . TYR A 1 90  ? 111.415 173.979 93.691  1.00 93.67  ? 48  TYR A N   1 
ATOM   65    C  CA  . TYR A 1 90  ? 111.021 175.285 94.194  1.00 94.17  ? 48  TYR A CA  1 
ATOM   66    C  C   . TYR A 1 90  ? 111.970 176.400 93.783  1.00 94.63  ? 48  TYR A C   1 
ATOM   67    O  O   . TYR A 1 90  ? 111.676 177.569 94.053  1.00 95.69  ? 48  TYR A O   1 
ATOM   68    C  CB  . TYR A 1 90  ? 110.910 175.254 95.725  1.00 92.94  ? 48  TYR A CB  1 
ATOM   69    C  CG  . TYR A 1 90  ? 110.096 174.095 96.248  1.00 93.66  ? 48  TYR A CG  1 
ATOM   70    C  CD1 . TYR A 1 90  ? 108.820 173.847 95.768  1.00 94.11  ? 48  TYR A CD1 1 
ATOM   71    C  CD2 . TYR A 1 90  ? 110.605 173.247 97.217  1.00 94.31  ? 48  TYR A CD2 1 
ATOM   72    C  CE1 . TYR A 1 90  ? 108.072 172.789 96.241  1.00 92.50  ? 48  TYR A CE1 1 
ATOM   73    C  CE2 . TYR A 1 90  ? 109.865 172.188 97.695  1.00 96.99  ? 48  TYR A CE2 1 
ATOM   74    C  CZ  . TYR A 1 90  ? 108.600 171.962 97.204  1.00 95.73  ? 48  TYR A CZ  1 
ATOM   75    O  OH  . TYR A 1 90  ? 107.862 170.904 97.681  1.00 93.81  ? 48  TYR A OH  1 
ATOM   76    N  N   . GLY A 1 91  ? 113.086 176.079 93.146  1.00 99.40  ? 49  GLY A N   1 
ATOM   77    C  CA  . GLY A 1 91  ? 114.032 177.098 92.722  1.00 100.70 ? 49  GLY A CA  1 
ATOM   78    C  C   . GLY A 1 91  ? 115.392 176.480 92.442  1.00 100.10 ? 49  GLY A C   1 
ATOM   79    O  O   . GLY A 1 91  ? 115.488 175.337 91.996  1.00 97.50  ? 49  GLY A O   1 
ATOM   80    N  N   . ARG A 1 92  ? 116.429 177.267 92.704  1.00 98.63  ? 50  ARG A N   1 
ATOM   81    C  CA  . ARG A 1 92  ? 117.808 176.826 92.581  1.00 96.30  ? 50  ARG A CA  1 
ATOM   82    C  C   . ARG A 1 92  ? 118.523 177.149 93.880  1.00 98.43  ? 50  ARG A C   1 
ATOM   83    O  O   . ARG A 1 92  ? 118.224 178.160 94.513  1.00 98.95  ? 50  ARG A O   1 
ATOM   84    C  CB  . ARG A 1 92  ? 118.517 177.513 91.408  1.00 98.53  ? 50  ARG A CB  1 
ATOM   85    C  CG  . ARG A 1 92  ? 117.575 178.081 90.357  1.00 100.12 ? 50  ARG A CG  1 
ATOM   86    C  CD  . ARG A 1 92  ? 118.338 178.701 89.202  1.00 98.11  ? 50  ARG A CD  1 
ATOM   87    N  NE  . ARG A 1 92  ? 119.267 177.756 88.597  1.00 102.46 ? 50  ARG A NE  1 
ATOM   88    C  CZ  . ARG A 1 92  ? 118.914 176.782 87.769  1.00 102.60 ? 50  ARG A CZ  1 
ATOM   89    N  NH1 . ARG A 1 92  ? 117.651 176.592 87.425  1.00 100.97 ? 50  ARG A NH1 1 
ATOM   90    N  NH2 . ARG A 1 92  ? 119.852 175.981 87.273  1.00 100.33 ? 50  ARG A NH2 1 
ATOM   91    N  N   . VAL A 1 93  ? 119.455 176.289 94.284  1.00 95.17  ? 51  VAL A N   1 
ATOM   92    C  CA  . VAL A 1 93  ? 120.229 176.504 95.500  1.00 94.69  ? 51  VAL A CA  1 
ATOM   93    C  C   . VAL A 1 93  ? 121.709 176.383 95.169  1.00 95.36  ? 51  VAL A C   1 
ATOM   94    O  O   . VAL A 1 93  ? 122.100 175.668 94.241  1.00 96.08  ? 51  VAL A O   1 
ATOM   95    C  CB  . VAL A 1 93  ? 119.838 175.521 96.627  1.00 90.97  ? 51  VAL A CB  1 
ATOM   96    C  CG1 . VAL A 1 93  ? 118.332 175.493 96.814  1.00 93.09  ? 51  VAL A CG1 1 
ATOM   97    C  CG2 . VAL A 1 93  ? 120.363 174.130 96.334  1.00 90.02  ? 51  VAL A CG2 1 
ATOM   98    N  N   . ARG A 1 94  ? 122.534 177.100 95.928  1.00 90.82  ? 52  ARG A N   1 
ATOM   99    C  CA  . ARG A 1 94  ? 123.981 177.072 95.752  1.00 90.47  ? 52  ARG A CA  1 
ATOM   100   C  C   . ARG A 1 94  ? 124.637 176.417 96.959  1.00 91.95  ? 52  ARG A C   1 
ATOM   101   O  O   . ARG A 1 94  ? 124.320 176.757 98.103  1.00 94.76  ? 52  ARG A O   1 
ATOM   102   C  CB  . ARG A 1 94  ? 124.545 178.479 95.554  1.00 91.34  ? 52  ARG A CB  1 
ATOM   103   C  CG  . ARG A 1 94  ? 126.005 178.491 95.126  1.00 92.13  ? 52  ARG A CG  1 
ATOM   104   C  CD  . ARG A 1 94  ? 126.539 179.901 94.960  1.00 92.98  ? 52  ARG A CD  1 
ATOM   105   N  NE  . ARG A 1 94  ? 125.774 180.666 93.985  1.00 94.18  ? 52  ARG A NE  1 
ATOM   106   C  CZ  . ARG A 1 94  ? 125.109 181.777 94.265  1.00 93.41  ? 52  ARG A CZ  1 
ATOM   107   N  NH1 . ARG A 1 94  ? 125.102 182.288 95.485  1.00 93.02  ? 52  ARG A NH1 1 
ATOM   108   N  NH2 . ARG A 1 94  ? 124.438 182.393 93.297  1.00 91.97  ? 52  ARG A NH2 1 
ATOM   109   N  N   . GLY A 1 95  ? 125.554 175.486 96.702  1.00 82.73  ? 53  GLY A N   1 
ATOM   110   C  CA  . GLY A 1 95  ? 126.244 174.787 97.768  1.00 81.02  ? 53  GLY A CA  1 
ATOM   111   C  C   . GLY A 1 95  ? 127.723 175.101 97.857  1.00 83.63  ? 53  GLY A C   1 
ATOM   112   O  O   . GLY A 1 95  ? 128.148 176.209 97.520  1.00 89.83  ? 53  GLY A O   1 
ATOM   113   N  N   . VAL A 1 96  ? 128.516 174.139 98.322  1.00 80.72  ? 54  VAL A N   1 
ATOM   114   C  CA  . VAL A 1 96  ? 129.963 174.262 98.428  1.00 80.80  ? 54  VAL A CA  1 
ATOM   115   C  C   . VAL A 1 96  ? 130.590 172.937 98.008  1.00 82.60  ? 54  VAL A C   1 
ATOM   116   O  O   . VAL A 1 96  ? 129.897 171.998 97.617  1.00 82.69  ? 54  VAL A O   1 
ATOM   117   C  CB  . VAL A 1 96  ? 130.418 174.653 99.848  1.00 81.06  ? 54  VAL A CB  1 
ATOM   118   C  CG1 . VAL A 1 96  ? 130.277 176.147 100.055 1.00 81.32  ? 54  VAL A CG1 1 
ATOM   119   C  CG2 . VAL A 1 96  ? 129.617 173.894 100.885 1.00 82.43  ? 54  VAL A CG2 1 
ATOM   120   N  N   . ARG A 1 97  ? 131.916 172.869 98.081  1.00 87.41  ? 55  ARG A N   1 
ATOM   121   C  CA  . ARG A 1 97  ? 132.685 171.692 97.681  1.00 88.33  ? 55  ARG A CA  1 
ATOM   122   C  C   . ARG A 1 97  ? 133.748 171.373 98.725  1.00 88.32  ? 55  ARG A C   1 
ATOM   123   O  O   . ARG A 1 97  ? 134.938 171.271 98.425  1.00 93.30  ? 55  ARG A O   1 
ATOM   124   C  CB  . ARG A 1 97  ? 133.311 171.880 96.302  1.00 89.60  ? 55  ARG A CB  1 
ATOM   125   C  CG  . ARG A 1 97  ? 133.857 170.596 95.691  1.00 87.88  ? 55  ARG A CG  1 
ATOM   126   C  CD  . ARG A 1 97  ? 134.215 170.773 94.234  1.00 90.08  ? 55  ARG A CD  1 
ATOM   127   N  NE  . ARG A 1 97  ? 133.031 170.860 93.390  1.00 91.46  ? 55  ARG A NE  1 
ATOM   128   C  CZ  . ARG A 1 97  ? 132.603 169.881 92.605  1.00 92.74  ? 55  ARG A CZ  1 
ATOM   129   N  NH1 . ARG A 1 97  ? 133.239 168.724 92.534  1.00 90.86  ? 55  ARG A NH1 1 
ATOM   130   N  NH2 . ARG A 1 97  ? 131.510 170.069 91.871  1.00 91.99  ? 55  ARG A NH2 1 
ATOM   131   N  N   . ARG A 1 98  ? 133.329 171.253 99.984  1.00 80.05  ? 56  ARG A N   1 
ATOM   132   C  CA  . ARG A 1 98  ? 134.271 171.062 101.080 1.00 82.17  ? 56  ARG A CA  1 
ATOM   133   C  C   . ARG A 1 98  ? 135.173 169.857 100.837 1.00 86.00  ? 56  ARG A C   1 
ATOM   134   O  O   . ARG A 1 98  ? 134.723 168.802 100.386 1.00 86.11  ? 56  ARG A O   1 
ATOM   135   C  CB  . ARG A 1 98  ? 133.515 170.886 102.397 1.00 83.26  ? 56  ARG A CB  1 
ATOM   136   C  CG  . ARG A 1 98  ? 134.305 171.306 103.622 1.00 84.44  ? 56  ARG A CG  1 
ATOM   137   C  CD  . ARG A 1 98  ? 134.457 172.812 103.676 1.00 86.18  ? 56  ARG A CD  1 
ATOM   138   N  NE  . ARG A 1 98  ? 133.167 173.479 103.572 1.00 86.72  ? 56  ARG A NE  1 
ATOM   139   C  CZ  . ARG A 1 98  ? 133.000 174.726 103.156 1.00 88.68  ? 56  ARG A CZ  1 
ATOM   140   N  NH1 . ARG A 1 98  ? 134.028 175.476 102.792 1.00 85.99  ? 56  ARG A NH1 1 
ATOM   141   N  NH2 . ARG A 1 98  ? 131.772 175.234 103.102 1.00 88.04  ? 56  ARG A NH2 1 
ATOM   142   N  N   . GLU A 1 99  ? 136.459 170.034 101.132 1.00 94.88  ? 57  GLU A N   1 
ATOM   143   C  CA  . GLU A 1 99  ? 137.471 169.000 100.954 1.00 94.84  ? 57  GLU A CA  1 
ATOM   144   C  C   . GLU A 1 99  ? 137.748 168.323 102.289 1.00 97.10  ? 57  GLU A C   1 
ATOM   145   O  O   . GLU A 1 99  ? 137.932 168.999 103.307 1.00 98.56  ? 57  GLU A O   1 
ATOM   146   C  CB  . GLU A 1 99  ? 138.762 169.594 100.390 1.00 95.71  ? 57  GLU A CB  1 
ATOM   147   C  CG  . GLU A 1 99  ? 138.678 170.016 98.934  1.00 98.69  ? 57  GLU A CG  1 
ATOM   148   C  CD  . GLU A 1 99  ? 138.945 168.870 97.980  1.00 100.85 ? 57  GLU A CD  1 
ATOM   149   O  OE1 . GLU A 1 99  ? 139.322 167.777 98.451  1.00 99.72  ? 57  GLU A OE1 1 
ATOM   150   O  OE2 . GLU A 1 99  ? 138.777 169.062 96.757  1.00 101.41 ? 57  GLU A OE2 1 
ATOM   151   N  N   . LEU A 1 100 ? 137.787 166.996 102.280 1.00 94.35  ? 58  LEU A N   1 
ATOM   152   C  CA  . LEU A 1 100 ? 137.941 166.220 103.500 1.00 93.16  ? 58  LEU A CA  1 
ATOM   153   C  C   . LEU A 1 100 ? 139.410 166.065 103.874 1.00 96.05  ? 58  LEU A C   1 
ATOM   154   O  O   . LEU A 1 100 ? 140.298 166.098 103.019 1.00 96.48  ? 58  LEU A O   1 
ATOM   155   C  CB  . LEU A 1 100 ? 137.297 164.845 103.345 1.00 92.30  ? 58  LEU A CB  1 
ATOM   156   C  CG  . LEU A 1 100 ? 135.793 164.907 103.101 1.00 92.97  ? 58  LEU A CG  1 
ATOM   157   C  CD1 . LEU A 1 100 ? 135.227 163.515 102.937 1.00 92.13  ? 58  LEU A CD1 1 
ATOM   158   C  CD2 . LEU A 1 100 ? 135.117 165.636 104.243 1.00 93.18  ? 58  LEU A CD2 1 
ATOM   159   N  N   . ASN A 1 101 ? 139.651 165.893 105.176 1.00 100.39 ? 59  ASN A N   1 
ATOM   160   C  CA  . ASN A 1 101 ? 141.018 165.779 105.677 1.00 99.83  ? 59  ASN A CA  1 
ATOM   161   C  C   . ASN A 1 101 ? 141.707 164.526 105.149 1.00 102.08 ? 59  ASN A C   1 
ATOM   162   O  O   . ASN A 1 101 ? 142.880 164.575 104.761 1.00 101.09 ? 59  ASN A O   1 
ATOM   163   C  CB  . ASN A 1 101 ? 141.014 165.783 107.205 1.00 96.75  ? 59  ASN A CB  1 
ATOM   164   N  N   . ASN A 1 102 ? 141.000 163.399 105.125 1.00 103.99 ? 60  ASN A N   1 
ATOM   165   C  CA  . ASN A 1 102 ? 141.610 162.139 104.731 1.00 100.93 ? 60  ASN A CA  1 
ATOM   166   C  C   . ASN A 1 102 ? 141.945 162.139 103.241 1.00 101.66 ? 60  ASN A C   1 
ATOM   167   O  O   . ASN A 1 102 ? 141.403 162.916 102.451 1.00 100.97 ? 60  ASN A O   1 
ATOM   168   C  CB  . ASN A 1 102 ? 140.687 160.968 105.064 1.00 98.20  ? 60  ASN A CB  1 
ATOM   169   C  CG  . ASN A 1 102 ? 141.428 159.649 105.153 1.00 98.74  ? 60  ASN A CG  1 
ATOM   170   O  OD1 . ASN A 1 102 ? 142.326 159.374 104.359 1.00 99.62  ? 60  ASN A OD1 1 
ATOM   171   N  ND2 . ASN A 1 102 ? 141.057 158.825 106.125 1.00 98.01  ? 60  ASN A ND2 1 
ATOM   172   N  N   . GLU A 1 103 ? 142.863 161.251 102.867 1.00 104.79 ? 61  GLU A N   1 
ATOM   173   C  CA  . GLU A 1 103 ? 143.350 161.153 101.498 1.00 105.81 ? 61  GLU A CA  1 
ATOM   174   C  C   . GLU A 1 103 ? 142.709 160.019 100.708 1.00 104.22 ? 61  GLU A C   1 
ATOM   175   O  O   . GLU A 1 103 ? 143.066 159.819 99.543  1.00 102.96 ? 61  GLU A O   1 
ATOM   176   C  CB  . GLU A 1 103 ? 144.873 160.987 101.494 1.00 103.59 ? 61  GLU A CB  1 
ATOM   177   C  CG  . GLU A 1 103 ? 145.387 159.919 102.445 1.00 105.41 ? 61  GLU A CG  1 
ATOM   178   C  CD  . GLU A 1 103 ? 145.563 158.572 101.773 1.00 105.68 ? 61  GLU A CD  1 
ATOM   179   O  OE1 . GLU A 1 103 ? 145.452 158.507 100.532 1.00 104.93 ? 61  GLU A OE1 1 
ATOM   180   O  OE2 . GLU A 1 103 ? 145.816 157.578 102.487 1.00 105.06 ? 61  GLU A OE2 1 
ATOM   181   N  N   . ILE A 1 104 ? 141.777 159.276 101.301 1.00 96.98  ? 62  ILE A N   1 
ATOM   182   C  CA  . ILE A 1 104 ? 141.091 158.193 100.609 1.00 97.41  ? 62  ILE A CA  1 
ATOM   183   C  C   . ILE A 1 104 ? 139.615 158.504 100.394 1.00 98.18  ? 62  ILE A C   1 
ATOM   184   O  O   . ILE A 1 104 ? 138.841 157.606 100.046 1.00 99.00  ? 62  ILE A O   1 
ATOM   185   C  CB  . ILE A 1 104 ? 141.263 156.857 101.349 1.00 96.75  ? 62  ILE A CB  1 
ATOM   186   C  CG1 . ILE A 1 104 ? 140.710 156.958 102.770 1.00 98.47  ? 62  ILE A CG1 1 
ATOM   187   C  CG2 . ILE A 1 104 ? 142.722 156.450 101.374 1.00 94.82  ? 62  ILE A CG2 1 
ATOM   188   C  CD1 . ILE A 1 104 ? 140.676 155.639 103.506 1.00 95.70  ? 62  ILE A CD1 1 
ATOM   189   N  N   . LEU A 1 105 ? 139.204 159.753 100.592 1.00 90.94  ? 63  LEU A N   1 
ATOM   190   C  CA  . LEU A 1 105 ? 137.820 160.165 100.408 1.00 91.40  ? 63  LEU A CA  1 
ATOM   191   C  C   . LEU A 1 105 ? 137.772 161.329 99.431  1.00 93.68  ? 63  LEU A C   1 
ATOM   192   O  O   . LEU A 1 105 ? 138.515 162.304 99.586  1.00 93.86  ? 63  LEU A O   1 
ATOM   193   C  CB  . LEU A 1 105 ? 137.181 160.567 101.738 1.00 90.92  ? 63  LEU A CB  1 
ATOM   194   C  CG  . LEU A 1 105 ? 137.599 159.774 102.974 1.00 89.75  ? 63  LEU A CG  1 
ATOM   195   C  CD1 . LEU A 1 105 ? 137.163 160.502 104.227 1.00 89.56  ? 63  LEU A CD1 1 
ATOM   196   C  CD2 . LEU A 1 105 ? 137.019 158.374 102.936 1.00 86.86  ? 63  LEU A CD2 1 
ATOM   197   N  N   . GLY A 1 106 ? 136.893 161.230 98.437  1.00 87.21  ? 64  GLY A N   1 
ATOM   198   C  CA  . GLY A 1 106 ? 136.736 162.274 97.454  1.00 85.76  ? 64  GLY A CA  1 
ATOM   199   C  C   . GLY A 1 106 ? 136.026 163.479 98.030  1.00 87.96  ? 64  GLY A C   1 
ATOM   200   O  O   . GLY A 1 106 ? 135.541 163.456 99.163  1.00 90.50  ? 64  GLY A O   1 
ATOM   201   N  N   . PRO A 1 107 ? 135.948 164.560 97.260  1.00 90.81  ? 65  PRO A N   1 
ATOM   202   C  CA  . PRO A 1 107 ? 135.300 165.769 97.769  1.00 90.22  ? 65  PRO A CA  1 
ATOM   203   C  C   . PRO A 1 107 ? 133.792 165.602 97.834  1.00 91.26  ? 65  PRO A C   1 
ATOM   204   O  O   . PRO A 1 107 ? 133.194 164.822 97.089  1.00 87.37  ? 65  PRO A O   1 
ATOM   205   C  CB  . PRO A 1 107 ? 135.710 166.846 96.756  1.00 86.11  ? 65  PRO A CB  1 
ATOM   206   C  CG  . PRO A 1 107 ? 136.231 166.089 95.537  1.00 88.19  ? 65  PRO A CG  1 
ATOM   207   C  CD  . PRO A 1 107 ? 136.091 164.615 95.798  1.00 88.78  ? 65  PRO A CD  1 
ATOM   208   N  N   . VAL A 1 108 ? 133.179 166.346 98.751  1.00 78.87  ? 66  VAL A N   1 
ATOM   209   C  CA  . VAL A 1 108 ? 131.756 166.236 99.042  1.00 72.02  ? 66  VAL A CA  1 
ATOM   210   C  C   . VAL A 1 108 ? 131.118 167.606 98.882  1.00 73.90  ? 66  VAL A C   1 
ATOM   211   O  O   . VAL A 1 108 ? 131.620 168.597 99.421  1.00 76.82  ? 66  VAL A O   1 
ATOM   212   C  CB  . VAL A 1 108 ? 131.513 165.683 100.455 1.00 66.70  ? 66  VAL A CB  1 
ATOM   213   C  CG1 . VAL A 1 108 ? 130.088 165.933 100.880 1.00 72.33  ? 66  VAL A CG1 1 
ATOM   214   C  CG2 . VAL A 1 108 ? 131.821 164.207 100.487 1.00 71.18  ? 66  VAL A CG2 1 
ATOM   215   N  N   . VAL A 1 109 ? 130.014 167.656 98.145  1.00 70.70  ? 67  VAL A N   1 
ATOM   216   C  CA  . VAL A 1 109 ? 129.263 168.885 97.935  1.00 67.66  ? 67  VAL A CA  1 
ATOM   217   C  C   . VAL A 1 109 ? 128.203 168.986 99.022  1.00 69.43  ? 67  VAL A C   1 
ATOM   218   O  O   . VAL A 1 109 ? 127.387 168.074 99.192  1.00 76.31  ? 67  VAL A O   1 
ATOM   219   C  CB  . VAL A 1 109 ? 128.628 168.907 96.538  1.00 69.29  ? 67  VAL A CB  1 
ATOM   220   C  CG1 . VAL A 1 109 ? 127.755 170.127 96.372  1.00 70.66  ? 67  VAL A CG1 1 
ATOM   221   C  CG2 . VAL A 1 109 ? 129.703 168.863 95.470  1.00 71.97  ? 67  VAL A CG2 1 
ATOM   222   N  N   . GLN A 1 110 ? 128.209 170.089 99.760  1.00 66.26  ? 68  GLN A N   1 
ATOM   223   C  CA  . GLN A 1 110 ? 127.311 170.282 100.890 1.00 68.17  ? 68  GLN A CA  1 
ATOM   224   C  C   . GLN A 1 110 ? 126.329 171.401 100.576 1.00 73.29  ? 68  GLN A C   1 
ATOM   225   O  O   . GLN A 1 110 ? 126.742 172.523 100.266 1.00 79.52  ? 68  GLN A O   1 
ATOM   226   C  CB  . GLN A 1 110 ? 128.095 170.610 102.159 1.00 67.16  ? 68  GLN A CB  1 
ATOM   227   C  CG  . GLN A 1 110 ? 129.264 169.689 102.426 1.00 71.59  ? 68  GLN A CG  1 
ATOM   228   C  CD  . GLN A 1 110 ? 130.176 170.220 103.510 1.00 76.28  ? 68  GLN A CD  1 
ATOM   229   O  OE1 . GLN A 1 110 ? 130.150 171.406 103.830 1.00 73.70  ? 68  GLN A OE1 1 
ATOM   230   N  NE2 . GLN A 1 110 ? 130.986 169.341 104.085 1.00 74.06  ? 68  GLN A NE2 1 
ATOM   231   N  N   . PHE A 1 111 ? 125.038 171.097 100.663 1.00 62.13  ? 69  PHE A N   1 
ATOM   232   C  CA  . PHE A 1 111 ? 123.974 172.095 100.592 1.00 61.56  ? 69  PHE A CA  1 
ATOM   233   C  C   . PHE A 1 111 ? 123.377 172.193 101.987 1.00 64.54  ? 69  PHE A C   1 
ATOM   234   O  O   . PHE A 1 111 ? 122.569 171.350 102.379 1.00 68.31  ? 69  PHE A O   1 
ATOM   235   C  CB  . PHE A 1 111 ? 122.912 171.715 99.569  1.00 59.38  ? 69  PHE A CB  1 
ATOM   236   C  CG  . PHE A 1 111 ? 123.455 171.429 98.207  1.00 59.75  ? 69  PHE A CG  1 
ATOM   237   C  CD1 . PHE A 1 111 ? 123.649 172.451 97.301  1.00 67.40  ? 69  PHE A CD1 1 
ATOM   238   C  CD2 . PHE A 1 111 ? 123.760 170.138 97.828  1.00 61.65  ? 69  PHE A CD2 1 
ATOM   239   C  CE1 . PHE A 1 111 ? 124.145 172.191 96.047  1.00 69.96  ? 69  PHE A CE1 1 
ATOM   240   C  CE2 . PHE A 1 111 ? 124.256 169.873 96.577  1.00 65.12  ? 69  PHE A CE2 1 
ATOM   241   C  CZ  . PHE A 1 111 ? 124.448 170.900 95.684  1.00 69.78  ? 69  PHE A CZ  1 
ATOM   242   N  N   . LEU A 1 112 ? 123.779 173.208 102.739 1.00 70.82  ? 70  LEU A N   1 
ATOM   243   C  CA  . LEU A 1 112 ? 123.371 173.352 104.128 1.00 67.31  ? 70  LEU A CA  1 
ATOM   244   C  C   . LEU A 1 112 ? 122.261 174.384 104.239 1.00 66.69  ? 70  LEU A C   1 
ATOM   245   O  O   . LEU A 1 112 ? 122.414 175.519 103.780 1.00 71.64  ? 70  LEU A O   1 
ATOM   246   C  CB  . LEU A 1 112 ? 124.557 173.756 105.002 1.00 64.66  ? 70  LEU A CB  1 
ATOM   247   C  CG  . LEU A 1 112 ? 125.874 173.044 104.704 1.00 65.64  ? 70  LEU A CG  1 
ATOM   248   C  CD1 . LEU A 1 112 ? 126.967 173.554 105.618 1.00 68.20  ? 70  LEU A CD1 1 
ATOM   249   C  CD2 . LEU A 1 112 ? 125.716 171.548 104.853 1.00 63.34  ? 70  LEU A CD2 1 
ATOM   250   N  N   . GLY A 1 113 ? 121.149 173.991 104.849 1.00 56.55  ? 71  GLY A N   1 
ATOM   251   C  CA  . GLY A 1 113 ? 120.062 174.913 105.079 1.00 57.93  ? 71  GLY A CA  1 
ATOM   252   C  C   . GLY A 1 113 ? 118.992 174.942 104.016 1.00 61.40  ? 71  GLY A C   1 
ATOM   253   O  O   . GLY A 1 113 ? 118.310 175.961 103.872 1.00 68.29  ? 71  GLY A O   1 
ATOM   254   N  N   . VAL A 1 114 ? 118.818 173.862 103.262 1.00 58.97  ? 72  VAL A N   1 
ATOM   255   C  CA  . VAL A 1 114 ? 117.769 173.810 102.248 1.00 56.27  ? 72  VAL A CA  1 
ATOM   256   C  C   . VAL A 1 114 ? 116.428 173.674 102.957 1.00 59.77  ? 72  VAL A C   1 
ATOM   257   O  O   . VAL A 1 114 ? 116.196 172.671 103.644 1.00 65.48  ? 72  VAL A O   1 
ATOM   258   C  CB  . VAL A 1 114 ? 117.994 172.649 101.269 1.00 47.41  ? 72  VAL A CB  1 
ATOM   259   C  CG1 . VAL A 1 114 ? 117.002 172.723 100.132 1.00 48.29  ? 72  VAL A CG1 1 
ATOM   260   C  CG2 . VAL A 1 114 ? 119.410 172.667 100.741 1.00 55.02  ? 72  VAL A CG2 1 
ATOM   261   N  N   . PRO A 1 115 ? 115.520 174.637 102.823 1.00 62.00  ? 73  PRO A N   1 
ATOM   262   C  CA  . PRO A 1 115 ? 114.234 174.532 103.518 1.00 58.63  ? 73  PRO A CA  1 
ATOM   263   C  C   . PRO A 1 115 ? 113.359 173.451 102.912 1.00 60.92  ? 73  PRO A C   1 
ATOM   264   O  O   . PRO A 1 115 ? 113.470 173.117 101.731 1.00 66.23  ? 73  PRO A O   1 
ATOM   265   C  CB  . PRO A 1 115 ? 113.614 175.919 103.326 1.00 52.84  ? 73  PRO A CB  1 
ATOM   266   C  CG  . PRO A 1 115 ? 114.226 176.423 102.078 1.00 56.96  ? 73  PRO A CG  1 
ATOM   267   C  CD  . PRO A 1 115 ? 115.629 175.888 102.057 1.00 61.25  ? 73  PRO A CD  1 
ATOM   268   N  N   . TYR A 1 116 ? 112.475 172.901 103.743 1.00 53.74  ? 74  TYR A N   1 
ATOM   269   C  CA  . TYR A 1 116 ? 111.523 171.902 103.288 1.00 55.65  ? 74  TYR A CA  1 
ATOM   270   C  C   . TYR A 1 116 ? 110.095 172.148 103.750 1.00 64.80  ? 74  TYR A C   1 
ATOM   271   O  O   . TYR A 1 116 ? 109.202 171.406 103.333 1.00 68.43  ? 74  TYR A O   1 
ATOM   272   C  CB  . TYR A 1 116 ? 111.959 170.496 103.731 1.00 50.76  ? 74  TYR A CB  1 
ATOM   273   C  CG  . TYR A 1 116 ? 111.988 170.274 105.224 1.00 54.29  ? 74  TYR A CG  1 
ATOM   274   C  CD1 . TYR A 1 116 ? 110.876 169.796 105.896 1.00 57.11  ? 74  TYR A CD1 1 
ATOM   275   C  CD2 . TYR A 1 116 ? 113.133 170.524 105.958 1.00 57.79  ? 74  TYR A CD2 1 
ATOM   276   C  CE1 . TYR A 1 116 ? 110.902 169.586 107.254 1.00 56.42  ? 74  TYR A CE1 1 
ATOM   277   C  CE2 . TYR A 1 116 ? 113.166 170.316 107.316 1.00 56.39  ? 74  TYR A CE2 1 
ATOM   278   C  CZ  . TYR A 1 116 ? 112.049 169.848 107.957 1.00 53.08  ? 74  TYR A CZ  1 
ATOM   279   O  OH  . TYR A 1 116 ? 112.080 169.640 109.312 1.00 59.11  ? 74  TYR A OH  1 
ATOM   280   N  N   . ALA A 1 117 ? 109.848 173.156 104.582 1.00 66.58  ? 75  ALA A N   1 
ATOM   281   C  CA  . ALA A 1 117 ? 108.496 173.481 105.008 1.00 65.15  ? 75  ALA A CA  1 
ATOM   282   C  C   . ALA A 1 117 ? 108.441 174.949 105.400 1.00 66.89  ? 75  ALA A C   1 
ATOM   283   O  O   . ALA A 1 117 ? 109.457 175.557 105.743 1.00 70.87  ? 75  ALA A O   1 
ATOM   284   C  CB  . ALA A 1 117 ? 108.043 172.595 106.172 1.00 65.92  ? 75  ALA A CB  1 
ATOM   285   N  N   . THR A 1 118 ? 107.238 175.513 105.344 1.00 80.01  ? 76  THR A N   1 
ATOM   286   C  CA  . THR A 1 118 ? 107.065 176.920 105.660 1.00 84.39  ? 76  THR A CA  1 
ATOM   287   C  C   . THR A 1 118 ? 107.289 177.163 107.150 1.00 84.35  ? 76  THR A C   1 
ATOM   288   O  O   . THR A 1 118 ? 106.995 176.299 107.979 1.00 86.50  ? 76  THR A O   1 
ATOM   289   C  CB  . THR A 1 118 ? 105.671 177.395 105.273 1.00 85.67  ? 76  THR A CB  1 
ATOM   290   O  OG1 . THR A 1 118 ? 104.708 176.416 105.673 1.00 87.37  ? 76  THR A OG1 1 
ATOM   291   C  CG2 . THR A 1 118 ? 105.581 177.614 103.774 1.00 83.03  ? 76  THR A CG2 1 
ATOM   292   N  N   . PRO A 1 119 ? 107.801 178.333 107.514 1.00 85.83  ? 77  PRO A N   1 
ATOM   293   C  CA  . PRO A 1 119 ? 108.090 178.618 108.919 1.00 89.66  ? 77  PRO A CA  1 
ATOM   294   C  C   . PRO A 1 119 ? 106.818 178.665 109.744 1.00 92.84  ? 77  PRO A C   1 
ATOM   295   O  O   . PRO A 1 119 ? 105.919 179.475 109.472 1.00 93.36  ? 77  PRO A O   1 
ATOM   296   C  CB  . PRO A 1 119 ? 108.767 179.995 108.865 1.00 92.74  ? 77  PRO A CB  1 
ATOM   297   C  CG  . PRO A 1 119 ? 109.235 180.147 107.465 1.00 89.16  ? 77  PRO A CG  1 
ATOM   298   C  CD  . PRO A 1 119 ? 108.229 179.432 106.633 1.00 87.05  ? 77  PRO A CD  1 
ATOM   299   N  N   . PRO A 1 120 ? 106.703 177.817 110.767 1.00 87.32  ? 78  PRO A N   1 
ATOM   300   C  CA  . PRO A 1 120 ? 105.515 177.823 111.645 1.00 83.76  ? 78  PRO A CA  1 
ATOM   301   C  C   . PRO A 1 120 ? 105.667 178.794 112.813 1.00 87.62  ? 78  PRO A C   1 
ATOM   302   O  O   . PRO A 1 120 ? 105.813 178.408 113.979 1.00 88.80  ? 78  PRO A O   1 
ATOM   303   C  CB  . PRO A 1 120 ? 105.449 176.366 112.101 1.00 77.41  ? 78  PRO A CB  1 
ATOM   304   C  CG  . PRO A 1 120 ? 106.891 175.968 112.193 1.00 77.15  ? 78  PRO A CG  1 
ATOM   305   C  CD  . PRO A 1 120 ? 107.630 176.725 111.113 1.00 79.97  ? 78  PRO A CD  1 
ATOM   306   N  N   . LEU A 1 121 ? 105.624 180.091 112.509 1.00 90.34  ? 79  LEU A N   1 
ATOM   307   C  CA  . LEU A 1 121 ? 105.924 181.110 113.510 1.00 90.42  ? 79  LEU A CA  1 
ATOM   308   C  C   . LEU A 1 121 ? 104.686 181.546 114.291 1.00 91.60  ? 79  LEU A C   1 
ATOM   309   O  O   . LEU A 1 121 ? 104.677 181.503 115.525 1.00 89.99  ? 79  LEU A O   1 
ATOM   310   C  CB  . LEU A 1 121 ? 106.579 182.323 112.845 1.00 90.71  ? 79  LEU A CB  1 
ATOM   311   C  CG  . LEU A 1 121 ? 107.876 182.102 112.072 1.00 86.39  ? 79  LEU A CG  1 
ATOM   312   C  CD1 . LEU A 1 121 ? 107.800 182.828 110.746 1.00 88.45  ? 79  LEU A CD1 1 
ATOM   313   C  CD2 . LEU A 1 121 ? 109.068 182.580 112.877 1.00 87.19  ? 79  LEU A CD2 1 
ATOM   314   N  N   . GLY A 1 122 ? 103.642 181.981 113.590 1.00 92.77  ? 80  GLY A N   1 
ATOM   315   C  CA  . GLY A 1 122 ? 102.506 182.588 114.256 1.00 91.80  ? 80  GLY A CA  1 
ATOM   316   C  C   . GLY A 1 122 ? 101.260 181.731 114.304 1.00 93.03  ? 80  GLY A C   1 
ATOM   317   O  O   . GLY A 1 122 ? 101.179 180.783 115.087 1.00 92.05  ? 80  GLY A O   1 
ATOM   318   N  N   . ALA A 1 123 ? 100.271 182.067 113.473 1.00 101.87 ? 81  ALA A N   1 
ATOM   319   C  CA  . ALA A 1 123 ? 99.023  181.315 113.433 1.00 100.88 ? 81  ALA A CA  1 
ATOM   320   C  C   . ALA A 1 123 ? 99.200  179.907 112.889 1.00 99.09  ? 81  ALA A C   1 
ATOM   321   O  O   . ALA A 1 123 ? 98.283  179.091 113.025 1.00 95.75  ? 81  ALA A O   1 
ATOM   322   C  CB  . ALA A 1 123 ? 97.985  182.061 112.595 1.00 99.56  ? 81  ALA A CB  1 
ATOM   323   N  N   . ARG A 1 124 ? 100.337 179.608 112.270 1.00 96.15  ? 82  ARG A N   1 
ATOM   324   C  CA  . ARG A 1 124 ? 100.641 178.261 111.814 1.00 96.68  ? 82  ARG A CA  1 
ATOM   325   C  C   . ARG A 1 124 ? 101.315 177.420 112.886 1.00 97.50  ? 82  ARG A C   1 
ATOM   326   O  O   . ARG A 1 124 ? 101.617 176.249 112.635 1.00 97.55  ? 82  ARG A O   1 
ATOM   327   C  CB  . ARG A 1 124 ? 101.524 178.312 110.565 1.00 97.12  ? 82  ARG A CB  1 
ATOM   328   C  CG  . ARG A 1 124 ? 101.066 177.393 109.445 1.00 97.65  ? 82  ARG A CG  1 
ATOM   329   C  CD  . ARG A 1 124 ? 101.823 177.652 108.150 1.00 94.50  ? 82  ARG A CD  1 
ATOM   330   N  NE  . ARG A 1 124 ? 101.736 179.042 107.719 1.00 94.87  ? 82  ARG A NE  1 
ATOM   331   C  CZ  . ARG A 1 124 ? 102.677 179.953 107.925 1.00 99.21  ? 82  ARG A CZ  1 
ATOM   332   N  NH1 . ARG A 1 124 ? 103.798 179.656 108.559 1.00 99.49  ? 82  ARG A NH1 1 
ATOM   333   N  NH2 . ARG A 1 124 ? 102.486 181.193 107.486 1.00 99.44  ? 82  ARG A NH2 1 
ATOM   334   N  N   . ARG A 1 125 ? 101.568 177.987 114.061 1.00 91.70  ? 83  ARG A N   1 
ATOM   335   C  CA  . ARG A 1 125 ? 102.103 177.212 115.169 1.00 87.89  ? 83  ARG A CA  1 
ATOM   336   C  C   . ARG A 1 125 ? 101.085 176.167 115.607 1.00 89.35  ? 83  ARG A C   1 
ATOM   337   O  O   . ARG A 1 125 ? 99.877  176.414 115.593 1.00 95.20  ? 83  ARG A O   1 
ATOM   338   C  CB  . ARG A 1 125 ? 102.459 178.133 116.336 1.00 84.77  ? 83  ARG A CB  1 
ATOM   339   C  CG  . ARG A 1 125 ? 102.879 177.418 117.602 1.00 83.28  ? 83  ARG A CG  1 
ATOM   340   C  CD  . ARG A 1 125 ? 103.069 178.395 118.741 1.00 83.17  ? 83  ARG A CD  1 
ATOM   341   N  NE  . ARG A 1 125 ? 104.218 179.261 118.518 1.00 88.60  ? 83  ARG A NE  1 
ATOM   342   C  CZ  . ARG A 1 125 ? 104.658 180.157 119.390 1.00 90.77  ? 83  ARG A CZ  1 
ATOM   343   N  NH1 . ARG A 1 125 ? 104.061 180.337 120.556 1.00 91.14  ? 83  ARG A NH1 1 
ATOM   344   N  NH2 . ARG A 1 125 ? 105.724 180.891 119.084 1.00 88.92  ? 83  ARG A NH2 1 
ATOM   345   N  N   . PHE A 1 126 ? 101.584 174.990 115.990 1.00 79.94  ? 84  PHE A N   1 
ATOM   346   C  CA  . PHE A 1 126 ? 100.742 173.857 116.375 1.00 77.65  ? 84  PHE A CA  1 
ATOM   347   C  C   . PHE A 1 126 ? 99.816  173.444 115.234 1.00 77.44  ? 84  PHE A C   1 
ATOM   348   O  O   . PHE A 1 126 ? 98.667  173.056 115.451 1.00 76.94  ? 84  PHE A O   1 
ATOM   349   C  CB  . PHE A 1 126 ? 99.942  174.155 117.643 1.00 74.33  ? 84  PHE A CB  1 
ATOM   350   C  CG  . PHE A 1 126 ? 100.793 174.421 118.846 1.00 80.12  ? 84  PHE A CG  1 
ATOM   351   C  CD1 . PHE A 1 126 ? 102.058 173.876 118.951 1.00 79.86  ? 84  PHE A CD1 1 
ATOM   352   C  CD2 . PHE A 1 126 ? 100.327 175.216 119.875 1.00 84.43  ? 84  PHE A CD2 1 
ATOM   353   C  CE1 . PHE A 1 126 ? 102.841 174.122 120.057 1.00 81.13  ? 84  PHE A CE1 1 
ATOM   354   C  CE2 . PHE A 1 126 ? 101.108 175.465 120.983 1.00 82.94  ? 84  PHE A CE2 1 
ATOM   355   C  CZ  . PHE A 1 126 ? 102.365 174.917 121.074 1.00 80.69  ? 84  PHE A CZ  1 
ATOM   356   N  N   . GLN A 1 127 ? 100.322 173.530 114.010 1.00 81.32  ? 85  GLN A N   1 
ATOM   357   C  CA  . GLN A 1 127 ? 99.637  173.044 112.825 1.00 81.93  ? 85  GLN A CA  1 
ATOM   358   C  C   . GLN A 1 127 ? 100.597 172.187 112.016 1.00 84.60  ? 85  GLN A C   1 
ATOM   359   O  O   . GLN A 1 127 ? 101.809 172.418 112.045 1.00 88.24  ? 85  GLN A O   1 
ATOM   360   C  CB  . GLN A 1 127 ? 99.123  174.200 111.953 1.00 84.27  ? 85  GLN A CB  1 
ATOM   361   C  CG  . GLN A 1 127 ? 98.267  175.223 112.682 1.00 87.88  ? 85  GLN A CG  1 
ATOM   362   C  CD  . GLN A 1 127 ? 96.828  174.781 112.838 1.00 88.23  ? 85  GLN A CD  1 
ATOM   363   O  OE1 . GLN A 1 127 ? 96.090  175.314 113.666 1.00 88.60  ? 85  GLN A OE1 1 
ATOM   364   N  NE2 . GLN A 1 127 ? 96.420  173.801 112.042 1.00 85.83  ? 85  GLN A NE2 1 
ATOM   365   N  N   . PRO A 1 128 ? 100.089 171.190 111.296 1.00 79.09  ? 86  PRO A N   1 
ATOM   366   C  CA  . PRO A 1 128 ? 100.974 170.351 110.497 1.00 76.48  ? 86  PRO A CA  1 
ATOM   367   C  C   . PRO A 1 128 ? 101.654 171.168 109.417 1.00 79.23  ? 86  PRO A C   1 
ATOM   368   O  O   . PRO A 1 128 ? 101.084 172.147 108.902 1.00 84.12  ? 86  PRO A O   1 
ATOM   369   C  CB  . PRO A 1 128 ? 100.025 169.303 109.900 1.00 77.07  ? 86  PRO A CB  1 
ATOM   370   C  CG  . PRO A 1 128 ? 98.672  169.902 109.999 1.00 77.87  ? 86  PRO A CG  1 
ATOM   371   C  CD  . PRO A 1 128 ? 98.690  170.746 111.224 1.00 77.58  ? 86  PRO A CD  1 
ATOM   372   N  N   . PRO A 1 129 ? 102.881 170.810 109.051 1.00 74.95  ? 87  PRO A N   1 
ATOM   373   C  CA  . PRO A 1 129 ? 103.618 171.599 108.060 1.00 78.66  ? 87  PRO A CA  1 
ATOM   374   C  C   . PRO A 1 129 ? 103.022 171.470 106.668 1.00 77.74  ? 87  PRO A C   1 
ATOM   375   O  O   . PRO A 1 129 ? 102.332 170.503 106.338 1.00 78.06  ? 87  PRO A O   1 
ATOM   376   C  CB  . PRO A 1 129 ? 105.026 171.001 108.113 1.00 78.54  ? 87  PRO A CB  1 
ATOM   377   C  CG  . PRO A 1 129 ? 104.804 169.608 108.559 1.00 75.06  ? 87  PRO A CG  1 
ATOM   378   C  CD  . PRO A 1 129 ? 103.667 169.666 109.533 1.00 70.53  ? 87  PRO A CD  1 
ATOM   379   N  N   . GLU A 1 130 ? 103.300 172.474 105.846 1.00 84.21  ? 88  GLU A N   1 
ATOM   380   C  CA  . GLU A 1 130 ? 102.915 172.485 104.442 1.00 87.60  ? 88  GLU A CA  1 
ATOM   381   C  C   . GLU A 1 130 ? 104.143 172.757 103.577 1.00 87.96  ? 88  GLU A C   1 
ATOM   382   O  O   . GLU A 1 130 ? 105.230 173.054 104.075 1.00 87.37  ? 88  GLU A O   1 
ATOM   383   C  CB  . GLU A 1 130 ? 101.815 173.517 104.183 1.00 87.07  ? 88  GLU A CB  1 
ATOM   384   C  CG  . GLU A 1 130 ? 102.188 174.934 104.563 1.00 90.10  ? 88  GLU A CG  1 
ATOM   385   C  CD  . GLU A 1 130 ? 100.978 175.791 104.867 1.00 92.69  ? 88  GLU A CD  1 
ATOM   386   O  OE1 . GLU A 1 130 ? 99.857  175.243 104.917 1.00 92.91  ? 88  GLU A OE1 1 
ATOM   387   O  OE2 . GLU A 1 130 ? 101.147 177.013 105.060 1.00 90.16  ? 88  GLU A OE2 1 
ATOM   388   N  N   . ALA A 1 131 ? 103.952 172.655 102.265 1.00 85.40  ? 89  ALA A N   1 
ATOM   389   C  CA  . ALA A 1 131 ? 105.051 172.817 101.330 1.00 84.55  ? 89  ALA A CA  1 
ATOM   390   C  C   . ALA A 1 131 ? 105.603 174.241 101.394 1.00 86.65  ? 89  ALA A C   1 
ATOM   391   O  O   . ALA A 1 131 ? 104.880 175.179 101.735 1.00 87.27  ? 89  ALA A O   1 
ATOM   392   C  CB  . ALA A 1 131 ? 104.584 172.499 99.912  1.00 88.22  ? 89  ALA A CB  1 
ATOM   393   N  N   . PRO A 1 132 ? 106.889 174.431 101.070 1.00 86.57  ? 90  PRO A N   1 
ATOM   394   C  CA  . PRO A 1 132 ? 107.483 175.769 101.197 1.00 88.14  ? 90  PRO A CA  1 
ATOM   395   C  C   . PRO A 1 132 ? 107.016 176.726 100.114 1.00 94.25  ? 90  PRO A C   1 
ATOM   396   O  O   . PRO A 1 132 ? 106.137 176.397 99.310  1.00 94.20  ? 90  PRO A O   1 
ATOM   397   C  CB  . PRO A 1 132 ? 108.993 175.505 101.088 1.00 80.96  ? 90  PRO A CB  1 
ATOM   398   C  CG  . PRO A 1 132 ? 109.154 174.023 100.948 1.00 81.05  ? 90  PRO A CG  1 
ATOM   399   C  CD  . PRO A 1 132 ? 107.847 173.463 100.520 1.00 80.67  ? 90  PRO A CD  1 
ATOM   400   N  N   . ALA A 1 133 ? 107.599 177.918 100.088 1.00 99.85  ? 91  ALA A N   1 
ATOM   401   C  CA  . ALA A 1 133 ? 107.289 178.928 99.088  1.00 98.91  ? 91  ALA A CA  1 
ATOM   402   C  C   . ALA A 1 133 ? 108.434 179.015 98.092  1.00 100.14 ? 91  ALA A C   1 
ATOM   403   O  O   . ALA A 1 133 ? 109.599 179.123 98.489  1.00 101.92 ? 91  ALA A O   1 
ATOM   404   C  CB  . ALA A 1 133 ? 107.049 180.290 99.742  1.00 98.50  ? 91  ALA A CB  1 
ATOM   405   N  N   . SER A 1 134 ? 108.103 178.961 96.805  1.00 98.27  ? 92  SER A N   1 
ATOM   406   C  CA  . SER A 1 134 ? 109.120 179.089 95.772  1.00 98.45  ? 92  SER A CA  1 
ATOM   407   C  C   . SER A 1 134 ? 109.760 180.469 95.830  1.00 96.86  ? 92  SER A C   1 
ATOM   408   O  O   . SER A 1 134 ? 109.096 181.470 96.111  1.00 98.49  ? 92  SER A O   1 
ATOM   409   C  CB  . SER A 1 134 ? 108.509 178.849 94.392  1.00 99.40  ? 92  SER A CB  1 
ATOM   410   O  OG  . SER A 1 134 ? 107.605 177.760 94.414  1.00 98.09  ? 92  SER A OG  1 
ATOM   411   N  N   . TRP A 1 135 ? 111.064 180.519 95.569  1.00 100.42 ? 93  TRP A N   1 
ATOM   412   C  CA  . TRP A 1 135 ? 111.788 181.774 95.584  1.00 103.81 ? 93  TRP A CA  1 
ATOM   413   C  C   . TRP A 1 135 ? 112.338 182.086 94.199  1.00 106.10 ? 93  TRP A C   1 
ATOM   414   O  O   . TRP A 1 135 ? 112.810 181.182 93.502  1.00 103.52 ? 93  TRP A O   1 
ATOM   415   C  CB  . TRP A 1 135 ? 112.942 181.737 96.594  1.00 102.52 ? 93  TRP A CB  1 
ATOM   416   C  CG  . TRP A 1 135 ? 113.827 180.547 96.435  1.00 103.78 ? 93  TRP A CG  1 
ATOM   417   C  CD1 . TRP A 1 135 ? 114.857 180.403 95.554  1.00 102.77 ? 93  TRP A CD1 1 
ATOM   418   C  CD2 . TRP A 1 135 ? 113.761 179.325 97.179  1.00 106.92 ? 93  TRP A CD2 1 
ATOM   419   N  NE1 . TRP A 1 135 ? 115.435 179.166 95.700  1.00 105.79 ? 93  TRP A NE1 1 
ATOM   420   C  CE2 . TRP A 1 135 ? 114.781 178.486 96.693  1.00 108.76 ? 93  TRP A CE2 1 
ATOM   421   C  CE3 . TRP A 1 135 ? 112.938 178.860 98.208  1.00 105.81 ? 93  TRP A CE3 1 
ATOM   422   C  CZ2 . TRP A 1 135 ? 115.001 177.209 97.203  1.00 105.23 ? 93  TRP A CZ2 1 
ATOM   423   C  CZ3 . TRP A 1 135 ? 113.158 177.595 98.710  1.00 103.66 ? 93  TRP A CZ3 1 
ATOM   424   C  CH2 . TRP A 1 135 ? 114.180 176.783 98.208  1.00 102.04 ? 93  TRP A CH2 1 
ATOM   425   N  N   . PRO A 1 136 ? 112.280 183.343 93.768  1.00 106.62 ? 94  PRO A N   1 
ATOM   426   C  CA  . PRO A 1 136 ? 112.851 183.701 92.468  1.00 103.94 ? 94  PRO A CA  1 
ATOM   427   C  C   . PRO A 1 136 ? 114.356 183.884 92.556  1.00 103.89 ? 94  PRO A C   1 
ATOM   428   O  O   . PRO A 1 136 ? 114.883 184.432 93.527  1.00 103.10 ? 94  PRO A O   1 
ATOM   429   C  CB  . PRO A 1 136 ? 112.149 185.021 92.131  1.00 105.69 ? 94  PRO A CB  1 
ATOM   430   C  CG  . PRO A 1 136 ? 111.862 185.627 93.463  1.00 104.44 ? 94  PRO A CG  1 
ATOM   431   C  CD  . PRO A 1 136 ? 111.618 184.487 94.419  1.00 103.13 ? 94  PRO A CD  1 
ATOM   432   N  N   . GLY A 1 137 ? 115.047 183.415 91.529  1.00 105.69 ? 95  GLY A N   1 
ATOM   433   C  CA  . GLY A 1 137 ? 116.488 183.575 91.439  1.00 107.24 ? 95  GLY A CA  1 
ATOM   434   C  C   . GLY A 1 137 ? 117.225 182.358 91.981  1.00 109.33 ? 95  GLY A C   1 
ATOM   435   O  O   . GLY A 1 137 ? 116.912 181.224 91.621  1.00 110.23 ? 95  GLY A O   1 
ATOM   436   N  N   . VAL A 1 138 ? 118.210 182.601 92.841  1.00 101.52 ? 96  VAL A N   1 
ATOM   437   C  CA  . VAL A 1 138 ? 119.044 181.555 93.417  1.00 99.01  ? 96  VAL A CA  1 
ATOM   438   C  C   . VAL A 1 138 ? 119.085 181.752 94.924  1.00 98.74  ? 96  VAL A C   1 
ATOM   439   O  O   . VAL A 1 138 ? 119.325 182.867 95.399  1.00 97.70  ? 96  VAL A O   1 
ATOM   440   C  CB  . VAL A 1 138 ? 120.468 181.575 92.828  1.00 95.66  ? 96  VAL A CB  1 
ATOM   441   C  CG1 . VAL A 1 138 ? 121.462 180.965 93.798  1.00 94.31  ? 96  VAL A CG1 1 
ATOM   442   C  CG2 . VAL A 1 138 ? 120.500 180.839 91.504  1.00 98.94  ? 96  VAL A CG2 1 
ATOM   443   N  N   . ARG A 1 139 ? 118.840 180.678 95.671  1.00 97.21  ? 97  ARG A N   1 
ATOM   444   C  CA  . ARG A 1 139 ? 118.978 180.681 97.118  1.00 95.99  ? 97  ARG A CA  1 
ATOM   445   C  C   . ARG A 1 139 ? 120.392 180.255 97.485  1.00 94.27  ? 97  ARG A C   1 
ATOM   446   O  O   . ARG A 1 139 ? 121.023 179.466 96.771  1.00 94.32  ? 97  ARG A O   1 
ATOM   447   C  CB  . ARG A 1 139 ? 117.952 179.768 97.789  1.00 94.17  ? 97  ARG A CB  1 
ATOM   448   C  CG  . ARG A 1 139 ? 117.810 180.041 99.278  1.00 93.86  ? 97  ARG A CG  1 
ATOM   449   C  CD  . ARG A 1 139 ? 116.769 179.164 99.944  1.00 94.29  ? 97  ARG A CD  1 
ATOM   450   N  NE  . ARG A 1 139 ? 116.009 179.912 100.939 1.00 97.43  ? 97  ARG A NE  1 
ATOM   451   C  CZ  . ARG A 1 139 ? 116.387 180.080 102.199 1.00 97.28  ? 97  ARG A CZ  1 
ATOM   452   N  NH1 . ARG A 1 139 ? 117.511 179.557 102.659 1.00 92.99  ? 97  ARG A NH1 1 
ATOM   453   N  NH2 . ARG A 1 139 ? 115.618 180.793 103.017 1.00 91.19  ? 97  ARG A NH2 1 
ATOM   454   N  N   . ASN A 1 140 ? 120.872 180.783 98.596  1.00 98.17  ? 98  ASN A N   1 
ATOM   455   C  CA  . ASN A 1 140 ? 122.281 180.786 98.955  1.00 97.64  ? 98  ASN A CA  1 
ATOM   456   C  C   . ASN A 1 140 ? 122.411 179.968 100.235 1.00 100.88 ? 98  ASN A C   1 
ATOM   457   O  O   . ASN A 1 140 ? 122.057 180.438 101.320 1.00 101.41 ? 98  ASN A O   1 
ATOM   458   C  CB  . ASN A 1 140 ? 122.710 182.247 99.083  1.00 102.27 ? 98  ASN A CB  1 
ATOM   459   C  CG  . ASN A 1 140 ? 124.000 182.479 99.842  1.00 105.90 ? 98  ASN A CG  1 
ATOM   460   O  OD1 . ASN A 1 140 ? 124.213 181.990 100.950 1.00 106.53 ? 98  ASN A OD1 1 
ATOM   461   N  ND2 . ASN A 1 140 ? 124.859 183.301 99.249  1.00 106.79 ? 98  ASN A ND2 1 
ATOM   462   N  N   . ALA A 1 141 ? 122.882 178.730 100.096 1.00 90.74  ? 99  ALA A N   1 
ATOM   463   C  CA  . ALA A 1 141 ? 122.853 177.727 101.159 1.00 82.91  ? 99  ALA A CA  1 
ATOM   464   C  C   . ALA A 1 141 ? 124.273 177.234 101.412 1.00 82.31  ? 99  ALA A C   1 
ATOM   465   O  O   . ALA A 1 141 ? 124.707 176.234 100.839 1.00 78.17  ? 99  ALA A O   1 
ATOM   466   C  CB  . ALA A 1 141 ? 121.925 176.579 100.784 1.00 80.57  ? 99  ALA A CB  1 
ATOM   467   N  N   . THR A 1 142 ? 124.994 177.941 102.280 1.00 88.24  ? 100 THR A N   1 
ATOM   468   C  CA  . THR A 1 142 ? 126.350 177.568 102.648 1.00 87.72  ? 100 THR A CA  1 
ATOM   469   C  C   . THR A 1 142 ? 126.588 177.592 104.151 1.00 88.32  ? 100 THR A C   1 
ATOM   470   O  O   . THR A 1 142 ? 127.666 177.186 104.595 1.00 83.81  ? 100 THR A O   1 
ATOM   471   C  CB  . THR A 1 142 ? 127.370 178.494 101.968 1.00 93.41  ? 100 THR A CB  1 
ATOM   472   O  OG1 . THR A 1 142 ? 127.061 179.859 102.276 1.00 94.02  ? 100 THR A OG1 1 
ATOM   473   C  CG2 . THR A 1 142 ? 127.346 178.309 100.461 1.00 90.75  ? 100 THR A CG2 1 
ATOM   474   N  N   . THR A 1 143 ? 125.623 178.054 104.941 1.00 90.40  ? 101 THR A N   1 
ATOM   475   C  CA  . THR A 1 143 ? 125.763 178.163 106.384 1.00 88.56  ? 101 THR A CA  1 
ATOM   476   C  C   . THR A 1 143 ? 124.751 177.258 107.069 1.00 86.77  ? 101 THR A C   1 
ATOM   477   O  O   . THR A 1 143 ? 123.656 177.024 106.553 1.00 86.52  ? 101 THR A O   1 
ATOM   478   C  CB  . THR A 1 143 ? 125.557 179.604 106.858 1.00 90.34  ? 101 THR A CB  1 
ATOM   479   O  OG1 . THR A 1 143 ? 124.175 179.959 106.715 1.00 92.38  ? 101 THR A OG1 1 
ATOM   480   C  CG2 . THR A 1 143 ? 126.409 180.563 106.040 1.00 88.15  ? 101 THR A CG2 1 
ATOM   481   N  N   . LEU A 1 144 ? 125.126 176.755 108.238 1.00 82.26  ? 102 LEU A N   1 
ATOM   482   C  CA  . LEU A 1 144 ? 124.260 175.839 108.970 1.00 81.45  ? 102 LEU A CA  1 
ATOM   483   C  C   . LEU A 1 144 ? 122.989 176.559 109.406 1.00 81.92  ? 102 LEU A C   1 
ATOM   484   O  O   . LEU A 1 144 ? 123.063 177.677 109.925 1.00 81.22  ? 102 LEU A O   1 
ATOM   485   C  CB  . LEU A 1 144 ? 124.989 175.266 110.178 1.00 78.92  ? 102 LEU A CB  1 
ATOM   486   C  CG  . LEU A 1 144 ? 126.124 174.302 109.842 1.00 81.12  ? 102 LEU A CG  1 
ATOM   487   C  CD1 . LEU A 1 144 ? 126.794 173.798 111.105 1.00 81.03  ? 102 LEU A CD1 1 
ATOM   488   C  CD2 . LEU A 1 144 ? 125.601 173.148 109.016 1.00 77.32  ? 102 LEU A CD2 1 
ATOM   489   N  N   . PRO A 1 145 ? 121.819 175.960 109.216 1.00 79.33  ? 103 PRO A N   1 
ATOM   490   C  CA  . PRO A 1 145 ? 120.568 176.646 109.525 1.00 78.04  ? 103 PRO A CA  1 
ATOM   491   C  C   . PRO A 1 145 ? 120.379 176.796 111.022 1.00 80.31  ? 103 PRO A C   1 
ATOM   492   O  O   . PRO A 1 145 ? 121.022 176.089 111.811 1.00 79.98  ? 103 PRO A O   1 
ATOM   493   C  CB  . PRO A 1 145 ? 119.506 175.720 108.919 1.00 77.02  ? 103 PRO A CB  1 
ATOM   494   C  CG  . PRO A 1 145 ? 120.132 174.385 108.945 1.00 78.28  ? 103 PRO A CG  1 
ATOM   495   C  CD  . PRO A 1 145 ? 121.588 174.610 108.680 1.00 80.28  ? 103 PRO A CD  1 
ATOM   496   N  N   . PRO A 1 146 ? 119.516 177.715 111.452 1.00 85.32  ? 104 PRO A N   1 
ATOM   497   C  CA  . PRO A 1 146 ? 119.274 177.881 112.887 1.00 83.02  ? 104 PRO A CA  1 
ATOM   498   C  C   . PRO A 1 146 ? 118.639 176.643 113.502 1.00 82.58  ? 104 PRO A C   1 
ATOM   499   O  O   . PRO A 1 146 ? 117.876 175.921 112.859 1.00 79.89  ? 104 PRO A O   1 
ATOM   500   C  CB  . PRO A 1 146 ? 118.327 179.085 112.948 1.00 78.93  ? 104 PRO A CB  1 
ATOM   501   C  CG  . PRO A 1 146 ? 117.712 179.159 111.601 1.00 79.71  ? 104 PRO A CG  1 
ATOM   502   C  CD  . PRO A 1 146 ? 118.768 178.698 110.653 1.00 81.44  ? 104 PRO A CD  1 
ATOM   503   N  N   . ALA A 1 147 ? 118.968 176.410 114.768 1.00 78.98  ? 105 ALA A N   1 
ATOM   504   C  CA  . ALA A 1 147 ? 118.434 175.294 115.528 1.00 76.79  ? 105 ALA A CA  1 
ATOM   505   C  C   . ALA A 1 147 ? 117.012 175.586 115.995 1.00 82.19  ? 105 ALA A C   1 
ATOM   506   O  O   . ALA A 1 147 ? 116.553 176.730 115.995 1.00 90.36  ? 105 ALA A O   1 
ATOM   507   C  CB  . ALA A 1 147 ? 119.324 175.004 116.732 1.00 77.19  ? 105 ALA A CB  1 
ATOM   508   N  N   . CYS A 1 148 ? 116.308 174.530 116.394 1.00 77.41  ? 106 CYS A N   1 
ATOM   509   C  CA  . CYS A 1 148 ? 114.977 174.722 116.947 1.00 77.53  ? 106 CYS A CA  1 
ATOM   510   C  C   . CYS A 1 148 ? 115.068 175.192 118.397 1.00 81.87  ? 106 CYS A C   1 
ATOM   511   O  O   . CYS A 1 148 ? 116.041 174.890 119.092 1.00 88.59  ? 106 CYS A O   1 
ATOM   512   C  CB  . CYS A 1 148 ? 114.172 173.432 116.871 1.00 78.42  ? 106 CYS A CB  1 
ATOM   513   S  SG  . CYS A 1 148 ? 113.800 172.882 115.195 1.00 90.65  ? 106 CYS A SG  1 
ATOM   514   N  N   . PRO A 1 149 ? 114.077 175.946 118.871 1.00 84.79  ? 107 PRO A N   1 
ATOM   515   C  CA  . PRO A 1 149 ? 114.127 176.437 120.252 1.00 85.96  ? 107 PRO A CA  1 
ATOM   516   C  C   . PRO A 1 149 ? 114.198 175.293 121.250 1.00 83.16  ? 107 PRO A C   1 
ATOM   517   O  O   . PRO A 1 149 ? 113.486 174.294 121.133 1.00 86.16  ? 107 PRO A O   1 
ATOM   518   C  CB  . PRO A 1 149 ? 112.822 177.227 120.392 1.00 87.04  ? 107 PRO A CB  1 
ATOM   519   C  CG  . PRO A 1 149 ? 112.482 177.627 119.006 1.00 85.08  ? 107 PRO A CG  1 
ATOM   520   C  CD  . PRO A 1 149 ? 112.918 176.486 118.142 1.00 84.36  ? 107 PRO A CD  1 
ATOM   521   N  N   . GLN A 1 150 ? 115.066 175.457 122.244 1.00 76.79  ? 108 GLN A N   1 
ATOM   522   C  CA  . GLN A 1 150 ? 115.284 174.443 123.264 1.00 72.08  ? 108 GLN A CA  1 
ATOM   523   C  C   . GLN A 1 150 ? 115.996 175.091 124.439 1.00 80.79  ? 108 GLN A C   1 
ATOM   524   O  O   . GLN A 1 150 ? 116.587 176.165 124.314 1.00 87.06  ? 108 GLN A O   1 
ATOM   525   C  CB  . GLN A 1 150 ? 116.097 173.270 122.716 1.00 69.07  ? 108 GLN A CB  1 
ATOM   526   C  CG  . GLN A 1 150 ? 117.374 173.697 122.034 1.00 74.32  ? 108 GLN A CG  1 
ATOM   527   C  CD  . GLN A 1 150 ? 117.997 172.590 121.225 1.00 77.91  ? 108 GLN A CD  1 
ATOM   528   O  OE1 . GLN A 1 150 ? 118.988 171.991 121.634 1.00 81.80  ? 108 GLN A OE1 1 
ATOM   529   N  NE2 . GLN A 1 150 ? 117.420 172.310 120.066 1.00 75.20  ? 108 GLN A NE2 1 
ATOM   530   N  N   . ASN A 1 151 ? 115.936 174.420 125.585 1.00 88.77  ? 109 ASN A N   1 
ATOM   531   C  CA  . ASN A 1 151 ? 116.565 174.889 126.818 1.00 88.80  ? 109 ASN A CA  1 
ATOM   532   C  C   . ASN A 1 151 ? 117.560 173.819 127.251 1.00 86.31  ? 109 ASN A C   1 
ATOM   533   O  O   . ASN A 1 151 ? 117.235 172.938 128.049 1.00 86.67  ? 109 ASN A O   1 
ATOM   534   C  CB  . ASN A 1 151 ? 115.523 175.166 127.896 1.00 89.53  ? 109 ASN A CB  1 
ATOM   535   C  CG  . ASN A 1 151 ? 116.099 175.897 129.088 1.00 90.31  ? 109 ASN A CG  1 
ATOM   536   O  OD1 . ASN A 1 151 ? 117.227 176.384 129.045 1.00 91.98  ? 109 ASN A OD1 1 
ATOM   537   N  ND2 . ASN A 1 151 ? 115.325 175.979 130.162 1.00 89.01  ? 109 ASN A ND2 1 
ATOM   538   N  N   . LEU A 1 152 ? 118.778 173.902 126.715 1.00 82.62  ? 110 LEU A N   1 
ATOM   539   C  CA  . LEU A 1 152 ? 119.780 172.881 126.997 1.00 84.99  ? 110 LEU A CA  1 
ATOM   540   C  C   . LEU A 1 152 ? 120.206 172.907 128.459 1.00 89.99  ? 110 LEU A C   1 
ATOM   541   O  O   . LEU A 1 152 ? 120.398 171.852 129.074 1.00 91.11  ? 110 LEU A O   1 
ATOM   542   C  CB  . LEU A 1 152 ? 120.988 173.072 126.084 1.00 85.64  ? 110 LEU A CB  1 
ATOM   543   C  CG  . LEU A 1 152 ? 121.704 171.791 125.669 1.00 84.29  ? 110 LEU A CG  1 
ATOM   544   C  CD1 . LEU A 1 152 ? 120.765 170.934 124.851 1.00 83.59  ? 110 LEU A CD1 1 
ATOM   545   C  CD2 . LEU A 1 152 ? 122.958 172.109 124.885 1.00 85.62  ? 110 LEU A CD2 1 
ATOM   546   N  N   . HIS A 1 153 ? 120.365 174.095 129.032 1.00 102.08 ? 111 HIS A N   1 
ATOM   547   C  CA  . HIS A 1 153 ? 120.805 174.236 130.420 1.00 102.15 ? 111 HIS A CA  1 
ATOM   548   C  C   . HIS A 1 153 ? 119.627 174.201 131.387 1.00 102.70 ? 111 HIS A C   1 
ATOM   549   O  O   . HIS A 1 153 ? 119.457 175.078 132.233 1.00 101.20 ? 111 HIS A O   1 
ATOM   550   C  CB  . HIS A 1 153 ? 121.610 175.519 130.577 1.00 99.05  ? 111 HIS A CB  1 
ATOM   551   C  CG  . HIS A 1 153 ? 122.712 175.660 129.575 1.00 103.13 ? 111 HIS A CG  1 
ATOM   552   N  ND1 . HIS A 1 153 ? 123.930 175.032 129.716 1.00 105.78 ? 111 HIS A ND1 1 
ATOM   553   C  CD2 . HIS A 1 153 ? 122.776 176.348 128.411 1.00 102.89 ? 111 HIS A CD2 1 
ATOM   554   C  CE1 . HIS A 1 153 ? 124.699 175.331 128.685 1.00 105.52 ? 111 HIS A CE1 1 
ATOM   555   N  NE2 . HIS A 1 153 ? 124.022 176.128 127.878 1.00 104.06 ? 111 HIS A NE2 1 
ATOM   556   N  N   . GLY A 1 154 ? 118.804 173.165 131.263 1.00 96.40  ? 112 GLY A N   1 
ATOM   557   C  CA  . GLY A 1 154 ? 117.659 172.993 132.132 1.00 93.34  ? 112 GLY A CA  1 
ATOM   558   C  C   . GLY A 1 154 ? 117.594 171.599 132.716 1.00 95.04  ? 112 GLY A C   1 
ATOM   559   O  O   . GLY A 1 154 ? 118.598 170.882 132.737 1.00 94.84  ? 112 GLY A O   1 
ATOM   560   N  N   . ALA A 1 155 ? 116.417 171.202 133.194 1.00 97.43  ? 113 ALA A N   1 
ATOM   561   C  CA  . ALA A 1 155 ? 116.236 169.878 133.788 1.00 95.34  ? 113 ALA A CA  1 
ATOM   562   C  C   . ALA A 1 155 ? 115.865 168.876 132.694 1.00 97.22  ? 113 ALA A C   1 
ATOM   563   O  O   . ALA A 1 155 ? 114.726 168.424 132.563 1.00 94.45  ? 113 ALA A O   1 
ATOM   564   C  CB  . ALA A 1 155 ? 115.187 169.929 134.890 1.00 93.07  ? 113 ALA A CB  1 
ATOM   565   N  N   . LEU A 1 156 ? 116.871 168.537 131.893 1.00 95.40  ? 114 LEU A N   1 
ATOM   566   C  CA  . LEU A 1 156 ? 116.694 167.569 130.827 1.00 90.48  ? 114 LEU A CA  1 
ATOM   567   C  C   . LEU A 1 156 ? 116.523 166.168 131.403 1.00 92.02  ? 114 LEU A C   1 
ATOM   568   O  O   . LEU A 1 156 ? 116.957 165.889 132.523 1.00 92.59  ? 114 LEU A O   1 
ATOM   569   C  CB  . LEU A 1 156 ? 117.894 167.590 129.886 1.00 89.28  ? 114 LEU A CB  1 
ATOM   570   C  CG  . LEU A 1 156 ? 118.071 168.812 128.991 1.00 91.60  ? 114 LEU A CG  1 
ATOM   571   C  CD1 . LEU A 1 156 ? 119.445 168.786 128.353 1.00 90.10  ? 114 LEU A CD1 1 
ATOM   572   C  CD2 . LEU A 1 156 ? 116.984 168.851 127.934 1.00 91.24  ? 114 LEU A CD2 1 
ATOM   573   N  N   . PRO A 1 157 ? 115.887 165.263 130.655 1.00 83.03  ? 115 PRO A N   1 
ATOM   574   C  CA  . PRO A 1 157 ? 115.901 163.852 131.055 1.00 81.60  ? 115 PRO A CA  1 
ATOM   575   C  C   . PRO A 1 157 ? 117.289 163.272 130.866 1.00 78.19  ? 115 PRO A C   1 
ATOM   576   O  O   . PRO A 1 157 ? 117.721 163.034 129.736 1.00 78.84  ? 115 PRO A O   1 
ATOM   577   C  CB  . PRO A 1 157 ? 114.876 163.203 130.116 1.00 73.11  ? 115 PRO A CB  1 
ATOM   578   C  CG  . PRO A 1 157 ? 114.073 164.340 129.565 1.00 74.94  ? 115 PRO A CG  1 
ATOM   579   C  CD  . PRO A 1 157 ? 115.013 165.495 129.496 1.00 76.86  ? 115 PRO A CD  1 
ATOM   580   N  N   . ALA A 1 158 ? 117.995 163.039 131.965 1.00 60.50  ? 116 ALA A N   1 
ATOM   581   C  CA  . ALA A 1 158 ? 119.418 162.747 131.924 1.00 58.79  ? 116 ALA A CA  1 
ATOM   582   C  C   . ALA A 1 158 ? 119.723 161.266 131.780 1.00 59.96  ? 116 ALA A C   1 
ATOM   583   O  O   . ALA A 1 158 ? 120.889 160.877 131.883 1.00 63.88  ? 116 ALA A O   1 
ATOM   584   C  CB  . ALA A 1 158 ? 120.103 163.295 133.178 1.00 62.44  ? 116 ALA A CB  1 
ATOM   585   N  N   . ILE A 1 159 ? 118.715 160.430 131.556 1.00 58.34  ? 117 ILE A N   1 
ATOM   586   C  CA  . ILE A 1 159 ? 118.928 159.004 131.369 1.00 63.13  ? 117 ILE A CA  1 
ATOM   587   C  C   . ILE A 1 159 ? 118.858 158.610 129.900 1.00 63.98  ? 117 ILE A C   1 
ATOM   588   O  O   . ILE A 1 159 ? 119.697 157.848 129.420 1.00 63.41  ? 117 ILE A O   1 
ATOM   589   C  CB  . ILE A 1 159 ? 117.917 158.196 132.207 1.00 57.21  ? 117 ILE A CB  1 
ATOM   590   C  CG1 . ILE A 1 159 ? 117.954 158.654 133.660 1.00 58.51  ? 117 ILE A CG1 1 
ATOM   591   C  CG2 . ILE A 1 159 ? 118.230 156.724 132.116 1.00 52.61  ? 117 ILE A CG2 1 
ATOM   592   C  CD1 . ILE A 1 159 ? 117.334 157.676 134.621 1.00 57.93  ? 117 ILE A CD1 1 
ATOM   593   N  N   . MET A 1 160 ? 117.870 159.120 129.170 1.00 56.56  ? 118 MET A N   1 
ATOM   594   C  CA  . MET A 1 160 ? 117.686 158.726 127.783 1.00 52.17  ? 118 MET A CA  1 
ATOM   595   C  C   . MET A 1 160 ? 118.673 159.387 126.834 1.00 61.06  ? 118 MET A C   1 
ATOM   596   O  O   . MET A 1 160 ? 118.803 158.930 125.694 1.00 67.97  ? 118 MET A O   1 
ATOM   597   C  CB  . MET A 1 160 ? 116.259 159.039 127.335 1.00 57.20  ? 118 MET A CB  1 
ATOM   598   C  CG  . MET A 1 160 ? 115.632 160.221 128.041 1.00 58.73  ? 118 MET A CG  1 
ATOM   599   S  SD  . MET A 1 160 ? 113.847 160.269 127.829 1.00 70.89  ? 118 MET A SD  1 
ATOM   600   C  CE  . MET A 1 160 ? 113.714 159.992 126.069 1.00 54.86  ? 118 MET A CE  1 
ATOM   601   N  N   . LEU A 1 161 ? 119.362 160.440 127.263 1.00 55.66  ? 119 LEU A N   1 
ATOM   602   C  CA  . LEU A 1 161 ? 120.284 161.131 126.378 1.00 55.87  ? 119 LEU A CA  1 
ATOM   603   C  C   . LEU A 1 161 ? 121.539 160.292 126.146 1.00 54.65  ? 119 LEU A C   1 
ATOM   604   O  O   . LEU A 1 161 ? 121.937 159.504 127.006 1.00 53.19  ? 119 LEU A O   1 
ATOM   605   C  CB  . LEU A 1 161 ? 120.669 162.484 126.961 1.00 50.34  ? 119 LEU A CB  1 
ATOM   606   C  CG  . LEU A 1 161 ? 119.551 163.514 127.077 1.00 48.56  ? 119 LEU A CG  1 
ATOM   607   C  CD1 . LEU A 1 161 ? 120.126 164.890 127.333 1.00 54.36  ? 119 LEU A CD1 1 
ATOM   608   C  CD2 . LEU A 1 161 ? 118.711 163.514 125.825 1.00 47.68  ? 119 LEU A CD2 1 
ATOM   609   N  N   . PRO A 1 162 ? 122.176 160.438 124.986 1.00 55.09  ? 120 PRO A N   1 
ATOM   610   C  CA  . PRO A 1 162 ? 123.440 159.738 124.752 1.00 55.03  ? 120 PRO A CA  1 
ATOM   611   C  C   . PRO A 1 162 ? 124.502 160.218 125.723 1.00 60.39  ? 120 PRO A C   1 
ATOM   612   O  O   . PRO A 1 162 ? 124.480 161.358 126.186 1.00 73.92  ? 120 PRO A O   1 
ATOM   613   C  CB  . PRO A 1 162 ? 123.790 160.110 123.309 1.00 57.12  ? 120 PRO A CB  1 
ATOM   614   C  CG  . PRO A 1 162 ? 122.497 160.506 122.699 1.00 58.12  ? 120 PRO A CG  1 
ATOM   615   C  CD  . PRO A 1 162 ? 121.746 161.185 123.796 1.00 56.48  ? 120 PRO A CD  1 
ATOM   616   N  N   . VAL A 1 163 ? 125.439 159.325 126.039 1.00 56.76  ? 121 VAL A N   1 
ATOM   617   C  CA  . VAL A 1 163 ? 126.432 159.633 127.061 1.00 56.79  ? 121 VAL A CA  1 
ATOM   618   C  C   . VAL A 1 163 ? 127.344 160.768 126.610 1.00 60.41  ? 121 VAL A C   1 
ATOM   619   O  O   . VAL A 1 163 ? 127.684 161.657 127.401 1.00 63.36  ? 121 VAL A O   1 
ATOM   620   C  CB  . VAL A 1 163 ? 127.219 158.365 127.432 1.00 56.08  ? 121 VAL A CB  1 
ATOM   621   C  CG1 . VAL A 1 163 ? 128.605 158.719 127.918 1.00 58.21  ? 121 VAL A CG1 1 
ATOM   622   C  CG2 . VAL A 1 163 ? 126.473 157.595 128.502 1.00 57.95  ? 121 VAL A CG2 1 
ATOM   623   N  N   . TRP A 1 164 ? 127.750 160.770 125.337 1.00 57.98  ? 122 TRP A N   1 
ATOM   624   C  CA  . TRP A 1 164 ? 128.604 161.849 124.855 1.00 55.32  ? 122 TRP A CA  1 
ATOM   625   C  C   . TRP A 1 164 ? 127.898 163.196 124.877 1.00 53.40  ? 122 TRP A C   1 
ATOM   626   O  O   . TRP A 1 164 ? 128.569 164.231 124.914 1.00 63.93  ? 122 TRP A O   1 
ATOM   627   C  CB  . TRP A 1 164 ? 129.115 161.553 123.442 1.00 58.64  ? 122 TRP A CB  1 
ATOM   628   C  CG  . TRP A 1 164 ? 128.054 161.222 122.435 1.00 63.57  ? 122 TRP A CG  1 
ATOM   629   C  CD1 . TRP A 1 164 ? 127.733 159.984 121.973 1.00 64.69  ? 122 TRP A CD1 1 
ATOM   630   C  CD2 . TRP A 1 164 ? 127.195 162.141 121.746 1.00 60.22  ? 122 TRP A CD2 1 
ATOM   631   N  NE1 . TRP A 1 164 ? 126.721 160.069 121.051 1.00 62.55  ? 122 TRP A NE1 1 
ATOM   632   C  CE2 . TRP A 1 164 ? 126.374 161.384 120.894 1.00 58.44  ? 122 TRP A CE2 1 
ATOM   633   C  CE3 . TRP A 1 164 ? 127.039 163.528 121.770 1.00 57.96  ? 122 TRP A CE3 1 
ATOM   634   C  CZ2 . TRP A 1 164 ? 125.410 161.965 120.081 1.00 55.48  ? 122 TRP A CZ2 1 
ATOM   635   C  CZ3 . TRP A 1 164 ? 126.083 164.101 120.963 1.00 50.50  ? 122 TRP A CZ3 1 
ATOM   636   C  CH2 . TRP A 1 164 ? 125.281 163.323 120.130 1.00 51.75  ? 122 TRP A CH2 1 
ATOM   637   N  N   . PHE A 1 165 ? 126.567 163.213 124.845 1.00 54.34  ? 123 PHE A N   1 
ATOM   638   C  CA  . PHE A 1 165 ? 125.850 164.480 124.916 1.00 50.72  ? 123 PHE A CA  1 
ATOM   639   C  C   . PHE A 1 165 ? 125.902 165.056 126.323 1.00 53.47  ? 123 PHE A C   1 
ATOM   640   O  O   . PHE A 1 165 ? 126.158 166.251 126.506 1.00 66.41  ? 123 PHE A O   1 
ATOM   641   C  CB  . PHE A 1 165 ? 124.404 164.294 124.464 1.00 57.42  ? 123 PHE A CB  1 
ATOM   642   C  CG  . PHE A 1 165 ? 123.667 165.579 124.263 1.00 57.43  ? 123 PHE A CG  1 
ATOM   643   C  CD1 . PHE A 1 165 ? 122.983 166.171 125.304 1.00 59.39  ? 123 PHE A CD1 1 
ATOM   644   C  CD2 . PHE A 1 165 ? 123.662 166.198 123.032 1.00 58.54  ? 123 PHE A CD2 1 
ATOM   645   C  CE1 . PHE A 1 165 ? 122.309 167.356 125.120 1.00 58.70  ? 123 PHE A CE1 1 
ATOM   646   C  CE2 . PHE A 1 165 ? 122.990 167.380 122.844 1.00 63.72  ? 123 PHE A CE2 1 
ATOM   647   C  CZ  . PHE A 1 165 ? 122.314 167.960 123.889 1.00 60.35  ? 123 PHE A CZ  1 
ATOM   648   N  N   . THR A 1 166 ? 125.664 164.221 127.332 1.00 55.44  ? 124 THR A N   1 
ATOM   649   C  CA  . THR A 1 166 ? 125.638 164.696 128.707 1.00 62.65  ? 124 THR A CA  1 
ATOM   650   C  C   . THR A 1 166 ? 127.024 164.827 129.322 1.00 66.25  ? 124 THR A C   1 
ATOM   651   O  O   . THR A 1 166 ? 127.158 165.474 130.365 1.00 68.04  ? 124 THR A O   1 
ATOM   652   C  CB  . THR A 1 166 ? 124.783 163.770 129.567 1.00 57.71  ? 124 THR A CB  1 
ATOM   653   O  OG1 . THR A 1 166 ? 125.304 162.439 129.500 1.00 58.90  ? 124 THR A OG1 1 
ATOM   654   C  CG2 . THR A 1 166 ? 123.356 163.771 129.065 1.00 57.56  ? 124 THR A CG2 1 
ATOM   655   N  N   . ASP A 1 167 ? 128.052 164.235 128.713 1.00 67.11  ? 125 ASP A N   1 
ATOM   656   C  CA  . ASP A 1 167 ? 129.413 164.468 129.182 1.00 65.31  ? 125 ASP A CA  1 
ATOM   657   C  C   . ASP A 1 167 ? 129.939 165.806 128.677 1.00 67.51  ? 125 ASP A C   1 
ATOM   658   O  O   . ASP A 1 167 ? 130.307 166.681 129.467 1.00 72.43  ? 125 ASP A O   1 
ATOM   659   C  CB  . ASP A 1 167 ? 130.331 163.329 128.737 1.00 67.35  ? 125 ASP A CB  1 
ATOM   660   C  CG  . ASP A 1 167 ? 130.218 162.112 129.626 1.00 72.58  ? 125 ASP A CG  1 
ATOM   661   O  OD1 . ASP A 1 167 ? 129.243 162.035 130.402 1.00 69.20  ? 125 ASP A OD1 1 
ATOM   662   O  OD2 . ASP A 1 167 ? 131.103 161.234 129.553 1.00 71.56  ? 125 ASP A OD2 1 
ATOM   663   N  N   . ASN A 1 168 ? 129.973 165.981 127.360 1.00 70.41  ? 126 ASN A N   1 
ATOM   664   C  CA  . ASN A 1 168 ? 130.447 167.223 126.751 1.00 70.97  ? 126 ASN A CA  1 
ATOM   665   C  C   . ASN A 1 168 ? 129.271 168.162 126.478 1.00 73.31  ? 126 ASN A C   1 
ATOM   666   O  O   . ASN A 1 168 ? 128.993 168.556 125.348 1.00 74.40  ? 126 ASN A O   1 
ATOM   667   C  CB  . ASN A 1 168 ? 131.221 166.914 125.477 1.00 73.08  ? 126 ASN A CB  1 
ATOM   668   C  CG  . ASN A 1 168 ? 131.962 165.600 125.558 1.00 76.85  ? 126 ASN A CG  1 
ATOM   669   O  OD1 . ASN A 1 168 ? 131.811 164.734 124.699 1.00 79.75  ? 126 ASN A OD1 1 
ATOM   670   N  ND2 . ASN A 1 168 ? 132.774 165.444 126.595 1.00 76.33  ? 126 ASN A ND2 1 
ATOM   671   N  N   . LEU A 1 169 ? 128.572 168.514 127.558 1.00 76.55  ? 127 LEU A N   1 
ATOM   672   C  CA  . LEU A 1 169 ? 127.380 169.343 127.423 1.00 75.27  ? 127 LEU A CA  1 
ATOM   673   C  C   . LEU A 1 169 ? 127.726 170.781 127.070 1.00 80.83  ? 127 LEU A C   1 
ATOM   674   O  O   . LEU A 1 169 ? 126.930 171.464 126.417 1.00 84.56  ? 127 LEU A O   1 
ATOM   675   C  CB  . LEU A 1 169 ? 126.562 169.297 128.712 1.00 75.76  ? 127 LEU A CB  1 
ATOM   676   C  CG  . LEU A 1 169 ? 125.148 169.867 128.636 1.00 78.14  ? 127 LEU A CG  1 
ATOM   677   C  CD1 . LEU A 1 169 ? 124.384 169.227 127.495 1.00 77.12  ? 127 LEU A CD1 1 
ATOM   678   C  CD2 . LEU A 1 169 ? 124.423 169.658 129.951 1.00 80.88  ? 127 LEU A CD2 1 
ATOM   679   N  N   . GLU A 1 170 ? 128.895 171.264 127.494 1.00 88.69  ? 128 GLU A N   1 
ATOM   680   C  CA  . GLU A 1 170 ? 129.285 172.632 127.166 1.00 87.18  ? 128 GLU A CA  1 
ATOM   681   C  C   . GLU A 1 170 ? 129.599 172.780 125.683 1.00 85.65  ? 128 GLU A C   1 
ATOM   682   O  O   . GLU A 1 170 ? 129.293 173.814 125.080 1.00 84.47  ? 128 GLU A O   1 
ATOM   683   C  CB  . GLU A 1 170 ? 130.476 173.062 128.024 1.00 87.82  ? 128 GLU A CB  1 
ATOM   684   C  CG  . GLU A 1 170 ? 131.754 172.275 127.785 1.00 90.01  ? 128 GLU A CG  1 
ATOM   685   C  CD  . GLU A 1 170 ? 132.068 171.316 128.915 1.00 93.99  ? 128 GLU A CD  1 
ATOM   686   O  OE1 . GLU A 1 170 ? 131.237 171.192 129.839 1.00 92.98  ? 128 GLU A OE1 1 
ATOM   687   O  OE2 . GLU A 1 170 ? 133.144 170.684 128.879 1.00 95.85  ? 128 GLU A OE2 1 
ATOM   688   N  N   . ALA A 1 171 ? 130.206 171.759 125.074 1.00 80.48  ? 129 ALA A N   1 
ATOM   689   C  CA  . ALA A 1 171 ? 130.496 171.823 123.647 1.00 77.83  ? 129 ALA A CA  1 
ATOM   690   C  C   . ALA A 1 171 ? 129.239 171.630 122.812 1.00 79.32  ? 129 ALA A C   1 
ATOM   691   O  O   . ALA A 1 171 ? 129.150 172.160 121.700 1.00 80.37  ? 129 ALA A O   1 
ATOM   692   C  CB  . ALA A 1 171 ? 131.545 170.778 123.273 1.00 78.54  ? 129 ALA A CB  1 
ATOM   693   N  N   . ALA A 1 172 ? 128.266 170.875 123.323 1.00 85.48  ? 130 ALA A N   1 
ATOM   694   C  CA  . ALA A 1 172 ? 127.013 170.686 122.603 1.00 83.17  ? 130 ALA A CA  1 
ATOM   695   C  C   . ALA A 1 172 ? 126.180 171.958 122.552 1.00 85.13  ? 130 ALA A C   1 
ATOM   696   O  O   . ALA A 1 172 ? 125.335 172.093 121.663 1.00 87.67  ? 130 ALA A O   1 
ATOM   697   C  CB  . ALA A 1 172 ? 126.205 169.557 123.240 1.00 72.22  ? 130 ALA A CB  1 
ATOM   698   N  N   . ALA A 1 173 ? 126.393 172.887 123.482 1.00 82.45  ? 131 ALA A N   1 
ATOM   699   C  CA  . ALA A 1 173 ? 125.689 174.161 123.451 1.00 80.35  ? 131 ALA A CA  1 
ATOM   700   C  C   . ALA A 1 173 ? 126.223 175.102 122.382 1.00 81.40  ? 131 ALA A C   1 
ATOM   701   O  O   . ALA A 1 173 ? 125.561 176.097 122.069 1.00 86.59  ? 131 ALA A O   1 
ATOM   702   C  CB  . ALA A 1 173 ? 125.766 174.840 124.821 1.00 78.50  ? 131 ALA A CB  1 
ATOM   703   N  N   . THR A 1 174 ? 127.404 174.822 121.827 1.00 79.96  ? 132 THR A N   1 
ATOM   704   C  CA  . THR A 1 174 ? 127.912 175.625 120.721 1.00 80.26  ? 132 THR A CA  1 
ATOM   705   C  C   . THR A 1 174 ? 126.999 175.529 119.508 1.00 84.20  ? 132 THR A C   1 
ATOM   706   O  O   . THR A 1 174 ? 126.682 176.544 118.878 1.00 85.14  ? 132 THR A O   1 
ATOM   707   C  CB  . THR A 1 174 ? 129.327 175.177 120.356 1.00 80.79  ? 132 THR A CB  1 
ATOM   708   O  OG1 . THR A 1 174 ? 130.229 175.537 121.408 1.00 85.33  ? 132 THR A OG1 1 
ATOM   709   C  CG2 . THR A 1 174 ? 129.776 175.823 119.061 1.00 79.47  ? 132 THR A CG2 1 
ATOM   710   N  N   . TYR A 1 175 ? 126.562 174.316 119.169 1.00 81.04  ? 133 TYR A N   1 
ATOM   711   C  CA  . TYR A 1 175 ? 125.708 174.135 118.001 1.00 78.15  ? 133 TYR A CA  1 
ATOM   712   C  C   . TYR A 1 175 ? 124.337 174.767 118.210 1.00 79.97  ? 133 TYR A C   1 
ATOM   713   O  O   . TYR A 1 175 ? 123.781 175.372 117.286 1.00 80.60  ? 133 TYR A O   1 
ATOM   714   C  CB  . TYR A 1 175 ? 125.585 172.650 117.677 1.00 70.14  ? 133 TYR A CB  1 
ATOM   715   C  CG  . TYR A 1 175 ? 126.922 171.992 117.439 1.00 71.52  ? 133 TYR A CG  1 
ATOM   716   C  CD1 . TYR A 1 175 ? 127.556 172.091 116.212 1.00 73.47  ? 133 TYR A CD1 1 
ATOM   717   C  CD2 . TYR A 1 175 ? 127.560 171.291 118.448 1.00 73.51  ? 133 TYR A CD2 1 
ATOM   718   C  CE1 . TYR A 1 175 ? 128.779 171.496 115.993 1.00 71.84  ? 133 TYR A CE1 1 
ATOM   719   C  CE2 . TYR A 1 175 ? 128.782 170.694 118.238 1.00 74.98  ? 133 TYR A CE2 1 
ATOM   720   C  CZ  . TYR A 1 175 ? 129.388 170.800 117.009 1.00 73.89  ? 133 TYR A CZ  1 
ATOM   721   O  OH  . TYR A 1 175 ? 130.607 170.206 116.795 1.00 76.39  ? 133 TYR A OH  1 
ATOM   722   N  N   . VAL A 1 176 ? 123.778 174.645 119.409 1.00 84.51  ? 134 VAL A N   1 
ATOM   723   C  CA  . VAL A 1 176 ? 122.482 175.272 119.718 1.00 81.46  ? 134 VAL A CA  1 
ATOM   724   C  C   . VAL A 1 176 ? 122.795 176.665 120.262 1.00 84.37  ? 134 VAL A C   1 
ATOM   725   O  O   . VAL A 1 176 ? 122.853 176.926 121.466 1.00 86.53  ? 134 VAL A O   1 
ATOM   726   C  CB  . VAL A 1 176 ? 121.612 174.389 120.634 1.00 79.91  ? 134 VAL A CB  1 
ATOM   727   C  CG1 . VAL A 1 176 ? 121.684 172.965 120.146 1.00 81.98  ? 134 VAL A CG1 1 
ATOM   728   C  CG2 . VAL A 1 176 ? 122.081 174.364 122.082 1.00 81.14  ? 134 VAL A CG2 1 
ATOM   729   N  N   . GLN A 1 177 ? 123.015 177.593 119.335 1.00 88.99  ? 135 GLN A N   1 
ATOM   730   C  CA  . GLN A 1 177 ? 123.328 178.965 119.708 1.00 87.53  ? 135 GLN A CA  1 
ATOM   731   C  C   . GLN A 1 177 ? 122.396 179.927 118.989 1.00 89.65  ? 135 GLN A C   1 
ATOM   732   O  O   . GLN A 1 177 ? 122.084 181.005 119.504 1.00 89.30  ? 135 GLN A O   1 
ATOM   733   C  CB  . GLN A 1 177 ? 124.786 179.289 119.387 1.00 88.25  ? 135 GLN A CB  1 
ATOM   734   C  CG  . GLN A 1 177 ? 125.399 180.336 120.296 1.00 90.70  ? 135 GLN A CG  1 
ATOM   735   C  CD  . GLN A 1 177 ? 126.878 180.112 120.522 1.00 93.64  ? 135 GLN A CD  1 
ATOM   736   O  OE1 . GLN A 1 177 ? 127.665 180.080 119.577 1.00 96.45  ? 135 GLN A OE1 1 
ATOM   737   N  NE2 . GLN A 1 177 ? 127.265 179.953 121.782 1.00 91.45  ? 135 GLN A NE2 1 
ATOM   738   N  N   . ASN A 1 178 ? 121.938 179.535 117.806 1.00 89.97  ? 136 ASN A N   1 
ATOM   739   C  CA  . ASN A 1 178 ? 121.058 180.352 116.980 1.00 92.97  ? 136 ASN A CA  1 
ATOM   740   C  C   . ASN A 1 178 ? 119.643 179.784 116.955 1.00 91.99  ? 136 ASN A C   1 
ATOM   741   O  O   . ASN A 1 178 ? 118.994 179.738 115.910 1.00 89.64  ? 136 ASN A O   1 
ATOM   742   C  CB  . ASN A 1 178 ? 121.613 180.475 115.565 1.00 92.01  ? 136 ASN A CB  1 
ATOM   743   C  CG  . ASN A 1 178 ? 121.377 181.844 114.967 1.00 95.50  ? 136 ASN A CG  1 
ATOM   744   O  OD1 . ASN A 1 178 ? 120.366 182.488 115.244 1.00 94.81  ? 136 ASN A OD1 1 
ATOM   745   N  ND2 . ASN A 1 178 ? 122.312 182.296 114.141 1.00 92.02  ? 136 ASN A ND2 1 
ATOM   746   N  N   . GLN A 1 179 ? 119.159 179.333 118.109 1.00 86.19  ? 137 GLN A N   1 
ATOM   747   C  CA  . GLN A 1 179 ? 117.833 178.737 118.196 1.00 81.93  ? 137 GLN A CA  1 
ATOM   748   C  C   . GLN A 1 179 ? 116.766 179.723 117.743 1.00 85.42  ? 137 GLN A C   1 
ATOM   749   O  O   . GLN A 1 179 ? 116.579 180.776 118.357 1.00 90.45  ? 137 GLN A O   1 
ATOM   750   C  CB  . GLN A 1 179 ? 117.562 178.285 119.628 1.00 78.19  ? 137 GLN A CB  1 
ATOM   751   C  CG  . GLN A 1 179 ? 118.720 177.556 120.271 1.00 82.28  ? 137 GLN A CG  1 
ATOM   752   C  CD  . GLN A 1 179 ? 118.594 177.488 121.775 1.00 86.58  ? 137 GLN A CD  1 
ATOM   753   O  OE1 . GLN A 1 179 ? 117.639 178.003 122.352 1.00 84.51  ? 137 GLN A OE1 1 
ATOM   754   N  NE2 . GLN A 1 179 ? 119.562 176.850 122.421 1.00 87.09  ? 137 GLN A NE2 1 
ATOM   755   N  N   . SER A 1 180 ? 116.067 179.379 116.665 1.00 80.12  ? 138 SER A N   1 
ATOM   756   C  CA  . SER A 1 180 ? 114.960 180.174 116.161 1.00 78.43  ? 138 SER A CA  1 
ATOM   757   C  C   . SER A 1 180 ? 113.801 179.254 115.816 1.00 78.70  ? 138 SER A C   1 
ATOM   758   O  O   . SER A 1 180 ? 113.997 178.083 115.488 1.00 77.60  ? 138 SER A O   1 
ATOM   759   C  CB  . SER A 1 180 ? 115.361 180.988 114.931 1.00 79.69  ? 138 SER A CB  1 
ATOM   760   O  OG  . SER A 1 180 ? 115.372 180.175 113.772 1.00 84.65  ? 138 SER A OG  1 
ATOM   761   N  N   . GLU A 1 181 ? 112.586 179.800 115.888 1.00 85.55  ? 139 GLU A N   1 
ATOM   762   C  CA  . GLU A 1 181 ? 111.394 178.981 115.690 1.00 86.30  ? 139 GLU A CA  1 
ATOM   763   C  C   . GLU A 1 181 ? 111.316 178.434 114.270 1.00 88.94  ? 139 GLU A C   1 
ATOM   764   O  O   . GLU A 1 181 ? 110.901 177.288 114.064 1.00 88.31  ? 139 GLU A O   1 
ATOM   765   C  CB  . GLU A 1 181 ? 110.142 179.787 116.026 1.00 86.38  ? 139 GLU A CB  1 
ATOM   766   C  CG  . GLU A 1 181 ? 108.879 178.951 116.107 1.00 85.64  ? 139 GLU A CG  1 
ATOM   767   C  CD  . GLU A 1 181 ? 107.807 179.595 116.958 1.00 88.78  ? 139 GLU A CD  1 
ATOM   768   O  OE1 . GLU A 1 181 ? 108.014 180.738 117.413 1.00 93.62  ? 139 GLU A OE1 1 
ATOM   769   O  OE2 . GLU A 1 181 ? 106.755 178.961 117.173 1.00 89.55  ? 139 GLU A OE2 1 
ATOM   770   N  N   . ASP A 1 182 ? 111.710 179.232 113.277 1.00 87.88  ? 140 ASP A N   1 
ATOM   771   C  CA  . ASP A 1 182 ? 111.660 178.807 111.877 1.00 83.21  ? 140 ASP A CA  1 
ATOM   772   C  C   . ASP A 1 182 ? 112.887 177.951 111.562 1.00 81.56  ? 140 ASP A C   1 
ATOM   773   O  O   . ASP A 1 182 ? 113.752 178.295 110.755 1.00 80.50  ? 140 ASP A O   1 
ATOM   774   C  CB  . ASP A 1 182 ? 111.559 180.016 110.957 1.00 85.35  ? 140 ASP A CB  1 
ATOM   775   C  CG  . ASP A 1 182 ? 112.738 180.954 111.089 1.00 85.19  ? 140 ASP A CG  1 
ATOM   776   O  OD1 . ASP A 1 182 ? 113.419 180.914 112.134 1.00 85.52  ? 140 ASP A OD1 1 
ATOM   777   O  OD2 . ASP A 1 182 ? 112.986 181.730 110.143 1.00 83.70  ? 140 ASP A OD2 1 
ATOM   778   N  N   . CYS A 1 183 ? 112.945 176.796 112.218 1.00 79.42  ? 141 CYS A N   1 
ATOM   779   C  CA  . CYS A 1 183 ? 114.104 175.920 112.146 1.00 83.05  ? 141 CYS A CA  1 
ATOM   780   C  C   . CYS A 1 183 ? 113.959 174.797 111.131 1.00 81.13  ? 141 CYS A C   1 
ATOM   781   O  O   . CYS A 1 183 ? 114.864 173.967 111.022 1.00 79.02  ? 141 CYS A O   1 
ATOM   782   C  CB  . CYS A 1 183 ? 114.389 175.321 113.522 1.00 82.93  ? 141 CYS A CB  1 
ATOM   783   S  SG  . CYS A 1 183 ? 112.979 174.500 114.287 1.00 80.83  ? 141 CYS A SG  1 
ATOM   784   N  N   . LEU A 1 184 ? 112.862 174.751 110.381 1.00 65.57  ? 142 LEU A N   1 
ATOM   785   C  CA  . LEU A 1 184 ? 112.629 173.636 109.475 1.00 54.06  ? 142 LEU A CA  1 
ATOM   786   C  C   . LEU A 1 184 ? 113.533 173.722 108.253 1.00 59.31  ? 142 LEU A C   1 
ATOM   787   O  O   . LEU A 1 184 ? 113.143 174.275 107.221 1.00 65.98  ? 142 LEU A O   1 
ATOM   788   C  CB  . LEU A 1 184 ? 111.162 173.590 109.050 1.00 56.69  ? 142 LEU A CB  1 
ATOM   789   C  CG  . LEU A 1 184 ? 110.146 173.533 110.189 1.00 58.11  ? 142 LEU A CG  1 
ATOM   790   C  CD1 . LEU A 1 184 ? 108.762 173.228 109.659 1.00 59.74  ? 142 LEU A CD1 1 
ATOM   791   C  CD2 . LEU A 1 184 ? 110.558 172.500 111.207 1.00 59.01  ? 142 LEU A CD2 1 
ATOM   792   N  N   . TYR A 1 185 ? 114.742 173.177 108.366 1.00 55.94  ? 143 TYR A N   1 
ATOM   793   C  CA  . TYR A 1 185 ? 115.679 173.094 107.257 1.00 55.09  ? 143 TYR A CA  1 
ATOM   794   C  C   . TYR A 1 185 ? 116.310 171.711 107.258 1.00 56.18  ? 143 TYR A C   1 
ATOM   795   O  O   . TYR A 1 185 ? 116.133 170.923 108.190 1.00 67.18  ? 143 TYR A O   1 
ATOM   796   C  CB  . TYR A 1 185 ? 116.764 174.172 107.346 1.00 58.50  ? 143 TYR A CB  1 
ATOM   797   C  CG  . TYR A 1 185 ? 116.246 175.590 107.269 1.00 63.83  ? 143 TYR A CG  1 
ATOM   798   C  CD1 . TYR A 1 185 ? 116.042 176.210 106.048 1.00 60.91  ? 143 TYR A CD1 1 
ATOM   799   C  CD2 . TYR A 1 185 ? 115.968 176.310 108.419 1.00 64.76  ? 143 TYR A CD2 1 
ATOM   800   C  CE1 . TYR A 1 185 ? 115.569 177.500 105.976 1.00 59.96  ? 143 TYR A CE1 1 
ATOM   801   C  CE2 . TYR A 1 185 ? 115.497 177.601 108.353 1.00 60.28  ? 143 TYR A CE2 1 
ATOM   802   C  CZ  . TYR A 1 185 ? 115.299 178.189 107.131 1.00 60.03  ? 143 TYR A CZ  1 
ATOM   803   O  OH  . TYR A 1 185 ? 114.828 179.477 107.070 1.00 71.23  ? 143 TYR A OH  1 
ATOM   804   N  N   . LEU A 1 186 ? 117.042 171.409 106.190 1.00 50.89  ? 144 LEU A N   1 
ATOM   805   C  CA  . LEU A 1 186 ? 117.787 170.163 106.117 1.00 52.04  ? 144 LEU A CA  1 
ATOM   806   C  C   . LEU A 1 186 ? 119.067 170.402 105.332 1.00 51.74  ? 144 LEU A C   1 
ATOM   807   O  O   . LEU A 1 186 ? 119.138 171.301 104.492 1.00 60.03  ? 144 LEU A O   1 
ATOM   808   C  CB  . LEU A 1 186 ? 116.962 169.035 105.484 1.00 48.86  ? 144 LEU A CB  1 
ATOM   809   C  CG  . LEU A 1 186 ? 116.450 169.162 104.053 1.00 47.60  ? 144 LEU A CG  1 
ATOM   810   C  CD1 . LEU A 1 186 ? 117.424 168.542 103.091 1.00 55.93  ? 144 LEU A CD1 1 
ATOM   811   C  CD2 . LEU A 1 186 ? 115.110 168.482 103.925 1.00 50.52  ? 144 LEU A CD2 1 
ATOM   812   N  N   . ASN A 1 187 ? 120.076 169.586 105.618 1.00 41.26  ? 145 ASN A N   1 
ATOM   813   C  CA  . ASN A 1 187 ? 121.395 169.700 105.020 1.00 43.87  ? 145 ASN A CA  1 
ATOM   814   C  C   . ASN A 1 187 ? 121.696 168.422 104.257 1.00 50.42  ? 145 ASN A C   1 
ATOM   815   O  O   . ASN A 1 187 ? 121.558 167.324 104.805 1.00 63.35  ? 145 ASN A O   1 
ATOM   816   C  CB  . ASN A 1 187 ? 122.455 169.937 106.093 1.00 50.42  ? 145 ASN A CB  1 
ATOM   817   C  CG  . ASN A 1 187 ? 121.927 170.735 107.265 1.00 55.71  ? 145 ASN A CG  1 
ATOM   818   O  OD1 . ASN A 1 187 ? 121.184 171.696 107.089 1.00 62.31  ? 145 ASN A OD1 1 
ATOM   819   N  ND2 . ASN A 1 187 ? 122.307 170.339 108.471 1.00 55.67  ? 145 ASN A ND2 1 
ATOM   820   N  N   . LEU A 1 188 ? 122.111 168.568 103.004 1.00 51.31  ? 146 LEU A N   1 
ATOM   821   C  CA  . LEU A 1 188 ? 122.439 167.445 102.138 1.00 43.76  ? 146 LEU A CA  1 
ATOM   822   C  C   . LEU A 1 188 ? 123.942 167.385 101.912 1.00 51.84  ? 146 LEU A C   1 
ATOM   823   O  O   . LEU A 1 188 ? 124.583 168.410 101.663 1.00 62.77  ? 146 LEU A O   1 
ATOM   824   C  CB  . LEU A 1 188 ? 121.729 167.557 100.789 1.00 42.01  ? 146 LEU A CB  1 
ATOM   825   C  CG  . LEU A 1 188 ? 120.205 167.626 100.789 1.00 46.69  ? 146 LEU A CG  1 
ATOM   826   C  CD1 . LEU A 1 188 ? 119.747 168.993 100.335 1.00 48.48  ? 146 LEU A CD1 1 
ATOM   827   C  CD2 . LEU A 1 188 ? 119.630 166.549 99.891  1.00 52.13  ? 146 LEU A CD2 1 
ATOM   828   N  N   . TYR A 1 189 ? 124.499 166.180 101.999 1.00 50.70  ? 147 TYR A N   1 
ATOM   829   C  CA  . TYR A 1 189 ? 125.902 165.924 101.702 1.00 50.34  ? 147 TYR A CA  1 
ATOM   830   C  C   . TYR A 1 189 ? 125.939 164.911 100.568 1.00 61.02  ? 147 TYR A C   1 
ATOM   831   O  O   . TYR A 1 189 ? 125.492 163.770 100.740 1.00 65.30  ? 147 TYR A O   1 
ATOM   832   C  CB  . TYR A 1 189 ? 126.638 165.407 102.933 1.00 50.58  ? 147 TYR A CB  1 
ATOM   833   C  CG  . TYR A 1 189 ? 126.464 166.275 104.157 1.00 54.48  ? 147 TYR A CG  1 
ATOM   834   C  CD1 . TYR A 1 189 ? 125.412 166.069 105.033 1.00 53.93  ? 147 TYR A CD1 1 
ATOM   835   C  CD2 . TYR A 1 189 ? 127.356 167.298 104.437 1.00 58.44  ? 147 TYR A CD2 1 
ATOM   836   C  CE1 . TYR A 1 189 ? 125.250 166.857 106.149 1.00 53.27  ? 147 TYR A CE1 1 
ATOM   837   C  CE2 . TYR A 1 189 ? 127.201 168.092 105.551 1.00 59.13  ? 147 TYR A CE2 1 
ATOM   838   C  CZ  . TYR A 1 189 ? 126.147 167.867 106.403 1.00 52.88  ? 147 TYR A CZ  1 
ATOM   839   O  OH  . TYR A 1 189 ? 125.987 168.656 107.516 1.00 53.53  ? 147 TYR A OH  1 
ATOM   840   N  N   . VAL A 1 190 ? 126.454 165.331 99.420  1.00 65.30  ? 148 VAL A N   1 
ATOM   841   C  CA  . VAL A 1 190 ? 126.440 164.560 98.181  1.00 61.62  ? 148 VAL A CA  1 
ATOM   842   C  C   . VAL A 1 190 ? 127.880 164.211 97.823  1.00 65.91  ? 148 VAL A C   1 
ATOM   843   O  O   . VAL A 1 190 ? 128.714 165.115 97.696  1.00 72.89  ? 148 VAL A O   1 
ATOM   844   C  CB  . VAL A 1 190 ? 125.772 165.341 97.040  1.00 56.49  ? 148 VAL A CB  1 
ATOM   845   C  CG1 . VAL A 1 190 ? 125.493 164.426 95.867  1.00 60.44  ? 148 VAL A CG1 1 
ATOM   846   C  CG2 . VAL A 1 190 ? 124.500 166.004 97.524  1.00 57.74  ? 148 VAL A CG2 1 
ATOM   847   N  N   . PRO A 1 191 ? 128.217 162.940 97.649  1.00 66.34  ? 149 PRO A N   1 
ATOM   848   C  CA  . PRO A 1 191 ? 129.569 162.586 97.219  1.00 68.39  ? 149 PRO A CA  1 
ATOM   849   C  C   . PRO A 1 191 ? 129.760 162.824 95.730  1.00 75.76  ? 149 PRO A C   1 
ATOM   850   O  O   . PRO A 1 191 ? 128.809 163.012 94.971  1.00 75.26  ? 149 PRO A O   1 
ATOM   851   C  CB  . PRO A 1 191 ? 129.660 161.096 97.552  1.00 64.23  ? 149 PRO A CB  1 
ATOM   852   C  CG  . PRO A 1 191 ? 128.267 160.619 97.399  1.00 61.79  ? 149 PRO A CG  1 
ATOM   853   C  CD  . PRO A 1 191 ? 127.368 161.753 97.821  1.00 61.71  ? 149 PRO A CD  1 
ATOM   854   N  N   . THR A 1 192 ? 131.024 162.813 95.321  1.00 83.19  ? 150 THR A N   1 
ATOM   855   C  CA  . THR A 1 192 ? 131.373 162.996 93.918  1.00 78.14  ? 150 THR A CA  1 
ATOM   856   C  C   . THR A 1 192 ? 132.361 161.929 93.457  1.00 77.75  ? 150 THR A C   1 
ATOM   857   O  O   . THR A 1 192 ? 131.971 160.912 92.884  1.00 71.85  ? 150 THR A O   1 
ATOM   858   C  CB  . THR A 1 192 ? 131.976 164.386 93.666  1.00 74.87  ? 150 THR A CB  1 
ATOM   859   O  OG1 . THR A 1 192 ? 133.020 164.633 94.614  1.00 77.82  ? 150 THR A OG1 1 
ATOM   860   C  CG2 . THR A 1 192 ? 130.913 165.459 93.805  1.00 70.14  ? 150 THR A CG2 1 
ATOM   861   N  N   . SER A 1 199 ? 125.196 149.932 89.623  1.00 97.44  ? 174 SER A N   1 
ATOM   862   C  CA  . SER A 1 199 ? 125.678 151.219 90.107  1.00 100.94 ? 174 SER A CA  1 
ATOM   863   C  C   . SER A 1 199 ? 124.833 152.357 89.549  1.00 101.91 ? 174 SER A C   1 
ATOM   864   O  O   . SER A 1 199 ? 125.252 153.063 88.632  1.00 102.69 ? 174 SER A O   1 
ATOM   865   C  CB  . SER A 1 199 ? 127.147 151.419 89.731  1.00 100.44 ? 174 SER A CB  1 
ATOM   866   O  OG  . SER A 1 199 ? 127.753 152.410 90.542  1.00 99.35  ? 174 SER A OG  1 
ATOM   867   N  N   . GLY A 1 200 ? 123.640 152.530 90.107  1.00 94.83  ? 175 GLY A N   1 
ATOM   868   C  CA  . GLY A 1 200 ? 122.730 153.574 89.690  1.00 94.11  ? 175 GLY A CA  1 
ATOM   869   C  C   . GLY A 1 200 ? 122.953 154.866 90.447  1.00 95.35  ? 175 GLY A C   1 
ATOM   870   O  O   . GLY A 1 200 ? 124.036 155.134 90.973  1.00 93.70  ? 175 GLY A O   1 
ATOM   871   N  N   . LYS A 1 201 ? 121.905 155.682 90.491  1.00 79.93  ? 176 LYS A N   1 
ATOM   872   C  CA  . LYS A 1 201 ? 121.963 156.932 91.232  1.00 77.70  ? 176 LYS A CA  1 
ATOM   873   C  C   . LYS A 1 201 ? 122.113 156.657 92.724  1.00 76.06  ? 176 LYS A C   1 
ATOM   874   O  O   . LYS A 1 201 ? 121.663 155.631 93.238  1.00 75.67  ? 176 LYS A O   1 
ATOM   875   C  CB  . LYS A 1 201 ? 120.714 157.767 90.963  1.00 72.78  ? 176 LYS A CB  1 
ATOM   876   C  CG  . LYS A 1 201 ? 120.328 157.825 89.497  1.00 71.20  ? 176 LYS A CG  1 
ATOM   877   C  CD  . LYS A 1 201 ? 118.935 158.396 89.304  1.00 75.30  ? 176 LYS A CD  1 
ATOM   878   C  CE  . LYS A 1 201 ? 117.871 157.379 89.670  1.00 75.83  ? 176 LYS A CE  1 
ATOM   879   N  NZ  . LYS A 1 201 ? 117.756 156.305 88.646  1.00 72.11  ? 176 LYS A NZ  1 
ATOM   880   N  N   . LYS A 1 202 ? 122.759 157.590 93.415  1.00 66.19  ? 177 LYS A N   1 
ATOM   881   C  CA  . LYS A 1 202 ? 123.168 157.359 94.792  1.00 61.47  ? 177 LYS A CA  1 
ATOM   882   C  C   . LYS A 1 202 ? 121.955 157.204 95.705  1.00 65.67  ? 177 LYS A C   1 
ATOM   883   O  O   . LYS A 1 202 ? 120.952 157.901 95.532  1.00 68.38  ? 177 LYS A O   1 
ATOM   884   C  CB  . LYS A 1 202 ? 124.040 158.510 95.279  1.00 61.19  ? 177 LYS A CB  1 
ATOM   885   C  CG  . LYS A 1 202 ? 125.117 158.903 94.296  1.00 65.83  ? 177 LYS A CG  1 
ATOM   886   C  CD  . LYS A 1 202 ? 125.833 160.159 94.733  1.00 66.11  ? 177 LYS A CD  1 
ATOM   887   C  CE  . LYS A 1 202 ? 126.903 160.535 93.734  1.00 65.04  ? 177 LYS A CE  1 
ATOM   888   N  NZ  . LYS A 1 202 ? 127.561 159.324 93.179  1.00 67.03  ? 177 LYS A NZ  1 
ATOM   889   N  N   . PRO A 1 203 ? 122.011 156.294 96.672  1.00 57.46  ? 178 PRO A N   1 
ATOM   890   C  CA  . PRO A 1 203 ? 120.934 156.194 97.659  1.00 55.48  ? 178 PRO A CA  1 
ATOM   891   C  C   . PRO A 1 203 ? 120.974 157.357 98.636  1.00 59.51  ? 178 PRO A C   1 
ATOM   892   O  O   . PRO A 1 203 ? 121.987 158.038 98.799  1.00 65.23  ? 178 PRO A O   1 
ATOM   893   C  CB  . PRO A 1 203 ? 121.221 154.869 98.372  1.00 52.75  ? 178 PRO A CB  1 
ATOM   894   C  CG  . PRO A 1 203 ? 122.228 154.171 97.519  1.00 51.15  ? 178 PRO A CG  1 
ATOM   895   C  CD  . PRO A 1 203 ? 123.011 155.235 96.850  1.00 54.51  ? 178 PRO A CD  1 
ATOM   896   N  N   . VAL A 1 204 ? 119.843 157.579 99.294  1.00 43.54  ? 179 VAL A N   1 
ATOM   897   C  CA  . VAL A 1 204 ? 119.695 158.642 100.278 1.00 43.22  ? 179 VAL A CA  1 
ATOM   898   C  C   . VAL A 1 204 ? 119.600 158.008 101.656 1.00 47.62  ? 179 VAL A C   1 
ATOM   899   O  O   . VAL A 1 204 ? 119.014 156.933 101.812 1.00 59.32  ? 179 VAL A O   1 
ATOM   900   C  CB  . VAL A 1 204 ? 118.459 159.512 99.985  1.00 42.73  ? 179 VAL A CB  1 
ATOM   901   C  CG1 . VAL A 1 204 ? 118.602 160.867 100.635 1.00 45.52  ? 179 VAL A CG1 1 
ATOM   902   C  CG2 . VAL A 1 204 ? 118.262 159.662 98.496  1.00 44.87  ? 179 VAL A CG2 1 
ATOM   903   N  N   . MET A 1 205 ? 120.192 158.663 102.651 1.00 38.81  ? 180 MET A N   1 
ATOM   904   C  CA  . MET A 1 205 ? 120.130 158.214 104.041 1.00 34.08  ? 180 MET A CA  1 
ATOM   905   C  C   . MET A 1 205 ? 119.730 159.408 104.900 1.00 42.85  ? 180 MET A C   1 
ATOM   906   O  O   . MET A 1 205 ? 120.543 160.304 105.141 1.00 62.86  ? 180 MET A O   1 
ATOM   907   C  CB  . MET A 1 205 ? 121.463 157.632 104.497 1.00 34.50  ? 180 MET A CB  1 
ATOM   908   C  CG  . MET A 1 205 ? 121.897 156.397 103.738 1.00 39.33  ? 180 MET A CG  1 
ATOM   909   S  SD  . MET A 1 205 ? 122.841 155.225 104.727 1.00 46.51  ? 180 MET A SD  1 
ATOM   910   C  CE  . MET A 1 205 ? 123.204 156.193 106.177 1.00 41.27  ? 180 MET A CE  1 
ATOM   911   N  N   . LEU A 1 206 ? 118.480 159.429 105.348 1.00 29.61  ? 181 LEU A N   1 
ATOM   912   C  CA  . LEU A 1 206 ? 117.992 160.474 106.235 1.00 30.44  ? 181 LEU A CA  1 
ATOM   913   C  C   . LEU A 1 206 ? 118.325 160.115 107.674 1.00 35.00  ? 181 LEU A C   1 
ATOM   914   O  O   . LEU A 1 206 ? 118.224 158.952 108.067 1.00 53.58  ? 181 LEU A O   1 
ATOM   915   C  CB  . LEU A 1 206 ? 116.485 160.661 106.077 1.00 31.69  ? 181 LEU A CB  1 
ATOM   916   C  CG  . LEU A 1 206 ? 115.881 161.879 106.775 1.00 32.94  ? 181 LEU A CG  1 
ATOM   917   C  CD1 . LEU A 1 206 ? 116.142 163.124 105.974 1.00 45.13  ? 181 LEU A CD1 1 
ATOM   918   C  CD2 . LEU A 1 206 ? 114.396 161.705 106.985 1.00 36.93  ? 181 LEU A CD2 1 
ATOM   919   N  N   . PHE A 1 207 ? 118.743 161.109 108.452 1.00 38.71  ? 182 PHE A N   1 
ATOM   920   C  CA  . PHE A 1 207 ? 119.142 160.891 109.838 1.00 37.02  ? 182 PHE A CA  1 
ATOM   921   C  C   . PHE A 1 207 ? 118.179 161.611 110.770 1.00 45.73  ? 182 PHE A C   1 
ATOM   922   O  O   . PHE A 1 207 ? 118.041 162.835 110.697 1.00 56.55  ? 182 PHE A O   1 
ATOM   923   C  CB  . PHE A 1 207 ? 120.570 161.376 110.075 1.00 33.10  ? 182 PHE A CB  1 
ATOM   924   C  CG  . PHE A 1 207 ? 121.073 161.114 111.462 1.00 38.18  ? 182 PHE A CG  1 
ATOM   925   C  CD1 . PHE A 1 207 ? 121.063 159.838 111.985 1.00 42.18  ? 182 PHE A CD1 1 
ATOM   926   C  CD2 . PHE A 1 207 ? 121.557 162.142 112.241 1.00 50.70  ? 182 PHE A CD2 1 
ATOM   927   C  CE1 . PHE A 1 207 ? 121.525 159.593 113.255 1.00 42.51  ? 182 PHE A CE1 1 
ATOM   928   C  CE2 . PHE A 1 207 ? 122.017 161.899 113.512 1.00 51.61  ? 182 PHE A CE2 1 
ATOM   929   C  CZ  . PHE A 1 207 ? 122.001 160.622 114.017 1.00 42.94  ? 182 PHE A CZ  1 
ATOM   930   N  N   . LEU A 1 208 ? 117.536 160.856 111.660 1.00 30.66  ? 183 LEU A N   1 
ATOM   931   C  CA  . LEU A 1 208 ? 116.616 161.410 112.651 1.00 31.43  ? 183 LEU A CA  1 
ATOM   932   C  C   . LEU A 1 208 ? 117.344 161.491 113.988 1.00 45.48  ? 183 LEU A C   1 
ATOM   933   O  O   . LEU A 1 208 ? 117.408 160.513 114.734 1.00 49.72  ? 183 LEU A O   1 
ATOM   934   C  CB  . LEU A 1 208 ? 115.358 160.561 112.766 1.00 35.38  ? 183 LEU A CB  1 
ATOM   935   C  CG  . LEU A 1 208 ? 114.653 160.143 111.484 1.00 25.98  ? 183 LEU A CG  1 
ATOM   936   C  CD1 . LEU A 1 208 ? 113.356 159.477 111.844 1.00 40.77  ? 183 LEU A CD1 1 
ATOM   937   C  CD2 . LEU A 1 208 ? 114.398 161.340 110.616 1.00 35.15  ? 183 LEU A CD2 1 
ATOM   938   N  N   . HIS A 1 209 ? 117.872 162.667 114.298 1.00 52.58  ? 184 HIS A N   1 
ATOM   939   C  CA  . HIS A 1 209 ? 118.676 162.855 115.491 1.00 48.44  ? 184 HIS A CA  1 
ATOM   940   C  C   . HIS A 1 209 ? 117.796 162.931 116.733 1.00 53.51  ? 184 HIS A C   1 
ATOM   941   O  O   . HIS A 1 209 ? 116.574 163.073 116.658 1.00 54.84  ? 184 HIS A O   1 
ATOM   942   C  CB  . HIS A 1 209 ? 119.505 164.127 115.370 1.00 50.19  ? 184 HIS A CB  1 
ATOM   943   C  CG  . HIS A 1 209 ? 118.679 165.371 115.371 1.00 49.10  ? 184 HIS A CG  1 
ATOM   944   N  ND1 . HIS A 1 209 ? 118.060 165.852 114.240 1.00 58.64  ? 184 HIS A ND1 1 
ATOM   945   C  CD2 . HIS A 1 209 ? 118.346 166.218 116.371 1.00 50.57  ? 184 HIS A CD2 1 
ATOM   946   C  CE1 . HIS A 1 209 ? 117.392 166.950 114.540 1.00 60.01  ? 184 HIS A CE1 1 
ATOM   947   N  NE2 . HIS A 1 209 ? 117.549 167.194 115.828 1.00 56.95  ? 184 HIS A NE2 1 
ATOM   948   N  N   . GLY A 1 210 ? 118.439 162.846 117.893 1.00 72.34  ? 185 GLY A N   1 
ATOM   949   C  CA  . GLY A 1 210 ? 117.742 163.029 119.150 1.00 64.94  ? 185 GLY A CA  1 
ATOM   950   C  C   . GLY A 1 210 ? 118.159 162.057 120.232 1.00 64.92  ? 185 GLY A C   1 
ATOM   951   O  O   . GLY A 1 210 ? 118.523 160.915 119.943 1.00 63.44  ? 185 GLY A O   1 
ATOM   952   N  N   . GLY A 1 211 ? 118.141 162.512 121.480 1.00 68.78  ? 186 GLY A N   1 
ATOM   953   C  CA  . GLY A 1 211 ? 118.303 161.626 122.615 1.00 66.19  ? 186 GLY A CA  1 
ATOM   954   C  C   . GLY A 1 211 ? 117.009 161.555 123.392 1.00 60.92  ? 186 GLY A C   1 
ATOM   955   O  O   . GLY A 1 211 ? 116.605 160.493 123.870 1.00 65.76  ? 186 GLY A O   1 
ATOM   956   N  N   . SER A 1 212 ? 116.360 162.701 123.521 1.00 46.81  ? 187 SER A N   1 
ATOM   957   C  CA  . SER A 1 212 ? 114.973 162.822 123.935 1.00 47.96  ? 187 SER A CA  1 
ATOM   958   C  C   . SER A 1 212 ? 114.251 163.627 122.861 1.00 62.06  ? 187 SER A C   1 
ATOM   959   O  O   . SER A 1 212 ? 114.807 163.913 121.798 1.00 72.92  ? 187 SER A O   1 
ATOM   960   C  CB  . SER A 1 212 ? 114.862 163.467 125.315 1.00 46.81  ? 187 SER A CB  1 
ATOM   961   O  OG  . SER A 1 212 ? 115.547 164.702 125.352 1.00 60.49  ? 187 SER A OG  1 
ATOM   962   N  N   . TYR A 1 213 ? 113.009 163.997 123.133 1.00 49.49  ? 188 TYR A N   1 
ATOM   963   C  CA  . TYR A 1 213 ? 112.244 164.782 122.179 1.00 44.16  ? 188 TYR A CA  1 
ATOM   964   C  C   . TYR A 1 213 ? 112.318 166.278 122.452 1.00 49.36  ? 188 TYR A C   1 
ATOM   965   O  O   . TYR A 1 213 ? 111.588 167.047 121.820 1.00 51.00  ? 188 TYR A O   1 
ATOM   966   C  CB  . TYR A 1 213 ? 110.791 164.320 122.171 1.00 42.92  ? 188 TYR A CB  1 
ATOM   967   C  CG  . TYR A 1 213 ? 110.618 162.874 121.782 1.00 42.44  ? 188 TYR A CG  1 
ATOM   968   C  CD1 . TYR A 1 213 ? 110.570 162.496 120.452 1.00 44.51  ? 188 TYR A CD1 1 
ATOM   969   C  CD2 . TYR A 1 213 ? 110.492 161.887 122.746 1.00 43.38  ? 188 TYR A CD2 1 
ATOM   970   C  CE1 . TYR A 1 213 ? 110.406 161.178 120.093 1.00 45.92  ? 188 TYR A CE1 1 
ATOM   971   C  CE2 . TYR A 1 213 ? 110.328 160.569 122.395 1.00 43.17  ? 188 TYR A CE2 1 
ATOM   972   C  CZ  . TYR A 1 213 ? 110.286 160.221 121.069 1.00 47.49  ? 188 TYR A CZ  1 
ATOM   973   O  OH  . TYR A 1 213 ? 110.120 158.909 120.716 1.00 48.37  ? 188 TYR A OH  1 
ATOM   974   N  N   . MET A 1 214 ? 113.180 166.708 123.374 1.00 65.93  ? 189 MET A N   1 
ATOM   975   C  CA  . MET A 1 214 ? 113.280 168.110 123.760 1.00 68.44  ? 189 MET A CA  1 
ATOM   976   C  C   . MET A 1 214 ? 114.679 168.675 123.544 1.00 70.41  ? 189 MET A C   1 
ATOM   977   O  O   . MET A 1 214 ? 115.009 169.726 124.101 1.00 74.45  ? 189 MET A O   1 
ATOM   978   C  CB  . MET A 1 214 ? 112.863 168.287 125.220 1.00 69.03  ? 189 MET A CB  1 
ATOM   979   C  CG  . MET A 1 214 ? 111.527 167.661 125.557 1.00 71.16  ? 189 MET A CG  1 
ATOM   980   S  SD  . MET A 1 214 ? 110.698 168.495 126.916 1.00 86.29  ? 189 MET A SD  1 
ATOM   981   C  CE  . MET A 1 214 ? 112.014 168.538 128.125 1.00 71.73  ? 189 MET A CE  1 
ATOM   982   N  N   . GLU A 1 215 ? 115.507 168.012 122.743 1.00 67.81  ? 190 GLU A N   1 
ATOM   983   C  CA  . GLU A 1 215 ? 116.886 168.445 122.572 1.00 65.83  ? 190 GLU A CA  1 
ATOM   984   C  C   . GLU A 1 215 ? 117.432 167.913 121.257 1.00 71.47  ? 190 GLU A C   1 
ATOM   985   O  O   . GLU A 1 215 ? 116.864 167.004 120.648 1.00 72.71  ? 190 GLU A O   1 
ATOM   986   C  CB  . GLU A 1 215 ? 117.757 167.980 123.743 1.00 63.77  ? 190 GLU A CB  1 
ATOM   987   C  CG  . GLU A 1 215 ? 117.914 166.467 123.840 1.00 72.80  ? 190 GLU A CG  1 
ATOM   988   C  CD  . GLU A 1 215 ? 118.967 165.910 122.901 1.00 78.46  ? 190 GLU A CD  1 
ATOM   989   O  OE1 . GLU A 1 215 ? 119.918 166.645 122.570 1.00 83.04  ? 190 GLU A OE1 1 
ATOM   990   O  OE2 . GLU A 1 215 ? 118.837 164.744 122.479 1.00 76.63  ? 190 GLU A OE2 1 
ATOM   991   N  N   . GLY A 1 216 ? 118.554 168.490 120.836 1.00 70.27  ? 191 GLY A N   1 
ATOM   992   C  CA  . GLY A 1 216 ? 119.305 167.962 119.716 1.00 69.18  ? 191 GLY A CA  1 
ATOM   993   C  C   . GLY A 1 216 ? 119.006 168.621 118.388 1.00 72.13  ? 191 GLY A C   1 
ATOM   994   O  O   . GLY A 1 216 ? 117.842 168.838 118.045 1.00 79.85  ? 191 GLY A O   1 
ATOM   995   N  N   . THR A 1 217 ? 120.053 168.944 117.630 1.00 63.04  ? 192 THR A N   1 
ATOM   996   C  CA  . THR A 1 217 ? 119.918 169.512 116.298 1.00 58.57  ? 192 THR A CA  1 
ATOM   997   C  C   . THR A 1 217 ? 120.827 168.768 115.333 1.00 63.21  ? 192 THR A C   1 
ATOM   998   O  O   . THR A 1 217 ? 121.822 168.159 115.727 1.00 72.05  ? 192 THR A O   1 
ATOM   999   C  CB  . THR A 1 217 ? 120.256 170.999 116.271 1.00 61.92  ? 192 THR A CB  1 
ATOM   1000  O  OG1 . THR A 1 217 ? 121.676 171.163 116.207 1.00 67.90  ? 192 THR A OG1 1 
ATOM   1001  C  CG2 . THR A 1 217 ? 119.731 171.671 117.511 1.00 69.63  ? 192 THR A CG2 1 
ATOM   1002  N  N   . GLY A 1 218 ? 120.474 168.832 114.053 1.00 53.75  ? 193 GLY A N   1 
ATOM   1003  C  CA  . GLY A 1 218 ? 121.184 168.064 113.052 1.00 56.54  ? 193 GLY A CA  1 
ATOM   1004  C  C   . GLY A 1 218 ? 122.562 168.583 112.716 1.00 63.34  ? 193 GLY A C   1 
ATOM   1005  O  O   . GLY A 1 218 ? 123.328 167.867 112.064 1.00 67.87  ? 193 GLY A O   1 
ATOM   1006  N  N   . ASN A 1 219 ? 122.900 169.799 113.142 1.00 65.02  ? 194 ASN A N   1 
ATOM   1007  C  CA  . ASN A 1 219 ? 124.212 170.352 112.837 1.00 61.10  ? 194 ASN A CA  1 
ATOM   1008  C  C   . ASN A 1 219 ? 125.328 169.715 113.651 1.00 58.28  ? 194 ASN A C   1 
ATOM   1009  O  O   . ASN A 1 219 ? 126.499 169.920 113.322 1.00 65.49  ? 194 ASN A O   1 
ATOM   1010  C  CB  . ASN A 1 219 ? 124.213 171.864 113.061 1.00 63.61  ? 194 ASN A CB  1 
ATOM   1011  C  CG  . ASN A 1 219 ? 122.968 172.534 112.525 1.00 67.42  ? 194 ASN A CG  1 
ATOM   1012  O  OD1 . ASN A 1 219 ? 122.449 173.472 113.127 1.00 69.86  ? 194 ASN A OD1 1 
ATOM   1013  N  ND2 . ASN A 1 219 ? 122.484 172.061 111.385 1.00 64.73  ? 194 ASN A ND2 1 
ATOM   1014  N  N   . MET A 1 220 ? 125.002 168.955 114.697 1.00 60.88  ? 195 MET A N   1 
ATOM   1015  C  CA  . MET A 1 220 ? 126.038 168.312 115.493 1.00 62.78  ? 195 MET A CA  1 
ATOM   1016  C  C   . MET A 1 220 ? 126.775 167.233 114.718 1.00 63.25  ? 195 MET A C   1 
ATOM   1017  O  O   . MET A 1 220 ? 127.912 166.904 115.070 1.00 69.06  ? 195 MET A O   1 
ATOM   1018  C  CB  . MET A 1 220 ? 125.440 167.702 116.762 1.00 62.22  ? 195 MET A CB  1 
ATOM   1019  C  CG  . MET A 1 220 ? 125.342 168.662 117.929 1.00 68.18  ? 195 MET A CG  1 
ATOM   1020  S  SD  . MET A 1 220 ? 124.519 167.956 119.362 1.00 69.81  ? 195 MET A SD  1 
ATOM   1021  C  CE  . MET A 1 220 ? 122.908 167.605 118.681 1.00 65.80  ? 195 MET A CE  1 
ATOM   1022  N  N   . PHE A 1 221 ? 126.161 166.678 113.679 1.00 59.60  ? 196 PHE A N   1 
ATOM   1023  C  CA  . PHE A 1 221 ? 126.715 165.550 112.944 1.00 60.35  ? 196 PHE A CA  1 
ATOM   1024  C  C   . PHE A 1 221 ? 127.101 166.002 111.545 1.00 65.42  ? 196 PHE A C   1 
ATOM   1025  O  O   . PHE A 1 221 ? 126.247 166.450 110.775 1.00 73.37  ? 196 PHE A O   1 
ATOM   1026  C  CB  . PHE A 1 221 ? 125.708 164.406 112.880 1.00 59.94  ? 196 PHE A CB  1 
ATOM   1027  C  CG  . PHE A 1 221 ? 125.237 163.947 114.221 1.00 64.19  ? 196 PHE A CG  1 
ATOM   1028  C  CD1 . PHE A 1 221 ? 126.005 163.086 114.979 1.00 65.23  ? 196 PHE A CD1 1 
ATOM   1029  C  CD2 . PHE A 1 221 ? 124.031 164.383 114.729 1.00 62.37  ? 196 PHE A CD2 1 
ATOM   1030  C  CE1 . PHE A 1 221 ? 125.576 162.667 116.211 1.00 61.15  ? 196 PHE A CE1 1 
ATOM   1031  C  CE2 . PHE A 1 221 ? 123.597 163.965 115.963 1.00 62.19  ? 196 PHE A CE2 1 
ATOM   1032  C  CZ  . PHE A 1 221 ? 124.370 163.107 116.705 1.00 64.66  ? 196 PHE A CZ  1 
ATOM   1033  N  N   . ASP A 1 222 ? 128.383 165.878 111.220 1.00 69.13  ? 197 ASP A N   1 
ATOM   1034  C  CA  . ASP A 1 222 ? 128.888 166.214 109.892 1.00 66.92  ? 197 ASP A CA  1 
ATOM   1035  C  C   . ASP A 1 222 ? 128.850 164.942 109.059 1.00 69.81  ? 197 ASP A C   1 
ATOM   1036  O  O   . ASP A 1 222 ? 129.784 164.140 109.065 1.00 73.21  ? 197 ASP A O   1 
ATOM   1037  C  CB  . ASP A 1 222 ? 130.292 166.797 109.985 1.00 73.46  ? 197 ASP A CB  1 
ATOM   1038  C  CG  . ASP A 1 222 ? 130.812 167.288 108.652 1.00 77.47  ? 197 ASP A CG  1 
ATOM   1039  O  OD1 . ASP A 1 222 ? 129.991 167.559 107.753 1.00 78.26  ? 197 ASP A OD1 1 
ATOM   1040  O  OD2 . ASP A 1 222 ? 132.046 167.403 108.503 1.00 75.62  ? 197 ASP A OD2 1 
ATOM   1041  N  N   . GLY A 1 223 ? 127.753 164.749 108.336 1.00 65.04  ? 198 GLY A N   1 
ATOM   1042  C  CA  . GLY A 1 223 ? 127.583 163.546 107.547 1.00 67.15  ? 198 GLY A CA  1 
ATOM   1043  C  C   . GLY A 1 223 ? 128.305 163.594 106.219 1.00 69.09  ? 198 GLY A C   1 
ATOM   1044  O  O   . GLY A 1 223 ? 127.750 163.202 105.190 1.00 71.34  ? 198 GLY A O   1 
ATOM   1045  N  N   . SER A 1 224 ? 129.548 164.070 106.229 1.00 65.46  ? 199 SER A N   1 
ATOM   1046  C  CA  . SER A 1 224 ? 130.343 164.190 105.015 1.00 60.04  ? 199 SER A CA  1 
ATOM   1047  C  C   . SER A 1 224 ? 131.335 163.055 104.833 1.00 60.97  ? 199 SER A C   1 
ATOM   1048  O  O   . SER A 1 224 ? 131.629 162.685 103.693 1.00 66.99  ? 199 SER A O   1 
ATOM   1049  C  CB  . SER A 1 224 ? 131.102 165.519 105.011 1.00 57.87  ? 199 SER A CB  1 
ATOM   1050  O  OG  . SER A 1 224 ? 131.872 165.653 103.834 1.00 67.25  ? 199 SER A OG  1 
ATOM   1051  N  N   . VAL A 1 225 ? 131.867 162.505 105.924 1.00 58.57  ? 200 VAL A N   1 
ATOM   1052  C  CA  . VAL A 1 225 ? 132.753 161.351 105.819 1.00 58.80  ? 200 VAL A CA  1 
ATOM   1053  C  C   . VAL A 1 225 ? 131.971 160.115 105.407 1.00 58.92  ? 200 VAL A C   1 
ATOM   1054  O  O   . VAL A 1 225 ? 132.470 159.270 104.656 1.00 67.88  ? 200 VAL A O   1 
ATOM   1055  C  CB  . VAL A 1 225 ? 133.499 161.129 107.143 1.00 57.58  ? 200 VAL A CB  1 
ATOM   1056  C  CG1 . VAL A 1 225 ? 134.699 160.236 106.923 1.00 55.82  ? 200 VAL A CG1 1 
ATOM   1057  C  CG2 . VAL A 1 225 ? 133.913 162.458 107.732 1.00 60.91  ? 200 VAL A CG2 1 
ATOM   1058  N  N   . LEU A 1 226 ? 130.743 159.974 105.907 1.00 50.97  ? 201 LEU A N   1 
ATOM   1059  C  CA  . LEU A 1 226 ? 129.916 158.839 105.516 1.00 46.32  ? 201 LEU A CA  1 
ATOM   1060  C  C   . LEU A 1 226 ? 129.520 158.927 104.049 1.00 54.81  ? 201 LEU A C   1 
ATOM   1061  O  O   . LEU A 1 226 ? 129.420 157.904 103.365 1.00 59.36  ? 201 LEU A O   1 
ATOM   1062  C  CB  . LEU A 1 226 ? 128.677 158.765 106.404 1.00 46.43  ? 201 LEU A CB  1 
ATOM   1063  C  CG  . LEU A 1 226 ? 127.648 157.684 106.084 1.00 45.92  ? 201 LEU A CG  1 
ATOM   1064  C  CD1 . LEU A 1 226 ? 128.299 156.323 106.048 1.00 42.26  ? 201 LEU A CD1 1 
ATOM   1065  C  CD2 . LEU A 1 226 ? 126.537 157.712 107.103 1.00 49.20  ? 201 LEU A CD2 1 
ATOM   1066  N  N   . ALA A 1 227 ? 129.291 160.140 103.549 1.00 60.80  ? 202 ALA A N   1 
ATOM   1067  C  CA  . ALA A 1 227 ? 128.877 160.304 102.160 1.00 58.37  ? 202 ALA A CA  1 
ATOM   1068  C  C   . ALA A 1 227 ? 130.001 159.940 101.199 1.00 62.42  ? 202 ALA A C   1 
ATOM   1069  O  O   . ALA A 1 227 ? 129.783 159.218 100.221 1.00 66.39  ? 202 ALA A O   1 
ATOM   1070  C  CB  . ALA A 1 227 ? 128.408 161.737 101.922 1.00 57.10  ? 202 ALA A CB  1 
ATOM   1071  N  N   . ALA A 1 228 ? 131.211 160.436 101.459 1.00 60.54  ? 203 ALA A N   1 
ATOM   1072  C  CA  . ALA A 1 228 ? 132.324 160.174 100.552 1.00 61.78  ? 203 ALA A CA  1 
ATOM   1073  C  C   . ALA A 1 228 ? 132.734 158.709 100.578 1.00 62.66  ? 203 ALA A C   1 
ATOM   1074  O  O   . ALA A 1 228 ? 133.079 158.139 99.537  1.00 64.97  ? 203 ALA A O   1 
ATOM   1075  C  CB  . ALA A 1 228 ? 133.512 161.063 100.909 1.00 59.00  ? 203 ALA A CB  1 
ATOM   1076  N  N   . TYR A 1 229 ? 132.719 158.087 101.757 1.00 52.55  ? 204 TYR A N   1 
ATOM   1077  C  CA  . TYR A 1 229 ? 133.159 156.701 101.866 1.00 52.93  ? 204 TYR A CA  1 
ATOM   1078  C  C   . TYR A 1 229 ? 132.189 155.753 101.175 1.00 54.56  ? 204 TYR A C   1 
ATOM   1079  O  O   . TYR A 1 229 ? 132.601 154.886 100.397 1.00 68.36  ? 204 TYR A O   1 
ATOM   1080  C  CB  . TYR A 1 229 ? 133.325 156.322 103.337 1.00 50.74  ? 204 TYR A CB  1 
ATOM   1081  C  CG  . TYR A 1 229 ? 133.885 154.936 103.564 1.00 49.87  ? 204 TYR A CG  1 
ATOM   1082  C  CD1 . TYR A 1 229 ? 133.077 153.816 103.467 1.00 51.21  ? 204 TYR A CD1 1 
ATOM   1083  C  CD2 . TYR A 1 229 ? 135.219 154.752 103.886 1.00 50.85  ? 204 TYR A CD2 1 
ATOM   1084  C  CE1 . TYR A 1 229 ? 133.581 152.557 103.672 1.00 57.13  ? 204 TYR A CE1 1 
ATOM   1085  C  CE2 . TYR A 1 229 ? 135.731 153.494 104.095 1.00 53.75  ? 204 TYR A CE2 1 
ATOM   1086  C  CZ  . TYR A 1 229 ? 134.906 152.399 103.987 1.00 55.69  ? 204 TYR A CZ  1 
ATOM   1087  O  OH  . TYR A 1 229 ? 135.404 151.136 104.194 1.00 50.36  ? 204 TYR A OH  1 
ATOM   1088  N  N   . GLY A 1 230 ? 130.900 155.890 101.451 1.00 43.70  ? 205 GLY A N   1 
ATOM   1089  C  CA  . GLY A 1 230 ? 129.935 154.966 100.905 1.00 49.54  ? 205 GLY A CA  1 
ATOM   1090  C  C   . GLY A 1 230 ? 129.347 155.328 99.565  1.00 51.92  ? 205 GLY A C   1 
ATOM   1091  O  O   . GLY A 1 230 ? 128.553 154.551 99.028  1.00 53.59  ? 205 GLY A O   1 
ATOM   1092  N  N   . ASN A 1 231 ? 129.718 156.476 98.998  1.00 63.16  ? 206 ASN A N   1 
ATOM   1093  C  CA  . ASN A 1 231 ? 129.134 156.965 97.748  1.00 71.33  ? 206 ASN A CA  1 
ATOM   1094  C  C   . ASN A 1 231 ? 127.615 157.071 97.851  1.00 69.45  ? 206 ASN A C   1 
ATOM   1095  O  O   . ASN A 1 231 ? 126.887 156.724 96.920  1.00 63.61  ? 206 ASN A O   1 
ATOM   1096  C  CB  . ASN A 1 231 ? 129.535 156.086 96.561  1.00 69.61  ? 206 ASN A CB  1 
ATOM   1097  C  CG  . ASN A 1 231 ? 130.897 156.440 96.006  1.00 74.78  ? 206 ASN A CG  1 
ATOM   1098  O  OD1 . ASN A 1 231 ? 131.073 157.490 95.390  1.00 79.31  ? 206 ASN A OD1 1 
ATOM   1099  N  ND2 . ASN A 1 231 ? 131.870 155.562 96.218  1.00 69.84  ? 206 ASN A ND2 1 
ATOM   1100  N  N   . VAL A 1 232 ? 127.133 157.556 98.994  1.00 59.90  ? 207 VAL A N   1 
ATOM   1101  C  CA  . VAL A 1 232 ? 125.709 157.733 99.239  1.00 56.22  ? 207 VAL A CA  1 
ATOM   1102  C  C   . VAL A 1 232 ? 125.460 159.173 99.657  1.00 56.54  ? 207 VAL A C   1 
ATOM   1103  O  O   . VAL A 1 232 ? 126.346 159.846 100.191 1.00 65.84  ? 207 VAL A O   1 
ATOM   1104  C  CB  . VAL A 1 232 ? 125.180 156.764 100.316 1.00 48.96  ? 207 VAL A CB  1 
ATOM   1105  C  CG1 . VAL A 1 232 ? 125.189 155.343 99.799  1.00 56.29  ? 207 VAL A CG1 1 
ATOM   1106  C  CG2 . VAL A 1 232 ? 126.007 156.874 101.572 1.00 46.47  ? 207 VAL A CG2 1 
ATOM   1107  N  N   . ILE A 1 233 ? 124.247 159.646 99.406  1.00 46.11  ? 208 ILE A N   1 
ATOM   1108  C  CA  . ILE A 1 233 ? 123.824 160.976 99.826  1.00 43.04  ? 208 ILE A CA  1 
ATOM   1109  C  C   . ILE A 1 233 ? 123.311 160.880 101.252 1.00 47.78  ? 208 ILE A C   1 
ATOM   1110  O  O   . ILE A 1 233 ? 122.527 159.982 101.574 1.00 55.37  ? 208 ILE A O   1 
ATOM   1111  C  CB  . ILE A 1 233 ? 122.742 161.529 98.887  1.00 44.63  ? 208 ILE A CB  1 
ATOM   1112  C  CG1 . ILE A 1 233 ? 123.348 161.930 97.549  1.00 49.86  ? 208 ILE A CG1 1 
ATOM   1113  C  CG2 . ILE A 1 233 ? 122.044 162.713 99.513  1.00 45.06  ? 208 ILE A CG2 1 
ATOM   1114  C  CD1 . ILE A 1 233 ? 122.371 162.615 96.637  1.00 53.79  ? 208 ILE A CD1 1 
ATOM   1115  N  N   . VAL A 1 234 ? 123.759 161.786 102.116 1.00 51.39  ? 209 VAL A N   1 
ATOM   1116  C  CA  . VAL A 1 234 ? 123.370 161.776 103.522 1.00 45.40  ? 209 VAL A CA  1 
ATOM   1117  C  C   . VAL A 1 234 ? 122.645 163.074 103.840 1.00 52.70  ? 209 VAL A C   1 
ATOM   1118  O  O   . VAL A 1 234 ? 123.161 164.162 103.564 1.00 62.19  ? 209 VAL A O   1 
ATOM   1119  C  CB  . VAL A 1 234 ? 124.582 161.585 104.449 1.00 43.96  ? 209 VAL A CB  1 
ATOM   1120  C  CG1 . VAL A 1 234 ? 124.165 161.732 105.891 1.00 50.08  ? 209 VAL A CG1 1 
ATOM   1121  C  CG2 . VAL A 1 234 ? 125.198 160.228 104.219 1.00 47.65  ? 209 VAL A CG2 1 
ATOM   1122  N  N   . VAL A 1 235 ? 121.458 162.964 104.428 1.00 41.55  ? 210 VAL A N   1 
ATOM   1123  C  CA  . VAL A 1 235 ? 120.616 164.113 104.728 1.00 37.12  ? 210 VAL A CA  1 
ATOM   1124  C  C   . VAL A 1 235 ? 120.417 164.186 106.233 1.00 38.17  ? 210 VAL A C   1 
ATOM   1125  O  O   . VAL A 1 235 ? 120.115 163.172 106.874 1.00 53.48  ? 210 VAL A O   1 
ATOM   1126  C  CB  . VAL A 1 235 ? 119.264 164.028 104.003 1.00 40.22  ? 210 VAL A CB  1 
ATOM   1127  C  CG1 . VAL A 1 235 ? 118.449 165.270 104.271 1.00 40.09  ? 210 VAL A CG1 1 
ATOM   1128  C  CG2 . VAL A 1 235 ? 119.482 163.844 102.521 1.00 43.90  ? 210 VAL A CG2 1 
ATOM   1129  N  N   . THR A 1 236 ? 120.605 165.376 106.795 1.00 44.66  ? 211 THR A N   1 
ATOM   1130  C  CA  . THR A 1 236 ? 120.429 165.606 108.223 1.00 51.12  ? 211 THR A CA  1 
ATOM   1131  C  C   . THR A 1 236 ? 119.547 166.830 108.403 1.00 55.83  ? 211 THR A C   1 
ATOM   1132  O  O   . THR A 1 236 ? 119.878 167.909 107.910 1.00 60.17  ? 211 THR A O   1 
ATOM   1133  C  CB  . THR A 1 236 ? 121.774 165.802 108.921 1.00 55.82  ? 211 THR A CB  1 
ATOM   1134  O  OG1 . THR A 1 236 ? 122.651 164.726 108.574 1.00 59.14  ? 211 THR A OG1 1 
ATOM   1135  C  CG2 . THR A 1 236 ? 121.583 165.795 110.410 1.00 58.48  ? 211 THR A CG2 1 
ATOM   1136  N  N   . LEU A 1 237 ? 118.441 166.672 109.116 1.00 60.35  ? 212 LEU A N   1 
ATOM   1137  C  CA  . LEU A 1 237 ? 117.392 167.679 109.149 1.00 57.63  ? 212 LEU A CA  1 
ATOM   1138  C  C   . LEU A 1 237 ? 117.271 168.310 110.530 1.00 53.01  ? 212 LEU A C   1 
ATOM   1139  O  O   . LEU A 1 237 ? 117.937 167.913 111.488 1.00 65.71  ? 212 LEU A O   1 
ATOM   1140  C  CB  . LEU A 1 237 ? 116.052 167.061 108.731 1.00 60.17  ? 212 LEU A CB  1 
ATOM   1141  C  CG  . LEU A 1 237 ? 115.220 166.374 109.815 1.00 55.82  ? 212 LEU A CG  1 
ATOM   1142  C  CD1 . LEU A 1 237 ? 113.886 165.975 109.252 1.00 58.76  ? 212 LEU A CD1 1 
ATOM   1143  C  CD2 . LEU A 1 237 ? 115.924 165.164 110.385 1.00 41.96  ? 212 LEU A CD2 1 
ATOM   1144  N  N   . ASN A 1 238 ? 116.405 169.317 110.616 1.00 45.57  ? 213 ASN A N   1 
ATOM   1145  C  CA  . ASN A 1 238 ? 115.967 169.890 111.881 1.00 46.55  ? 213 ASN A CA  1 
ATOM   1146  C  C   . ASN A 1 238 ? 114.448 169.822 111.938 1.00 57.40  ? 213 ASN A C   1 
ATOM   1147  O  O   . ASN A 1 238 ? 113.775 170.146 110.956 1.00 62.87  ? 213 ASN A O   1 
ATOM   1148  C  CB  . ASN A 1 238 ? 116.433 171.336 112.029 1.00 52.52  ? 213 ASN A CB  1 
ATOM   1149  C  CG  . ASN A 1 238 ? 117.908 171.445 112.328 1.00 64.93  ? 213 ASN A CG  1 
ATOM   1150  O  OD1 . ASN A 1 238 ? 118.302 171.892 113.402 1.00 71.23  ? 213 ASN A OD1 1 
ATOM   1151  N  ND2 . ASN A 1 238 ? 118.734 171.040 111.376 1.00 65.98  ? 213 ASN A ND2 1 
ATOM   1152  N  N   . TYR A 1 239 ? 113.911 169.400 113.079 1.00 57.87  ? 214 TYR A N   1 
ATOM   1153  C  CA  . TYR A 1 239 ? 112.471 169.289 113.248 1.00 52.05  ? 214 TYR A CA  1 
ATOM   1154  C  C   . TYR A 1 239 ? 112.080 169.848 114.606 1.00 52.82  ? 214 TYR A C   1 
ATOM   1155  O  O   . TYR A 1 239 ? 112.897 169.924 115.524 1.00 58.69  ? 214 TYR A O   1 
ATOM   1156  C  CB  . TYR A 1 239 ? 111.992 167.839 113.099 1.00 51.51  ? 214 TYR A CB  1 
ATOM   1157  C  CG  . TYR A 1 239 ? 112.550 166.873 114.121 1.00 52.85  ? 214 TYR A CG  1 
ATOM   1158  C  CD1 . TYR A 1 239 ? 111.901 166.656 115.326 1.00 51.35  ? 214 TYR A CD1 1 
ATOM   1159  C  CD2 . TYR A 1 239 ? 113.712 166.163 113.871 1.00 52.35  ? 214 TYR A CD2 1 
ATOM   1160  C  CE1 . TYR A 1 239 ? 112.401 165.773 116.255 1.00 52.33  ? 214 TYR A CE1 1 
ATOM   1161  C  CE2 . TYR A 1 239 ? 114.218 165.279 114.796 1.00 51.90  ? 214 TYR A CE2 1 
ATOM   1162  C  CZ  . TYR A 1 239 ? 113.558 165.087 115.985 1.00 50.47  ? 214 TYR A CZ  1 
ATOM   1163  O  OH  . TYR A 1 239 ? 114.058 164.205 116.911 1.00 54.46  ? 214 TYR A OH  1 
ATOM   1164  N  N   . ARG A 1 240 ? 110.816 170.249 114.720 1.00 51.28  ? 215 ARG A N   1 
ATOM   1165  C  CA  . ARG A 1 240 ? 110.330 170.864 115.947 1.00 47.28  ? 215 ARG A CA  1 
ATOM   1166  C  C   . ARG A 1 240 ? 110.436 169.895 117.116 1.00 51.22  ? 215 ARG A C   1 
ATOM   1167  O  O   . ARG A 1 240 ? 110.127 168.709 116.991 1.00 57.51  ? 215 ARG A O   1 
ATOM   1168  C  CB  . ARG A 1 240 ? 108.886 171.320 115.769 1.00 46.42  ? 215 ARG A CB  1 
ATOM   1169  C  CG  . ARG A 1 240 ? 108.741 172.535 114.882 1.00 48.29  ? 215 ARG A CG  1 
ATOM   1170  C  CD  . ARG A 1 240 ? 107.303 172.987 114.807 1.00 47.49  ? 215 ARG A CD  1 
ATOM   1171  N  NE  . ARG A 1 240 ? 106.591 172.341 113.715 1.00 46.43  ? 215 ARG A NE  1 
ATOM   1172  C  CZ  . ARG A 1 240 ? 105.275 172.364 113.567 1.00 53.29  ? 215 ARG A CZ  1 
ATOM   1173  N  NH1 . ARG A 1 240 ? 104.495 172.985 114.433 1.00 57.14  ? 215 ARG A NH1 1 
ATOM   1174  N  NH2 . ARG A 1 240 ? 104.729 171.749 112.523 1.00 51.76  ? 215 ARG A NH2 1 
ATOM   1175  N  N   . LEU A 1 241 ? 110.872 170.411 118.261 1.00 60.54  ? 216 LEU A N   1 
ATOM   1176  C  CA  . LEU A 1 241 ? 111.214 169.594 119.415 1.00 54.89  ? 216 LEU A CA  1 
ATOM   1177  C  C   . LEU A 1 241 ? 110.478 170.085 120.650 1.00 60.33  ? 216 LEU A C   1 
ATOM   1178  O  O   . LEU A 1 241 ? 110.352 171.292 120.869 1.00 63.26  ? 216 LEU A O   1 
ATOM   1179  C  CB  . LEU A 1 241 ? 112.716 169.629 119.684 1.00 48.51  ? 216 LEU A CB  1 
ATOM   1180  C  CG  . LEU A 1 241 ? 113.626 169.118 118.576 1.00 55.54  ? 216 LEU A CG  1 
ATOM   1181  C  CD1 . LEU A 1 241 ? 114.861 169.986 118.497 1.00 56.90  ? 216 LEU A CD1 1 
ATOM   1182  C  CD2 . LEU A 1 241 ? 114.000 167.672 118.819 1.00 55.12  ? 216 LEU A CD2 1 
ATOM   1183  N  N   . GLY A 1 242 ? 110.013 169.143 121.459 1.00 61.38  ? 217 GLY A N   1 
ATOM   1184  C  CA  . GLY A 1 242 ? 109.456 169.501 122.752 1.00 63.84  ? 217 GLY A CA  1 
ATOM   1185  C  C   . GLY A 1 242 ? 108.140 170.236 122.623 1.00 65.06  ? 217 GLY A C   1 
ATOM   1186  O  O   . GLY A 1 242 ? 107.250 169.839 121.862 1.00 65.63  ? 217 GLY A O   1 
ATOM   1187  N  N   . VAL A 1 243 ? 108.026 171.338 123.367 1.00 67.70  ? 218 VAL A N   1 
ATOM   1188  C  CA  . VAL A 1 243 ? 106.744 172.022 123.525 1.00 66.96  ? 218 VAL A CA  1 
ATOM   1189  C  C   . VAL A 1 243 ? 106.196 172.473 122.181 1.00 68.40  ? 218 VAL A C   1 
ATOM   1190  O  O   . VAL A 1 243 ? 105.007 172.301 121.891 1.00 74.05  ? 218 VAL A O   1 
ATOM   1191  C  CB  . VAL A 1 243 ? 106.893 173.208 124.491 1.00 65.31  ? 218 VAL A CB  1 
ATOM   1192  C  CG1 . VAL A 1 243 ? 105.535 173.666 124.959 1.00 66.48  ? 218 VAL A CG1 1 
ATOM   1193  C  CG2 . VAL A 1 243 ? 107.766 172.822 125.666 1.00 71.88  ? 218 VAL A CG2 1 
ATOM   1194  N  N   . LEU A 1 244 ? 107.044 173.063 121.343 1.00 65.02  ? 219 LEU A N   1 
ATOM   1195  C  CA  . LEU A 1 244 ? 106.578 173.568 120.060 1.00 65.24  ? 219 LEU A CA  1 
ATOM   1196  C  C   . LEU A 1 244 ? 106.279 172.465 119.059 1.00 66.97  ? 219 LEU A C   1 
ATOM   1197  O  O   . LEU A 1 244 ? 105.713 172.756 118.001 1.00 70.39  ? 219 LEU A O   1 
ATOM   1198  C  CB  . LEU A 1 244 ? 107.609 174.530 119.475 1.00 65.71  ? 219 LEU A CB  1 
ATOM   1199  C  CG  . LEU A 1 244 ? 107.932 175.736 120.350 1.00 70.49  ? 219 LEU A CG  1 
ATOM   1200  C  CD1 . LEU A 1 244 ? 109.220 176.379 119.901 1.00 72.12  ? 219 LEU A CD1 1 
ATOM   1201  C  CD2 . LEU A 1 244 ? 106.796 176.736 120.296 1.00 68.18  ? 219 LEU A CD2 1 
ATOM   1202  N  N   . GLY A 1 245 ? 106.632 171.220 119.356 1.00 63.50  ? 220 GLY A N   1 
ATOM   1203  C  CA  . GLY A 1 245 ? 106.500 170.181 118.359 1.00 62.20  ? 220 GLY A CA  1 
ATOM   1204  C  C   . GLY A 1 245 ? 105.712 168.966 118.789 1.00 62.66  ? 220 GLY A C   1 
ATOM   1205  O  O   . GLY A 1 245 ? 105.341 168.145 117.949 1.00 67.88  ? 220 GLY A O   1 
ATOM   1206  N  N   . PHE A 1 246 ? 105.447 168.826 120.086 1.00 53.66  ? 221 PHE A N   1 
ATOM   1207  C  CA  . PHE A 1 246 ? 104.749 167.638 120.557 1.00 54.88  ? 221 PHE A CA  1 
ATOM   1208  C  C   . PHE A 1 246 ? 103.667 167.944 121.584 1.00 55.69  ? 221 PHE A C   1 
ATOM   1209  O  O   . PHE A 1 246 ? 103.067 167.004 122.118 1.00 58.41  ? 221 PHE A O   1 
ATOM   1210  C  CB  . PHE A 1 246 ? 105.745 166.635 121.141 1.00 57.01  ? 221 PHE A CB  1 
ATOM   1211  C  CG  . PHE A 1 246 ? 106.691 166.058 120.128 1.00 49.70  ? 221 PHE A CG  1 
ATOM   1212  C  CD1 . PHE A 1 246 ? 106.265 165.108 119.226 1.00 46.92  ? 221 PHE A CD1 1 
ATOM   1213  C  CD2 . PHE A 1 246 ? 108.009 166.461 120.087 1.00 51.38  ? 221 PHE A CD2 1 
ATOM   1214  C  CE1 . PHE A 1 246 ? 107.134 164.578 118.301 1.00 45.56  ? 221 PHE A CE1 1 
ATOM   1215  C  CE2 . PHE A 1 246 ? 108.878 165.931 119.164 1.00 52.95  ? 221 PHE A CE2 1 
ATOM   1216  C  CZ  . PHE A 1 246 ? 108.441 164.990 118.271 1.00 44.42  ? 221 PHE A CZ  1 
ATOM   1217  N  N   . LEU A 1 247 ? 103.399 169.213 121.879 1.00 69.49  ? 222 LEU A N   1 
ATOM   1218  C  CA  . LEU A 1 247 ? 102.325 169.555 122.801 1.00 71.92  ? 222 LEU A CA  1 
ATOM   1219  C  C   . LEU A 1 247 ? 100.989 169.095 122.240 1.00 74.36  ? 222 LEU A C   1 
ATOM   1220  O  O   . LEU A 1 247 ? 100.671 169.346 121.076 1.00 78.17  ? 222 LEU A O   1 
ATOM   1221  C  CB  . LEU A 1 247 ? 102.300 171.062 123.051 1.00 74.53  ? 222 LEU A CB  1 
ATOM   1222  C  CG  . LEU A 1 247 ? 101.174 171.608 123.934 1.00 75.23  ? 222 LEU A CG  1 
ATOM   1223  C  CD1 . LEU A 1 247 ? 101.725 172.583 124.953 1.00 75.90  ? 222 LEU A CD1 1 
ATOM   1224  C  CD2 . LEU A 1 247 ? 100.095 172.278 123.100 1.00 75.23  ? 222 LEU A CD2 1 
ATOM   1225  N  N   . SER A 1 248 ? 100.203 168.422 123.076 1.00 76.63  ? 223 SER A N   1 
ATOM   1226  C  CA  . SER A 1 248 ? 98.903  167.925 122.659 1.00 77.27  ? 223 SER A CA  1 
ATOM   1227  C  C   . SER A 1 248 ? 97.975  167.879 123.859 1.00 81.18  ? 223 SER A C   1 
ATOM   1228  O  O   . SER A 1 248 ? 98.422  167.778 125.004 1.00 84.03  ? 223 SER A O   1 
ATOM   1229  C  CB  . SER A 1 248 ? 99.001  166.534 122.031 1.00 76.61  ? 223 SER A CB  1 
ATOM   1230  O  OG  . SER A 1 248 ? 97.774  165.841 122.164 1.00 79.01  ? 223 SER A OG  1 
ATOM   1231  N  N   . THR A 1 249 ? 96.673  167.948 123.583 1.00 87.59  ? 224 THR A N   1 
ATOM   1232  C  CA  . THR A 1 249 ? 95.660  167.848 124.620 1.00 87.60  ? 224 THR A CA  1 
ATOM   1233  C  C   . THR A 1 249 ? 94.812  166.591 124.517 1.00 86.23  ? 224 THR A C   1 
ATOM   1234  O  O   . THR A 1 249 ? 94.207  166.193 125.516 1.00 87.20  ? 224 THR A O   1 
ATOM   1235  C  CB  . THR A 1 249 ? 94.732  169.072 124.586 1.00 87.78  ? 224 THR A CB  1 
ATOM   1236  O  OG1 . THR A 1 249 ? 93.964  169.056 123.379 1.00 88.42  ? 224 THR A OG1 1 
ATOM   1237  C  CG2 . THR A 1 249 ? 95.541  170.352 124.639 1.00 86.18  ? 224 THR A CG2 1 
ATOM   1238  N  N   . GLY A 1 250 ? 94.761  165.957 123.351 1.00 84.78  ? 225 GLY A N   1 
ATOM   1239  C  CA  . GLY A 1 250 ? 93.943  164.777 123.169 1.00 86.60  ? 225 GLY A CA  1 
ATOM   1240  C  C   . GLY A 1 250 ? 92.827  164.999 122.173 1.00 87.03  ? 225 GLY A C   1 
ATOM   1241  O  O   . GLY A 1 250 ? 92.526  164.119 121.361 1.00 87.73  ? 225 GLY A O   1 
ATOM   1242  N  N   . ASP A 1 251 ? 92.206  166.172 122.221 1.00 94.84  ? 226 ASP A N   1 
ATOM   1243  C  CA  . ASP A 1 251 ? 91.154  166.522 121.282 1.00 95.55  ? 226 ASP A CA  1 
ATOM   1244  C  C   . ASP A 1 251 ? 91.766  167.231 120.074 1.00 96.81  ? 226 ASP A C   1 
ATOM   1245  O  O   . ASP A 1 251 ? 92.985  167.259 119.894 1.00 94.46  ? 226 ASP A O   1 
ATOM   1246  C  CB  . ASP A 1 251 ? 90.082  167.365 121.971 1.00 95.09  ? 226 ASP A CB  1 
ATOM   1247  C  CG  . ASP A 1 251 ? 90.652  168.582 122.673 1.00 99.51  ? 226 ASP A CG  1 
ATOM   1248  O  OD1 . ASP A 1 251 ? 91.870  168.825 122.563 1.00 100.75 ? 226 ASP A OD1 1 
ATOM   1249  O  OD2 . ASP A 1 251 ? 89.874  169.301 123.333 1.00 101.58 ? 226 ASP A OD2 1 
ATOM   1250  N  N   . GLN A 1 252 ? 90.919  167.821 119.234 1.00 96.71  ? 227 GLN A N   1 
ATOM   1251  C  CA  . GLN A 1 252 ? 91.373  168.439 117.996 1.00 95.22  ? 227 GLN A CA  1 
ATOM   1252  C  C   . GLN A 1 252 ? 91.902  169.853 118.189 1.00 95.09  ? 227 GLN A C   1 
ATOM   1253  O  O   . GLN A 1 252 ? 92.321  170.476 117.208 1.00 97.01  ? 227 GLN A O   1 
ATOM   1254  C  CB  . GLN A 1 252 ? 90.240  168.449 116.964 1.00 95.28  ? 227 GLN A CB  1 
ATOM   1255  C  CG  . GLN A 1 252 ? 89.969  167.109 116.270 1.00 95.33  ? 227 GLN A CG  1 
ATOM   1256  C  CD  . GLN A 1 252 ? 89.723  165.951 117.226 1.00 97.09  ? 227 GLN A CD  1 
ATOM   1257  O  OE1 . GLN A 1 252 ? 89.389  166.147 118.394 1.00 97.48  ? 227 GLN A OE1 1 
ATOM   1258  N  NE2 . GLN A 1 252 ? 89.887  164.733 116.727 1.00 96.86  ? 227 GLN A NE2 1 
ATOM   1259  N  N   . ALA A 1 253 ? 91.883  170.380 119.415 1.00 97.16  ? 228 ALA A N   1 
ATOM   1260  C  CA  . ALA A 1 253 ? 92.487  171.685 119.663 1.00 99.51  ? 228 ALA A CA  1 
ATOM   1261  C  C   . ALA A 1 253 ? 93.986  171.652 119.398 1.00 99.99  ? 228 ALA A C   1 
ATOM   1262  O  O   . ALA A 1 253 ? 94.545  172.592 118.823 1.00 98.47  ? 228 ALA A O   1 
ATOM   1263  C  CB  . ALA A 1 253 ? 92.204  172.132 121.095 1.00 99.47  ? 228 ALA A CB  1 
ATOM   1264  N  N   . ALA A 1 254 ? 94.653  170.576 119.819 1.00 90.18  ? 229 ALA A N   1 
ATOM   1265  C  CA  . ALA A 1 254 ? 96.063  170.355 119.506 1.00 85.85  ? 229 ALA A CA  1 
ATOM   1266  C  C   . ALA A 1 254 ? 96.279  168.845 119.504 1.00 86.42  ? 229 ALA A C   1 
ATOM   1267  O  O   . ALA A 1 254 ? 96.401  168.236 120.570 1.00 89.91  ? 229 ALA A O   1 
ATOM   1268  C  CB  . ALA A 1 254 ? 96.973  171.054 120.506 1.00 84.03  ? 229 ALA A CB  1 
ATOM   1269  N  N   . LYS A 1 255 ? 96.309  168.251 118.310 1.00 80.92  ? 230 LYS A N   1 
ATOM   1270  C  CA  . LYS A 1 255 ? 96.413  166.798 118.210 1.00 82.01  ? 230 LYS A CA  1 
ATOM   1271  C  C   . LYS A 1 255 ? 97.793  166.303 118.625 1.00 78.11  ? 230 LYS A C   1 
ATOM   1272  O  O   . LYS A 1 255 ? 97.914  165.254 119.268 1.00 75.78  ? 230 LYS A O   1 
ATOM   1273  C  CB  . LYS A 1 255 ? 96.084  166.347 116.789 1.00 80.56  ? 230 LYS A CB  1 
ATOM   1274  C  CG  . LYS A 1 255 ? 94.620  166.036 116.567 1.00 78.66  ? 230 LYS A CG  1 
ATOM   1275  C  CD  . LYS A 1 255 ? 94.416  165.230 115.299 1.00 80.08  ? 230 LYS A CD  1 
ATOM   1276  C  CE  . LYS A 1 255 ? 93.750  163.898 115.596 1.00 80.16  ? 230 LYS A CE  1 
ATOM   1277  N  NZ  . LYS A 1 255 ? 93.290  163.219 114.356 1.00 81.32  ? 230 LYS A NZ  1 
ATOM   1278  N  N   . GLY A 1 256 ? 98.840  167.031 118.264 1.00 66.21  ? 231 GLY A N   1 
ATOM   1279  C  CA  . GLY A 1 256 ? 100.193 166.644 118.605 1.00 71.16  ? 231 GLY A CA  1 
ATOM   1280  C  C   . GLY A 1 256 ? 100.926 166.020 117.436 1.00 76.13  ? 231 GLY A C   1 
ATOM   1281  O  O   . GLY A 1 256 ? 100.462 166.012 116.293 1.00 79.94  ? 231 GLY A O   1 
ATOM   1282  N  N   . ASN A 1 257 ? 102.104 165.478 117.751 1.00 59.86  ? 232 ASN A N   1 
ATOM   1283  C  CA  . ASN A 1 257 ? 102.974 164.832 116.767 1.00 48.12  ? 232 ASN A CA  1 
ATOM   1284  C  C   . ASN A 1 257 ? 103.345 165.781 115.633 1.00 57.68  ? 232 ASN A C   1 
ATOM   1285  O  O   . ASN A 1 257 ? 103.319 165.411 114.460 1.00 64.91  ? 232 ASN A O   1 
ATOM   1286  C  CB  . ASN A 1 257 ? 102.332 163.567 116.203 1.00 45.66  ? 232 ASN A CB  1 
ATOM   1287  C  CG  . ASN A 1 257 ? 101.933 162.599 117.273 1.00 51.44  ? 232 ASN A CG  1 
ATOM   1288  O  OD1 . ASN A 1 257 ? 101.948 162.927 118.455 1.00 65.14  ? 232 ASN A OD1 1 
ATOM   1289  N  ND2 . ASN A 1 257 ? 101.562 161.394 116.871 1.00 56.85  ? 232 ASN A ND2 1 
ATOM   1290  N  N   . TYR A 1 258 ? 103.687 167.021 115.975 1.00 56.33  ? 233 TYR A N   1 
ATOM   1291  C  CA  . TYR A 1 258 ? 104.113 167.953 114.941 1.00 56.30  ? 233 TYR A CA  1 
ATOM   1292  C  C   . TYR A 1 258 ? 105.539 167.682 114.487 1.00 57.08  ? 233 TYR A C   1 
ATOM   1293  O  O   . TYR A 1 258 ? 105.871 167.930 113.324 1.00 68.63  ? 233 TYR A O   1 
ATOM   1294  C  CB  . TYR A 1 258 ? 103.956 169.389 115.434 1.00 59.20  ? 233 TYR A CB  1 
ATOM   1295  C  CG  . TYR A 1 258 ? 102.573 169.667 115.971 1.00 60.79  ? 233 TYR A CG  1 
ATOM   1296  C  CD1 . TYR A 1 258 ? 101.453 169.445 115.189 1.00 63.18  ? 233 TYR A CD1 1 
ATOM   1297  C  CD2 . TYR A 1 258 ? 102.388 170.131 117.262 1.00 63.29  ? 233 TYR A CD2 1 
ATOM   1298  C  CE1 . TYR A 1 258 ? 100.191 169.683 115.672 1.00 62.92  ? 233 TYR A CE1 1 
ATOM   1299  C  CE2 . TYR A 1 258 ? 101.128 170.372 117.755 1.00 64.75  ? 233 TYR A CE2 1 
ATOM   1300  C  CZ  . TYR A 1 258 ? 100.033 170.147 116.955 1.00 67.32  ? 233 TYR A CZ  1 
ATOM   1301  O  OH  . TYR A 1 258 ? 98.770  170.386 117.440 1.00 74.50  ? 233 TYR A OH  1 
ATOM   1302  N  N   . GLY A 1 259 ? 106.390 167.164 115.371 1.00 51.79  ? 234 GLY A N   1 
ATOM   1303  C  CA  . GLY A 1 259 ? 107.721 166.766 114.946 1.00 52.90  ? 234 GLY A CA  1 
ATOM   1304  C  C   . GLY A 1 259 ? 107.701 165.594 113.984 1.00 57.49  ? 234 GLY A C   1 
ATOM   1305  O  O   . GLY A 1 259 ? 108.471 165.556 113.020 1.00 63.60  ? 234 GLY A O   1 
ATOM   1306  N  N   . LEU A 1 260 ? 106.826 164.619 114.231 1.00 49.80  ? 235 LEU A N   1 
ATOM   1307  C  CA  . LEU A 1 260 ? 106.712 163.490 113.316 1.00 51.82  ? 235 LEU A CA  1 
ATOM   1308  C  C   . LEU A 1 260 ? 106.232 163.945 111.944 1.00 52.23  ? 235 LEU A C   1 
ATOM   1309  O  O   . LEU A 1 260 ? 106.729 163.476 110.915 1.00 61.27  ? 235 LEU A O   1 
ATOM   1310  C  CB  . LEU A 1 260 ? 105.771 162.434 113.895 1.00 49.66  ? 235 LEU A CB  1 
ATOM   1311  C  CG  . LEU A 1 260 ? 106.278 161.589 115.064 1.00 43.78  ? 235 LEU A CG  1 
ATOM   1312  C  CD1 . LEU A 1 260 ? 105.375 160.399 115.280 1.00 50.08  ? 235 LEU A CD1 1 
ATOM   1313  C  CD2 . LEU A 1 260 ? 107.689 161.126 114.815 1.00 51.47  ? 235 LEU A CD2 1 
ATOM   1314  N  N   . LEU A 1 261 ? 105.268 164.864 111.906 1.00 47.98  ? 236 LEU A N   1 
ATOM   1315  C  CA  . LEU A 1 261 ? 104.812 165.385 110.623 1.00 54.23  ? 236 LEU A CA  1 
ATOM   1316  C  C   . LEU A 1 261 ? 105.881 166.236 109.949 1.00 58.38  ? 236 LEU A C   1 
ATOM   1317  O  O   . LEU A 1 261 ? 105.951 166.268 108.718 1.00 65.76  ? 236 LEU A O   1 
ATOM   1318  C  CB  . LEU A 1 261 ? 103.521 166.178 110.807 1.00 54.40  ? 236 LEU A CB  1 
ATOM   1319  C  CG  . LEU A 1 261 ? 102.360 165.345 111.347 1.00 53.31  ? 236 LEU A CG  1 
ATOM   1320  C  CD1 . LEU A 1 261 ? 101.197 166.228 111.754 1.00 58.01  ? 236 LEU A CD1 1 
ATOM   1321  C  CD2 . LEU A 1 261 ? 101.927 164.326 110.316 1.00 55.55  ? 236 LEU A CD2 1 
ATOM   1322  N  N   . ASP A 1 262 ? 106.730 166.915 110.723 1.00 61.53  ? 237 ASP A N   1 
ATOM   1323  C  CA  . ASP A 1 262 ? 107.864 167.614 110.123 1.00 61.80  ? 237 ASP A CA  1 
ATOM   1324  C  C   . ASP A 1 262 ? 108.841 166.636 109.482 1.00 63.14  ? 237 ASP A C   1 
ATOM   1325  O  O   . ASP A 1 262 ? 109.340 166.878 108.375 1.00 67.17  ? 237 ASP A O   1 
ATOM   1326  C  CB  . ASP A 1 262 ? 108.570 168.467 111.173 1.00 57.04  ? 237 ASP A CB  1 
ATOM   1327  C  CG  . ASP A 1 262 ? 107.735 169.646 111.618 1.00 67.96  ? 237 ASP A CG  1 
ATOM   1328  O  OD1 . ASP A 1 262 ? 106.552 169.713 111.229 1.00 66.48  ? 237 ASP A OD1 1 
ATOM   1329  O  OD2 . ASP A 1 262 ? 108.257 170.506 112.356 1.00 71.32  ? 237 ASP A OD2 1 
ATOM   1330  N  N   . GLN A 1 263 ? 109.129 165.525 110.161 1.00 47.79  ? 238 GLN A N   1 
ATOM   1331  C  CA  . GLN A 1 263 ? 110.007 164.511 109.580 1.00 38.11  ? 238 GLN A CA  1 
ATOM   1332  C  C   . GLN A 1 263 ? 109.392 163.905 108.325 1.00 47.96  ? 238 GLN A C   1 
ATOM   1333  O  O   . GLN A 1 263 ? 110.093 163.648 107.339 1.00 57.86  ? 238 GLN A O   1 
ATOM   1334  C  CB  . GLN A 1 263 ? 110.310 163.422 110.604 1.00 32.12  ? 238 GLN A CB  1 
ATOM   1335  C  CG  . GLN A 1 263 ? 111.336 163.819 111.636 1.00 48.05  ? 238 GLN A CG  1 
ATOM   1336  C  CD  . GLN A 1 263 ? 111.191 163.043 112.921 1.00 46.76  ? 238 GLN A CD  1 
ATOM   1337  O  OE1 . GLN A 1 263 ? 110.137 162.482 113.199 1.00 40.90  ? 238 GLN A OE1 1 
ATOM   1338  N  NE2 . GLN A 1 263 ? 112.252 163.003 113.712 1.00 44.52  ? 238 GLN A NE2 1 
ATOM   1339  N  N   . ILE A 1 264 ? 108.082 163.672 108.342 1.00 47.84  ? 239 ILE A N   1 
ATOM   1340  C  CA  . ILE A 1 264 ? 107.414 163.127 107.166 1.00 44.19  ? 239 ILE A CA  1 
ATOM   1341  C  C   . ILE A 1 264 ? 107.434 164.132 106.019 1.00 50.25  ? 239 ILE A C   1 
ATOM   1342  O  O   . ILE A 1 264 ? 107.586 163.756 104.852 1.00 56.11  ? 239 ILE A O   1 
ATOM   1343  C  CB  . ILE A 1 264 ? 105.985 162.689 107.528 1.00 45.93  ? 239 ILE A CB  1 
ATOM   1344  C  CG1 . ILE A 1 264 ? 106.025 161.345 108.250 1.00 43.93  ? 239 ILE A CG1 1 
ATOM   1345  C  CG2 . ILE A 1 264 ? 105.118 162.602 106.293 1.00 49.75  ? 239 ILE A CG2 1 
ATOM   1346  C  CD1 . ILE A 1 264 ? 104.741 160.988 108.942 1.00 54.42  ? 239 ILE A CD1 1 
ATOM   1347  N  N   . GLN A 1 265 ? 107.293 165.424 106.325 1.00 54.95  ? 240 GLN A N   1 
ATOM   1348  C  CA  . GLN A 1 265 ? 107.397 166.444 105.285 1.00 49.14  ? 240 GLN A CA  1 
ATOM   1349  C  C   . GLN A 1 265 ? 108.798 166.485 104.693 1.00 55.09  ? 240 GLN A C   1 
ATOM   1350  O  O   . GLN A 1 265 ? 108.963 166.669 103.483 1.00 68.69  ? 240 GLN A O   1 
ATOM   1351  C  CB  . GLN A 1 265 ? 107.018 167.811 105.844 1.00 48.79  ? 240 GLN A CB  1 
ATOM   1352  C  CG  . GLN A 1 265 ? 105.966 168.534 105.030 1.00 59.55  ? 240 GLN A CG  1 
ATOM   1353  C  CD  . GLN A 1 265 ? 106.418 168.816 103.614 1.00 66.23  ? 240 GLN A CD  1 
ATOM   1354  O  OE1 . GLN A 1 265 ? 107.581 169.125 103.372 1.00 63.81  ? 240 GLN A OE1 1 
ATOM   1355  N  NE2 . GLN A 1 265 ? 105.494 168.712 102.667 1.00 64.30  ? 240 GLN A NE2 1 
ATOM   1356  N  N   . ALA A 1 266 ? 109.823 166.330 105.532 1.00 48.52  ? 241 ALA A N   1 
ATOM   1357  C  CA  . ALA A 1 266 ? 111.184 166.250 105.012 1.00 47.31  ? 241 ALA A CA  1 
ATOM   1358  C  C   . ALA A 1 266 ? 111.356 165.033 104.115 1.00 47.32  ? 241 ALA A C   1 
ATOM   1359  O  O   . ALA A 1 266 ? 112.014 165.109 103.071 1.00 55.37  ? 241 ALA A O   1 
ATOM   1360  C  CB  . ALA A 1 266 ? 112.188 166.211 106.159 1.00 46.32  ? 241 ALA A CB  1 
ATOM   1361  N  N   . LEU A 1 267 ? 110.773 163.900 104.506 1.00 45.75  ? 242 LEU A N   1 
ATOM   1362  C  CA  . LEU A 1 267 ? 110.832 162.713 103.657 1.00 44.58  ? 242 LEU A CA  1 
ATOM   1363  C  C   . LEU A 1 267 ? 110.122 162.951 102.332 1.00 48.46  ? 242 LEU A C   1 
ATOM   1364  O  O   . LEU A 1 267 ? 110.569 162.472 101.289 1.00 55.11  ? 242 LEU A O   1 
ATOM   1365  C  CB  . LEU A 1 267 ? 110.227 161.511 104.378 1.00 42.72  ? 242 LEU A CB  1 
ATOM   1366  C  CG  . LEU A 1 267 ? 111.171 160.671 105.235 1.00 42.29  ? 242 LEU A CG  1 
ATOM   1367  C  CD1 . LEU A 1 267 ? 110.403 159.560 105.913 1.00 42.74  ? 242 LEU A CD1 1 
ATOM   1368  C  CD2 . LEU A 1 267 ? 112.291 160.106 104.392 1.00 43.24  ? 242 LEU A CD2 1 
ATOM   1369  N  N   . ARG A 1 268 ? 109.003 163.676 102.357 1.00 52.16  ? 243 ARG A N   1 
ATOM   1370  C  CA  . ARG A 1 268 ? 108.284 163.989 101.124 1.00 49.26  ? 243 ARG A CA  1 
ATOM   1371  C  C   . ARG A 1 268 ? 109.106 164.895 100.214 1.00 50.35  ? 243 ARG A C   1 
ATOM   1372  O  O   . ARG A 1 268 ? 109.157 164.688 98.994  1.00 62.38  ? 243 ARG A O   1 
ATOM   1373  C  CB  . ARG A 1 268 ? 106.946 164.642 101.457 1.00 51.03  ? 243 ARG A CB  1 
ATOM   1374  C  CG  . ARG A 1 268 ? 105.844 164.327 100.476 1.00 58.01  ? 243 ARG A CG  1 
ATOM   1375  C  CD  . ARG A 1 268 ? 104.582 165.098 100.810 1.00 59.41  ? 243 ARG A CD  1 
ATOM   1376  N  NE  . ARG A 1 268 ? 104.069 164.774 102.135 1.00 55.37  ? 243 ARG A NE  1 
ATOM   1377  C  CZ  . ARG A 1 268 ? 103.358 163.692 102.416 1.00 62.18  ? 243 ARG A CZ  1 
ATOM   1378  N  NH1 . ARG A 1 268 ? 103.072 162.793 101.489 1.00 62.67  ? 243 ARG A NH1 1 
ATOM   1379  N  NH2 . ARG A 1 268 ? 102.920 163.508 103.658 1.00 62.90  ? 243 ARG A NH2 1 
ATOM   1380  N  N   . TRP A 1 269 ? 109.744 165.914 100.790 1.00 44.84  ? 244 TRP A N   1 
ATOM   1381  C  CA  . TRP A 1 269 ? 110.622 166.778 100.009 1.00 45.10  ? 244 TRP A CA  1 
ATOM   1382  C  C   . TRP A 1 269 ? 111.762 165.982 99.397  1.00 45.11  ? 244 TRP A C   1 
ATOM   1383  O  O   . TRP A 1 269 ? 112.118 166.191 98.233  1.00 49.38  ? 244 TRP A O   1 
ATOM   1384  C  CB  . TRP A 1 269 ? 111.169 167.900 100.886 1.00 48.44  ? 244 TRP A CB  1 
ATOM   1385  C  CG  . TRP A 1 269 ? 111.945 168.939 100.139 1.00 50.55  ? 244 TRP A CG  1 
ATOM   1386  C  CD1 . TRP A 1 269 ? 111.481 170.135 99.686  1.00 54.97  ? 244 TRP A CD1 1 
ATOM   1387  C  CD2 . TRP A 1 269 ? 113.329 168.882 99.773  1.00 47.04  ? 244 TRP A CD2 1 
ATOM   1388  N  NE1 . TRP A 1 269 ? 112.485 170.825 99.055  1.00 48.61  ? 244 TRP A NE1 1 
ATOM   1389  C  CE2 . TRP A 1 269 ? 113.630 170.076 99.096  1.00 51.26  ? 244 TRP A CE2 1 
ATOM   1390  C  CE3 . TRP A 1 269 ? 114.341 167.938 99.952  1.00 45.60  ? 244 TRP A CE3 1 
ATOM   1391  C  CZ2 . TRP A 1 269 ? 114.897 170.348 98.596  1.00 56.00  ? 244 TRP A CZ2 1 
ATOM   1392  C  CZ3 . TRP A 1 269 ? 115.597 168.211 99.454  1.00 44.24  ? 244 TRP A CZ3 1 
ATOM   1393  C  CH2 . TRP A 1 269 ? 115.864 169.404 98.784  1.00 50.65  ? 244 TRP A CH2 1 
ATOM   1394  N  N   . LEU A 1 270 ? 112.348 165.063 100.165 1.00 50.37  ? 245 LEU A N   1 
ATOM   1395  C  CA  . LEU A 1 270 ? 113.382 164.194 99.614  1.00 47.46  ? 245 LEU A CA  1 
ATOM   1396  C  C   . LEU A 1 270 ? 112.829 163.328 98.489  1.00 52.77  ? 245 LEU A C   1 
ATOM   1397  O  O   . LEU A 1 270 ? 113.477 163.155 97.455  1.00 55.98  ? 245 LEU A O   1 
ATOM   1398  C  CB  . LEU A 1 270 ? 113.978 163.318 100.715 1.00 45.37  ? 245 LEU A CB  1 
ATOM   1399  C  CG  . LEU A 1 270 ? 115.038 163.942 101.618 1.00 48.76  ? 245 LEU A CG  1 
ATOM   1400  C  CD1 . LEU A 1 270 ? 115.893 162.866 102.250 1.00 50.49  ? 245 LEU A CD1 1 
ATOM   1401  C  CD2 . LEU A 1 270 ? 115.896 164.898 100.828 1.00 55.81  ? 245 LEU A CD2 1 
ATOM   1402  N  N   . SER A 1 271 ? 111.625 162.788 98.668  1.00 60.32  ? 246 SER A N   1 
ATOM   1403  C  CA  . SER A 1 271 ? 111.059 161.888 97.670  1.00 55.82  ? 246 SER A CA  1 
ATOM   1404  C  C   . SER A 1 271 ? 110.810 162.606 96.353  1.00 54.71  ? 246 SER A C   1 
ATOM   1405  O  O   . SER A 1 271 ? 111.027 162.036 95.278  1.00 53.99  ? 246 SER A O   1 
ATOM   1406  C  CB  . SER A 1 271 ? 109.763 161.273 98.193  1.00 51.69  ? 246 SER A CB  1 
ATOM   1407  O  OG  . SER A 1 271 ? 109.264 160.306 97.287  1.00 58.62  ? 246 SER A OG  1 
ATOM   1408  N  N   . GLU A 1 272 ? 110.348 163.852 96.410  1.00 59.84  ? 247 GLU A N   1 
ATOM   1409  C  CA  . GLU A 1 272 ? 109.984 164.571 95.197  1.00 60.04  ? 247 GLU A CA  1 
ATOM   1410  C  C   . GLU A 1 272 ? 111.023 165.602 94.758  1.00 61.06  ? 247 GLU A C   1 
ATOM   1411  O  O   . GLU A 1 272 ? 110.755 166.368 93.830  1.00 61.51  ? 247 GLU A O   1 
ATOM   1412  C  CB  . GLU A 1 272 ? 108.619 165.240 95.371  1.00 60.21  ? 247 GLU A CB  1 
ATOM   1413  C  CG  . GLU A 1 272 ? 108.638 166.529 96.166  1.00 65.69  ? 247 GLU A CG  1 
ATOM   1414  C  CD  . GLU A 1 272 ? 107.255 166.948 96.619  1.00 73.06  ? 247 GLU A CD  1 
ATOM   1415  O  OE1 . GLU A 1 272 ? 106.321 166.129 96.505  1.00 70.30  ? 247 GLU A OE1 1 
ATOM   1416  O  OE2 . GLU A 1 272 ? 107.102 168.094 97.093  1.00 72.66  ? 247 GLU A OE2 1 
ATOM   1417  N  N   . ASN A 1 273 ? 112.203 165.641 95.386  1.00 62.45  ? 248 ASN A N   1 
ATOM   1418  C  CA  . ASN A 1 273 ? 113.214 166.604 94.962  1.00 57.57  ? 248 ASN A CA  1 
ATOM   1419  C  C   . ASN A 1 273 ? 114.649 166.086 94.975  1.00 59.47  ? 248 ASN A C   1 
ATOM   1420  O  O   . ASN A 1 273 ? 115.566 166.881 94.742  1.00 59.77  ? 248 ASN A O   1 
ATOM   1421  C  CB  . ASN A 1 273 ? 113.146 167.865 95.828  1.00 61.70  ? 248 ASN A CB  1 
ATOM   1422  C  CG  . ASN A 1 273 ? 112.255 168.933 95.237  1.00 63.88  ? 248 ASN A CG  1 
ATOM   1423  O  OD1 . ASN A 1 273 ? 112.736 169.885 94.623  1.00 65.91  ? 248 ASN A OD1 1 
ATOM   1424  N  ND2 . ASN A 1 273 ? 110.951 168.786 95.420  1.00 63.82  ? 248 ASN A ND2 1 
ATOM   1425  N  N   . ILE A 1 274 ? 114.898 164.798 95.234  1.00 60.41  ? 249 ILE A N   1 
ATOM   1426  C  CA  . ILE A 1 274 ? 116.285 164.351 95.363  1.00 61.99  ? 249 ILE A CA  1 
ATOM   1427  C  C   . ILE A 1 274 ? 116.891 163.966 94.022  1.00 70.25  ? 249 ILE A C   1 
ATOM   1428  O  O   . ILE A 1 274 ? 118.122 164.004 93.872  1.00 75.87  ? 249 ILE A O   1 
ATOM   1429  C  CB  . ILE A 1 274 ? 116.416 163.160 96.334  1.00 57.84  ? 249 ILE A CB  1 
ATOM   1430  C  CG1 . ILE A 1 274 ? 117.876 162.749 96.510  1.00 60.65  ? 249 ILE A CG1 1 
ATOM   1431  C  CG2 . ILE A 1 274 ? 115.677 161.967 95.788  1.00 64.69  ? 249 ILE A CG2 1 
ATOM   1432  C  CD1 . ILE A 1 274 ? 118.713 163.774 97.244  1.00 62.73  ? 249 ILE A CD1 1 
ATOM   1433  N  N   . ALA A 1 275 ? 116.068 163.643 93.022  1.00 71.95  ? 250 ALA A N   1 
ATOM   1434  C  CA  . ALA A 1 275 ? 116.607 163.248 91.727  1.00 69.88  ? 250 ALA A CA  1 
ATOM   1435  C  C   . ALA A 1 275 ? 117.396 164.377 91.079  1.00 67.01  ? 250 ALA A C   1 
ATOM   1436  O  O   . ALA A 1 275 ? 118.267 164.124 90.240  1.00 69.83  ? 250 ALA A O   1 
ATOM   1437  C  CB  . ALA A 1 275 ? 115.478 162.788 90.807  1.00 69.70  ? 250 ALA A CB  1 
ATOM   1438  N  N   . HIS A 1 276 ? 117.108 165.625 91.450  1.00 66.84  ? 251 HIS A N   1 
ATOM   1439  C  CA  . HIS A 1 276 ? 117.868 166.748 90.916  1.00 66.86  ? 251 HIS A CA  1 
ATOM   1440  C  C   . HIS A 1 276 ? 119.290 166.774 91.458  1.00 67.58  ? 251 HIS A C   1 
ATOM   1441  O  O   . HIS A 1 276 ? 120.200 167.268 90.784  1.00 75.41  ? 251 HIS A O   1 
ATOM   1442  C  CB  . HIS A 1 276 ? 117.160 168.062 91.237  1.00 64.46  ? 251 HIS A CB  1 
ATOM   1443  C  CG  . HIS A 1 276 ? 115.754 168.129 90.734  1.00 68.90  ? 251 HIS A CG  1 
ATOM   1444  N  ND1 . HIS A 1 276 ? 114.901 169.164 91.049  1.00 69.85  ? 251 HIS A ND1 1 
ATOM   1445  C  CD2 . HIS A 1 276 ? 115.050 167.291 89.937  1.00 67.07  ? 251 HIS A CD2 1 
ATOM   1446  C  CE1 . HIS A 1 276 ? 113.732 168.960 90.470  1.00 69.54  ? 251 HIS A CE1 1 
ATOM   1447  N  NE2 . HIS A 1 276 ? 113.796 167.830 89.790  1.00 70.89  ? 251 HIS A NE2 1 
ATOM   1448  N  N   . PHE A 1 277 ? 119.500 166.255 92.663  1.00 63.76  ? 252 PHE A N   1 
ATOM   1449  C  CA  . PHE A 1 277 ? 120.810 166.239 93.294  1.00 67.50  ? 252 PHE A CA  1 
ATOM   1450  C  C   . PHE A 1 277 ? 121.605 164.989 92.956  1.00 66.86  ? 252 PHE A C   1 
ATOM   1451  O  O   . PHE A 1 277 ? 122.697 164.798 93.499  1.00 71.24  ? 252 PHE A O   1 
ATOM   1452  C  CB  . PHE A 1 277 ? 120.667 166.365 94.810  1.00 59.95  ? 252 PHE A CB  1 
ATOM   1453  C  CG  . PHE A 1 277 ? 120.186 167.709 95.262  1.00 60.60  ? 252 PHE A CG  1 
ATOM   1454  C  CD1 . PHE A 1 277 ? 118.843 168.023 95.232  1.00 63.24  ? 252 PHE A CD1 1 
ATOM   1455  C  CD2 . PHE A 1 277 ? 121.076 168.658 95.717  1.00 66.25  ? 252 PHE A CD2 1 
ATOM   1456  C  CE1 . PHE A 1 277 ? 118.398 169.255 95.646  1.00 64.81  ? 252 PHE A CE1 1 
ATOM   1457  C  CE2 . PHE A 1 277 ? 120.635 169.892 96.132  1.00 66.86  ? 252 PHE A CE2 1 
ATOM   1458  C  CZ  . PHE A 1 277 ? 119.294 170.190 96.096  1.00 66.11  ? 252 PHE A CZ  1 
ATOM   1459  N  N   . GLY A 1 278 ? 121.085 164.136 92.079  1.00 65.20  ? 253 GLY A N   1 
ATOM   1460  C  CA  . GLY A 1 278 ? 121.741 162.898 91.731  1.00 69.42  ? 253 GLY A CA  1 
ATOM   1461  C  C   . GLY A 1 278 ? 121.340 161.703 92.564  1.00 69.22  ? 253 GLY A C   1 
ATOM   1462  O  O   . GLY A 1 278 ? 121.773 160.586 92.258  1.00 70.27  ? 253 GLY A O   1 
ATOM   1463  N  N   . GLY A 1 279 ? 120.526 161.897 93.598  1.00 66.99  ? 254 GLY A N   1 
ATOM   1464  C  CA  . GLY A 1 279 ? 120.112 160.799 94.442  1.00 68.76  ? 254 GLY A CA  1 
ATOM   1465  C  C   . GLY A 1 279 ? 119.047 159.930 93.807  1.00 70.76  ? 254 GLY A C   1 
ATOM   1466  O  O   . GLY A 1 279 ? 118.465 160.256 92.774  1.00 66.23  ? 254 GLY A O   1 
ATOM   1467  N  N   . ASP A 1 280 ? 118.793 158.796 94.453  1.00 73.40  ? 255 ASP A N   1 
ATOM   1468  C  CA  . ASP A 1 280 ? 117.827 157.819 93.967  1.00 70.07  ? 255 ASP A CA  1 
ATOM   1469  C  C   . ASP A 1 280 ? 116.583 157.848 94.840  1.00 70.81  ? 255 ASP A C   1 
ATOM   1470  O  O   . ASP A 1 280 ? 116.626 157.362 95.980  1.00 77.20  ? 255 ASP A O   1 
ATOM   1471  C  CB  . ASP A 1 280 ? 118.444 156.422 93.965  1.00 67.18  ? 255 ASP A CB  1 
ATOM   1472  C  CG  . ASP A 1 280 ? 117.866 155.534 92.889  1.00 77.35  ? 255 ASP A CG  1 
ATOM   1473  O  OD1 . ASP A 1 280 ? 116.698 155.750 92.507  1.00 79.71  ? 255 ASP A OD1 1 
ATOM   1474  O  OD2 . ASP A 1 280 ? 118.579 154.622 92.423  1.00 78.97  ? 255 ASP A OD2 1 
ATOM   1475  N  N   . PRO A 1 281 ? 115.456 158.375 94.362  1.00 70.67  ? 256 PRO A N   1 
ATOM   1476  C  CA  . PRO A 1 281 ? 114.272 158.519 95.214  1.00 67.00  ? 256 PRO A CA  1 
ATOM   1477  C  C   . PRO A 1 281 ? 113.527 157.224 95.495  1.00 73.35  ? 256 PRO A C   1 
ATOM   1478  O  O   . PRO A 1 281 ? 112.426 157.277 96.048  1.00 77.07  ? 256 PRO A O   1 
ATOM   1479  C  CB  . PRO A 1 281 ? 113.393 159.479 94.400  1.00 72.77  ? 256 PRO A CB  1 
ATOM   1480  C  CG  . PRO A 1 281 ? 113.747 159.187 92.996  1.00 77.20  ? 256 PRO A CG  1 
ATOM   1481  C  CD  . PRO A 1 281 ? 115.213 158.852 92.991  1.00 77.12  ? 256 PRO A CD  1 
ATOM   1482  N  N   . GLU A 1 282 ? 114.085 156.071 95.129  1.00 77.89  ? 257 GLU A N   1 
ATOM   1483  C  CA  . GLU A 1 282 ? 113.474 154.783 95.430  1.00 75.40  ? 257 GLU A CA  1 
ATOM   1484  C  C   . GLU A 1 282 ? 114.342 153.929 96.344  1.00 73.19  ? 257 GLU A C   1 
ATOM   1485  O  O   . GLU A 1 282 ? 114.090 152.726 96.470  1.00 75.51  ? 257 GLU A O   1 
ATOM   1486  C  CB  . GLU A 1 282 ? 113.171 154.021 94.137  1.00 75.85  ? 257 GLU A CB  1 
ATOM   1487  C  CG  . GLU A 1 282 ? 112.059 154.633 93.304  1.00 80.44  ? 257 GLU A CG  1 
ATOM   1488  C  CD  . GLU A 1 282 ? 110.682 154.150 93.718  1.00 83.29  ? 257 GLU A CD  1 
ATOM   1489  O  OE1 . GLU A 1 282 ? 110.494 152.921 93.836  1.00 82.45  ? 257 GLU A OE1 1 
ATOM   1490  O  OE2 . GLU A 1 282 ? 109.785 154.996 93.918  1.00 83.30  ? 257 GLU A OE2 1 
ATOM   1491  N  N   . ARG A 1 283 ? 115.358 154.510 96.977  1.00 61.37  ? 258 ARG A N   1 
ATOM   1492  C  CA  . ARG A 1 283 ? 116.240 153.782 97.883  1.00 64.47  ? 258 ARG A CA  1 
ATOM   1493  C  C   . ARG A 1 283 ? 116.542 154.629 99.116  1.00 68.88  ? 258 ARG A C   1 
ATOM   1494  O  O   . ARG A 1 283 ? 117.681 154.723 99.571  1.00 72.47  ? 258 ARG A O   1 
ATOM   1495  C  CB  . ARG A 1 283 ? 117.525 153.367 97.170  1.00 65.02  ? 258 ARG A CB  1 
ATOM   1496  C  CG  . ARG A 1 283 ? 117.315 152.344 96.071  1.00 65.11  ? 258 ARG A CG  1 
ATOM   1497  C  CD  . ARG A 1 283 ? 118.589 151.587 95.753  1.00 66.25  ? 258 ARG A CD  1 
ATOM   1498  N  NE  . ARG A 1 283 ? 119.522 152.389 94.973  1.00 67.21  ? 258 ARG A NE  1 
ATOM   1499  C  CZ  . ARG A 1 283 ? 120.655 151.929 94.463  1.00 63.89  ? 258 ARG A CZ  1 
ATOM   1500  N  NH1 . ARG A 1 283 ? 121.019 150.668 94.613  1.00 62.05  ? 258 ARG A NH1 1 
ATOM   1501  N  NH2 . ARG A 1 283 ? 121.444 152.756 93.787  1.00 68.10  ? 258 ARG A NH2 1 
ATOM   1502  N  N   . ILE A 1 284 ? 115.512 155.255 99.677  1.00 54.66  ? 259 ILE A N   1 
ATOM   1503  C  CA  . ILE A 1 284 ? 115.688 156.172 100.799 1.00 47.92  ? 259 ILE A CA  1 
ATOM   1504  C  C   . ILE A 1 284 ? 115.705 155.369 102.095 1.00 44.18  ? 259 ILE A C   1 
ATOM   1505  O  O   . ILE A 1 284 ? 114.661 154.923 102.571 1.00 51.49  ? 259 ILE A O   1 
ATOM   1506  C  CB  . ILE A 1 284 ? 114.588 157.238 100.830 1.00 48.74  ? 259 ILE A CB  1 
ATOM   1507  C  CG1 . ILE A 1 284 ? 114.542 158.002 99.512  1.00 47.50  ? 259 ILE A CG1 1 
ATOM   1508  C  CG2 . ILE A 1 284 ? 114.810 158.200 101.979 1.00 51.80  ? 259 ILE A CG2 1 
ATOM   1509  C  CD1 . ILE A 1 284 ? 113.479 159.065 99.475  1.00 49.87  ? 259 ILE A CD1 1 
ATOM   1510  N  N   . THR A 1 285 ? 116.888 155.192 102.672 1.00 38.08  ? 260 THR A N   1 
ATOM   1511  C  CA  . THR A 1 285 ? 117.030 154.585 103.986 1.00 40.68  ? 260 THR A CA  1 
ATOM   1512  C  C   . THR A 1 285 ? 116.957 155.665 105.053 1.00 48.07  ? 260 THR A C   1 
ATOM   1513  O  O   . THR A 1 285 ? 117.542 156.738 104.903 1.00 61.35  ? 260 THR A O   1 
ATOM   1514  C  CB  . THR A 1 285 ? 118.358 153.839 104.090 1.00 48.53  ? 260 THR A CB  1 
ATOM   1515  O  OG1 . THR A 1 285 ? 118.271 152.613 103.360 1.00 60.91  ? 260 THR A OG1 1 
ATOM   1516  C  CG2 . THR A 1 285 ? 118.696 153.535 105.530 1.00 46.63  ? 260 THR A CG2 1 
ATOM   1517  N  N   . ILE A 1 286 ? 116.229 155.383 106.127 1.00 36.24  ? 261 ILE A N   1 
ATOM   1518  C  CA  . ILE A 1 286 ? 116.035 156.323 107.221 1.00 30.60  ? 261 ILE A CA  1 
ATOM   1519  C  C   . ILE A 1 286 ? 116.574 155.679 108.488 1.00 27.02  ? 261 ILE A C   1 
ATOM   1520  O  O   . ILE A 1 286 ? 116.218 154.541 108.806 1.00 52.27  ? 261 ILE A O   1 
ATOM   1521  C  CB  . ILE A 1 286 ? 114.552 156.706 107.363 1.00 25.55  ? 261 ILE A CB  1 
ATOM   1522  C  CG1 . ILE A 1 286 ? 114.301 157.518 108.621 1.00 40.27  ? 261 ILE A CG1 1 
ATOM   1523  C  CG2 . ILE A 1 286 ? 113.676 155.479 107.385 1.00 32.63  ? 261 ILE A CG2 1 
ATOM   1524  C  CD1 . ILE A 1 286 ? 112.857 157.903 108.763 1.00 42.09  ? 261 ILE A CD1 1 
ATOM   1525  N  N   . PHE A 1 287 ? 117.447 156.389 109.199 1.00 22.05  ? 262 PHE A N   1 
ATOM   1526  C  CA  . PHE A 1 287 ? 118.114 155.804 110.352 1.00 32.50  ? 262 PHE A CA  1 
ATOM   1527  C  C   . PHE A 1 287 ? 118.311 156.849 111.438 1.00 37.30  ? 262 PHE A C   1 
ATOM   1528  O  O   . PHE A 1 287 ? 118.355 158.050 111.173 1.00 56.28  ? 262 PHE A O   1 
ATOM   1529  C  CB  . PHE A 1 287 ? 119.454 155.167 109.958 1.00 37.16  ? 262 PHE A CB  1 
ATOM   1530  C  CG  . PHE A 1 287 ? 120.588 156.138 109.792 1.00 33.13  ? 262 PHE A CG  1 
ATOM   1531  C  CD1 . PHE A 1 287 ? 120.517 157.166 108.881 1.00 40.32  ? 262 PHE A CD1 1 
ATOM   1532  C  CD2 . PHE A 1 287 ? 121.752 155.983 110.517 1.00 36.55  ? 262 PHE A CD2 1 
ATOM   1533  C  CE1 . PHE A 1 287 ? 121.568 158.042 108.723 1.00 40.99  ? 262 PHE A CE1 1 
ATOM   1534  C  CE2 . PHE A 1 287 ? 122.804 156.853 110.358 1.00 38.60  ? 262 PHE A CE2 1 
ATOM   1535  C  CZ  . PHE A 1 287 ? 122.712 157.883 109.461 1.00 39.77  ? 262 PHE A CZ  1 
ATOM   1536  N  N   . GLY A 1 288 ? 118.418 156.371 112.672 1.00 29.82  ? 263 GLY A N   1 
ATOM   1537  C  CA  . GLY A 1 288 ? 118.632 157.250 113.803 1.00 36.91  ? 263 GLY A CA  1 
ATOM   1538  C  C   . GLY A 1 288 ? 118.904 156.453 115.056 1.00 40.19  ? 263 GLY A C   1 
ATOM   1539  O  O   . GLY A 1 288 ? 118.549 155.275 115.153 1.00 41.62  ? 263 GLY A O   1 
ATOM   1540  N  N   . SER A 1 289 ? 119.538 157.115 116.019 1.00 49.13  ? 264 SER A N   1 
ATOM   1541  C  CA  . SER A 1 289 ? 119.932 156.495 117.275 1.00 45.93  ? 264 SER A CA  1 
ATOM   1542  C  C   . SER A 1 289 ? 119.337 157.259 118.444 1.00 45.86  ? 264 SER A C   1 
ATOM   1543  O  O   . SER A 1 289 ? 119.355 158.491 118.462 1.00 57.00  ? 264 SER A O   1 
ATOM   1544  C  CB  . SER A 1 289 ? 121.453 156.454 117.424 1.00 57.31  ? 264 SER A CB  1 
ATOM   1545  O  OG  . SER A 1 289 ? 121.828 156.443 118.790 1.00 55.15  ? 264 SER A OG  1 
ATOM   1546  N  N   . GLY A 1 290 ? 118.829 156.523 119.426 1.00 34.83  ? 265 GLY A N   1 
ATOM   1547  C  CA  . GLY A 1 290 ? 118.227 157.137 120.591 1.00 42.46  ? 265 GLY A CA  1 
ATOM   1548  C  C   . GLY A 1 290 ? 116.757 157.430 120.391 1.00 44.94  ? 265 GLY A C   1 
ATOM   1549  O  O   . GLY A 1 290 ? 116.038 156.621 119.802 1.00 49.51  ? 265 GLY A O   1 
ATOM   1550  N  N   . ALA A 1 291 ? 116.298 158.587 120.871 1.00 56.72  ? 266 ALA A N   1 
ATOM   1551  C  CA  . ALA A 1 291 ? 114.896 158.949 120.696 1.00 52.09  ? 266 ALA A CA  1 
ATOM   1552  C  C   . ALA A 1 291 ? 114.540 159.056 119.224 1.00 51.33  ? 266 ALA A C   1 
ATOM   1553  O  O   . ALA A 1 291 ? 113.430 158.692 118.820 1.00 62.97  ? 266 ALA A O   1 
ATOM   1554  C  CB  . ALA A 1 291 ? 114.590 160.262 121.407 1.00 54.99  ? 266 ALA A CB  1 
ATOM   1555  N  N   . GLY A 1 292 ? 115.469 159.544 118.406 1.00 39.11  ? 267 GLY A N   1 
ATOM   1556  C  CA  . GLY A 1 292 ? 115.233 159.560 116.976 1.00 37.17  ? 267 GLY A CA  1 
ATOM   1557  C  C   . GLY A 1 292 ? 114.923 158.179 116.442 1.00 43.96  ? 267 GLY A C   1 
ATOM   1558  O  O   . GLY A 1 292 ? 114.055 158.017 115.582 1.00 52.88  ? 267 GLY A O   1 
ATOM   1559  N  N   . ALA A 1 293 ? 115.605 157.160 116.972 1.00 37.99  ? 268 ALA A N   1 
ATOM   1560  C  CA  . ALA A 1 293 ? 115.313 155.786 116.579 1.00 33.05  ? 268 ALA A CA  1 
ATOM   1561  C  C   . ALA A 1 293 ? 113.856 155.445 116.834 1.00 35.82  ? 268 ALA A C   1 
ATOM   1562  O  O   . ALA A 1 293 ? 113.209 154.801 116.001 1.00 50.79  ? 268 ALA A O   1 
ATOM   1563  C  CB  . ALA A 1 293 ? 116.222 154.819 117.328 1.00 43.82  ? 268 ALA A CB  1 
ATOM   1564  N  N   . SER A 1 294 ? 113.313 155.890 117.968 1.00 33.45  ? 269 SER A N   1 
ATOM   1565  C  CA  . SER A 1 294 ? 111.897 155.671 118.232 1.00 29.89  ? 269 SER A CA  1 
ATOM   1566  C  C   . SER A 1 294 ? 111.046 156.265 117.123 1.00 38.45  ? 269 SER A C   1 
ATOM   1567  O  O   . SER A 1 294 ? 110.109 155.620 116.639 1.00 49.95  ? 269 SER A O   1 
ATOM   1568  C  CB  . SER A 1 294 ? 111.512 156.267 119.582 1.00 35.52  ? 269 SER A CB  1 
ATOM   1569  O  OG  . SER A 1 294 ? 112.077 155.526 120.646 1.00 48.76  ? 269 SER A OG  1 
ATOM   1570  N  N   . CYS A 1 295 ? 111.384 157.478 116.679 1.00 42.33  ? 270 CYS A N   1 
ATOM   1571  C  CA  . CYS A 1 295 ? 110.659 158.087 115.571 1.00 34.92  ? 270 CYS A CA  1 
ATOM   1572  C  C   . CYS A 1 295 ? 110.668 157.177 114.354 1.00 40.83  ? 270 CYS A C   1 
ATOM   1573  O  O   . CYS A 1 295 ? 109.641 157.018 113.684 1.00 51.06  ? 270 CYS A O   1 
ATOM   1574  C  CB  . CYS A 1 295 ? 111.261 159.446 115.229 1.00 30.06  ? 270 CYS A CB  1 
ATOM   1575  S  SG  . CYS A 1 295 ? 111.165 160.656 116.554 1.00 51.91  ? 270 CYS A SG  1 
ATOM   1576  N  N   . VAL A 1 296 ? 111.804 156.531 114.079 1.00 33.48  ? 271 VAL A N   1 
ATOM   1577  C  CA  . VAL A 1 296 ? 111.859 155.588 112.967 1.00 29.36  ? 271 VAL A CA  1 
ATOM   1578  C  C   . VAL A 1 296 ? 110.797 154.515 113.144 1.00 42.65  ? 271 VAL A C   1 
ATOM   1579  O  O   . VAL A 1 296 ? 109.973 154.277 112.253 1.00 55.21  ? 271 VAL A O   1 
ATOM   1580  C  CB  . VAL A 1 296 ? 113.260 154.967 112.851 1.00 20.79  ? 271 VAL A CB  1 
ATOM   1581  C  CG1 . VAL A 1 296 ? 113.286 153.959 111.732 1.00 20.95  ? 271 VAL A CG1 1 
ATOM   1582  C  CG2 . VAL A 1 296 ? 114.289 156.039 112.621 1.00 38.91  ? 271 VAL A CG2 1 
ATOM   1583  N  N   . ASN A 1 297 ? 110.753 153.900 114.323 1.00 30.42  ? 272 ASN A N   1 
ATOM   1584  C  CA  . ASN A 1 297 ? 109.787 152.836 114.536 1.00 24.64  ? 272 ASN A CA  1 
ATOM   1585  C  C   . ASN A 1 297 ? 108.364 153.355 114.622 1.00 39.58  ? 272 ASN A C   1 
ATOM   1586  O  O   . ASN A 1 297 ? 107.430 152.549 114.610 1.00 53.97  ? 272 ASN A O   1 
ATOM   1587  C  CB  . ASN A 1 297 ? 110.140 152.052 115.792 1.00 35.27  ? 272 ASN A CB  1 
ATOM   1588  C  CG  . ASN A 1 297 ? 110.962 150.828 115.490 1.00 47.81  ? 272 ASN A CG  1 
ATOM   1589  O  OD1 . ASN A 1 297 ? 110.431 149.729 115.363 1.00 54.53  ? 272 ASN A OD1 1 
ATOM   1590  N  ND2 . ASN A 1 297 ? 112.267 151.010 115.368 1.00 39.85  ? 272 ASN A ND2 1 
ATOM   1591  N  N   . LEU A 1 298 ? 108.171 154.669 114.713 1.00 31.94  ? 273 LEU A N   1 
ATOM   1592  C  CA  . LEU A 1 298 ? 106.837 155.234 114.600 1.00 29.55  ? 273 LEU A CA  1 
ATOM   1593  C  C   . LEU A 1 298 ? 106.529 155.717 113.194 1.00 33.81  ? 273 LEU A C   1 
ATOM   1594  O  O   . LEU A 1 298 ? 105.354 155.886 112.859 1.00 42.68  ? 273 LEU A O   1 
ATOM   1595  C  CB  . LEU A 1 298 ? 106.656 156.389 115.589 1.00 27.26  ? 273 LEU A CB  1 
ATOM   1596  C  CG  . LEU A 1 298 ? 106.825 156.027 117.064 1.00 25.22  ? 273 LEU A CG  1 
ATOM   1597  C  CD1 . LEU A 1 298 ? 106.899 157.269 117.915 1.00 32.03  ? 273 LEU A CD1 1 
ATOM   1598  C  CD2 . LEU A 1 298 ? 105.684 155.153 117.519 1.00 34.92  ? 273 LEU A CD2 1 
ATOM   1599  N  N   . LEU A 1 299 ? 107.552 155.940 112.367 1.00 35.61  ? 274 LEU A N   1 
ATOM   1600  C  CA  . LEU A 1 299 ? 107.317 156.261 110.968 1.00 31.83  ? 274 LEU A CA  1 
ATOM   1601  C  C   . LEU A 1 299 ? 107.046 155.019 110.137 1.00 37.56  ? 274 LEU A C   1 
ATOM   1602  O  O   . LEU A 1 299 ? 106.541 155.135 109.017 1.00 46.41  ? 274 LEU A O   1 
ATOM   1603  C  CB  . LEU A 1 299 ? 108.509 157.022 110.390 1.00 29.22  ? 274 LEU A CB  1 
ATOM   1604  C  CG  . LEU A 1 299 ? 108.692 158.454 110.887 1.00 30.36  ? 274 LEU A CG  1 
ATOM   1605  C  CD1 . LEU A 1 299 ? 109.690 159.192 110.027 1.00 30.26  ? 274 LEU A CD1 1 
ATOM   1606  C  CD2 . LEU A 1 299 ? 107.369 159.185 110.905 1.00 34.62  ? 274 LEU A CD2 1 
ATOM   1607  N  N   . ILE A 1 300 ? 107.386 153.840 110.654 1.00 39.61  ? 275 ILE A N   1 
ATOM   1608  C  CA  . ILE A 1 300 ? 107.027 152.596 109.986 1.00 32.46  ? 275 ILE A CA  1 
ATOM   1609  C  C   . ILE A 1 300 ? 105.531 152.342 110.104 1.00 43.07  ? 275 ILE A C   1 
ATOM   1610  O  O   . ILE A 1 300 ? 104.886 151.893 109.149 1.00 51.70  ? 275 ILE A O   1 
ATOM   1611  C  CB  . ILE A 1 300 ? 107.850 151.434 110.565 1.00 26.30  ? 275 ILE A CB  1 
ATOM   1612  C  CG1 . ILE A 1 300 ? 109.321 151.600 110.198 1.00 33.11  ? 275 ILE A CG1 1 
ATOM   1613  C  CG2 . ILE A 1 300 ? 107.326 150.107 110.074 1.00 31.99  ? 275 ILE A CG2 1 
ATOM   1614  C  CD1 . ILE A 1 300 ? 110.143 150.381 110.462 1.00 31.89  ? 275 ILE A CD1 1 
ATOM   1615  N  N   . LEU A 1 301 ? 104.954 152.631 111.268 1.00 37.55  ? 276 LEU A N   1 
ATOM   1616  C  CA  . LEU A 1 301 ? 103.555 152.322 111.527 1.00 36.69  ? 276 LEU A CA  1 
ATOM   1617  C  C   . LEU A 1 301 ? 102.601 153.418 111.070 1.00 44.74  ? 276 LEU A C   1 
ATOM   1618  O  O   . LEU A 1 301 ? 101.385 153.226 111.151 1.00 56.25  ? 276 LEU A O   1 
ATOM   1619  C  CB  . LEU A 1 301 ? 103.350 152.052 113.018 1.00 36.93  ? 276 LEU A CB  1 
ATOM   1620  C  CG  . LEU A 1 301 ? 104.437 151.223 113.701 1.00 38.25  ? 276 LEU A CG  1 
ATOM   1621  C  CD1 . LEU A 1 301 ? 104.129 151.060 115.172 1.00 39.71  ? 276 LEU A CD1 1 
ATOM   1622  C  CD2 . LEU A 1 301 ? 104.579 149.872 113.039 1.00 41.89  ? 276 LEU A CD2 1 
ATOM   1623  N  N   . SER A 1 302 ? 103.113 154.549 110.595 1.00 46.64  ? 277 SER A N   1 
ATOM   1624  C  CA  . SER A 1 302 ? 102.277 155.648 110.136 1.00 41.82  ? 277 SER A CA  1 
ATOM   1625  C  C   . SER A 1 302 ? 101.963 155.475 108.659 1.00 54.43  ? 277 SER A C   1 
ATOM   1626  O  O   . SER A 1 302 ? 102.874 155.368 107.834 1.00 60.48  ? 277 SER A O   1 
ATOM   1627  C  CB  . SER A 1 302 ? 102.975 156.988 110.360 1.00 50.68  ? 277 SER A CB  1 
ATOM   1628  O  OG  . SER A 1 302 ? 102.618 157.556 111.604 1.00 55.72  ? 277 SER A OG  1 
ATOM   1629  N  N   . HIS A 1 303 ? 100.673 155.462 108.325 1.00 74.00  ? 278 HIS A N   1 
ATOM   1630  C  CA  . HIS A 1 303 ? 100.272 155.384 106.927 1.00 73.33  ? 278 HIS A CA  1 
ATOM   1631  C  C   . HIS A 1 303 ? 100.607 156.650 106.153 1.00 74.56  ? 278 HIS A C   1 
ATOM   1632  O  O   . HIS A 1 303 ? 100.536 156.636 104.920 1.00 73.57  ? 278 HIS A O   1 
ATOM   1633  C  CB  . HIS A 1 303 ? 98.777  155.093 106.822 1.00 68.01  ? 278 HIS A CB  1 
ATOM   1634  C  CG  . HIS A 1 303 ? 97.922  156.040 107.601 1.00 74.90  ? 278 HIS A CG  1 
ATOM   1635  N  ND1 . HIS A 1 303 ? 97.200  157.052 107.006 1.00 76.35  ? 278 HIS A ND1 1 
ATOM   1636  C  CD2 . HIS A 1 303 ? 97.673  156.130 108.929 1.00 75.70  ? 278 HIS A CD2 1 
ATOM   1637  C  CE1 . HIS A 1 303 ? 96.543  157.724 107.934 1.00 80.27  ? 278 HIS A CE1 1 
ATOM   1638  N  NE2 . HIS A 1 303 ? 96.814  157.186 109.110 1.00 78.31  ? 278 HIS A NE2 1 
ATOM   1639  N  N   . HIS A 1 304 ? 100.961 157.738 106.841 1.00 72.18  ? 279 HIS A N   1 
ATOM   1640  C  CA  . HIS A 1 304 ? 101.401 158.943 106.147 1.00 67.81  ? 279 HIS A CA  1 
ATOM   1641  C  C   . HIS A 1 304 ? 102.670 158.679 105.351 1.00 68.77  ? 279 HIS A C   1 
ATOM   1642  O  O   . HIS A 1 304 ? 102.814 159.155 104.220 1.00 75.40  ? 279 HIS A O   1 
ATOM   1643  C  CB  . HIS A 1 304 ? 101.629 160.072 107.149 1.00 65.24  ? 279 HIS A CB  1 
ATOM   1644  C  CG  . HIS A 1 304 ? 100.370 160.619 107.741 1.00 68.67  ? 279 HIS A CG  1 
ATOM   1645  N  ND1 . HIS A 1 304 ? 100.254 161.925 108.162 1.00 74.91  ? 279 HIS A ND1 1 
ATOM   1646  C  CD2 . HIS A 1 304 ? 99.171  160.038 107.980 1.00 69.41  ? 279 HIS A CD2 1 
ATOM   1647  C  CE1 . HIS A 1 304 ? 99.038  162.126 108.636 1.00 72.89  ? 279 HIS A CE1 1 
ATOM   1648  N  NE2 . HIS A 1 304 ? 98.361  160.997 108.538 1.00 72.41  ? 279 HIS A NE2 1 
ATOM   1649  N  N   . SER A 1 305 ? 103.603 157.923 105.928 1.00 60.07  ? 280 SER A N   1 
ATOM   1650  C  CA  . SER A 1 305 ? 104.855 157.571 105.263 1.00 63.67  ? 280 SER A CA  1 
ATOM   1651  C  C   . SER A 1 305 ? 104.701 156.179 104.661 1.00 62.49  ? 280 SER A C   1 
ATOM   1652  O  O   . SER A 1 305 ? 105.187 155.182 105.192 1.00 59.50  ? 280 SER A O   1 
ATOM   1653  C  CB  . SER A 1 305 ? 106.014 157.631 106.245 1.00 59.47  ? 280 SER A CB  1 
ATOM   1654  O  OG  . SER A 1 305 ? 106.260 156.351 106.794 1.00 57.27  ? 280 SER A OG  1 
ATOM   1655  N  N   . GLU A 1 306 ? 104.012 156.119 103.522 1.00 74.77  ? 281 GLU A N   1 
ATOM   1656  C  CA  . GLU A 1 306 ? 103.756 154.842 102.865 1.00 77.44  ? 281 GLU A CA  1 
ATOM   1657  C  C   . GLU A 1 306 ? 104.852 154.499 101.862 1.00 78.65  ? 281 GLU A C   1 
ATOM   1658  O  O   . GLU A 1 306 ? 105.547 153.490 102.011 1.00 78.78  ? 281 GLU A O   1 
ATOM   1659  C  CB  . GLU A 1 306 ? 102.389 154.869 102.174 1.00 77.85  ? 281 GLU A CB  1 
ATOM   1660  C  CG  . GLU A 1 306 ? 102.123 153.659 101.301 1.00 77.36  ? 281 GLU A CG  1 
ATOM   1661  C  CD  . GLU A 1 306 ? 100.649 153.323 101.196 1.00 82.31  ? 281 GLU A CD  1 
ATOM   1662  O  OE1 . GLU A 1 306 ? 99.829  154.037 101.810 1.00 82.45  ? 281 GLU A OE1 1 
ATOM   1663  O  OE2 . GLU A 1 306 ? 100.310 152.343 100.500 1.00 83.43  ? 281 GLU A OE2 1 
ATOM   1664  N  N   . GLY A 1 307 ? 105.022 155.334 100.844 1.00 70.41  ? 282 GLY A N   1 
ATOM   1665  C  CA  . GLY A 1 307 ? 106.015 155.077 99.823  1.00 66.99  ? 282 GLY A CA  1 
ATOM   1666  C  C   . GLY A 1 307 ? 107.164 156.058 99.866  1.00 69.95  ? 282 GLY A C   1 
ATOM   1667  O  O   . GLY A 1 307 ? 107.911 156.191 98.893  1.00 75.31  ? 282 GLY A O   1 
ATOM   1668  N  N   . LEU A 1 308 ? 107.311 156.761 100.989 1.00 59.68  ? 283 LEU A N   1 
ATOM   1669  C  CA  . LEU A 1 308 ? 108.356 157.773 101.085 1.00 62.12  ? 283 LEU A CA  1 
ATOM   1670  C  C   . LEU A 1 308 ? 109.732 157.141 101.250 1.00 58.88  ? 283 LEU A C   1 
ATOM   1671  O  O   . LEU A 1 308 ? 110.703 157.600 100.640 1.00 65.05  ? 283 LEU A O   1 
ATOM   1672  C  CB  . LEU A 1 308 ? 108.056 158.744 102.227 1.00 56.34  ? 283 LEU A CB  1 
ATOM   1673  C  CG  . LEU A 1 308 ? 107.043 159.881 102.014 1.00 57.26  ? 283 LEU A CG  1 
ATOM   1674  C  CD1 . LEU A 1 308 ? 105.882 159.508 101.112 1.00 60.94  ? 283 LEU A CD1 1 
ATOM   1675  C  CD2 . LEU A 1 308 ? 106.518 160.375 103.346 1.00 61.67  ? 283 LEU A CD2 1 
ATOM   1676  N  N   . PHE A 1 309 ? 109.844 156.088 102.056 1.00 45.31  ? 284 PHE A N   1 
ATOM   1677  C  CA  . PHE A 1 309 ? 111.109 155.389 102.227 1.00 46.87  ? 284 PHE A CA  1 
ATOM   1678  C  C   . PHE A 1 309 ? 110.892 153.892 102.063 1.00 50.29  ? 284 PHE A C   1 
ATOM   1679  O  O   . PHE A 1 309 ? 109.764 153.420 101.910 1.00 56.16  ? 284 PHE A O   1 
ATOM   1680  C  CB  . PHE A 1 309 ? 111.755 155.702 103.582 1.00 45.54  ? 284 PHE A CB  1 
ATOM   1681  C  CG  . PHE A 1 309 ? 110.961 155.237 104.764 1.00 41.42  ? 284 PHE A CG  1 
ATOM   1682  C  CD1 . PHE A 1 309 ? 109.946 156.011 105.281 1.00 47.97  ? 284 PHE A CD1 1 
ATOM   1683  C  CD2 . PHE A 1 309 ? 111.255 154.040 105.379 1.00 35.90  ? 284 PHE A CD2 1 
ATOM   1684  C  CE1 . PHE A 1 309 ? 109.230 155.587 106.373 1.00 46.09  ? 284 PHE A CE1 1 
ATOM   1685  C  CE2 . PHE A 1 309 ? 110.543 153.617 106.471 1.00 41.10  ? 284 PHE A CE2 1 
ATOM   1686  C  CZ  . PHE A 1 309 ? 109.531 154.391 106.967 1.00 41.43  ? 284 PHE A CZ  1 
ATOM   1687  N  N   . GLN A 1 310 ? 111.994 153.141 102.086 1.00 47.65  ? 285 GLN A N   1 
ATOM   1688  C  CA  . GLN A 1 310 ? 111.932 151.714 101.797 1.00 40.40  ? 285 GLN A CA  1 
ATOM   1689  C  C   . GLN A 1 310 ? 112.638 150.858 102.840 1.00 44.66  ? 285 GLN A C   1 
ATOM   1690  O  O   . GLN A 1 310 ? 112.292 149.687 103.012 1.00 53.42  ? 285 GLN A O   1 
ATOM   1691  C  CB  . GLN A 1 310 ? 112.530 151.429 100.421 1.00 39.22  ? 285 GLN A CB  1 
ATOM   1692  C  CG  . GLN A 1 310 ? 111.658 151.872 99.272  1.00 48.76  ? 285 GLN A CG  1 
ATOM   1693  C  CD  . GLN A 1 310 ? 112.087 153.202 98.713  1.00 58.28  ? 285 GLN A CD  1 
ATOM   1694  O  OE1 . GLN A 1 310 ? 113.153 153.710 99.052  1.00 58.56  ? 285 GLN A OE1 1 
ATOM   1695  N  NE2 . GLN A 1 310 ? 111.261 153.778 97.850  1.00 56.46  ? 285 GLN A NE2 1 
ATOM   1696  N  N   . LYS A 1 311 ? 113.629 151.413 103.529 1.00 44.53  ? 286 LYS A N   1 
ATOM   1697  C  CA  . LYS A 1 311 ? 114.395 150.672 104.519 1.00 37.95  ? 286 LYS A CA  1 
ATOM   1698  C  C   . LYS A 1 311 ? 114.427 151.454 105.822 1.00 42.47  ? 286 LYS A C   1 
ATOM   1699  O  O   . LYS A 1 311 ? 113.937 152.580 105.906 1.00 57.46  ? 286 LYS A O   1 
ATOM   1700  C  CB  . LYS A 1 311 ? 115.819 150.393 104.028 1.00 35.55  ? 286 LYS A CB  1 
ATOM   1701  C  CG  . LYS A 1 311 ? 115.881 149.721 102.673 1.00 45.56  ? 286 LYS A CG  1 
ATOM   1702  C  CD  . LYS A 1 311 ? 117.223 149.940 102.012 1.00 45.14  ? 286 LYS A CD  1 
ATOM   1703  C  CE  . LYS A 1 311 ? 117.222 149.424 100.594 1.00 44.56  ? 286 LYS A CE  1 
ATOM   1704  N  NZ  . LYS A 1 311 ? 116.881 147.983 100.555 1.00 44.47  ? 286 LYS A NZ  1 
ATOM   1705  N  N   . ALA A 1 312 ? 115.007 150.846 106.851 1.00 30.58  ? 287 ALA A N   1 
ATOM   1706  C  CA  . ALA A 1 312 ? 115.093 151.497 108.148 1.00 23.05  ? 287 ALA A CA  1 
ATOM   1707  C  C   . ALA A 1 312 ? 116.242 150.889 108.932 1.00 25.44  ? 287 ALA A C   1 
ATOM   1708  O  O   . ALA A 1 312 ? 116.458 149.680 108.879 1.00 42.65  ? 287 ALA A O   1 
ATOM   1709  C  CB  . ALA A 1 312 ? 113.787 151.354 108.931 1.00 32.25  ? 287 ALA A CB  1 
ATOM   1710  N  N   . ILE A 1 313 ? 116.971 151.733 109.654 1.00 20.84  ? 288 ILE A N   1 
ATOM   1711  C  CA  . ILE A 1 313 ? 118.061 151.305 110.525 1.00 20.73  ? 288 ILE A CA  1 
ATOM   1712  C  C   . ILE A 1 313 ? 117.790 151.932 111.885 1.00 34.57  ? 288 ILE A C   1 
ATOM   1713  O  O   . ILE A 1 313 ? 118.062 153.118 112.091 1.00 46.00  ? 288 ILE A O   1 
ATOM   1714  C  CB  . ILE A 1 313 ? 119.438 151.718 109.998 1.00 21.93  ? 288 ILE A CB  1 
ATOM   1715  C  CG1 . ILE A 1 313 ? 119.664 151.196 108.582 1.00 35.63  ? 288 ILE A CG1 1 
ATOM   1716  C  CG2 . ILE A 1 313 ? 120.525 151.226 110.919 1.00 26.25  ? 288 ILE A CG2 1 
ATOM   1717  C  CD1 . ILE A 1 313 ? 120.902 151.754 107.929 1.00 30.59  ? 288 ILE A CD1 1 
ATOM   1718  N  N   . ALA A 1 314 ? 117.258 151.147 112.815 1.00 31.55  ? 289 ALA A N   1 
ATOM   1719  C  CA  . ALA A 1 314 ? 116.940 151.625 114.154 1.00 27.34  ? 289 ALA A CA  1 
ATOM   1720  C  C   . ALA A 1 314 ? 117.979 151.079 115.122 1.00 26.12  ? 289 ALA A C   1 
ATOM   1721  O  O   . ALA A 1 314 ? 117.983 149.884 115.420 1.00 49.26  ? 289 ALA A O   1 
ATOM   1722  C  CB  . ALA A 1 314 ? 115.535 151.196 114.563 1.00 25.48  ? 289 ALA A CB  1 
ATOM   1723  N  N   . GLN A 1 315 ? 118.850 151.949 115.619 1.00 24.16  ? 290 GLN A N   1 
ATOM   1724  C  CA  . GLN A 1 315 ? 119.921 151.554 116.523 1.00 30.99  ? 290 GLN A CA  1 
ATOM   1725  C  C   . GLN A 1 315 ? 119.666 152.150 117.900 1.00 39.49  ? 290 GLN A C   1 
ATOM   1726  O  O   . GLN A 1 315 ? 119.524 153.368 118.034 1.00 47.31  ? 290 GLN A O   1 
ATOM   1727  C  CB  . GLN A 1 315 ? 121.282 151.996 115.988 1.00 33.89  ? 290 GLN A CB  1 
ATOM   1728  C  CG  . GLN A 1 315 ? 121.336 153.419 115.483 1.00 38.06  ? 290 GLN A CG  1 
ATOM   1729  C  CD  . GLN A 1 315 ? 122.416 153.626 114.449 1.00 36.88  ? 290 GLN A CD  1 
ATOM   1730  O  OE1 . GLN A 1 315 ? 122.857 152.682 113.803 1.00 36.25  ? 290 GLN A OE1 1 
ATOM   1731  N  NE2 . GLN A 1 315 ? 122.848 154.866 114.285 1.00 35.44  ? 290 GLN A NE2 1 
ATOM   1732  N  N   . SER A 1 316 ? 119.609 151.287 118.916 1.00 37.20  ? 291 SER A N   1 
ATOM   1733  C  CA  . SER A 1 316 ? 119.430 151.694 120.309 1.00 35.89  ? 291 SER A CA  1 
ATOM   1734  C  C   . SER A 1 316 ? 118.159 152.524 120.484 1.00 36.70  ? 291 SER A C   1 
ATOM   1735  O  O   . SER A 1 316 ? 118.192 153.697 120.856 1.00 50.34  ? 291 SER A O   1 
ATOM   1736  C  CB  . SER A 1 316 ? 120.656 152.454 120.817 1.00 44.13  ? 291 SER A CB  1 
ATOM   1737  O  OG  . SER A 1 316 ? 121.847 151.795 120.439 1.00 50.84  ? 291 SER A OG  1 
ATOM   1738  N  N   . GLY A 1 317 ? 117.027 151.892 120.205 1.00 25.98  ? 292 GLY A N   1 
ATOM   1739  C  CA  . GLY A 1 317 ? 115.757 152.573 120.332 1.00 44.67  ? 292 GLY A CA  1 
ATOM   1740  C  C   . GLY A 1 317 ? 114.607 151.796 119.730 1.00 54.90  ? 292 GLY A C   1 
ATOM   1741  O  O   . GLY A 1 317 ? 114.783 151.078 118.743 1.00 62.79  ? 292 GLY A O   1 
ATOM   1742  N  N   . THR A 1 318 ? 113.422 151.933 120.319 1.00 45.03  ? 293 THR A N   1 
ATOM   1743  C  CA  . THR A 1 318 ? 112.227 151.253 119.849 1.00 37.58  ? 293 THR A CA  1 
ATOM   1744  C  C   . THR A 1 318 ? 111.021 152.147 120.091 1.00 46.25  ? 293 THR A C   1 
ATOM   1745  O  O   . THR A 1 318 ? 111.132 153.236 120.661 1.00 50.72  ? 293 THR A O   1 
ATOM   1746  C  CB  . THR A 1 318 ? 112.047 149.908 120.547 1.00 43.30  ? 293 THR A CB  1 
ATOM   1747  O  OG1 . THR A 1 318 ? 112.431 150.035 121.920 1.00 50.37  ? 293 THR A OG1 1 
ATOM   1748  C  CG2 . THR A 1 318 ? 112.892 148.851 119.884 1.00 46.12  ? 293 THR A CG2 1 
ATOM   1749  N  N   . ALA A 1 319 ? 109.858 151.680 119.648 1.00 41.45  ? 294 ALA A N   1 
ATOM   1750  C  CA  . ALA A 1 319 ? 108.606 152.396 119.829 1.00 41.80  ? 294 ALA A CA  1 
ATOM   1751  C  C   . ALA A 1 319 ? 107.781 151.853 120.984 1.00 45.02  ? 294 ALA A C   1 
ATOM   1752  O  O   . ALA A 1 319 ? 106.654 152.309 121.192 1.00 50.93  ? 294 ALA A O   1 
ATOM   1753  C  CB  . ALA A 1 319 ? 107.784 152.350 118.544 1.00 45.39  ? 294 ALA A CB  1 
ATOM   1754  N  N   . ILE A 1 320 ? 108.310 150.891 121.738 1.00 42.00  ? 295 ILE A N   1 
ATOM   1755  C  CA  . ILE A 1 320 ? 107.562 150.231 122.799 1.00 43.63  ? 295 ILE A CA  1 
ATOM   1756  C  C   . ILE A 1 320 ? 108.215 150.372 124.164 1.00 49.99  ? 295 ILE A C   1 
ATOM   1757  O  O   . ILE A 1 320 ? 107.718 149.792 125.132 1.00 54.86  ? 295 ILE A O   1 
ATOM   1758  C  CB  . ILE A 1 320 ? 107.329 148.743 122.472 1.00 45.45  ? 295 ILE A CB  1 
ATOM   1759  C  CG1 . ILE A 1 320 ? 108.645 147.978 122.494 1.00 43.13  ? 295 ILE A CG1 1 
ATOM   1760  C  CG2 . ILE A 1 320 ? 106.684 148.598 121.118 1.00 45.07  ? 295 ILE A CG2 1 
ATOM   1761  C  CD1 . ILE A 1 320 ? 108.512 146.557 122.024 1.00 46.74  ? 295 ILE A CD1 1 
ATOM   1762  N  N   . SER A 1 321 ? 109.305 151.126 124.279 1.00 46.04  ? 296 SER A N   1 
ATOM   1763  C  CA  . SER A 1 321 ? 109.920 151.351 125.578 1.00 42.45  ? 296 SER A CA  1 
ATOM   1764  C  C   . SER A 1 321 ? 109.039 152.272 126.417 1.00 50.04  ? 296 SER A C   1 
ATOM   1765  O  O   . SER A 1 321 ? 108.013 152.784 125.964 1.00 54.18  ? 296 SER A O   1 
ATOM   1766  C  CB  . SER A 1 321 ? 111.320 151.933 125.415 1.00 43.13  ? 296 SER A CB  1 
ATOM   1767  O  OG  . SER A 1 321 ? 112.056 151.235 124.429 1.00 50.51  ? 296 SER A OG  1 
ATOM   1768  N  N   . SER A 1 322 ? 109.448 152.487 127.669 1.00 46.69  ? 297 SER A N   1 
ATOM   1769  C  CA  . SER A 1 322 ? 108.645 153.308 128.568 1.00 43.95  ? 297 SER A CA  1 
ATOM   1770  C  C   . SER A 1 322 ? 108.672 154.778 128.174 1.00 42.35  ? 297 SER A C   1 
ATOM   1771  O  O   . SER A 1 322 ? 107.712 155.505 128.442 1.00 47.72  ? 297 SER A O   1 
ATOM   1772  C  CB  . SER A 1 322 ? 109.126 153.140 130.006 1.00 37.65  ? 297 SER A CB  1 
ATOM   1773  O  OG  . SER A 1 322 ? 110.351 153.813 130.214 1.00 35.43  ? 297 SER A OG  1 
ATOM   1774  N  N   . TRP A 1 323 ? 109.751 155.232 127.540 1.00 39.23  ? 298 TRP A N   1 
ATOM   1775  C  CA  . TRP A 1 323 ? 109.913 156.628 127.158 1.00 42.19  ? 298 TRP A CA  1 
ATOM   1776  C  C   . TRP A 1 323 ? 109.798 156.833 125.652 1.00 44.04  ? 298 TRP A C   1 
ATOM   1777  O  O   . TRP A 1 323 ? 110.396 157.759 125.104 1.00 57.91  ? 298 TRP A O   1 
ATOM   1778  C  CB  . TRP A 1 323 ? 111.251 157.165 127.654 1.00 41.38  ? 298 TRP A CB  1 
ATOM   1779  C  CG  . TRP A 1 323 ? 112.408 156.270 127.357 1.00 40.99  ? 298 TRP A CG  1 
ATOM   1780  C  CD1 . TRP A 1 323 ? 112.617 155.546 126.224 1.00 45.08  ? 298 TRP A CD1 1 
ATOM   1781  C  CD2 . TRP A 1 323 ? 113.521 156.003 128.211 1.00 38.79  ? 298 TRP A CD2 1 
ATOM   1782  N  NE1 . TRP A 1 323 ? 113.790 154.844 126.320 1.00 34.49  ? 298 TRP A NE1 1 
ATOM   1783  C  CE2 . TRP A 1 323 ? 114.363 155.110 127.533 1.00 32.07  ? 298 TRP A CE2 1 
ATOM   1784  C  CE3 . TRP A 1 323 ? 113.886 156.435 129.487 1.00 42.98  ? 298 TRP A CE3 1 
ATOM   1785  C  CZ2 . TRP A 1 323 ? 115.541 154.644 128.083 1.00 38.14  ? 298 TRP A CZ2 1 
ATOM   1786  C  CZ3 . TRP A 1 323 ? 115.055 155.970 130.028 1.00 42.22  ? 298 TRP A CZ3 1 
ATOM   1787  C  CH2 . TRP A 1 323 ? 115.871 155.085 129.329 1.00 40.10  ? 298 TRP A CH2 1 
ATOM   1788  N  N   . SER A 1 324 ? 109.048 155.975 124.968 1.00 35.64  ? 299 SER A N   1 
ATOM   1789  C  CA  . SER A 1 324 ? 108.912 156.109 123.525 1.00 33.45  ? 299 SER A CA  1 
ATOM   1790  C  C   . SER A 1 324 ? 107.751 157.010 123.136 1.00 39.06  ? 299 SER A C   1 
ATOM   1791  O  O   . SER A 1 324 ? 107.884 157.820 122.215 1.00 44.19  ? 299 SER A O   1 
ATOM   1792  C  CB  . SER A 1 324 ? 108.730 154.738 122.883 1.00 42.57  ? 299 SER A CB  1 
ATOM   1793  O  OG  . SER A 1 324 ? 107.355 154.456 122.708 1.00 57.72  ? 299 SER A OG  1 
ATOM   1794  N  N   . VAL A 1 325 ? 106.614 156.889 123.819 1.00 43.42  ? 300 VAL A N   1 
ATOM   1795  C  CA  . VAL A 1 325 ? 105.436 157.698 123.545 1.00 40.41  ? 300 VAL A CA  1 
ATOM   1796  C  C   . VAL A 1 325 ? 104.923 158.287 124.852 1.00 44.15  ? 300 VAL A C   1 
ATOM   1797  O  O   . VAL A 1 325 ? 105.408 157.977 125.938 1.00 50.88  ? 300 VAL A O   1 
ATOM   1798  C  CB  . VAL A 1 325 ? 104.322 156.897 122.843 1.00 29.48  ? 300 VAL A CB  1 
ATOM   1799  C  CG1 . VAL A 1 325 ? 104.659 156.695 121.389 1.00 35.74  ? 300 VAL A CG1 1 
ATOM   1800  C  CG2 . VAL A 1 325 ? 104.142 155.563 123.519 1.00 37.87  ? 300 VAL A CG2 1 
ATOM   1801  N  N   . ASN A 1 326 ? 103.925 159.154 124.727 1.00 56.29  ? 301 ASN A N   1 
ATOM   1802  C  CA  . ASN A 1 326 ? 103.319 159.847 125.857 1.00 53.68  ? 301 ASN A CA  1 
ATOM   1803  C  C   . ASN A 1 326 ? 101.852 159.448 125.920 1.00 64.41  ? 301 ASN A C   1 
ATOM   1804  O  O   . ASN A 1 326 ? 101.059 159.853 125.065 1.00 71.04  ? 301 ASN A O   1 
ATOM   1805  C  CB  . ASN A 1 326 ? 103.471 161.357 125.709 1.00 54.44  ? 301 ASN A CB  1 
ATOM   1806  C  CG  . ASN A 1 326 ? 103.078 162.105 126.955 1.00 58.96  ? 301 ASN A CG  1 
ATOM   1807  O  OD1 . ASN A 1 326 ? 102.919 161.516 128.021 1.00 60.91  ? 301 ASN A OD1 1 
ATOM   1808  N  ND2 . ASN A 1 326 ? 102.919 163.415 126.830 1.00 59.47  ? 301 ASN A ND2 1 
ATOM   1809  N  N   . TYR A 1 327 ? 101.491 158.650 126.922 1.00 65.11  ? 302 TYR A N   1 
ATOM   1810  C  CA  . TYR A 1 327 ? 100.123 158.174 127.061 1.00 60.96  ? 302 TYR A CA  1 
ATOM   1811  C  C   . TYR A 1 327 ? 99.246  159.099 127.889 1.00 65.26  ? 302 TYR A C   1 
ATOM   1812  O  O   . TYR A 1 327 ? 98.032  158.882 127.950 1.00 75.12  ? 302 TYR A O   1 
ATOM   1813  C  CB  . TYR A 1 327 ? 100.109 156.780 127.689 1.00 64.56  ? 302 TYR A CB  1 
ATOM   1814  C  CG  . TYR A 1 327 ? 100.701 155.708 126.810 1.00 65.10  ? 302 TYR A CG  1 
ATOM   1815  C  CD1 . TYR A 1 327 ? 100.043 155.275 125.671 1.00 65.27  ? 302 TYR A CD1 1 
ATOM   1816  C  CD2 . TYR A 1 327 ? 101.915 155.126 127.126 1.00 66.98  ? 302 TYR A CD2 1 
ATOM   1817  C  CE1 . TYR A 1 327 ? 100.580 154.297 124.871 1.00 66.99  ? 302 TYR A CE1 1 
ATOM   1818  C  CE2 . TYR A 1 327 ? 102.459 154.148 126.333 1.00 69.59  ? 302 TYR A CE2 1 
ATOM   1819  C  CZ  . TYR A 1 327 ? 101.789 153.736 125.207 1.00 74.26  ? 302 TYR A CZ  1 
ATOM   1820  O  OH  . TYR A 1 327 ? 102.341 152.756 124.417 1.00 77.76  ? 302 TYR A OH  1 
ATOM   1821  N  N   . GLN A 1 328 ? 99.820  160.114 128.527 1.00 61.47  ? 303 GLN A N   1 
ATOM   1822  C  CA  . GLN A 1 328 ? 99.069  161.086 129.319 1.00 63.40  ? 303 GLN A CA  1 
ATOM   1823  C  C   . GLN A 1 328 ? 99.487  162.487 128.899 1.00 63.22  ? 303 GLN A C   1 
ATOM   1824  O  O   . GLN A 1 328 ? 100.172 163.197 129.643 1.00 64.28  ? 303 GLN A O   1 
ATOM   1825  C  CB  . GLN A 1 328 ? 99.296  160.866 130.814 1.00 64.50  ? 303 GLN A CB  1 
ATOM   1826  C  CG  . GLN A 1 328 ? 98.788  159.530 131.318 1.00 65.99  ? 303 GLN A CG  1 
ATOM   1827  C  CD  . GLN A 1 328 ? 99.170  159.264 132.758 1.00 70.62  ? 303 GLN A CD  1 
ATOM   1828  O  OE1 . GLN A 1 328 ? 99.894  160.045 133.375 1.00 67.60  ? 303 GLN A OE1 1 
ATOM   1829  N  NE2 . GLN A 1 328 ? 98.682  158.157 133.303 1.00 69.91  ? 303 GLN A NE2 1 
ATOM   1830  N  N   . PRO A 1 329 ? 99.092  162.917 127.704 1.00 67.59  ? 304 PRO A N   1 
ATOM   1831  C  CA  . PRO A 1 329 ? 99.542  164.223 127.212 1.00 70.24  ? 304 PRO A CA  1 
ATOM   1832  C  C   . PRO A 1 329 ? 98.778  165.378 127.836 1.00 73.18  ? 304 PRO A C   1 
ATOM   1833  O  O   . PRO A 1 329 ? 99.328  166.471 128.015 1.00 71.22  ? 304 PRO A O   1 
ATOM   1834  C  CB  . PRO A 1 329 ? 99.286  164.127 125.706 1.00 65.44  ? 304 PRO A CB  1 
ATOM   1835  C  CG  . PRO A 1 329 ? 98.124  163.205 125.594 1.00 67.57  ? 304 PRO A CG  1 
ATOM   1836  C  CD  . PRO A 1 329 ? 98.206  162.238 126.742 1.00 65.93  ? 304 PRO A CD  1 
ATOM   1837  N  N   . LEU A 1 330 ? 97.507  165.142 128.173 1.00 79.79  ? 305 LEU A N   1 
ATOM   1838  C  CA  . LEU A 1 330 ? 96.673  166.213 128.707 1.00 77.07  ? 305 LEU A CA  1 
ATOM   1839  C  C   . LEU A 1 330 ? 97.196  166.706 130.048 1.00 78.36  ? 305 LEU A C   1 
ATOM   1840  O  O   . LEU A 1 330 ? 97.180  167.911 130.321 1.00 82.54  ? 305 LEU A O   1 
ATOM   1841  C  CB  . LEU A 1 330 ? 95.227  165.738 128.842 1.00 75.80  ? 305 LEU A CB  1 
ATOM   1842  C  CG  . LEU A 1 330 ? 94.216  166.781 129.332 1.00 77.26  ? 305 LEU A CG  1 
ATOM   1843  C  CD1 . LEU A 1 330 ? 94.421  168.119 128.637 1.00 76.47  ? 305 LEU A CD1 1 
ATOM   1844  C  CD2 . LEU A 1 330 ? 92.789  166.293 129.145 1.00 78.77  ? 305 LEU A CD2 1 
ATOM   1845  N  N   . LYS A 1 331 ? 97.663  165.791 130.899 1.00 75.64  ? 306 LYS A N   1 
ATOM   1846  C  CA  . LYS A 1 331 ? 98.136  166.183 132.222 1.00 77.33  ? 306 LYS A CA  1 
ATOM   1847  C  C   . LYS A 1 331 ? 99.299  167.161 132.124 1.00 75.47  ? 306 LYS A C   1 
ATOM   1848  O  O   . LYS A 1 331 ? 99.275  168.241 132.727 1.00 77.94  ? 306 LYS A O   1 
ATOM   1849  C  CB  . LYS A 1 331 ? 98.541  164.941 133.014 1.00 75.79  ? 306 LYS A CB  1 
ATOM   1850  C  CG  . LYS A 1 331 ? 99.127  165.235 134.376 1.00 74.68  ? 306 LYS A CG  1 
ATOM   1851  C  CD  . LYS A 1 331 ? 99.137  163.991 135.244 1.00 76.12  ? 306 LYS A CD  1 
ATOM   1852  C  CE  . LYS A 1 331 ? 100.497 163.318 135.228 1.00 78.45  ? 306 LYS A CE  1 
ATOM   1853  N  NZ  . LYS A 1 331 ? 101.525 164.130 135.933 1.00 79.77  ? 306 LYS A NZ  1 
ATOM   1854  N  N   . TYR A 1 332 ? 100.322 166.810 131.346 1.00 68.72  ? 307 TYR A N   1 
ATOM   1855  C  CA  . TYR A 1 332 ? 101.490 167.675 131.233 1.00 67.28  ? 307 TYR A CA  1 
ATOM   1856  C  C   . TYR A 1 332 ? 101.183 168.930 130.431 1.00 68.80  ? 307 TYR A C   1 
ATOM   1857  O  O   . TYR A 1 332 ? 101.744 169.994 130.715 1.00 74.28  ? 307 TYR A O   1 
ATOM   1858  C  CB  . TYR A 1 332 ? 102.651 166.904 130.616 1.00 68.48  ? 307 TYR A CB  1 
ATOM   1859  C  CG  . TYR A 1 332 ? 103.098 165.742 131.466 1.00 68.52  ? 307 TYR A CG  1 
ATOM   1860  C  CD1 . TYR A 1 332 ? 102.485 164.504 131.359 1.00 66.58  ? 307 TYR A CD1 1 
ATOM   1861  C  CD2 . TYR A 1 332 ? 104.119 165.887 132.387 1.00 71.38  ? 307 TYR A CD2 1 
ATOM   1862  C  CE1 . TYR A 1 332 ? 102.884 163.443 132.139 1.00 68.84  ? 307 TYR A CE1 1 
ATOM   1863  C  CE2 . TYR A 1 332 ? 104.525 164.831 133.172 1.00 71.20  ? 307 TYR A CE2 1 
ATOM   1864  C  CZ  . TYR A 1 332 ? 103.905 163.611 133.044 1.00 72.68  ? 307 TYR A CZ  1 
ATOM   1865  O  OH  . TYR A 1 332 ? 104.308 162.553 133.824 1.00 76.42  ? 307 TYR A OH  1 
ATOM   1866  N  N   . THR A 1 333 ? 100.294 168.836 129.440 1.00 79.91  ? 308 THR A N   1 
ATOM   1867  C  CA  . THR A 1 333 ? 99.878  170.035 128.723 1.00 81.62  ? 308 THR A CA  1 
ATOM   1868  C  C   . THR A 1 333 ? 99.221  171.030 129.667 1.00 81.82  ? 308 THR A C   1 
ATOM   1869  O  O   . THR A 1 333 ? 99.526  172.227 129.632 1.00 82.48  ? 308 THR A O   1 
ATOM   1870  C  CB  . THR A 1 333 ? 98.922  169.669 127.590 1.00 80.62  ? 308 THR A CB  1 
ATOM   1871  O  OG1 . THR A 1 333 ? 99.638  168.970 126.566 1.00 85.46  ? 308 THR A OG1 1 
ATOM   1872  C  CG2 . THR A 1 333 ? 98.303  170.917 126.996 1.00 76.27  ? 308 THR A CG2 1 
ATOM   1873  N  N   . ARG A 1 334 ? 98.327  170.549 130.535 1.00 91.32  ? 309 ARG A N   1 
ATOM   1874  C  CA  . ARG A 1 334 ? 97.670  171.431 131.492 1.00 87.70  ? 309 ARG A CA  1 
ATOM   1875  C  C   . ARG A 1 334 ? 98.658  171.970 132.515 1.00 87.66  ? 309 ARG A C   1 
ATOM   1876  O  O   . ARG A 1 334 ? 98.552  173.127 132.933 1.00 93.35  ? 309 ARG A O   1 
ATOM   1877  C  CB  . ARG A 1 334 ? 96.526  170.695 132.184 1.00 88.01  ? 309 ARG A CB  1 
ATOM   1878  C  CG  . ARG A 1 334 ? 95.311  170.505 131.302 1.00 87.13  ? 309 ARG A CG  1 
ATOM   1879  C  CD  . ARG A 1 334 ? 94.060  170.275 132.126 1.00 90.81  ? 309 ARG A CD  1 
ATOM   1880  N  NE  . ARG A 1 334 ? 92.854  170.439 131.325 1.00 94.19  ? 309 ARG A NE  1 
ATOM   1881  C  CZ  . ARG A 1 334 ? 92.292  171.608 131.051 1.00 95.18  ? 309 ARG A CZ  1 
ATOM   1882  N  NH1 . ARG A 1 334 ? 92.799  172.742 131.504 1.00 92.15  ? 309 ARG A NH1 1 
ATOM   1883  N  NH2 . ARG A 1 334 ? 91.193  171.639 130.302 1.00 93.95  ? 309 ARG A NH2 1 
ATOM   1884  N  N   . LEU A 1 335 ? 99.621  171.148 132.938 1.00 78.91  ? 310 LEU A N   1 
ATOM   1885  C  CA  . LEU A 1 335 ? 100.640 171.632 133.865 1.00 78.72  ? 310 LEU A CA  1 
ATOM   1886  C  C   . LEU A 1 335 ? 101.432 172.777 133.249 1.00 80.34  ? 310 LEU A C   1 
ATOM   1887  O  O   . LEU A 1 335 ? 101.656 173.811 133.890 1.00 83.82  ? 310 LEU A O   1 
ATOM   1888  C  CB  . LEU A 1 335 ? 101.571 170.490 134.267 1.00 80.29  ? 310 LEU A CB  1 
ATOM   1889  C  CG  . LEU A 1 335 ? 101.338 169.847 135.633 1.00 83.52  ? 310 LEU A CG  1 
ATOM   1890  C  CD1 . LEU A 1 335 ? 99.926  169.302 135.742 1.00 81.90  ? 310 LEU A CD1 1 
ATOM   1891  C  CD2 . LEU A 1 335 ? 102.358 168.750 135.877 1.00 82.07  ? 310 LEU A CD2 1 
ATOM   1892  N  N   . LEU A 1 336 ? 101.848 172.618 131.992 1.00 85.48  ? 311 LEU A N   1 
ATOM   1893  C  CA  . LEU A 1 336 ? 102.577 173.688 131.319 1.00 85.85  ? 311 LEU A CA  1 
ATOM   1894  C  C   . LEU A 1 336 ? 101.704 174.919 131.124 1.00 87.58  ? 311 LEU A C   1 
ATOM   1895  O  O   . LEU A 1 336 ? 102.173 176.049 131.288 1.00 89.20  ? 311 LEU A O   1 
ATOM   1896  C  CB  . LEU A 1 336 ? 103.111 173.207 129.974 1.00 83.40  ? 311 LEU A CB  1 
ATOM   1897  C  CG  . LEU A 1 336 ? 103.757 174.334 129.172 1.00 82.78  ? 311 LEU A CG  1 
ATOM   1898  C  CD1 . LEU A 1 336 ? 105.264 174.327 129.349 1.00 83.35  ? 311 LEU A CD1 1 
ATOM   1899  C  CD2 . LEU A 1 336 ? 103.370 174.252 127.713 1.00 81.59  ? 311 LEU A CD2 1 
ATOM   1900  N  N   . ALA A 1 337 ? 100.437 174.723 130.757 1.00 93.09  ? 312 ALA A N   1 
ATOM   1901  C  CA  . ALA A 1 337 ? 99.545  175.857 130.549 1.00 92.11  ? 312 ALA A CA  1 
ATOM   1902  C  C   . ALA A 1 337 ? 99.349  176.645 131.836 1.00 92.10  ? 312 ALA A C   1 
ATOM   1903  O  O   . ALA A 1 337 ? 99.357  177.880 131.826 1.00 93.81  ? 312 ALA A O   1 
ATOM   1904  C  CB  . ALA A 1 337 ? 98.205  175.372 130.003 1.00 93.65  ? 312 ALA A CB  1 
ATOM   1905  N  N   . ALA A 1 338 ? 99.172  175.945 132.957 1.00 94.25  ? 313 ALA A N   1 
ATOM   1906  C  CA  . ALA A 1 338 ? 99.059  176.621 134.244 1.00 95.29  ? 313 ALA A CA  1 
ATOM   1907  C  C   . ALA A 1 338 ? 100.353 177.337 134.606 1.00 98.44  ? 313 ALA A C   1 
ATOM   1908  O  O   . ALA A 1 338 ? 100.325 178.453 135.137 1.00 100.13 ? 313 ALA A O   1 
ATOM   1909  C  CB  . ALA A 1 338 ? 98.678  175.617 135.330 1.00 93.69  ? 313 ALA A CB  1 
ATOM   1910  N  N   . LYS A 1 339 ? 101.500 176.708 134.334 1.00 96.52  ? 314 LYS A N   1 
ATOM   1911  C  CA  . LYS A 1 339 ? 102.776 177.335 134.663 1.00 94.19  ? 314 LYS A CA  1 
ATOM   1912  C  C   . LYS A 1 339 ? 103.010 178.598 133.844 1.00 93.64  ? 314 LYS A C   1 
ATOM   1913  O  O   . LYS A 1 339 ? 103.513 179.599 134.368 1.00 90.60  ? 314 LYS A O   1 
ATOM   1914  C  CB  . LYS A 1 339 ? 103.916 176.340 134.451 1.00 91.16  ? 314 LYS A CB  1 
ATOM   1915  C  CG  . LYS A 1 339 ? 105.220 176.745 135.116 1.00 91.88  ? 314 LYS A CG  1 
ATOM   1916  C  CD  . LYS A 1 339 ? 106.255 175.639 135.036 1.00 93.95  ? 314 LYS A CD  1 
ATOM   1917  C  CE  . LYS A 1 339 ? 105.636 174.282 135.313 1.00 95.35  ? 314 LYS A CE  1 
ATOM   1918  N  NZ  . LYS A 1 339 ? 105.448 174.049 136.768 1.00 93.63  ? 314 LYS A NZ  1 
ATOM   1919  N  N   . VAL A 1 340 ? 102.661 178.571 132.557 1.00 103.94 ? 315 VAL A N   1 
ATOM   1920  C  CA  . VAL A 1 340 ? 102.961 179.703 131.686 1.00 105.46 ? 315 VAL A CA  1 
ATOM   1921  C  C   . VAL A 1 340 ? 102.057 180.888 132.000 1.00 106.85 ? 315 VAL A C   1 
ATOM   1922  O  O   . VAL A 1 340 ? 102.472 182.045 131.860 1.00 106.14 ? 315 VAL A O   1 
ATOM   1923  C  CB  . VAL A 1 340 ? 102.877 179.278 130.205 1.00 104.03 ? 315 VAL A CB  1 
ATOM   1924  C  CG1 . VAL A 1 340 ? 101.442 179.272 129.707 1.00 102.88 ? 315 VAL A CG1 1 
ATOM   1925  C  CG2 . VAL A 1 340 ? 103.744 180.180 129.346 1.00 102.62 ? 315 VAL A CG2 1 
ATOM   1926  N  N   . GLY A 1 341 ? 100.822 180.637 132.432 1.00 113.12 ? 316 GLY A N   1 
ATOM   1927  C  CA  . GLY A 1 341 ? 99.952  181.721 132.840 1.00 113.51 ? 316 GLY A CA  1 
ATOM   1928  C  C   . GLY A 1 341 ? 98.543  181.700 132.284 1.00 114.02 ? 316 GLY A C   1 
ATOM   1929  O  O   . GLY A 1 341 ? 97.808  182.677 132.451 1.00 114.98 ? 316 GLY A O   1 
ATOM   1930  N  N   . CYS A 1 342 ? 98.140  180.615 131.627 1.00 116.93 ? 317 CYS A N   1 
ATOM   1931  C  CA  . CYS A 1 342 ? 96.771  180.520 131.128 1.00 118.69 ? 317 CYS A CA  1 
ATOM   1932  C  C   . CYS A 1 342 ? 96.339  179.065 131.073 1.00 117.71 ? 317 CYS A C   1 
ATOM   1933  O  O   . CYS A 1 342 ? 96.947  178.261 130.362 1.00 119.41 ? 317 CYS A O   1 
ATOM   1934  C  CB  . CYS A 1 342 ? 96.633  181.178 129.752 1.00 120.48 ? 317 CYS A CB  1 
ATOM   1935  S  SG  . CYS A 1 342 ? 97.583  180.461 128.396 1.00 125.35 ? 317 CYS A SG  1 
ATOM   1936  N  N   . ASP A 1 343 ? 95.287  178.732 131.820 1.00 115.21 ? 318 ASP A N   1 
ATOM   1937  C  CA  . ASP A 1 343 ? 94.706  177.389 131.836 1.00 116.57 ? 318 ASP A CA  1 
ATOM   1938  C  C   . ASP A 1 343 ? 93.188  177.534 131.801 1.00 116.65 ? 318 ASP A C   1 
ATOM   1939  O  O   . ASP A 1 343 ? 92.543  177.656 132.845 1.00 116.06 ? 318 ASP A O   1 
ATOM   1940  C  CB  . ASP A 1 343 ? 95.168  176.603 133.057 1.00 115.72 ? 318 ASP A CB  1 
ATOM   1941  C  CG  . ASP A 1 343 ? 94.744  175.150 133.006 1.00 116.14 ? 318 ASP A CG  1 
ATOM   1942  O  OD1 . ASP A 1 343 ? 94.320  174.691 131.924 1.00 114.92 ? 318 ASP A OD1 1 
ATOM   1943  O  OD2 . ASP A 1 343 ? 94.833  174.467 134.048 1.00 115.68 ? 318 ASP A OD2 1 
ATOM   1944  N  N   . ARG A 1 344 ? 92.621  177.520 130.598 1.00 119.89 ? 319 ARG A N   1 
ATOM   1945  C  CA  . ARG A 1 344 ? 91.178  177.575 130.424 1.00 119.37 ? 319 ARG A CA  1 
ATOM   1946  C  C   . ARG A 1 344 ? 90.616  176.165 130.319 1.00 119.43 ? 319 ARG A C   1 
ATOM   1947  O  O   . ARG A 1 344 ? 91.241  175.277 129.735 1.00 119.19 ? 319 ARG A O   1 
ATOM   1948  C  CB  . ARG A 1 344 ? 90.810  178.374 129.174 1.00 118.18 ? 319 ARG A CB  1 
ATOM   1949  C  CG  . ARG A 1 344 ? 91.772  179.499 128.842 1.00 117.90 ? 319 ARG A CG  1 
ATOM   1950  C  CD  . ARG A 1 344 ? 91.340  180.803 129.480 1.00 118.19 ? 319 ARG A CD  1 
ATOM   1951  N  NE  . ARG A 1 344 ? 92.310  181.865 129.247 1.00 119.97 ? 319 ARG A NE  1 
ATOM   1952  C  CZ  . ARG A 1 344 ? 93.282  182.189 130.087 1.00 119.88 ? 319 ARG A CZ  1 
ATOM   1953  N  NH1 . ARG A 1 344 ? 93.450  181.546 131.231 1.00 117.30 ? 319 ARG A NH1 1 
ATOM   1954  N  NH2 . ARG A 1 344 ? 94.104  183.187 129.774 1.00 119.06 ? 319 ARG A NH2 1 
ATOM   1955  N  N   . GLU A 1 345 ? 89.423  175.968 130.884 1.00 122.32 ? 320 GLU A N   1 
ATOM   1956  C  CA  . GLU A 1 345 ? 88.791  174.655 130.840 1.00 121.70 ? 320 GLU A CA  1 
ATOM   1957  C  C   . GLU A 1 345 ? 88.448  174.229 129.421 1.00 121.32 ? 320 GLU A C   1 
ATOM   1958  O  O   . GLU A 1 345 ? 88.196  173.042 129.186 1.00 119.12 ? 320 GLU A O   1 
ATOM   1959  C  CB  . GLU A 1 345 ? 87.535  174.647 131.711 1.00 120.71 ? 320 GLU A CB  1 
ATOM   1960  C  CG  . GLU A 1 345 ? 87.775  175.128 133.130 1.00 121.22 ? 320 GLU A CG  1 
ATOM   1961  C  CD  . GLU A 1 345 ? 88.835  174.318 133.846 1.00 121.71 ? 320 GLU A CD  1 
ATOM   1962  O  OE1 . GLU A 1 345 ? 88.868  173.083 133.663 1.00 121.30 ? 320 GLU A OE1 1 
ATOM   1963  O  OE2 . GLU A 1 345 ? 89.639  174.917 134.591 1.00 120.95 ? 320 GLU A OE2 1 
ATOM   1964  N  N   . ASP A 1 346 ? 88.426  175.163 128.475 1.00 126.29 ? 321 ASP A N   1 
ATOM   1965  C  CA  . ASP A 1 346 ? 88.269  174.835 127.066 1.00 126.40 ? 321 ASP A CA  1 
ATOM   1966  C  C   . ASP A 1 346 ? 89.649  174.708 126.436 1.00 126.77 ? 321 ASP A C   1 
ATOM   1967  O  O   . ASP A 1 346 ? 90.476  175.618 126.549 1.00 125.65 ? 321 ASP A O   1 
ATOM   1968  C  CB  . ASP A 1 346 ? 87.448  175.902 126.341 1.00 125.68 ? 321 ASP A CB  1 
ATOM   1969  C  CG  . ASP A 1 346 ? 86.813  175.379 125.069 1.00 126.58 ? 321 ASP A CG  1 
ATOM   1970  O  OD1 . ASP A 1 346 ? 86.729  174.143 124.913 1.00 126.28 ? 321 ASP A OD1 1 
ATOM   1971  O  OD2 . ASP A 1 346 ? 86.399  176.201 124.225 1.00 125.79 ? 321 ASP A OD2 1 
ATOM   1972  N  N   . SER A 1 347 ? 89.895  173.571 125.783 1.00 117.51 ? 322 SER A N   1 
ATOM   1973  C  CA  . SER A 1 347 ? 91.226  173.294 125.257 1.00 116.57 ? 322 SER A CA  1 
ATOM   1974  C  C   . SER A 1 347 ? 91.610  174.280 124.162 1.00 115.82 ? 322 SER A C   1 
ATOM   1975  O  O   . SER A 1 347 ? 92.765  174.713 124.085 1.00 114.82 ? 322 SER A O   1 
ATOM   1976  C  CB  . SER A 1 347 ? 91.294  171.860 124.739 1.00 114.61 ? 322 SER A CB  1 
ATOM   1977  O  OG  . SER A 1 347 ? 91.028  170.936 125.779 1.00 113.08 ? 322 SER A OG  1 
ATOM   1978  N  N   . THR A 1 348 ? 90.656  174.645 123.304 1.00 118.00 ? 323 THR A N   1 
ATOM   1979  C  CA  . THR A 1 348 ? 90.967  175.543 122.196 1.00 119.72 ? 323 THR A CA  1 
ATOM   1980  C  C   . THR A 1 348 ? 91.409  176.913 122.697 1.00 120.55 ? 323 THR A C   1 
ATOM   1981  O  O   . THR A 1 348 ? 92.327  177.520 122.132 1.00 121.14 ? 323 THR A O   1 
ATOM   1982  C  CB  . THR A 1 348 ? 89.761  175.672 121.267 1.00 118.76 ? 323 THR A CB  1 
ATOM   1983  O  OG1 . THR A 1 348 ? 89.067  174.420 121.207 1.00 116.90 ? 323 THR A OG1 1 
ATOM   1984  C  CG2 . THR A 1 348 ? 90.214  176.050 119.869 1.00 117.81 ? 323 THR A CG2 1 
ATOM   1985  N  N   . GLU A 1 349 ? 90.770  177.418 123.755 1.00 121.96 ? 324 GLU A N   1 
ATOM   1986  C  CA  . GLU A 1 349 ? 91.153  178.718 124.297 1.00 123.32 ? 324 GLU A CA  1 
ATOM   1987  C  C   . GLU A 1 349 ? 92.579  178.699 124.837 1.00 124.62 ? 324 GLU A C   1 
ATOM   1988  O  O   . GLU A 1 349 ? 93.364  179.619 124.575 1.00 122.49 ? 324 GLU A O   1 
ATOM   1989  C  CB  . GLU A 1 349 ? 90.172  179.139 125.390 1.00 124.39 ? 324 GLU A CB  1 
ATOM   1990  C  CG  . GLU A 1 349 ? 88.770  179.429 124.886 1.00 124.58 ? 324 GLU A CG  1 
ATOM   1991  C  CD  . GLU A 1 349 ? 87.886  180.049 125.950 1.00 126.27 ? 324 GLU A CD  1 
ATOM   1992  O  OE1 . GLU A 1 349 ? 88.080  179.732 127.143 1.00 125.90 ? 324 GLU A OE1 1 
ATOM   1993  O  OE2 . GLU A 1 349 ? 87.000  180.855 125.595 1.00 125.39 ? 324 GLU A OE2 1 
ATOM   1994  N  N   . ALA A 1 350 ? 92.933  177.657 125.592 1.00 120.30 ? 325 ALA A N   1 
ATOM   1995  C  CA  . ALA A 1 350 ? 94.289  177.556 126.121 1.00 119.19 ? 325 ALA A CA  1 
ATOM   1996  C  C   . ALA A 1 350 ? 95.306  177.389 125.001 1.00 119.34 ? 325 ALA A C   1 
ATOM   1997  O  O   . ALA A 1 350 ? 96.403  177.958 125.058 1.00 118.95 ? 325 ALA A O   1 
ATOM   1998  C  CB  . ALA A 1 350 ? 94.382  176.397 127.112 1.00 117.94 ? 325 ALA A CB  1 
ATOM   1999  N  N   . VAL A 1 351 ? 94.961  176.610 123.974 1.00 110.10 ? 326 VAL A N   1 
ATOM   2000  C  CA  . VAL A 1 351 ? 95.862  176.431 122.841 1.00 107.98 ? 326 VAL A CA  1 
ATOM   2001  C  C   . VAL A 1 351 ? 96.097  177.760 122.135 1.00 110.52 ? 326 VAL A C   1 
ATOM   2002  O  O   . VAL A 1 351 ? 97.229  178.090 121.763 1.00 107.97 ? 326 VAL A O   1 
ATOM   2003  C  CB  . VAL A 1 351 ? 95.305  175.365 121.881 1.00 107.22 ? 326 VAL A CB  1 
ATOM   2004  C  CG1 . VAL A 1 351 ? 96.003  175.439 120.536 1.00 108.24 ? 326 VAL A CG1 1 
ATOM   2005  C  CG2 . VAL A 1 351 ? 95.461  173.983 122.489 1.00 106.90 ? 326 VAL A CG2 1 
ATOM   2006  N  N   . GLU A 1 352 ? 95.034  178.545 121.942 1.00 120.64 ? 327 GLU A N   1 
ATOM   2007  C  CA  . GLU A 1 352 ? 95.188  179.856 121.319 1.00 120.44 ? 327 GLU A CA  1 
ATOM   2008  C  C   . GLU A 1 352 ? 96.045  180.779 122.177 1.00 121.35 ? 327 GLU A C   1 
ATOM   2009  O  O   . GLU A 1 352 ? 96.908  181.501 121.657 1.00 123.00 ? 327 GLU A O   1 
ATOM   2010  C  CB  . GLU A 1 352 ? 93.818  180.478 121.062 1.00 118.30 ? 327 GLU A CB  1 
ATOM   2011  C  CG  . GLU A 1 352 ? 93.832  181.569 120.010 1.00 120.64 ? 327 GLU A CG  1 
ATOM   2012  C  CD  . GLU A 1 352 ? 94.279  181.063 118.655 1.00 121.84 ? 327 GLU A CD  1 
ATOM   2013  O  OE1 . GLU A 1 352 ? 93.743  180.031 118.200 1.00 119.91 ? 327 GLU A OE1 1 
ATOM   2014  O  OE2 . GLU A 1 352 ? 95.165  181.696 118.046 1.00 122.72 ? 327 GLU A OE2 1 
ATOM   2015  N  N   . CYS A 1 353 ? 95.828  180.767 123.495 1.00 115.47 ? 328 CYS A N   1 
ATOM   2016  C  CA  . CYS A 1 353 ? 96.664  181.576 124.375 1.00 114.53 ? 328 CYS A CA  1 
ATOM   2017  C  C   . CYS A 1 353 ? 98.129  181.193 124.235 1.00 115.05 ? 328 CYS A C   1 
ATOM   2018  O  O   . CYS A 1 353 ? 99.001  182.063 124.143 1.00 114.01 ? 328 CYS A O   1 
ATOM   2019  C  CB  . CYS A 1 353 ? 96.226  181.425 125.828 1.00 115.74 ? 328 CYS A CB  1 
ATOM   2020  S  SG  . CYS A 1 353 ? 97.528  181.921 126.986 1.00 127.26 ? 328 CYS A SG  1 
ATOM   2021  N  N   . LEU A 1 354 ? 98.416  179.890 124.208 1.00 107.88 ? 329 LEU A N   1 
ATOM   2022  C  CA  . LEU A 1 354 ? 99.790  179.438 124.019 1.00 106.68 ? 329 LEU A CA  1 
ATOM   2023  C  C   . LEU A 1 354 ? 100.336 179.896 122.673 1.00 105.95 ? 329 LEU A C   1 
ATOM   2024  O  O   . LEU A 1 354 ? 101.504 180.287 122.568 1.00 104.39 ? 329 LEU A O   1 
ATOM   2025  C  CB  . LEU A 1 354 ? 99.858  177.917 124.148 1.00 106.71 ? 329 LEU A CB  1 
ATOM   2026  C  CG  . LEU A 1 354 ? 99.671  177.397 125.574 1.00 104.86 ? 329 LEU A CG  1 
ATOM   2027  C  CD1 . LEU A 1 354 ? 99.296  175.929 125.577 1.00 102.74 ? 329 LEU A CD1 1 
ATOM   2028  C  CD2 . LEU A 1 354 ? 100.929 177.630 126.386 1.00 105.05 ? 329 LEU A CD2 1 
ATOM   2029  N  N   . ARG A 1 355 ? 99.502  179.859 121.632 1.00 98.35  ? 330 ARG A N   1 
ATOM   2030  C  CA  . ARG A 1 355 ? 99.911  180.374 120.331 1.00 97.01  ? 330 ARG A CA  1 
ATOM   2031  C  C   . ARG A 1 355 ? 100.217 181.863 120.376 1.00 95.45  ? 330 ARG A C   1 
ATOM   2032  O  O   . ARG A 1 355 ? 100.979 182.354 119.537 1.00 92.52  ? 330 ARG A O   1 
ATOM   2033  C  CB  . ARG A 1 355 ? 98.826  180.107 119.287 1.00 94.22  ? 330 ARG A CB  1 
ATOM   2034  C  CG  . ARG A 1 355 ? 98.658  178.647 118.929 1.00 96.17  ? 330 ARG A CG  1 
ATOM   2035  C  CD  . ARG A 1 355 ? 98.002  178.475 117.575 1.00 93.75  ? 330 ARG A CD  1 
ATOM   2036  N  NE  . ARG A 1 355 ? 97.088  177.341 117.571 1.00 94.21  ? 330 ARG A NE  1 
ATOM   2037  C  CZ  . ARG A 1 355 ? 96.602  176.772 116.478 1.00 95.90  ? 330 ARG A CZ  1 
ATOM   2038  N  NH1 . ARG A 1 355 ? 96.934  177.197 115.271 1.00 95.42  ? 330 ARG A NH1 1 
ATOM   2039  N  NH2 . ARG A 1 355 ? 95.763  175.748 116.599 1.00 95.32  ? 330 ARG A NH2 1 
ATOM   2040  N  N   . ARG A 1 356 ? 99.644  182.590 121.333 1.00 109.65 ? 331 ARG A N   1 
ATOM   2041  C  CA  . ARG A 1 356 ? 99.901  184.016 121.476 1.00 109.42 ? 331 ARG A CA  1 
ATOM   2042  C  C   . ARG A 1 356 ? 101.122 184.324 122.339 1.00 109.13 ? 331 ARG A C   1 
ATOM   2043  O  O   . ARG A 1 356 ? 101.398 185.500 122.595 1.00 109.62 ? 331 ARG A O   1 
ATOM   2044  C  CB  . ARG A 1 356 ? 98.674  184.720 122.058 1.00 108.56 ? 331 ARG A CB  1 
ATOM   2045  C  CG  . ARG A 1 356 ? 97.468  184.737 121.139 1.00 107.37 ? 331 ARG A CG  1 
ATOM   2046  C  CD  . ARG A 1 356 ? 96.194  184.966 121.930 1.00 108.56 ? 331 ARG A CD  1 
ATOM   2047  N  NE  . ARG A 1 356 ? 96.436  185.765 123.124 1.00 111.46 ? 331 ARG A NE  1 
ATOM   2048  C  CZ  . ARG A 1 356 ? 95.568  185.914 124.115 1.00 110.67 ? 331 ARG A CZ  1 
ATOM   2049  N  NH1 . ARG A 1 356 ? 94.383  185.327 124.090 1.00 110.64 ? 331 ARG A NH1 1 
ATOM   2050  N  NH2 . ARG A 1 356 ? 95.898  186.669 125.159 1.00 110.32 ? 331 ARG A NH2 1 
ATOM   2051  N  N   . LYS A 1 357 ? 101.854 183.309 122.792 1.00 107.15 ? 332 LYS A N   1 
ATOM   2052  C  CA  . LYS A 1 357 ? 103.005 183.500 123.663 1.00 105.30 ? 332 LYS A CA  1 
ATOM   2053  C  C   . LYS A 1 357 ? 104.299 183.233 122.906 1.00 106.57 ? 332 LYS A C   1 
ATOM   2054  O  O   . LYS A 1 357 ? 104.343 182.413 121.986 1.00 110.34 ? 332 LYS A O   1 
ATOM   2055  C  CB  . LYS A 1 357 ? 102.927 182.589 124.889 1.00 104.06 ? 332 LYS A CB  1 
ATOM   2056  C  CG  . LYS A 1 357 ? 101.636 182.727 125.665 1.00 107.28 ? 332 LYS A CG  1 
ATOM   2057  C  CD  . LYS A 1 357 ? 101.839 182.467 127.141 1.00 107.48 ? 332 LYS A CD  1 
ATOM   2058  C  CE  . LYS A 1 357 ? 100.776 183.166 127.968 1.00 106.89 ? 332 LYS A CE  1 
ATOM   2059  N  NZ  . LYS A 1 357 ? 100.331 184.441 127.342 1.00 107.20 ? 332 LYS A NZ  1 
ATOM   2060  N  N   . SER A 1 358 ? 105.355 183.937 123.305 1.00 100.70 ? 333 SER A N   1 
ATOM   2061  C  CA  . SER A 1 358 ? 106.645 183.793 122.648 1.00 102.67 ? 333 SER A CA  1 
ATOM   2062  C  C   . SER A 1 358 ? 107.222 182.404 122.893 1.00 104.39 ? 333 SER A C   1 
ATOM   2063  O  O   . SER A 1 358 ? 106.964 181.771 123.919 1.00 106.80 ? 333 SER A O   1 
ATOM   2064  C  CB  . SER A 1 358 ? 107.622 184.857 123.144 1.00 102.46 ? 333 SER A CB  1 
ATOM   2065  O  OG  . SER A 1 358 ? 108.017 184.601 124.479 1.00 100.28 ? 333 SER A OG  1 
ATOM   2066  N  N   . SER A 1 359 ? 108.012 181.930 121.925 1.00 101.04 ? 334 SER A N   1 
ATOM   2067  C  CA  . SER A 1 359 ? 108.586 180.592 122.019 1.00 99.71  ? 334 SER A CA  1 
ATOM   2068  C  C   . SER A 1 359 ? 109.537 180.470 123.202 1.00 100.26 ? 334 SER A C   1 
ATOM   2069  O  O   . SER A 1 359 ? 109.516 179.466 123.924 1.00 101.05 ? 334 SER A O   1 
ATOM   2070  C  CB  . SER A 1 359 ? 109.310 180.242 120.722 1.00 99.36  ? 334 SER A CB  1 
ATOM   2071  O  OG  . SER A 1 359 ? 110.550 180.920 120.641 1.00 98.74  ? 334 SER A OG  1 
ATOM   2072  N  N   . ARG A 1 360 ? 110.386 181.478 123.414 1.00 98.09  ? 335 ARG A N   1 
ATOM   2073  C  CA  . ARG A 1 360 ? 111.353 181.411 124.504 1.00 97.73  ? 335 ARG A CA  1 
ATOM   2074  C  C   . ARG A 1 360 ? 110.669 181.364 125.862 1.00 98.40  ? 335 ARG A C   1 
ATOM   2075  O  O   . ARG A 1 360 ? 111.233 180.829 126.822 1.00 97.68  ? 335 ARG A O   1 
ATOM   2076  C  CB  . ARG A 1 360 ? 112.305 182.604 124.438 1.00 98.68  ? 335 ARG A CB  1 
ATOM   2077  C  CG  . ARG A 1 360 ? 113.247 182.586 123.249 1.00 101.08 ? 335 ARG A CG  1 
ATOM   2078  C  CD  . ARG A 1 360 ? 114.698 182.540 123.695 1.00 99.52  ? 335 ARG A CD  1 
ATOM   2079  N  NE  . ARG A 1 360 ? 114.975 181.385 124.540 1.00 101.00 ? 335 ARG A NE  1 
ATOM   2080  C  CZ  . ARG A 1 360 ? 115.222 180.164 124.085 1.00 99.54  ? 335 ARG A CZ  1 
ATOM   2081  N  NH1 . ARG A 1 360 ? 115.237 179.900 122.789 1.00 96.51  ? 335 ARG A NH1 1 
ATOM   2082  N  NH2 . ARG A 1 360 ? 115.461 179.185 124.952 1.00 96.50  ? 335 ARG A NH2 1 
ATOM   2083  N  N   . GLU A 1 361 ? 109.464 181.919 125.968 1.00 102.29 ? 336 GLU A N   1 
ATOM   2084  C  CA  . GLU A 1 361 ? 108.790 181.951 127.259 1.00 103.55 ? 336 GLU A CA  1 
ATOM   2085  C  C   . GLU A 1 361 ? 108.203 180.593 127.622 1.00 101.69 ? 336 GLU A C   1 
ATOM   2086  O  O   . GLU A 1 361 ? 108.240 180.193 128.790 1.00 103.33 ? 336 GLU A O   1 
ATOM   2087  C  CB  . GLU A 1 361 ? 107.707 183.030 127.255 1.00 103.36 ? 336 GLU A CB  1 
ATOM   2088  C  CG  . GLU A 1 361 ? 106.611 182.832 128.280 1.00 105.38 ? 336 GLU A CG  1 
ATOM   2089  C  CD  . GLU A 1 361 ? 105.577 183.935 128.233 1.00 106.71 ? 336 GLU A CD  1 
ATOM   2090  O  OE1 . GLU A 1 361 ? 105.956 185.095 127.967 1.00 107.79 ? 336 GLU A OE1 1 
ATOM   2091  O  OE2 . GLU A 1 361 ? 104.387 183.647 128.472 1.00 104.86 ? 336 GLU A OE2 1 
ATOM   2092  N  N   . LEU A 1 362 ? 107.668 179.865 126.643 1.00 88.68  ? 337 LEU A N   1 
ATOM   2093  C  CA  . LEU A 1 362 ? 107.080 178.558 126.897 1.00 90.54  ? 337 LEU A CA  1 
ATOM   2094  C  C   . LEU A 1 362 ? 108.045 177.404 126.655 1.00 88.06  ? 337 LEU A C   1 
ATOM   2095  O  O   . LEU A 1 362 ? 107.668 176.248 126.862 1.00 86.67  ? 337 LEU A O   1 
ATOM   2096  C  CB  . LEU A 1 362 ? 105.805 178.377 126.059 1.00 89.62  ? 337 LEU A CB  1 
ATOM   2097  C  CG  . LEU A 1 362 ? 105.754 178.503 124.532 1.00 88.64  ? 337 LEU A CG  1 
ATOM   2098  C  CD1 . LEU A 1 362 ? 106.626 177.496 123.804 1.00 87.01  ? 337 LEU A CD1 1 
ATOM   2099  C  CD2 . LEU A 1 362 ? 104.314 178.381 124.070 1.00 89.62  ? 337 LEU A CD2 1 
ATOM   2100  N  N   . VAL A 1 363 ? 109.270 177.683 126.221 1.00 89.85  ? 338 VAL A N   1 
ATOM   2101  C  CA  . VAL A 1 363 ? 110.274 176.634 126.081 1.00 88.07  ? 338 VAL A CA  1 
ATOM   2102  C  C   . VAL A 1 363 ? 111.178 176.567 127.304 1.00 90.43  ? 338 VAL A C   1 
ATOM   2103  O  O   . VAL A 1 363 ? 111.540 175.479 127.758 1.00 89.31  ? 338 VAL A O   1 
ATOM   2104  C  CB  . VAL A 1 363 ? 111.082 176.852 124.788 1.00 86.92  ? 338 VAL A CB  1 
ATOM   2105  C  CG1 . VAL A 1 363 ? 112.445 176.200 124.892 1.00 87.09  ? 338 VAL A CG1 1 
ATOM   2106  C  CG2 . VAL A 1 363 ? 110.324 176.295 123.601 1.00 87.57  ? 338 VAL A CG2 1 
ATOM   2107  N  N   . ASP A 1 364 ? 111.540 177.718 127.867 1.00 100.73 ? 339 ASP A N   1 
ATOM   2108  C  CA  . ASP A 1 364 ? 112.429 177.767 129.021 1.00 98.80  ? 339 ASP A CA  1 
ATOM   2109  C  C   . ASP A 1 364 ? 111.750 177.365 130.323 1.00 98.82  ? 339 ASP A C   1 
ATOM   2110  O  O   . ASP A 1 364 ? 112.430 177.279 131.350 1.00 98.91  ? 339 ASP A O   1 
ATOM   2111  C  CB  . ASP A 1 364 ? 113.035 179.166 129.159 1.00 100.25 ? 339 ASP A CB  1 
ATOM   2112  C  CG  . ASP A 1 364 ? 114.110 179.439 128.123 1.00 102.19 ? 339 ASP A CG  1 
ATOM   2113  O  OD1 . ASP A 1 364 ? 113.775 179.897 127.013 1.00 99.26  ? 339 ASP A OD1 1 
ATOM   2114  O  OD2 . ASP A 1 364 ? 115.298 179.195 128.421 1.00 103.46 ? 339 ASP A OD2 1 
ATOM   2115  N  N   . GLN A 1 365 ? 110.442 177.121 130.317 1.00 100.02 ? 340 GLN A N   1 
ATOM   2116  C  CA  . GLN A 1 365 ? 109.789 176.582 131.499 1.00 98.62  ? 340 GLN A CA  1 
ATOM   2117  C  C   . GLN A 1 365 ? 110.248 175.148 131.746 1.00 100.35 ? 340 GLN A C   1 
ATOM   2118  O  O   . GLN A 1 365 ? 110.736 174.457 130.849 1.00 102.30 ? 340 GLN A O   1 
ATOM   2119  C  CB  . GLN A 1 365 ? 108.268 176.626 131.350 1.00 95.23  ? 340 GLN A CB  1 
ATOM   2120  C  CG  . GLN A 1 365 ? 107.692 178.008 131.085 1.00 99.03  ? 340 GLN A CG  1 
ATOM   2121  C  CD  . GLN A 1 365 ? 108.019 179.011 132.176 1.00 101.11 ? 340 GLN A CD  1 
ATOM   2122  O  OE1 . GLN A 1 365 ? 108.307 178.641 133.314 1.00 101.51 ? 340 GLN A OE1 1 
ATOM   2123  N  NE2 . GLN A 1 365 ? 107.977 180.291 131.831 1.00 100.10 ? 340 GLN A NE2 1 
ATOM   2124  N  N   . ASP A 1 366 ? 110.087 174.702 132.989 1.00 93.74  ? 341 ASP A N   1 
ATOM   2125  C  CA  . ASP A 1 366 ? 110.554 173.389 133.422 1.00 93.34  ? 341 ASP A CA  1 
ATOM   2126  C  C   . ASP A 1 366 ? 109.362 172.562 133.885 1.00 91.42  ? 341 ASP A C   1 
ATOM   2127  O  O   . ASP A 1 366 ? 108.753 172.866 134.916 1.00 90.77  ? 341 ASP A O   1 
ATOM   2128  C  CB  . ASP A 1 366 ? 111.592 173.526 134.534 1.00 94.31  ? 341 ASP A CB  1 
ATOM   2129  C  CG  . ASP A 1 366 ? 111.735 172.263 135.357 1.00 97.51  ? 341 ASP A CG  1 
ATOM   2130  O  OD1 . ASP A 1 366 ? 112.101 171.217 134.784 1.00 96.98  ? 341 ASP A OD1 1 
ATOM   2131  O  OD2 . ASP A 1 366 ? 111.482 172.317 136.579 1.00 96.08  ? 341 ASP A OD2 1 
ATOM   2132  N  N   . VAL A 1 367 ? 109.032 171.521 133.126 1.00 81.51  ? 342 VAL A N   1 
ATOM   2133  C  CA  . VAL A 1 367 ? 108.001 170.559 133.497 1.00 82.06  ? 342 VAL A CA  1 
ATOM   2134  C  C   . VAL A 1 367 ? 108.674 169.198 133.587 1.00 78.71  ? 342 VAL A C   1 
ATOM   2135  O  O   . VAL A 1 367 ? 109.153 168.666 132.578 1.00 80.48  ? 342 VAL A O   1 
ATOM   2136  C  CB  . VAL A 1 367 ? 106.840 170.534 132.496 1.00 84.89  ? 342 VAL A CB  1 
ATOM   2137  C  CG1 . VAL A 1 367 ? 105.916 169.371 132.794 1.00 82.50  ? 342 VAL A CG1 1 
ATOM   2138  C  CG2 . VAL A 1 367 ? 106.080 171.844 132.535 1.00 82.91  ? 342 VAL A CG2 1 
ATOM   2139  N  N   . GLN A 1 368 ? 108.708 168.630 134.789 1.00 80.02  ? 343 GLN A N   1 
ATOM   2140  C  CA  . GLN A 1 368 ? 109.421 167.383 135.021 1.00 83.90  ? 343 GLN A CA  1 
ATOM   2141  C  C   . GLN A 1 368 ? 108.474 166.203 134.866 1.00 83.20  ? 343 GLN A C   1 
ATOM   2142  O  O   . GLN A 1 368 ? 107.473 166.130 135.590 1.00 83.00  ? 343 GLN A O   1 
ATOM   2143  C  CB  . GLN A 1 368 ? 110.042 167.371 136.406 1.00 87.49  ? 343 GLN A CB  1 
ATOM   2144  C  CG  . GLN A 1 368 ? 111.356 166.610 136.490 1.00 85.28  ? 343 GLN A CG  1 
ATOM   2145  C  CD  . GLN A 1 368 ? 112.451 167.234 135.650 1.00 86.20  ? 343 GLN A CD  1 
ATOM   2146  O  OE1 . GLN A 1 368 ? 112.380 168.408 135.288 1.00 83.58  ? 343 GLN A OE1 1 
ATOM   2147  N  NE2 . GLN A 1 368 ? 113.471 166.447 135.332 1.00 86.65  ? 343 GLN A NE2 1 
ATOM   2148  N  N   . PRO A 1 369 ? 108.741 165.274 133.958 1.00 71.82  ? 344 PRO A N   1 
ATOM   2149  C  CA  . PRO A 1 369 ? 107.902 164.083 133.840 1.00 70.89  ? 344 PRO A CA  1 
ATOM   2150  C  C   . PRO A 1 369 ? 108.226 163.077 134.935 1.00 75.06  ? 344 PRO A C   1 
ATOM   2151  O  O   . PRO A 1 369 ? 109.229 163.181 135.640 1.00 73.52  ? 344 PRO A O   1 
ATOM   2152  C  CB  . PRO A 1 369 ? 108.279 163.538 132.464 1.00 67.62  ? 344 PRO A CB  1 
ATOM   2153  C  CG  . PRO A 1 369 ? 109.714 163.912 132.325 1.00 66.52  ? 344 PRO A CG  1 
ATOM   2154  C  CD  . PRO A 1 369 ? 109.880 165.239 133.025 1.00 70.34  ? 344 PRO A CD  1 
ATOM   2155  N  N   . ALA A 1 370 ? 107.349 162.087 135.066 1.00 69.85  ? 345 ALA A N   1 
ATOM   2156  C  CA  . ALA A 1 370 ? 107.630 160.980 135.965 1.00 64.52  ? 345 ALA A CA  1 
ATOM   2157  C  C   . ALA A 1 370 ? 108.870 160.238 135.486 1.00 69.30  ? 345 ALA A C   1 
ATOM   2158  O  O   . ALA A 1 370 ? 109.193 160.236 134.297 1.00 77.86  ? 345 ALA A O   1 
ATOM   2159  C  CB  . ALA A 1 370 ? 106.435 160.033 136.038 1.00 67.38  ? 345 ALA A CB  1 
ATOM   2160  N  N   . ARG A 1 371 ? 109.582 159.624 136.426 1.00 66.24  ? 346 ARG A N   1 
ATOM   2161  C  CA  . ARG A 1 371 ? 110.838 158.970 136.089 1.00 62.23  ? 346 ARG A CA  1 
ATOM   2162  C  C   . ARG A 1 371 ? 110.608 157.859 135.073 1.00 67.91  ? 346 ARG A C   1 
ATOM   2163  O  O   . ARG A 1 371 ? 109.607 157.141 135.131 1.00 69.66  ? 346 ARG A O   1 
ATOM   2164  C  CB  . ARG A 1 371 ? 111.503 158.411 137.344 1.00 63.21  ? 346 ARG A CB  1 
ATOM   2165  C  CG  . ARG A 1 371 ? 112.457 159.381 138.014 1.00 65.21  ? 346 ARG A CG  1 
ATOM   2166  C  CD  . ARG A 1 371 ? 113.255 158.708 139.112 1.00 64.71  ? 346 ARG A CD  1 
ATOM   2167  N  NE  . ARG A 1 371 ? 114.270 157.813 138.574 1.00 68.81  ? 346 ARG A NE  1 
ATOM   2168  C  CZ  . ARG A 1 371 ? 115.531 158.157 138.358 1.00 74.58  ? 346 ARG A CZ  1 
ATOM   2169  N  NH1 . ARG A 1 371 ? 115.971 159.373 138.632 1.00 71.43  ? 346 ARG A NH1 1 
ATOM   2170  N  NH2 . ARG A 1 371 ? 116.373 157.258 137.855 1.00 71.37  ? 346 ARG A NH2 1 
ATOM   2171  N  N   . TYR A 1 372 ? 111.545 157.732 134.132 1.00 57.51  ? 347 TYR A N   1 
ATOM   2172  C  CA  . TYR A 1 372 ? 111.454 156.770 133.032 1.00 52.55  ? 347 TYR A CA  1 
ATOM   2173  C  C   . TYR A 1 372 ? 110.206 157.006 132.187 1.00 56.67  ? 347 TYR A C   1 
ATOM   2174  O  O   . TYR A 1 372 ? 109.571 156.065 131.711 1.00 65.40  ? 347 TYR A O   1 
ATOM   2175  C  CB  . TYR A 1 372 ? 111.496 155.328 133.542 1.00 46.91  ? 347 TYR A CB  1 
ATOM   2176  C  CG  . TYR A 1 372 ? 112.567 155.072 134.572 1.00 46.37  ? 347 TYR A CG  1 
ATOM   2177  C  CD1 . TYR A 1 372 ? 113.817 155.647 134.454 1.00 53.24  ? 347 TYR A CD1 1 
ATOM   2178  C  CD2 . TYR A 1 372 ? 112.324 154.255 135.660 1.00 53.72  ? 347 TYR A CD2 1 
ATOM   2179  C  CE1 . TYR A 1 372 ? 114.793 155.418 135.391 1.00 56.35  ? 347 TYR A CE1 1 
ATOM   2180  C  CE2 . TYR A 1 372 ? 113.295 154.020 136.602 1.00 58.40  ? 347 TYR A CE2 1 
ATOM   2181  C  CZ  . TYR A 1 372 ? 114.529 154.605 136.462 1.00 57.67  ? 347 TYR A CZ  1 
ATOM   2182  O  OH  . TYR A 1 372 ? 115.510 154.377 137.397 1.00 57.98  ? 347 TYR A OH  1 
ATOM   2183  N  N   . HIS A 1 373 ? 109.852 158.275 132.003 1.00 52.27  ? 348 HIS A N   1 
ATOM   2184  C  CA  . HIS A 1 373 ? 108.757 158.672 131.130 1.00 50.28  ? 348 HIS A CA  1 
ATOM   2185  C  C   . HIS A 1 373 ? 109.119 160.017 130.515 1.00 55.37  ? 348 HIS A C   1 
ATOM   2186  O  O   . HIS A 1 373 ? 110.178 160.581 130.798 1.00 61.79  ? 348 HIS A O   1 
ATOM   2187  C  CB  . HIS A 1 373 ? 107.429 158.731 131.890 1.00 48.73  ? 348 HIS A CB  1 
ATOM   2188  C  CG  . HIS A 1 373 ? 106.929 157.395 132.346 1.00 53.69  ? 348 HIS A CG  1 
ATOM   2189  N  ND1 . HIS A 1 373 ? 106.175 156.568 131.544 1.00 60.52  ? 348 HIS A ND1 1 
ATOM   2190  C  CD2 . HIS A 1 373 ? 107.071 156.745 133.525 1.00 53.20  ? 348 HIS A CD2 1 
ATOM   2191  C  CE1 . HIS A 1 373 ? 105.877 155.465 132.206 1.00 55.70  ? 348 HIS A CE1 1 
ATOM   2192  N  NE2 . HIS A 1 373 ? 106.408 155.548 133.412 1.00 49.17  ? 348 HIS A NE2 1 
ATOM   2193  N  N   . ILE A 1 374 ? 108.239 160.535 129.663 1.00 51.01  ? 349 ILE A N   1 
ATOM   2194  C  CA  . ILE A 1 374 ? 108.477 161.813 129.006 1.00 54.15  ? 349 ILE A CA  1 
ATOM   2195  C  C   . ILE A 1 374 ? 107.268 162.715 129.195 1.00 59.82  ? 349 ILE A C   1 
ATOM   2196  O  O   . ILE A 1 374 ? 106.138 162.249 129.369 1.00 62.02  ? 349 ILE A O   1 
ATOM   2197  C  CB  . ILE A 1 374 ? 108.791 161.655 127.503 1.00 48.39  ? 349 ILE A CB  1 
ATOM   2198  C  CG1 . ILE A 1 374 ? 107.702 160.845 126.809 1.00 49.30  ? 349 ILE A CG1 1 
ATOM   2199  C  CG2 . ILE A 1 374 ? 110.142 161.007 127.306 1.00 52.63  ? 349 ILE A CG2 1 
ATOM   2200  C  CD1 . ILE A 1 374 ? 107.894 160.739 125.326 1.00 48.22  ? 349 ILE A CD1 1 
ATOM   2201  N  N   . ALA A 1 375 ? 107.519 164.024 129.168 1.00 65.57  ? 350 ALA A N   1 
ATOM   2202  C  CA  . ALA A 1 375 ? 106.435 164.995 129.232 1.00 60.30  ? 350 ALA A CA  1 
ATOM   2203  C  C   . ALA A 1 375 ? 105.827 165.226 127.856 1.00 62.72  ? 350 ALA A C   1 
ATOM   2204  O  O   . ALA A 1 375 ? 104.653 164.921 127.623 1.00 65.49  ? 350 ALA A O   1 
ATOM   2205  C  CB  . ALA A 1 375 ? 106.944 166.312 129.819 1.00 60.64  ? 350 ALA A CB  1 
ATOM   2206  N  N   . PHE A 1 376 ? 106.619 165.746 126.925 1.00 64.46  ? 351 PHE A N   1 
ATOM   2207  C  CA  . PHE A 1 376 ? 106.160 166.051 125.578 1.00 63.19  ? 351 PHE A CA  1 
ATOM   2208  C  C   . PHE A 1 376 ? 106.864 165.131 124.592 1.00 60.97  ? 351 PHE A C   1 
ATOM   2209  O  O   . PHE A 1 376 ? 108.095 165.147 124.493 1.00 68.24  ? 351 PHE A O   1 
ATOM   2210  C  CB  . PHE A 1 376 ? 106.424 167.515 125.235 1.00 66.14  ? 351 PHE A CB  1 
ATOM   2211  C  CG  . PHE A 1 376 ? 105.848 168.481 126.226 1.00 70.38  ? 351 PHE A CG  1 
ATOM   2212  C  CD1 . PHE A 1 376 ? 104.513 168.825 126.180 1.00 66.32  ? 351 PHE A CD1 1 
ATOM   2213  C  CD2 . PHE A 1 376 ? 106.644 169.044 127.204 1.00 67.32  ? 351 PHE A CD2 1 
ATOM   2214  C  CE1 . PHE A 1 376 ? 103.986 169.711 127.088 1.00 65.01  ? 351 PHE A CE1 1 
ATOM   2215  C  CE2 . PHE A 1 376 ? 106.119 169.930 128.114 1.00 64.26  ? 351 PHE A CE2 1 
ATOM   2216  C  CZ  . PHE A 1 376 ? 104.790 170.263 128.055 1.00 65.44  ? 351 PHE A CZ  1 
ATOM   2217  N  N   . GLY A 1 377 ? 106.082 164.345 123.861 1.00 45.58  ? 352 GLY A N   1 
ATOM   2218  C  CA  . GLY A 1 377 ? 106.601 163.411 122.895 1.00 44.13  ? 352 GLY A CA  1 
ATOM   2219  C  C   . GLY A 1 377 ? 105.498 162.936 121.977 1.00 50.07  ? 352 GLY A C   1 
ATOM   2220  O  O   . GLY A 1 377 ? 104.416 163.525 121.931 1.00 64.68  ? 352 GLY A O   1 
ATOM   2221  N  N   . PRO A 1 378 ? 105.745 161.869 121.222 1.00 36.38  ? 353 PRO A N   1 
ATOM   2222  C  CA  . PRO A 1 378 ? 104.706 161.348 120.331 1.00 36.00  ? 353 PRO A CA  1 
ATOM   2223  C  C   . PRO A 1 378 ? 103.475 160.928 121.115 1.00 43.41  ? 353 PRO A C   1 
ATOM   2224  O  O   . PRO A 1 378 ? 103.571 160.384 122.216 1.00 51.64  ? 353 PRO A O   1 
ATOM   2225  C  CB  . PRO A 1 378 ? 105.383 160.151 119.659 1.00 26.87  ? 353 PRO A CB  1 
ATOM   2226  C  CG  . PRO A 1 378 ? 106.831 160.414 119.797 1.00 35.09  ? 353 PRO A CG  1 
ATOM   2227  C  CD  . PRO A 1 378 ? 106.993 161.106 121.106 1.00 38.94  ? 353 PRO A CD  1 
ATOM   2228  N  N   . VAL A 1 379 ? 102.309 161.189 120.537 1.00 54.46  ? 354 VAL A N   1 
ATOM   2229  C  CA  . VAL A 1 379 ? 101.030 160.947 121.189 1.00 51.74  ? 354 VAL A CA  1 
ATOM   2230  C  C   . VAL A 1 379 ? 100.228 159.981 120.334 1.00 59.79  ? 354 VAL A C   1 
ATOM   2231  O  O   . VAL A 1 379 ? 100.237 160.076 119.103 1.00 66.95  ? 354 VAL A O   1 
ATOM   2232  C  CB  . VAL A 1 379 ? 100.250 162.258 121.410 1.00 59.06  ? 354 VAL A CB  1 
ATOM   2233  C  CG1 . VAL A 1 379 ? 99.051  162.014 122.298 1.00 65.82  ? 354 VAL A CG1 1 
ATOM   2234  C  CG2 . VAL A 1 379 ? 101.152 163.316 122.012 1.00 55.63  ? 354 VAL A CG2 1 
ATOM   2235  N  N   . VAL A 1 380 ? 99.543  159.046 120.988 1.00 60.53  ? 355 VAL A N   1 
ATOM   2236  C  CA  . VAL A 1 380 ? 98.695  158.074 120.302 1.00 64.67  ? 355 VAL A CA  1 
ATOM   2237  C  C   . VAL A 1 380 ? 97.353  158.752 120.037 1.00 70.19  ? 355 VAL A C   1 
ATOM   2238  O  O   . VAL A 1 380 ? 96.503  158.831 120.924 1.00 74.88  ? 355 VAL A O   1 
ATOM   2239  C  CB  . VAL A 1 380 ? 98.528  156.793 121.118 1.00 61.42  ? 355 VAL A CB  1 
ATOM   2240  C  CG1 . VAL A 1 380 ? 97.566  155.851 120.428 1.00 62.59  ? 355 VAL A CG1 1 
ATOM   2241  C  CG2 . VAL A 1 380 ? 99.870  156.129 121.327 1.00 65.36  ? 355 VAL A CG2 1 
ATOM   2242  N  N   . ASP A 1 381 ? 97.153  159.242 118.815 1.00 72.12  ? 356 ASP A N   1 
ATOM   2243  C  CA  . ASP A 1 381 ? 95.941  159.976 118.473 1.00 71.60  ? 356 ASP A CA  1 
ATOM   2244  C  C   . ASP A 1 381 ? 95.030  159.220 117.518 1.00 76.57  ? 356 ASP A C   1 
ATOM   2245  O  O   . ASP A 1 381 ? 93.851  159.020 117.821 1.00 83.86  ? 356 ASP A O   1 
ATOM   2246  C  CB  . ASP A 1 381 ? 96.301  161.347 117.880 1.00 74.03  ? 356 ASP A CB  1 
ATOM   2247  C  CG  . ASP A 1 381 ? 97.285  161.253 116.733 1.00 81.61  ? 356 ASP A CG  1 
ATOM   2248  O  OD1 . ASP A 1 381 ? 97.016  160.505 115.771 1.00 82.99  ? 356 ASP A OD1 1 
ATOM   2249  O  OD2 . ASP A 1 381 ? 98.328  161.936 116.788 1.00 82.84  ? 356 ASP A OD2 1 
ATOM   2250  N  N   . GLY A 1 382 ? 95.542  158.790 116.369 1.00 76.27  ? 357 GLY A N   1 
ATOM   2251  C  CA  . GLY A 1 382 ? 94.715  158.101 115.400 1.00 77.67  ? 357 GLY A CA  1 
ATOM   2252  C  C   . GLY A 1 382 ? 95.039  158.464 113.967 1.00 78.79  ? 357 GLY A C   1 
ATOM   2253  O  O   . GLY A 1 382 ? 94.680  157.733 113.040 1.00 78.21  ? 357 GLY A O   1 
ATOM   2254  N  N   . ASP A 1 383 ? 95.712  159.597 113.769 1.00 82.34  ? 358 ASP A N   1 
ATOM   2255  C  CA  . ASP A 1 383 ? 96.140  160.005 112.435 1.00 80.80  ? 358 ASP A CA  1 
ATOM   2256  C  C   . ASP A 1 383 ? 97.564  159.543 112.144 1.00 78.81  ? 358 ASP A C   1 
ATOM   2257  O  O   . ASP A 1 383 ? 97.794  158.768 111.211 1.00 78.86  ? 358 ASP A O   1 
ATOM   2258  C  CB  . ASP A 1 383 ? 96.033  161.527 112.285 1.00 82.16  ? 358 ASP A CB  1 
ATOM   2259  C  CG  . ASP A 1 383 ? 94.687  161.969 111.748 1.00 85.44  ? 358 ASP A CG  1 
ATOM   2260  O  OD1 . ASP A 1 383 ? 94.130  161.265 110.880 1.00 85.48  ? 358 ASP A OD1 1 
ATOM   2261  O  OD2 . ASP A 1 383 ? 94.188  163.025 112.193 1.00 83.84  ? 358 ASP A OD2 1 
ATOM   2262  N  N   . VAL A 1 384 ? 98.527  160.003 112.942 1.00 68.54  ? 359 VAL A N   1 
ATOM   2263  C  CA  . VAL A 1 384 ? 99.920  159.646 112.705 1.00 69.97  ? 359 VAL A CA  1 
ATOM   2264  C  C   . VAL A 1 384 ? 100.240 158.292 113.321 1.00 75.33  ? 359 VAL A C   1 
ATOM   2265  O  O   . VAL A 1 384 ? 100.759 157.396 112.647 1.00 83.65  ? 359 VAL A O   1 
ATOM   2266  C  CB  . VAL A 1 384 ? 100.854 160.746 113.236 1.00 71.48  ? 359 VAL A CB  1 
ATOM   2267  C  CG1 . VAL A 1 384 ? 102.200 160.661 112.549 1.00 72.32  ? 359 VAL A CG1 1 
ATOM   2268  C  CG2 . VAL A 1 384 ? 100.233 162.109 113.022 1.00 72.40  ? 359 VAL A CG2 1 
ATOM   2269  N  N   . VAL A 1 385 ? 99.939  158.115 114.602 1.00 70.27  ? 360 VAL A N   1 
ATOM   2270  C  CA  . VAL A 1 385 ? 100.095 156.814 115.245 1.00 71.74  ? 360 VAL A CA  1 
ATOM   2271  C  C   . VAL A 1 385 ? 98.700  156.289 115.562 1.00 72.21  ? 360 VAL A C   1 
ATOM   2272  O  O   . VAL A 1 385 ? 98.070  156.746 116.526 1.00 74.70  ? 360 VAL A O   1 
ATOM   2273  C  CB  . VAL A 1 385 ? 100.969 156.906 116.504 1.00 68.45  ? 360 VAL A CB  1 
ATOM   2274  C  CG1 . VAL A 1 385 ? 101.559 155.551 116.832 1.00 65.71  ? 360 VAL A CG1 1 
ATOM   2275  C  CG2 . VAL A 1 385 ? 102.067 157.930 116.309 1.00 66.14  ? 360 VAL A CG2 1 
ATOM   2276  N  N   . PRO A 1 386 ? 98.174  155.351 114.771 1.00 65.19  ? 361 PRO A N   1 
ATOM   2277  C  CA  . PRO A 1 386 ? 96.765  154.952 114.948 1.00 68.41  ? 361 PRO A CA  1 
ATOM   2278  C  C   . PRO A 1 386 ? 96.439  154.386 116.320 1.00 67.02  ? 361 PRO A C   1 
ATOM   2279  O  O   . PRO A 1 386 ? 95.378  154.695 116.876 1.00 67.29  ? 361 PRO A O   1 
ATOM   2280  C  CB  . PRO A 1 386 ? 96.566  153.912 113.837 1.00 71.35  ? 361 PRO A CB  1 
ATOM   2281  C  CG  . PRO A 1 386 ? 97.609  154.234 112.819 1.00 64.99  ? 361 PRO A CG  1 
ATOM   2282  C  CD  . PRO A 1 386 ? 98.790  154.716 113.596 1.00 59.59  ? 361 PRO A CD  1 
ATOM   2283  N  N   . ASP A 1 387 ? 97.316  153.565 116.887 1.00 70.60  ? 362 ASP A N   1 
ATOM   2284  C  CA  . ASP A 1 387 ? 97.020  152.876 118.136 1.00 70.53  ? 362 ASP A CA  1 
ATOM   2285  C  C   . ASP A 1 387 ? 98.299  152.780 118.958 1.00 73.62  ? 362 ASP A C   1 
ATOM   2286  O  O   . ASP A 1 387 ? 99.324  153.383 118.626 1.00 75.70  ? 362 ASP A O   1 
ATOM   2287  C  CB  . ASP A 1 387 ? 96.414  151.495 117.858 1.00 71.61  ? 362 ASP A CB  1 
ATOM   2288  C  CG  . ASP A 1 387 ? 95.146  151.247 118.639 1.00 78.01  ? 362 ASP A CG  1 
ATOM   2289  O  OD1 . ASP A 1 387 ? 94.842  152.049 119.547 1.00 81.13  ? 362 ASP A OD1 1 
ATOM   2290  O  OD2 . ASP A 1 387 ? 94.454  150.249 118.348 1.00 74.97  ? 362 ASP A OD2 1 
ATOM   2291  N  N   . ASP A 1 388 ? 98.231  152.022 120.042 1.00 66.88  ? 363 ASP A N   1 
ATOM   2292  C  CA  . ASP A 1 388 ? 99.410  151.768 120.851 1.00 62.37  ? 363 ASP A CA  1 
ATOM   2293  C  C   . ASP A 1 388 ? 100.445 151.027 120.009 1.00 63.38  ? 363 ASP A C   1 
ATOM   2294  O  O   . ASP A 1 388 ? 100.118 149.997 119.407 1.00 76.48  ? 363 ASP A O   1 
ATOM   2295  C  CB  . ASP A 1 388 ? 99.022  150.944 122.077 1.00 65.19  ? 363 ASP A CB  1 
ATOM   2296  C  CG  . ASP A 1 388 ? 100.140 150.829 123.090 1.00 73.36  ? 363 ASP A CG  1 
ATOM   2297  O  OD1 . ASP A 1 388 ? 101.149 151.546 122.957 1.00 73.07  ? 363 ASP A OD1 1 
ATOM   2298  O  OD2 . ASP A 1 388 ? 100.009 150.016 124.029 1.00 76.76  ? 363 ASP A OD2 1 
ATOM   2299  N  N   . PRO A 1 389 ? 101.683 151.519 119.921 1.00 47.96  ? 364 PRO A N   1 
ATOM   2300  C  CA  . PRO A 1 389 ? 102.677 150.837 119.077 1.00 48.34  ? 364 PRO A CA  1 
ATOM   2301  C  C   . PRO A 1 389 ? 102.922 149.389 119.456 1.00 50.93  ? 364 PRO A C   1 
ATOM   2302  O  O   . PRO A 1 389 ? 103.260 148.586 118.581 1.00 58.80  ? 364 PRO A O   1 
ATOM   2303  C  CB  . PRO A 1 389 ? 103.932 151.693 119.270 1.00 48.51  ? 364 PRO A CB  1 
ATOM   2304  C  CG  . PRO A 1 389 ? 103.403 153.044 119.547 1.00 57.96  ? 364 PRO A CG  1 
ATOM   2305  C  CD  . PRO A 1 389 ? 102.152 152.845 120.352 1.00 58.02  ? 364 PRO A CD  1 
ATOM   2306  N  N   . GLU A 1 390 ? 102.771 149.025 120.729 1.00 56.73  ? 365 GLU A N   1 
ATOM   2307  C  CA  . GLU A 1 390 ? 102.912 147.627 121.113 1.00 51.89  ? 365 GLU A CA  1 
ATOM   2308  C  C   . GLU A 1 390 ? 101.808 146.757 120.531 1.00 58.88  ? 365 GLU A C   1 
ATOM   2309  O  O   . GLU A 1 390 ? 102.001 145.547 120.386 1.00 63.83  ? 365 GLU A O   1 
ATOM   2310  C  CB  . GLU A 1 390 ? 102.921 147.499 122.635 1.00 58.31  ? 365 GLU A CB  1 
ATOM   2311  C  CG  . GLU A 1 390 ? 103.536 146.214 123.153 1.00 62.68  ? 365 GLU A CG  1 
ATOM   2312  C  CD  . GLU A 1 390 ? 103.868 146.289 124.629 1.00 66.44  ? 365 GLU A CD  1 
ATOM   2313  O  OE1 . GLU A 1 390 ? 103.774 147.393 125.205 1.00 65.97  ? 365 GLU A OE1 1 
ATOM   2314  O  OE2 . GLU A 1 390 ? 104.223 145.247 125.215 1.00 63.24  ? 365 GLU A OE2 1 
ATOM   2315  N  N   . ILE A 1 391 ? 100.663 147.346 120.198 1.00 70.01  ? 366 ILE A N   1 
ATOM   2316  C  CA  . ILE A 1 391 ? 99.552  146.594 119.628 1.00 67.06  ? 366 ILE A CA  1 
ATOM   2317  C  C   . ILE A 1 391 ? 99.563  146.636 118.102 1.00 65.34  ? 366 ILE A C   1 
ATOM   2318  O  O   . ILE A 1 391 ? 99.153  145.669 117.453 1.00 68.45  ? 366 ILE A O   1 
ATOM   2319  C  CB  . ILE A 1 391 ? 98.226  147.130 120.194 1.00 60.01  ? 366 ILE A CB  1 
ATOM   2320  C  CG1 . ILE A 1 391 ? 98.024  146.635 121.624 1.00 66.10  ? 366 ILE A CG1 1 
ATOM   2321  C  CG2 . ILE A 1 391 ? 97.050  146.727 119.330 1.00 56.85  ? 366 ILE A CG2 1 
ATOM   2322  C  CD1 . ILE A 1 391 ? 97.907  145.133 121.732 1.00 65.07  ? 366 ILE A CD1 1 
ATOM   2323  N  N   . LEU A 1 392 ? 100.047 147.730 117.512 1.00 61.65  ? 367 LEU A N   1 
ATOM   2324  C  CA  . LEU A 1 392 ? 100.033 147.857 116.060 1.00 54.08  ? 367 LEU A CA  1 
ATOM   2325  C  C   . LEU A 1 392 ? 100.935 146.826 115.397 1.00 59.50  ? 367 LEU A C   1 
ATOM   2326  O  O   . LEU A 1 392 ? 100.598 146.304 114.330 1.00 70.08  ? 367 LEU A O   1 
ATOM   2327  C  CB  . LEU A 1 392 ? 100.448 149.266 115.653 1.00 53.80  ? 367 LEU A CB  1 
ATOM   2328  C  CG  . LEU A 1 392 ? 99.348  150.313 115.771 1.00 57.33  ? 367 LEU A CG  1 
ATOM   2329  C  CD1 . LEU A 1 392 ? 99.787  151.607 115.133 1.00 63.25  ? 367 LEU A CD1 1 
ATOM   2330  C  CD2 . LEU A 1 392 ? 98.082  149.803 115.124 1.00 65.10  ? 367 LEU A CD2 1 
ATOM   2331  N  N   . MET A 1 393 ? 102.086 146.526 115.995 1.00 43.73  ? 368 MET A N   1 
ATOM   2332  C  CA  . MET A 1 393 ? 102.999 145.582 115.368 1.00 49.56  ? 368 MET A CA  1 
ATOM   2333  C  C   . MET A 1 393 ? 102.695 144.134 115.709 1.00 54.15  ? 368 MET A C   1 
ATOM   2334  O  O   . MET A 1 393 ? 103.170 143.239 115.004 1.00 63.77  ? 368 MET A O   1 
ATOM   2335  C  CB  . MET A 1 393 ? 104.452 145.892 115.738 1.00 49.18  ? 368 MET A CB  1 
ATOM   2336  C  CG  . MET A 1 393 ? 104.712 146.078 117.210 1.00 55.72  ? 368 MET A CG  1 
ATOM   2337  S  SD  . MET A 1 393 ? 106.314 146.834 117.524 1.00 70.63  ? 368 MET A SD  1 
ATOM   2338  C  CE  . MET A 1 393 ? 106.564 147.741 116.004 1.00 47.62  ? 368 MET A CE  1 
ATOM   2339  N  N   . GLN A 1 394 ? 101.920 143.872 116.761 1.00 55.93  ? 369 GLN A N   1 
ATOM   2340  C  CA  . GLN A 1 394 ? 101.484 142.502 117.006 1.00 61.39  ? 369 GLN A CA  1 
ATOM   2341  C  C   . GLN A 1 394 ? 100.497 142.037 115.947 1.00 61.57  ? 369 GLN A C   1 
ATOM   2342  O  O   . GLN A 1 394 ? 100.484 140.856 115.587 1.00 60.68  ? 369 GLN A O   1 
ATOM   2343  C  CB  . GLN A 1 394 ? 100.862 142.379 118.394 1.00 57.97  ? 369 GLN A CB  1 
ATOM   2344  C  CG  . GLN A 1 394 ? 101.852 142.044 119.484 1.00 54.90  ? 369 GLN A CG  1 
ATOM   2345  C  CD  . GLN A 1 394 ? 101.213 142.039 120.851 1.00 65.42  ? 369 GLN A CD  1 
ATOM   2346  O  OE1 . GLN A 1 394 ? 99.999  142.193 120.980 1.00 69.90  ? 369 GLN A OE1 1 
ATOM   2347  N  NE2 . GLN A 1 394 ? 102.027 141.864 121.885 1.00 64.09  ? 369 GLN A NE2 1 
ATOM   2348  N  N   . GLN A 1 395 ? 99.672  142.946 115.438 1.00 68.83  ? 370 GLN A N   1 
ATOM   2349  C  CA  . GLN A 1 395 ? 98.684  142.642 114.417 1.00 67.23  ? 370 GLN A CA  1 
ATOM   2350  C  C   . GLN A 1 395 ? 99.207  142.866 113.004 1.00 67.44  ? 370 GLN A C   1 
ATOM   2351  O  O   . GLN A 1 395 ? 98.436  142.763 112.048 1.00 66.31  ? 370 GLN A O   1 
ATOM   2352  C  CB  . GLN A 1 395 ? 97.425  143.477 114.649 1.00 59.67  ? 370 GLN A CB  1 
ATOM   2353  C  CG  . GLN A 1 395 ? 96.909  143.402 116.071 1.00 64.86  ? 370 GLN A CG  1 
ATOM   2354  C  CD  . GLN A 1 395 ? 95.727  144.314 116.310 1.00 74.99  ? 370 GLN A CD  1 
ATOM   2355  O  OE1 . GLN A 1 395 ? 95.696  145.446 115.832 1.00 76.90  ? 370 GLN A OE1 1 
ATOM   2356  N  NE2 . GLN A 1 395 ? 94.743  143.824 117.052 1.00 70.53  ? 370 GLN A NE2 1 
ATOM   2357  N  N   . GLY A 1 396 ? 100.491 143.170 112.853 1.00 59.43  ? 371 GLY A N   1 
ATOM   2358  C  CA  . GLY A 1 396 ? 101.092 143.303 111.542 1.00 57.17  ? 371 GLY A CA  1 
ATOM   2359  C  C   . GLY A 1 396 ? 100.611 144.479 110.722 1.00 60.59  ? 371 GLY A C   1 
ATOM   2360  O  O   . GLY A 1 396 ? 100.257 144.315 109.552 1.00 71.48  ? 371 GLY A O   1 
ATOM   2361  N  N   . GLU A 1 397 ? 100.590 145.669 111.316 1.00 58.70  ? 372 GLU A N   1 
ATOM   2362  C  CA  . GLU A 1 397 ? 100.199 146.884 110.604 1.00 60.37  ? 372 GLU A CA  1 
ATOM   2363  C  C   . GLU A 1 397 ? 101.438 147.665 110.164 1.00 60.75  ? 372 GLU A C   1 
ATOM   2364  O  O   . GLU A 1 397 ? 101.725 148.762 110.638 1.00 64.00  ? 372 GLU A O   1 
ATOM   2365  C  CB  . GLU A 1 397 ? 99.287  147.734 111.478 1.00 60.51  ? 372 GLU A CB  1 
ATOM   2366  C  CG  . GLU A 1 397 ? 98.092  146.983 112.009 1.00 66.51  ? 372 GLU A CG  1 
ATOM   2367  C  CD  . GLU A 1 397 ? 96.874  147.153 111.138 1.00 68.73  ? 372 GLU A CD  1 
ATOM   2368  O  OE1 . GLU A 1 397 ? 96.257  148.236 111.186 1.00 73.84  ? 372 GLU A OE1 1 
ATOM   2369  O  OE2 . GLU A 1 397 ? 96.531  146.204 110.405 1.00 68.24  ? 372 GLU A OE2 1 
ATOM   2370  N  N   . PHE A 1 398 ? 102.174 147.074 109.226 1.00 55.71  ? 373 PHE A N   1 
ATOM   2371  C  CA  . PHE A 1 398 ? 103.313 147.743 108.613 1.00 52.84  ? 373 PHE A CA  1 
ATOM   2372  C  C   . PHE A 1 398 ? 103.515 147.175 107.216 1.00 52.65  ? 373 PHE A C   1 
ATOM   2373  O  O   . PHE A 1 398 ? 102.975 146.123 106.872 1.00 62.57  ? 373 PHE A O   1 
ATOM   2374  C  CB  . PHE A 1 398 ? 104.585 147.606 109.458 1.00 56.94  ? 373 PHE A CB  1 
ATOM   2375  C  CG  . PHE A 1 398 ? 104.733 146.276 110.134 1.00 50.50  ? 373 PHE A CG  1 
ATOM   2376  C  CD1 . PHE A 1 398 ? 105.392 145.240 109.509 1.00 55.47  ? 373 PHE A CD1 1 
ATOM   2377  C  CD2 . PHE A 1 398 ? 104.233 146.071 111.402 1.00 45.18  ? 373 PHE A CD2 1 
ATOM   2378  C  CE1 . PHE A 1 398 ? 105.534 144.024 110.128 1.00 50.30  ? 373 PHE A CE1 1 
ATOM   2379  C  CE2 . PHE A 1 398 ? 104.374 144.856 112.023 1.00 49.40  ? 373 PHE A CE2 1 
ATOM   2380  C  CZ  . PHE A 1 398 ? 105.024 143.832 111.386 1.00 45.74  ? 373 PHE A CZ  1 
ATOM   2381  N  N   . LEU A 1 399 ? 104.302 147.884 106.410 1.00 42.91  ? 374 LEU A N   1 
ATOM   2382  C  CA  . LEU A 1 399 ? 104.381 147.638 104.973 1.00 54.00  ? 374 LEU A CA  1 
ATOM   2383  C  C   . LEU A 1 399 ? 105.694 146.994 104.540 1.00 66.90  ? 374 LEU A C   1 
ATOM   2384  O  O   . LEU A 1 399 ? 106.221 147.309 103.472 1.00 70.28  ? 374 LEU A O   1 
ATOM   2385  C  CB  . LEU A 1 399 ? 104.179 148.928 104.185 1.00 57.96  ? 374 LEU A CB  1 
ATOM   2386  C  CG  . LEU A 1 399 ? 102.776 149.366 103.784 1.00 55.47  ? 374 LEU A CG  1 
ATOM   2387  C  CD1 . LEU A 1 399 ? 102.019 149.878 104.983 1.00 60.83  ? 374 LEU A CD1 1 
ATOM   2388  C  CD2 . LEU A 1 399 ? 102.857 150.424 102.710 1.00 58.60  ? 374 LEU A CD2 1 
ATOM   2389  N  N   . ASN A 1 400 ? 106.233 146.078 105.344 1.00 64.96  ? 375 ASN A N   1 
ATOM   2390  C  CA  . ASN A 1 400 ? 107.366 145.245 104.935 1.00 66.42  ? 375 ASN A CA  1 
ATOM   2391  C  C   . ASN A 1 400 ? 108.567 146.128 104.565 1.00 71.86  ? 375 ASN A C   1 
ATOM   2392  O  O   . ASN A 1 400 ? 108.927 146.326 103.408 1.00 70.03  ? 375 ASN A O   1 
ATOM   2393  C  CB  . ASN A 1 400 ? 106.908 144.278 103.825 1.00 62.45  ? 375 ASN A CB  1 
ATOM   2394  C  CG  . ASN A 1 400 ? 108.045 143.676 103.005 1.00 67.24  ? 375 ASN A CG  1 
ATOM   2395  O  OD1 . ASN A 1 400 ? 108.601 144.304 102.108 1.00 64.90  ? 375 ASN A OD1 1 
ATOM   2396  N  ND2 . ASN A 1 400 ? 108.383 142.432 103.314 1.00 66.47  ? 375 ASN A ND2 1 
ATOM   2397  N  N   . TYR A 1 401 ? 109.109 146.760 105.602 1.00 56.14  ? 376 TYR A N   1 
ATOM   2398  C  CA  . TYR A 1 401 ? 110.327 147.550 105.487 1.00 40.75  ? 376 TYR A CA  1 
ATOM   2399  C  C   . TYR A 1 401 ? 111.514 146.721 105.959 1.00 52.07  ? 376 TYR A C   1 
ATOM   2400  O  O   . TYR A 1 401 ? 111.464 146.123 107.037 1.00 63.22  ? 376 TYR A O   1 
ATOM   2401  C  CB  . TYR A 1 401 ? 110.236 148.830 106.314 1.00 32.83  ? 376 TYR A CB  1 
ATOM   2402  C  CG  . TYR A 1 401 ? 109.144 149.782 105.900 1.00 43.58  ? 376 TYR A CG  1 
ATOM   2403  C  CD1 . TYR A 1 401 ? 109.294 150.598 104.795 1.00 54.10  ? 376 TYR A CD1 1 
ATOM   2404  C  CD2 . TYR A 1 401 ? 107.975 149.883 106.629 1.00 51.70  ? 376 TYR A CD2 1 
ATOM   2405  C  CE1 . TYR A 1 401 ? 108.303 151.477 104.420 1.00 49.54  ? 376 TYR A CE1 1 
ATOM   2406  C  CE2 . TYR A 1 401 ? 106.978 150.761 106.261 1.00 49.11  ? 376 TYR A CE2 1 
ATOM   2407  C  CZ  . TYR A 1 401 ? 107.149 151.554 105.157 1.00 45.99  ? 376 TYR A CZ  1 
ATOM   2408  O  OH  . TYR A 1 401 ? 106.159 152.430 104.787 1.00 51.04  ? 376 TYR A OH  1 
ATOM   2409  N  N   . ASP A 1 402 ? 112.574 146.686 105.153 1.00 55.86  ? 377 ASP A N   1 
ATOM   2410  C  CA  . ASP A 1 402 ? 113.803 146.025 105.572 1.00 52.03  ? 377 ASP A CA  1 
ATOM   2411  C  C   . ASP A 1 402 ? 114.383 146.738 106.783 1.00 51.78  ? 377 ASP A C   1 
ATOM   2412  O  O   . ASP A 1 402 ? 114.495 147.965 106.795 1.00 66.34  ? 377 ASP A O   1 
ATOM   2413  C  CB  . ASP A 1 402 ? 114.814 146.016 104.431 1.00 54.57  ? 377 ASP A CB  1 
ATOM   2414  C  CG  . ASP A 1 402 ? 114.259 145.396 103.173 1.00 66.40  ? 377 ASP A CG  1 
ATOM   2415  O  OD1 . ASP A 1 402 ? 113.090 144.963 103.198 1.00 69.63  ? 377 ASP A OD1 1 
ATOM   2416  O  OD2 . ASP A 1 402 ? 114.987 145.336 102.161 1.00 67.40  ? 377 ASP A OD2 1 
ATOM   2417  N  N   . MET A 1 403 ? 114.765 145.971 107.799 1.00 33.51  ? 378 MET A N   1 
ATOM   2418  C  CA  . MET A 1 403 ? 115.132 146.538 109.086 1.00 37.06  ? 378 MET A CA  1 
ATOM   2419  C  C   . MET A 1 403 ? 116.518 146.085 109.506 1.00 35.82  ? 378 MET A C   1 
ATOM   2420  O  O   . MET A 1 403 ? 116.906 144.938 109.279 1.00 47.74  ? 378 MET A O   1 
ATOM   2421  C  CB  . MET A 1 403 ? 114.120 146.153 110.164 1.00 33.68  ? 378 MET A CB  1 
ATOM   2422  C  CG  . MET A 1 403 ? 112.849 146.964 110.120 1.00 43.75  ? 378 MET A CG  1 
ATOM   2423  S  SD  . MET A 1 403 ? 112.924 148.394 111.210 1.00 66.04  ? 378 MET A SD  1 
ATOM   2424  C  CE  . MET A 1 403 ? 112.982 147.598 112.806 1.00 41.29  ? 378 MET A CE  1 
ATOM   2425  N  N   . LEU A 1 404 ? 117.253 146.993 110.140 1.00 19.09  ? 379 LEU A N   1 
ATOM   2426  C  CA  . LEU A 1 404 ? 118.558 146.704 110.728 1.00 22.61  ? 379 LEU A CA  1 
ATOM   2427  C  C   . LEU A 1 404 ? 118.528 147.258 112.148 1.00 37.56  ? 379 LEU A C   1 
ATOM   2428  O  O   . LEU A 1 404 ? 118.718 148.459 112.352 1.00 51.95  ? 379 LEU A O   1 
ATOM   2429  C  CB  . LEU A 1 404 ? 119.684 147.321 109.908 1.00 30.04  ? 379 LEU A CB  1 
ATOM   2430  C  CG  . LEU A 1 404 ? 121.120 146.857 110.143 1.00 24.45  ? 379 LEU A CG  1 
ATOM   2431  C  CD1 . LEU A 1 404 ? 121.892 146.897 108.847 1.00 27.87  ? 379 LEU A CD1 1 
ATOM   2432  C  CD2 . LEU A 1 404 ? 121.794 147.730 111.167 1.00 39.63  ? 379 LEU A CD2 1 
ATOM   2433  N  N   . ILE A 1 405 ? 118.287 146.389 113.120 1.00 17.91  ? 380 ILE A N   1 
ATOM   2434  C  CA  . ILE A 1 405 ? 118.164 146.789 114.509 1.00 12.12  ? 380 ILE A CA  1 
ATOM   2435  C  C   . ILE A 1 405 ? 119.462 146.467 115.230 1.00 29.07  ? 380 ILE A C   1 
ATOM   2436  O  O   . ILE A 1 405 ? 120.279 145.669 114.770 1.00 50.60  ? 380 ILE A O   1 
ATOM   2437  C  CB  . ILE A 1 405 ? 116.965 146.103 115.185 1.00 14.50  ? 380 ILE A CB  1 
ATOM   2438  C  CG1 . ILE A 1 405 ? 115.863 145.894 114.162 1.00 23.38  ? 380 ILE A CG1 1 
ATOM   2439  C  CG2 . ILE A 1 405 ? 116.432 146.947 116.316 1.00 27.09  ? 380 ILE A CG2 1 
ATOM   2440  C  CD1 . ILE A 1 405 ? 114.737 145.082 114.670 1.00 41.18  ? 380 ILE A CD1 1 
ATOM   2441  N  N   . GLY A 1 406 ? 119.659 147.093 116.383 1.00 33.59  ? 381 GLY A N   1 
ATOM   2442  C  CA  . GLY A 1 406 ? 120.910 146.909 117.089 1.00 34.40  ? 381 GLY A CA  1 
ATOM   2443  C  C   . GLY A 1 406 ? 120.851 147.368 118.524 1.00 37.95  ? 381 GLY A C   1 
ATOM   2444  O  O   . GLY A 1 406 ? 119.975 148.139 118.923 1.00 44.08  ? 381 GLY A O   1 
ATOM   2445  N  N   . VAL A 1 407 ? 121.810 146.873 119.298 1.00 51.44  ? 382 VAL A N   1 
ATOM   2446  C  CA  . VAL A 1 407 ? 121.877 147.112 120.735 1.00 32.33  ? 382 VAL A CA  1 
ATOM   2447  C  C   . VAL A 1 407 ? 123.340 147.214 121.145 1.00 43.29  ? 382 VAL A C   1 
ATOM   2448  O  O   . VAL A 1 407 ? 124.182 146.463 120.649 1.00 58.43  ? 382 VAL A O   1 
ATOM   2449  C  CB  . VAL A 1 407 ? 121.175 145.987 121.519 1.00 21.24  ? 382 VAL A CB  1 
ATOM   2450  C  CG1 . VAL A 1 407 ? 121.391 146.161 122.983 1.00 31.03  ? 382 VAL A CG1 1 
ATOM   2451  C  CG2 . VAL A 1 407 ? 119.698 145.966 121.224 1.00 40.04  ? 382 VAL A CG2 1 
ATOM   2452  N  N   . ASN A 1 408 ? 123.649 148.141 122.045 1.00 37.94  ? 383 ASN A N   1 
ATOM   2453  C  CA  . ASN A 1 408 ? 124.974 148.196 122.644 1.00 38.75  ? 383 ASN A CA  1 
ATOM   2454  C  C   . ASN A 1 408 ? 125.041 147.275 123.859 1.00 44.05  ? 383 ASN A C   1 
ATOM   2455  O  O   . ASN A 1 408 ? 124.019 146.874 124.415 1.00 53.36  ? 383 ASN A O   1 
ATOM   2456  C  CB  . ASN A 1 408 ? 125.330 149.624 123.046 1.00 38.58  ? 383 ASN A CB  1 
ATOM   2457  C  CG  . ASN A 1 408 ? 125.303 150.574 121.880 1.00 45.90  ? 383 ASN A CG  1 
ATOM   2458  O  OD1 . ASN A 1 408 ? 124.635 150.324 120.883 1.00 51.80  ? 383 ASN A OD1 1 
ATOM   2459  N  ND2 . ASN A 1 408 ? 126.030 151.672 121.995 1.00 46.42  ? 383 ASN A ND2 1 
ATOM   2460  N  N   . GLN A 1 409 ? 126.264 146.936 124.270 1.00 51.99  ? 384 GLN A N   1 
ATOM   2461  C  CA  . GLN A 1 409 ? 126.422 145.998 125.377 1.00 46.16  ? 384 GLN A CA  1 
ATOM   2462  C  C   . GLN A 1 409 ? 125.802 146.552 126.653 1.00 58.33  ? 384 GLN A C   1 
ATOM   2463  O  O   . GLN A 1 409 ? 124.847 145.983 127.191 1.00 68.42  ? 384 GLN A O   1 
ATOM   2464  C  CB  . GLN A 1 409 ? 127.897 145.659 125.597 1.00 55.06  ? 384 GLN A CB  1 
ATOM   2465  C  CG  . GLN A 1 409 ? 128.216 145.256 127.037 1.00 60.57  ? 384 GLN A CG  1 
ATOM   2466  C  CD  . GLN A 1 409 ? 129.488 144.458 127.175 1.00 63.22  ? 384 GLN A CD  1 
ATOM   2467  O  OE1 . GLN A 1 409 ? 130.543 144.861 126.698 1.00 61.13  ? 384 GLN A OE1 1 
ATOM   2468  N  NE2 . GLN A 1 409 ? 129.395 143.313 127.835 1.00 66.44  ? 384 GLN A NE2 1 
ATOM   2469  N  N   . GLY A 1 410 ? 126.333 147.662 127.157 1.00 48.12  ? 385 GLY A N   1 
ATOM   2470  C  CA  . GLY A 1 410 ? 125.763 148.259 128.345 1.00 47.43  ? 385 GLY A CA  1 
ATOM   2471  C  C   . GLY A 1 410 ? 125.368 149.701 128.140 1.00 48.28  ? 385 GLY A C   1 
ATOM   2472  O  O   . GLY A 1 410 ? 126.228 150.580 128.085 1.00 55.09  ? 385 GLY A O   1 
ATOM   2473  N  N   . GLU A 1 411 ? 124.066 149.967 128.075 1.00 44.83  ? 386 GLU A N   1 
ATOM   2474  C  CA  . GLU A 1 411 ? 123.575 151.311 127.826 1.00 40.88  ? 386 GLU A CA  1 
ATOM   2475  C  C   . GLU A 1 411 ? 123.008 151.993 129.055 1.00 44.10  ? 386 GLU A C   1 
ATOM   2476  O  O   . GLU A 1 411 ? 122.850 153.215 129.042 1.00 54.37  ? 386 GLU A O   1 
ATOM   2477  C  CB  . GLU A 1 411 ? 122.494 151.292 126.740 1.00 42.21  ? 386 GLU A CB  1 
ATOM   2478  C  CG  . GLU A 1 411 ? 122.642 150.176 125.746 1.00 46.76  ? 386 GLU A CG  1 
ATOM   2479  C  CD  . GLU A 1 411 ? 121.574 150.224 124.687 1.00 58.21  ? 386 GLU A CD  1 
ATOM   2480  O  OE1 . GLU A 1 411 ? 121.067 151.327 124.410 1.00 56.87  ? 386 GLU A OE1 1 
ATOM   2481  O  OE2 . GLU A 1 411 ? 121.240 149.164 124.129 1.00 64.09  ? 386 GLU A OE2 1 
ATOM   2482  N  N   . GLY A 1 412 ? 122.704 151.247 130.109 1.00 41.73  ? 387 GLY A N   1 
ATOM   2483  C  CA  . GLY A 1 412 ? 122.184 151.851 131.315 1.00 40.18  ? 387 GLY A CA  1 
ATOM   2484  C  C   . GLY A 1 412 ? 123.296 152.399 132.176 1.00 46.57  ? 387 GLY A C   1 
ATOM   2485  O  O   . GLY A 1 412 ? 123.196 152.407 133.404 1.00 57.43  ? 387 GLY A O   1 
ATOM   2486  N  N   . LEU A 1 413 ? 124.363 152.874 131.531 1.00 42.58  ? 388 LEU A N   1 
ATOM   2487  C  CA  . LEU A 1 413 ? 125.523 153.376 132.253 1.00 41.65  ? 388 LEU A CA  1 
ATOM   2488  C  C   . LEU A 1 413 ? 125.172 154.537 133.169 1.00 48.77  ? 388 LEU A C   1 
ATOM   2489  O  O   . LEU A 1 413 ? 125.883 154.775 134.150 1.00 60.09  ? 388 LEU A O   1 
ATOM   2490  C  CB  . LEU A 1 413 ? 126.608 153.790 131.260 1.00 43.80  ? 388 LEU A CB  1 
ATOM   2491  C  CG  . LEU A 1 413 ? 127.911 154.330 131.840 1.00 41.88  ? 388 LEU A CG  1 
ATOM   2492  C  CD1 . LEU A 1 413 ? 128.491 153.335 132.814 1.00 49.85  ? 388 LEU A CD1 1 
ATOM   2493  C  CD2 . LEU A 1 413 ? 128.894 154.610 130.732 1.00 46.84  ? 388 LEU A CD2 1 
ATOM   2494  N  N   . LYS A 1 414 ? 124.090 155.253 132.886 1.00 46.07  ? 389 LYS A N   1 
ATOM   2495  C  CA  . LYS A 1 414 ? 123.642 156.330 133.753 1.00 45.99  ? 389 LYS A CA  1 
ATOM   2496  C  C   . LYS A 1 414 ? 122.659 155.868 134.820 1.00 48.85  ? 389 LYS A C   1 
ATOM   2497  O  O   . LYS A 1 414 ? 122.303 156.664 135.694 1.00 56.44  ? 389 LYS A O   1 
ATOM   2498  C  CB  . LYS A 1 414 ? 123.018 157.443 132.916 1.00 47.90  ? 389 LYS A CB  1 
ATOM   2499  C  CG  . LYS A 1 414 ? 123.743 157.673 131.609 1.00 47.51  ? 389 LYS A CG  1 
ATOM   2500  C  CD  . LYS A 1 414 ? 123.239 158.913 130.911 1.00 51.88  ? 389 LYS A CD  1 
ATOM   2501  C  CE  . LYS A 1 414 ? 123.921 160.152 131.447 1.00 54.87  ? 389 LYS A CE  1 
ATOM   2502  N  NZ  . LYS A 1 414 ? 123.089 161.354 131.199 1.00 56.04  ? 389 LYS A NZ  1 
ATOM   2503  N  N   . PHE A 1 415 ? 122.204 154.614 134.769 1.00 43.59  ? 390 PHE A N   1 
ATOM   2504  C  CA  . PHE A 1 415 ? 121.463 154.058 135.897 1.00 40.31  ? 390 PHE A CA  1 
ATOM   2505  C  C   . PHE A 1 415 ? 122.350 153.972 137.127 1.00 52.28  ? 390 PHE A C   1 
ATOM   2506  O  O   . PHE A 1 415 ? 121.929 154.323 138.235 1.00 60.86  ? 390 PHE A O   1 
ATOM   2507  C  CB  . PHE A 1 415 ? 120.920 152.676 135.542 1.00 34.11  ? 390 PHE A CB  1 
ATOM   2508  C  CG  . PHE A 1 415 ? 119.956 152.118 136.551 1.00 38.79  ? 390 PHE A CG  1 
ATOM   2509  C  CD1 . PHE A 1 415 ? 119.071 152.942 137.216 1.00 47.74  ? 390 PHE A CD1 1 
ATOM   2510  C  CD2 . PHE A 1 415 ? 119.930 150.763 136.827 1.00 40.73  ? 390 PHE A CD2 1 
ATOM   2511  C  CE1 . PHE A 1 415 ? 118.182 152.424 138.133 1.00 52.67  ? 390 PHE A CE1 1 
ATOM   2512  C  CE2 . PHE A 1 415 ? 119.043 150.243 137.742 1.00 35.79  ? 390 PHE A CE2 1 
ATOM   2513  C  CZ  . PHE A 1 415 ? 118.171 151.072 138.395 1.00 45.78  ? 390 PHE A CZ  1 
ATOM   2514  N  N   . VAL A 1 416 ? 123.582 153.510 136.949 1.00 59.04  ? 391 VAL A N   1 
ATOM   2515  C  CA  . VAL A 1 416 ? 124.563 153.435 138.027 1.00 55.75  ? 391 VAL A CA  1 
ATOM   2516  C  C   . VAL A 1 416 ? 125.502 154.631 137.864 1.00 59.73  ? 391 VAL A C   1 
ATOM   2517  O  O   . VAL A 1 416 ? 126.536 154.582 137.198 1.00 61.92  ? 391 VAL A O   1 
ATOM   2518  C  CB  . VAL A 1 416 ? 125.272 152.079 138.051 1.00 53.10  ? 391 VAL A CB  1 
ATOM   2519  C  CG1 . VAL A 1 416 ? 124.238 150.993 138.104 1.00 57.13  ? 391 VAL A CG1 1 
ATOM   2520  C  CG2 . VAL A 1 416 ? 126.071 151.832 136.784 1.00 47.07  ? 391 VAL A CG2 1 
ATOM   2521  N  N   . GLU A 1 417 ? 125.123 155.742 138.483 1.00 72.86  ? 392 GLU A N   1 
ATOM   2522  C  CA  . GLU A 1 417 ? 125.928 156.953 138.461 1.00 73.36  ? 392 GLU A CA  1 
ATOM   2523  C  C   . GLU A 1 417 ? 126.258 157.482 139.843 1.00 75.78  ? 392 GLU A C   1 
ATOM   2524  O  O   . GLU A 1 417 ? 127.348 158.024 140.035 1.00 74.95  ? 392 GLU A O   1 
ATOM   2525  C  CB  . GLU A 1 417 ? 125.219 158.059 137.663 1.00 72.27  ? 392 GLU A CB  1 
ATOM   2526  N  N   . ASP A 1 418 ? 125.352 157.338 140.811 1.00 90.33  ? 393 ASP A N   1 
ATOM   2527  C  CA  . ASP A 1 418 ? 125.654 157.712 142.185 1.00 92.23  ? 393 ASP A CA  1 
ATOM   2528  C  C   . ASP A 1 418 ? 126.684 156.794 142.828 1.00 93.04  ? 393 ASP A C   1 
ATOM   2529  O  O   . ASP A 1 418 ? 127.219 157.136 143.887 1.00 93.28  ? 393 ASP A O   1 
ATOM   2530  C  CB  . ASP A 1 418 ? 124.372 157.715 143.018 1.00 91.38  ? 393 ASP A CB  1 
ATOM   2531  N  N   . SER A 1 419 ? 126.971 155.644 142.216 1.00 90.14  ? 394 SER A N   1 
ATOM   2532  C  CA  . SER A 1 419 ? 127.931 154.683 142.746 1.00 88.55  ? 394 SER A CA  1 
ATOM   2533  C  C   . SER A 1 419 ? 129.078 154.428 141.775 1.00 88.63  ? 394 SER A C   1 
ATOM   2534  O  O   . SER A 1 419 ? 129.769 153.412 141.892 1.00 87.76  ? 394 SER A O   1 
ATOM   2535  C  CB  . SER A 1 419 ? 127.231 153.370 143.089 1.00 86.15  ? 394 SER A CB  1 
ATOM   2536  O  OG  . SER A 1 419 ? 126.820 152.703 141.910 1.00 81.42  ? 394 SER A OG  1 
ATOM   2537  N  N   . ALA A 1 420 ? 129.288 155.323 140.815 1.00 97.28  ? 395 ALA A N   1 
ATOM   2538  C  CA  . ALA A 1 420 ? 130.357 155.182 139.837 1.00 98.88  ? 395 ALA A CA  1 
ATOM   2539  C  C   . ALA A 1 420 ? 131.674 155.779 140.311 1.00 100.69 ? 395 ALA A C   1 
ATOM   2540  O  O   . ALA A 1 420 ? 132.658 155.745 139.565 1.00 100.70 ? 395 ALA A O   1 
ATOM   2541  C  CB  . ALA A 1 420 ? 129.947 155.826 138.511 1.00 97.22  ? 395 ALA A CB  1 
ATOM   2542  N  N   . GLU A 1 421 ? 131.714 156.328 141.522 1.00 102.71 ? 396 GLU A N   1 
ATOM   2543  C  CA  . GLU A 1 421 ? 132.917 156.912 142.105 1.00 100.34 ? 396 GLU A CA  1 
ATOM   2544  C  C   . GLU A 1 421 ? 133.184 156.301 143.474 1.00 99.78  ? 396 GLU A C   1 
ATOM   2545  O  O   . GLU A 1 421 ? 133.454 156.994 144.456 1.00 100.53 ? 396 GLU A O   1 
ATOM   2546  C  CB  . GLU A 1 421 ? 132.798 158.430 142.200 1.00 97.96  ? 396 GLU A CB  1 
ATOM   2547  N  N   . SER A 1 422 ? 133.097 154.975 143.550 1.00 101.07 ? 397 SER A N   1 
ATOM   2548  C  CA  . SER A 1 422 ? 133.390 154.237 144.768 1.00 104.26 ? 397 SER A CA  1 
ATOM   2549  C  C   . SER A 1 422 ? 134.404 153.146 144.463 1.00 105.61 ? 397 SER A C   1 
ATOM   2550  O  O   . SER A 1 422 ? 134.451 152.614 143.350 1.00 101.73 ? 397 SER A O   1 
ATOM   2551  C  CB  . SER A 1 422 ? 132.126 153.615 145.377 1.00 100.41 ? 397 SER A CB  1 
ATOM   2552  O  OG  . SER A 1 422 ? 131.440 154.546 146.195 1.00 99.34  ? 397 SER A OG  1 
ATOM   2553  N  N   . GLU A 1 423 ? 135.228 152.825 145.464 1.00 110.83 ? 398 GLU A N   1 
ATOM   2554  C  CA  . GLU A 1 423 ? 136.223 151.773 145.289 1.00 108.99 ? 398 GLU A CA  1 
ATOM   2555  C  C   . GLU A 1 423 ? 135.559 150.430 145.020 1.00 110.15 ? 398 GLU A C   1 
ATOM   2556  O  O   . GLU A 1 423 ? 135.974 149.691 144.120 1.00 109.14 ? 398 GLU A O   1 
ATOM   2557  C  CB  . GLU A 1 423 ? 137.123 151.692 146.522 1.00 106.12 ? 398 GLU A CB  1 
ATOM   2558  N  N   . ASP A 1 424 ? 134.521 150.102 145.783 1.00 103.25 ? 399 ASP A N   1 
ATOM   2559  C  CA  . ASP A 1 424 ? 133.738 148.898 145.567 1.00 100.68 ? 399 ASP A CA  1 
ATOM   2560  C  C   . ASP A 1 424 ? 132.467 149.246 144.799 1.00 98.70  ? 399 ASP A C   1 
ATOM   2561  O  O   . ASP A 1 424 ? 132.221 150.398 144.437 1.00 97.25  ? 399 ASP A O   1 
ATOM   2562  C  CB  . ASP A 1 424 ? 133.417 148.219 146.901 1.00 99.91  ? 399 ASP A CB  1 
ATOM   2563  C  CG  . ASP A 1 424 ? 132.784 149.166 147.900 1.00 103.27 ? 399 ASP A CG  1 
ATOM   2564  O  OD1 . ASP A 1 424 ? 133.220 150.334 147.972 1.00 103.87 ? 399 ASP A OD1 1 
ATOM   2565  O  OD2 . ASP A 1 424 ? 131.852 148.741 148.616 1.00 102.07 ? 399 ASP A OD2 1 
ATOM   2566  N  N   . GLY A 1 425 ? 131.645 148.234 144.551 1.00 87.38  ? 400 GLY A N   1 
ATOM   2567  C  CA  . GLY A 1 425 ? 130.423 148.445 143.805 1.00 87.18  ? 400 GLY A CA  1 
ATOM   2568  C  C   . GLY A 1 425 ? 129.320 149.029 144.659 1.00 87.55  ? 400 GLY A C   1 
ATOM   2569  O  O   . GLY A 1 425 ? 129.562 149.937 145.459 1.00 88.54  ? 400 GLY A O   1 
ATOM   2570  N  N   . VAL A 1 426 ? 128.105 148.524 144.498 1.00 70.00  ? 401 VAL A N   1 
ATOM   2571  C  CA  . VAL A 1 426 ? 126.966 148.969 145.288 1.00 68.93  ? 401 VAL A CA  1 
ATOM   2572  C  C   . VAL A 1 426 ? 126.754 147.982 146.425 1.00 70.00  ? 401 VAL A C   1 
ATOM   2573  O  O   . VAL A 1 426 ? 127.010 146.780 146.280 1.00 69.96  ? 401 VAL A O   1 
ATOM   2574  C  CB  . VAL A 1 426 ? 125.703 149.118 144.417 1.00 68.77  ? 401 VAL A CB  1 
ATOM   2575  C  CG1 . VAL A 1 426 ? 126.050 149.794 143.108 1.00 70.78  ? 401 VAL A CG1 1 
ATOM   2576  C  CG2 . VAL A 1 426 ? 125.051 147.776 144.160 1.00 67.74  ? 401 VAL A CG2 1 
ATOM   2577  N  N   . SER A 1 427 ? 126.325 148.494 147.572 1.00 69.59  ? 402 SER A N   1 
ATOM   2578  C  CA  . SER A 1 427 ? 126.115 147.654 148.738 1.00 69.81  ? 402 SER A CA  1 
ATOM   2579  C  C   . SER A 1 427 ? 124.808 146.879 148.613 1.00 68.31  ? 402 SER A C   1 
ATOM   2580  O  O   . SER A 1 427 ? 123.876 147.289 147.918 1.00 77.16  ? 402 SER A O   1 
ATOM   2581  C  CB  . SER A 1 427 ? 126.104 148.498 150.012 1.00 74.57  ? 402 SER A CB  1 
ATOM   2582  O  OG  . SER A 1 427 ? 127.275 149.289 150.108 1.00 78.87  ? 402 SER A OG  1 
ATOM   2583  N  N   . ALA A 1 428 ? 124.747 145.743 149.311 1.00 61.34  ? 403 ALA A N   1 
ATOM   2584  C  CA  . ALA A 1 428 ? 123.533 144.935 149.302 1.00 61.57  ? 403 ALA A CA  1 
ATOM   2585  C  C   . ALA A 1 428 ? 122.344 145.707 149.848 1.00 63.63  ? 403 ALA A C   1 
ATOM   2586  O  O   . ALA A 1 428 ? 121.199 145.427 149.477 1.00 61.60  ? 403 ALA A O   1 
ATOM   2587  C  CB  . ALA A 1 428 ? 123.743 143.656 150.110 1.00 64.79  ? 403 ALA A CB  1 
ATOM   2588  N  N   . SER A 1 429 ? 122.589 146.670 150.735 1.00 73.91  ? 404 SER A N   1 
ATOM   2589  C  CA  . SER A 1 429 ? 121.506 147.514 151.223 1.00 74.13  ? 404 SER A CA  1 
ATOM   2590  C  C   . SER A 1 429 ? 121.058 148.514 150.168 1.00 71.92  ? 404 SER A C   1 
ATOM   2591  O  O   . SER A 1 429 ? 119.918 148.990 150.214 1.00 72.47  ? 404 SER A O   1 
ATOM   2592  C  CB  . SER A 1 429 ? 121.940 148.241 152.495 1.00 78.18  ? 404 SER A CB  1 
ATOM   2593  O  OG  . SER A 1 429 ? 122.464 147.333 153.448 1.00 79.17  ? 404 SER A OG  1 
ATOM   2594  N  N   . ALA A 1 430 ? 121.933 148.849 149.218 1.00 70.38  ? 405 ALA A N   1 
ATOM   2595  C  CA  . ALA A 1 430 ? 121.583 149.771 148.146 1.00 68.71  ? 405 ALA A CA  1 
ATOM   2596  C  C   . ALA A 1 430 ? 121.163 149.067 146.865 1.00 68.25  ? 405 ALA A C   1 
ATOM   2597  O  O   . ALA A 1 430 ? 120.432 149.657 146.065 1.00 67.87  ? 405 ALA A O   1 
ATOM   2598  C  CB  . ALA A 1 430 ? 122.757 150.705 147.843 1.00 60.85  ? 405 ALA A CB  1 
ATOM   2599  N  N   . PHE A 1 431 ? 121.601 147.827 146.650 1.00 62.68  ? 406 PHE A N   1 
ATOM   2600  C  CA  . PHE A 1 431 ? 121.116 147.061 145.511 1.00 47.12  ? 406 PHE A CA  1 
ATOM   2601  C  C   . PHE A 1 431 ? 119.657 146.675 145.683 1.00 53.22  ? 406 PHE A C   1 
ATOM   2602  O  O   . PHE A 1 431 ? 118.948 146.492 144.690 1.00 65.98  ? 406 PHE A O   1 
ATOM   2603  C  CB  . PHE A 1 431 ? 121.975 145.813 145.314 1.00 54.78  ? 406 PHE A CB  1 
ATOM   2604  C  CG  . PHE A 1 431 ? 121.432 144.850 144.299 1.00 58.00  ? 406 PHE A CG  1 
ATOM   2605  C  CD1 . PHE A 1 431 ? 121.648 145.050 142.949 1.00 58.60  ? 406 PHE A CD1 1 
ATOM   2606  C  CD2 . PHE A 1 431 ? 120.724 143.732 144.694 1.00 57.66  ? 406 PHE A CD2 1 
ATOM   2607  C  CE1 . PHE A 1 431 ? 121.158 144.163 142.016 1.00 49.23  ? 406 PHE A CE1 1 
ATOM   2608  C  CE2 . PHE A 1 431 ? 120.235 142.845 143.763 1.00 59.40  ? 406 PHE A CE2 1 
ATOM   2609  C  CZ  . PHE A 1 431 ? 120.452 143.063 142.425 1.00 55.00  ? 406 PHE A CZ  1 
ATOM   2610  N  N   . ASP A 1 432 ? 119.195 146.543 146.924 1.00 65.84  ? 407 ASP A N   1 
ATOM   2611  C  CA  . ASP A 1 432 ? 117.784 146.306 147.193 1.00 65.12  ? 407 ASP A CA  1 
ATOM   2612  C  C   . ASP A 1 432 ? 116.963 147.584 147.148 1.00 63.12  ? 407 ASP A C   1 
ATOM   2613  O  O   . ASP A 1 432 ? 115.733 147.514 147.216 1.00 62.94  ? 407 ASP A O   1 
ATOM   2614  C  CB  . ASP A 1 432 ? 117.611 145.644 148.561 1.00 70.92  ? 407 ASP A CB  1 
ATOM   2615  C  CG  . ASP A 1 432 ? 117.913 144.160 148.534 1.00 78.96  ? 407 ASP A CG  1 
ATOM   2616  O  OD1 . ASP A 1 432 ? 118.145 143.618 147.434 1.00 79.33  ? 407 ASP A OD1 1 
ATOM   2617  O  OD2 . ASP A 1 432 ? 117.918 143.534 149.615 1.00 78.59  ? 407 ASP A OD2 1 
ATOM   2618  N  N   . PHE A 1 433 ? 117.614 148.741 147.041 1.00 60.59  ? 408 PHE A N   1 
ATOM   2619  C  CA  . PHE A 1 433 ? 116.945 150.034 147.017 1.00 60.17  ? 408 PHE A CA  1 
ATOM   2620  C  C   . PHE A 1 433 ? 116.702 150.519 145.593 1.00 68.85  ? 408 PHE A C   1 
ATOM   2621  O  O   . PHE A 1 433 ? 115.598 150.969 145.268 1.00 70.37  ? 408 PHE A O   1 
ATOM   2622  C  CB  . PHE A 1 433 ? 117.777 151.059 147.792 1.00 59.91  ? 408 PHE A CB  1 
ATOM   2623  C  CG  . PHE A 1 433 ? 117.039 152.323 148.115 1.00 68.02  ? 408 PHE A CG  1 
ATOM   2624  C  CD1 . PHE A 1 433 ? 115.663 152.323 148.250 1.00 69.34  ? 408 PHE A CD1 1 
ATOM   2625  C  CD2 . PHE A 1 433 ? 117.724 153.513 148.285 1.00 69.35  ? 408 PHE A CD2 1 
ATOM   2626  C  CE1 . PHE A 1 433 ? 114.984 153.487 148.549 1.00 67.96  ? 408 PHE A CE1 1 
ATOM   2627  C  CE2 . PHE A 1 433 ? 117.051 154.678 148.583 1.00 66.14  ? 408 PHE A CE2 1 
ATOM   2628  C  CZ  . PHE A 1 433 ? 115.679 154.665 148.715 1.00 65.42  ? 408 PHE A CZ  1 
ATOM   2629  N  N   . THR A 1 434 ? 117.724 150.437 144.736 1.00 63.75  ? 409 THR A N   1 
ATOM   2630  C  CA  . THR A 1 434 ? 117.548 150.836 143.344 1.00 56.30  ? 409 THR A CA  1 
ATOM   2631  C  C   . THR A 1 434 ? 116.537 149.946 142.640 1.00 58.49  ? 409 THR A C   1 
ATOM   2632  O  O   . THR A 1 434 ? 115.734 150.431 141.842 1.00 65.43  ? 409 THR A O   1 
ATOM   2633  C  CB  . THR A 1 434 ? 118.877 150.798 142.599 1.00 49.56  ? 409 THR A CB  1 
ATOM   2634  O  OG1 . THR A 1 434 ? 119.192 149.442 142.275 1.00 54.40  ? 409 THR A OG1 1 
ATOM   2635  C  CG2 . THR A 1 434 ? 119.982 151.386 143.444 1.00 56.99  ? 409 THR A CG2 1 
ATOM   2636  N  N   . VAL A 1 435 ? 116.561 148.641 142.916 1.00 46.42  ? 410 VAL A N   1 
ATOM   2637  C  CA  . VAL A 1 435 ? 115.593 147.740 142.297 1.00 44.49  ? 410 VAL A CA  1 
ATOM   2638  C  C   . VAL A 1 435 ? 114.180 148.059 142.771 1.00 51.79  ? 410 VAL A C   1 
ATOM   2639  O  O   . VAL A 1 435 ? 113.226 148.035 141.983 1.00 62.91  ? 410 VAL A O   1 
ATOM   2640  C  CB  . VAL A 1 435 ? 115.968 146.276 142.576 1.00 36.88  ? 410 VAL A CB  1 
ATOM   2641  C  CG1 . VAL A 1 435 ? 114.908 145.355 142.035 1.00 38.04  ? 410 VAL A CG1 1 
ATOM   2642  C  CG2 . VAL A 1 435 ? 117.299 145.954 141.945 1.00 41.89  ? 410 VAL A CG2 1 
ATOM   2643  N  N   . SER A 1 436 ? 114.016 148.354 144.062 1.00 53.91  ? 411 SER A N   1 
ATOM   2644  C  CA  . SER A 1 436 ? 112.691 148.694 144.571 1.00 55.43  ? 411 SER A CA  1 
ATOM   2645  C  C   . SER A 1 436 ? 112.177 149.991 143.961 1.00 59.43  ? 411 SER A C   1 
ATOM   2646  O  O   . SER A 1 436 ? 111.003 150.085 143.588 1.00 67.18  ? 411 SER A O   1 
ATOM   2647  C  CB  . SER A 1 436 ? 112.719 148.795 146.093 1.00 63.05  ? 411 SER A CB  1 
ATOM   2648  O  OG  . SER A 1 436 ? 111.445 148.506 146.635 1.00 65.10  ? 411 SER A OG  1 
ATOM   2649  N  N   . ASN A 1 437 ? 113.038 151.005 143.851 1.00 55.61  ? 412 ASN A N   1 
ATOM   2650  C  CA  . ASN A 1 437 ? 112.629 152.244 143.195 1.00 61.77  ? 412 ASN A CA  1 
ATOM   2651  C  C   . ASN A 1 437 ? 112.317 152.008 141.723 1.00 64.26  ? 412 ASN A C   1 
ATOM   2652  O  O   . ASN A 1 437 ? 111.377 152.593 141.177 1.00 68.74  ? 412 ASN A O   1 
ATOM   2653  C  CB  . ASN A 1 437 ? 113.716 153.305 143.348 1.00 60.85  ? 412 ASN A CB  1 
ATOM   2654  C  CG  . ASN A 1 437 ? 113.827 153.821 144.765 1.00 67.27  ? 412 ASN A CG  1 
ATOM   2655  O  OD1 . ASN A 1 437 ? 112.829 154.193 145.382 1.00 71.70  ? 412 ASN A OD1 1 
ATOM   2656  N  ND2 . ASN A 1 437 ? 115.044 153.850 145.291 1.00 65.81  ? 412 ASN A ND2 1 
ATOM   2657  N  N   . PHE A 1 438 ? 113.101 151.153 141.069 1.00 50.69  ? 413 PHE A N   1 
ATOM   2658  C  CA  . PHE A 1 438 ? 112.864 150.787 139.680 1.00 42.12  ? 413 PHE A CA  1 
ATOM   2659  C  C   . PHE A 1 438 ? 111.472 150.194 139.500 1.00 50.02  ? 413 PHE A C   1 
ATOM   2660  O  O   . PHE A 1 438 ? 110.705 150.624 138.629 1.00 59.64  ? 413 PHE A O   1 
ATOM   2661  C  CB  . PHE A 1 438 ? 113.965 149.808 139.263 1.00 45.05  ? 413 PHE A CB  1 
ATOM   2662  C  CG  . PHE A 1 438 ? 113.725 149.092 137.972 1.00 47.28  ? 413 PHE A CG  1 
ATOM   2663  C  CD1 . PHE A 1 438 ? 113.054 147.888 137.949 1.00 46.28  ? 413 PHE A CD1 1 
ATOM   2664  C  CD2 . PHE A 1 438 ? 114.240 149.585 136.793 1.00 48.78  ? 413 PHE A CD2 1 
ATOM   2665  C  CE1 . PHE A 1 438 ? 112.861 147.219 136.772 1.00 42.40  ? 413 PHE A CE1 1 
ATOM   2666  C  CE2 . PHE A 1 438 ? 114.051 148.916 135.614 1.00 46.78  ? 413 PHE A CE2 1 
ATOM   2667  C  CZ  . PHE A 1 438 ? 113.361 147.733 135.605 1.00 44.97  ? 413 PHE A CZ  1 
ATOM   2668  N  N   . VAL A 1 439 ? 111.121 149.216 140.335 1.00 52.12  ? 414 VAL A N   1 
ATOM   2669  C  CA  . VAL A 1 439 ? 109.805 148.593 140.236 1.00 51.01  ? 414 VAL A CA  1 
ATOM   2670  C  C   . VAL A 1 439 ? 108.708 149.598 140.569 1.00 57.39  ? 414 VAL A C   1 
ATOM   2671  O  O   . VAL A 1 439 ? 107.670 149.647 139.898 1.00 64.60  ? 414 VAL A O   1 
ATOM   2672  C  CB  . VAL A 1 439 ? 109.732 147.347 141.134 1.00 44.19  ? 414 VAL A CB  1 
ATOM   2673  C  CG1 . VAL A 1 439 ? 108.297 146.911 141.320 1.00 53.16  ? 414 VAL A CG1 1 
ATOM   2674  C  CG2 . VAL A 1 439 ? 110.533 146.230 140.525 1.00 46.12  ? 414 VAL A CG2 1 
ATOM   2675  N  N   . ASP A 1 440 ? 108.916 150.421 141.600 1.00 62.21  ? 415 ASP A N   1 
ATOM   2676  C  CA  . ASP A 1 440 ? 107.913 151.414 141.968 1.00 66.65  ? 415 ASP A CA  1 
ATOM   2677  C  C   . ASP A 1 440 ? 107.680 152.422 140.851 1.00 70.88  ? 415 ASP A C   1 
ATOM   2678  O  O   . ASP A 1 440 ? 106.560 152.917 140.687 1.00 74.52  ? 415 ASP A O   1 
ATOM   2679  C  CB  . ASP A 1 440 ? 108.339 152.138 143.244 1.00 67.38  ? 415 ASP A CB  1 
ATOM   2680  C  CG  . ASP A 1 440 ? 107.696 151.561 144.485 1.00 76.77  ? 415 ASP A CG  1 
ATOM   2681  O  OD1 . ASP A 1 440 ? 106.749 150.759 144.347 1.00 80.95  ? 415 ASP A OD1 1 
ATOM   2682  O  OD2 . ASP A 1 440 ? 108.135 151.910 145.601 1.00 75.33  ? 415 ASP A OD2 1 
ATOM   2683  N  N   . ASN A 1 441 ? 108.717 152.738 140.078 1.00 60.69  ? 416 ASN A N   1 
ATOM   2684  C  CA  . ASN A 1 441 ? 108.610 153.743 139.032 1.00 54.87  ? 416 ASN A CA  1 
ATOM   2685  C  C   . ASN A 1 441 ? 108.140 153.181 137.701 1.00 58.71  ? 416 ASN A C   1 
ATOM   2686  O  O   . ASN A 1 441 ? 107.619 153.941 136.879 1.00 65.48  ? 416 ASN A O   1 
ATOM   2687  C  CB  . ASN A 1 441 ? 109.959 154.434 138.826 1.00 50.17  ? 416 ASN A CB  1 
ATOM   2688  C  CG  . ASN A 1 441 ? 110.272 155.429 139.916 1.00 61.00  ? 416 ASN A CG  1 
ATOM   2689  O  OD1 . ASN A 1 441 ? 109.376 156.065 140.465 1.00 65.51  ? 416 ASN A OD1 1 
ATOM   2690  N  ND2 . ASN A 1 441 ? 111.550 155.573 140.237 1.00 64.76  ? 416 ASN A ND2 1 
ATOM   2691  N  N   . LEU A 1 442 ? 108.306 151.883 137.462 1.00 51.33  ? 417 LEU A N   1 
ATOM   2692  C  CA  . LEU A 1 442 ? 107.932 151.301 136.178 1.00 46.13  ? 417 LEU A CA  1 
ATOM   2693  C  C   . LEU A 1 442 ? 106.687 150.433 136.224 1.00 49.56  ? 417 LEU A C   1 
ATOM   2694  O  O   . LEU A 1 442 ? 105.947 150.387 135.241 1.00 59.43  ? 417 LEU A O   1 
ATOM   2695  C  CB  . LEU A 1 442 ? 109.095 150.490 135.609 1.00 40.32  ? 417 LEU A CB  1 
ATOM   2696  C  CG  . LEU A 1 442 ? 110.000 151.365 134.753 1.00 41.32  ? 417 LEU A CG  1 
ATOM   2697  C  CD1 . LEU A 1 442 ? 111.333 150.714 134.520 1.00 50.32  ? 417 LEU A CD1 1 
ATOM   2698  C  CD2 . LEU A 1 442 ? 109.311 151.631 133.438 1.00 50.17  ? 417 LEU A CD2 1 
ATOM   2699  N  N   . TYR A 1 443 ? 106.426 149.732 137.325 1.00 50.05  ? 418 TYR A N   1 
ATOM   2700  C  CA  . TYR A 1 443 ? 105.224 148.917 137.438 1.00 56.22  ? 418 TYR A CA  1 
ATOM   2701  C  C   . TYR A 1 443 ? 104.248 149.469 138.468 1.00 61.83  ? 418 TYR A C   1 
ATOM   2702  O  O   . TYR A 1 443 ? 103.101 149.773 138.129 1.00 59.65  ? 418 TYR A O   1 
ATOM   2703  C  CB  . TYR A 1 443 ? 105.604 147.470 137.772 1.00 52.29  ? 418 TYR A CB  1 
ATOM   2704  C  CG  . TYR A 1 443 ? 106.459 146.817 136.711 1.00 52.13  ? 418 TYR A CG  1 
ATOM   2705  C  CD1 . TYR A 1 443 ? 107.838 146.906 136.752 1.00 53.34  ? 418 TYR A CD1 1 
ATOM   2706  C  CD2 . TYR A 1 443 ? 105.882 146.121 135.662 1.00 55.56  ? 418 TYR A CD2 1 
ATOM   2707  C  CE1 . TYR A 1 443 ? 108.616 146.317 135.787 1.00 55.91  ? 418 TYR A CE1 1 
ATOM   2708  C  CE2 . TYR A 1 443 ? 106.653 145.529 134.693 1.00 51.19  ? 418 TYR A CE2 1 
ATOM   2709  C  CZ  . TYR A 1 443 ? 108.019 145.631 134.760 1.00 50.34  ? 418 TYR A CZ  1 
ATOM   2710  O  OH  . TYR A 1 443 ? 108.793 145.041 133.792 1.00 47.68  ? 418 TYR A OH  1 
ATOM   2711  N  N   . GLY A 1 444 ? 104.674 149.617 139.720 1.00 87.31  ? 419 GLY A N   1 
ATOM   2712  C  CA  . GLY A 1 444 ? 103.816 150.190 140.741 1.00 86.84  ? 419 GLY A CA  1 
ATOM   2713  C  C   . GLY A 1 444 ? 102.543 149.421 141.011 1.00 94.41  ? 419 GLY A C   1 
ATOM   2714  O  O   . GLY A 1 444 ? 101.620 149.966 141.621 1.00 94.45  ? 419 GLY A O   1 
ATOM   2715  N  N   . TYR A 1 445 ? 102.465 148.169 140.579 1.00 106.95 ? 420 TYR A N   1 
ATOM   2716  C  CA  . TYR A 1 445 ? 101.244 147.387 140.742 1.00 103.27 ? 420 TYR A CA  1 
ATOM   2717  C  C   . TYR A 1 445 ? 101.084 146.976 142.199 1.00 105.39 ? 420 TYR A C   1 
ATOM   2718  O  O   . TYR A 1 445 ? 101.984 146.334 142.751 1.00 104.70 ? 420 TYR A O   1 
ATOM   2719  C  CB  . TYR A 1 445 ? 101.283 146.157 139.842 1.00 103.59 ? 420 TYR A CB  1 
ATOM   2720  C  CG  . TYR A 1 445 ? 99.941  145.772 139.258 1.00 109.63 ? 420 TYR A CG  1 
ATOM   2721  C  CD1 . TYR A 1 445 ? 98.841  145.559 140.078 1.00 107.51 ? 420 TYR A CD1 1 
ATOM   2722  C  CD2 . TYR A 1 445 ? 99.776  145.622 137.888 1.00 109.96 ? 420 TYR A CD2 1 
ATOM   2723  C  CE1 . TYR A 1 445 ? 97.613  145.207 139.550 1.00 106.99 ? 420 TYR A CE1 1 
ATOM   2724  C  CE2 . TYR A 1 445 ? 98.552  145.271 137.350 1.00 107.04 ? 420 TYR A CE2 1 
ATOM   2725  C  CZ  . TYR A 1 445 ? 97.474  145.065 138.186 1.00 108.33 ? 420 TYR A CZ  1 
ATOM   2726  O  OH  . TYR A 1 445 ? 96.253  144.713 137.657 1.00 108.74 ? 420 TYR A OH  1 
ATOM   2727  N  N   . PRO A 1 446 ? 99.975  147.322 142.857 1.00 112.74 ? 421 PRO A N   1 
ATOM   2728  C  CA  . PRO A 1 446 ? 99.806  146.921 144.264 1.00 112.41 ? 421 PRO A CA  1 
ATOM   2729  C  C   . PRO A 1 446 ? 99.800  145.417 144.475 1.00 113.31 ? 421 PRO A C   1 
ATOM   2730  O  O   . PRO A 1 446 ? 100.151 144.955 145.568 1.00 110.93 ? 421 PRO A O   1 
ATOM   2731  C  CB  . PRO A 1 446 ? 98.459  147.549 144.647 1.00 112.32 ? 421 PRO A CB  1 
ATOM   2732  C  CG  . PRO A 1 446 ? 98.271  148.672 143.676 1.00 110.89 ? 421 PRO A CG  1 
ATOM   2733  C  CD  . PRO A 1 446 ? 98.890  148.202 142.394 1.00 111.95 ? 421 PRO A CD  1 
ATOM   2734  N  N   . GLU A 1 447 ? 99.409  144.636 143.468 1.00 113.60 ? 422 GLU A N   1 
ATOM   2735  C  CA  . GLU A 1 447 ? 99.366  143.185 143.622 1.00 112.82 ? 422 GLU A CA  1 
ATOM   2736  C  C   . GLU A 1 447 ? 100.745 142.565 143.431 1.00 113.78 ? 422 GLU A C   1 
ATOM   2737  O  O   . GLU A 1 447 ? 101.299 141.955 144.351 1.00 110.62 ? 422 GLU A O   1 
ATOM   2738  C  CB  . GLU A 1 447 ? 98.365  142.582 142.634 1.00 109.68 ? 422 GLU A CB  1 
ATOM   2739  N  N   . GLY A 1 448 ? 101.314 142.711 142.239 1.00 107.30 ? 423 GLY A N   1 
ATOM   2740  C  CA  . GLY A 1 448 ? 102.600 142.115 141.939 1.00 104.22 ? 423 GLY A CA  1 
ATOM   2741  C  C   . GLY A 1 448 ? 103.776 143.030 142.207 1.00 105.10 ? 423 GLY A C   1 
ATOM   2742  O  O   . GLY A 1 448 ? 104.638 143.208 141.342 1.00 104.82 ? 423 GLY A O   1 
ATOM   2743  N  N   . LYS A 1 449 ? 103.820 143.629 143.397 1.00 98.57  ? 424 LYS A N   1 
ATOM   2744  C  CA  . LYS A 1 449 ? 104.948 144.462 143.786 1.00 98.11  ? 424 LYS A CA  1 
ATOM   2745  C  C   . LYS A 1 449 ? 105.936 143.746 144.692 1.00 98.27  ? 424 LYS A C   1 
ATOM   2746  O  O   . LYS A 1 449 ? 107.091 144.174 144.780 1.00 99.43  ? 424 LYS A O   1 
ATOM   2747  C  CB  . LYS A 1 449 ? 104.461 145.733 144.491 1.00 96.05  ? 424 LYS A CB  1 
ATOM   2748  N  N   . ASP A 1 450 ? 105.513 142.675 145.366 1.00 87.22  ? 425 ASP A N   1 
ATOM   2749  C  CA  . ASP A 1 450 ? 106.395 141.927 146.248 1.00 85.84  ? 425 ASP A CA  1 
ATOM   2750  C  C   . ASP A 1 450 ? 106.837 140.591 145.675 1.00 83.14  ? 425 ASP A C   1 
ATOM   2751  O  O   . ASP A 1 450 ? 107.875 140.075 146.096 1.00 78.88  ? 425 ASP A O   1 
ATOM   2752  C  CB  . ASP A 1 450 ? 105.718 141.687 147.604 1.00 87.32  ? 425 ASP A CB  1 
ATOM   2753  C  CG  . ASP A 1 450 ? 104.229 141.438 147.477 1.00 90.34  ? 425 ASP A CG  1 
ATOM   2754  O  OD1 . ASP A 1 450 ? 103.711 141.508 146.343 1.00 89.70  ? 425 ASP A OD1 1 
ATOM   2755  O  OD2 . ASP A 1 450 ? 103.577 141.174 148.509 1.00 86.76  ? 425 ASP A OD2 1 
ATOM   2756  N  N   . VAL A 1 451 ? 106.087 140.021 144.739 1.00 67.83  ? 426 VAL A N   1 
ATOM   2757  C  CA  . VAL A 1 451 ? 106.529 138.812 144.053 1.00 60.29  ? 426 VAL A CA  1 
ATOM   2758  C  C   . VAL A 1 451 ? 107.453 139.152 142.894 1.00 68.83  ? 426 VAL A C   1 
ATOM   2759  O  O   . VAL A 1 451 ? 108.436 138.449 142.649 1.00 74.71  ? 426 VAL A O   1 
ATOM   2760  C  CB  . VAL A 1 451 ? 105.312 137.996 143.580 1.00 54.66  ? 426 VAL A CB  1 
ATOM   2761  C  CG1 . VAL A 1 451 ? 105.760 136.806 142.761 1.00 52.75  ? 426 VAL A CG1 1 
ATOM   2762  C  CG2 . VAL A 1 451 ? 104.491 137.544 144.769 1.00 65.01  ? 426 VAL A CG2 1 
ATOM   2763  N  N   . LEU A 1 452 ? 107.155 140.235 142.175 1.00 68.73  ? 427 LEU A N   1 
ATOM   2764  C  CA  . LEU A 1 452 ? 108.000 140.642 141.059 1.00 62.54  ? 427 LEU A CA  1 
ATOM   2765  C  C   . LEU A 1 452 ? 109.337 141.188 141.543 1.00 63.91  ? 427 LEU A C   1 
ATOM   2766  O  O   . LEU A 1 452 ? 110.384 140.893 140.955 1.00 67.19  ? 427 LEU A O   1 
ATOM   2767  C  CB  . LEU A 1 452 ? 107.272 141.680 140.211 1.00 57.57  ? 427 LEU A CB  1 
ATOM   2768  C  CG  . LEU A 1 452 ? 108.026 142.220 139.004 1.00 58.04  ? 427 LEU A CG  1 
ATOM   2769  C  CD1 . LEU A 1 452 ? 108.494 141.079 138.134 1.00 60.43  ? 427 LEU A CD1 1 
ATOM   2770  C  CD2 . LEU A 1 452 ? 107.129 143.150 138.222 1.00 66.87  ? 427 LEU A CD2 1 
ATOM   2771  N  N   . ARG A 1 453 ? 109.327 141.987 142.610 1.00 64.40  ? 428 ARG A N   1 
ATOM   2772  C  CA  . ARG A 1 453 ? 110.574 142.567 143.093 1.00 59.68  ? 428 ARG A CA  1 
ATOM   2773  C  C   . ARG A 1 453 ? 111.539 141.489 143.561 1.00 64.97  ? 428 ARG A C   1 
ATOM   2774  O  O   . ARG A 1 453 ? 112.732 141.539 143.250 1.00 71.37  ? 428 ARG A O   1 
ATOM   2775  C  CB  . ARG A 1 453 ? 110.301 143.555 144.220 1.00 60.98  ? 428 ARG A CB  1 
ATOM   2776  C  CG  . ARG A 1 453 ? 111.545 144.266 144.695 1.00 64.24  ? 428 ARG A CG  1 
ATOM   2777  C  CD  . ARG A 1 453 ? 111.213 145.389 145.654 1.00 70.40  ? 428 ARG A CD  1 
ATOM   2778  N  NE  . ARG A 1 453 ? 110.669 144.887 146.909 1.00 73.17  ? 428 ARG A NE  1 
ATOM   2779  C  CZ  . ARG A 1 453 ? 109.383 144.914 147.227 1.00 76.85  ? 428 ARG A CZ  1 
ATOM   2780  N  NH1 . ARG A 1 453 ? 108.478 145.414 146.402 1.00 76.49  ? 428 ARG A NH1 1 
ATOM   2781  N  NH2 . ARG A 1 453 ? 108.996 144.425 148.402 1.00 76.01  ? 428 ARG A NH2 1 
ATOM   2782  N  N   . GLU A 1 454 ? 111.038 140.493 144.293 1.00 73.03  ? 429 GLU A N   1 
ATOM   2783  C  CA  . GLU A 1 454 ? 111.909 139.430 144.780 1.00 67.84  ? 429 GLU A CA  1 
ATOM   2784  C  C   . GLU A 1 454 ? 112.463 138.593 143.636 1.00 62.66  ? 429 GLU A C   1 
ATOM   2785  O  O   . GLU A 1 454 ? 113.630 138.191 143.667 1.00 68.14  ? 429 GLU A O   1 
ATOM   2786  C  CB  . GLU A 1 454 ? 111.165 138.549 145.780 1.00 64.00  ? 429 GLU A CB  1 
ATOM   2787  C  CG  . GLU A 1 454 ? 110.708 139.286 147.026 1.00 75.91  ? 429 GLU A CG  1 
ATOM   2788  C  CD  . GLU A 1 454 ? 111.862 139.706 147.911 1.00 80.59  ? 429 GLU A CD  1 
ATOM   2789  O  OE1 . GLU A 1 454 ? 112.939 139.080 147.822 1.00 79.65  ? 429 GLU A OE1 1 
ATOM   2790  O  OE2 . GLU A 1 454 ? 111.695 140.663 148.695 1.00 78.25  ? 429 GLU A OE2 1 
ATOM   2791  N  N   . THR A 1 455 ? 111.655 138.329 142.607 1.00 43.70  ? 430 THR A N   1 
ATOM   2792  C  CA  . THR A 1 455 ? 112.150 137.487 141.526 1.00 43.19  ? 430 THR A CA  1 
ATOM   2793  C  C   . THR A 1 455 ? 113.140 138.227 140.632 1.00 53.08  ? 430 THR A C   1 
ATOM   2794  O  O   . THR A 1 455 ? 114.099 137.615 140.150 1.00 59.88  ? 430 THR A O   1 
ATOM   2795  C  CB  . THR A 1 455 ? 110.993 136.915 140.708 1.00 42.39  ? 430 THR A CB  1 
ATOM   2796  O  OG1 . THR A 1 455 ? 111.498 135.936 139.796 1.00 49.87  ? 430 THR A OG1 1 
ATOM   2797  C  CG2 . THR A 1 455 ? 110.305 137.984 139.924 1.00 52.32  ? 430 THR A CG2 1 
ATOM   2798  N  N   . ILE A 1 456 ? 112.963 139.537 140.413 1.00 50.08  ? 431 ILE A N   1 
ATOM   2799  C  CA  . ILE A 1 456 ? 113.984 140.256 139.648 1.00 42.44  ? 431 ILE A CA  1 
ATOM   2800  C  C   . ILE A 1 456 ? 115.176 140.644 140.504 1.00 45.15  ? 431 ILE A C   1 
ATOM   2801  O  O   . ILE A 1 456 ? 116.209 141.043 139.957 1.00 54.22  ? 431 ILE A O   1 
ATOM   2802  C  CB  . ILE A 1 456 ? 113.470 141.525 138.943 1.00 37.64  ? 431 ILE A CB  1 
ATOM   2803  C  CG1 . ILE A 1 456 ? 113.506 142.728 139.874 1.00 43.87  ? 431 ILE A CG1 1 
ATOM   2804  C  CG2 . ILE A 1 456 ? 112.081 141.319 138.395 1.00 47.43  ? 431 ILE A CG2 1 
ATOM   2805  C  CD1 . ILE A 1 456 ? 112.959 143.970 139.238 1.00 49.97  ? 431 ILE A CD1 1 
ATOM   2806  N  N   . LYS A 1 457 ? 115.063 140.550 141.830 1.00 54.56  ? 432 LYS A N   1 
ATOM   2807  C  CA  . LYS A 1 457 ? 116.252 140.598 142.671 1.00 49.67  ? 432 LYS A CA  1 
ATOM   2808  C  C   . LYS A 1 457 ? 117.027 139.292 142.588 1.00 50.90  ? 432 LYS A C   1 
ATOM   2809  O  O   . LYS A 1 457 ? 118.261 139.298 142.559 1.00 56.66  ? 432 LYS A O   1 
ATOM   2810  C  CB  . LYS A 1 457 ? 115.866 140.885 144.119 1.00 56.04  ? 432 LYS A CB  1 
ATOM   2811  C  CG  . LYS A 1 457 ? 115.936 142.335 144.529 1.00 54.24  ? 432 LYS A CG  1 
ATOM   2812  C  CD  . LYS A 1 457 ? 115.536 142.481 145.982 1.00 56.94  ? 432 LYS A CD  1 
ATOM   2813  C  CE  . LYS A 1 457 ? 114.769 143.762 146.219 1.00 66.38  ? 432 LYS A CE  1 
ATOM   2814  N  NZ  . LYS A 1 457 ? 113.849 143.649 147.385 1.00 65.30  ? 432 LYS A NZ  1 
ATOM   2815  N  N   . PHE A 1 458 ? 116.318 138.161 142.567 1.00 38.21  ? 433 PHE A N   1 
ATOM   2816  C  CA  . PHE A 1 458 ? 116.989 136.868 142.480 1.00 41.52  ? 433 PHE A CA  1 
ATOM   2817  C  C   . PHE A 1 458 ? 117.640 136.665 141.120 1.00 49.73  ? 433 PHE A C   1 
ATOM   2818  O  O   . PHE A 1 458 ? 118.732 136.095 141.030 1.00 62.74  ? 433 PHE A O   1 
ATOM   2819  C  CB  . PHE A 1 458 ? 116.005 135.735 142.758 1.00 32.82  ? 433 PHE A CB  1 
ATOM   2820  C  CG  . PHE A 1 458 ? 116.423 134.417 142.171 1.00 31.60  ? 433 PHE A CG  1 
ATOM   2821  C  CD1 . PHE A 1 458 ? 117.352 133.629 142.809 1.00 41.97  ? 433 PHE A CD1 1 
ATOM   2822  C  CD2 . PHE A 1 458 ? 115.893 133.973 140.977 1.00 43.47  ? 433 PHE A CD2 1 
ATOM   2823  C  CE1 . PHE A 1 458 ? 117.740 132.424 142.272 1.00 44.77  ? 433 PHE A CE1 1 
ATOM   2824  C  CE2 . PHE A 1 458 ? 116.282 132.769 140.436 1.00 41.49  ? 433 PHE A CE2 1 
ATOM   2825  C  CZ  . PHE A 1 458 ? 117.206 131.995 141.085 1.00 38.01  ? 433 PHE A CZ  1 
ATOM   2826  N  N   . MET A 1 459 ? 116.975 137.091 140.046 1.00 45.56  ? 434 MET A N   1 
ATOM   2827  C  CA  . MET A 1 459 ? 117.512 136.826 138.717 1.00 46.42  ? 434 MET A CA  1 
ATOM   2828  C  C   . MET A 1 459 ? 118.769 137.643 138.446 1.00 47.85  ? 434 MET A C   1 
ATOM   2829  O  O   . MET A 1 459 ? 119.727 137.135 137.854 1.00 54.06  ? 434 MET A O   1 
ATOM   2830  C  CB  . MET A 1 459 ? 116.451 137.098 137.658 1.00 39.70  ? 434 MET A CB  1 
ATOM   2831  C  CG  . MET A 1 459 ? 116.699 136.379 136.350 1.00 46.51  ? 434 MET A CG  1 
ATOM   2832  S  SD  . MET A 1 459 ? 116.185 134.656 136.390 1.00 71.20  ? 434 MET A SD  1 
ATOM   2833  C  CE  . MET A 1 459 ? 114.755 134.756 137.460 1.00 49.37  ? 434 MET A CE  1 
ATOM   2834  N  N   . TYR A 1 460 ? 118.786 138.905 138.860 1.00 41.59  ? 435 TYR A N   1 
ATOM   2835  C  CA  . TYR A 1 460 ? 119.911 139.795 138.574 1.00 44.42  ? 435 TYR A CA  1 
ATOM   2836  C  C   . TYR A 1 460 ? 120.872 139.874 139.758 1.00 50.74  ? 435 TYR A C   1 
ATOM   2837  O  O   . TYR A 1 460 ? 121.157 140.943 140.290 1.00 50.49  ? 435 TYR A O   1 
ATOM   2838  C  CB  . TYR A 1 460 ? 119.403 141.176 138.182 1.00 42.99  ? 435 TYR A CB  1 
ATOM   2839  C  CG  . TYR A 1 460 ? 118.835 141.220 136.789 1.00 44.57  ? 435 TYR A CG  1 
ATOM   2840  C  CD1 . TYR A 1 460 ? 119.663 141.328 135.687 1.00 46.93  ? 435 TYR A CD1 1 
ATOM   2841  C  CD2 . TYR A 1 460 ? 117.473 141.138 136.575 1.00 48.27  ? 435 TYR A CD2 1 
ATOM   2842  C  CE1 . TYR A 1 460 ? 119.150 141.360 134.417 1.00 43.30  ? 435 TYR A CE1 1 
ATOM   2843  C  CE2 . TYR A 1 460 ? 116.953 141.169 135.307 1.00 46.71  ? 435 TYR A CE2 1 
ATOM   2844  C  CZ  . TYR A 1 460 ? 117.794 141.280 134.234 1.00 44.81  ? 435 TYR A CZ  1 
ATOM   2845  O  OH  . TYR A 1 460 ? 117.272 141.312 132.967 1.00 51.91  ? 435 TYR A OH  1 
ATOM   2846  N  N   . THR A 1 461 ? 121.383 138.714 140.163 1.00 55.59  ? 436 THR A N   1 
ATOM   2847  C  CA  . THR A 1 461 ? 122.478 138.657 141.120 1.00 56.06  ? 436 THR A CA  1 
ATOM   2848  C  C   . THR A 1 461 ? 123.314 137.425 140.822 1.00 57.29  ? 436 THR A C   1 
ATOM   2849  O  O   . THR A 1 461 ? 122.775 136.345 140.573 1.00 63.61  ? 436 THR A O   1 
ATOM   2850  C  CB  . THR A 1 461 ? 121.986 138.630 142.571 1.00 48.69  ? 436 THR A CB  1 
ATOM   2851  O  OG1 . THR A 1 461 ? 123.079 138.313 143.438 1.00 57.61  ? 436 THR A OG1 1 
ATOM   2852  C  CG2 . THR A 1 461 ? 120.914 137.598 142.751 1.00 51.08  ? 436 THR A CG2 1 
ATOM   2853  N  N   . ASP A 1 462 ? 124.632 137.598 140.833 1.00 71.75  ? 437 ASP A N   1 
ATOM   2854  C  CA  . ASP A 1 462 ? 125.557 136.508 140.536 1.00 74.38  ? 437 ASP A CA  1 
ATOM   2855  C  C   . ASP A 1 462 ? 125.701 135.662 141.791 1.00 80.32  ? 437 ASP A C   1 
ATOM   2856  O  O   . ASP A 1 462 ? 126.371 136.057 142.747 1.00 83.21  ? 437 ASP A O   1 
ATOM   2857  C  CB  . ASP A 1 462 ? 126.901 137.058 140.079 1.00 75.29  ? 437 ASP A CB  1 
ATOM   2858  C  CG  . ASP A 1 462 ? 127.621 136.120 139.141 1.00 79.19  ? 437 ASP A CG  1 
ATOM   2859  O  OD1 . ASP A 1 462 ? 126.941 135.333 138.452 1.00 76.56  ? 437 ASP A OD1 1 
ATOM   2860  O  OD2 . ASP A 1 462 ? 128.868 136.166 139.095 1.00 82.13  ? 437 ASP A OD2 1 
ATOM   2861  N  N   . TRP A 1 463 ? 125.070 134.485 141.795 1.00 64.01  ? 438 TRP A N   1 
ATOM   2862  C  CA  . TRP A 1 463 ? 125.029 133.676 143.008 1.00 55.43  ? 438 TRP A CA  1 
ATOM   2863  C  C   . TRP A 1 463 ? 126.358 132.999 143.306 1.00 61.86  ? 438 TRP A C   1 
ATOM   2864  O  O   . TRP A 1 463 ? 126.608 132.639 144.460 1.00 66.58  ? 438 TRP A O   1 
ATOM   2865  C  CB  . TRP A 1 463 ? 123.916 132.639 142.906 1.00 56.29  ? 438 TRP A CB  1 
ATOM   2866  C  CG  . TRP A 1 463 ? 122.564 133.231 143.084 1.00 55.86  ? 438 TRP A CG  1 
ATOM   2867  C  CD1 . TRP A 1 463 ? 121.624 133.413 142.123 1.00 58.13  ? 438 TRP A CD1 1 
ATOM   2868  C  CD2 . TRP A 1 463 ? 122.001 133.734 144.298 1.00 58.13  ? 438 TRP A CD2 1 
ATOM   2869  N  NE1 . TRP A 1 463 ? 120.506 133.993 142.660 1.00 58.20  ? 438 TRP A NE1 1 
ATOM   2870  C  CE2 . TRP A 1 463 ? 120.712 134.201 143.996 1.00 56.07  ? 438 TRP A CE2 1 
ATOM   2871  C  CE3 . TRP A 1 463 ? 122.461 133.834 145.611 1.00 63.20  ? 438 TRP A CE3 1 
ATOM   2872  C  CZ2 . TRP A 1 463 ? 119.877 134.759 144.957 1.00 54.82  ? 438 TRP A CZ2 1 
ATOM   2873  C  CZ3 . TRP A 1 463 ? 121.630 134.388 146.563 1.00 64.66  ? 438 TRP A CZ3 1 
ATOM   2874  C  CH2 . TRP A 1 463 ? 120.353 134.843 146.231 1.00 56.44  ? 438 TRP A CH2 1 
ATOM   2875  N  N   . ALA A 1 464 ? 127.216 132.819 142.302 1.00 78.43  ? 439 ALA A N   1 
ATOM   2876  C  CA  . ALA A 1 464 ? 128.555 132.310 142.564 1.00 79.93  ? 439 ALA A CA  1 
ATOM   2877  C  C   . ALA A 1 464 ? 129.451 133.357 143.213 1.00 84.32  ? 439 ALA A C   1 
ATOM   2878  O  O   . ALA A 1 464 ? 130.490 133.001 143.777 1.00 82.97  ? 439 ALA A O   1 
ATOM   2879  C  CB  . ALA A 1 464 ? 129.189 131.812 141.266 1.00 79.56  ? 439 ALA A CB  1 
ATOM   2880  N  N   . ASP A 1 465 ? 129.073 134.630 143.145 1.00 85.40  ? 440 ASP A N   1 
ATOM   2881  C  CA  . ASP A 1 465 ? 129.820 135.754 143.705 1.00 76.82  ? 440 ASP A CA  1 
ATOM   2882  C  C   . ASP A 1 465 ? 128.882 136.668 144.479 1.00 75.03  ? 440 ASP A C   1 
ATOM   2883  O  O   . ASP A 1 465 ? 128.852 137.884 144.285 1.00 79.44  ? 440 ASP A O   1 
ATOM   2884  C  CB  . ASP A 1 465 ? 130.546 136.529 142.613 1.00 78.59  ? 440 ASP A CB  1 
ATOM   2885  C  CG  . ASP A 1 465 ? 132.048 136.420 142.727 1.00 84.80  ? 440 ASP A CG  1 
ATOM   2886  O  OD1 . ASP A 1 465 ? 132.522 135.668 143.602 1.00 81.87  ? 440 ASP A OD1 1 
ATOM   2887  O  OD2 . ASP A 1 465 ? 132.755 137.086 141.943 1.00 89.72  ? 440 ASP A OD2 1 
ATOM   2888  N  N   . ARG A 1 466 ? 128.091 136.067 145.371 1.00 68.41  ? 441 ARG A N   1 
ATOM   2889  C  CA  . ARG A 1 466 ? 126.986 136.772 146.014 1.00 66.98  ? 441 ARG A CA  1 
ATOM   2890  C  C   . ARG A 1 466 ? 127.442 138.029 146.743 1.00 72.92  ? 441 ARG A C   1 
ATOM   2891  O  O   . ARG A 1 466 ? 126.669 138.986 146.864 1.00 75.73  ? 441 ARG A O   1 
ATOM   2892  C  CB  . ARG A 1 466 ? 126.274 135.825 146.980 1.00 70.19  ? 441 ARG A CB  1 
ATOM   2893  C  CG  . ARG A 1 466 ? 125.118 136.435 147.748 1.00 70.50  ? 441 ARG A CG  1 
ATOM   2894  C  CD  . ARG A 1 466 ? 124.851 135.661 149.031 1.00 74.51  ? 441 ARG A CD  1 
ATOM   2895  N  NE  . ARG A 1 466 ? 124.031 134.477 148.800 1.00 74.87  ? 441 ARG A NE  1 
ATOM   2896  C  CZ  . ARG A 1 466 ? 124.510 133.250 148.646 1.00 76.81  ? 441 ARG A CZ  1 
ATOM   2897  N  NH1 . ARG A 1 466 ? 125.809 133.003 148.689 1.00 75.27  ? 441 ARG A NH1 1 
ATOM   2898  N  NH2 . ARG A 1 466 ? 123.664 132.244 148.442 1.00 74.98  ? 441 ARG A NH2 1 
ATOM   2899  N  N   . ASP A 1 467 ? 128.680 138.061 147.223 1.00 83.78  ? 442 ASP A N   1 
ATOM   2900  C  CA  . ASP A 1 467 ? 129.190 139.190 147.993 1.00 81.50  ? 442 ASP A CA  1 
ATOM   2901  C  C   . ASP A 1 467 ? 130.395 139.829 147.313 1.00 85.44  ? 442 ASP A C   1 
ATOM   2902  O  O   . ASP A 1 467 ? 131.404 140.128 147.954 1.00 90.07  ? 442 ASP A O   1 
ATOM   2903  C  CB  . ASP A 1 467 ? 129.542 138.760 149.414 1.00 77.23  ? 442 ASP A CB  1 
ATOM   2904  N  N   . ASN A 1 468 ? 130.308 140.048 146.000 1.00 84.98  ? 443 ASN A N   1 
ATOM   2905  C  CA  . ASN A 1 468 ? 131.422 140.657 145.283 1.00 82.25  ? 443 ASN A CA  1 
ATOM   2906  C  C   . ASN A 1 468 ? 131.416 142.174 145.416 1.00 87.29  ? 443 ASN A C   1 
ATOM   2907  O  O   . ASN A 1 468 ? 132.476 142.787 145.579 1.00 91.84  ? 443 ASN A O   1 
ATOM   2908  C  CB  . ASN A 1 468 ? 131.386 140.254 143.810 1.00 83.47  ? 443 ASN A CB  1 
ATOM   2909  C  CG  . ASN A 1 468 ? 132.733 140.404 143.130 1.00 89.64  ? 443 ASN A CG  1 
ATOM   2910  O  OD1 . ASN A 1 468 ? 133.504 141.309 143.443 1.00 93.15  ? 443 ASN A OD1 1 
ATOM   2911  N  ND2 . ASN A 1 468 ? 133.023 139.511 142.192 1.00 89.03  ? 443 ASN A ND2 1 
ATOM   2912  N  N   . GLY A 1 469 ? 130.244 142.795 145.355 1.00 83.14  ? 444 GLY A N   1 
ATOM   2913  C  CA  . GLY A 1 469 ? 130.165 144.240 145.423 1.00 82.60  ? 444 GLY A CA  1 
ATOM   2914  C  C   . GLY A 1 469 ? 130.161 144.898 144.059 1.00 84.52  ? 444 GLY A C   1 
ATOM   2915  O  O   . GLY A 1 469 ? 129.184 145.553 143.688 1.00 89.32  ? 444 GLY A O   1 
ATOM   2916  N  N   . GLU A 1 470 ? 131.248 144.741 143.303 1.00 84.75  ? 445 GLU A N   1 
ATOM   2917  C  CA  . GLU A 1 470 ? 131.276 145.262 141.941 1.00 81.19  ? 445 GLU A CA  1 
ATOM   2918  C  C   . GLU A 1 470 ? 130.282 144.528 141.052 1.00 87.19  ? 445 GLU A C   1 
ATOM   2919  O  O   . GLU A 1 470 ? 129.588 145.151 140.234 1.00 92.09  ? 445 GLU A O   1 
ATOM   2920  C  CB  . GLU A 1 470 ? 132.686 145.158 141.367 1.00 82.33  ? 445 GLU A CB  1 
ATOM   2921  C  CG  . GLU A 1 470 ? 132.832 145.743 139.975 1.00 89.49  ? 445 GLU A CG  1 
ATOM   2922  C  CD  . GLU A 1 470 ? 132.666 144.704 138.883 1.00 93.37  ? 445 GLU A CD  1 
ATOM   2923  O  OE1 . GLU A 1 470 ? 132.452 143.520 139.214 1.00 91.16  ? 445 GLU A OE1 1 
ATOM   2924  O  OE2 . GLU A 1 470 ? 132.751 145.072 137.693 1.00 92.17  ? 445 GLU A OE2 1 
ATOM   2925  N  N   . MET A 1 471 ? 130.190 143.205 141.197 1.00 82.29  ? 446 MET A N   1 
ATOM   2926  C  CA  . MET A 1 471 ? 129.237 142.448 140.402 1.00 82.37  ? 446 MET A CA  1 
ATOM   2927  C  C   . MET A 1 471 ? 127.877 142.540 141.084 1.00 85.07  ? 446 MET A C   1 
ATOM   2928  O  O   . MET A 1 471 ? 127.175 141.540 141.274 1.00 87.48  ? 446 MET A O   1 
ATOM   2929  C  CB  . MET A 1 471 ? 129.709 140.999 140.239 1.00 81.31  ? 446 MET A CB  1 
ATOM   2930  C  CG  . MET A 1 471 ? 128.864 140.133 139.313 1.00 85.97  ? 446 MET A CG  1 
ATOM   2931  S  SD  . MET A 1 471 ? 129.513 140.062 137.634 1.00 101.38 ? 446 MET A SD  1 
ATOM   2932  C  CE  . MET A 1 471 ? 130.858 138.900 137.848 1.00 88.77  ? 446 MET A CE  1 
ATOM   2933  N  N   . ARG A 1 472 ? 127.523 143.740 141.476 1.00 61.07  ? 447 ARG A N   1 
ATOM   2934  C  CA  . ARG A 1 472 ? 126.175 144.205 141.755 1.00 58.71  ? 447 ARG A CA  1 
ATOM   2935  C  C   . ARG A 1 472 ? 125.901 145.513 141.040 1.00 68.99  ? 447 ARG A C   1 
ATOM   2936  O  O   . ARG A 1 472 ? 124.805 145.703 140.517 1.00 81.60  ? 447 ARG A O   1 
ATOM   2937  C  CB  . ARG A 1 472 ? 125.950 144.356 143.261 1.00 62.46  ? 447 ARG A CB  1 
ATOM   2938  C  CG  . ARG A 1 472 ? 125.619 143.043 143.949 1.00 67.19  ? 447 ARG A CG  1 
ATOM   2939  C  CD  . ARG A 1 472 ? 125.087 143.258 145.350 1.00 67.73  ? 447 ARG A CD  1 
ATOM   2940  N  NE  . ARG A 1 472 ? 126.032 143.980 146.190 1.00 66.31  ? 447 ARG A NE  1 
ATOM   2941  C  CZ  . ARG A 1 472 ? 126.394 143.590 147.403 1.00 68.30  ? 447 ARG A CZ  1 
ATOM   2942  N  NH1 . ARG A 1 472 ? 125.919 142.480 147.942 1.00 69.47  ? 447 ARG A NH1 1 
ATOM   2943  N  NH2 . ARG A 1 472 ? 127.257 144.331 148.092 1.00 71.82  ? 447 ARG A NH2 1 
ATOM   2944  N  N   . ARG A 1 473 ? 126.895 146.397 140.956 1.00 71.84  ? 448 ARG A N   1 
ATOM   2945  C  CA  . ARG A 1 473 ? 126.808 147.519 140.031 1.00 67.73  ? 448 ARG A CA  1 
ATOM   2946  C  C   . ARG A 1 473 ? 126.719 147.027 138.596 1.00 72.04  ? 448 ARG A C   1 
ATOM   2947  O  O   . ARG A 1 473 ? 125.925 147.545 137.798 1.00 80.44  ? 448 ARG A O   1 
ATOM   2948  C  CB  . ARG A 1 473 ? 128.015 148.437 140.206 1.00 64.49  ? 448 ARG A CB  1 
ATOM   2949  C  CG  . ARG A 1 473 ? 128.416 149.161 138.943 1.00 71.21  ? 448 ARG A CG  1 
ATOM   2950  C  CD  . ARG A 1 473 ? 129.862 149.603 138.992 1.00 75.32  ? 448 ARG A CD  1 
ATOM   2951  N  NE  . ARG A 1 473 ? 130.184 150.281 140.241 1.00 79.49  ? 448 ARG A NE  1 
ATOM   2952  C  CZ  . ARG A 1 473 ? 131.405 150.362 140.751 1.00 81.27  ? 448 ARG A CZ  1 
ATOM   2953  N  NH1 . ARG A 1 473 ? 132.447 149.827 140.139 1.00 79.74  ? 448 ARG A NH1 1 
ATOM   2954  N  NH2 . ARG A 1 473 ? 131.585 151.002 141.903 1.00 79.57  ? 448 ARG A NH2 1 
ATOM   2955  N  N   . LYS A 1 474 ? 127.521 146.017 138.249 1.00 65.81  ? 449 LYS A N   1 
ATOM   2956  C  CA  . LYS A 1 474 ? 127.456 145.472 136.898 1.00 61.56  ? 449 LYS A CA  1 
ATOM   2957  C  C   . LYS A 1 474 ? 126.079 144.894 136.602 1.00 60.81  ? 449 LYS A C   1 
ATOM   2958  O  O   . LYS A 1 474 ? 125.530 145.104 135.514 1.00 67.04  ? 449 LYS A O   1 
ATOM   2959  C  CB  . LYS A 1 474 ? 128.536 144.413 136.700 1.00 64.59  ? 449 LYS A CB  1 
ATOM   2960  C  CG  . LYS A 1 474 ? 129.777 144.932 136.004 1.00 69.71  ? 449 LYS A CG  1 
ATOM   2961  C  CD  . LYS A 1 474 ? 129.414 145.745 134.776 1.00 70.24  ? 449 LYS A CD  1 
ATOM   2962  C  CE  . LYS A 1 474 ? 130.652 146.167 134.006 1.00 71.41  ? 449 LYS A CE  1 
ATOM   2963  N  NZ  . LYS A 1 474 ? 131.363 144.999 133.420 1.00 71.04  ? 449 LYS A NZ  1 
ATOM   2964  N  N   . THR A 1 475 ? 125.493 144.177 137.562 1.00 49.88  ? 450 THR A N   1 
ATOM   2965  C  CA  . THR A 1 475 ? 124.181 143.591 137.321 1.00 43.70  ? 450 THR A CA  1 
ATOM   2966  C  C   . THR A 1 475 ? 123.077 144.640 137.337 1.00 54.92  ? 450 THR A C   1 
ATOM   2967  O  O   . THR A 1 475 ? 122.066 144.466 136.659 1.00 64.32  ? 450 THR A O   1 
ATOM   2968  C  CB  . THR A 1 475 ? 123.887 142.496 138.338 1.00 46.82  ? 450 THR A CB  1 
ATOM   2969  O  OG1 . THR A 1 475 ? 123.948 143.039 139.659 1.00 64.95  ? 450 THR A OG1 1 
ATOM   2970  C  CG2 . THR A 1 475 ? 124.899 141.377 138.207 1.00 51.70  ? 450 THR A CG2 1 
ATOM   2971  N  N   . LEU A 1 476 ? 123.245 145.736 138.078 1.00 49.51  ? 451 LEU A N   1 
ATOM   2972  C  CA  . LEU A 1 476 ? 122.286 146.836 137.994 1.00 46.95  ? 451 LEU A CA  1 
ATOM   2973  C  C   . LEU A 1 476 ? 122.299 147.468 136.607 1.00 46.43  ? 451 LEU A C   1 
ATOM   2974  O  O   . LEU A 1 476 ? 121.244 147.726 136.007 1.00 54.56  ? 451 LEU A O   1 
ATOM   2975  C  CB  . LEU A 1 476 ? 122.609 147.883 139.053 1.00 44.45  ? 451 LEU A CB  1 
ATOM   2976  C  CG  . LEU A 1 476 ? 121.999 147.723 140.437 1.00 45.64  ? 451 LEU A CG  1 
ATOM   2977  C  CD1 . LEU A 1 476 ? 122.086 149.044 141.170 1.00 47.76  ? 451 LEU A CD1 1 
ATOM   2978  C  CD2 . LEU A 1 476 ? 120.568 147.264 140.320 1.00 51.49  ? 451 LEU A CD2 1 
ATOM   2979  N  N   . LEU A 1 477 ? 123.497 147.739 136.088 1.00 47.08  ? 452 LEU A N   1 
ATOM   2980  C  CA  . LEU A 1 477 ? 123.613 148.264 134.733 1.00 45.05  ? 452 LEU A CA  1 
ATOM   2981  C  C   . LEU A 1 477 ? 123.000 147.303 133.724 1.00 47.59  ? 452 LEU A C   1 
ATOM   2982  O  O   . LEU A 1 477 ? 122.271 147.722 132.814 1.00 53.18  ? 452 LEU A O   1 
ATOM   2983  C  CB  . LEU A 1 477 ? 125.082 148.529 134.413 1.00 41.50  ? 452 LEU A CB  1 
ATOM   2984  C  CG  . LEU A 1 477 ? 125.500 148.808 132.976 1.00 46.36  ? 452 LEU A CG  1 
ATOM   2985  C  CD1 . LEU A 1 477 ? 126.589 149.850 132.976 1.00 52.74  ? 452 LEU A CD1 1 
ATOM   2986  C  CD2 . LEU A 1 477 ? 125.997 147.545 132.310 1.00 52.67  ? 452 LEU A CD2 1 
ATOM   2987  N  N   . ALA A 1 478 ? 123.274 146.006 133.879 1.00 41.53  ? 453 ALA A N   1 
ATOM   2988  C  CA  . ALA A 1 478 ? 122.704 145.015 132.975 1.00 38.06  ? 453 ALA A CA  1 
ATOM   2989  C  C   . ALA A 1 478 ? 121.189 144.960 133.099 1.00 39.40  ? 453 ALA A C   1 
ATOM   2990  O  O   . ALA A 1 478 ? 120.492 144.740 132.108 1.00 56.74  ? 453 ALA A O   1 
ATOM   2991  C  CB  . ALA A 1 478 ? 123.312 143.644 133.248 1.00 42.44  ? 453 ALA A CB  1 
ATOM   2992  N  N   . LEU A 1 479 ? 120.660 145.154 134.307 1.00 29.06  ? 454 LEU A N   1 
ATOM   2993  C  CA  . LEU A 1 479 ? 119.214 145.148 134.503 1.00 38.14  ? 454 LEU A CA  1 
ATOM   2994  C  C   . LEU A 1 479 ? 118.556 146.286 133.743 1.00 36.58  ? 454 LEU A C   1 
ATOM   2995  O  O   . LEU A 1 479 ? 117.565 146.084 133.029 1.00 35.06  ? 454 LEU A O   1 
ATOM   2996  C  CB  . LEU A 1 479 ? 118.897 145.246 135.996 1.00 42.64  ? 454 LEU A CB  1 
ATOM   2997  C  CG  . LEU A 1 479 ? 117.556 145.816 136.460 1.00 33.77  ? 454 LEU A CG  1 
ATOM   2998  C  CD1 . LEU A 1 479 ? 116.394 145.037 135.896 1.00 40.39  ? 454 LEU A CD1 1 
ATOM   2999  C  CD2 . LEU A 1 479 ? 117.494 145.826 137.970 1.00 37.09  ? 454 LEU A CD2 1 
ATOM   3000  N  N   . PHE A 1 480 ? 119.089 147.498 133.894 1.00 43.93  ? 455 PHE A N   1 
ATOM   3001  C  CA  . PHE A 1 480 ? 118.497 148.629 133.186 1.00 24.50  ? 455 PHE A CA  1 
ATOM   3002  C  C   . PHE A 1 480 ? 118.616 148.456 131.678 1.00 32.11  ? 455 PHE A C   1 
ATOM   3003  O  O   . PHE A 1 480 ? 117.652 148.698 130.939 1.00 44.90  ? 455 PHE A O   1 
ATOM   3004  C  CB  . PHE A 1 480 ? 119.142 149.936 133.624 1.00 27.62  ? 455 PHE A CB  1 
ATOM   3005  C  CG  . PHE A 1 480 ? 118.254 151.125 133.449 1.00 36.16  ? 455 PHE A CG  1 
ATOM   3006  C  CD1 . PHE A 1 480 ? 116.945 151.093 133.886 1.00 35.35  ? 455 PHE A CD1 1 
ATOM   3007  C  CD2 . PHE A 1 480 ? 118.718 152.270 132.834 1.00 39.74  ? 455 PHE A CD2 1 
ATOM   3008  C  CE1 . PHE A 1 480 ? 116.125 152.184 133.723 1.00 46.33  ? 455 PHE A CE1 1 
ATOM   3009  C  CE2 . PHE A 1 480 ? 117.900 153.361 132.670 1.00 34.97  ? 455 PHE A CE2 1 
ATOM   3010  C  CZ  . PHE A 1 480 ? 116.604 153.318 133.114 1.00 39.91  ? 455 PHE A CZ  1 
ATOM   3011  N  N   . THR A 1 481 ? 119.785 148.018 131.202 1.00 28.98  ? 456 THR A N   1 
ATOM   3012  C  CA  . THR A 1 481 ? 119.958 147.807 129.770 1.00 18.47  ? 456 THR A CA  1 
ATOM   3013  C  C   . THR A 1 481 ? 118.994 146.753 129.247 1.00 21.46  ? 456 THR A C   1 
ATOM   3014  O  O   . THR A 1 481 ? 118.377 146.935 128.193 1.00 43.42  ? 456 THR A O   1 
ATOM   3015  C  CB  . THR A 1 481 ? 121.398 147.408 129.470 1.00 25.49  ? 456 THR A CB  1 
ATOM   3016  O  OG1 . THR A 1 481 ? 122.226 148.573 129.489 1.00 43.34  ? 456 THR A OG1 1 
ATOM   3017  C  CG2 . THR A 1 481 ? 121.499 146.755 128.111 1.00 22.52  ? 456 THR A CG2 1 
ATOM   3018  N  N   . ASP A 1 482 ? 118.839 145.647 129.975 1.00 19.31  ? 457 ASP A N   1 
ATOM   3019  C  CA  . ASP A 1 482 ? 117.971 144.573 129.515 1.00 20.94  ? 457 ASP A CA  1 
ATOM   3020  C  C   . ASP A 1 482 ? 116.518 145.007 129.480 1.00 24.45  ? 457 ASP A C   1 
ATOM   3021  O  O   . ASP A 1 482 ? 115.793 144.671 128.541 1.00 37.91  ? 457 ASP A O   1 
ATOM   3022  C  CB  . ASP A 1 482 ? 118.137 143.347 130.405 1.00 28.09  ? 457 ASP A CB  1 
ATOM   3023  C  CG  . ASP A 1 482 ? 119.192 142.403 129.894 1.00 41.56  ? 457 ASP A CG  1 
ATOM   3024  O  OD1 . ASP A 1 482 ? 119.032 141.900 128.767 1.00 54.16  ? 457 ASP A OD1 1 
ATOM   3025  O  OD2 . ASP A 1 482 ? 120.184 142.169 130.611 1.00 34.96  ? 457 ASP A OD2 1 
ATOM   3026  N  N   . HIS A 1 483 ? 116.064 145.745 130.491 1.00 28.04  ? 458 HIS A N   1 
ATOM   3027  C  CA  . HIS A 1 483 ? 114.655 146.115 130.493 1.00 24.64  ? 458 HIS A CA  1 
ATOM   3028  C  C   . HIS A 1 483 ? 114.352 147.167 129.441 1.00 29.07  ? 458 HIS A C   1 
ATOM   3029  O  O   . HIS A 1 483 ? 113.352 147.058 128.726 1.00 46.82  ? 458 HIS A O   1 
ATOM   3030  C  CB  . HIS A 1 483 ? 114.215 146.621 131.858 1.00 33.28  ? 458 HIS A CB  1 
ATOM   3031  C  CG  . HIS A 1 483 ? 112.752 146.915 131.929 1.00 27.80  ? 458 HIS A CG  1 
ATOM   3032  N  ND1 . HIS A 1 483 ? 112.221 147.881 132.753 1.00 33.15  ? 458 HIS A ND1 1 
ATOM   3033  C  CD2 . HIS A 1 483 ? 111.706 146.374 131.262 1.00 37.96  ? 458 HIS A CD2 1 
ATOM   3034  C  CE1 . HIS A 1 483 ? 110.911 147.917 132.598 1.00 34.43  ? 458 HIS A CE1 1 
ATOM   3035  N  NE2 . HIS A 1 483 ? 110.572 147.012 131.700 1.00 39.67  ? 458 HIS A NE2 1 
ATOM   3036  N  N   . GLN A 1 484 ? 115.192 148.194 129.329 1.00 33.69  ? 459 GLN A N   1 
ATOM   3037  C  CA  . GLN A 1 484 ? 114.814 149.319 128.484 1.00 16.97  ? 459 GLN A CA  1 
ATOM   3038  C  C   . GLN A 1 484 ? 115.191 149.130 127.021 1.00 35.22  ? 459 GLN A C   1 
ATOM   3039  O  O   . GLN A 1 484 ? 114.417 149.509 126.137 1.00 47.60  ? 459 GLN A O   1 
ATOM   3040  C  CB  . GLN A 1 484 ? 115.445 150.603 129.014 1.00 7.83   ? 459 GLN A CB  1 
ATOM   3041  C  CG  . GLN A 1 484 ? 114.976 150.980 130.394 1.00 22.91  ? 459 GLN A CG  1 
ATOM   3042  C  CD  . GLN A 1 484 ? 113.633 151.659 130.378 1.00 34.01  ? 459 GLN A CD  1 
ATOM   3043  O  OE1 . GLN A 1 484 ? 112.623 151.071 130.752 1.00 38.41  ? 459 GLN A OE1 1 
ATOM   3044  N  NE2 . GLN A 1 484 ? 113.611 152.907 129.942 1.00 43.34  ? 459 GLN A NE2 1 
ATOM   3045  N  N   . TRP A 1 485 ? 116.352 148.549 126.734 1.00 30.35  ? 460 TRP A N   1 
ATOM   3046  C  CA  . TRP A 1 485 ? 116.904 148.586 125.387 1.00 12.61  ? 460 TRP A CA  1 
ATOM   3047  C  C   . TRP A 1 485 ? 117.030 147.234 124.703 1.00 17.78  ? 460 TRP A C   1 
ATOM   3048  O  O   . TRP A 1 485 ? 116.886 147.178 123.484 1.00 35.28  ? 460 TRP A O   1 
ATOM   3049  C  CB  . TRP A 1 485 ? 118.285 149.249 125.402 1.00 9.42   ? 460 TRP A CB  1 
ATOM   3050  C  CG  . TRP A 1 485 ? 118.242 150.738 125.488 1.00 25.65  ? 460 TRP A CG  1 
ATOM   3051  C  CD1 . TRP A 1 485 ? 117.894 151.603 124.500 1.00 42.87  ? 460 TRP A CD1 1 
ATOM   3052  C  CD2 . TRP A 1 485 ? 118.567 151.540 126.625 1.00 23.56  ? 460 TRP A CD2 1 
ATOM   3053  N  NE1 . TRP A 1 485 ? 117.979 152.894 124.949 1.00 30.21  ? 460 TRP A NE1 1 
ATOM   3054  C  CE2 . TRP A 1 485 ? 118.391 152.881 126.254 1.00 28.66  ? 460 TRP A CE2 1 
ATOM   3055  C  CE3 . TRP A 1 485 ? 118.985 151.254 127.924 1.00 29.36  ? 460 TRP A CE3 1 
ATOM   3056  C  CZ2 . TRP A 1 485 ? 118.622 153.930 127.129 1.00 29.20  ? 460 TRP A CZ2 1 
ATOM   3057  C  CZ3 . TRP A 1 485 ? 119.212 152.296 128.790 1.00 26.34  ? 460 TRP A CZ3 1 
ATOM   3058  C  CH2 . TRP A 1 485 ? 119.029 153.616 128.392 1.00 28.46  ? 460 TRP A CH2 1 
ATOM   3059  N  N   . VAL A 1 486 ? 117.313 146.154 125.430 1.00 14.10  ? 461 VAL A N   1 
ATOM   3060  C  CA  . VAL A 1 486 ? 117.530 144.867 124.773 1.00 16.53  ? 461 VAL A CA  1 
ATOM   3061  C  C   . VAL A 1 486 ? 116.212 144.145 124.538 1.00 31.38  ? 461 VAL A C   1 
ATOM   3062  O  O   . VAL A 1 486 ? 115.939 143.671 123.430 1.00 44.86  ? 461 VAL A O   1 
ATOM   3063  C  CB  . VAL A 1 486 ? 118.495 143.990 125.589 1.00 18.07  ? 461 VAL A CB  1 
ATOM   3064  C  CG1 . VAL A 1 486 ? 118.599 142.617 124.961 1.00 2.10   ? 461 VAL A CG1 1 
ATOM   3065  C  CG2 . VAL A 1 486 ? 119.851 144.632 125.677 1.00 28.20  ? 461 VAL A CG2 1 
ATOM   3066  N  N   . ALA A 1 487 ? 115.393 144.017 125.580 1.00 32.41  ? 462 ALA A N   1 
ATOM   3067  C  CA  . ALA A 1 487 ? 114.131 143.296 125.435 1.00 21.94  ? 462 ALA A CA  1 
ATOM   3068  C  C   . ALA A 1 487 ? 113.188 143.953 124.437 1.00 36.57  ? 462 ALA A C   1 
ATOM   3069  O  O   . ALA A 1 487 ? 112.627 143.233 123.595 1.00 46.81  ? 462 ALA A O   1 
ATOM   3070  C  CB  . ALA A 1 487 ? 113.475 143.118 126.807 1.00 18.62  ? 462 ALA A CB  1 
ATOM   3071  N  N   . PRO A 1 488 ? 112.946 145.271 124.468 1.00 29.94  ? 463 PRO A N   1 
ATOM   3072  C  CA  . PRO A 1 488 ? 112.128 145.868 123.400 1.00 25.30  ? 463 PRO A CA  1 
ATOM   3073  C  C   . PRO A 1 488 ? 112.719 145.711 122.011 1.00 35.69  ? 463 PRO A C   1 
ATOM   3074  O  O   . PRO A 1 488 ? 111.970 145.511 121.049 1.00 45.20  ? 463 PRO A O   1 
ATOM   3075  C  CB  . PRO A 1 488 ? 112.047 147.339 123.817 1.00 24.25  ? 463 PRO A CB  1 
ATOM   3076  C  CG  . PRO A 1 488 ? 112.163 147.296 125.278 1.00 27.95  ? 463 PRO A CG  1 
ATOM   3077  C  CD  . PRO A 1 488 ? 113.194 146.248 125.540 1.00 28.35  ? 463 PRO A CD  1 
ATOM   3078  N  N   . ALA A 1 489 ? 114.043 145.799 121.870 1.00 35.91  ? 464 ALA A N   1 
ATOM   3079  C  CA  . ALA A 1 489 ? 114.643 145.633 120.552 1.00 21.87  ? 464 ALA A CA  1 
ATOM   3080  C  C   . ALA A 1 489 ? 114.431 144.223 120.025 1.00 31.16  ? 464 ALA A C   1 
ATOM   3081  O  O   . ALA A 1 489 ? 114.080 144.038 118.855 1.00 49.79  ? 464 ALA A O   1 
ATOM   3082  C  CB  . ALA A 1 489 ? 116.129 145.970 120.598 1.00 14.91  ? 464 ALA A CB  1 
ATOM   3083  N  N   . VAL A 1 490 ? 114.615 143.213 120.876 1.00 21.99  ? 465 VAL A N   1 
ATOM   3084  C  CA  . VAL A 1 490 ? 114.388 141.840 120.440 1.00 25.82  ? 465 VAL A CA  1 
ATOM   3085  C  C   . VAL A 1 490 ? 112.908 141.605 120.161 1.00 36.76  ? 465 VAL A C   1 
ATOM   3086  O  O   . VAL A 1 490 ? 112.550 140.876 119.231 1.00 47.04  ? 465 VAL A O   1 
ATOM   3087  C  CB  . VAL A 1 490 ? 114.942 140.849 121.475 1.00 21.07  ? 465 VAL A CB  1 
ATOM   3088  C  CG1 . VAL A 1 490 ? 114.540 139.440 121.122 1.00 25.17  ? 465 VAL A CG1 1 
ATOM   3089  C  CG2 . VAL A 1 490 ? 116.448 140.958 121.540 1.00 20.06  ? 465 VAL A CG2 1 
ATOM   3090  N  N   . ALA A 1 491 ? 112.024 142.223 120.948 1.00 37.67  ? 466 ALA A N   1 
ATOM   3091  C  CA  . ALA A 1 491 ? 110.592 142.073 120.708 1.00 24.24  ? 466 ALA A CA  1 
ATOM   3092  C  C   . ALA A 1 491 ? 110.196 142.646 119.354 1.00 36.90  ? 466 ALA A C   1 
ATOM   3093  O  O   . ALA A 1 491 ? 109.454 142.014 118.593 1.00 48.04  ? 466 ALA A O   1 
ATOM   3094  C  CB  . ALA A 1 491 ? 109.801 142.746 121.825 1.00 26.25  ? 466 ALA A CB  1 
ATOM   3095  N  N   . THR A 1 492 ? 110.689 143.845 119.029 1.00 33.93  ? 467 THR A N   1 
ATOM   3096  C  CA  . THR A 1 492 ? 110.377 144.435 117.730 1.00 19.69  ? 467 THR A CA  1 
ATOM   3097  C  C   . THR A 1 492 ? 111.006 143.639 116.599 1.00 29.56  ? 467 THR A C   1 
ATOM   3098  O  O   . THR A 1 492 ? 110.406 143.496 115.529 1.00 47.63  ? 467 THR A O   1 
ATOM   3099  C  CB  . THR A 1 492 ? 110.831 145.890 117.668 1.00 17.31  ? 467 THR A CB  1 
ATOM   3100  O  OG1 . THR A 1 492 ? 112.237 145.966 117.908 1.00 38.94  ? 467 THR A OG1 1 
ATOM   3101  C  CG2 . THR A 1 492 ? 110.104 146.716 118.696 1.00 36.87  ? 467 THR A CG2 1 
ATOM   3102  N  N   . ALA A 1 493 ? 112.210 143.106 116.811 1.00 21.28  ? 468 ALA A N   1 
ATOM   3103  C  CA  . ALA A 1 493 ? 112.827 142.276 115.785 1.00 23.33  ? 468 ALA A CA  1 
ATOM   3104  C  C   . ALA A 1 493 ? 111.996 141.030 115.512 1.00 35.81  ? 468 ALA A C   1 
ATOM   3105  O  O   . ALA A 1 493 ? 111.768 140.669 114.353 1.00 52.21  ? 468 ALA A O   1 
ATOM   3106  C  CB  . ALA A 1 493 ? 114.244 141.898 116.202 1.00 18.58  ? 468 ALA A CB  1 
ATOM   3107  N  N   . LYS A 1 494 ? 111.524 140.366 116.567 1.00 31.53  ? 469 LYS A N   1 
ATOM   3108  C  CA  . LYS A 1 494 ? 110.697 139.180 116.382 1.00 26.48  ? 469 LYS A CA  1 
ATOM   3109  C  C   . LYS A 1 494 ? 109.382 139.524 115.701 1.00 32.64  ? 469 LYS A C   1 
ATOM   3110  O  O   . LYS A 1 494 ? 108.918 138.785 114.827 1.00 50.63  ? 469 LYS A O   1 
ATOM   3111  C  CB  . LYS A 1 494 ? 110.434 138.504 117.724 1.00 32.28  ? 469 LYS A CB  1 
ATOM   3112  C  CG  . LYS A 1 494 ? 111.605 137.713 118.252 1.00 37.65  ? 469 LYS A CG  1 
ATOM   3113  C  CD  . LYS A 1 494 ? 111.163 136.728 119.310 1.00 38.18  ? 469 LYS A CD  1 
ATOM   3114  C  CE  . LYS A 1 494 ? 110.255 137.386 120.323 1.00 44.22  ? 469 LYS A CE  1 
ATOM   3115  N  NZ  . LYS A 1 494 ? 109.814 136.424 121.364 1.00 46.04  ? 469 LYS A NZ  1 
ATOM   3116  N  N   . LEU A 1 495 ? 108.758 140.637 116.090 1.00 33.33  ? 470 LEU A N   1 
ATOM   3117  C  CA  . LEU A 1 495 ? 107.477 140.995 115.491 1.00 36.37  ? 470 LEU A CA  1 
ATOM   3118  C  C   . LEU A 1 495 ? 107.632 141.371 114.024 1.00 45.33  ? 470 LEU A C   1 
ATOM   3119  O  O   . LEU A 1 495 ? 106.739 141.100 113.215 1.00 54.42  ? 470 LEU A O   1 
ATOM   3120  C  CB  . LEU A 1 495 ? 106.831 142.130 116.274 1.00 36.28  ? 470 LEU A CB  1 
ATOM   3121  C  CG  . LEU A 1 495 ? 106.212 141.652 117.581 1.00 43.97  ? 470 LEU A CG  1 
ATOM   3122  C  CD1 . LEU A 1 495 ? 105.693 142.815 118.395 1.00 42.13  ? 470 LEU A CD1 1 
ATOM   3123  C  CD2 . LEU A 1 495 ? 105.106 140.665 117.284 1.00 49.97  ? 470 LEU A CD2 1 
ATOM   3124  N  N   . HIS A 1 496 ? 108.747 142.005 113.659 1.00 45.40  ? 471 HIS A N   1 
ATOM   3125  C  CA  . HIS A 1 496 ? 108.973 142.321 112.255 1.00 37.37  ? 471 HIS A CA  1 
ATOM   3126  C  C   . HIS A 1 496 ? 109.344 141.083 111.453 1.00 41.65  ? 471 HIS A C   1 
ATOM   3127  O  O   . HIS A 1 496 ? 108.991 140.984 110.275 1.00 52.56  ? 471 HIS A O   1 
ATOM   3128  C  CB  . HIS A 1 496 ? 110.061 143.381 112.118 1.00 36.05  ? 471 HIS A CB  1 
ATOM   3129  C  CG  . HIS A 1 496 ? 109.560 144.782 112.264 1.00 41.88  ? 471 HIS A CG  1 
ATOM   3130  N  ND1 . HIS A 1 496 ? 108.968 145.242 113.419 1.00 51.27  ? 471 HIS A ND1 1 
ATOM   3131  C  CD2 . HIS A 1 496 ? 109.562 145.823 111.401 1.00 49.24  ? 471 HIS A CD2 1 
ATOM   3132  C  CE1 . HIS A 1 496 ? 108.627 146.508 113.262 1.00 53.27  ? 471 HIS A CE1 1 
ATOM   3133  N  NE2 . HIS A 1 496 ? 108.975 146.884 112.046 1.00 52.50  ? 471 HIS A NE2 1 
ATOM   3134  N  N   . ALA A 1 497 ? 110.057 140.134 112.061 1.00 39.44  ? 472 ALA A N   1 
ATOM   3135  C  CA  . ALA A 1 497 ? 110.450 138.934 111.336 1.00 37.15  ? 472 ALA A CA  1 
ATOM   3136  C  C   . ALA A 1 497 ? 109.299 137.950 111.176 1.00 45.79  ? 472 ALA A C   1 
ATOM   3137  O  O   . ALA A 1 497 ? 109.274 137.194 110.201 1.00 55.05  ? 472 ALA A O   1 
ATOM   3138  C  CB  . ALA A 1 497 ? 111.622 138.256 112.040 1.00 38.75  ? 472 ALA A CB  1 
ATOM   3139  N  N   . ASP A 1 498 ? 108.348 137.936 112.112 1.00 55.38  ? 473 ASP A N   1 
ATOM   3140  C  CA  . ASP A 1 498 ? 107.222 137.016 112.009 1.00 55.65  ? 473 ASP A CA  1 
ATOM   3141  C  C   . ASP A 1 498 ? 106.296 137.357 110.853 1.00 57.20  ? 473 ASP A C   1 
ATOM   3142  O  O   . ASP A 1 498 ? 105.488 136.512 110.457 1.00 61.27  ? 473 ASP A O   1 
ATOM   3143  C  CB  . ASP A 1 498 ? 106.425 137.001 113.311 1.00 54.17  ? 473 ASP A CB  1 
ATOM   3144  C  CG  . ASP A 1 498 ? 107.071 136.146 114.371 1.00 60.08  ? 473 ASP A CG  1 
ATOM   3145  O  OD1 . ASP A 1 498 ? 108.132 135.561 114.081 1.00 55.51  ? 473 ASP A OD1 1 
ATOM   3146  O  OD2 . ASP A 1 498 ? 106.524 136.060 115.489 1.00 65.10  ? 473 ASP A OD2 1 
ATOM   3147  N  N   . TYR A 1 499 ? 106.383 138.570 110.313 1.00 52.90  ? 474 TYR A N   1 
ATOM   3148  C  CA  . TYR A 1 499 ? 105.613 138.959 109.141 1.00 49.21  ? 474 TYR A CA  1 
ATOM   3149  C  C   . TYR A 1 499 ? 106.483 139.047 107.895 1.00 52.70  ? 474 TYR A C   1 
ATOM   3150  O  O   . TYR A 1 499 ? 106.127 139.743 106.941 1.00 58.10  ? 474 TYR A O   1 
ATOM   3151  C  CB  . TYR A 1 499 ? 104.893 140.280 109.395 1.00 47.82  ? 474 TYR A CB  1 
ATOM   3152  C  CG  . TYR A 1 499 ? 103.759 140.145 110.376 1.00 51.22  ? 474 TYR A CG  1 
ATOM   3153  C  CD1 . TYR A 1 499 ? 103.986 140.205 111.738 1.00 56.61  ? 474 TYR A CD1 1 
ATOM   3154  C  CD2 . TYR A 1 499 ? 102.463 139.940 109.940 1.00 56.65  ? 474 TYR A CD2 1 
ATOM   3155  C  CE1 . TYR A 1 499 ? 102.955 140.075 112.636 1.00 61.34  ? 474 TYR A CE1 1 
ATOM   3156  C  CE2 . TYR A 1 499 ? 101.425 139.808 110.831 1.00 56.25  ? 474 TYR A CE2 1 
ATOM   3157  C  CZ  . TYR A 1 499 ? 101.677 139.876 112.177 1.00 59.04  ? 474 TYR A CZ  1 
ATOM   3158  O  OH  . TYR A 1 499 ? 100.643 139.745 113.071 1.00 60.00  ? 474 TYR A OH  1 
ATOM   3159  N  N   . GLN A 1 500 ? 107.624 138.358 107.899 1.00 56.52  ? 475 GLN A N   1 
ATOM   3160  C  CA  . GLN A 1 500 ? 108.479 138.186 106.727 1.00 57.24  ? 475 GLN A CA  1 
ATOM   3161  C  C   . GLN A 1 500 ? 108.972 139.528 106.182 1.00 62.29  ? 475 GLN A C   1 
ATOM   3162  O  O   . GLN A 1 500 ? 108.705 139.907 105.042 1.00 69.15  ? 475 GLN A O   1 
ATOM   3163  C  CB  . GLN A 1 500 ? 107.756 137.379 105.644 1.00 57.70  ? 475 GLN A CB  1 
ATOM   3164  C  CG  . GLN A 1 500 ? 106.973 136.193 106.177 1.00 60.14  ? 475 GLN A CG  1 
ATOM   3165  C  CD  . GLN A 1 500 ? 107.845 134.984 106.431 1.00 67.22  ? 475 GLN A CD  1 
ATOM   3166  O  OE1 . GLN A 1 500 ? 108.920 134.847 105.850 1.00 71.07  ? 475 GLN A OE1 1 
ATOM   3167  N  NE2 . GLN A 1 500 ? 107.386 134.097 107.304 1.00 66.30  ? 475 GLN A NE2 1 
ATOM   3168  N  N   . SER A 1 501 ? 109.706 140.247 107.028 1.00 52.04  ? 476 SER A N   1 
ATOM   3169  C  CA  . SER A 1 501 ? 110.446 141.426 106.609 1.00 48.34  ? 476 SER A CA  1 
ATOM   3170  C  C   . SER A 1 501 ? 111.888 141.251 107.070 1.00 50.46  ? 476 SER A C   1 
ATOM   3171  O  O   . SER A 1 501 ? 112.127 140.983 108.258 1.00 58.33  ? 476 SER A O   1 
ATOM   3172  C  CB  . SER A 1 501 ? 109.843 142.710 107.184 1.00 42.63  ? 476 SER A CB  1 
ATOM   3173  O  OG  . SER A 1 501 ? 109.559 142.566 108.559 1.00 57.57  ? 476 SER A OG  1 
ATOM   3174  N  N   . PRO A 1 502 ? 112.867 141.382 106.177 1.00 43.94  ? 477 PRO A N   1 
ATOM   3175  C  CA  . PRO A 1 502 ? 114.253 141.042 106.537 1.00 44.48  ? 477 PRO A CA  1 
ATOM   3176  C  C   . PRO A 1 502 ? 114.770 141.911 107.671 1.00 47.71  ? 477 PRO A C   1 
ATOM   3177  O  O   . PRO A 1 502 ? 114.872 143.131 107.545 1.00 66.66  ? 477 PRO A O   1 
ATOM   3178  C  CB  . PRO A 1 502 ? 115.025 141.292 105.236 1.00 47.99  ? 477 PRO A CB  1 
ATOM   3179  C  CG  . PRO A 1 502 ? 113.994 141.301 104.163 1.00 50.62  ? 477 PRO A CG  1 
ATOM   3180  C  CD  . PRO A 1 502 ? 112.757 141.845 104.787 1.00 48.37  ? 477 PRO A CD  1 
ATOM   3181  N  N   . VAL A 1 503 ? 115.108 141.267 108.784 1.00 25.31  ? 478 VAL A N   1 
ATOM   3182  C  CA  . VAL A 1 503 ? 115.591 141.946 109.979 1.00 19.39  ? 478 VAL A CA  1 
ATOM   3183  C  C   . VAL A 1 503 ? 117.011 141.482 110.253 1.00 24.65  ? 478 VAL A C   1 
ATOM   3184  O  O   . VAL A 1 503 ? 117.269 140.278 110.332 1.00 45.72  ? 478 VAL A O   1 
ATOM   3185  C  CB  . VAL A 1 503 ? 114.688 141.669 111.191 1.00 24.51  ? 478 VAL A CB  1 
ATOM   3186  C  CG1 . VAL A 1 503 ? 115.351 142.149 112.454 1.00 27.24  ? 478 VAL A CG1 1 
ATOM   3187  C  CG2 . VAL A 1 503 ? 113.356 142.342 111.008 1.00 35.60  ? 478 VAL A CG2 1 
ATOM   3188  N  N   . TYR A 1 504 ? 117.926 142.432 110.390 1.00 25.95  ? 479 TYR A N   1 
ATOM   3189  C  CA  . TYR A 1 504 ? 119.315 142.143 110.718 1.00 30.82  ? 479 TYR A CA  1 
ATOM   3190  C  C   . TYR A 1 504 ? 119.615 142.723 112.091 1.00 38.95  ? 479 TYR A C   1 
ATOM   3191  O  O   . TYR A 1 504 ? 119.523 143.937 112.284 1.00 50.97  ? 479 TYR A O   1 
ATOM   3192  C  CB  . TYR A 1 504 ? 120.261 142.725 109.670 1.00 32.27  ? 479 TYR A CB  1 
ATOM   3193  C  CG  . TYR A 1 504 ? 120.153 142.076 108.312 1.00 26.05  ? 479 TYR A CG  1 
ATOM   3194  C  CD1 . TYR A 1 504 ? 119.122 142.397 107.451 1.00 30.92  ? 479 TYR A CD1 1 
ATOM   3195  C  CD2 . TYR A 1 504 ? 121.085 141.148 107.894 1.00 34.10  ? 479 TYR A CD2 1 
ATOM   3196  C  CE1 . TYR A 1 504 ? 119.020 141.811 106.218 1.00 31.50  ? 479 TYR A CE1 1 
ATOM   3197  C  CE2 . TYR A 1 504 ? 120.990 140.556 106.663 1.00 31.28  ? 479 TYR A CE2 1 
ATOM   3198  C  CZ  . TYR A 1 504 ? 119.956 140.890 105.828 1.00 32.98  ? 479 TYR A CZ  1 
ATOM   3199  O  OH  . TYR A 1 504 ? 119.857 140.300 104.592 1.00 43.20  ? 479 TYR A OH  1 
ATOM   3200  N  N   . PHE A 1 505 ? 119.984 141.865 113.032 1.00 21.50  ? 480 PHE A N   1 
ATOM   3201  C  CA  . PHE A 1 505 ? 120.223 142.265 114.411 1.00 13.13  ? 480 PHE A CA  1 
ATOM   3202  C  C   . PHE A 1 505 ? 121.720 142.371 114.650 1.00 24.05  ? 480 PHE A C   1 
ATOM   3203  O  O   . PHE A 1 505 ? 122.469 141.460 114.293 1.00 43.45  ? 480 PHE A O   1 
ATOM   3204  C  CB  . PHE A 1 505 ? 119.600 141.255 115.372 1.00 17.61  ? 480 PHE A CB  1 
ATOM   3205  C  CG  . PHE A 1 505 ? 119.336 141.797 116.742 1.00 23.34  ? 480 PHE A CG  1 
ATOM   3206  C  CD1 . PHE A 1 505 ? 118.144 142.416 117.034 1.00 34.33  ? 480 PHE A CD1 1 
ATOM   3207  C  CD2 . PHE A 1 505 ? 120.274 141.668 117.742 1.00 35.62  ? 480 PHE A CD2 1 
ATOM   3208  C  CE1 . PHE A 1 505 ? 117.901 142.905 118.291 1.00 40.97  ? 480 PHE A CE1 1 
ATOM   3209  C  CE2 . PHE A 1 505 ? 120.032 142.156 119.000 1.00 27.64  ? 480 PHE A CE2 1 
ATOM   3210  C  CZ  . PHE A 1 505 ? 118.847 142.774 119.274 1.00 24.25  ? 480 PHE A CZ  1 
ATOM   3211  N  N   . TYR A 1 506 ? 122.156 143.479 115.244 1.00 26.29  ? 481 TYR A N   1 
ATOM   3212  C  CA  . TYR A 1 506 ? 123.565 143.674 115.543 1.00 18.43  ? 481 TYR A CA  1 
ATOM   3213  C  C   . TYR A 1 506 ? 123.748 144.074 116.996 1.00 26.31  ? 481 TYR A C   1 
ATOM   3214  O  O   . TYR A 1 506 ? 122.884 144.714 117.600 1.00 48.46  ? 481 TYR A O   1 
ATOM   3215  C  CB  . TYR A 1 506 ? 124.207 144.727 114.620 1.00 26.70  ? 481 TYR A CB  1 
ATOM   3216  C  CG  . TYR A 1 506 ? 124.075 146.169 115.059 1.00 33.43  ? 481 TYR A CG  1 
ATOM   3217  C  CD1 . TYR A 1 506 ? 124.934 146.714 115.997 1.00 41.32  ? 481 TYR A CD1 1 
ATOM   3218  C  CD2 . TYR A 1 506 ? 123.119 146.997 114.500 1.00 29.60  ? 481 TYR A CD2 1 
ATOM   3219  C  CE1 . TYR A 1 506 ? 124.820 148.020 116.390 1.00 42.22  ? 481 TYR A CE1 1 
ATOM   3220  C  CE2 . TYR A 1 506 ? 123.004 148.311 114.885 1.00 22.89  ? 481 TYR A CE2 1 
ATOM   3221  C  CZ  . TYR A 1 506 ? 123.856 148.812 115.833 1.00 34.13  ? 481 TYR A CZ  1 
ATOM   3222  O  OH  . TYR A 1 506 ? 123.758 150.118 116.230 1.00 46.25  ? 481 TYR A OH  1 
ATOM   3223  N  N   . THR A 1 507 ? 124.897 143.703 117.548 1.00 35.36  ? 482 THR A N   1 
ATOM   3224  C  CA  . THR A 1 507 ? 125.286 144.088 118.895 1.00 32.21  ? 482 THR A CA  1 
ATOM   3225  C  C   . THR A 1 507 ? 126.647 144.762 118.843 1.00 44.80  ? 482 THR A C   1 
ATOM   3226  O  O   . THR A 1 507 ? 127.592 144.217 118.267 1.00 65.47  ? 482 THR A O   1 
ATOM   3227  C  CB  . THR A 1 507 ? 125.323 142.879 119.816 1.00 26.62  ? 482 THR A CB  1 
ATOM   3228  O  OG1 . THR A 1 507 ? 124.134 142.112 119.623 1.00 42.56  ? 482 THR A OG1 1 
ATOM   3229  C  CG2 . THR A 1 507 ? 125.381 143.327 121.246 1.00 33.79  ? 482 THR A CG2 1 
ATOM   3230  N  N   . PHE A 1 508 ? 126.742 145.940 119.443 1.00 33.13  ? 483 PHE A N   1 
ATOM   3231  C  CA  . PHE A 1 508 ? 127.949 146.752 119.403 1.00 28.42  ? 483 PHE A CA  1 
ATOM   3232  C  C   . PHE A 1 508 ? 128.649 146.683 120.750 1.00 37.90  ? 483 PHE A C   1 
ATOM   3233  O  O   . PHE A 1 508 ? 128.022 146.904 121.788 1.00 59.33  ? 483 PHE A O   1 
ATOM   3234  C  CB  . PHE A 1 508 ? 127.615 148.199 119.053 1.00 28.10  ? 483 PHE A CB  1 
ATOM   3235  C  CG  . PHE A 1 508 ? 128.744 148.939 118.412 1.00 40.32  ? 483 PHE A CG  1 
ATOM   3236  C  CD1 . PHE A 1 508 ? 129.044 148.746 117.080 1.00 46.74  ? 483 PHE A CD1 1 
ATOM   3237  C  CD2 . PHE A 1 508 ? 129.505 149.829 119.139 1.00 46.53  ? 483 PHE A CD2 1 
ATOM   3238  C  CE1 . PHE A 1 508 ? 130.080 149.421 116.489 1.00 49.18  ? 483 PHE A CE1 1 
ATOM   3239  C  CE2 . PHE A 1 508 ? 130.541 150.508 118.550 1.00 46.87  ? 483 PHE A CE2 1 
ATOM   3240  C  CZ  . PHE A 1 508 ? 130.830 150.303 117.225 1.00 49.42  ? 483 PHE A CZ  1 
ATOM   3241  N  N   . TYR A 1 509 ? 129.944 146.386 120.731 1.00 43.00  ? 484 TYR A N   1 
ATOM   3242  C  CA  . TYR A 1 509 ? 130.699 146.150 121.954 1.00 48.52  ? 484 TYR A CA  1 
ATOM   3243  C  C   . TYR A 1 509 ? 131.844 147.130 122.148 1.00 57.81  ? 484 TYR A C   1 
ATOM   3244  O  O   . TYR A 1 509 ? 132.011 147.667 123.248 1.00 61.57  ? 484 TYR A O   1 
ATOM   3245  C  CB  . TYR A 1 509 ? 131.220 144.709 121.957 1.00 49.35  ? 484 TYR A CB  1 
ATOM   3246  C  CG  . TYR A 1 509 ? 130.282 143.745 122.638 1.00 54.69  ? 484 TYR A CG  1 
ATOM   3247  C  CD1 . TYR A 1 509 ? 129.261 143.131 121.936 1.00 57.24  ? 484 TYR A CD1 1 
ATOM   3248  C  CD2 . TYR A 1 509 ? 130.386 143.484 123.990 1.00 57.49  ? 484 TYR A CD2 1 
ATOM   3249  C  CE1 . TYR A 1 509 ? 128.393 142.260 122.558 1.00 55.01  ? 484 TYR A CE1 1 
ATOM   3250  C  CE2 . TYR A 1 509 ? 129.524 142.609 124.616 1.00 53.96  ? 484 TYR A CE2 1 
ATOM   3251  C  CZ  . TYR A 1 509 ? 128.529 142.004 123.897 1.00 54.06  ? 484 TYR A CZ  1 
ATOM   3252  O  OH  . TYR A 1 509 ? 127.667 141.138 124.523 1.00 63.30  ? 484 TYR A OH  1 
ATOM   3253  N  N   . HIS A 1 510 ? 132.641 147.381 121.115 1.00 62.50  ? 485 HIS A N   1 
ATOM   3254  C  CA  . HIS A 1 510 ? 133.779 148.279 121.244 1.00 57.30  ? 485 HIS A CA  1 
ATOM   3255  C  C   . HIS A 1 510 ? 133.318 149.712 121.480 1.00 57.79  ? 485 HIS A C   1 
ATOM   3256  O  O   . HIS A 1 510 ? 132.205 150.098 121.121 1.00 60.21  ? 485 HIS A O   1 
ATOM   3257  C  CB  . HIS A 1 510 ? 134.646 148.209 119.990 1.00 56.68  ? 485 HIS A CB  1 
ATOM   3258  C  CG  . HIS A 1 510 ? 135.991 148.842 120.147 1.00 62.18  ? 485 HIS A CG  1 
ATOM   3259  N  ND1 . HIS A 1 510 ? 137.016 148.246 120.848 1.00 65.52  ? 485 HIS A ND1 1 
ATOM   3260  C  CD2 . HIS A 1 510 ? 136.481 150.018 119.689 1.00 62.22  ? 485 HIS A CD2 1 
ATOM   3261  C  CE1 . HIS A 1 510 ? 138.080 149.029 120.818 1.00 65.21  ? 485 HIS A CE1 1 
ATOM   3262  N  NE2 . HIS A 1 510 ? 137.781 150.110 120.122 1.00 67.45  ? 485 HIS A NE2 1 
ATOM   3263  N  N   . HIS A 1 511 ? 134.185 150.504 122.105 1.00 73.91  ? 486 HIS A N   1 
ATOM   3264  C  CA  . HIS A 1 511 ? 133.899 151.910 122.341 1.00 77.41  ? 486 HIS A CA  1 
ATOM   3265  C  C   . HIS A 1 511 ? 135.205 152.686 122.411 1.00 80.58  ? 486 HIS A C   1 
ATOM   3266  O  O   . HIS A 1 511 ? 136.237 152.157 122.830 1.00 78.73  ? 486 HIS A O   1 
ATOM   3267  C  CB  . HIS A 1 511 ? 133.099 152.120 123.628 1.00 73.85  ? 486 HIS A CB  1 
ATOM   3268  C  CG  . HIS A 1 511 ? 133.887 151.870 124.874 1.00 76.66  ? 486 HIS A CG  1 
ATOM   3269  N  ND1 . HIS A 1 511 ? 134.722 150.784 125.021 1.00 76.05  ? 486 HIS A ND1 1 
ATOM   3270  C  CD2 . HIS A 1 511 ? 133.965 152.564 126.033 1.00 75.71  ? 486 HIS A CD2 1 
ATOM   3271  C  CE1 . HIS A 1 511 ? 135.281 150.820 126.217 1.00 79.79  ? 486 HIS A CE1 1 
ATOM   3272  N  NE2 . HIS A 1 511 ? 134.838 151.890 126.851 1.00 82.99  ? 486 HIS A NE2 1 
ATOM   3273  N  N   . CYS A 1 512 ? 135.146 153.948 121.997 1.00 91.88  ? 487 CYS A N   1 
ATOM   3274  C  CA  . CYS A 1 512 ? 136.322 154.805 122.029 1.00 89.04  ? 487 CYS A CA  1 
ATOM   3275  C  C   . CYS A 1 512 ? 136.701 155.142 123.464 1.00 90.24  ? 487 CYS A C   1 
ATOM   3276  O  O   . CYS A 1 512 ? 135.841 155.435 124.298 1.00 93.28  ? 487 CYS A O   1 
ATOM   3277  C  CB  . CYS A 1 512 ? 136.061 156.088 121.243 1.00 91.70  ? 487 CYS A CB  1 
ATOM   3278  S  SG  . CYS A 1 512 ? 134.352 156.666 121.322 1.00 95.35  ? 487 CYS A SG  1 
ATOM   3279  N  N   . GLN A 1 513 ? 138.000 155.115 123.746 1.00 99.13  ? 488 GLN A N   1 
ATOM   3280  C  CA  . GLN A 1 513 ? 138.503 155.394 125.089 1.00 100.02 ? 488 GLN A CA  1 
ATOM   3281  C  C   . GLN A 1 513 ? 138.308 156.873 125.391 1.00 101.10 ? 488 GLN A C   1 
ATOM   3282  O  O   . GLN A 1 513 ? 139.123 157.712 125.005 1.00 101.12 ? 488 GLN A O   1 
ATOM   3283  C  CB  . GLN A 1 513 ? 139.970 155.000 125.200 1.00 100.74 ? 488 GLN A CB  1 
ATOM   3284  C  CG  . GLN A 1 513 ? 140.200 153.550 125.583 1.00 100.66 ? 488 GLN A CG  1 
ATOM   3285  C  CD  . GLN A 1 513 ? 140.179 152.622 124.386 1.00 102.97 ? 488 GLN A CD  1 
ATOM   3286  O  OE1 . GLN A 1 513 ? 140.821 152.886 123.369 1.00 103.24 ? 488 GLN A OE1 1 
ATOM   3287  N  NE2 . GLN A 1 513 ? 139.441 151.524 124.501 1.00 102.19 ? 488 GLN A NE2 1 
ATOM   3288  N  N   . ALA A 1 514 ? 137.237 157.195 126.110 1.00 106.70 ? 489 ALA A N   1 
ATOM   3289  C  CA  . ALA A 1 514 ? 136.883 158.579 126.389 1.00 105.15 ? 489 ALA A CA  1 
ATOM   3290  C  C   . ALA A 1 514 ? 137.806 159.143 127.465 1.00 106.90 ? 489 ALA A C   1 
ATOM   3291  O  O   . ALA A 1 514 ? 138.835 158.556 127.811 1.00 108.74 ? 489 ALA A O   1 
ATOM   3292  C  CB  . ALA A 1 514 ? 135.415 158.675 126.790 1.00 104.44 ? 489 ALA A CB  1 
ATOM   3293  N  N   . GLU A 1 515 ? 137.447 160.306 128.008 1.00 109.13 ? 490 GLU A N   1 
ATOM   3294  C  CA  . GLU A 1 515 ? 138.239 160.954 129.047 1.00 110.54 ? 490 GLU A CA  1 
ATOM   3295  C  C   . GLU A 1 515 ? 137.714 160.638 130.443 1.00 110.88 ? 490 GLU A C   1 
ATOM   3296  O  O   . GLU A 1 515 ? 138.429 160.053 131.261 1.00 110.95 ? 490 GLU A O   1 
ATOM   3297  C  CB  . GLU A 1 515 ? 138.266 162.471 128.817 1.00 107.34 ? 490 GLU A CB  1 
ATOM   3298  N  N   . GLY A 1 516 ? 136.468 161.004 130.726 1.00 110.92 ? 491 GLY A N   1 
ATOM   3299  C  CA  . GLY A 1 516 ? 135.873 160.788 132.026 1.00 111.00 ? 491 GLY A CA  1 
ATOM   3300  C  C   . GLY A 1 516 ? 135.165 159.469 132.205 1.00 111.72 ? 491 GLY A C   1 
ATOM   3301  O  O   . GLY A 1 516 ? 134.559 159.236 133.256 1.00 109.74 ? 491 GLY A O   1 
ATOM   3302  N  N   . ARG A 1 517 ? 135.220 158.594 131.209 1.00 101.51 ? 492 ARG A N   1 
ATOM   3303  C  CA  . ARG A 1 517 ? 134.513 157.327 131.292 1.00 99.93  ? 492 ARG A CA  1 
ATOM   3304  C  C   . ARG A 1 517 ? 135.208 156.388 132.275 1.00 104.60 ? 492 ARG A C   1 
ATOM   3305  O  O   . ARG A 1 517 ? 136.436 156.265 132.254 1.00 105.58 ? 492 ARG A O   1 
ATOM   3306  C  CB  . ARG A 1 517 ? 134.431 156.670 129.918 1.00 95.64  ? 492 ARG A CB  1 
ATOM   3307  C  CG  . ARG A 1 517 ? 133.439 155.535 129.866 1.00 98.43  ? 492 ARG A CG  1 
ATOM   3308  C  CD  . ARG A 1 517 ? 132.015 156.061 129.942 1.00 99.55  ? 492 ARG A CD  1 
ATOM   3309  N  NE  . ARG A 1 517 ? 131.556 156.770 128.752 1.00 97.79  ? 492 ARG A NE  1 
ATOM   3310  C  CZ  . ARG A 1 517 ? 131.630 156.322 127.504 1.00 98.80  ? 492 ARG A CZ  1 
ATOM   3311  N  NH1 . ARG A 1 517 ? 132.083 155.110 127.222 1.00 96.72  ? 492 ARG A NH1 1 
ATOM   3312  N  NH2 . ARG A 1 517 ? 131.212 157.102 126.512 1.00 97.87  ? 492 ARG A NH2 1 
ATOM   3313  N  N   . PRO A 1 518 ? 134.454 155.717 133.146 1.00 105.54 ? 493 PRO A N   1 
ATOM   3314  C  CA  . PRO A 1 518 ? 135.073 154.747 134.056 1.00 101.59 ? 493 PRO A CA  1 
ATOM   3315  C  C   . PRO A 1 518 ? 135.670 153.574 133.296 1.00 102.31 ? 493 PRO A C   1 
ATOM   3316  O  O   . PRO A 1 518 ? 135.205 153.199 132.218 1.00 100.88 ? 493 PRO A O   1 
ATOM   3317  C  CB  . PRO A 1 518 ? 133.907 154.300 134.946 1.00 100.50 ? 493 PRO A CB  1 
ATOM   3318  C  CG  . PRO A 1 518 ? 132.893 155.383 134.830 1.00 102.82 ? 493 PRO A CG  1 
ATOM   3319  C  CD  . PRO A 1 518 ? 133.024 155.909 133.436 1.00 103.48 ? 493 PRO A CD  1 
ATOM   3320  N  N   . GLU A 1 519 ? 136.724 152.995 133.876 1.00 103.17 ? 494 GLU A N   1 
ATOM   3321  C  CA  . GLU A 1 519 ? 137.392 151.864 133.240 1.00 102.93 ? 494 GLU A CA  1 
ATOM   3322  C  C   . GLU A 1 519 ? 136.474 150.651 133.157 1.00 104.39 ? 494 GLU A C   1 
ATOM   3323  O  O   . GLU A 1 519 ? 136.468 149.936 132.149 1.00 103.38 ? 494 GLU A O   1 
ATOM   3324  C  CB  . GLU A 1 519 ? 138.672 151.515 133.998 1.00 102.88 ? 494 GLU A CB  1 
ATOM   3325  N  N   . TRP A 1 520 ? 135.694 150.399 134.210 1.00 96.25  ? 495 TRP A N   1 
ATOM   3326  C  CA  . TRP A 1 520 ? 134.786 149.259 134.209 1.00 95.32  ? 495 TRP A CA  1 
ATOM   3327  C  C   . TRP A 1 520 ? 133.650 149.421 133.209 1.00 98.04  ? 495 TRP A C   1 
ATOM   3328  O  O   . TRP A 1 520 ? 132.992 148.430 132.875 1.00 97.65  ? 495 TRP A O   1 
ATOM   3329  C  CB  . TRP A 1 520 ? 134.213 149.044 135.609 1.00 94.03  ? 495 TRP A CB  1 
ATOM   3330  C  CG  . TRP A 1 520 ? 133.429 150.214 136.115 1.00 95.03  ? 495 TRP A CG  1 
ATOM   3331  C  CD1 . TRP A 1 520 ? 133.896 151.242 136.877 1.00 94.11  ? 495 TRP A CD1 1 
ATOM   3332  C  CD2 . TRP A 1 520 ? 132.037 150.473 135.901 1.00 99.57  ? 495 TRP A CD2 1 
ATOM   3333  N  NE1 . TRP A 1 520 ? 132.883 152.128 137.149 1.00 94.75  ? 495 TRP A NE1 1 
ATOM   3334  C  CE2 . TRP A 1 520 ? 131.731 151.679 136.560 1.00 97.58  ? 495 TRP A CE2 1 
ATOM   3335  C  CE3 . TRP A 1 520 ? 131.019 149.803 135.215 1.00 97.16  ? 495 TRP A CE3 1 
ATOM   3336  C  CZ2 . TRP A 1 520 ? 130.453 152.229 136.555 1.00 94.60  ? 495 TRP A CZ2 1 
ATOM   3337  C  CZ3 . TRP A 1 520 ? 129.753 150.350 135.211 1.00 98.03  ? 495 TRP A CZ3 1 
ATOM   3338  C  CH2 . TRP A 1 520 ? 129.480 151.551 135.876 1.00 96.70  ? 495 TRP A CH2 1 
ATOM   3339  N  N   . ALA A 1 521 ? 133.406 150.638 132.730 1.00 99.08  ? 496 ALA A N   1 
ATOM   3340  C  CA  . ALA A 1 521 ? 132.302 150.891 131.820 1.00 97.37  ? 496 ALA A CA  1 
ATOM   3341  C  C   . ALA A 1 521 ? 132.583 150.281 130.450 1.00 94.88  ? 496 ALA A C   1 
ATOM   3342  O  O   . ALA A 1 521 ? 133.702 149.871 130.133 1.00 94.10  ? 496 ALA A O   1 
ATOM   3343  C  CB  . ALA A 1 521 ? 132.048 152.391 131.687 1.00 92.94  ? 496 ALA A CB  1 
ATOM   3344  N  N   . ASP A 1 522 ? 131.538 150.224 129.631 1.00 77.40  ? 497 ASP A N   1 
ATOM   3345  C  CA  . ASP A 1 522 ? 131.632 149.672 128.290 1.00 76.19  ? 497 ASP A CA  1 
ATOM   3346  C  C   . ASP A 1 522 ? 130.805 150.549 127.356 1.00 81.86  ? 497 ASP A C   1 
ATOM   3347  O  O   . ASP A 1 522 ? 130.433 151.673 127.703 1.00 86.04  ? 497 ASP A O   1 
ATOM   3348  C  CB  . ASP A 1 522 ? 131.193 148.205 128.278 1.00 71.82  ? 497 ASP A CB  1 
ATOM   3349  C  CG  . ASP A 1 522 ? 131.693 147.469 127.062 1.00 79.42  ? 497 ASP A CG  1 
ATOM   3350  O  OD1 . ASP A 1 522 ? 131.179 147.741 125.959 1.00 80.42  ? 497 ASP A OD1 1 
ATOM   3351  O  OD2 . ASP A 1 522 ? 132.612 146.637 127.202 1.00 83.68  ? 497 ASP A OD2 1 
ATOM   3352  N  N   . ALA A 1 523 ? 130.529 150.038 126.155 1.00 59.71  ? 498 ALA A N   1 
ATOM   3353  C  CA  . ALA A 1 523 ? 129.839 150.813 125.133 1.00 53.77  ? 498 ALA A CA  1 
ATOM   3354  C  C   . ALA A 1 523 ? 128.493 151.296 125.640 1.00 57.65  ? 498 ALA A C   1 
ATOM   3355  O  O   . ALA A 1 523 ? 127.572 150.498 125.816 1.00 63.38  ? 498 ALA A O   1 
ATOM   3356  C  CB  . ALA A 1 523 ? 129.655 149.981 123.866 1.00 49.50  ? 498 ALA A CB  1 
ATOM   3357  N  N   . ALA A 1 524 ? 128.366 152.599 125.858 1.00 55.05  ? 499 ALA A N   1 
ATOM   3358  C  CA  . ALA A 1 524 ? 127.179 153.171 126.471 1.00 49.96  ? 499 ALA A CA  1 
ATOM   3359  C  C   . ALA A 1 524 ? 126.175 153.570 125.395 1.00 50.04  ? 499 ALA A C   1 
ATOM   3360  O  O   . ALA A 1 524 ? 126.326 153.241 124.217 1.00 61.39  ? 499 ALA A O   1 
ATOM   3361  C  CB  . ALA A 1 524 ? 127.563 154.354 127.352 1.00 52.26  ? 499 ALA A CB  1 
ATOM   3362  N  N   . HIS A 1 525 ? 125.131 154.286 125.796 1.00 44.93  ? 500 HIS A N   1 
ATOM   3363  C  CA  . HIS A 1 525 ? 124.116 154.717 124.848 1.00 52.04  ? 500 HIS A CA  1 
ATOM   3364  C  C   . HIS A 1 525 ? 124.685 155.782 123.923 1.00 60.58  ? 500 HIS A C   1 
ATOM   3365  O  O   . HIS A 1 525 ? 125.328 156.733 124.375 1.00 63.78  ? 500 HIS A O   1 
ATOM   3366  C  CB  . HIS A 1 525 ? 122.898 155.257 125.588 1.00 49.11  ? 500 HIS A CB  1 
ATOM   3367  C  CG  . HIS A 1 525 ? 121.725 155.527 124.701 1.00 55.25  ? 500 HIS A CG  1 
ATOM   3368  N  ND1 . HIS A 1 525 ? 120.692 156.360 125.069 1.00 55.26  ? 500 HIS A ND1 1 
ATOM   3369  C  CD2 . HIS A 1 525 ? 121.421 155.073 123.464 1.00 53.40  ? 500 HIS A CD2 1 
ATOM   3370  C  CE1 . HIS A 1 525 ? 119.803 156.410 124.095 1.00 52.15  ? 500 HIS A CE1 1 
ATOM   3371  N  NE2 . HIS A 1 525 ? 120.221 155.638 123.109 1.00 53.05  ? 500 HIS A NE2 1 
ATOM   3372  N  N   . GLY A 1 526 ? 124.447 155.625 122.627 1.00 59.42  ? 501 GLY A N   1 
ATOM   3373  C  CA  . GLY A 1 526 ? 124.946 156.580 121.665 1.00 57.30  ? 501 GLY A CA  1 
ATOM   3374  C  C   . GLY A 1 526 ? 126.418 156.465 121.356 1.00 61.03  ? 501 GLY A C   1 
ATOM   3375  O  O   . GLY A 1 526 ? 126.974 157.379 120.741 1.00 67.01  ? 501 GLY A O   1 
ATOM   3376  N  N   . ASP A 1 527 ? 127.071 155.378 121.764 1.00 58.78  ? 502 ASP A N   1 
ATOM   3377  C  CA  . ASP A 1 527 ? 128.477 155.156 121.464 1.00 58.17  ? 502 ASP A CA  1 
ATOM   3378  C  C   . ASP A 1 527 ? 128.682 154.348 120.192 1.00 65.61  ? 502 ASP A C   1 
ATOM   3379  O  O   . ASP A 1 527 ? 129.707 153.673 120.055 1.00 74.95  ? 502 ASP A O   1 
ATOM   3380  C  CB  . ASP A 1 527 ? 129.169 154.471 122.641 1.00 59.88  ? 502 ASP A CB  1 
ATOM   3381  C  CG  . ASP A 1 527 ? 129.853 155.457 123.561 1.00 67.43  ? 502 ASP A CG  1 
ATOM   3382  O  OD1 . ASP A 1 527 ? 129.800 156.669 123.272 1.00 65.96  ? 502 ASP A OD1 1 
ATOM   3383  O  OD2 . ASP A 1 527 ? 130.441 155.027 124.574 1.00 73.09  ? 502 ASP A OD2 1 
ATOM   3384  N  N   . GLU A 1 528 ? 127.718 154.380 119.273 1.00 60.05  ? 503 GLU A N   1 
ATOM   3385  C  CA  . GLU A 1 528 ? 127.907 153.870 117.926 1.00 55.33  ? 503 GLU A CA  1 
ATOM   3386  C  C   . GLU A 1 528 ? 127.851 154.960 116.873 1.00 60.03  ? 503 GLU A C   1 
ATOM   3387  O  O   . GLU A 1 528 ? 128.277 154.723 115.741 1.00 72.18  ? 503 GLU A O   1 
ATOM   3388  C  CB  . GLU A 1 528 ? 126.852 152.810 117.592 1.00 52.69  ? 503 GLU A CB  1 
ATOM   3389  C  CG  . GLU A 1 528 ? 125.469 153.375 117.359 1.00 65.64  ? 503 GLU A CG  1 
ATOM   3390  C  CD  . GLU A 1 528 ? 124.697 153.580 118.647 1.00 74.14  ? 503 GLU A CD  1 
ATOM   3391  O  OE1 . GLU A 1 528 ? 124.863 152.758 119.572 1.00 69.69  ? 503 GLU A OE1 1 
ATOM   3392  O  OE2 . GLU A 1 528 ? 123.923 154.559 118.734 1.00 72.64  ? 503 GLU A OE2 1 
ATOM   3393  N  N   . LEU A 1 529 ? 127.329 156.135 117.215 1.00 57.01  ? 504 LEU A N   1 
ATOM   3394  C  CA  . LEU A 1 529 ? 127.319 157.251 116.276 1.00 59.05  ? 504 LEU A CA  1 
ATOM   3395  C  C   . LEU A 1 529 ? 128.705 157.665 115.795 1.00 62.09  ? 504 LEU A C   1 
ATOM   3396  O  O   . LEU A 1 529 ? 128.837 157.966 114.597 1.00 68.00  ? 504 LEU A O   1 
ATOM   3397  C  CB  . LEU A 1 529 ? 126.585 158.442 116.899 1.00 61.20  ? 504 LEU A CB  1 
ATOM   3398  C  CG  . LEU A 1 529 ? 125.071 158.287 116.977 1.00 56.62  ? 504 LEU A CG  1 
ATOM   3399  C  CD1 . LEU A 1 529 ? 124.443 159.551 117.512 1.00 64.71  ? 504 LEU A CD1 1 
ATOM   3400  C  CD2 . LEU A 1 529 ? 124.508 157.945 115.616 1.00 55.85  ? 504 LEU A CD2 1 
ATOM   3401  N  N   . PRO A 1 530 ? 129.748 157.741 116.632 1.00 56.78  ? 505 PRO A N   1 
ATOM   3402  C  CA  . PRO A 1 530 ? 131.062 158.116 116.085 1.00 55.01  ? 505 PRO A CA  1 
ATOM   3403  C  C   . PRO A 1 530 ? 131.526 157.197 114.975 1.00 59.38  ? 505 PRO A C   1 
ATOM   3404  O  O   . PRO A 1 530 ? 132.132 157.660 114.003 1.00 69.95  ? 505 PRO A O   1 
ATOM   3405  C  CB  . PRO A 1 530 ? 131.990 158.034 117.302 1.00 59.16  ? 505 PRO A CB  1 
ATOM   3406  C  CG  . PRO A 1 530 ? 131.117 158.136 118.465 1.00 58.03  ? 505 PRO A CG  1 
ATOM   3407  C  CD  . PRO A 1 530 ? 129.807 157.547 118.090 1.00 57.61  ? 505 PRO A CD  1 
ATOM   3408  N  N   . TYR A 1 531 ? 131.249 155.901 115.091 1.00 53.34  ? 506 TYR A N   1 
ATOM   3409  C  CA  . TYR A 1 531 ? 131.714 154.946 114.095 1.00 52.30  ? 506 TYR A CA  1 
ATOM   3410  C  C   . TYR A 1 531 ? 130.864 154.987 112.833 1.00 57.94  ? 506 TYR A C   1 
ATOM   3411  O  O   . TYR A 1 531 ? 131.389 154.840 111.726 1.00 65.63  ? 506 TYR A O   1 
ATOM   3412  C  CB  . TYR A 1 531 ? 131.737 153.545 114.700 1.00 47.05  ? 506 TYR A CB  1 
ATOM   3413  C  CG  . TYR A 1 531 ? 132.720 153.429 115.836 1.00 51.80  ? 506 TYR A CG  1 
ATOM   3414  C  CD1 . TYR A 1 531 ? 132.381 153.826 117.116 1.00 56.59  ? 506 TYR A CD1 1 
ATOM   3415  C  CD2 . TYR A 1 531 ? 133.996 152.947 115.623 1.00 59.30  ? 506 TYR A CD2 1 
ATOM   3416  C  CE1 . TYR A 1 531 ? 133.278 153.736 118.150 1.00 57.99  ? 506 TYR A CE1 1 
ATOM   3417  C  CE2 . TYR A 1 531 ? 134.899 152.853 116.652 1.00 64.89  ? 506 TYR A CE2 1 
ATOM   3418  C  CZ  . TYR A 1 531 ? 134.535 153.249 117.912 1.00 63.16  ? 506 TYR A CZ  1 
ATOM   3419  O  OH  . TYR A 1 531 ? 135.440 153.154 118.941 1.00 64.27  ? 506 TYR A OH  1 
ATOM   3420  N  N   . VAL A 1 532 ? 129.556 155.193 112.975 1.00 51.02  ? 507 VAL A N   1 
ATOM   3421  C  CA  . VAL A 1 532 ? 128.687 155.254 111.805 1.00 44.24  ? 507 VAL A CA  1 
ATOM   3422  C  C   . VAL A 1 532 ? 128.970 156.505 110.987 1.00 48.33  ? 507 VAL A C   1 
ATOM   3423  O  O   . VAL A 1 532 ? 128.937 156.475 109.752 1.00 55.58  ? 507 VAL A O   1 
ATOM   3424  C  CB  . VAL A 1 532 ? 127.214 155.183 112.235 1.00 42.07  ? 507 VAL A CB  1 
ATOM   3425  C  CG1 . VAL A 1 532 ? 126.311 155.348 111.035 1.00 45.20  ? 507 VAL A CG1 1 
ATOM   3426  C  CG2 . VAL A 1 532 ? 126.941 153.867 112.920 1.00 50.60  ? 507 VAL A CG2 1 
ATOM   3427  N  N   . PHE A 1 533 ? 129.257 157.620 111.651 1.00 45.67  ? 508 PHE A N   1 
ATOM   3428  C  CA  . PHE A 1 533 ? 129.448 158.895 110.978 1.00 45.92  ? 508 PHE A CA  1 
ATOM   3429  C  C   . PHE A 1 533 ? 130.899 159.166 110.616 1.00 51.83  ? 508 PHE A C   1 
ATOM   3430  O  O   . PHE A 1 533 ? 131.217 160.274 110.178 1.00 57.09  ? 508 PHE A O   1 
ATOM   3431  C  CB  . PHE A 1 533 ? 128.906 160.031 111.842 1.00 47.76  ? 508 PHE A CB  1 
ATOM   3432  C  CG  . PHE A 1 533 ? 127.468 160.339 111.584 1.00 52.87  ? 508 PHE A CG  1 
ATOM   3433  C  CD1 . PHE A 1 533 ? 127.091 161.021 110.447 1.00 60.35  ? 508 PHE A CD1 1 
ATOM   3434  C  CD2 . PHE A 1 533 ? 126.493 159.933 112.465 1.00 53.76  ? 508 PHE A CD2 1 
ATOM   3435  C  CE1 . PHE A 1 533 ? 125.773 161.299 110.200 1.00 54.12  ? 508 PHE A CE1 1 
ATOM   3436  C  CE2 . PHE A 1 533 ? 125.175 160.209 112.221 1.00 56.63  ? 508 PHE A CE2 1 
ATOM   3437  C  CZ  . PHE A 1 533 ? 124.816 160.894 111.087 1.00 56.65  ? 508 PHE A CZ  1 
ATOM   3438  N  N   . GLY A 1 534 ? 131.781 158.190 110.800 1.00 56.44  ? 509 GLY A N   1 
ATOM   3439  C  CA  . GLY A 1 534 ? 133.162 158.336 110.387 1.00 57.99  ? 509 GLY A CA  1 
ATOM   3440  C  C   . GLY A 1 534 ? 133.943 159.395 111.126 1.00 61.95  ? 509 GLY A C   1 
ATOM   3441  O  O   . GLY A 1 534 ? 134.796 160.052 110.527 1.00 73.75  ? 509 GLY A O   1 
ATOM   3442  N  N   . VAL A 1 535 ? 133.668 159.589 112.416 1.00 59.53  ? 510 VAL A N   1 
ATOM   3443  C  CA  . VAL A 1 535 ? 134.489 160.500 113.217 1.00 63.76  ? 510 VAL A CA  1 
ATOM   3444  C  C   . VAL A 1 535 ? 135.935 160.035 113.313 1.00 72.19  ? 510 VAL A C   1 
ATOM   3445  O  O   . VAL A 1 535 ? 136.837 160.875 113.181 1.00 74.71  ? 510 VAL A O   1 
ATOM   3446  C  CB  . VAL A 1 535 ? 133.837 160.735 114.586 1.00 62.50  ? 510 VAL A CB  1 
ATOM   3447  C  CG1 . VAL A 1 535 ? 134.666 161.704 115.400 1.00 69.18  ? 510 VAL A CG1 1 
ATOM   3448  C  CG2 . VAL A 1 535 ? 132.435 161.269 114.412 1.00 62.25  ? 510 VAL A CG2 1 
ATOM   3449  N  N   . PRO A 1 536 ? 136.245 158.751 113.542 1.00 68.00  ? 511 PRO A N   1 
ATOM   3450  C  CA  . PRO A 1 536 ? 137.658 158.362 113.677 1.00 67.35  ? 511 PRO A CA  1 
ATOM   3451  C  C   . PRO A 1 536 ? 138.498 158.626 112.441 1.00 69.20  ? 511 PRO A C   1 
ATOM   3452  O  O   . PRO A 1 536 ? 139.727 158.682 112.552 1.00 74.96  ? 511 PRO A O   1 
ATOM   3453  C  CB  . PRO A 1 536 ? 137.579 156.862 113.982 1.00 68.09  ? 511 PRO A CB  1 
ATOM   3454  C  CG  . PRO A 1 536 ? 136.257 156.675 114.576 1.00 65.92  ? 511 PRO A CG  1 
ATOM   3455  C  CD  . PRO A 1 536 ? 135.362 157.610 113.839 1.00 67.77  ? 511 PRO A CD  1 
ATOM   3456  N  N   . MET A 1 537 ? 137.886 158.779 111.270 1.00 67.65  ? 512 MET A N   1 
ATOM   3457  C  CA  . MET A 1 537 ? 138.648 159.045 110.058 1.00 66.91  ? 512 MET A CA  1 
ATOM   3458  C  C   . MET A 1 537 ? 139.033 160.509 109.904 1.00 70.63  ? 512 MET A C   1 
ATOM   3459  O  O   . MET A 1 537 ? 139.770 160.841 108.970 1.00 76.81  ? 512 MET A O   1 
ATOM   3460  C  CB  . MET A 1 537 ? 137.859 158.588 108.834 1.00 62.20  ? 512 MET A CB  1 
ATOM   3461  C  CG  . MET A 1 537 ? 137.781 157.089 108.701 1.00 65.91  ? 512 MET A CG  1 
ATOM   3462  S  SD  . MET A 1 537 ? 136.951 156.587 107.193 1.00 88.77  ? 512 MET A SD  1 
ATOM   3463  C  CE  . MET A 1 537 ? 136.957 154.819 107.415 1.00 68.96  ? 512 MET A CE  1 
ATOM   3464  N  N   . VAL A 1 538 ? 138.551 161.387 110.779 1.00 63.62  ? 513 VAL A N   1 
ATOM   3465  C  CA  . VAL A 1 538 ? 138.953 162.789 110.772 1.00 69.51  ? 513 VAL A CA  1 
ATOM   3466  C  C   . VAL A 1 538 ? 139.553 163.236 112.093 1.00 72.72  ? 513 VAL A C   1 
ATOM   3467  O  O   . VAL A 1 538 ? 139.971 164.399 112.202 1.00 73.86  ? 513 VAL A O   1 
ATOM   3468  C  CB  . VAL A 1 538 ? 137.780 163.715 110.389 1.00 68.98  ? 513 VAL A CB  1 
ATOM   3469  C  CG1 . VAL A 1 538 ? 137.078 163.189 109.161 1.00 68.76  ? 513 VAL A CG1 1 
ATOM   3470  C  CG2 . VAL A 1 538 ? 136.810 163.845 111.545 1.00 68.59  ? 513 VAL A CG2 1 
ATOM   3471  N  N   . GLY A 1 539 ? 139.609 162.370 113.097 1.00 78.27  ? 514 GLY A N   1 
ATOM   3472  C  CA  . GLY A 1 539 ? 140.198 162.707 114.378 1.00 81.12  ? 514 GLY A CA  1 
ATOM   3473  C  C   . GLY A 1 539 ? 139.165 163.205 115.369 1.00 83.33  ? 514 GLY A C   1 
ATOM   3474  O  O   . GLY A 1 539 ? 137.973 163.335 115.079 1.00 80.89  ? 514 GLY A O   1 
ATOM   3475  N  N   . ALA A 1 540 ? 139.657 163.490 116.570 1.00 90.47  ? 515 ALA A N   1 
ATOM   3476  C  CA  . ALA A 1 540 ? 138.793 163.948 117.646 1.00 87.90  ? 515 ALA A CA  1 
ATOM   3477  C  C   . ALA A 1 540 ? 138.242 165.336 117.348 1.00 88.44  ? 515 ALA A C   1 
ATOM   3478  O  O   . ALA A 1 540 ? 138.953 166.211 116.848 1.00 92.22  ? 515 ALA A O   1 
ATOM   3479  C  CB  . ALA A 1 540 ? 139.558 163.963 118.966 1.00 85.24  ? 515 ALA A CB  1 
ATOM   3480  N  N   . THR A 1 541 ? 136.968 165.533 117.659 1.00 88.84  ? 516 THR A N   1 
ATOM   3481  C  CA  . THR A 1 541 ? 136.312 166.826 117.560 1.00 90.48  ? 516 THR A CA  1 
ATOM   3482  C  C   . THR A 1 541 ? 136.032 167.352 118.962 1.00 91.34  ? 516 THR A C   1 
ATOM   3483  O  O   . THR A 1 541 ? 136.406 166.743 119.967 1.00 92.21  ? 516 THR A O   1 
ATOM   3484  C  CB  . THR A 1 541 ? 135.021 166.723 116.745 1.00 92.91  ? 516 THR A CB  1 
ATOM   3485  O  OG1 . THR A 1 541 ? 133.950 166.306 117.598 1.00 91.89  ? 516 THR A OG1 1 
ATOM   3486  C  CG2 . THR A 1 541 ? 135.179 165.716 115.620 1.00 91.21  ? 516 THR A CG2 1 
ATOM   3487  N  N   . ASP A 1 542 ? 135.367 168.506 119.028 1.00 91.29  ? 517 ASP A N   1 
ATOM   3488  C  CA  . ASP A 1 542 ? 134.986 169.052 120.326 1.00 90.53  ? 517 ASP A CA  1 
ATOM   3489  C  C   . ASP A 1 542 ? 133.940 168.177 121.005 1.00 88.64  ? 517 ASP A C   1 
ATOM   3490  O  O   . ASP A 1 542 ? 133.914 168.073 122.236 1.00 86.10  ? 517 ASP A O   1 
ATOM   3491  C  CB  . ASP A 1 542 ? 134.478 170.483 120.167 1.00 90.43  ? 517 ASP A CB  1 
ATOM   3492  C  CG  . ASP A 1 542 ? 133.564 170.646 118.974 1.00 91.89  ? 517 ASP A CG  1 
ATOM   3493  O  OD1 . ASP A 1 542 ? 133.357 169.654 118.247 1.00 92.46  ? 517 ASP A OD1 1 
ATOM   3494  O  OD2 . ASP A 1 542 ? 133.053 171.766 118.762 1.00 89.17  ? 517 ASP A OD2 1 
ATOM   3495  N  N   . LEU A 1 543 ? 133.064 167.550 120.219 1.00 87.94  ? 518 LEU A N   1 
ATOM   3496  C  CA  . LEU A 1 543 ? 132.038 166.676 120.775 1.00 87.65  ? 518 LEU A CA  1 
ATOM   3497  C  C   . LEU A 1 543 ? 132.575 165.294 121.129 1.00 87.51  ? 518 LEU A C   1 
ATOM   3498  O  O   . LEU A 1 543 ? 132.026 164.635 122.017 1.00 83.95  ? 518 LEU A O   1 
ATOM   3499  C  CB  . LEU A 1 543 ? 130.874 166.548 119.794 1.00 84.56  ? 518 LEU A CB  1 
ATOM   3500  C  CG  . LEU A 1 543 ? 129.475 166.438 120.394 1.00 81.59  ? 518 LEU A CG  1 
ATOM   3501  C  CD1 . LEU A 1 543 ? 129.163 167.646 121.257 1.00 80.26  ? 518 LEU A CD1 1 
ATOM   3502  C  CD2 . LEU A 1 543 ? 128.450 166.290 119.289 1.00 82.36  ? 518 LEU A CD2 1 
ATOM   3503  N  N   . PHE A 1 544 ? 133.624 164.832 120.445 1.00 89.67  ? 519 PHE A N   1 
ATOM   3504  C  CA  . PHE A 1 544 ? 134.189 163.495 120.646 1.00 88.36  ? 519 PHE A CA  1 
ATOM   3505  C  C   . PHE A 1 544 ? 135.695 163.610 120.841 1.00 92.57  ? 519 PHE A C   1 
ATOM   3506  O  O   . PHE A 1 544 ? 136.468 163.486 119.881 1.00 96.65  ? 519 PHE A O   1 
ATOM   3507  C  CB  . PHE A 1 544 ? 133.862 162.574 119.470 1.00 84.47  ? 519 PHE A CB  1 
ATOM   3508  C  CG  . PHE A 1 544 ? 132.394 162.450 119.183 1.00 88.15  ? 519 PHE A CG  1 
ATOM   3509  C  CD1 . PHE A 1 544 ? 131.748 163.384 118.397 1.00 89.40  ? 519 PHE A CD1 1 
ATOM   3510  C  CD2 . PHE A 1 544 ? 131.662 161.398 119.695 1.00 88.47  ? 519 PHE A CD2 1 
ATOM   3511  C  CE1 . PHE A 1 544 ? 130.400 163.272 118.129 1.00 88.75  ? 519 PHE A CE1 1 
ATOM   3512  C  CE2 . PHE A 1 544 ? 130.312 161.285 119.431 1.00 86.96  ? 519 PHE A CE2 1 
ATOM   3513  C  CZ  . PHE A 1 544 ? 129.683 162.221 118.645 1.00 87.22  ? 519 PHE A CZ  1 
ATOM   3514  N  N   . PRO A 1 545 ? 136.152 163.849 122.076 1.00 101.86 ? 520 PRO A N   1 
ATOM   3515  C  CA  . PRO A 1 545 ? 137.580 164.115 122.301 1.00 102.37 ? 520 PRO A CA  1 
ATOM   3516  C  C   . PRO A 1 545 ? 138.439 162.902 122.640 1.00 103.65 ? 520 PRO A C   1 
ATOM   3517  O  O   . PRO A 1 545 ? 139.552 163.073 123.146 1.00 105.07 ? 520 PRO A O   1 
ATOM   3518  C  CB  . PRO A 1 545 ? 137.555 165.100 123.473 1.00 99.28  ? 520 PRO A CB  1 
ATOM   3519  C  CG  . PRO A 1 545 ? 136.356 164.684 124.255 1.00 100.82 ? 520 PRO A CG  1 
ATOM   3520  C  CD  . PRO A 1 545 ? 135.340 164.173 123.260 1.00 100.42 ? 520 PRO A CD  1 
ATOM   3521  N  N   . CYS A 1 546 ? 137.969 161.685 122.382 1.00 112.08 ? 521 CYS A N   1 
ATOM   3522  C  CA  . CYS A 1 546 ? 138.803 160.506 122.596 1.00 113.94 ? 521 CYS A CA  1 
ATOM   3523  C  C   . CYS A 1 546 ? 139.937 160.468 121.580 1.00 114.33 ? 521 CYS A C   1 
ATOM   3524  O  O   . CYS A 1 546 ? 139.868 161.116 120.530 1.00 112.83 ? 521 CYS A O   1 
ATOM   3525  C  CB  . CYS A 1 546 ? 137.977 159.233 122.475 1.00 112.98 ? 521 CYS A CB  1 
ATOM   3526  S  SG  . CYS A 1 546 ? 136.268 159.407 122.993 1.00 126.26 ? 521 CYS A SG  1 
ATOM   3527  N  N   . ASN A 1 547 ? 140.994 159.709 121.883 1.00 116.39 ? 522 ASN A N   1 
ATOM   3528  C  CA  . ASN A 1 547 ? 141.999 159.509 120.849 1.00 114.84 ? 522 ASN A CA  1 
ATOM   3529  C  C   . ASN A 1 547 ? 141.707 158.189 120.149 1.00 113.19 ? 522 ASN A C   1 
ATOM   3530  O  O   . ASN A 1 547 ? 141.471 157.166 120.800 1.00 111.47 ? 522 ASN A O   1 
ATOM   3531  C  CB  . ASN A 1 547 ? 143.451 159.515 121.353 1.00 115.93 ? 522 ASN A CB  1 
ATOM   3532  C  CG  . ASN A 1 547 ? 143.697 160.478 122.502 1.00 118.16 ? 522 ASN A CG  1 
ATOM   3533  O  OD1 . ASN A 1 547 ? 143.506 161.690 122.360 1.00 117.29 ? 522 ASN A OD1 1 
ATOM   3534  N  ND2 . ASN A 1 547 ? 144.287 159.969 123.606 1.00 119.18 ? 522 ASN A ND2 1 
ATOM   3535  N  N   . PHE A 1 548 ? 141.714 158.214 118.824 1.00 92.81  ? 523 PHE A N   1 
ATOM   3536  C  CA  . PHE A 1 548 ? 141.312 157.077 118.012 1.00 90.57  ? 523 PHE A CA  1 
ATOM   3537  C  C   . PHE A 1 548 ? 142.552 156.384 117.470 1.00 93.45  ? 523 PHE A C   1 
ATOM   3538  O  O   . PHE A 1 548 ? 143.436 157.037 116.907 1.00 95.02  ? 523 PHE A O   1 
ATOM   3539  C  CB  . PHE A 1 548 ? 140.402 157.528 116.871 1.00 89.60  ? 523 PHE A CB  1 
ATOM   3540  C  CG  . PHE A 1 548 ? 139.029 157.943 117.318 1.00 92.50  ? 523 PHE A CG  1 
ATOM   3541  C  CD1 . PHE A 1 548 ? 138.075 156.999 117.645 1.00 92.41  ? 523 PHE A CD1 1 
ATOM   3542  C  CD2 . PHE A 1 548 ? 138.704 159.281 117.429 1.00 93.61  ? 523 PHE A CD2 1 
ATOM   3543  C  CE1 . PHE A 1 548 ? 136.819 157.383 118.052 1.00 89.82  ? 523 PHE A CE1 1 
ATOM   3544  C  CE2 . PHE A 1 548 ? 137.449 159.669 117.843 1.00 93.19  ? 523 PHE A CE2 1 
ATOM   3545  C  CZ  . PHE A 1 548 ? 136.507 158.718 118.155 1.00 91.07  ? 523 PHE A CZ  1 
ATOM   3546  N  N   . SER A 1 549 ? 142.616 155.068 117.652 1.00 89.88  ? 524 SER A N   1 
ATOM   3547  C  CA  . SER A 1 549 ? 143.747 154.268 117.210 1.00 87.73  ? 524 SER A CA  1 
ATOM   3548  C  C   . SER A 1 549 ? 143.451 153.676 115.833 1.00 88.03  ? 524 SER A C   1 
ATOM   3549  O  O   . SER A 1 549 ? 142.479 154.042 115.169 1.00 92.13  ? 524 SER A O   1 
ATOM   3550  C  CB  . SER A 1 549 ? 144.061 153.187 118.242 1.00 89.11  ? 524 SER A CB  1 
ATOM   3551  O  OG  . SER A 1 549 ? 142.878 152.602 118.753 1.00 85.30  ? 524 SER A OG  1 
ATOM   3552  N  N   . LYS A 1 550 ? 144.302 152.754 115.382 1.00 81.27  ? 525 LYS A N   1 
ATOM   3553  C  CA  . LYS A 1 550 ? 144.065 152.107 114.097 1.00 82.15  ? 525 LYS A CA  1 
ATOM   3554  C  C   . LYS A 1 550 ? 142.877 151.158 114.168 1.00 84.71  ? 525 LYS A C   1 
ATOM   3555  O  O   . LYS A 1 550 ? 142.142 150.998 113.185 1.00 88.12  ? 525 LYS A O   1 
ATOM   3556  C  CB  . LYS A 1 550 ? 145.321 151.367 113.644 1.00 83.09  ? 525 LYS A CB  1 
ATOM   3557  N  N   . ASN A 1 551 ? 142.673 150.514 115.320 1.00 79.55  ? 526 ASN A N   1 
ATOM   3558  C  CA  . ASN A 1 551 ? 141.529 149.622 115.472 1.00 82.76  ? 526 ASN A CA  1 
ATOM   3559  C  C   . ASN A 1 551 ? 140.217 150.386 115.360 1.00 82.52  ? 526 ASN A C   1 
ATOM   3560  O  O   . ASN A 1 551 ? 139.251 149.894 114.766 1.00 78.20  ? 526 ASN A O   1 
ATOM   3561  C  CB  . ASN A 1 551 ? 141.607 148.884 116.807 1.00 81.82  ? 526 ASN A CB  1 
ATOM   3562  C  CG  . ASN A 1 551 ? 142.777 147.930 116.876 1.00 83.64  ? 526 ASN A CG  1 
ATOM   3563  O  OD1 . ASN A 1 551 ? 142.611 146.717 116.750 1.00 80.98  ? 526 ASN A OD1 1 
ATOM   3564  N  ND2 . ASN A 1 551 ? 143.970 148.471 117.080 1.00 86.98  ? 526 ASN A ND2 1 
ATOM   3565  N  N   . ASP A 1 552 ? 140.163 151.591 115.931 1.00 79.21  ? 527 ASP A N   1 
ATOM   3566  C  CA  . ASP A 1 552 ? 138.959 152.406 115.824 1.00 73.89  ? 527 ASP A CA  1 
ATOM   3567  C  C   . ASP A 1 552 ? 138.670 152.773 114.377 1.00 75.72  ? 527 ASP A C   1 
ATOM   3568  O  O   . ASP A 1 552 ? 137.514 152.755 113.945 1.00 80.94  ? 527 ASP A O   1 
ATOM   3569  C  CB  . ASP A 1 552 ? 139.102 153.663 116.677 1.00 77.10  ? 527 ASP A CB  1 
ATOM   3570  C  CG  . ASP A 1 552 ? 139.350 153.349 118.132 1.00 81.95  ? 527 ASP A CG  1 
ATOM   3571  O  OD1 . ASP A 1 552 ? 138.534 152.615 118.726 1.00 81.74  ? 527 ASP A OD1 1 
ATOM   3572  O  OD2 . ASP A 1 552 ? 140.362 153.829 118.683 1.00 84.18  ? 527 ASP A OD2 1 
ATOM   3573  N  N   . VAL A 1 553 ? 139.707 153.113 113.611 1.00 72.56  ? 528 VAL A N   1 
ATOM   3574  C  CA  . VAL A 1 553 ? 139.508 153.443 112.205 1.00 71.75  ? 528 VAL A CA  1 
ATOM   3575  C  C   . VAL A 1 553 ? 139.037 152.220 111.429 1.00 73.44  ? 528 VAL A C   1 
ATOM   3576  O  O   . VAL A 1 553 ? 138.158 152.319 110.565 1.00 81.20  ? 528 VAL A O   1 
ATOM   3577  C  CB  . VAL A 1 553 ? 140.793 154.038 111.608 1.00 70.47  ? 528 VAL A CB  1 
ATOM   3578  C  CG1 . VAL A 1 553 ? 140.612 154.295 110.128 1.00 73.40  ? 528 VAL A CG1 1 
ATOM   3579  C  CG2 . VAL A 1 553 ? 141.155 155.322 112.329 1.00 69.63  ? 528 VAL A CG2 1 
ATOM   3580  N  N   . MET A 1 554 ? 139.607 151.049 111.721 1.00 66.48  ? 529 MET A N   1 
ATOM   3581  C  CA  . MET A 1 554 ? 139.155 149.831 111.056 1.00 67.34  ? 529 MET A CA  1 
ATOM   3582  C  C   . MET A 1 554 ? 137.690 149.548 111.361 1.00 71.22  ? 529 MET A C   1 
ATOM   3583  O  O   . MET A 1 554 ? 136.911 149.210 110.461 1.00 73.07  ? 529 MET A O   1 
ATOM   3584  C  CB  . MET A 1 554 ? 140.024 148.647 111.476 1.00 70.88  ? 529 MET A CB  1 
ATOM   3585  C  CG  . MET A 1 554 ? 139.593 147.315 110.883 1.00 75.12  ? 529 MET A CG  1 
ATOM   3586  S  SD  . MET A 1 554 ? 138.571 146.331 111.998 1.00 96.38  ? 529 MET A SD  1 
ATOM   3587  C  CE  . MET A 1 554 ? 139.822 145.518 112.989 1.00 73.47  ? 529 MET A CE  1 
ATOM   3588  N  N   . LEU A 1 555 ? 137.294 149.687 112.628 1.00 61.95  ? 530 LEU A N   1 
ATOM   3589  C  CA  . LEU A 1 555 ? 135.906 149.433 112.999 1.00 62.97  ? 530 LEU A CA  1 
ATOM   3590  C  C   . LEU A 1 555 ? 134.966 150.447 112.363 1.00 59.09  ? 530 LEU A C   1 
ATOM   3591  O  O   . LEU A 1 555 ? 133.864 150.093 111.929 1.00 69.43  ? 530 LEU A O   1 
ATOM   3592  C  CB  . LEU A 1 555 ? 135.755 149.447 114.515 1.00 57.33  ? 530 LEU A CB  1 
ATOM   3593  C  CG  . LEU A 1 555 ? 134.493 148.766 115.023 1.00 49.84  ? 530 LEU A CG  1 
ATOM   3594  C  CD1 . LEU A 1 555 ? 134.442 147.343 114.524 1.00 51.62  ? 530 LEU A CD1 1 
ATOM   3595  C  CD2 . LEU A 1 555 ? 134.463 148.802 116.527 1.00 53.36  ? 530 LEU A CD2 1 
ATOM   3596  N  N   . SER A 1 556 ? 135.373 151.717 112.314 1.00 44.67  ? 531 SER A N   1 
ATOM   3597  C  CA  . SER A 1 556 ? 134.551 152.726 111.660 1.00 45.65  ? 531 SER A CA  1 
ATOM   3598  C  C   . SER A 1 556 ? 134.369 152.403 110.188 1.00 48.14  ? 531 SER A C   1 
ATOM   3599  O  O   . SER A 1 556 ? 133.259 152.505 109.657 1.00 52.84  ? 531 SER A O   1 
ATOM   3600  C  CB  . SER A 1 556 ? 135.176 154.107 111.833 1.00 53.91  ? 531 SER A CB  1 
ATOM   3601  O  OG  . SER A 1 556 ? 134.470 155.075 111.082 1.00 53.00  ? 531 SER A OG  1 
ATOM   3602  N  N   . ALA A 1 557 ? 135.446 151.992 109.515 1.00 56.13  ? 532 ALA A N   1 
ATOM   3603  C  CA  . ALA A 1 557 ? 135.332 151.602 108.115 1.00 58.19  ? 532 ALA A CA  1 
ATOM   3604  C  C   . ALA A 1 557 ? 134.384 150.427 107.952 1.00 60.77  ? 532 ALA A C   1 
ATOM   3605  O  O   . ALA A 1 557 ? 133.559 150.408 107.032 1.00 67.84  ? 532 ALA A O   1 
ATOM   3606  C  CB  . ALA A 1 557 ? 136.707 151.257 107.549 1.00 57.90  ? 532 ALA A CB  1 
ATOM   3607  N  N   . VAL A 1 558 ? 134.469 149.447 108.851 1.00 50.82  ? 533 VAL A N   1 
ATOM   3608  C  CA  . VAL A 1 558 ? 133.641 148.253 108.722 1.00 50.32  ? 533 VAL A CA  1 
ATOM   3609  C  C   . VAL A 1 558 ? 132.166 148.591 108.905 1.00 60.87  ? 533 VAL A C   1 
ATOM   3610  O  O   . VAL A 1 558 ? 131.315 148.168 108.113 1.00 68.09  ? 533 VAL A O   1 
ATOM   3611  C  CB  . VAL A 1 558 ? 134.101 147.176 109.715 1.00 52.30  ? 533 VAL A CB  1 
ATOM   3612  C  CG1 . VAL A 1 558 ? 133.006 146.152 109.924 1.00 57.04  ? 533 VAL A CG1 1 
ATOM   3613  C  CG2 . VAL A 1 558 ? 135.362 146.523 109.205 1.00 60.92  ? 533 VAL A CG2 1 
ATOM   3614  N  N   . VAL A 1 559 ? 131.835 149.357 109.948 1.00 50.50  ? 534 VAL A N   1 
ATOM   3615  C  CA  . VAL A 1 559 ? 130.426 149.652 110.196 1.00 36.34  ? 534 VAL A CA  1 
ATOM   3616  C  C   . VAL A 1 559 ? 129.879 150.609 109.143 1.00 46.08  ? 534 VAL A C   1 
ATOM   3617  O  O   . VAL A 1 559 ? 128.706 150.518 108.764 1.00 50.85  ? 534 VAL A O   1 
ATOM   3618  C  CB  . VAL A 1 559 ? 130.206 150.179 111.625 1.00 27.08  ? 534 VAL A CB  1 
ATOM   3619  C  CG1 . VAL A 1 559 ? 130.844 149.247 112.626 1.00 42.65  ? 534 VAL A CG1 1 
ATOM   3620  C  CG2 . VAL A 1 559 ? 130.738 151.577 111.779 1.00 44.67  ? 534 VAL A CG2 1 
ATOM   3621  N  N   . MET A 1 560 ? 130.705 151.529 108.637 1.00 51.31  ? 535 MET A N   1 
ATOM   3622  C  CA  . MET A 1 560 ? 130.240 152.387 107.554 1.00 47.08  ? 535 MET A CA  1 
ATOM   3623  C  C   . MET A 1 560 ? 129.983 151.579 106.291 1.00 52.09  ? 535 MET A C   1 
ATOM   3624  O  O   . MET A 1 560 ? 129.002 151.827 105.580 1.00 60.09  ? 535 MET A O   1 
ATOM   3625  C  CB  . MET A 1 560 ? 131.246 153.504 107.294 1.00 35.08  ? 535 MET A CB  1 
ATOM   3626  C  CG  . MET A 1 560 ? 131.146 154.631 108.298 1.00 44.49  ? 535 MET A CG  1 
ATOM   3627  S  SD  . MET A 1 560 ? 131.979 156.148 107.815 1.00 65.94  ? 535 MET A SD  1 
ATOM   3628  C  CE  . MET A 1 560 ? 133.342 155.492 106.877 1.00 58.03  ? 535 MET A CE  1 
ATOM   3629  N  N   . THR A 1 561 ? 130.837 150.593 106.006 1.00 49.21  ? 536 THR A N   1 
ATOM   3630  C  CA  . THR A 1 561 ? 130.590 149.712 104.872 1.00 49.09  ? 536 THR A CA  1 
ATOM   3631  C  C   . THR A 1 561 ? 129.305 148.919 105.061 1.00 49.96  ? 536 THR A C   1 
ATOM   3632  O  O   . THR A 1 561 ? 128.526 148.760 104.118 1.00 58.47  ? 536 THR A O   1 
ATOM   3633  C  CB  . THR A 1 561 ? 131.770 148.767 104.668 1.00 50.87  ? 536 THR A CB  1 
ATOM   3634  O  OG1 . THR A 1 561 ? 132.972 149.530 104.517 1.00 60.38  ? 536 THR A OG1 1 
ATOM   3635  C  CG2 . THR A 1 561 ? 131.562 147.926 103.428 1.00 47.83  ? 536 THR A CG2 1 
ATOM   3636  N  N   . TYR A 1 562 ? 129.062 148.416 106.273 1.00 38.27  ? 537 TYR A N   1 
ATOM   3637  C  CA  . TYR A 1 562 ? 127.834 147.665 106.529 1.00 47.53  ? 537 TYR A CA  1 
ATOM   3638  C  C   . TYR A 1 562 ? 126.601 148.537 106.320 1.00 51.83  ? 537 TYR A C   1 
ATOM   3639  O  O   . TYR A 1 562 ? 125.650 148.140 105.634 1.00 62.52  ? 537 TYR A O   1 
ATOM   3640  C  CB  . TYR A 1 562 ? 127.851 147.101 107.949 1.00 48.66  ? 537 TYR A CB  1 
ATOM   3641  C  CG  . TYR A 1 562 ? 128.495 145.741 108.079 1.00 45.92  ? 537 TYR A CG  1 
ATOM   3642  C  CD1 . TYR A 1 562 ? 128.181 144.717 107.207 1.00 46.60  ? 537 TYR A CD1 1 
ATOM   3643  C  CD2 . TYR A 1 562 ? 129.414 145.483 109.082 1.00 49.76  ? 537 TYR A CD2 1 
ATOM   3644  C  CE1 . TYR A 1 562 ? 128.766 143.478 107.328 1.00 51.20  ? 537 TYR A CE1 1 
ATOM   3645  C  CE2 . TYR A 1 562 ? 130.002 144.249 109.209 1.00 44.84  ? 537 TYR A CE2 1 
ATOM   3646  C  CZ  . TYR A 1 562 ? 129.675 143.250 108.330 1.00 49.19  ? 537 TYR A CZ  1 
ATOM   3647  O  OH  . TYR A 1 562 ? 130.260 142.015 108.451 1.00 57.82  ? 537 TYR A OH  1 
ATOM   3648  N  N   . TRP A 1 563 ? 126.606 149.738 106.900 1.00 32.20  ? 538 TRP A N   1 
ATOM   3649  C  CA  . TRP A 1 563 ? 125.457 150.630 106.785 1.00 32.07  ? 538 TRP A CA  1 
ATOM   3650  C  C   . TRP A 1 563 ? 125.216 151.042 105.338 1.00 42.99  ? 538 TRP A C   1 
ATOM   3651  O  O   . TRP A 1 563 ? 124.071 151.060 104.871 1.00 53.83  ? 538 TRP A O   1 
ATOM   3652  C  CB  . TRP A 1 563 ? 125.669 151.863 107.661 1.00 37.53  ? 538 TRP A CB  1 
ATOM   3653  C  CG  . TRP A 1 563 ? 125.164 151.762 109.078 1.00 38.52  ? 538 TRP A CG  1 
ATOM   3654  C  CD1 . TRP A 1 563 ? 124.461 152.710 109.750 1.00 38.84  ? 538 TRP A CD1 1 
ATOM   3655  C  CD2 . TRP A 1 563 ? 125.350 150.676 110.002 1.00 41.15  ? 538 TRP A CD2 1 
ATOM   3656  N  NE1 . TRP A 1 563 ? 124.184 152.285 111.023 1.00 49.19  ? 538 TRP A NE1 1 
ATOM   3657  C  CE2 . TRP A 1 563 ? 124.720 151.039 111.201 1.00 36.49  ? 538 TRP A CE2 1 
ATOM   3658  C  CE3 . TRP A 1 563 ? 125.981 149.433 109.928 1.00 41.21  ? 538 TRP A CE3 1 
ATOM   3659  C  CZ2 . TRP A 1 563 ? 124.701 150.210 112.311 1.00 27.92  ? 538 TRP A CZ2 1 
ATOM   3660  C  CZ3 . TRP A 1 563 ? 125.961 148.613 111.033 1.00 36.18  ? 538 TRP A CZ3 1 
ATOM   3661  C  CH2 . TRP A 1 563 ? 125.326 149.004 112.206 1.00 33.11  ? 538 TRP A CH2 1 
ATOM   3662  N  N   . THR A 1 564 ? 126.282 151.371 104.605 1.00 41.67  ? 539 THR A N   1 
ATOM   3663  C  CA  . THR A 1 564 ? 126.114 151.795 103.221 1.00 37.09  ? 539 THR A CA  1 
ATOM   3664  C  C   . THR A 1 564 ? 125.718 150.636 102.314 1.00 49.23  ? 539 THR A C   1 
ATOM   3665  O  O   . THR A 1 564 ? 124.945 150.832 101.371 1.00 58.29  ? 539 THR A O   1 
ATOM   3666  C  CB  . THR A 1 564 ? 127.389 152.462 102.726 1.00 42.23  ? 539 THR A CB  1 
ATOM   3667  O  OG1 . THR A 1 564 ? 128.514 151.643 103.059 1.00 53.32  ? 539 THR A OG1 1 
ATOM   3668  C  CG2 . THR A 1 564 ? 127.552 153.811 103.389 1.00 44.58  ? 539 THR A CG2 1 
ATOM   3669  N  N   . ASN A 1 565 ? 126.211 149.424 102.582 1.00 47.17  ? 540 ASN A N   1 
ATOM   3670  C  CA  . ASN A 1 565 ? 125.731 148.260 101.849 1.00 43.89  ? 540 ASN A CA  1 
ATOM   3671  C  C   . ASN A 1 565 ? 124.244 148.055 102.079 1.00 48.14  ? 540 ASN A C   1 
ATOM   3672  O  O   . ASN A 1 565 ? 123.498 147.748 101.142 1.00 56.98  ? 540 ASN A O   1 
ATOM   3673  C  CB  . ASN A 1 565 ? 126.500 147.011 102.272 1.00 46.57  ? 540 ASN A CB  1 
ATOM   3674  C  CG  . ASN A 1 565 ? 127.911 146.992 101.751 1.00 60.70  ? 540 ASN A CG  1 
ATOM   3675  O  OD1 . ASN A 1 565 ? 128.351 147.929 101.092 1.00 68.24  ? 540 ASN A OD1 1 
ATOM   3676  N  ND2 . ASN A 1 565 ? 128.636 145.922 102.046 1.00 59.74  ? 540 ASN A ND2 1 
ATOM   3677  N  N   . PHE A 1 566 ? 123.796 148.210 103.326 1.00 38.12  ? 541 PHE A N   1 
ATOM   3678  C  CA  . PHE A 1 566 ? 122.371 148.086 103.603 1.00 39.00  ? 541 PHE A CA  1 
ATOM   3679  C  C   . PHE A 1 566 ? 121.573 149.141 102.853 1.00 47.07  ? 541 PHE A C   1 
ATOM   3680  O  O   . PHE A 1 566 ? 120.526 148.839 102.271 1.00 54.46  ? 541 PHE A O   1 
ATOM   3681  C  CB  . PHE A 1 566 ? 122.111 148.190 105.101 1.00 43.45  ? 541 PHE A CB  1 
ATOM   3682  C  CG  . PHE A 1 566 ? 120.682 147.958 105.476 1.00 44.02  ? 541 PHE A CG  1 
ATOM   3683  C  CD1 . PHE A 1 566 ? 120.182 146.677 105.569 1.00 39.05  ? 541 PHE A CD1 1 
ATOM   3684  C  CD2 . PHE A 1 566 ? 119.838 149.019 105.723 1.00 38.02  ? 541 PHE A CD2 1 
ATOM   3685  C  CE1 . PHE A 1 566 ? 118.874 146.460 105.906 1.00 30.32  ? 541 PHE A CE1 1 
ATOM   3686  C  CE2 . PHE A 1 566 ? 118.529 148.807 106.059 1.00 41.51  ? 541 PHE A CE2 1 
ATOM   3687  C  CZ  . PHE A 1 566 ? 118.046 147.525 106.151 1.00 39.56  ? 541 PHE A CZ  1 
ATOM   3688  N  N   . ALA A 1 567 ? 122.053 150.384 102.850 1.00 42.94  ? 542 ALA A N   1 
ATOM   3689  C  CA  . ALA A 1 567 ? 121.339 151.440 102.140 1.00 32.74  ? 542 ALA A CA  1 
ATOM   3690  C  C   . ALA A 1 567 ? 121.327 151.204 100.638 1.00 44.01  ? 542 ALA A C   1 
ATOM   3691  O  O   . ALA A 1 567 ? 120.403 151.650 99.951  1.00 49.97  ? 542 ALA A O   1 
ATOM   3692  C  CB  . ALA A 1 567 ? 121.959 152.797 102.445 1.00 30.93  ? 542 ALA A CB  1 
ATOM   3693  N  N   . LYS A 1 568 ? 122.343 150.521 100.111 1.00 49.78  ? 543 LYS A N   1 
ATOM   3694  C  CA  . LYS A 1 568 ? 122.406 150.265 98.676  1.00 43.97  ? 543 LYS A CA  1 
ATOM   3695  C  C   . LYS A 1 568 ? 121.482 149.124 98.267  1.00 49.14  ? 543 LYS A C   1 
ATOM   3696  O  O   . LYS A 1 568 ? 120.591 149.304 97.431  1.00 53.73  ? 543 LYS A O   1 
ATOM   3697  C  CB  . LYS A 1 568 ? 123.845 149.953 98.260  1.00 44.39  ? 543 LYS A CB  1 
ATOM   3698  C  CG  . LYS A 1 568 ? 124.738 151.165 98.121  1.00 46.40  ? 543 LYS A CG  1 
ATOM   3699  C  CD  . LYS A 1 568 ? 126.148 150.747 97.762  1.00 50.61  ? 543 LYS A CD  1 
ATOM   3700  C  CE  . LYS A 1 568 ? 127.145 151.834 98.096  1.00 49.05  ? 543 LYS A CE  1 
ATOM   3701  N  NZ  . LYS A 1 568 ? 128.449 151.265 98.530  1.00 51.49  ? 543 LYS A NZ  1 
ATOM   3702  N  N   . THR A 1 569 ? 121.680 147.939 98.845  1.00 58.88  ? 544 THR A N   1 
ATOM   3703  C  CA  . THR A 1 569 ? 121.002 146.740 98.371  1.00 61.53  ? 544 THR A CA  1 
ATOM   3704  C  C   . THR A 1 569 ? 120.091 146.076 99.395  1.00 60.12  ? 544 THR A C   1 
ATOM   3705  O  O   . THR A 1 569 ? 119.435 145.085 99.058  1.00 62.80  ? 544 THR A O   1 
ATOM   3706  C  CB  . THR A 1 569 ? 122.028 145.709 97.887  1.00 60.99  ? 544 THR A CB  1 
ATOM   3707  O  OG1 . THR A 1 569 ? 122.816 145.261 98.994  1.00 55.01  ? 544 THR A OG1 1 
ATOM   3708  C  CG2 . THR A 1 569 ? 122.940 146.325 96.845  1.00 61.96  ? 544 THR A CG2 1 
ATOM   3709  N  N   . GLY A 1 570 ? 120.023 146.580 100.624 1.00 52.52  ? 545 GLY A N   1 
ATOM   3710  C  CA  . GLY A 1 570 ? 119.197 145.934 101.624 1.00 51.07  ? 545 GLY A CA  1 
ATOM   3711  C  C   . GLY A 1 570 ? 119.774 144.660 102.192 1.00 53.05  ? 545 GLY A C   1 
ATOM   3712  O  O   . GLY A 1 570 ? 119.032 143.843 102.738 1.00 56.50  ? 545 GLY A O   1 
ATOM   3713  N  N   . ASP A 1 571 ? 121.081 144.469 102.075 1.00 56.78  ? 546 ASP A N   1 
ATOM   3714  C  CA  . ASP A 1 571 ? 121.774 143.293 102.578 1.00 55.40  ? 546 ASP A CA  1 
ATOM   3715  C  C   . ASP A 1 571 ? 123.217 143.684 102.869 1.00 66.63  ? 546 ASP A C   1 
ATOM   3716  O  O   . ASP A 1 571 ? 123.952 144.059 101.948 1.00 80.69  ? 546 ASP A O   1 
ATOM   3717  C  CB  . ASP A 1 571 ? 121.694 142.155 101.561 1.00 61.94  ? 546 ASP A CB  1 
ATOM   3718  C  CG  . ASP A 1 571 ? 122.531 140.956 101.949 1.00 70.41  ? 546 ASP A CG  1 
ATOM   3719  O  OD1 . ASP A 1 571 ? 122.801 140.774 103.153 1.00 70.12  ? 546 ASP A OD1 1 
ATOM   3720  O  OD2 . ASP A 1 571 ? 122.918 140.188 101.044 1.00 73.31  ? 546 ASP A OD2 1 
ATOM   3721  N  N   . PRO A 1 572 ? 123.662 143.612 104.122 1.00 52.68  ? 547 PRO A N   1 
ATOM   3722  C  CA  . PRO A 1 572 ? 124.958 144.200 104.486 1.00 57.81  ? 547 PRO A CA  1 
ATOM   3723  C  C   . PRO A 1 572 ? 126.181 143.540 103.862 1.00 64.23  ? 547 PRO A C   1 
ATOM   3724  O  O   . PRO A 1 572 ? 127.310 143.918 104.188 1.00 64.19  ? 547 PRO A O   1 
ATOM   3725  C  CB  . PRO A 1 572 ? 124.980 144.051 106.012 1.00 45.39  ? 547 PRO A CB  1 
ATOM   3726  C  CG  . PRO A 1 572 ? 123.567 143.964 106.398 1.00 48.79  ? 547 PRO A CG  1 
ATOM   3727  C  CD  . PRO A 1 572 ? 122.908 143.193 105.310 1.00 52.42  ? 547 PRO A CD  1 
ATOM   3728  N  N   . ASN A 1 573 ? 125.997 142.566 102.972 1.00 71.20  ? 548 ASN A N   1 
ATOM   3729  C  CA  . ASN A 1 573 ? 127.128 141.870 102.379 1.00 73.53  ? 548 ASN A CA  1 
ATOM   3730  C  C   . ASN A 1 573 ? 127.190 141.932 100.860 1.00 75.16  ? 548 ASN A C   1 
ATOM   3731  O  O   . ASN A 1 573 ? 128.238 141.601 100.295 1.00 78.01  ? 548 ASN A O   1 
ATOM   3732  C  CB  . ASN A 1 573 ? 127.123 140.393 102.801 1.00 69.58  ? 548 ASN A CB  1 
ATOM   3733  C  CG  . ASN A 1 573 ? 126.727 140.206 104.240 1.00 66.25  ? 548 ASN A CG  1 
ATOM   3734  O  OD1 . ASN A 1 573 ? 127.533 140.404 105.146 1.00 70.05  ? 548 ASN A OD1 1 
ATOM   3735  N  ND2 . ASN A 1 573 ? 125.478 139.823 104.463 1.00 61.41  ? 548 ASN A ND2 1 
ATOM   3736  N  N   . GLN A 1 574 ? 126.122 142.337 100.185 1.00 76.60  ? 549 GLN A N   1 
ATOM   3737  C  CA  . GLN A 1 574 ? 126.070 142.157 98.740  1.00 80.32  ? 549 GLN A CA  1 
ATOM   3738  C  C   . GLN A 1 574 ? 127.042 143.063 97.984  1.00 84.22  ? 549 GLN A C   1 
ATOM   3739  O  O   . GLN A 1 574 ? 127.996 142.555 97.383  1.00 85.57  ? 549 GLN A O   1 
ATOM   3740  C  CB  . GLN A 1 574 ? 124.640 142.362 98.231  1.00 73.87  ? 549 GLN A CB  1 
ATOM   3741  N  N   . PRO A 1 575 ? 126.859 144.397 97.980  1.00 74.34  ? 550 PRO A N   1 
ATOM   3742  C  CA  . PRO A 1 575 ? 127.583 145.215 96.997  1.00 71.45  ? 550 PRO A CA  1 
ATOM   3743  C  C   . PRO A 1 575 ? 129.084 145.325 97.230  1.00 75.21  ? 550 PRO A C   1 
ATOM   3744  O  O   . PRO A 1 575 ? 129.867 145.063 96.314  1.00 76.88  ? 550 PRO A O   1 
ATOM   3745  C  CB  . PRO A 1 575 ? 126.901 146.580 97.115  1.00 66.18  ? 550 PRO A CB  1 
ATOM   3746  C  CG  . PRO A 1 575 ? 126.424 146.638 98.507  1.00 71.79  ? 550 PRO A CG  1 
ATOM   3747  C  CD  . PRO A 1 575 ? 126.188 145.234 98.991  1.00 68.24  ? 550 PRO A CD  1 
ATOM   3748  N  N   . VAL A 1 576 ? 129.504 145.700 98.433  1.00 81.49  ? 551 VAL A N   1 
ATOM   3749  C  CA  . VAL A 1 576 ? 130.903 145.997 98.717  1.00 79.18  ? 551 VAL A CA  1 
ATOM   3750  C  C   . VAL A 1 576 ? 131.420 144.948 99.699  1.00 79.90  ? 551 VAL A C   1 
ATOM   3751  O  O   . VAL A 1 576 ? 131.092 145.004 100.893 1.00 81.68  ? 551 VAL A O   1 
ATOM   3752  C  CB  . VAL A 1 576 ? 131.083 147.414 99.277  1.00 74.57  ? 551 VAL A CB  1 
ATOM   3753  C  CG1 . VAL A 1 576 ? 132.547 147.809 99.243  1.00 72.47  ? 551 VAL A CG1 1 
ATOM   3754  C  CG2 . VAL A 1 576 ? 130.245 148.407 98.494  1.00 70.98  ? 551 VAL A CG2 1 
ATOM   3755  N  N   . PRO A 1 577 ? 132.226 143.988 99.256  1.00 86.69  ? 552 PRO A N   1 
ATOM   3756  C  CA  . PRO A 1 577 ? 132.796 143.015 100.191 1.00 87.89  ? 552 PRO A CA  1 
ATOM   3757  C  C   . PRO A 1 577 ? 133.764 143.674 101.159 1.00 86.78  ? 552 PRO A C   1 
ATOM   3758  O  O   . PRO A 1 577 ? 134.395 144.688 100.853 1.00 85.16  ? 552 PRO A O   1 
ATOM   3759  C  CB  . PRO A 1 577 ? 133.517 142.023 99.273  1.00 89.59  ? 552 PRO A CB  1 
ATOM   3760  C  CG  . PRO A 1 577 ? 133.822 142.811 98.043  1.00 87.21  ? 552 PRO A CG  1 
ATOM   3761  C  CD  . PRO A 1 577 ? 132.663 143.749 97.871  1.00 86.50  ? 552 PRO A CD  1 
ATOM   3762  N  N   . GLN A 1 578 ? 133.873 143.077 102.344 1.00 86.15  ? 553 GLN A N   1 
ATOM   3763  C  CA  . GLN A 1 578 ? 134.716 143.636 103.392 1.00 86.60  ? 553 GLN A CA  1 
ATOM   3764  C  C   . GLN A 1 578 ? 136.183 143.619 102.986 1.00 91.21  ? 553 GLN A C   1 
ATOM   3765  O  O   . GLN A 1 578 ? 136.664 142.670 102.362 1.00 93.80  ? 553 GLN A O   1 
ATOM   3766  C  CB  . GLN A 1 578 ? 134.525 142.857 104.691 1.00 85.46  ? 553 GLN A CB  1 
ATOM   3767  C  CG  . GLN A 1 578 ? 133.179 143.078 105.340 1.00 86.94  ? 553 GLN A CG  1 
ATOM   3768  C  CD  . GLN A 1 578 ? 132.918 144.538 105.619 1.00 86.41  ? 553 GLN A CD  1 
ATOM   3769  O  OE1 . GLN A 1 578 ? 133.659 145.182 106.359 1.00 85.71  ? 553 GLN A OE1 1 
ATOM   3770  N  NE2 . GLN A 1 578 ? 131.863 145.073 105.023 1.00 86.79  ? 553 GLN A NE2 1 
ATOM   3771  N  N   . ASP A 1 579 ? 136.895 144.680 103.352 1.00 102.51 ? 554 ASP A N   1 
ATOM   3772  C  CA  . ASP A 1 579 ? 138.325 144.785 103.086 1.00 102.06 ? 554 ASP A CA  1 
ATOM   3773  C  C   . ASP A 1 579 ? 138.981 145.784 104.034 1.00 101.32 ? 554 ASP A C   1 
ATOM   3774  O  O   . ASP A 1 579 ? 138.344 146.287 104.962 1.00 102.09 ? 554 ASP A O   1 
ATOM   3775  C  CB  . ASP A 1 579 ? 138.575 145.194 101.635 1.00 101.22 ? 554 ASP A CB  1 
ATOM   3776  C  CG  . ASP A 1 579 ? 139.946 144.782 101.143 1.00 102.91 ? 554 ASP A CG  1 
ATOM   3777  O  OD1 . ASP A 1 579 ? 140.947 145.175 101.776 1.00 102.37 ? 554 ASP A OD1 1 
ATOM   3778  O  OD2 . ASP A 1 579 ? 140.023 144.062 100.125 1.00 104.70 ? 554 ASP A OD2 1 
ATOM   3779  N  N   . ARG A 1 589 ? 139.054 140.416 111.261 1.00 83.67  ? 564 ARG A N   1 
ATOM   3780  C  CA  . ARG A 1 589 ? 138.420 139.123 111.034 1.00 88.15  ? 564 ARG A CA  1 
ATOM   3781  C  C   . ARG A 1 589 ? 137.068 139.302 110.355 1.00 90.36  ? 564 ARG A C   1 
ATOM   3782  O  O   . ARG A 1 589 ? 136.307 138.350 110.194 1.00 90.51  ? 564 ARG A O   1 
ATOM   3783  C  CB  . ARG A 1 589 ? 138.258 138.367 112.353 1.00 84.16  ? 564 ARG A CB  1 
ATOM   3784  N  N   . PHE A 1 590 ? 136.786 140.539 109.951 1.00 84.71  ? 565 PHE A N   1 
ATOM   3785  C  CA  . PHE A 1 590 ? 135.509 140.904 109.351 1.00 86.14  ? 565 PHE A CA  1 
ATOM   3786  C  C   . PHE A 1 590 ? 135.325 140.367 107.939 1.00 88.45  ? 565 PHE A C   1 
ATOM   3787  O  O   . PHE A 1 590 ? 134.209 140.436 107.414 1.00 87.87  ? 565 PHE A O   1 
ATOM   3788  C  CB  . PHE A 1 590 ? 135.381 142.425 109.348 1.00 84.80  ? 565 PHE A CB  1 
ATOM   3789  C  CG  . PHE A 1 590 ? 134.750 142.986 110.587 1.00 86.94  ? 565 PHE A CG  1 
ATOM   3790  C  CD1 . PHE A 1 590 ? 133.504 142.559 110.999 1.00 85.62  ? 565 PHE A CD1 1 
ATOM   3791  C  CD2 . PHE A 1 590 ? 135.432 143.896 111.373 1.00 83.68  ? 565 PHE A CD2 1 
ATOM   3792  C  CE1 . PHE A 1 590 ? 132.926 143.077 112.134 1.00 83.44  ? 565 PHE A CE1 1 
ATOM   3793  C  CE2 . PHE A 1 590 ? 134.862 144.404 112.517 1.00 84.01  ? 565 PHE A CE2 1 
ATOM   3794  C  CZ  . PHE A 1 590 ? 133.611 143.989 112.900 1.00 85.81  ? 565 PHE A CZ  1 
ATOM   3795  N  N   . GLU A 1 591 ? 136.377 139.841 107.312 1.00 93.97  ? 566 GLU A N   1 
ATOM   3796  C  CA  . GLU A 1 591 ? 136.278 139.455 105.908 1.00 92.01  ? 566 GLU A CA  1 
ATOM   3797  C  C   . GLU A 1 591 ? 135.423 138.207 105.726 1.00 89.79  ? 566 GLU A C   1 
ATOM   3798  O  O   . GLU A 1 591 ? 134.575 138.150 104.828 1.00 91.81  ? 566 GLU A O   1 
ATOM   3799  C  CB  . GLU A 1 591 ? 137.674 139.236 105.324 1.00 93.42  ? 566 GLU A CB  1 
ATOM   3800  C  CG  . GLU A 1 591 ? 138.436 140.514 105.018 1.00 93.59  ? 566 GLU A CG  1 
ATOM   3801  C  CD  . GLU A 1 591 ? 138.960 141.199 106.262 1.00 94.36  ? 566 GLU A CD  1 
ATOM   3802  O  OE1 . GLU A 1 591 ? 139.602 140.519 107.090 1.00 91.10  ? 566 GLU A OE1 1 
ATOM   3803  O  OE2 . GLU A 1 591 ? 138.732 142.417 106.413 1.00 94.86  ? 566 GLU A OE2 1 
ATOM   3804  N  N   . GLU A 1 592 ? 135.626 137.198 106.568 1.00 90.37  ? 567 GLU A N   1 
ATOM   3805  C  CA  . GLU A 1 592 ? 135.048 135.879 106.344 1.00 92.48  ? 567 GLU A CA  1 
ATOM   3806  C  C   . GLU A 1 592 ? 133.726 135.653 107.066 1.00 92.86  ? 567 GLU A C   1 
ATOM   3807  O  O   . GLU A 1 592 ? 133.186 134.545 106.992 1.00 89.74  ? 567 GLU A O   1 
ATOM   3808  C  CB  . GLU A 1 592 ? 136.045 134.794 106.764 1.00 93.63  ? 567 GLU A CB  1 
ATOM   3809  C  CG  . GLU A 1 592 ? 137.233 134.641 105.825 1.00 95.15  ? 567 GLU A CG  1 
ATOM   3810  C  CD  . GLU A 1 592 ? 136.877 133.908 104.546 1.00 96.27  ? 567 GLU A CD  1 
ATOM   3811  O  OE1 . GLU A 1 592 ? 136.610 132.691 104.611 1.00 97.70  ? 567 GLU A OE1 1 
ATOM   3812  O  OE2 . GLU A 1 592 ? 136.867 134.548 103.473 1.00 96.01  ? 567 GLU A OE2 1 
ATOM   3813  N  N   . VAL A 1 593 ? 133.189 136.656 107.753 1.00 87.60  ? 568 VAL A N   1 
ATOM   3814  C  CA  . VAL A 1 593 ? 131.944 136.501 108.499 1.00 83.01  ? 568 VAL A CA  1 
ATOM   3815  C  C   . VAL A 1 593 ? 130.783 136.975 107.637 1.00 78.33  ? 568 VAL A C   1 
ATOM   3816  O  O   . VAL A 1 593 ? 130.813 138.081 107.087 1.00 75.06  ? 568 VAL A O   1 
ATOM   3817  C  CB  . VAL A 1 593 ? 131.996 137.269 109.829 1.00 80.76  ? 568 VAL A CB  1 
ATOM   3818  C  CG1 . VAL A 1 593 ? 132.818 136.498 110.844 1.00 80.52  ? 568 VAL A CG1 1 
ATOM   3819  C  CG2 . VAL A 1 593 ? 132.573 138.653 109.625 1.00 77.05  ? 568 VAL A CG2 1 
ATOM   3820  N  N   . VAL A 1 594 ? 129.760 136.135 107.517 1.00 62.54  ? 569 VAL A N   1 
ATOM   3821  C  CA  . VAL A 1 594 ? 128.573 136.440 106.730 1.00 65.17  ? 569 VAL A CA  1 
ATOM   3822  C  C   . VAL A 1 594 ? 127.438 136.732 107.700 1.00 65.83  ? 569 VAL A C   1 
ATOM   3823  O  O   . VAL A 1 594 ? 127.103 135.895 108.547 1.00 65.11  ? 569 VAL A O   1 
ATOM   3824  C  CB  . VAL A 1 594 ? 128.211 135.290 105.780 1.00 66.76  ? 569 VAL A CB  1 
ATOM   3825  C  CG1 . VAL A 1 594 ? 126.728 135.307 105.456 1.00 64.94  ? 569 VAL A CG1 1 
ATOM   3826  C  CG2 . VAL A 1 594 ? 129.033 135.382 104.510 1.00 66.92  ? 569 VAL A CG2 1 
ATOM   3827  N  N   . TRP A 1 595 ? 126.852 137.918 107.578 1.00 55.72  ? 570 TRP A N   1 
ATOM   3828  C  CA  . TRP A 1 595 ? 125.775 138.345 108.460 1.00 42.91  ? 570 TRP A CA  1 
ATOM   3829  C  C   . TRP A 1 595 ? 124.471 137.701 108.009 1.00 44.69  ? 570 TRP A C   1 
ATOM   3830  O  O   . TRP A 1 595 ? 124.039 137.895 106.868 1.00 48.01  ? 570 TRP A O   1 
ATOM   3831  C  CB  . TRP A 1 595 ? 125.673 139.866 108.443 1.00 44.48  ? 570 TRP A CB  1 
ATOM   3832  C  CG  . TRP A 1 595 ? 124.849 140.456 109.539 1.00 46.83  ? 570 TRP A CG  1 
ATOM   3833  C  CD1 . TRP A 1 595 ? 123.974 139.807 110.350 1.00 44.91  ? 570 TRP A CD1 1 
ATOM   3834  C  CD2 . TRP A 1 595 ? 124.822 141.829 109.937 1.00 40.56  ? 570 TRP A CD2 1 
ATOM   3835  N  NE1 . TRP A 1 595 ? 123.402 140.689 111.229 1.00 43.22  ? 570 TRP A NE1 1 
ATOM   3836  C  CE2 . TRP A 1 595 ? 123.910 141.938 110.993 1.00 40.13  ? 570 TRP A CE2 1 
ATOM   3837  C  CE3 . TRP A 1 595 ? 125.482 142.977 109.500 1.00 45.71  ? 570 TRP A CE3 1 
ATOM   3838  C  CZ2 . TRP A 1 595 ? 123.641 143.145 111.618 1.00 44.63  ? 570 TRP A CZ2 1 
ATOM   3839  C  CZ3 . TRP A 1 595 ? 125.214 144.170 110.123 1.00 44.96  ? 570 TRP A CZ3 1 
ATOM   3840  C  CH2 . TRP A 1 595 ? 124.304 144.248 111.168 1.00 38.25  ? 570 TRP A CH2 1 
ATOM   3841  N  N   . SER A 1 596 ? 123.847 136.937 108.899 1.00 45.21  ? 571 SER A N   1 
ATOM   3842  C  CA  . SER A 1 596 ? 122.613 136.228 108.596 1.00 45.84  ? 571 SER A CA  1 
ATOM   3843  C  C   . SER A 1 596 ? 121.406 137.015 109.090 1.00 43.98  ? 571 SER A C   1 
ATOM   3844  O  O   . SER A 1 596 ? 121.519 137.947 109.887 1.00 48.75  ? 571 SER A O   1 
ATOM   3845  C  CB  . SER A 1 596 ? 122.628 134.835 109.226 1.00 44.22  ? 571 SER A CB  1 
ATOM   3846  O  OG  . SER A 1 596 ? 123.873 134.198 109.019 1.00 51.41  ? 571 SER A OG  1 
ATOM   3847  N  N   . LYS A 1 597 ? 120.232 136.611 108.617 1.00 35.62  ? 572 LYS A N   1 
ATOM   3848  C  CA  . LYS A 1 597 ? 118.999 137.281 108.992 1.00 35.12  ? 572 LYS A CA  1 
ATOM   3849  C  C   . LYS A 1 597 ? 118.657 136.985 110.450 1.00 41.33  ? 572 LYS A C   1 
ATOM   3850  O  O   . LYS A 1 597 ? 119.407 136.331 111.177 1.00 56.64  ? 572 LYS A O   1 
ATOM   3851  C  CB  . LYS A 1 597 ? 117.860 136.848 108.075 1.00 33.78  ? 572 LYS A CB  1 
ATOM   3852  C  CG  . LYS A 1 597 ? 118.022 137.271 106.632 1.00 40.67  ? 572 LYS A CG  1 
ATOM   3853  C  CD  . LYS A 1 597 ? 116.729 137.067 105.870 1.00 42.61  ? 572 LYS A CD  1 
ATOM   3854  C  CE  . LYS A 1 597 ? 116.850 137.570 104.449 1.00 47.03  ? 572 LYS A CE  1 
ATOM   3855  N  NZ  . LYS A 1 597 ? 117.593 138.855 104.393 1.00 49.44  ? 572 LYS A NZ  1 
ATOM   3856  N  N   . PHE A 1 598 ? 117.504 137.479 110.883 1.00 30.92  ? 573 PHE A N   1 
ATOM   3857  C  CA  . PHE A 1 598 ? 117.014 137.290 112.245 1.00 35.46  ? 573 PHE A CA  1 
ATOM   3858  C  C   . PHE A 1 598 ? 115.696 136.532 112.144 1.00 42.45  ? 573 PHE A C   1 
ATOM   3859  O  O   . PHE A 1 598 ? 114.624 137.136 112.082 1.00 50.45  ? 573 PHE A O   1 
ATOM   3860  C  CB  . PHE A 1 598 ? 116.853 138.637 112.950 1.00 41.20  ? 573 PHE A CB  1 
ATOM   3861  C  CG  . PHE A 1 598 ? 116.417 138.542 114.382 1.00 31.94  ? 573 PHE A CG  1 
ATOM   3862  C  CD1 . PHE A 1 598 ? 115.083 138.468 114.714 1.00 26.63  ? 573 PHE A CD1 1 
ATOM   3863  C  CD2 . PHE A 1 598 ? 117.344 138.567 115.396 1.00 39.01  ? 573 PHE A CD2 1 
ATOM   3864  C  CE1 . PHE A 1 598 ? 114.689 138.393 116.024 1.00 34.71  ? 573 PHE A CE1 1 
ATOM   3865  C  CE2 . PHE A 1 598 ? 116.951 138.494 116.706 1.00 39.22  ? 573 PHE A CE2 1 
ATOM   3866  C  CZ  . PHE A 1 598 ? 115.623 138.406 117.019 1.00 43.09  ? 573 PHE A CZ  1 
ATOM   3867  N  N   . ASN A 1 599 ? 115.775 135.207 112.103 1.00 45.38  ? 574 ASN A N   1 
ATOM   3868  C  CA  . ASN A 1 599 ? 114.576 134.386 112.135 1.00 42.69  ? 574 ASN A CA  1 
ATOM   3869  C  C   . ASN A 1 599 ? 114.134 134.193 113.577 1.00 47.82  ? 574 ASN A C   1 
ATOM   3870  O  O   . ASN A 1 599 ? 114.962 134.045 114.477 1.00 55.31  ? 574 ASN A O   1 
ATOM   3871  C  CB  . ASN A 1 599 ? 114.829 133.034 111.471 1.00 38.43  ? 574 ASN A CB  1 
ATOM   3872  N  N   . SER A 1 600 ? 112.820 134.208 113.798 1.00 49.16  ? 575 SER A N   1 
ATOM   3873  C  CA  . SER A 1 600 ? 112.308 134.110 115.159 1.00 51.02  ? 575 SER A CA  1 
ATOM   3874  C  C   . SER A 1 600 ? 112.636 132.768 115.798 1.00 56.54  ? 575 SER A C   1 
ATOM   3875  O  O   . SER A 1 600 ? 112.842 132.699 117.014 1.00 60.63  ? 575 SER A O   1 
ATOM   3876  C  CB  . SER A 1 600 ? 110.802 134.341 115.171 1.00 52.21  ? 575 SER A CB  1 
ATOM   3877  O  OG  . SER A 1 600 ? 110.217 133.791 116.336 1.00 56.57  ? 575 SER A OG  1 
ATOM   3878  N  N   . LYS A 1 601 ? 112.678 131.695 115.007 1.00 60.59  ? 576 LYS A N   1 
ATOM   3879  C  CA  . LYS A 1 601 ? 112.985 130.379 115.558 1.00 57.92  ? 576 LYS A CA  1 
ATOM   3880  C  C   . LYS A 1 601 ? 114.424 130.309 116.054 1.00 58.14  ? 576 LYS A C   1 
ATOM   3881  O  O   . LYS A 1 601 ? 114.691 129.752 117.124 1.00 64.41  ? 576 LYS A O   1 
ATOM   3882  C  CB  . LYS A 1 601 ? 112.723 129.282 114.521 1.00 60.91  ? 576 LYS A CB  1 
ATOM   3883  C  CG  . LYS A 1 601 ? 111.283 129.181 113.993 1.00 65.29  ? 576 LYS A CG  1 
ATOM   3884  C  CD  . LYS A 1 601 ? 110.924 130.284 113.001 1.00 68.18  ? 576 LYS A CD  1 
ATOM   3885  C  CE  . LYS A 1 601 ? 109.468 130.211 112.579 1.00 64.53  ? 576 LYS A CE  1 
ATOM   3886  N  NZ  . LYS A 1 601 ? 108.993 131.502 112.009 1.00 58.27  ? 576 LYS A NZ  1 
ATOM   3887  N  N   . GLU A 1 602 ? 115.363 130.866 115.293 1.00 58.22  ? 577 GLU A N   1 
ATOM   3888  C  CA  . GLU A 1 602 ? 116.773 130.907 115.671 1.00 58.34  ? 577 GLU A CA  1 
ATOM   3889  C  C   . GLU A 1 602 ? 117.273 132.328 115.458 1.00 64.11  ? 577 GLU A C   1 
ATOM   3890  O  O   . GLU A 1 602 ? 117.481 132.751 114.317 1.00 73.10  ? 577 GLU A O   1 
ATOM   3891  C  CB  . GLU A 1 602 ? 117.590 129.909 114.856 1.00 57.42  ? 577 GLU A CB  1 
ATOM   3892  C  CG  . GLU A 1 602 ? 118.996 129.700 115.370 1.00 62.64  ? 577 GLU A CG  1 
ATOM   3893  C  CD  . GLU A 1 602 ? 119.707 128.570 114.658 1.00 72.62  ? 577 GLU A CD  1 
ATOM   3894  O  OE1 . GLU A 1 602 ? 119.329 128.260 113.509 1.00 72.66  ? 577 GLU A OE1 1 
ATOM   3895  O  OE2 . GLU A 1 602 ? 120.643 127.989 115.246 1.00 71.69  ? 577 GLU A OE2 1 
ATOM   3896  N  N   . LYS A 1 603 ? 117.478 133.059 116.551 1.00 48.79  ? 578 LYS A N   1 
ATOM   3897  C  CA  . LYS A 1 603 ? 117.693 134.503 116.489 1.00 44.63  ? 578 LYS A CA  1 
ATOM   3898  C  C   . LYS A 1 603 ? 119.165 134.817 116.224 1.00 49.43  ? 578 LYS A C   1 
ATOM   3899  O  O   . LYS A 1 603 ? 119.897 135.314 117.078 1.00 58.52  ? 578 LYS A O   1 
ATOM   3900  C  CB  . LYS A 1 603 ? 117.208 135.159 117.774 1.00 50.95  ? 578 LYS A CB  1 
ATOM   3901  C  CG  . LYS A 1 603 ? 115.936 134.557 118.335 1.00 49.79  ? 578 LYS A CG  1 
ATOM   3902  C  CD  . LYS A 1 603 ? 115.465 135.324 119.553 1.00 46.44  ? 578 LYS A CD  1 
ATOM   3903  C  CE  . LYS A 1 603 ? 114.375 134.575 120.280 1.00 41.13  ? 578 LYS A CE  1 
ATOM   3904  N  NZ  . LYS A 1 603 ? 113.372 134.045 119.329 1.00 46.10  ? 578 LYS A NZ  1 
ATOM   3905  N  N   . GLN A 1 604 ? 119.585 134.543 114.993 1.00 55.25  ? 579 GLN A N   1 
ATOM   3906  C  CA  . GLN A 1 604 ? 120.947 134.858 114.583 1.00 53.03  ? 579 GLN A CA  1 
ATOM   3907  C  C   . GLN A 1 604 ? 121.177 136.363 114.585 1.00 51.79  ? 579 GLN A C   1 
ATOM   3908  O  O   . GLN A 1 604 ? 120.337 137.136 114.122 1.00 62.10  ? 579 GLN A O   1 
ATOM   3909  C  CB  . GLN A 1 604 ? 121.224 134.296 113.192 1.00 51.09  ? 579 GLN A CB  1 
ATOM   3910  C  CG  . GLN A 1 604 ? 121.267 132.786 113.127 1.00 53.77  ? 579 GLN A CG  1 
ATOM   3911  C  CD  . GLN A 1 604 ? 122.619 132.265 112.698 1.00 62.88  ? 579 GLN A CD  1 
ATOM   3912  O  OE1 . GLN A 1 604 ? 123.195 132.736 111.719 1.00 67.40  ? 579 GLN A OE1 1 
ATOM   3913  N  NE2 . GLN A 1 604 ? 123.137 131.288 113.430 1.00 61.68  ? 579 GLN A NE2 1 
ATOM   3914  N  N   . TYR A 1 605 ? 122.329 136.779 115.106 1.00 30.31  ? 580 TYR A N   1 
ATOM   3915  C  CA  . TYR A 1 605 ? 122.727 138.178 115.094 1.00 29.81  ? 580 TYR A CA  1 
ATOM   3916  C  C   . TYR A 1 605 ? 124.225 138.250 114.841 1.00 41.37  ? 580 TYR A C   1 
ATOM   3917  O  O   . TYR A 1 605 ? 124.901 137.226 114.721 1.00 66.35  ? 580 TYR A O   1 
ATOM   3918  C  CB  . TYR A 1 605 ? 122.327 138.878 116.397 1.00 36.44  ? 580 TYR A CB  1 
ATOM   3919  C  CG  . TYR A 1 605 ? 123.197 138.577 117.593 1.00 22.01  ? 580 TYR A CG  1 
ATOM   3920  C  CD1 . TYR A 1 605 ? 124.311 139.343 117.876 1.00 36.18  ? 580 TYR A CD1 1 
ATOM   3921  C  CD2 . TYR A 1 605 ? 122.883 137.546 118.454 1.00 35.24  ? 580 TYR A CD2 1 
ATOM   3922  C  CE1 . TYR A 1 605 ? 125.096 139.079 118.968 1.00 44.49  ? 580 TYR A CE1 1 
ATOM   3923  C  CE2 . TYR A 1 605 ? 123.665 137.275 119.550 1.00 41.88  ? 580 TYR A CE2 1 
ATOM   3924  C  CZ  . TYR A 1 605 ? 124.768 138.045 119.801 1.00 42.68  ? 580 TYR A CZ  1 
ATOM   3925  O  OH  . TYR A 1 605 ? 125.554 137.780 120.893 1.00 48.45  ? 580 TYR A OH  1 
ATOM   3926  N  N   . LEU A 1 606 ? 124.750 139.467 114.745 1.00 32.97  ? 581 LEU A N   1 
ATOM   3927  C  CA  . LEU A 1 606 ? 126.172 139.691 114.520 1.00 33.52  ? 581 LEU A CA  1 
ATOM   3928  C  C   . LEU A 1 606 ? 126.748 140.472 115.688 1.00 35.67  ? 581 LEU A C   1 
ATOM   3929  O  O   . LEU A 1 606 ? 126.159 141.461 116.128 1.00 50.11  ? 581 LEU A O   1 
ATOM   3930  C  CB  . LEU A 1 606 ? 126.423 140.441 113.215 1.00 43.90  ? 581 LEU A CB  1 
ATOM   3931  C  CG  . LEU A 1 606 ? 127.890 140.752 112.922 1.00 47.72  ? 581 LEU A CG  1 
ATOM   3932  C  CD1 . LEU A 1 606 ? 128.599 139.528 112.384 1.00 51.47  ? 581 LEU A CD1 1 
ATOM   3933  C  CD2 . LEU A 1 606 ? 128.001 141.889 111.936 1.00 45.66  ? 581 LEU A CD2 1 
ATOM   3934  N  N   . HIS A 1 607 ? 127.900 140.026 116.180 1.00 45.04  ? 582 HIS A N   1 
ATOM   3935  C  CA  . HIS A 1 607 ? 128.524 140.584 117.377 1.00 44.72  ? 582 HIS A CA  1 
ATOM   3936  C  C   . HIS A 1 607 ? 129.624 141.547 116.943 1.00 49.01  ? 582 HIS A C   1 
ATOM   3937  O  O   . HIS A 1 607 ? 130.811 141.237 116.984 1.00 66.76  ? 582 HIS A O   1 
ATOM   3938  C  CB  . HIS A 1 607 ? 129.055 139.454 118.250 1.00 50.95  ? 582 HIS A CB  1 
ATOM   3939  C  CG  . HIS A 1 607 ? 129.841 139.908 119.438 1.00 56.12  ? 582 HIS A CG  1 
ATOM   3940  N  ND1 . HIS A 1 607 ? 131.097 140.465 119.332 1.00 66.99  ? 582 HIS A ND1 1 
ATOM   3941  C  CD2 . HIS A 1 607 ? 129.568 139.846 120.761 1.00 56.48  ? 582 HIS A CD2 1 
ATOM   3942  C  CE1 . HIS A 1 607 ? 131.554 140.748 120.538 1.00 61.95  ? 582 HIS A CE1 1 
ATOM   3943  N  NE2 . HIS A 1 607 ? 130.646 140.380 121.423 1.00 64.13  ? 582 HIS A NE2 1 
ATOM   3944  N  N   . ILE A 1 608 ? 129.210 142.742 116.524 1.00 36.41  ? 583 ILE A N   1 
ATOM   3945  C  CA  . ILE A 1 608 ? 130.151 143.720 115.990 1.00 42.62  ? 583 ILE A CA  1 
ATOM   3946  C  C   . ILE A 1 608 ? 131.144 144.116 117.070 1.00 39.63  ? 583 ILE A C   1 
ATOM   3947  O  O   . ILE A 1 608 ? 130.765 144.425 118.205 1.00 46.19  ? 583 ILE A O   1 
ATOM   3948  C  CB  . ILE A 1 608 ? 129.409 144.946 115.442 1.00 43.62  ? 583 ILE A CB  1 
ATOM   3949  C  CG1 . ILE A 1 608 ? 128.654 144.591 114.166 1.00 42.44  ? 583 ILE A CG1 1 
ATOM   3950  C  CG2 . ILE A 1 608 ? 130.377 146.065 115.153 1.00 37.99  ? 583 ILE A CG2 1 
ATOM   3951  C  CD1 . ILE A 1 608 ? 127.880 145.740 113.591 1.00 36.80  ? 583 ILE A CD1 1 
ATOM   3952  N  N   . GLY A 1 609 ? 132.423 144.102 116.721 1.00 56.29  ? 584 GLY A N   1 
ATOM   3953  C  CA  . GLY A 1 609 ? 133.465 144.421 117.672 1.00 63.13  ? 584 GLY A CA  1 
ATOM   3954  C  C   . GLY A 1 609 ? 134.819 144.075 117.088 1.00 67.20  ? 584 GLY A C   1 
ATOM   3955  O  O   . GLY A 1 609 ? 134.940 143.760 115.903 1.00 68.65  ? 584 GLY A O   1 
ATOM   3956  N  N   . LEU A 1 610 ? 135.836 144.138 117.945 1.00 68.83  ? 585 LEU A N   1 
ATOM   3957  C  CA  . LEU A 1 610 ? 137.181 143.796 117.502 1.00 65.61  ? 585 LEU A CA  1 
ATOM   3958  C  C   . LEU A 1 610 ? 137.318 142.320 117.155 1.00 70.93  ? 585 LEU A C   1 
ATOM   3959  O  O   . LEU A 1 610 ? 138.217 141.959 116.388 1.00 74.17  ? 585 LEU A O   1 
ATOM   3960  C  CB  . LEU A 1 610 ? 138.199 144.181 118.573 1.00 67.19  ? 585 LEU A CB  1 
ATOM   3961  C  CG  . LEU A 1 610 ? 138.613 145.652 118.599 1.00 67.43  ? 585 LEU A CG  1 
ATOM   3962  C  CD1 . LEU A 1 610 ? 139.982 145.801 119.232 1.00 71.35  ? 585 LEU A CD1 1 
ATOM   3963  C  CD2 . LEU A 1 610 ? 138.608 146.239 117.199 1.00 65.08  ? 585 LEU A CD2 1 
ATOM   3964  N  N   . LYS A 1 611 ? 136.451 141.464 117.692 1.00 70.64  ? 586 LYS A N   1 
ATOM   3965  C  CA  . LYS A 1 611 ? 136.465 140.027 117.414 1.00 72.76  ? 586 LYS A CA  1 
ATOM   3966  C  C   . LYS A 1 611 ? 135.065 139.590 117.002 1.00 73.90  ? 586 LYS A C   1 
ATOM   3967  O  O   . LYS A 1 611 ? 134.352 138.933 117.769 1.00 77.29  ? 586 LYS A O   1 
ATOM   3968  C  CB  . LYS A 1 611 ? 136.953 139.238 118.628 1.00 72.06  ? 586 LYS A CB  1 
ATOM   3969  N  N   . PRO A 1 612 ? 134.642 139.941 115.791 1.00 61.30  ? 587 PRO A N   1 
ATOM   3970  C  CA  . PRO A 1 612 ? 133.271 139.642 115.372 1.00 63.08  ? 587 PRO A CA  1 
ATOM   3971  C  C   . PRO A 1 612 ? 133.035 138.157 115.174 1.00 61.12  ? 587 PRO A C   1 
ATOM   3972  O  O   . PRO A 1 612 ? 133.947 137.395 114.852 1.00 72.88  ? 587 PRO A O   1 
ATOM   3973  C  CB  . PRO A 1 612 ? 133.142 140.389 114.046 1.00 61.28  ? 587 PRO A CB  1 
ATOM   3974  C  CG  . PRO A 1 612 ? 134.525 140.406 113.523 1.00 64.43  ? 587 PRO A CG  1 
ATOM   3975  C  CD  . PRO A 1 612 ? 135.415 140.577 114.714 1.00 58.54  ? 587 PRO A CD  1 
ATOM   3976  N  N   . ARG A 1 613 ? 131.780 137.758 115.357 1.00 54.94  ? 588 ARG A N   1 
ATOM   3977  C  CA  . ARG A 1 613 ? 131.341 136.396 115.097 1.00 63.80  ? 588 ARG A CA  1 
ATOM   3978  C  C   . ARG A 1 613 ? 129.824 136.376 115.106 1.00 60.96  ? 588 ARG A C   1 
ATOM   3979  O  O   . ARG A 1 613 ? 129.200 137.053 115.922 1.00 63.39  ? 588 ARG A O   1 
ATOM   3980  C  CB  . ARG A 1 613 ? 131.893 135.418 116.141 1.00 66.34  ? 588 ARG A CB  1 
ATOM   3981  C  CG  . ARG A 1 613 ? 131.909 135.961 117.557 1.00 65.68  ? 588 ARG A CG  1 
ATOM   3982  C  CD  . ARG A 1 613 ? 132.418 134.923 118.540 1.00 67.92  ? 588 ARG A CD  1 
ATOM   3983  N  NE  . ARG A 1 613 ? 132.038 135.241 119.911 1.00 70.93  ? 588 ARG A NE  1 
ATOM   3984  C  CZ  . ARG A 1 613 ? 132.662 136.125 120.677 1.00 72.17  ? 588 ARG A CZ  1 
ATOM   3985  N  NH1 . ARG A 1 613 ? 133.709 136.804 120.238 1.00 68.70  ? 588 ARG A NH1 1 
ATOM   3986  N  NH2 . ARG A 1 613 ? 132.223 136.334 121.915 1.00 69.32  ? 588 ARG A NH2 1 
ATOM   3987  N  N   . VAL A 1 614 ? 129.237 135.598 114.199 1.00 43.00  ? 589 VAL A N   1 
ATOM   3988  C  CA  . VAL A 1 614 ? 127.785 135.488 114.105 1.00 38.00  ? 589 VAL A CA  1 
ATOM   3989  C  C   . VAL A 1 614 ? 127.323 134.563 115.227 1.00 44.70  ? 589 VAL A C   1 
ATOM   3990  O  O   . VAL A 1 614 ? 127.382 133.340 115.102 1.00 64.64  ? 589 VAL A O   1 
ATOM   3991  C  CB  . VAL A 1 614 ? 127.340 134.980 112.734 1.00 40.63  ? 589 VAL A CB  1 
ATOM   3992  C  CG1 . VAL A 1 614 ? 125.835 134.848 112.684 1.00 38.53  ? 589 VAL A CG1 1 
ATOM   3993  C  CG2 . VAL A 1 614 ? 127.823 135.918 111.659 1.00 54.78  ? 589 VAL A CG2 1 
ATOM   3994  N  N   . ARG A 1 615 ? 126.860 135.144 116.327 1.00 40.23  ? 590 ARG A N   1 
ATOM   3995  C  CA  . ARG A 1 615 ? 126.366 134.371 117.456 1.00 47.21  ? 590 ARG A CA  1 
ATOM   3996  C  C   . ARG A 1 615 ? 124.946 133.896 117.156 1.00 50.81  ? 590 ARG A C   1 
ATOM   3997  O  O   . ARG A 1 615 ? 124.459 133.998 116.028 1.00 50.90  ? 590 ARG A O   1 
ATOM   3998  C  CB  . ARG A 1 615 ? 126.453 135.198 118.731 1.00 53.86  ? 590 ARG A CB  1 
ATOM   3999  C  CG  . ARG A 1 615 ? 127.767 135.939 118.890 1.00 53.47  ? 590 ARG A CG  1 
ATOM   4000  C  CD  . ARG A 1 615 ? 128.787 135.100 119.636 1.00 57.26  ? 590 ARG A CD  1 
ATOM   4001  N  NE  . ARG A 1 615 ? 128.157 134.172 120.567 1.00 67.30  ? 590 ARG A NE  1 
ATOM   4002  C  CZ  . ARG A 1 615 ? 127.756 134.493 121.789 1.00 64.31  ? 590 ARG A CZ  1 
ATOM   4003  N  NH1 . ARG A 1 615 ? 127.918 135.713 122.271 1.00 58.22  ? 590 ARG A NH1 1 
ATOM   4004  N  NH2 . ARG A 1 615 ? 127.174 133.566 122.544 1.00 59.80  ? 590 ARG A NH2 1 
ATOM   4005  N  N   . ASP A 1 616 ? 124.253 133.366 118.164 1.00 59.79  ? 591 ASP A N   1 
ATOM   4006  C  CA  . ASP A 1 616 ? 122.984 132.701 117.900 1.00 59.95  ? 591 ASP A CA  1 
ATOM   4007  C  C   . ASP A 1 616 ? 121.836 133.190 118.775 1.00 62.68  ? 591 ASP A C   1 
ATOM   4008  O  O   . ASP A 1 616 ? 120.673 133.094 118.375 1.00 68.92  ? 591 ASP A O   1 
ATOM   4009  C  CB  . ASP A 1 616 ? 123.142 131.192 118.069 1.00 67.23  ? 591 ASP A CB  1 
ATOM   4010  C  CG  . ASP A 1 616 ? 122.021 130.416 117.418 1.00 71.36  ? 591 ASP A CG  1 
ATOM   4011  O  OD1 . ASP A 1 616 ? 122.056 130.247 116.182 1.00 74.46  ? 591 ASP A OD1 1 
ATOM   4012  O  OD2 . ASP A 1 616 ? 121.102 129.979 118.140 1.00 71.69  ? 591 ASP A OD2 1 
ATOM   4013  N  N   . ASN A 1 617 ? 122.133 133.693 119.969 1.00 62.90  ? 592 ASN A N   1 
ATOM   4014  C  CA  . ASN A 1 617 ? 121.096 134.191 120.865 1.00 64.32  ? 592 ASN A CA  1 
ATOM   4015  C  C   . ASN A 1 617 ? 121.721 135.206 121.805 1.00 70.88  ? 592 ASN A C   1 
ATOM   4016  O  O   . ASN A 1 617 ? 122.693 134.889 122.496 1.00 75.84  ? 592 ASN A O   1 
ATOM   4017  C  CB  . ASN A 1 617 ? 120.457 133.058 121.673 1.00 61.15  ? 592 ASN A CB  1 
ATOM   4018  C  CG  . ASN A 1 617 ? 119.288 132.418 120.964 1.00 63.36  ? 592 ASN A CG  1 
ATOM   4019  O  OD1 . ASN A 1 617 ? 119.440 131.406 120.284 1.00 68.88  ? 592 ASN A OD1 1 
ATOM   4020  N  ND2 . ASN A 1 617 ? 118.110 132.998 121.125 1.00 65.51  ? 592 ASN A ND2 1 
ATOM   4021  N  N   . TYR A 1 618 ? 121.169 136.414 121.839 1.00 46.65  ? 593 TYR A N   1 
ATOM   4022  C  CA  . TYR A 1 618 ? 121.701 137.480 122.678 1.00 46.15  ? 593 TYR A CA  1 
ATOM   4023  C  C   . TYR A 1 618 ? 120.971 137.468 124.010 1.00 47.03  ? 593 TYR A C   1 
ATOM   4024  O  O   . TYR A 1 618 ? 119.772 137.755 124.065 1.00 52.86  ? 593 TYR A O   1 
ATOM   4025  C  CB  . TYR A 1 618 ? 121.563 138.842 122.008 1.00 45.72  ? 593 TYR A CB  1 
ATOM   4026  C  CG  . TYR A 1 618 ? 122.301 139.925 122.751 1.00 38.30  ? 593 TYR A CG  1 
ATOM   4027  C  CD1 . TYR A 1 618 ? 123.637 139.776 123.075 1.00 40.64  ? 593 TYR A CD1 1 
ATOM   4028  C  CD2 . TYR A 1 618 ? 121.660 141.083 123.144 1.00 40.00  ? 593 TYR A CD2 1 
ATOM   4029  C  CE1 . TYR A 1 618 ? 124.316 140.752 123.755 1.00 42.27  ? 593 TYR A CE1 1 
ATOM   4030  C  CE2 . TYR A 1 618 ? 122.332 142.064 123.827 1.00 48.27  ? 593 TYR A CE2 1 
ATOM   4031  C  CZ  . TYR A 1 618 ? 123.659 141.893 124.130 1.00 48.69  ? 593 TYR A CZ  1 
ATOM   4032  O  OH  . TYR A 1 618 ? 124.337 142.871 124.813 1.00 56.89  ? 593 TYR A OH  1 
ATOM   4033  N  N   . ARG A 1 619 ? 121.700 137.157 125.079 1.00 42.62  ? 594 ARG A N   1 
ATOM   4034  C  CA  . ARG A 1 619 ? 121.174 137.170 126.440 1.00 38.82  ? 594 ARG A CA  1 
ATOM   4035  C  C   . ARG A 1 619 ? 119.824 136.466 126.501 1.00 45.51  ? 594 ARG A C   1 
ATOM   4036  O  O   . ARG A 1 619 ? 118.813 137.035 126.909 1.00 54.95  ? 594 ARG A O   1 
ATOM   4037  C  CB  . ARG A 1 619 ? 121.069 138.601 126.969 1.00 31.44  ? 594 ARG A CB  1 
ATOM   4038  C  CG  . ARG A 1 619 ? 122.231 139.032 127.835 1.00 33.06  ? 594 ARG A CG  1 
ATOM   4039  C  CD  . ARG A 1 619 ? 121.964 140.384 128.458 1.00 34.90  ? 594 ARG A CD  1 
ATOM   4040  N  NE  . ARG A 1 619 ? 123.061 140.815 129.314 1.00 44.05  ? 594 ARG A NE  1 
ATOM   4041  C  CZ  . ARG A 1 619 ? 123.217 140.443 130.577 1.00 54.55  ? 594 ARG A CZ  1 
ATOM   4042  N  NH1 . ARG A 1 619 ? 122.364 139.624 131.166 1.00 50.88  ? 594 ARG A NH1 1 
ATOM   4043  N  NH2 . ARG A 1 619 ? 124.257 140.903 131.266 1.00 57.18  ? 594 ARG A NH2 1 
ATOM   4044  N  N   . ALA A 1 620 ? 119.824 135.206 126.064 1.00 39.01  ? 595 ALA A N   1 
ATOM   4045  C  CA  . ALA A 1 620 ? 118.571 134.476 125.915 1.00 40.15  ? 595 ALA A CA  1 
ATOM   4046  C  C   . ALA A 1 620 ? 117.833 134.367 127.240 1.00 39.68  ? 595 ALA A C   1 
ATOM   4047  O  O   . ALA A 1 620 ? 116.607 134.512 127.289 1.00 45.37  ? 595 ALA A O   1 
ATOM   4048  C  CB  . ALA A 1 620 ? 118.838 133.089 125.337 1.00 43.56  ? 595 ALA A CB  1 
ATOM   4049  N  N   . ASN A 1 621 ? 118.565 134.128 128.326 1.00 42.25  ? 596 ASN A N   1 
ATOM   4050  C  CA  . ASN A 1 621 ? 117.925 133.939 129.622 1.00 47.67  ? 596 ASN A CA  1 
ATOM   4051  C  C   . ASN A 1 621 ? 117.183 135.194 130.065 1.00 52.21  ? 596 ASN A C   1 
ATOM   4052  O  O   . ASN A 1 621 ? 115.993 135.142 130.387 1.00 58.53  ? 596 ASN A O   1 
ATOM   4053  C  CB  . ASN A 1 621 ? 118.971 133.536 130.657 1.00 47.55  ? 596 ASN A CB  1 
ATOM   4054  C  CG  . ASN A 1 621 ? 118.354 133.108 131.963 1.00 57.27  ? 596 ASN A CG  1 
ATOM   4055  O  OD1 . ASN A 1 621 ? 117.173 132.777 132.022 1.00 66.01  ? 596 ASN A OD1 1 
ATOM   4056  N  ND2 . ASN A 1 621 ? 119.150 133.112 133.024 1.00 52.27  ? 596 ASN A ND2 1 
ATOM   4057  N  N   . LYS A 1 622 ? 117.864 136.341 130.066 1.00 38.55  ? 597 LYS A N   1 
ATOM   4058  C  CA  . LYS A 1 622 ? 117.243 137.558 130.578 1.00 36.73  ? 597 LYS A CA  1 
ATOM   4059  C  C   . LYS A 1 622 ? 116.186 138.094 129.621 1.00 33.95  ? 597 LYS A C   1 
ATOM   4060  O  O   . LYS A 1 622 ? 115.165 138.636 130.057 1.00 44.34  ? 597 LYS A O   1 
ATOM   4061  C  CB  . LYS A 1 622 ? 118.309 138.612 130.850 1.00 43.10  ? 597 LYS A CB  1 
ATOM   4062  C  CG  . LYS A 1 622 ? 119.478 138.093 131.650 1.00 39.95  ? 597 LYS A CG  1 
ATOM   4063  C  CD  . LYS A 1 622 ? 119.071 137.787 133.071 1.00 36.22  ? 597 LYS A CD  1 
ATOM   4064  C  CE  . LYS A 1 622 ? 120.223 137.182 133.847 1.00 43.93  ? 597 LYS A CE  1 
ATOM   4065  N  NZ  . LYS A 1 622 ? 119.770 136.593 135.135 1.00 50.28  ? 597 LYS A NZ  1 
ATOM   4066  N  N   . VAL A 1 623 ? 116.409 137.957 128.314 1.00 31.28  ? 598 VAL A N   1 
ATOM   4067  C  CA  . VAL A 1 623 ? 115.393 138.373 127.353 1.00 35.12  ? 598 VAL A CA  1 
ATOM   4068  C  C   . VAL A 1 623 ? 114.130 137.540 127.522 1.00 43.82  ? 598 VAL A C   1 
ATOM   4069  O  O   . VAL A 1 623 ? 113.012 138.069 127.501 1.00 55.17  ? 598 VAL A O   1 
ATOM   4070  C  CB  . VAL A 1 623 ? 115.947 138.286 125.921 1.00 31.77  ? 598 VAL A CB  1 
ATOM   4071  C  CG1 . VAL A 1 623 ? 114.823 138.320 124.918 1.00 24.55  ? 598 VAL A CG1 1 
ATOM   4072  C  CG2 . VAL A 1 623 ? 116.914 139.418 125.670 1.00 38.61  ? 598 VAL A CG2 1 
ATOM   4073  N  N   . ALA A 1 624 ? 114.284 136.226 127.702 1.00 38.36  ? 599 ALA A N   1 
ATOM   4074  C  CA  . ALA A 1 624 ? 113.123 135.379 127.949 1.00 36.82  ? 599 ALA A CA  1 
ATOM   4075  C  C   . ALA A 1 624 ? 112.463 135.724 129.275 1.00 39.29  ? 599 ALA A C   1 
ATOM   4076  O  O   . ALA A 1 624 ? 111.238 135.653 129.402 1.00 34.49  ? 599 ALA A O   1 
ATOM   4077  C  CB  . ALA A 1 624 ? 113.528 133.910 127.920 1.00 44.79  ? 599 ALA A CB  1 
ATOM   4078  N  N   . PHE A 1 625 ? 113.260 136.096 130.277 1.00 37.58  ? 600 PHE A N   1 
ATOM   4079  C  CA  . PHE A 1 625 ? 112.695 136.521 131.553 1.00 31.17  ? 600 PHE A CA  1 
ATOM   4080  C  C   . PHE A 1 625 ? 111.832 137.763 131.387 1.00 37.28  ? 600 PHE A C   1 
ATOM   4081  O  O   . PHE A 1 625 ? 110.747 137.857 131.970 1.00 44.50  ? 600 PHE A O   1 
ATOM   4082  C  CB  . PHE A 1 625 ? 113.819 136.778 132.557 1.00 28.01  ? 600 PHE A CB  1 
ATOM   4083  C  CG  . PHE A 1 625 ? 113.372 137.463 133.813 1.00 24.33  ? 600 PHE A CG  1 
ATOM   4084  C  CD1 . PHE A 1 625 ? 112.276 137.015 134.512 1.00 33.36  ? 600 PHE A CD1 1 
ATOM   4085  C  CD2 . PHE A 1 625 ? 114.060 138.548 134.301 1.00 32.47  ? 600 PHE A CD2 1 
ATOM   4086  C  CE1 . PHE A 1 625 ? 111.872 137.643 135.662 1.00 29.71  ? 600 PHE A CE1 1 
ATOM   4087  C  CE2 . PHE A 1 625 ? 113.656 139.176 135.450 1.00 31.10  ? 600 PHE A CE2 1 
ATOM   4088  C  CZ  . PHE A 1 625 ? 112.562 138.722 136.129 1.00 26.67  ? 600 PHE A CZ  1 
ATOM   4089  N  N   . TRP A 1 626 ? 112.295 138.727 130.593 1.00 39.52  ? 601 TRP A N   1 
ATOM   4090  C  CA  . TRP A 1 626 ? 111.569 139.985 130.467 1.00 27.59  ? 601 TRP A CA  1 
ATOM   4091  C  C   . TRP A 1 626 ? 110.397 139.894 129.502 1.00 35.42  ? 601 TRP A C   1 
ATOM   4092  O  O   . TRP A 1 626 ? 109.457 140.686 129.611 1.00 41.36  ? 601 TRP A O   1 
ATOM   4093  C  CB  . TRP A 1 626 ? 112.517 141.099 130.031 1.00 19.54  ? 601 TRP A CB  1 
ATOM   4094  C  CG  . TRP A 1 626 ? 113.343 141.597 131.148 1.00 21.69  ? 601 TRP A CG  1 
ATOM   4095  C  CD1 . TRP A 1 626 ? 114.687 141.480 131.281 1.00 34.80  ? 601 TRP A CD1 1 
ATOM   4096  C  CD2 . TRP A 1 626 ? 112.880 142.275 132.316 1.00 24.94  ? 601 TRP A CD2 1 
ATOM   4097  N  NE1 . TRP A 1 626 ? 115.096 142.050 132.457 1.00 33.91  ? 601 TRP A NE1 1 
ATOM   4098  C  CE2 . TRP A 1 626 ? 114.001 142.547 133.110 1.00 27.69  ? 601 TRP A CE2 1 
ATOM   4099  C  CE3 . TRP A 1 626 ? 111.625 142.683 132.764 1.00 35.21  ? 601 TRP A CE3 1 
ATOM   4100  C  CZ2 . TRP A 1 626 ? 113.908 143.206 134.323 1.00 38.70  ? 601 TRP A CZ2 1 
ATOM   4101  C  CZ3 . TRP A 1 626 ? 111.535 143.336 133.969 1.00 42.15  ? 601 TRP A CZ3 1 
ATOM   4102  C  CH2 . TRP A 1 626 ? 112.668 143.592 134.735 1.00 41.96  ? 601 TRP A CH2 1 
ATOM   4103  N  N   . LEU A 1 627 ? 110.423 138.953 128.562 1.00 35.77  ? 602 LEU A N   1 
ATOM   4104  C  CA  . LEU A 1 627 ? 109.343 138.859 127.589 1.00 29.09  ? 602 LEU A CA  1 
ATOM   4105  C  C   . LEU A 1 627 ? 108.312 137.788 127.908 1.00 46.40  ? 602 LEU A C   1 
ATOM   4106  O  O   . LEU A 1 627 ? 107.151 137.938 127.519 1.00 51.53  ? 602 LEU A O   1 
ATOM   4107  C  CB  . LEU A 1 627 ? 109.905 138.589 126.192 1.00 29.62  ? 602 LEU A CB  1 
ATOM   4108  C  CG  . LEU A 1 627 ? 110.840 139.629 125.586 1.00 39.45  ? 602 LEU A CG  1 
ATOM   4109  C  CD1 . LEU A 1 627 ? 111.347 139.131 124.254 1.00 40.89  ? 602 LEU A CD1 1 
ATOM   4110  C  CD2 . LEU A 1 627 ? 110.132 140.952 125.422 1.00 36.78  ? 602 LEU A CD2 1 
ATOM   4111  N  N   . GLU A 1 628 ? 108.687 136.716 128.605 1.00 54.93  ? 603 GLU A N   1 
ATOM   4112  C  CA  . GLU A 1 628 ? 107.817 135.558 128.749 1.00 51.06  ? 603 GLU A CA  1 
ATOM   4113  C  C   . GLU A 1 628 ? 107.394 135.248 130.176 1.00 53.53  ? 603 GLU A C   1 
ATOM   4114  O  O   . GLU A 1 628 ? 106.306 134.707 130.364 1.00 60.46  ? 603 GLU A O   1 
ATOM   4115  C  CB  . GLU A 1 628 ? 108.494 134.314 128.157 1.00 51.23  ? 603 GLU A CB  1 
ATOM   4116  C  CG  . GLU A 1 628 ? 109.290 134.599 126.897 1.00 58.17  ? 603 GLU A CG  1 
ATOM   4117  C  CD  . GLU A 1 628 ? 109.275 133.445 125.919 1.00 69.18  ? 603 GLU A CD  1 
ATOM   4118  O  OE1 . GLU A 1 628 ? 108.623 132.423 126.215 1.00 68.62  ? 603 GLU A OE1 1 
ATOM   4119  O  OE2 . GLU A 1 628 ? 109.912 133.559 124.852 1.00 66.67  ? 603 GLU A OE2 1 
ATOM   4120  N  N   . LEU A 1 629 ? 108.209 135.559 131.182 1.00 41.37  ? 604 LEU A N   1 
ATOM   4121  C  CA  . LEU A 1 629 ? 107.829 135.283 132.563 1.00 30.12  ? 604 LEU A CA  1 
ATOM   4122  C  C   . LEU A 1 629 ? 107.211 136.482 133.265 1.00 40.04  ? 604 LEU A C   1 
ATOM   4123  O  O   . LEU A 1 629 ? 106.189 136.331 133.937 1.00 60.79  ? 604 LEU A O   1 
ATOM   4124  C  CB  . LEU A 1 629 ? 109.035 134.800 133.374 1.00 30.31  ? 604 LEU A CB  1 
ATOM   4125  C  CG  . LEU A 1 629 ? 108.853 134.820 134.894 1.00 26.50  ? 604 LEU A CG  1 
ATOM   4126  C  CD1 . LEU A 1 629 ? 107.749 133.880 135.312 1.00 40.72  ? 604 LEU A CD1 1 
ATOM   4127  C  CD2 . LEU A 1 629 ? 110.136 134.459 135.604 1.00 36.74  ? 604 LEU A CD2 1 
ATOM   4128  N  N   . VAL A 1 630 ? 107.807 137.668 133.127 1.00 31.17  ? 605 VAL A N   1 
ATOM   4129  C  CA  . VAL A 1 630 ? 107.300 138.840 133.847 1.00 23.52  ? 605 VAL A CA  1 
ATOM   4130  C  C   . VAL A 1 630 ? 105.829 139.110 133.563 1.00 40.62  ? 605 VAL A C   1 
ATOM   4131  O  O   . VAL A 1 630 ? 105.096 139.443 134.505 1.00 53.29  ? 605 VAL A O   1 
ATOM   4132  C  CB  . VAL A 1 630 ? 108.203 140.052 133.585 1.00 24.57  ? 605 VAL A CB  1 
ATOM   4133  C  CG1 . VAL A 1 630 ? 107.422 141.335 133.711 1.00 42.61  ? 605 VAL A CG1 1 
ATOM   4134  C  CG2 . VAL A 1 630 ? 109.345 140.054 134.567 1.00 29.55  ? 605 VAL A CG2 1 
ATOM   4135  N  N   . PRO A 1 631 ? 105.320 138.987 132.332 1.00 46.09  ? 606 PRO A N   1 
ATOM   4136  C  CA  . PRO A 1 631 ? 103.873 139.173 132.133 1.00 51.43  ? 606 PRO A CA  1 
ATOM   4137  C  C   . PRO A 1 631 ? 103.010 138.219 132.941 1.00 53.42  ? 606 PRO A C   1 
ATOM   4138  O  O   . PRO A 1 631 ? 101.843 138.535 133.199 1.00 56.93  ? 606 PRO A O   1 
ATOM   4139  C  CB  . PRO A 1 631 ? 103.699 138.943 130.628 1.00 49.74  ? 606 PRO A CB  1 
ATOM   4140  C  CG  . PRO A 1 631 ? 104.984 139.353 130.055 1.00 46.39  ? 606 PRO A CG  1 
ATOM   4141  C  CD  . PRO A 1 631 ? 106.020 138.904 131.038 1.00 46.52  ? 606 PRO A CD  1 
ATOM   4142  N  N   . HIS A 1 632 ? 103.538 137.067 133.350 1.00 50.19  ? 607 HIS A N   1 
ATOM   4143  C  CA  . HIS A 1 632 ? 102.782 136.119 134.158 1.00 46.36  ? 607 HIS A CA  1 
ATOM   4144  C  C   . HIS A 1 632 ? 102.797 136.450 135.642 1.00 51.66  ? 607 HIS A C   1 
ATOM   4145  O  O   . HIS A 1 632 ? 102.140 135.751 136.418 1.00 57.47  ? 607 HIS A O   1 
ATOM   4146  C  CB  . HIS A 1 632 ? 103.321 134.704 133.955 1.00 45.54  ? 607 HIS A CB  1 
ATOM   4147  C  CG  . HIS A 1 632 ? 102.945 134.099 132.642 1.00 57.41  ? 607 HIS A CG  1 
ATOM   4148  N  ND1 . HIS A 1 632 ? 102.156 132.975 132.540 1.00 61.25  ? 607 HIS A ND1 1 
ATOM   4149  C  CD2 . HIS A 1 632 ? 103.250 134.462 131.374 1.00 60.28  ? 607 HIS A CD2 1 
ATOM   4150  C  CE1 . HIS A 1 632 ? 101.990 132.670 131.265 1.00 64.75  ? 607 HIS A CE1 1 
ATOM   4151  N  NE2 . HIS A 1 632 ? 102.644 133.557 130.537 1.00 66.99  ? 607 HIS A NE2 1 
ATOM   4152  N  N   . LEU A 1 633 ? 103.520 137.481 136.058 1.00 42.68  ? 608 LEU A N   1 
ATOM   4153  C  CA  . LEU A 1 633 ? 103.591 137.832 137.469 1.00 42.25  ? 608 LEU A CA  1 
ATOM   4154  C  C   . LEU A 1 633 ? 102.782 139.087 137.766 1.00 47.90  ? 608 LEU A C   1 
ATOM   4155  O  O   . LEU A 1 633 ? 103.197 140.196 137.434 1.00 54.41  ? 608 LEU A O   1 
ATOM   4156  C  CB  . LEU A 1 633 ? 105.043 138.032 137.900 1.00 37.11  ? 608 LEU A CB  1 
ATOM   4157  C  CG  . LEU A 1 633 ? 106.013 136.872 137.684 1.00 32.64  ? 608 LEU A CG  1 
ATOM   4158  C  CD1 . LEU A 1 633 ? 107.206 137.044 138.578 1.00 36.52  ? 608 LEU A CD1 1 
ATOM   4159  C  CD2 . LEU A 1 633 ? 105.351 135.537 137.949 1.00 43.35  ? 608 LEU A CD2 1 
ATOM   4160  N  N   . ARG B 1 82  ? 139.971 77.756  161.428 1.00 82.67  ? 40  ARG B N   1 
ATOM   4161  C  CA  . ARG B 1 82  ? 140.207 78.816  162.399 1.00 85.16  ? 40  ARG B CA  1 
ATOM   4162  C  C   . ARG B 1 82  ? 138.931 79.609  162.650 1.00 85.78  ? 40  ARG B C   1 
ATOM   4163  O  O   . ARG B 1 82  ? 138.610 80.530  161.904 1.00 85.39  ? 40  ARG B O   1 
ATOM   4164  C  CB  . ARG B 1 82  ? 141.323 79.743  161.918 1.00 84.24  ? 40  ARG B CB  1 
ATOM   4165  C  CG  . ARG B 1 82  ? 141.722 80.809  162.921 1.00 81.64  ? 40  ARG B CG  1 
ATOM   4166  C  CD  . ARG B 1 82  ? 142.765 80.295  163.892 1.00 82.49  ? 40  ARG B CD  1 
ATOM   4167  N  NE  . ARG B 1 82  ? 142.565 80.832  165.232 1.00 85.10  ? 40  ARG B NE  1 
ATOM   4168  C  CZ  . ARG B 1 82  ? 141.745 80.310  166.134 1.00 86.35  ? 40  ARG B CZ  1 
ATOM   4169  N  NH1 . ARG B 1 82  ? 141.040 79.221  165.878 1.00 80.83  ? 40  ARG B NH1 1 
ATOM   4170  N  NH2 . ARG B 1 82  ? 141.632 80.894  167.323 1.00 86.74  ? 40  ARG B NH2 1 
ATOM   4171  N  N   . PHE B 1 83  ? 138.200 79.238  163.703 1.00 85.70  ? 41  PHE B N   1 
ATOM   4172  C  CA  . PHE B 1 83  ? 136.948 79.889  164.083 1.00 81.10  ? 41  PHE B CA  1 
ATOM   4173  C  C   . PHE B 1 83  ? 137.161 80.606  165.409 1.00 83.55  ? 41  PHE B C   1 
ATOM   4174  O  O   . PHE B 1 83  ? 136.857 80.049  166.474 1.00 82.95  ? 41  PHE B O   1 
ATOM   4175  C  CB  . PHE B 1 83  ? 135.809 78.872  164.201 1.00 76.63  ? 41  PHE B CB  1 
ATOM   4176  C  CG  . PHE B 1 83  ? 135.350 78.298  162.888 1.00 80.28  ? 41  PHE B CG  1 
ATOM   4177  C  CD1 . PHE B 1 83  ? 136.011 78.584  161.708 1.00 81.77  ? 41  PHE B CD1 1 
ATOM   4178  C  CD2 . PHE B 1 83  ? 134.248 77.463  162.842 1.00 81.27  ? 41  PHE B CD2 1 
ATOM   4179  C  CE1 . PHE B 1 83  ? 135.585 78.049  160.511 1.00 85.11  ? 41  PHE B CE1 1 
ATOM   4180  C  CE2 . PHE B 1 83  ? 133.816 76.927  161.648 1.00 83.39  ? 41  PHE B CE2 1 
ATOM   4181  C  CZ  . PHE B 1 83  ? 134.484 77.220  160.481 1.00 85.29  ? 41  PHE B CZ  1 
ATOM   4182  N  N   . PRO B 1 84  ? 137.679 81.833  165.404 1.00 80.62  ? 42  PRO B N   1 
ATOM   4183  C  CA  . PRO B 1 84  ? 137.958 82.520  166.671 1.00 78.09  ? 42  PRO B CA  1 
ATOM   4184  C  C   . PRO B 1 84  ? 136.693 82.755  167.480 1.00 76.31  ? 42  PRO B C   1 
ATOM   4185  O  O   . PRO B 1 84  ? 135.627 83.043  166.935 1.00 76.84  ? 42  PRO B O   1 
ATOM   4186  C  CB  . PRO B 1 84  ? 138.597 83.840  166.226 1.00 73.99  ? 42  PRO B CB  1 
ATOM   4187  C  CG  . PRO B 1 84  ? 138.175 84.015  164.816 1.00 76.24  ? 42  PRO B CG  1 
ATOM   4188  C  CD  . PRO B 1 84  ? 138.063 82.645  164.240 1.00 76.55  ? 42  PRO B CD  1 
ATOM   4189  N  N   . VAL B 1 85  ? 136.826 82.631  168.796 1.00 80.76  ? 43  VAL B N   1 
ATOM   4190  C  CA  . VAL B 1 85  ? 135.722 82.799  169.732 1.00 82.48  ? 43  VAL B CA  1 
ATOM   4191  C  C   . VAL B 1 85  ? 136.009 84.036  170.568 1.00 84.41  ? 43  VAL B C   1 
ATOM   4192  O  O   . VAL B 1 85  ? 137.050 84.117  171.231 1.00 80.22  ? 43  VAL B O   1 
ATOM   4193  C  CB  . VAL B 1 85  ? 135.541 81.562  170.624 1.00 78.41  ? 43  VAL B CB  1 
ATOM   4194  C  CG1 . VAL B 1 85  ? 134.515 81.834  171.706 1.00 79.27  ? 43  VAL B CG1 1 
ATOM   4195  C  CG2 . VAL B 1 85  ? 135.132 80.362  169.791 1.00 75.38  ? 43  VAL B CG2 1 
ATOM   4196  N  N   . VAL B 1 86  ? 135.090 84.997  170.539 1.00 87.35  ? 44  VAL B N   1 
ATOM   4197  C  CA  . VAL B 1 86  ? 135.219 86.243  171.284 1.00 84.04  ? 44  VAL B CA  1 
ATOM   4198  C  C   . VAL B 1 86  ? 134.091 86.310  172.302 1.00 83.66  ? 44  VAL B C   1 
ATOM   4199  O  O   . VAL B 1 86  ? 132.925 86.079  171.961 1.00 82.80  ? 44  VAL B O   1 
ATOM   4200  C  CB  . VAL B 1 86  ? 135.194 87.465  170.353 1.00 78.07  ? 44  VAL B CB  1 
ATOM   4201  C  CG1 . VAL B 1 86  ? 135.254 88.741  171.166 1.00 79.30  ? 44  VAL B CG1 1 
ATOM   4202  C  CG2 . VAL B 1 86  ? 136.351 87.402  169.376 1.00 79.92  ? 44  VAL B CG2 1 
ATOM   4203  N  N   . ASN B 1 87  ? 134.439 86.621  173.547 1.00 88.09  ? 45  ASN B N   1 
ATOM   4204  C  CA  . ASN B 1 87  ? 133.474 86.682  174.635 1.00 87.07  ? 45  ASN B CA  1 
ATOM   4205  C  C   . ASN B 1 87  ? 132.874 88.080  174.704 1.00 87.29  ? 45  ASN B C   1 
ATOM   4206  O  O   . ASN B 1 87  ? 133.601 89.063  174.882 1.00 85.88  ? 45  ASN B O   1 
ATOM   4207  C  CB  . ASN B 1 87  ? 134.141 86.317  175.960 1.00 85.86  ? 45  ASN B CB  1 
ATOM   4208  C  CG  . ASN B 1 87  ? 133.253 86.588  177.159 1.00 87.37  ? 45  ASN B CG  1 
ATOM   4209  O  OD1 . ASN B 1 87  ? 133.143 87.722  177.623 1.00 89.67  ? 45  ASN B OD1 1 
ATOM   4210  N  ND2 . ASN B 1 87  ? 132.619 85.541  177.672 1.00 84.83  ? 45  ASN B ND2 1 
ATOM   4211  N  N   . THR B 1 88  ? 131.555 88.167  174.568 1.00 90.39  ? 46  THR B N   1 
ATOM   4212  C  CA  . THR B 1 88  ? 130.837 89.423  174.698 1.00 87.78  ? 46  THR B CA  1 
ATOM   4213  C  C   . THR B 1 88  ? 130.330 89.577  176.130 1.00 88.49  ? 46  THR B C   1 
ATOM   4214  O  O   . THR B 1 88  ? 130.529 88.712  176.985 1.00 88.64  ? 46  THR B O   1 
ATOM   4215  C  CB  . THR B 1 88  ? 129.684 89.494  173.697 1.00 82.00  ? 46  THR B CB  1 
ATOM   4216  O  OG1 . THR B 1 88  ? 128.543 88.816  174.235 1.00 83.91  ? 46  THR B OG1 1 
ATOM   4217  C  CG2 . THR B 1 88  ? 130.080 88.838  172.391 1.00 83.50  ? 46  THR B CG2 1 
ATOM   4218  N  N   . ALA B 1 89  ? 129.658 90.699  176.393 1.00 89.70  ? 47  ALA B N   1 
ATOM   4219  C  CA  . ALA B 1 89  ? 129.127 90.951  177.726 1.00 87.31  ? 47  ALA B CA  1 
ATOM   4220  C  C   . ALA B 1 89  ? 127.978 90.023  178.088 1.00 89.20  ? 47  ALA B C   1 
ATOM   4221  O  O   . ALA B 1 89  ? 127.574 89.996  179.255 1.00 91.82  ? 47  ALA B O   1 
ATOM   4222  C  CB  . ALA B 1 89  ? 128.671 92.404  177.850 1.00 87.81  ? 47  ALA B CB  1 
ATOM   4223  N  N   . TYR B 1 90  ? 127.442 89.271  177.127 1.00 92.68  ? 48  TYR B N   1 
ATOM   4224  C  CA  . TYR B 1 90  ? 126.349 88.347  177.384 1.00 95.23  ? 48  TYR B CA  1 
ATOM   4225  C  C   . TYR B 1 90  ? 126.728 86.888  177.182 1.00 93.79  ? 48  TYR B C   1 
ATOM   4226  O  O   . TYR B 1 90  ? 125.975 86.008  177.613 1.00 94.64  ? 48  TYR B O   1 
ATOM   4227  C  CB  . TYR B 1 90  ? 125.148 88.682  176.487 1.00 94.23  ? 48  TYR B CB  1 
ATOM   4228  C  CG  . TYR B 1 90  ? 124.702 90.124  176.570 1.00 93.44  ? 48  TYR B CG  1 
ATOM   4229  C  CD1 . TYR B 1 90  ? 125.233 91.084  175.722 1.00 92.50  ? 48  TYR B CD1 1 
ATOM   4230  C  CD2 . TYR B 1 90  ? 123.746 90.523  177.493 1.00 92.70  ? 48  TYR B CD2 1 
ATOM   4231  C  CE1 . TYR B 1 90  ? 124.829 92.401  175.793 1.00 93.10  ? 48  TYR B CE1 1 
ATOM   4232  C  CE2 . TYR B 1 90  ? 123.335 91.838  177.570 1.00 94.67  ? 48  TYR B CE2 1 
ATOM   4233  C  CZ  . TYR B 1 90  ? 123.880 92.773  176.718 1.00 96.14  ? 48  TYR B CZ  1 
ATOM   4234  O  OH  . TYR B 1 90  ? 123.476 94.085  176.789 1.00 96.25  ? 48  TYR B OH  1 
ATOM   4235  N  N   . GLY B 1 91  ? 127.861 86.605  176.549 1.00 94.71  ? 49  GLY B N   1 
ATOM   4236  C  CA  . GLY B 1 91  ? 128.242 85.228  176.300 1.00 95.34  ? 49  GLY B CA  1 
ATOM   4237  C  C   . GLY B 1 91  ? 129.409 85.159  175.337 1.00 95.50  ? 49  GLY B C   1 
ATOM   4238  O  O   . GLY B 1 91  ? 130.165 86.120  175.187 1.00 96.17  ? 49  GLY B O   1 
ATOM   4239  N  N   . ARG B 1 92  ? 129.542 84.006  174.692 1.00 95.10  ? 50  ARG B N   1 
ATOM   4240  C  CA  . ARG B 1 92  ? 130.615 83.746  173.745 1.00 94.14  ? 50  ARG B CA  1 
ATOM   4241  C  C   . ARG B 1 92  ? 130.020 83.397  172.391 1.00 97.81  ? 50  ARG B C   1 
ATOM   4242  O  O   . ARG B 1 92  ? 129.062 82.625  172.309 1.00 100.11 ? 50  ARG B O   1 
ATOM   4243  C  CB  . ARG B 1 92  ? 131.512 82.606  174.232 1.00 96.81  ? 50  ARG B CB  1 
ATOM   4244  C  CG  . ARG B 1 92  ? 132.797 83.062  174.900 1.00 99.35  ? 50  ARG B CG  1 
ATOM   4245  C  CD  . ARG B 1 92  ? 133.620 81.892  175.424 1.00 99.83  ? 50  ARG B CD  1 
ATOM   4246  N  NE  . ARG B 1 92  ? 133.257 81.526  176.788 1.00 100.71 ? 50  ARG B NE  1 
ATOM   4247  C  CZ  . ARG B 1 92  ? 132.275 80.696  177.117 1.00 99.05  ? 50  ARG B CZ  1 
ATOM   4248  N  NH1 . ARG B 1 92  ? 131.537 80.098  176.199 1.00 97.43  ? 50  ARG B NH1 1 
ATOM   4249  N  NH2 . ARG B 1 92  ? 132.032 80.456  178.402 1.00 98.23  ? 50  ARG B NH2 1 
ATOM   4250  N  N   . VAL B 1 93  ? 130.587 83.969  171.333 1.00 87.20  ? 51  VAL B N   1 
ATOM   4251  C  CA  . VAL B 1 93  ? 130.122 83.732  169.973 1.00 86.38  ? 51  VAL B CA  1 
ATOM   4252  C  C   . VAL B 1 93  ? 131.286 83.215  169.140 1.00 85.79  ? 51  VAL B C   1 
ATOM   4253  O  O   . VAL B 1 93  ? 132.449 83.549  169.386 1.00 85.75  ? 51  VAL B O   1 
ATOM   4254  C  CB  . VAL B 1 93  ? 129.515 85.003  169.339 1.00 83.73  ? 51  VAL B CB  1 
ATOM   4255  C  CG1 . VAL B 1 93  ? 128.335 85.489  170.156 1.00 82.34  ? 51  VAL B CG1 1 
ATOM   4256  C  CG2 . VAL B 1 93  ? 130.562 86.092  169.221 1.00 83.55  ? 51  VAL B CG2 1 
ATOM   4257  N  N   . ARG B 1 94  ? 130.964 82.386  168.152 1.00 84.30  ? 52  ARG B N   1 
ATOM   4258  C  CA  . ARG B 1 94  ? 131.958 81.793  167.267 1.00 85.29  ? 52  ARG B CA  1 
ATOM   4259  C  C   . ARG B 1 94  ? 131.820 82.383  165.871 1.00 84.18  ? 52  ARG B C   1 
ATOM   4260  O  O   . ARG B 1 94  ? 130.725 82.388  165.301 1.00 84.90  ? 52  ARG B O   1 
ATOM   4261  C  CB  . ARG B 1 94  ? 131.805 80.272  167.208 1.00 84.74  ? 52  ARG B CB  1 
ATOM   4262  C  CG  . ARG B 1 94  ? 133.077 79.540  166.811 1.00 82.33  ? 52  ARG B CG  1 
ATOM   4263  C  CD  . ARG B 1 94  ? 132.787 78.157  166.236 1.00 82.17  ? 52  ARG B CD  1 
ATOM   4264  N  NE  . ARG B 1 94  ? 131.734 77.435  166.942 1.00 85.54  ? 52  ARG B NE  1 
ATOM   4265  C  CZ  . ARG B 1 94  ? 131.792 77.051  168.210 1.00 86.16  ? 52  ARG B CZ  1 
ATOM   4266  N  NH1 . ARG B 1 94  ? 132.860 77.279  168.956 1.00 86.05  ? 52  ARG B NH1 1 
ATOM   4267  N  NH2 . ARG B 1 94  ? 130.755 76.409  168.740 1.00 83.16  ? 52  ARG B NH2 1 
ATOM   4268  N  N   . GLY B 1 95  ? 132.931 82.875  165.322 1.00 77.63  ? 53  GLY B N   1 
ATOM   4269  C  CA  . GLY B 1 95  ? 132.962 83.441  164.001 1.00 75.89  ? 53  GLY B CA  1 
ATOM   4270  C  C   . GLY B 1 95  ? 133.641 82.539  162.992 1.00 77.61  ? 53  GLY B C   1 
ATOM   4271  O  O   . GLY B 1 95  ? 133.765 81.322  163.180 1.00 84.22  ? 53  GLY B O   1 
ATOM   4272  N  N   . VAL B 1 96  ? 134.081 83.145  161.893 1.00 76.88  ? 54  VAL B N   1 
ATOM   4273  C  CA  . VAL B 1 96  ? 134.822 82.465  160.845 1.00 79.04  ? 54  VAL B CA  1 
ATOM   4274  C  C   . VAL B 1 96  ? 136.054 83.298  160.511 1.00 79.56  ? 54  VAL B C   1 
ATOM   4275  O  O   . VAL B 1 96  ? 136.312 84.328  161.128 1.00 83.18  ? 54  VAL B O   1 
ATOM   4276  C  CB  . VAL B 1 96  ? 133.967 82.219  159.587 1.00 79.58  ? 54  VAL B CB  1 
ATOM   4277  C  CG1 . VAL B 1 96  ? 132.979 81.103  159.838 1.00 80.48  ? 54  VAL B CG1 1 
ATOM   4278  C  CG2 . VAL B 1 96  ? 133.245 83.487  159.189 1.00 79.36  ? 54  VAL B CG2 1 
ATOM   4279  N  N   . ARG B 1 97  ? 136.825 82.834  159.535 1.00 86.88  ? 55  ARG B N   1 
ATOM   4280  C  CA  . ARG B 1 97  ? 138.037 83.529  159.112 1.00 89.31  ? 55  ARG B CA  1 
ATOM   4281  C  C   . ARG B 1 97  ? 138.116 83.568  157.591 1.00 90.51  ? 55  ARG B C   1 
ATOM   4282  O  O   . ARG B 1 97  ? 139.128 83.208  156.988 1.00 94.13  ? 55  ARG B O   1 
ATOM   4283  C  CB  . ARG B 1 97  ? 139.284 82.884  159.708 1.00 88.60  ? 55  ARG B CB  1 
ATOM   4284  C  CG  . ARG B 1 97  ? 140.475 83.823  159.779 1.00 88.41  ? 55  ARG B CG  1 
ATOM   4285  C  CD  . ARG B 1 97  ? 141.781 83.067  159.653 1.00 93.07  ? 55  ARG B CD  1 
ATOM   4286  N  NE  . ARG B 1 97  ? 142.913 83.962  159.448 1.00 94.75  ? 55  ARG B NE  1 
ATOM   4287  C  CZ  . ARG B 1 97  ? 143.515 84.641  160.414 1.00 95.00  ? 55  ARG B CZ  1 
ATOM   4288  N  NH1 . ARG B 1 97  ? 143.107 84.567  161.671 1.00 93.53  ? 55  ARG B NH1 1 
ATOM   4289  N  NH2 . ARG B 1 97  ? 144.554 85.415  160.113 1.00 93.50  ? 55  ARG B NH2 1 
ATOM   4290  N  N   . ARG B 1 98  ? 137.030 83.994  156.951 1.00 86.29  ? 56  ARG B N   1 
ATOM   4291  C  CA  . ARG B 1 98  ? 136.987 84.031  155.497 1.00 85.95  ? 56  ARG B CA  1 
ATOM   4292  C  C   . ARG B 1 98  ? 138.100 84.907  154.938 1.00 87.13  ? 56  ARG B C   1 
ATOM   4293  O  O   . ARG B 1 98  ? 138.380 85.991  155.454 1.00 87.82  ? 56  ARG B O   1 
ATOM   4294  C  CB  . ARG B 1 98  ? 135.631 84.546  155.024 1.00 85.30  ? 56  ARG B CB  1 
ATOM   4295  C  CG  . ARG B 1 98  ? 134.510 83.539  155.170 1.00 87.41  ? 56  ARG B CG  1 
ATOM   4296  C  CD  . ARG B 1 98  ? 134.397 82.663  153.938 1.00 88.66  ? 56  ARG B CD  1 
ATOM   4297  N  NE  . ARG B 1 98  ? 133.068 82.078  153.814 1.00 90.94  ? 56  ARG B NE  1 
ATOM   4298  C  CZ  . ARG B 1 98  ? 132.021 82.701  153.291 1.00 94.01  ? 56  ARG B CZ  1 
ATOM   4299  N  NH1 . ARG B 1 98  ? 132.117 83.930  152.810 1.00 90.96  ? 56  ARG B NH1 1 
ATOM   4300  N  NH2 . ARG B 1 98  ? 130.849 82.075  153.250 1.00 93.44  ? 56  ARG B NH2 1 
ATOM   4301  N  N   . GLU B 1 99  ? 138.742 84.421  153.880 1.00 96.87  ? 57  GLU B N   1 
ATOM   4302  C  CA  . GLU B 1 99  ? 139.803 85.138  153.189 1.00 96.07  ? 57  GLU B CA  1 
ATOM   4303  C  C   . GLU B 1 99  ? 139.302 85.589  151.825 1.00 97.85  ? 57  GLU B C   1 
ATOM   4304  O  O   . GLU B 1 99  ? 138.575 84.857  151.147 1.00 97.35  ? 57  GLU B O   1 
ATOM   4305  C  CB  . GLU B 1 99  ? 141.048 84.264  153.030 1.00 95.01  ? 57  GLU B CB  1 
ATOM   4306  C  CG  . GLU B 1 99  ? 142.316 85.043  152.721 1.00 95.47  ? 57  GLU B CG  1 
ATOM   4307  C  CD  . GLU B 1 99  ? 143.551 84.162  152.695 1.00 99.17  ? 57  GLU B CD  1 
ATOM   4308  O  OE1 . GLU B 1 99  ? 143.398 82.923  152.676 1.00 99.82  ? 57  GLU B OE1 1 
ATOM   4309  O  OE2 . GLU B 1 99  ? 144.674 84.708  152.693 1.00 97.26  ? 57  GLU B OE2 1 
ATOM   4310  N  N   . LEU B 1 100 ? 139.693 86.794  151.428 1.00 98.02  ? 58  LEU B N   1 
ATOM   4311  C  CA  . LEU B 1 100 ? 139.121 87.416  150.246 1.00 98.14  ? 58  LEU B CA  1 
ATOM   4312  C  C   . LEU B 1 100 ? 139.782 86.898  148.972 1.00 99.58  ? 58  LEU B C   1 
ATOM   4313  O  O   . LEU B 1 100 ? 140.897 86.370  148.984 1.00 98.42  ? 58  LEU B O   1 
ATOM   4314  C  CB  . LEU B 1 100 ? 139.254 88.935  150.326 1.00 95.86  ? 58  LEU B CB  1 
ATOM   4315  C  CG  . LEU B 1 100 ? 138.844 89.523  151.673 1.00 94.52  ? 58  LEU B CG  1 
ATOM   4316  C  CD1 . LEU B 1 100 ? 138.963 91.028  151.649 1.00 91.77  ? 58  LEU B CD1 1 
ATOM   4317  C  CD2 . LEU B 1 100 ? 137.432 89.101  152.017 1.00 97.54  ? 58  LEU B CD2 1 
ATOM   4318  N  N   . ASN B 1 101 ? 139.063 87.060  147.858 1.00 104.36 ? 59  ASN B N   1 
ATOM   4319  C  CA  . ASN B 1 101 ? 139.582 86.635  146.563 1.00 102.67 ? 59  ASN B CA  1 
ATOM   4320  C  C   . ASN B 1 101 ? 140.808 87.446  146.162 1.00 104.23 ? 59  ASN B C   1 
ATOM   4321  O  O   . ASN B 1 101 ? 141.764 86.899  145.601 1.00 104.97 ? 59  ASN B O   1 
ATOM   4322  C  CB  . ASN B 1 101 ? 138.491 86.750  145.499 1.00 99.86  ? 59  ASN B CB  1 
ATOM   4323  N  N   . ASN B 1 102 ? 140.798 88.747  146.437 1.00 100.15 ? 60  ASN B N   1 
ATOM   4324  C  CA  . ASN B 1 102 ? 141.930 89.589  146.087 1.00 100.28 ? 60  ASN B CA  1 
ATOM   4325  C  C   . ASN B 1 102 ? 143.151 89.218  146.925 1.00 100.10 ? 60  ASN B C   1 
ATOM   4326  O  O   . ASN B 1 102 ? 143.053 88.566  147.968 1.00 97.21  ? 60  ASN B O   1 
ATOM   4327  C  CB  . ASN B 1 102 ? 141.582 91.066  146.276 1.00 98.77  ? 60  ASN B CB  1 
ATOM   4328  C  CG  . ASN B 1 102 ? 142.490 91.985  145.483 1.00 96.61  ? 60  ASN B CG  1 
ATOM   4329  O  OD1 . ASN B 1 102 ? 143.704 91.998  145.680 1.00 95.67  ? 60  ASN B OD1 1 
ATOM   4330  N  ND2 . ASN B 1 102 ? 141.904 92.758  144.577 1.00 95.22  ? 60  ASN B ND2 1 
ATOM   4331  N  N   . GLU B 1 103 ? 144.318 89.641  146.445 1.00 105.71 ? 61  GLU B N   1 
ATOM   4332  C  CA  . GLU B 1 103 ? 145.584 89.258  147.055 1.00 104.25 ? 61  GLU B CA  1 
ATOM   4333  C  C   . GLU B 1 103 ? 146.087 90.286  148.061 1.00 103.58 ? 61  GLU B C   1 
ATOM   4334  O  O   . GLU B 1 103 ? 146.628 89.911  149.106 1.00 102.92 ? 61  GLU B O   1 
ATOM   4335  C  CB  . GLU B 1 103 ? 146.639 89.040  145.967 1.00 105.53 ? 61  GLU B CB  1 
ATOM   4336  C  CG  . GLU B 1 103 ? 146.094 88.408  144.696 1.00 105.93 ? 61  GLU B CG  1 
ATOM   4337  C  CD  . GLU B 1 103 ? 145.661 89.439  143.671 1.00 106.35 ? 61  GLU B CD  1 
ATOM   4338  O  OE1 . GLU B 1 103 ? 146.292 90.515  143.606 1.00 106.56 ? 61  GLU B OE1 1 
ATOM   4339  O  OE2 . GLU B 1 103 ? 144.689 89.175  142.932 1.00 104.60 ? 61  GLU B OE2 1 
ATOM   4340  N  N   . ILE B 1 104 ? 145.929 91.577  147.764 1.00 97.97  ? 62  ILE B N   1 
ATOM   4341  C  CA  . ILE B 1 104 ? 146.449 92.608  148.657 1.00 99.48  ? 62  ILE B CA  1 
ATOM   4342  C  C   . ILE B 1 104 ? 145.664 92.638  149.964 1.00 102.62 ? 62  ILE B C   1 
ATOM   4343  O  O   . ILE B 1 104 ? 146.235 92.860  151.039 1.00 103.81 ? 62  ILE B O   1 
ATOM   4344  C  CB  . ILE B 1 104 ? 146.444 93.979  147.957 1.00 98.53  ? 62  ILE B CB  1 
ATOM   4345  C  CG1 . ILE B 1 104 ? 145.033 94.355  147.502 1.00 100.13 ? 62  ILE B CG1 1 
ATOM   4346  C  CG2 . ILE B 1 104 ? 147.395 93.970  146.773 1.00 99.93  ? 62  ILE B CG2 1 
ATOM   4347  C  CD1 . ILE B 1 104 ? 144.841 95.837  147.268 1.00 97.80  ? 62  ILE B CD1 1 
ATOM   4348  N  N   . LEU B 1 105 ? 144.355 92.417  149.899 1.00 91.90  ? 63  LEU B N   1 
ATOM   4349  C  CA  . LEU B 1 105 ? 143.519 92.507  151.087 1.00 89.63  ? 63  LEU B CA  1 
ATOM   4350  C  C   . LEU B 1 105 ? 143.714 91.289  151.981 1.00 91.78  ? 63  LEU B C   1 
ATOM   4351  O  O   . LEU B 1 105 ? 143.732 90.149  151.511 1.00 90.32  ? 63  LEU B O   1 
ATOM   4352  C  CB  . LEU B 1 105 ? 142.051 92.631  150.690 1.00 86.32  ? 63  LEU B CB  1 
ATOM   4353  C  CG  . LEU B 1 105 ? 141.754 93.508  149.476 1.00 83.84  ? 63  LEU B CG  1 
ATOM   4354  C  CD1 . LEU B 1 105 ? 140.346 93.263  148.979 1.00 86.06  ? 63  LEU B CD1 1 
ATOM   4355  C  CD2 . LEU B 1 105 ? 141.950 94.965  149.823 1.00 85.69  ? 63  LEU B CD2 1 
ATOM   4356  N  N   . GLY B 1 106 ? 143.855 91.537  153.282 1.00 86.52  ? 64  GLY B N   1 
ATOM   4357  C  CA  . GLY B 1 106 ? 143.997 90.466  154.236 1.00 86.15  ? 64  GLY B CA  1 
ATOM   4358  C  C   . GLY B 1 106 ? 142.671 89.819  154.567 1.00 89.43  ? 64  GLY B C   1 
ATOM   4359  O  O   . GLY B 1 106 ? 141.600 90.232  154.105 1.00 88.82  ? 64  GLY B O   1 
ATOM   4360  N  N   . PRO B 1 107 ? 142.730 88.775  155.386 1.00 95.16  ? 65  PRO B N   1 
ATOM   4361  C  CA  . PRO B 1 107 ? 141.512 88.065  155.779 1.00 92.51  ? 65  PRO B CA  1 
ATOM   4362  C  C   . PRO B 1 107 ? 140.755 88.807  156.871 1.00 93.10  ? 65  PRO B C   1 
ATOM   4363  O  O   . PRO B 1 107 ? 141.303 89.639  157.596 1.00 92.67  ? 65  PRO B O   1 
ATOM   4364  C  CB  . PRO B 1 107 ? 142.038 86.715  156.299 1.00 88.74  ? 65  PRO B CB  1 
ATOM   4365  C  CG  . PRO B 1 107 ? 143.545 86.755  156.122 1.00 92.59  ? 65  PRO B CG  1 
ATOM   4366  C  CD  . PRO B 1 107 ? 143.920 88.193  156.019 1.00 92.62  ? 65  PRO B CD  1 
ATOM   4367  N  N   . VAL B 1 108 ? 139.468 88.484  156.974 1.00 85.38  ? 66  VAL B N   1 
ATOM   4368  C  CA  . VAL B 1 108 ? 138.582 89.091  157.955 1.00 79.15  ? 66  VAL B CA  1 
ATOM   4369  C  C   . VAL B 1 108 ? 137.958 87.988  158.801 1.00 79.12  ? 66  VAL B C   1 
ATOM   4370  O  O   . VAL B 1 108 ? 138.062 86.802  158.496 1.00 84.04  ? 66  VAL B O   1 
ATOM   4371  C  CB  . VAL B 1 108 ? 137.486 89.948  157.304 1.00 74.66  ? 66  VAL B CB  1 
ATOM   4372  C  CG1 . VAL B 1 108 ? 138.098 90.970  156.372 1.00 77.82  ? 66  VAL B CG1 1 
ATOM   4373  C  CG2 . VAL B 1 108 ? 136.500 89.063  156.579 1.00 75.94  ? 66  VAL B CG2 1 
ATOM   4374  N  N   . VAL B 1 109 ? 137.299 88.404  159.877 1.00 69.85  ? 67  VAL B N   1 
ATOM   4375  C  CA  . VAL B 1 109 ? 136.600 87.507  160.785 1.00 70.67  ? 67  VAL B CA  1 
ATOM   4376  C  C   . VAL B 1 109 ? 135.179 88.029  160.929 1.00 74.47  ? 67  VAL B C   1 
ATOM   4377  O  O   . VAL B 1 109 ? 134.976 89.157  161.391 1.00 83.23  ? 67  VAL B O   1 
ATOM   4378  C  CB  . VAL B 1 109 ? 137.296 87.428  162.153 1.00 72.32  ? 67  VAL B CB  1 
ATOM   4379  C  CG1 . VAL B 1 109 ? 136.415 86.731  163.161 1.00 76.14  ? 67  VAL B CG1 1 
ATOM   4380  C  CG2 . VAL B 1 109 ? 138.629 86.721  162.026 1.00 76.00  ? 67  VAL B CG2 1 
ATOM   4381  N  N   . GLN B 1 110 ? 134.202 87.221  160.534 1.00 66.54  ? 68  GLN B N   1 
ATOM   4382  C  CA  . GLN B 1 110 ? 132.813 87.652  160.452 1.00 67.19  ? 68  GLN B CA  1 
ATOM   4383  C  C   . GLN B 1 110 ? 131.995 86.960  161.531 1.00 70.30  ? 68  GLN B C   1 
ATOM   4384  O  O   . GLN B 1 110 ? 131.906 85.729  161.552 1.00 80.83  ? 68  GLN B O   1 
ATOM   4385  C  CB  . GLN B 1 110 ? 132.237 87.348  159.071 1.00 68.25  ? 68  GLN B CB  1 
ATOM   4386  C  CG  . GLN B 1 110 ? 133.274 87.329  157.967 1.00 70.57  ? 68  GLN B CG  1 
ATOM   4387  C  CD  . GLN B 1 110 ? 132.682 86.975  156.622 1.00 72.27  ? 68  GLN B CD  1 
ATOM   4388  O  OE1 . GLN B 1 110 ? 131.646 86.318  156.541 1.00 67.83  ? 68  GLN B OE1 1 
ATOM   4389  N  NE2 . GLN B 1 110 ? 133.335 87.414  155.554 1.00 74.08  ? 68  GLN B NE2 1 
ATOM   4390  N  N   . PHE B 1 111 ? 131.408 87.750  162.425 1.00 64.77  ? 69  PHE B N   1 
ATOM   4391  C  CA  . PHE B 1 111 ? 130.477 87.240  163.432 1.00 67.45  ? 69  PHE B CA  1 
ATOM   4392  C  C   . PHE B 1 111 ? 129.034 87.461  162.983 1.00 71.76  ? 69  PHE B C   1 
ATOM   4393  O  O   . PHE B 1 111 ? 128.239 88.107  163.660 1.00 74.24  ? 69  PHE B O   1 
ATOM   4394  C  CB  . PHE B 1 111 ? 130.734 87.906  164.780 1.00 64.22  ? 69  PHE B CB  1 
ATOM   4395  C  CG  . PHE B 1 111 ? 132.145 87.781  165.265 1.00 63.58  ? 69  PHE B CG  1 
ATOM   4396  C  CD1 . PHE B 1 111 ? 133.115 88.672  164.852 1.00 65.28  ? 69  PHE B CD1 1 
ATOM   4397  C  CD2 . PHE B 1 111 ? 132.499 86.780  166.146 1.00 71.13  ? 69  PHE B CD2 1 
ATOM   4398  C  CE1 . PHE B 1 111 ? 134.407 88.562  165.302 1.00 69.29  ? 69  PHE B CE1 1 
ATOM   4399  C  CE2 . PHE B 1 111 ? 133.793 86.665  166.598 1.00 75.40  ? 69  PHE B CE2 1 
ATOM   4400  C  CZ  . PHE B 1 111 ? 134.748 87.556  166.175 1.00 75.05  ? 69  PHE B CZ  1 
ATOM   4401  N  N   . LEU B 1 112 ? 128.699 86.911  161.820 1.00 69.81  ? 70  LEU B N   1 
ATOM   4402  C  CA  . LEU B 1 112 ? 127.384 87.126  161.225 1.00 66.07  ? 70  LEU B CA  1 
ATOM   4403  C  C   . LEU B 1 112 ? 126.304 86.501  162.099 1.00 68.65  ? 70  LEU B C   1 
ATOM   4404  O  O   . LEU B 1 112 ? 126.243 85.277  162.239 1.00 70.66  ? 70  LEU B O   1 
ATOM   4405  C  CB  . LEU B 1 112 ? 127.342 86.534  159.822 1.00 64.16  ? 70  LEU B CB  1 
ATOM   4406  C  CG  . LEU B 1 112 ? 128.558 86.785  158.937 1.00 68.02  ? 70  LEU B CG  1 
ATOM   4407  C  CD1 . LEU B 1 112 ? 128.756 85.632  157.973 1.00 72.55  ? 70  LEU B CD1 1 
ATOM   4408  C  CD2 . LEU B 1 112 ? 128.389 88.081  158.181 1.00 69.58  ? 70  LEU B CD2 1 
ATOM   4409  N  N   . GLY B 1 113 ? 125.449 87.333  162.686 1.00 63.78  ? 71  GLY B N   1 
ATOM   4410  C  CA  . GLY B 1 113 ? 124.281 86.830  163.379 1.00 65.86  ? 71  GLY B CA  1 
ATOM   4411  C  C   . GLY B 1 113 ? 124.188 87.151  164.856 1.00 67.71  ? 71  GLY B C   1 
ATOM   4412  O  O   . GLY B 1 113 ? 123.329 86.602  165.550 1.00 72.21  ? 71  GLY B O   1 
ATOM   4413  N  N   . VAL B 1 114 ? 125.046 88.030  165.353 1.00 59.91  ? 72  VAL B N   1 
ATOM   4414  C  CA  . VAL B 1 114 ? 125.012 88.369  166.781 1.00 59.92  ? 72  VAL B CA  1 
ATOM   4415  C  C   . VAL B 1 114 ? 123.729 89.133  167.087 1.00 65.45  ? 72  VAL B C   1 
ATOM   4416  O  O   . VAL B 1 114 ? 123.392 90.082  166.361 1.00 74.42  ? 72  VAL B O   1 
ATOM   4417  C  CB  . VAL B 1 114 ? 126.242 89.191  167.161 1.00 57.32  ? 72  VAL B CB  1 
ATOM   4418  C  CG1 . VAL B 1 114 ? 126.256 89.454  168.651 1.00 58.05  ? 72  VAL B CG1 1 
ATOM   4419  C  CG2 . VAL B 1 114 ? 127.506 88.475  166.742 1.00 62.87  ? 72  VAL B CG2 1 
ATOM   4420  N  N   . PRO B 1 115 ? 122.980 88.763  168.120 1.00 71.13  ? 73  PRO B N   1 
ATOM   4421  C  CA  . PRO B 1 115 ? 121.793 89.535  168.491 1.00 69.76  ? 73  PRO B CA  1 
ATOM   4422  C  C   . PRO B 1 115 ? 122.156 90.760  169.314 1.00 72.02  ? 73  PRO B C   1 
ATOM   4423  O  O   . PRO B 1 115 ? 123.235 90.854  169.899 1.00 75.67  ? 73  PRO B O   1 
ATOM   4424  C  CB  . PRO B 1 115 ? 120.979 88.542  169.323 1.00 68.11  ? 73  PRO B CB  1 
ATOM   4425  C  CG  . PRO B 1 115 ? 122.011 87.689  169.962 1.00 69.98  ? 73  PRO B CG  1 
ATOM   4426  C  CD  . PRO B 1 115 ? 123.143 87.570  168.969 1.00 72.92  ? 73  PRO B CD  1 
ATOM   4427  N  N   . TYR B 1 116 ? 121.223 91.711  169.352 1.00 66.71  ? 74  TYR B N   1 
ATOM   4428  C  CA  . TYR B 1 116 ? 121.403 92.895  170.179 1.00 66.34  ? 74  TYR B CA  1 
ATOM   4429  C  C   . TYR B 1 116 ? 120.158 93.309  170.950 1.00 71.34  ? 74  TYR B C   1 
ATOM   4430  O  O   . TYR B 1 116 ? 120.217 94.303  171.680 1.00 73.82  ? 74  TYR B O   1 
ATOM   4431  C  CB  . TYR B 1 116 ? 121.891 94.078  169.329 1.00 59.66  ? 74  TYR B CB  1 
ATOM   4432  C  CG  . TYR B 1 116 ? 120.945 94.511  168.235 1.00 65.18  ? 74  TYR B CG  1 
ATOM   4433  C  CD1 . TYR B 1 116 ? 121.035 93.974  166.964 1.00 66.04  ? 74  TYR B CD1 1 
ATOM   4434  C  CD2 . TYR B 1 116 ? 119.977 95.475  168.468 1.00 66.59  ? 74  TYR B CD2 1 
ATOM   4435  C  CE1 . TYR B 1 116 ? 120.183 94.373  165.962 1.00 65.36  ? 74  TYR B CE1 1 
ATOM   4436  C  CE2 . TYR B 1 116 ? 119.122 95.878  167.471 1.00 66.56  ? 74  TYR B CE2 1 
ATOM   4437  C  CZ  . TYR B 1 116 ? 119.230 95.324  166.221 1.00 64.32  ? 74  TYR B CZ  1 
ATOM   4438  O  OH  . TYR B 1 116 ? 118.378 95.720  165.220 1.00 67.96  ? 74  TYR B OH  1 
ATOM   4439  N  N   . ALA B 1 117 ? 119.045 92.592  170.824 1.00 72.91  ? 75  ALA B N   1 
ATOM   4440  C  CA  . ALA B 1 117 ? 117.845 92.920  171.577 1.00 71.54  ? 75  ALA B CA  1 
ATOM   4441  C  C   . ALA B 1 117 ? 116.945 91.695  171.630 1.00 77.31  ? 75  ALA B C   1 
ATOM   4442  O  O   . ALA B 1 117 ? 117.050 90.791  170.797 1.00 79.34  ? 75  ALA B O   1 
ATOM   4443  C  CB  . ALA B 1 117 ? 117.101 94.108  170.962 1.00 73.93  ? 75  ALA B CB  1 
ATOM   4444  N  N   . THR B 1 118 ? 116.059 91.678  172.621 1.00 90.09  ? 76  THR B N   1 
ATOM   4445  C  CA  . THR B 1 118 ? 115.102 90.588  172.729 1.00 90.52  ? 76  THR B CA  1 
ATOM   4446  C  C   . THR B 1 118 ? 114.091 90.670  171.590 1.00 89.00  ? 76  THR B C   1 
ATOM   4447  O  O   . THR B 1 118 ? 113.598 91.756  171.272 1.00 89.09  ? 76  THR B O   1 
ATOM   4448  C  CB  . THR B 1 118 ? 114.369 90.622  174.067 1.00 90.26  ? 76  THR B CB  1 
ATOM   4449  O  OG1 . THR B 1 118 ? 113.327 91.603  174.017 1.00 93.27  ? 76  THR B OG1 1 
ATOM   4450  C  CG2 . THR B 1 118 ? 115.321 90.956  175.188 1.00 87.92  ? 76  THR B CG2 1 
ATOM   4451  N  N   . PRO B 1 119 ? 113.758 89.546  170.967 1.00 86.30  ? 77  PRO B N   1 
ATOM   4452  C  CA  . PRO B 1 119 ? 112.868 89.568  169.807 1.00 87.48  ? 77  PRO B CA  1 
ATOM   4453  C  C   . PRO B 1 119 ? 111.469 90.005  170.199 1.00 93.26  ? 77  PRO B C   1 
ATOM   4454  O  O   . PRO B 1 119 ? 110.925 89.546  171.213 1.00 95.33  ? 77  PRO B O   1 
ATOM   4455  C  CB  . PRO B 1 119 ? 112.880 88.109  169.327 1.00 88.96  ? 77  PRO B CB  1 
ATOM   4456  C  CG  . PRO B 1 119 ? 114.041 87.466  170.018 1.00 88.35  ? 77  PRO B CG  1 
ATOM   4457  C  CD  . PRO B 1 119 ? 114.195 88.184  171.305 1.00 87.95  ? 77  PRO B CD  1 
ATOM   4458  N  N   . PRO B 1 120 ? 110.852 90.896  169.420 1.00 87.76  ? 78  PRO B N   1 
ATOM   4459  C  CA  . PRO B 1 120 ? 109.490 91.388  169.716 1.00 83.34  ? 78  PRO B CA  1 
ATOM   4460  C  C   . PRO B 1 120 ? 108.371 90.562  169.079 1.00 86.17  ? 78  PRO B C   1 
ATOM   4461  O  O   . PRO B 1 120 ? 107.717 90.956  168.114 1.00 87.73  ? 78  PRO B O   1 
ATOM   4462  C  CB  . PRO B 1 120 ? 109.524 92.807  169.152 1.00 79.99  ? 78  PRO B CB  1 
ATOM   4463  C  CG  . PRO B 1 120 ? 110.441 92.693  167.971 1.00 77.15  ? 78  PRO B CG  1 
ATOM   4464  C  CD  . PRO B 1 120 ? 111.453 91.613  168.281 1.00 81.14  ? 78  PRO B CD  1 
ATOM   4465  N  N   . LEU B 1 121 ? 108.129 89.376  169.636 1.00 87.24  ? 79  LEU B N   1 
ATOM   4466  C  CA  . LEU B 1 121 ? 107.122 88.471  169.086 1.00 86.09  ? 79  LEU B CA  1 
ATOM   4467  C  C   . LEU B 1 121 ? 105.727 88.741  169.647 1.00 86.39  ? 79  LEU B C   1 
ATOM   4468  O  O   . LEU B 1 121 ? 104.783 88.985  168.890 1.00 85.28  ? 79  LEU B O   1 
ATOM   4469  C  CB  . LEU B 1 121 ? 107.524 87.014  169.339 1.00 82.86  ? 79  LEU B CB  1 
ATOM   4470  C  CG  . LEU B 1 121 ? 108.406 86.331  168.293 1.00 83.45  ? 79  LEU B CG  1 
ATOM   4471  C  CD1 . LEU B 1 121 ? 107.775 86.426  166.918 1.00 84.63  ? 79  LEU B CD1 1 
ATOM   4472  C  CD2 . LEU B 1 121 ? 109.789 86.927  168.273 1.00 80.56  ? 79  LEU B CD2 1 
ATOM   4473  N  N   . GLY B 1 122 ? 105.582 88.693  170.966 1.00 91.82  ? 80  GLY B N   1 
ATOM   4474  C  CA  . GLY B 1 122 ? 104.269 88.798  171.570 1.00 93.00  ? 80  GLY B CA  1 
ATOM   4475  C  C   . GLY B 1 122 ? 103.887 90.202  171.982 1.00 92.16  ? 80  GLY B C   1 
ATOM   4476  O  O   . GLY B 1 122 ? 103.713 91.081  171.134 1.00 90.13  ? 80  GLY B O   1 
ATOM   4477  N  N   . ALA B 1 123 ? 103.744 90.421  173.290 1.00 94.72  ? 81  ALA B N   1 
ATOM   4478  C  CA  . ALA B 1 123 ? 103.406 91.742  173.801 1.00 93.70  ? 81  ALA B CA  1 
ATOM   4479  C  C   . ALA B 1 123 ? 104.536 92.745  173.632 1.00 92.95  ? 81  ALA B C   1 
ATOM   4480  O  O   . ALA B 1 123 ? 104.303 93.946  173.798 1.00 90.63  ? 81  ALA B O   1 
ATOM   4481  C  CB  . ALA B 1 123 ? 103.014 91.652  175.276 1.00 94.45  ? 81  ALA B CB  1 
ATOM   4482  N  N   . ARG B 1 124 ? 105.747 92.289  173.317 1.00 95.53  ? 82  ARG B N   1 
ATOM   4483  C  CA  . ARG B 1 124 ? 106.848 93.202  173.052 1.00 94.86  ? 82  ARG B CA  1 
ATOM   4484  C  C   . ARG B 1 124 ? 106.785 93.811  171.661 1.00 96.53  ? 82  ARG B C   1 
ATOM   4485  O  O   . ARG B 1 124 ? 107.572 94.716  171.365 1.00 95.53  ? 82  ARG B O   1 
ATOM   4486  C  CB  . ARG B 1 124 ? 108.188 92.489  173.241 1.00 93.71  ? 82  ARG B CB  1 
ATOM   4487  C  CG  . ARG B 1 124 ? 108.251 91.624  174.481 1.00 95.53  ? 82  ARG B CG  1 
ATOM   4488  C  CD  . ARG B 1 124 ? 109.399 90.640  174.408 1.00 94.78  ? 82  ARG B CD  1 
ATOM   4489  N  NE  . ARG B 1 124 ? 110.641 91.236  174.883 1.00 99.11  ? 82  ARG B NE  1 
ATOM   4490  C  CZ  . ARG B 1 124 ? 111.080 91.157  176.131 1.00 98.20  ? 82  ARG B CZ  1 
ATOM   4491  N  NH1 . ARG B 1 124 ? 110.397 90.515  177.065 1.00 95.06  ? 82  ARG B NH1 1 
ATOM   4492  N  NH2 . ARG B 1 124 ? 112.232 91.740  176.452 1.00 96.09  ? 82  ARG B NH2 1 
ATOM   4493  N  N   . ARG B 1 125 ? 105.888 93.335  170.802 1.00 91.28  ? 83  ARG B N   1 
ATOM   4494  C  CA  . ARG B 1 125 ? 105.669 93.990  169.522 1.00 87.47  ? 83  ARG B CA  1 
ATOM   4495  C  C   . ARG B 1 125 ? 105.094 95.380  169.752 1.00 89.76  ? 83  ARG B C   1 
ATOM   4496  O  O   . ARG B 1 125 ? 104.309 95.596  170.679 1.00 95.33  ? 83  ARG B O   1 
ATOM   4497  C  CB  . ARG B 1 125 ? 104.728 93.163  168.651 1.00 83.60  ? 83  ARG B CB  1 
ATOM   4498  C  CG  . ARG B 1 125 ? 104.442 93.785  167.301 1.00 86.67  ? 83  ARG B CG  1 
ATOM   4499  C  CD  . ARG B 1 125 ? 103.229 93.156  166.651 1.00 87.46  ? 83  ARG B CD  1 
ATOM   4500  N  NE  . ARG B 1 125 ? 103.548 91.867  166.054 1.00 90.25  ? 83  ARG B NE  1 
ATOM   4501  C  CZ  . ARG B 1 125 ? 102.660 91.073  165.475 1.00 87.51  ? 83  ARG B CZ  1 
ATOM   4502  N  NH1 . ARG B 1 125 ? 101.381 91.401  165.408 1.00 87.75  ? 83  ARG B NH1 1 
ATOM   4503  N  NH2 . ARG B 1 125 ? 103.066 89.921  164.951 1.00 86.17  ? 83  ARG B NH2 1 
ATOM   4504  N  N   . PHE B 1 126 ? 105.499 96.329  168.907 1.00 79.38  ? 84  PHE B N   1 
ATOM   4505  C  CA  . PHE B 1 126 ? 105.133 97.736  169.063 1.00 78.36  ? 84  PHE B CA  1 
ATOM   4506  C  C   . PHE B 1 126 ? 105.608 98.290  170.402 1.00 78.89  ? 84  PHE B C   1 
ATOM   4507  O  O   . PHE B 1 126 ? 104.956 99.149  170.998 1.00 80.68  ? 84  PHE B O   1 
ATOM   4508  C  CB  . PHE B 1 126 ? 103.626 97.949  168.897 1.00 75.73  ? 84  PHE B CB  1 
ATOM   4509  C  CG  . PHE B 1 126 ? 103.110 97.585  167.536 1.00 79.27  ? 84  PHE B CG  1 
ATOM   4510  C  CD1 . PHE B 1 126 ? 103.739 98.046  166.398 1.00 78.51  ? 84  PHE B CD1 1 
ATOM   4511  C  CD2 . PHE B 1 126 ? 101.999 96.778  167.395 1.00 82.54  ? 84  PHE B CD2 1 
ATOM   4512  C  CE1 . PHE B 1 126 ? 103.267 97.711  165.149 1.00 76.89  ? 84  PHE B CE1 1 
ATOM   4513  C  CE2 . PHE B 1 126 ? 101.527 96.441  166.145 1.00 81.25  ? 84  PHE B CE2 1 
ATOM   4514  C  CZ  . PHE B 1 126 ? 102.161 96.907  165.024 1.00 76.71  ? 84  PHE B CZ  1 
ATOM   4515  N  N   . GLN B 1 127 ? 106.746 97.800  170.882 1.00 84.48  ? 85  GLN B N   1 
ATOM   4516  C  CA  . GLN B 1 127 ? 107.393 98.294  172.085 1.00 85.54  ? 85  GLN B CA  1 
ATOM   4517  C  C   . GLN B 1 127 ? 108.867 98.540  171.806 1.00 87.15  ? 85  GLN B C   1 
ATOM   4518  O  O   . GLN B 1 127 ? 109.459 97.872  170.953 1.00 88.12  ? 85  GLN B O   1 
ATOM   4519  C  CB  . GLN B 1 127 ? 107.251 97.298  173.246 1.00 85.34  ? 85  GLN B CB  1 
ATOM   4520  C  CG  . GLN B 1 127 ? 105.826 96.862  173.530 1.00 87.03  ? 85  GLN B CG  1 
ATOM   4521  C  CD  . GLN B 1 127 ? 105.069 97.861  174.374 1.00 90.04  ? 85  GLN B CD  1 
ATOM   4522  O  OE1 . GLN B 1 127 ? 103.842 97.932  174.321 1.00 92.70  ? 85  GLN B OE1 1 
ATOM   4523  N  NE2 . GLN B 1 127 ? 105.797 98.640  175.162 1.00 88.77  ? 85  GLN B NE2 1 
ATOM   4524  N  N   . PRO B 1 128 ? 109.484 99.490  172.504 1.00 82.25  ? 86  PRO B N   1 
ATOM   4525  C  CA  . PRO B 1 128 ? 110.907 99.732  172.299 1.00 81.30  ? 86  PRO B CA  1 
ATOM   4526  C  C   . PRO B 1 128 ? 111.715 98.515  172.693 1.00 83.81  ? 86  PRO B C   1 
ATOM   4527  O  O   . PRO B 1 128 ? 111.308 97.737  173.576 1.00 89.97  ? 86  PRO B O   1 
ATOM   4528  C  CB  . PRO B 1 128 ? 111.198 100.926 173.221 1.00 82.47  ? 86  PRO B CB  1 
ATOM   4529  C  CG  . PRO B 1 128 ? 110.090 100.932 174.208 1.00 82.20  ? 86  PRO B CG  1 
ATOM   4530  C  CD  . PRO B 1 128 ? 108.897 100.429 173.472 1.00 82.84  ? 86  PRO B CD  1 
ATOM   4531  N  N   . PRO B 1 129 ? 112.867 98.302  172.062 1.00 77.28  ? 87  PRO B N   1 
ATOM   4532  C  CA  . PRO B 1 129 ? 113.639 97.085  172.326 1.00 78.88  ? 87  PRO B CA  1 
ATOM   4533  C  C   . PRO B 1 129 ? 114.231 97.057  173.727 1.00 82.63  ? 87  PRO B C   1 
ATOM   4534  O  O   . PRO B 1 129 ? 114.500 98.094  174.339 1.00 82.62  ? 87  PRO B O   1 
ATOM   4535  C  CB  . PRO B 1 129 ? 114.739 97.140  171.264 1.00 79.06  ? 87  PRO B CB  1 
ATOM   4536  C  CG  . PRO B 1 129 ? 114.951 98.591  171.066 1.00 75.36  ? 87  PRO B CG  1 
ATOM   4537  C  CD  . PRO B 1 129 ? 113.580 99.206  171.147 1.00 78.33  ? 87  PRO B CD  1 
ATOM   4538  N  N   . GLU B 1 130 ? 114.425 95.843  174.237 1.00 90.80  ? 88  GLU B N   1 
ATOM   4539  C  CA  . GLU B 1 130 ? 115.102 95.620  175.504 1.00 91.42  ? 88  GLU B CA  1 
ATOM   4540  C  C   . GLU B 1 130 ? 116.431 94.914  175.266 1.00 91.06  ? 88  GLU B C   1 
ATOM   4541  O  O   . GLU B 1 130 ? 116.657 94.300  174.221 1.00 88.07  ? 88  GLU B O   1 
ATOM   4542  C  CB  . GLU B 1 130 ? 114.253 94.789  176.483 1.00 92.39  ? 88  GLU B CB  1 
ATOM   4543  C  CG  . GLU B 1 130 ? 112.879 95.354  176.866 1.00 94.59  ? 88  GLU B CG  1 
ATOM   4544  C  CD  . GLU B 1 130 ? 111.812 95.192  175.793 1.00 96.73  ? 88  GLU B CD  1 
ATOM   4545  O  OE1 . GLU B 1 130 ? 110.657 94.884  176.157 1.00 93.96  ? 88  GLU B OE1 1 
ATOM   4546  O  OE2 . GLU B 1 130 ? 112.119 95.327  174.594 1.00 94.92  ? 88  GLU B OE2 1 
ATOM   4547  N  N   . ALA B 1 131 ? 117.314 95.014  176.256 1.00 91.25  ? 89  ALA B N   1 
ATOM   4548  C  CA  . ALA B 1 131 ? 118.611 94.365  176.174 1.00 90.04  ? 89  ALA B CA  1 
ATOM   4549  C  C   . ALA B 1 131 ? 118.444 92.845  176.192 1.00 91.57  ? 89  ALA B C   1 
ATOM   4550  O  O   . ALA B 1 131 ? 117.534 92.324  176.839 1.00 93.00  ? 89  ALA B O   1 
ATOM   4551  C  CB  . ALA B 1 131 ? 119.498 94.808  177.333 1.00 90.62  ? 89  ALA B CB  1 
ATOM   4552  N  N   . PRO B 1 132 ? 119.329 92.107  175.506 1.00 91.22  ? 90  PRO B N   1 
ATOM   4553  C  CA  . PRO B 1 132 ? 119.117 90.660  175.346 1.00 92.66  ? 90  PRO B CA  1 
ATOM   4554  C  C   . PRO B 1 132 ? 119.302 89.870  176.632 1.00 97.15  ? 90  PRO B C   1 
ATOM   4555  O  O   . PRO B 1 132 ? 119.520 90.439  177.706 1.00 96.32  ? 90  PRO B O   1 
ATOM   4556  C  CB  . PRO B 1 132 ? 120.169 90.258  174.301 1.00 87.10  ? 90  PRO B CB  1 
ATOM   4557  C  CG  . PRO B 1 132 ? 120.842 91.521  173.869 1.00 87.57  ? 90  PRO B CG  1 
ATOM   4558  C  CD  . PRO B 1 132 ? 120.610 92.535  174.928 1.00 89.39  ? 90  PRO B CD  1 
ATOM   4559  N  N   . ALA B 1 133 ? 119.210 88.548  176.526 1.00 99.87  ? 91  ALA B N   1 
ATOM   4560  C  CA  . ALA B 1 133 ? 119.416 87.644  177.646 1.00 97.86  ? 91  ALA B CA  1 
ATOM   4561  C  C   . ALA B 1 133 ? 120.660 86.800  177.404 1.00 99.48  ? 91  ALA B C   1 
ATOM   4562  O  O   . ALA B 1 133 ? 120.890 86.325  176.288 1.00 100.45 ? 91  ALA B O   1 
ATOM   4563  C  CB  . ALA B 1 133 ? 118.201 86.739  177.854 1.00 96.25  ? 91  ALA B CB  1 
ATOM   4564  N  N   . SER B 1 134 ? 121.458 86.621  178.453 1.00 101.01 ? 92  SER B N   1 
ATOM   4565  C  CA  . SER B 1 134 ? 122.687 85.848  178.334 1.00 100.16 ? 92  SER B CA  1 
ATOM   4566  C  C   . SER B 1 134 ? 122.378 84.392  178.008 1.00 99.42  ? 92  SER B C   1 
ATOM   4567  O  O   . SER B 1 134 ? 121.437 83.802  178.544 1.00 100.43 ? 92  SER B O   1 
ATOM   4568  C  CB  . SER B 1 134 ? 123.491 85.935  179.631 1.00 101.08 ? 92  SER B CB  1 
ATOM   4569  O  OG  . SER B 1 134 ? 123.473 87.251  180.157 1.00 98.27  ? 92  SER B OG  1 
ATOM   4570  N  N   . TRP B 1 135 ? 123.181 83.811  177.120 1.00 101.89 ? 93  TRP B N   1 
ATOM   4571  C  CA  . TRP B 1 135 ? 123.025 82.423  176.722 1.00 102.59 ? 93  TRP B CA  1 
ATOM   4572  C  C   . TRP B 1 135 ? 124.183 81.597  177.252 1.00 105.81 ? 93  TRP B C   1 
ATOM   4573  O  O   . TRP B 1 135 ? 125.346 81.972  177.054 1.00 105.38 ? 93  TRP B O   1 
ATOM   4574  C  CB  . TRP B 1 135 ? 122.950 82.299  175.196 1.00 103.46 ? 93  TRP B CB  1 
ATOM   4575  C  CG  . TRP B 1 135 ? 124.079 82.976  174.484 1.00 105.54 ? 93  TRP B CG  1 
ATOM   4576  C  CD1 . TRP B 1 135 ? 125.232 82.400  174.043 1.00 102.21 ? 93  TRP B CD1 1 
ATOM   4577  C  CD2 . TRP B 1 135 ? 124.161 84.361  174.129 1.00 106.58 ? 93  TRP B CD2 1 
ATOM   4578  N  NE1 . TRP B 1 135 ? 126.029 83.340  173.439 1.00 103.84 ? 93  TRP B NE1 1 
ATOM   4579  C  CE2 . TRP B 1 135 ? 125.393 84.552  173.478 1.00 106.21 ? 93  TRP B CE2 1 
ATOM   4580  C  CE3 . TRP B 1 135 ? 123.312 85.457  174.299 1.00 104.86 ? 93  TRP B CE3 1 
ATOM   4581  C  CZ2 . TRP B 1 135 ? 125.796 85.793  172.996 1.00 105.00 ? 93  TRP B CZ2 1 
ATOM   4582  C  CZ3 . TRP B 1 135 ? 123.715 86.688  173.822 1.00 101.49 ? 93  TRP B CZ3 1 
ATOM   4583  C  CH2 . TRP B 1 135 ? 124.945 86.846  173.179 1.00 100.94 ? 93  TRP B CH2 1 
ATOM   4584  N  N   . PRO B 1 136 ? 123.916 80.482  177.933 1.00 114.47 ? 94  PRO B N   1 
ATOM   4585  C  CA  . PRO B 1 136 ? 125.009 79.657  178.464 1.00 113.51 ? 94  PRO B CA  1 
ATOM   4586  C  C   . PRO B 1 136 ? 125.610 78.782  177.372 1.00 113.35 ? 94  PRO B C   1 
ATOM   4587  O  O   . PRO B 1 136 ? 124.902 78.027  176.702 1.00 113.09 ? 94  PRO B O   1 
ATOM   4588  C  CB  . PRO B 1 136 ? 124.323 78.815  179.544 1.00 114.44 ? 94  PRO B CB  1 
ATOM   4589  C  CG  . PRO B 1 136 ? 122.911 78.696  179.071 1.00 112.92 ? 94  PRO B CG  1 
ATOM   4590  C  CD  . PRO B 1 136 ? 122.590 79.953  178.299 1.00 112.52 ? 94  PRO B CD  1 
ATOM   4591  N  N   . GLY B 1 137 ? 126.927 78.888  177.198 1.00 105.35 ? 95  GLY B N   1 
ATOM   4592  C  CA  . GLY B 1 137 ? 127.643 78.114  176.206 1.00 104.37 ? 95  GLY B CA  1 
ATOM   4593  C  C   . GLY B 1 137 ? 128.284 79.006  175.157 1.00 104.33 ? 95  GLY B C   1 
ATOM   4594  O  O   . GLY B 1 137 ? 128.651 80.155  175.435 1.00 103.56 ? 95  GLY B O   1 
ATOM   4595  N  N   . VAL B 1 138 ? 128.419 78.460  173.952 1.00 101.05 ? 96  VAL B N   1 
ATOM   4596  C  CA  . VAL B 1 138 ? 128.975 79.174  172.808 1.00 99.93  ? 96  VAL B CA  1 
ATOM   4597  C  C   . VAL B 1 138 ? 127.923 79.197  171.710 1.00 98.61  ? 96  VAL B C   1 
ATOM   4598  O  O   . VAL B 1 138 ? 127.398 78.146  171.326 1.00 97.64  ? 96  VAL B O   1 
ATOM   4599  C  CB  . VAL B 1 138 ? 130.276 78.523  172.307 1.00 97.65  ? 96  VAL B CB  1 
ATOM   4600  C  CG1 . VAL B 1 138 ? 130.524 78.881  170.859 1.00 97.00  ? 96  VAL B CG1 1 
ATOM   4601  C  CG2 . VAL B 1 138 ? 131.447 78.961  173.160 1.00 95.67  ? 96  VAL B CG2 1 
ATOM   4602  N  N   . ARG B 1 139 ? 127.620 80.390  171.209 1.00 94.57  ? 97  ARG B N   1 
ATOM   4603  C  CA  . ARG B 1 139 ? 126.620 80.581  170.170 1.00 94.33  ? 97  ARG B CA  1 
ATOM   4604  C  C   . ARG B 1 139 ? 127.302 80.651  168.813 1.00 91.12  ? 97  ARG B C   1 
ATOM   4605  O  O   . ARG B 1 139 ? 128.258 81.411  168.630 1.00 90.18  ? 97  ARG B O   1 
ATOM   4606  C  CB  . ARG B 1 139 ? 125.816 81.857  170.421 1.00 95.06  ? 97  ARG B CB  1 
ATOM   4607  C  CG  . ARG B 1 139 ? 124.945 82.280  169.253 1.00 92.19  ? 97  ARG B CG  1 
ATOM   4608  C  CD  . ARG B 1 139 ? 124.366 83.671  169.459 1.00 90.07  ? 97  ARG B CD  1 
ATOM   4609  N  NE  . ARG B 1 139 ? 123.242 83.918  168.565 1.00 92.23  ? 97  ARG B NE  1 
ATOM   4610  C  CZ  . ARG B 1 139 ? 121.985 83.602  168.842 1.00 94.48  ? 97  ARG B CZ  1 
ATOM   4611  N  NH1 . ARG B 1 139 ? 121.649 83.050  169.995 1.00 94.44  ? 97  ARG B NH1 1 
ATOM   4612  N  NH2 . ARG B 1 139 ? 121.041 83.846  167.937 1.00 89.72  ? 97  ARG B NH2 1 
ATOM   4613  N  N   . ASN B 1 140 ? 126.810 79.859  167.867 1.00 96.95  ? 98  ASN B N   1 
ATOM   4614  C  CA  . ASN B 1 140 ? 127.329 79.906  166.509 1.00 97.43  ? 98  ASN B CA  1 
ATOM   4615  C  C   . ASN B 1 140 ? 126.899 81.203  165.840 1.00 100.51 ? 98  ASN B C   1 
ATOM   4616  O  O   . ASN B 1 140 ? 125.705 81.513  165.782 1.00 100.89 ? 98  ASN B O   1 
ATOM   4617  C  CB  . ASN B 1 140 ? 126.826 78.712  165.706 1.00 98.25  ? 98  ASN B CB  1 
ATOM   4618  C  CG  . ASN B 1 140 ? 127.598 77.447  165.990 1.00 101.49 ? 98  ASN B CG  1 
ATOM   4619  O  OD1 . ASN B 1 140 ? 128.826 77.450  166.057 1.00 101.48 ? 98  ASN B OD1 1 
ATOM   4620  N  ND2 . ASN B 1 140 ? 126.874 76.349  166.153 1.00 103.59 ? 98  ASN B ND2 1 
ATOM   4621  N  N   . ALA B 1 141 ? 127.867 81.963  165.338 1.00 87.23  ? 99  ALA B N   1 
ATOM   4622  C  CA  . ALA B 1 141 ? 127.596 83.143  164.525 1.00 80.56  ? 99  ALA B CA  1 
ATOM   4623  C  C   . ALA B 1 141 ? 128.288 82.932  163.185 1.00 82.91  ? 99  ALA B C   1 
ATOM   4624  O  O   . ALA B 1 141 ? 129.401 83.408  162.961 1.00 81.97  ? 99  ALA B O   1 
ATOM   4625  C  CB  . ALA B 1 141 ? 128.073 84.402  165.220 1.00 79.28  ? 99  ALA B CB  1 
ATOM   4626  N  N   . THR B 1 142 ? 127.627 82.211  162.301 1.00 88.74  ? 100 THR B N   1 
ATOM   4627  C  CA  . THR B 1 142 ? 128.128 81.977  160.952 1.00 87.93  ? 100 THR B CA  1 
ATOM   4628  C  C   . THR B 1 142 ? 127.085 82.248  159.879 1.00 90.64  ? 100 THR B C   1 
ATOM   4629  O  O   . THR B 1 142 ? 127.429 82.753  158.808 1.00 88.59  ? 100 THR B O   1 
ATOM   4630  C  CB  . THR B 1 142 ? 128.636 80.537  160.822 1.00 91.84  ? 100 THR B CB  1 
ATOM   4631  O  OG1 . THR B 1 142 ? 129.477 80.221  161.938 1.00 94.27  ? 100 THR B OG1 1 
ATOM   4632  C  CG2 . THR B 1 142 ? 129.424 80.368  159.537 1.00 93.90  ? 100 THR B CG2 1 
ATOM   4633  N  N   . THR B 1 143 ? 125.823 81.926  160.139 1.00 91.63  ? 101 THR B N   1 
ATOM   4634  C  CA  . THR B 1 143 ? 124.774 82.099  159.149 1.00 89.61  ? 101 THR B CA  1 
ATOM   4635  C  C   . THR B 1 143 ? 124.277 83.536  159.131 1.00 88.70  ? 101 THR B C   1 
ATOM   4636  O  O   . THR B 1 143 ? 124.216 84.207  160.164 1.00 89.10  ? 101 THR B O   1 
ATOM   4637  C  CB  . THR B 1 143 ? 123.603 81.163  159.440 1.00 88.98  ? 101 THR B CB  1 
ATOM   4638  O  OG1 . THR B 1 143 ? 122.799 81.722  160.486 1.00 87.31  ? 101 THR B OG1 1 
ATOM   4639  C  CG2 . THR B 1 143 ? 124.109 79.795  159.872 1.00 90.54  ? 101 THR B CG2 1 
ATOM   4640  N  N   . LEU B 1 144 ? 123.919 84.005  157.943 1.00 85.67  ? 102 LEU B N   1 
ATOM   4641  C  CA  . LEU B 1 144 ? 123.307 85.321  157.822 1.00 82.34  ? 102 LEU B CA  1 
ATOM   4642  C  C   . LEU B 1 144 ? 121.928 85.296  158.469 1.00 84.56  ? 102 LEU B C   1 
ATOM   4643  O  O   . LEU B 1 144 ? 121.096 84.455  158.111 1.00 88.47  ? 102 LEU B O   1 
ATOM   4644  C  CB  . LEU B 1 144 ? 123.199 85.734  156.360 1.00 82.76  ? 102 LEU B CB  1 
ATOM   4645  C  CG  . LEU B 1 144 ? 124.520 85.942  155.625 1.00 84.72  ? 102 LEU B CG  1 
ATOM   4646  C  CD1 . LEU B 1 144 ? 124.269 86.319  154.175 1.00 82.49  ? 102 LEU B CD1 1 
ATOM   4647  C  CD2 . LEU B 1 144 ? 125.346 87.001  156.324 1.00 83.03  ? 102 LEU B CD2 1 
ATOM   4648  N  N   . PRO B 1 145 ? 121.648 86.186  159.412 1.00 77.48  ? 103 PRO B N   1 
ATOM   4649  C  CA  . PRO B 1 145 ? 120.381 86.134  160.138 1.00 77.27  ? 103 PRO B CA  1 
ATOM   4650  C  C   . PRO B 1 145 ? 119.208 86.454  159.230 1.00 79.82  ? 103 PRO B C   1 
ATOM   4651  O  O   . PRO B 1 145 ? 119.382 87.056  158.161 1.00 78.78  ? 103 PRO B O   1 
ATOM   4652  C  CB  . PRO B 1 145 ? 120.556 87.205  161.223 1.00 76.14  ? 103 PRO B CB  1 
ATOM   4653  C  CG  . PRO B 1 145 ? 121.629 88.090  160.719 1.00 76.97  ? 103 PRO B CG  1 
ATOM   4654  C  CD  . PRO B 1 145 ? 122.552 87.212  159.951 1.00 78.98  ? 103 PRO B CD  1 
ATOM   4655  N  N   . PRO B 1 146 ? 118.000 86.050  159.615 1.00 80.58  ? 104 PRO B N   1 
ATOM   4656  C  CA  . PRO B 1 146 ? 116.823 86.345  158.794 1.00 78.97  ? 104 PRO B CA  1 
ATOM   4657  C  C   . PRO B 1 146 ? 116.537 87.836  158.709 1.00 76.07  ? 104 PRO B C   1 
ATOM   4658  O  O   . PRO B 1 146 ? 116.850 88.607  159.618 1.00 76.22  ? 104 PRO B O   1 
ATOM   4659  C  CB  . PRO B 1 146 ? 115.694 85.612  159.526 1.00 77.41  ? 104 PRO B CB  1 
ATOM   4660  C  CG  . PRO B 1 146 ? 116.181 85.476  160.926 1.00 72.77  ? 104 PRO B CG  1 
ATOM   4661  C  CD  . PRO B 1 146 ? 117.651 85.251  160.800 1.00 75.37  ? 104 PRO B CD  1 
ATOM   4662  N  N   . ALA B 1 147 ? 115.930 88.234  157.595 1.00 68.22  ? 105 ALA B N   1 
ATOM   4663  C  CA  . ALA B 1 147 ? 115.523 89.614  157.396 1.00 71.91  ? 105 ALA B CA  1 
ATOM   4664  C  C   . ALA B 1 147 ? 114.202 89.892  158.110 1.00 77.11  ? 105 ALA B C   1 
ATOM   4665  O  O   . ALA B 1 147 ? 113.490 88.981  158.534 1.00 83.33  ? 105 ALA B O   1 
ATOM   4666  C  CB  . ALA B 1 147 ? 115.397 89.923  155.907 1.00 73.56  ? 105 ALA B CB  1 
ATOM   4667  N  N   . CYS B 1 148 ? 113.879 91.178  158.249 1.00 78.20  ? 106 CYS B N   1 
ATOM   4668  C  CA  . CYS B 1 148 ? 112.632 91.572  158.884 1.00 77.46  ? 106 CYS B CA  1 
ATOM   4669  C  C   . CYS B 1 148 ? 111.469 91.444  157.901 1.00 83.06  ? 106 CYS B C   1 
ATOM   4670  O  O   . CYS B 1 148 ? 111.668 91.526  156.687 1.00 88.53  ? 106 CYS B O   1 
ATOM   4671  C  CB  . CYS B 1 148 ? 112.725 93.002  159.397 1.00 76.14  ? 106 CYS B CB  1 
ATOM   4672  S  SG  . CYS B 1 148 ? 113.963 93.244  160.686 1.00 95.46  ? 106 CYS B SG  1 
ATOM   4673  N  N   . PRO B 1 149 ? 110.249 91.236  158.401 1.00 80.31  ? 107 PRO B N   1 
ATOM   4674  C  CA  . PRO B 1 149 ? 109.115 91.011  157.497 1.00 78.67  ? 107 PRO B CA  1 
ATOM   4675  C  C   . PRO B 1 149 ? 108.907 92.178  156.545 1.00 75.79  ? 107 PRO B C   1 
ATOM   4676  O  O   . PRO B 1 149 ? 108.955 93.344  156.938 1.00 78.83  ? 107 PRO B O   1 
ATOM   4677  C  CB  . PRO B 1 149 ? 107.931 90.847  158.454 1.00 79.68  ? 107 PRO B CB  1 
ATOM   4678  C  CG  . PRO B 1 149 ? 108.540 90.388  159.724 1.00 78.08  ? 107 PRO B CG  1 
ATOM   4679  C  CD  . PRO B 1 149 ? 109.857 91.092  159.812 1.00 79.40  ? 107 PRO B CD  1 
ATOM   4680  N  N   . GLN B 1 150 ? 108.656 91.844  155.284 1.00 73.34  ? 108 GLN B N   1 
ATOM   4681  C  CA  . GLN B 1 150 ? 108.523 92.822  154.214 1.00 68.68  ? 108 GLN B CA  1 
ATOM   4682  C  C   . GLN B 1 150 ? 107.886 92.123  153.023 1.00 79.43  ? 108 GLN B C   1 
ATOM   4683  O  O   . GLN B 1 150 ? 107.704 90.903  153.020 1.00 88.64  ? 108 GLN B O   1 
ATOM   4684  C  CB  . GLN B 1 150 ? 109.874 93.423  153.834 1.00 66.48  ? 108 GLN B CB  1 
ATOM   4685  C  CG  . GLN B 1 150 ? 110.900 92.382  153.459 1.00 67.69  ? 108 GLN B CG  1 
ATOM   4686  C  CD  . GLN B 1 150 ? 112.312 92.884  153.604 1.00 74.20  ? 108 GLN B CD  1 
ATOM   4687  O  OE1 . GLN B 1 150 ? 112.962 93.226  152.619 1.00 78.90  ? 108 GLN B OE1 1 
ATOM   4688  N  NE2 . GLN B 1 150 ? 112.800 92.931  154.835 1.00 74.40  ? 108 GLN B NE2 1 
ATOM   4689  N  N   . ASN B 1 151 ? 107.547 92.913  152.005 1.00 81.92  ? 109 ASN B N   1 
ATOM   4690  C  CA  . ASN B 1 151 ? 106.924 92.396  150.783 1.00 78.51  ? 109 ASN B CA  1 
ATOM   4691  C  C   . ASN B 1 151 ? 107.421 93.241  149.612 1.00 79.63  ? 109 ASN B C   1 
ATOM   4692  O  O   . ASN B 1 151 ? 106.863 94.301  149.322 1.00 84.31  ? 109 ASN B O   1 
ATOM   4693  C  CB  . ASN B 1 151 ? 105.407 92.420  150.893 1.00 81.25  ? 109 ASN B CB  1 
ATOM   4694  C  CG  . ASN B 1 151 ? 104.727 91.834  149.676 1.00 84.39  ? 109 ASN B CG  1 
ATOM   4695  O  OD1 . ASN B 1 151 ? 104.715 92.440  148.606 1.00 85.83  ? 109 ASN B OD1 1 
ATOM   4696  N  ND2 . ASN B 1 151 ? 104.151 90.650  149.834 1.00 84.63  ? 109 ASN B ND2 1 
ATOM   4697  N  N   . LEU B 1 152 ? 108.471 92.763  148.941 1.00 77.12  ? 110 LEU B N   1 
ATOM   4698  C  CA  . LEU B 1 152 ? 108.995 93.496  147.793 1.00 81.27  ? 110 LEU B CA  1 
ATOM   4699  C  C   . LEU B 1 152 ? 108.060 93.399  146.596 1.00 87.87  ? 110 LEU B C   1 
ATOM   4700  O  O   . LEU B 1 152 ? 107.806 94.400  145.918 1.00 91.38  ? 110 LEU B O   1 
ATOM   4701  C  CB  . LEU B 1 152 ? 110.385 92.986  147.423 1.00 81.17  ? 110 LEU B CB  1 
ATOM   4702  C  CG  . LEU B 1 152 ? 111.341 92.620  148.553 1.00 81.75  ? 110 LEU B CG  1 
ATOM   4703  C  CD1 . LEU B 1 152 ? 112.675 92.215  147.969 1.00 80.84  ? 110 LEU B CD1 1 
ATOM   4704  C  CD2 . LEU B 1 152 ? 111.515 93.792  149.495 1.00 83.06  ? 110 LEU B CD2 1 
ATOM   4705  N  N   . HIS B 1 153 ? 107.538 92.205  146.316 1.00 99.81  ? 111 HIS B N   1 
ATOM   4706  C  CA  . HIS B 1 153 ? 106.645 92.002  145.176 1.00 99.69  ? 111 HIS B CA  1 
ATOM   4707  C  C   . HIS B 1 153 ? 105.248 92.506  145.537 1.00 98.40  ? 111 HIS B C   1 
ATOM   4708  O  O   . HIS B 1 153 ? 104.275 91.757  145.647 1.00 97.28  ? 111 HIS B O   1 
ATOM   4709  C  CB  . HIS B 1 153 ? 106.630 90.537  144.762 1.00 99.85  ? 111 HIS B CB  1 
ATOM   4710  C  CG  . HIS B 1 153 ? 107.892 90.089  144.096 1.00 103.03 ? 111 HIS B CG  1 
ATOM   4711  N  ND1 . HIS B 1 153 ? 108.659 89.049  144.575 1.00 102.38 ? 111 HIS B ND1 1 
ATOM   4712  C  CD2 . HIS B 1 153 ? 108.522 90.540  142.986 1.00 101.40 ? 111 HIS B CD2 1 
ATOM   4713  C  CE1 . HIS B 1 153 ? 109.707 88.880  143.790 1.00 101.98 ? 111 HIS B CE1 1 
ATOM   4714  N  NE2 . HIS B 1 153 ? 109.648 89.772  142.817 1.00 101.46 ? 111 HIS B NE2 1 
ATOM   4715  N  N   . GLY B 1 154 ? 105.166 93.812  145.724 1.00 91.11  ? 112 GLY B N   1 
ATOM   4716  C  CA  . GLY B 1 154 ? 103.923 94.474  146.076 1.00 90.26  ? 112 GLY B CA  1 
ATOM   4717  C  C   . GLY B 1 154 ? 103.977 95.923  145.667 1.00 93.22  ? 112 GLY B C   1 
ATOM   4718  O  O   . GLY B 1 154 ? 104.578 96.273  144.647 1.00 91.26  ? 112 GLY B O   1 
ATOM   4719  N  N   . ALA B 1 155 ? 103.350 96.776  146.470 1.00 100.69 ? 113 ALA B N   1 
ATOM   4720  C  CA  . ALA B 1 155 ? 103.288 98.210  146.206 1.00 98.59  ? 113 ALA B CA  1 
ATOM   4721  C  C   . ALA B 1 155 ? 104.385 98.893  147.013 1.00 98.70  ? 113 ALA B C   1 
ATOM   4722  O  O   . ALA B 1 155 ? 104.231 99.137  148.212 1.00 98.04  ? 113 ALA B O   1 
ATOM   4723  C  CB  . ALA B 1 155 ? 101.910 98.763  146.552 1.00 95.45  ? 113 ALA B CB  1 
ATOM   4724  N  N   . LEU B 1 156 ? 105.497 99.201  146.348 1.00 92.75  ? 114 LEU B N   1 
ATOM   4725  C  CA  . LEU B 1 156 ? 106.614 99.896  146.960 1.00 89.64  ? 114 LEU B CA  1 
ATOM   4726  C  C   . LEU B 1 156 ? 106.818 101.257 146.306 1.00 91.49  ? 114 LEU B C   1 
ATOM   4727  O  O   . LEU B 1 156 ? 106.553 101.422 145.111 1.00 91.73  ? 114 LEU B O   1 
ATOM   4728  C  CB  . LEU B 1 156 ? 107.911 99.090  146.831 1.00 85.61  ? 114 LEU B CB  1 
ATOM   4729  C  CG  . LEU B 1 156 ? 108.065 97.884  147.750 1.00 89.60  ? 114 LEU B CG  1 
ATOM   4730  C  CD1 . LEU B 1 156 ? 109.390 97.201  147.483 1.00 88.21  ? 114 LEU B CD1 1 
ATOM   4731  C  CD2 . LEU B 1 156 ? 107.959 98.313  149.201 1.00 91.78  ? 114 LEU B CD2 1 
ATOM   4732  N  N   . PRO B 1 157 ? 107.291 102.252 147.055 1.00 82.31  ? 115 PRO B N   1 
ATOM   4733  C  CA  . PRO B 1 157 ? 107.628 103.532 146.425 1.00 76.35  ? 115 PRO B CA  1 
ATOM   4734  C  C   . PRO B 1 157 ? 108.878 103.392 145.580 1.00 74.46  ? 115 PRO B C   1 
ATOM   4735  O  O   . PRO B 1 157 ? 109.987 103.328 146.112 1.00 75.99  ? 115 PRO B O   1 
ATOM   4736  C  CB  . PRO B 1 157 ? 107.851 104.469 147.620 1.00 70.69  ? 115 PRO B CB  1 
ATOM   4737  C  CG  . PRO B 1 157 ? 107.281 103.749 148.806 1.00 68.20  ? 115 PRO B CG  1 
ATOM   4738  C  CD  . PRO B 1 157 ? 107.453 102.301 148.515 1.00 71.72  ? 115 PRO B CD  1 
ATOM   4739  N  N   . ALA B 1 158 ? 108.714 103.343 144.261 1.00 66.13  ? 116 ALA B N   1 
ATOM   4740  C  CA  . ALA B 1 158 ? 109.845 103.071 143.386 1.00 66.03  ? 116 ALA B CA  1 
ATOM   4741  C  C   . ALA B 1 158 ? 110.727 104.287 143.166 1.00 65.05  ? 116 ALA B C   1 
ATOM   4742  O  O   . ALA B 1 158 ? 111.862 104.134 142.706 1.00 64.39  ? 116 ALA B O   1 
ATOM   4743  C  CB  . ALA B 1 158 ? 109.355 102.546 142.037 1.00 65.53  ? 116 ALA B CB  1 
ATOM   4744  N  N   . ILE B 1 159 ? 110.237 105.486 143.476 1.00 55.53  ? 117 ILE B N   1 
ATOM   4745  C  CA  . ILE B 1 159 ? 111.018 106.690 143.218 1.00 59.54  ? 117 ILE B CA  1 
ATOM   4746  C  C   . ILE B 1 159 ? 112.200 106.781 144.175 1.00 63.72  ? 117 ILE B C   1 
ATOM   4747  O  O   . ILE B 1 159 ? 113.328 107.077 143.765 1.00 59.90  ? 117 ILE B O   1 
ATOM   4748  C  CB  . ILE B 1 159 ? 110.119 107.932 143.311 1.00 54.04  ? 117 ILE B CB  1 
ATOM   4749  C  CG1 . ILE B 1 159 ? 109.150 107.971 142.138 1.00 56.44  ? 117 ILE B CG1 1 
ATOM   4750  C  CG2 . ILE B 1 159 ? 110.953 109.180 143.285 1.00 52.93  ? 117 ILE B CG2 1 
ATOM   4751  C  CD1 . ILE B 1 159 ? 107.707 107.844 142.554 1.00 62.82  ? 117 ILE B CD1 1 
ATOM   4752  N  N   . MET B 1 160 ? 111.967 106.523 145.461 1.00 54.34  ? 118 MET B N   1 
ATOM   4753  C  CA  . MET B 1 160 ? 112.999 106.708 146.470 1.00 45.64  ? 118 MET B CA  1 
ATOM   4754  C  C   . MET B 1 160 ? 113.957 105.533 146.580 1.00 55.38  ? 118 MET B C   1 
ATOM   4755  O  O   . MET B 1 160 ? 115.014 105.681 147.200 1.00 65.61  ? 118 MET B O   1 
ATOM   4756  C  CB  . MET B 1 160 ? 112.360 106.963 147.834 1.00 50.00  ? 118 MET B CB  1 
ATOM   4757  C  CG  . MET B 1 160 ? 111.050 106.240 148.046 1.00 54.28  ? 118 MET B CG  1 
ATOM   4758  S  SD  . MET B 1 160 ? 110.140 106.866 149.465 1.00 64.84  ? 118 MET B SD  1 
ATOM   4759  C  CE  . MET B 1 160 ? 111.403 106.793 150.725 1.00 51.67  ? 118 MET B CE  1 
ATOM   4760  N  N   . LEU B 1 161 ? 113.621 104.381 146.012 1.00 55.22  ? 119 LEU B N   1 
ATOM   4761  C  CA  . LEU B 1 161 ? 114.479 103.217 146.142 1.00 50.61  ? 119 LEU B CA  1 
ATOM   4762  C  C   . LEU B 1 161 ? 115.731 103.381 145.284 1.00 47.41  ? 119 LEU B C   1 
ATOM   4763  O  O   . LEU B 1 161 ? 115.695 104.034 144.240 1.00 55.00  ? 119 LEU B O   1 
ATOM   4764  C  CB  . LEU B 1 161 ? 113.730 101.956 145.730 1.00 51.18  ? 119 LEU B CB  1 
ATOM   4765  C  CG  . LEU B 1 161 ? 112.577 101.528 146.634 1.00 50.91  ? 119 LEU B CG  1 
ATOM   4766  C  CD1 . LEU B 1 161 ? 112.056 100.168 146.226 1.00 53.93  ? 119 LEU B CD1 1 
ATOM   4767  C  CD2 . LEU B 1 161 ? 113.004 101.523 148.076 1.00 49.33  ? 119 LEU B CD2 1 
ATOM   4768  N  N   . PRO B 1 162 ? 116.852 102.800 145.703 1.00 41.04  ? 120 PRO B N   1 
ATOM   4769  C  CA  . PRO B 1 162 ? 118.061 102.871 144.883 1.00 47.98  ? 120 PRO B CA  1 
ATOM   4770  C  C   . PRO B 1 162 ? 117.849 102.179 143.548 1.00 57.57  ? 120 PRO B C   1 
ATOM   4771  O  O   . PRO B 1 162 ? 117.043 101.258 143.425 1.00 71.58  ? 120 PRO B O   1 
ATOM   4772  C  CB  . PRO B 1 162 ? 119.109 102.144 145.731 1.00 49.34  ? 120 PRO B CB  1 
ATOM   4773  C  CG  . PRO B 1 162 ? 118.582 102.202 147.113 1.00 48.66  ? 120 PRO B CG  1 
ATOM   4774  C  CD  . PRO B 1 162 ? 117.099 102.108 146.974 1.00 46.63  ? 120 PRO B CD  1 
ATOM   4775  N  N   . VAL B 1 163 ? 118.576 102.649 142.536 1.00 54.37  ? 121 VAL B N   1 
ATOM   4776  C  CA  . VAL B 1 163 ? 118.399 102.117 141.188 1.00 53.56  ? 121 VAL B CA  1 
ATOM   4777  C  C   . VAL B 1 163 ? 118.767 100.639 141.133 1.00 62.71  ? 121 VAL B C   1 
ATOM   4778  O  O   . VAL B 1 163 ? 118.057 99.833  140.518 1.00 63.60  ? 121 VAL B O   1 
ATOM   4779  C  CB  . VAL B 1 163 ? 119.207 102.950 140.179 1.00 56.69  ? 121 VAL B CB  1 
ATOM   4780  C  CG1 . VAL B 1 163 ? 119.613 102.106 138.990 1.00 59.79  ? 121 VAL B CG1 1 
ATOM   4781  C  CG2 . VAL B 1 163 ? 118.377 104.125 139.715 1.00 55.29  ? 121 VAL B CG2 1 
ATOM   4782  N  N   . TRP B 1 164 ? 119.874 100.254 141.773 1.00 59.92  ? 122 TRP B N   1 
ATOM   4783  C  CA  . TRP B 1 164 ? 120.291 98.857  141.723 1.00 52.25  ? 122 TRP B CA  1 
ATOM   4784  C  C   . TRP B 1 164 ? 119.309 97.947  142.446 1.00 53.90  ? 122 TRP B C   1 
ATOM   4785  O  O   . TRP B 1 164 ? 119.237 96.753  142.142 1.00 63.45  ? 122 TRP B O   1 
ATOM   4786  C  CB  . TRP B 1 164 ? 121.694 98.695  142.306 1.00 54.87  ? 122 TRP B CB  1 
ATOM   4787  C  CG  . TRP B 1 164 ? 121.856 99.235  143.688 1.00 58.76  ? 122 TRP B CG  1 
ATOM   4788  C  CD1 . TRP B 1 164 ? 122.393 100.433 144.034 1.00 60.10  ? 122 TRP B CD1 1 
ATOM   4789  C  CD2 . TRP B 1 164 ? 121.490 98.590  144.915 1.00 56.52  ? 122 TRP B CD2 1 
ATOM   4790  N  NE1 . TRP B 1 164 ? 122.380 100.582 145.397 1.00 63.00  ? 122 TRP B NE1 1 
ATOM   4791  C  CE2 . TRP B 1 164 ? 121.830 99.462  145.960 1.00 53.67  ? 122 TRP B CE2 1 
ATOM   4792  C  CE3 . TRP B 1 164 ? 120.907 97.361  145.228 1.00 58.51  ? 122 TRP B CE3 1 
ATOM   4793  C  CZ2 . TRP B 1 164 ? 121.604 99.149  147.293 1.00 50.69  ? 122 TRP B CZ2 1 
ATOM   4794  C  CZ3 . TRP B 1 164 ? 120.682 97.053  146.552 1.00 56.22  ? 122 TRP B CZ3 1 
ATOM   4795  C  CH2 . TRP B 1 164 ? 121.030 97.941  147.567 1.00 52.96  ? 122 TRP B CH2 1 
ATOM   4796  N  N   . PHE B 1 165 ? 118.552 98.482  143.403 1.00 56.21  ? 123 PHE B N   1 
ATOM   4797  C  CA  . PHE B 1 165 ? 117.563 97.665  144.096 1.00 50.90  ? 123 PHE B CA  1 
ATOM   4798  C  C   . PHE B 1 165 ? 116.359 97.395  143.209 1.00 51.44  ? 123 PHE B C   1 
ATOM   4799  O  O   . PHE B 1 165 ? 115.851 96.271  143.169 1.00 67.55  ? 123 PHE B O   1 
ATOM   4800  C  CB  . PHE B 1 165 ? 117.128 98.348  145.389 1.00 58.07  ? 123 PHE B CB  1 
ATOM   4801  C  CG  . PHE B 1 165 ? 116.238 97.507  146.251 1.00 58.20  ? 123 PHE B CG  1 
ATOM   4802  C  CD1 . PHE B 1 165 ? 114.870 97.495  146.057 1.00 57.61  ? 123 PHE B CD1 1 
ATOM   4803  C  CD2 . PHE B 1 165 ? 116.769 96.737  147.265 1.00 59.39  ? 123 PHE B CD2 1 
ATOM   4804  C  CE1 . PHE B 1 165 ? 114.053 96.722  146.850 1.00 59.39  ? 123 PHE B CE1 1 
ATOM   4805  C  CE2 . PHE B 1 165 ? 115.956 95.964  148.060 1.00 65.48  ? 123 PHE B CE2 1 
ATOM   4806  C  CZ  . PHE B 1 165 ? 114.597 95.957  147.852 1.00 64.17  ? 123 PHE B CZ  1 
ATOM   4807  N  N   . THR B 1 166 ? 115.882 98.416  142.496 1.00 56.14  ? 124 THR B N   1 
ATOM   4808  C  CA  . THR B 1 166 ? 114.705 98.239  141.655 1.00 62.62  ? 124 THR B CA  1 
ATOM   4809  C  C   . THR B 1 166 ? 115.036 97.455  140.391 1.00 69.79  ? 124 THR B C   1 
ATOM   4810  O  O   . THR B 1 166 ? 114.266 96.581  139.979 1.00 73.97  ? 124 THR B O   1 
ATOM   4811  C  CB  . THR B 1 166 ? 114.105 99.600  141.307 1.00 62.93  ? 124 THR B CB  1 
ATOM   4812  O  OG1 . THR B 1 166 ? 113.398 100.111 142.442 1.00 61.85  ? 124 THR B OG1 1 
ATOM   4813  C  CG2 . THR B 1 166 ? 113.142 99.478  140.142 1.00 64.07  ? 124 THR B CG2 1 
ATOM   4814  N  N   . ASP B 1 167 ? 116.182 97.743  139.770 1.00 73.01  ? 125 ASP B N   1 
ATOM   4815  C  CA  . ASP B 1 167 ? 116.562 97.049  138.542 1.00 70.72  ? 125 ASP B CA  1 
ATOM   4816  C  C   . ASP B 1 167 ? 116.701 95.551  138.779 1.00 73.49  ? 125 ASP B C   1 
ATOM   4817  O  O   . ASP B 1 167 ? 115.978 94.743  138.187 1.00 78.39  ? 125 ASP B O   1 
ATOM   4818  C  CB  . ASP B 1 167 ? 117.867 97.628  137.995 1.00 69.23  ? 125 ASP B CB  1 
ATOM   4819  C  CG  . ASP B 1 167 ? 117.658 98.923  137.242 1.00 75.29  ? 125 ASP B CG  1 
ATOM   4820  O  OD1 . ASP B 1 167 ? 116.502 99.389  137.173 1.00 71.57  ? 125 ASP B OD1 1 
ATOM   4821  O  OD2 . ASP B 1 167 ? 118.649 99.475  136.719 1.00 73.80  ? 125 ASP B OD2 1 
ATOM   4822  N  N   . ASN B 1 168 ? 117.626 95.163  139.650 1.00 68.87  ? 126 ASN B N   1 
ATOM   4823  C  CA  . ASN B 1 168 ? 117.857 93.756  139.967 1.00 67.18  ? 126 ASN B CA  1 
ATOM   4824  C  C   . ASN B 1 168 ? 117.009 93.306  141.149 1.00 65.57  ? 126 ASN B C   1 
ATOM   4825  O  O   . ASN B 1 168 ? 117.512 92.790  142.144 1.00 67.39  ? 126 ASN B O   1 
ATOM   4826  C  CB  . ASN B 1 168 ? 119.338 93.529  140.234 1.00 65.80  ? 126 ASN B CB  1 
ATOM   4827  C  CG  . ASN B 1 168 ? 120.217 94.198  139.204 1.00 71.86  ? 126 ASN B CG  1 
ATOM   4828  O  OD1 . ASN B 1 168 ? 121.003 95.086  139.527 1.00 76.89  ? 126 ASN B OD1 1 
ATOM   4829  N  ND2 . ASN B 1 168 ? 120.085 93.779  137.953 1.00 73.82  ? 126 ASN B ND2 1 
ATOM   4830  N  N   . LEU B 1 169 ? 115.696 93.508  141.040 1.00 65.74  ? 127 LEU B N   1 
ATOM   4831  C  CA  . LEU B 1 169 ? 114.801 93.147  142.132 1.00 69.33  ? 127 LEU B CA  1 
ATOM   4832  C  C   . LEU B 1 169 ? 114.714 91.638  142.312 1.00 74.31  ? 127 LEU B C   1 
ATOM   4833  O  O   . LEU B 1 169 ? 114.548 91.160  143.439 1.00 81.86  ? 127 LEU B O   1 
ATOM   4834  C  CB  . LEU B 1 169 ? 113.415 93.740  141.887 1.00 70.77  ? 127 LEU B CB  1 
ATOM   4835  C  CG  . LEU B 1 169 ? 112.452 93.746  143.072 1.00 72.02  ? 127 LEU B CG  1 
ATOM   4836  C  CD1 . LEU B 1 169 ? 113.147 94.246  144.319 1.00 71.76  ? 127 LEU B CD1 1 
ATOM   4837  C  CD2 . LEU B 1 169 ? 111.238 94.599  142.758 1.00 72.96  ? 127 LEU B CD2 1 
ATOM   4838  N  N   . GLU B 1 170 ? 114.822 90.873  141.223 1.00 84.57  ? 128 GLU B N   1 
ATOM   4839  C  CA  . GLU B 1 170 ? 114.766 89.419  141.334 1.00 85.02  ? 128 GLU B CA  1 
ATOM   4840  C  C   . GLU B 1 170 ? 115.924 88.885  142.167 1.00 84.54  ? 128 GLU B C   1 
ATOM   4841  O  O   . GLU B 1 170 ? 115.734 88.006  143.015 1.00 82.01  ? 128 GLU B O   1 
ATOM   4842  C  CB  . GLU B 1 170 ? 114.774 88.784  139.943 1.00 87.03  ? 128 GLU B CB  1 
ATOM   4843  C  CG  . GLU B 1 170 ? 113.677 89.286  139.019 1.00 88.96  ? 128 GLU B CG  1 
ATOM   4844  C  CD  . GLU B 1 170 ? 114.188 90.285  138.000 1.00 93.01  ? 128 GLU B CD  1 
ATOM   4845  O  OE1 . GLU B 1 170 ? 115.352 90.151  137.570 1.00 92.15  ? 128 GLU B OE1 1 
ATOM   4846  O  OE2 . GLU B 1 170 ? 113.427 91.205  137.631 1.00 90.87  ? 128 GLU B OE2 1 
ATOM   4847  N  N   . ALA B 1 171 ? 117.132 89.403  141.940 1.00 84.06  ? 129 ALA B N   1 
ATOM   4848  C  CA  . ALA B 1 171 ? 118.278 88.967  142.728 1.00 82.46  ? 129 ALA B CA  1 
ATOM   4849  C  C   . ALA B 1 171 ? 118.249 89.554  144.132 1.00 81.35  ? 129 ALA B C   1 
ATOM   4850  O  O   . ALA B 1 171 ? 118.710 88.910  145.080 1.00 80.77  ? 129 ALA B O   1 
ATOM   4851  C  CB  . ALA B 1 171 ? 119.579 89.343  142.022 1.00 79.91  ? 129 ALA B CB  1 
ATOM   4852  N  N   . ALA B 1 172 ? 117.724 90.771  144.284 1.00 81.24  ? 130 ALA B N   1 
ATOM   4853  C  CA  . ALA B 1 172 ? 117.633 91.376  145.608 1.00 79.29  ? 130 ALA B CA  1 
ATOM   4854  C  C   . ALA B 1 172 ? 116.680 90.601  146.507 1.00 80.68  ? 130 ALA B C   1 
ATOM   4855  O  O   . ALA B 1 172 ? 116.942 90.439  147.704 1.00 81.04  ? 130 ALA B O   1 
ATOM   4856  C  CB  . ALA B 1 172 ? 117.196 92.834  145.490 1.00 71.06  ? 130 ALA B CB  1 
ATOM   4857  N  N   . ALA B 1 173 ? 115.569 90.112  145.952 1.00 81.79  ? 131 ALA B N   1 
ATOM   4858  C  CA  . ALA B 1 173 ? 114.605 89.349  146.734 1.00 77.89  ? 131 ALA B CA  1 
ATOM   4859  C  C   . ALA B 1 173 ? 115.165 88.026  147.237 1.00 76.10  ? 131 ALA B C   1 
ATOM   4860  O  O   . ALA B 1 173 ? 114.554 87.411  148.116 1.00 77.27  ? 131 ALA B O   1 
ATOM   4861  C  CB  . ALA B 1 173 ? 113.345 89.094  145.909 1.00 75.30  ? 131 ALA B CB  1 
ATOM   4862  N  N   . THR B 1 174 ? 116.296 87.569  146.696 1.00 79.00  ? 132 THR B N   1 
ATOM   4863  C  CA  . THR B 1 174 ? 116.925 86.356  147.204 1.00 80.34  ? 132 THR B CA  1 
ATOM   4864  C  C   . THR B 1 174 ? 117.376 86.532  148.649 1.00 84.96  ? 132 THR B C   1 
ATOM   4865  O  O   . THR B 1 174 ? 117.202 85.630  149.476 1.00 86.85  ? 132 THR B O   1 
ATOM   4866  C  CB  . THR B 1 174 ? 118.107 85.972  146.313 1.00 79.69  ? 132 THR B CB  1 
ATOM   4867  O  OG1 . THR B 1 174 ? 117.624 85.316  145.135 1.00 83.47  ? 132 THR B OG1 1 
ATOM   4868  C  CG2 . THR B 1 174 ? 119.063 85.049  147.046 1.00 76.15  ? 132 THR B CG2 1 
ATOM   4869  N  N   . TYR B 1 175 ? 117.947 87.695  148.975 1.00 80.70  ? 133 TYR B N   1 
ATOM   4870  C  CA  . TYR B 1 175 ? 118.467 87.918  150.321 1.00 75.86  ? 133 TYR B CA  1 
ATOM   4871  C  C   . TYR B 1 175 ? 117.356 87.899  151.363 1.00 78.24  ? 133 TYR B C   1 
ATOM   4872  O  O   . TYR B 1 175 ? 117.528 87.337  152.450 1.00 79.03  ? 133 TYR B O   1 
ATOM   4873  C  CB  . TYR B 1 175 ? 119.234 89.236  150.373 1.00 71.47  ? 133 TYR B CB  1 
ATOM   4874  C  CG  . TYR B 1 175 ? 120.493 89.224  149.544 1.00 73.09  ? 133 TYR B CG  1 
ATOM   4875  C  CD1 . TYR B 1 175 ? 121.698 88.810  150.088 1.00 73.31  ? 133 TYR B CD1 1 
ATOM   4876  C  CD2 . TYR B 1 175 ? 120.476 89.616  148.216 1.00 73.48  ? 133 TYR B CD2 1 
ATOM   4877  C  CE1 . TYR B 1 175 ? 122.851 88.792  149.335 1.00 71.01  ? 133 TYR B CE1 1 
ATOM   4878  C  CE2 . TYR B 1 175 ? 121.624 89.603  147.454 1.00 76.60  ? 133 TYR B CE2 1 
ATOM   4879  C  CZ  . TYR B 1 175 ? 122.809 89.189  148.018 1.00 77.15  ? 133 TYR B CZ  1 
ATOM   4880  O  OH  . TYR B 1 175 ? 123.958 89.173  147.264 1.00 82.01  ? 133 TYR B OH  1 
ATOM   4881  N  N   . VAL B 1 176 ? 116.211 88.506  151.057 1.00 85.81  ? 134 VAL B N   1 
ATOM   4882  C  CA  . VAL B 1 176 ? 115.061 88.484  151.964 1.00 83.66  ? 134 VAL B CA  1 
ATOM   4883  C  C   . VAL B 1 176 ? 114.189 87.294  151.555 1.00 84.86  ? 134 VAL B C   1 
ATOM   4884  O  O   . VAL B 1 176 ? 113.388 87.344  150.623 1.00 87.30  ? 134 VAL B O   1 
ATOM   4885  C  CB  . VAL B 1 176 ? 114.329 89.833  152.005 1.00 81.47  ? 134 VAL B CB  1 
ATOM   4886  C  CG1 . VAL B 1 176 ? 115.350 90.948  152.082 1.00 85.21  ? 134 VAL B CG1 1 
ATOM   4887  C  CG2 . VAL B 1 176 ? 113.465 90.101  150.784 1.00 78.07  ? 134 VAL B CG2 1 
ATOM   4888  N  N   . GLN B 1 177 ? 114.405 86.172  152.239 1.00 89.25  ? 135 GLN B N   1 
ATOM   4889  C  CA  . GLN B 1 177 ? 113.680 84.944  151.942 1.00 88.72  ? 135 GLN B CA  1 
ATOM   4890  C  C   . GLN B 1 177 ? 113.157 84.316  153.224 1.00 89.63  ? 135 GLN B C   1 
ATOM   4891  O  O   . GLN B 1 177 ? 112.106 83.669  153.225 1.00 90.11  ? 135 GLN B O   1 
ATOM   4892  C  CB  . GLN B 1 177 ? 114.579 83.952  151.205 1.00 86.12  ? 135 GLN B CB  1 
ATOM   4893  C  CG  . GLN B 1 177 ? 114.275 83.806  149.731 1.00 86.09  ? 135 GLN B CG  1 
ATOM   4894  C  CD  . GLN B 1 177 ? 115.250 82.878  149.041 1.00 91.17  ? 135 GLN B CD  1 
ATOM   4895  O  OE1 . GLN B 1 177 ? 116.216 82.417  149.647 1.00 93.13  ? 135 GLN B OE1 1 
ATOM   4896  N  NE2 . GLN B 1 177 ? 115.006 82.600  147.766 1.00 89.60  ? 135 GLN B NE2 1 
ATOM   4897  N  N   . ASN B 1 178 ? 113.889 84.504  154.318 1.00 87.22  ? 136 ASN B N   1 
ATOM   4898  C  CA  . ASN B 1 178 ? 113.548 83.931  155.617 1.00 87.25  ? 136 ASN B CA  1 
ATOM   4899  C  C   . ASN B 1 178 ? 112.975 84.975  156.560 1.00 86.78  ? 136 ASN B C   1 
ATOM   4900  O  O   . ASN B 1 178 ? 113.247 84.945  157.761 1.00 88.45  ? 136 ASN B O   1 
ATOM   4901  C  CB  . ASN B 1 178 ? 114.774 83.270  156.234 1.00 87.50  ? 136 ASN B CB  1 
ATOM   4902  C  CG  . ASN B 1 178 ? 115.748 82.772  155.192 1.00 89.43  ? 136 ASN B CG  1 
ATOM   4903  O  OD1 . ASN B 1 178 ? 115.432 81.875  154.410 1.00 89.41  ? 136 ASN B OD1 1 
ATOM   4904  N  ND2 . ASN B 1 178 ? 116.941 83.352  155.172 1.00 89.15  ? 136 ASN B ND2 1 
ATOM   4905  N  N   . GLN B 1 179 ? 112.180 85.907  156.041 1.00 79.32  ? 137 GLN B N   1 
ATOM   4906  C  CA  . GLN B 1 179 ? 111.670 87.014  156.839 1.00 76.33  ? 137 GLN B CA  1 
ATOM   4907  C  C   . GLN B 1 179 ? 110.953 86.515  158.084 1.00 78.65  ? 137 GLN B C   1 
ATOM   4908  O  O   . GLN B 1 179 ? 109.921 85.847  157.996 1.00 84.24  ? 137 GLN B O   1 
ATOM   4909  C  CB  . GLN B 1 179 ? 110.731 87.868  155.989 1.00 70.07  ? 137 GLN B CB  1 
ATOM   4910  C  CG  . GLN B 1 179 ? 111.195 88.035  154.562 1.00 72.73  ? 137 GLN B CG  1 
ATOM   4911  C  CD  . GLN B 1 179 ? 110.059 88.358  153.626 1.00 79.66  ? 137 GLN B CD  1 
ATOM   4912  O  OE1 . GLN B 1 179 ? 108.901 88.399  154.035 1.00 79.00  ? 137 GLN B OE1 1 
ATOM   4913  N  NE2 . GLN B 1 179 ? 110.381 88.590  152.360 1.00 81.28  ? 137 GLN B NE2 1 
ATOM   4914  N  N   . SER B 1 180 ? 111.511 86.842  159.245 1.00 73.24  ? 138 SER B N   1 
ATOM   4915  C  CA  . SER B 1 180 ? 110.946 86.456  160.526 1.00 74.20  ? 138 SER B CA  1 
ATOM   4916  C  C   . SER B 1 180 ? 110.895 87.669  161.441 1.00 74.95  ? 138 SER B C   1 
ATOM   4917  O  O   . SER B 1 180 ? 111.713 88.585  161.328 1.00 73.06  ? 138 SER B O   1 
ATOM   4918  C  CB  . SER B 1 180 ? 111.761 85.339  161.183 1.00 78.48  ? 138 SER B CB  1 
ATOM   4919  O  OG  . SER B 1 180 ? 110.934 84.498  161.966 1.00 80.89  ? 138 SER B OG  1 
ATOM   4920  N  N   . GLU B 1 181 ? 109.924 87.667  162.354 1.00 88.05  ? 139 GLU B N   1 
ATOM   4921  C  CA  . GLU B 1 181 ? 109.796 88.771  163.297 1.00 87.93  ? 139 GLU B CA  1 
ATOM   4922  C  C   . GLU B 1 181 ? 110.963 88.830  164.272 1.00 88.85  ? 139 GLU B C   1 
ATOM   4923  O  O   . GLU B 1 181 ? 111.143 89.851  164.943 1.00 89.17  ? 139 GLU B O   1 
ATOM   4924  C  CB  . GLU B 1 181 ? 108.477 88.661  164.061 1.00 88.35  ? 139 GLU B CB  1 
ATOM   4925  C  CG  . GLU B 1 181 ? 107.766 89.988  164.263 1.00 88.00  ? 139 GLU B CG  1 
ATOM   4926  C  CD  . GLU B 1 181 ? 106.457 89.839  165.008 1.00 89.45  ? 139 GLU B CD  1 
ATOM   4927  O  OE1 . GLU B 1 181 ? 106.465 89.269  166.115 1.00 90.51  ? 139 GLU B OE1 1 
ATOM   4928  O  OE2 . GLU B 1 181 ? 105.417 90.288  164.488 1.00 90.48  ? 139 GLU B OE2 1 
ATOM   4929  N  N   . ASP B 1 182 ? 111.749 87.760  164.370 1.00 90.13  ? 140 ASP B N   1 
ATOM   4930  C  CA  . ASP B 1 182 ? 112.967 87.752  165.179 1.00 89.65  ? 140 ASP B CA  1 
ATOM   4931  C  C   . ASP B 1 182 ? 114.158 88.072  164.274 1.00 90.73  ? 140 ASP B C   1 
ATOM   4932  O  O   . ASP B 1 182 ? 115.002 87.230  163.965 1.00 89.88  ? 140 ASP B O   1 
ATOM   4933  C  CB  . ASP B 1 182 ? 113.127 86.408  165.879 1.00 89.69  ? 140 ASP B CB  1 
ATOM   4934  C  CG  . ASP B 1 182 ? 114.325 86.365  166.808 1.00 94.19  ? 140 ASP B CG  1 
ATOM   4935  O  OD1 . ASP B 1 182 ? 115.023 87.392  166.946 1.00 90.27  ? 140 ASP B OD1 1 
ATOM   4936  O  OD2 . ASP B 1 182 ? 114.565 85.298  167.410 1.00 93.06  ? 140 ASP B OD2 1 
ATOM   4937  N  N   . CYS B 1 183 ? 114.205 89.331  163.842 1.00 84.14  ? 141 CYS B N   1 
ATOM   4938  C  CA  . CYS B 1 183 ? 115.199 89.787  162.880 1.00 82.70  ? 141 CYS B CA  1 
ATOM   4939  C  C   . CYS B 1 183 ? 116.217 90.743  163.481 1.00 78.22  ? 141 CYS B C   1 
ATOM   4940  O  O   . CYS B 1 183 ? 117.035 91.298  162.744 1.00 76.43  ? 141 CYS B O   1 
ATOM   4941  C  CB  . CYS B 1 183 ? 114.510 90.451  161.690 1.00 80.50  ? 141 CYS B CB  1 
ATOM   4942  S  SG  . CYS B 1 183 ? 113.498 91.878  162.112 1.00 80.73  ? 141 CYS B SG  1 
ATOM   4943  N  N   . LEU B 1 184 ? 116.195 90.948  164.793 1.00 70.64  ? 142 LEU B N   1 
ATOM   4944  C  CA  . LEU B 1 184 ? 117.116 91.880  165.440 1.00 67.70  ? 142 LEU B CA  1 
ATOM   4945  C  C   . LEU B 1 184 ? 118.474 91.205  165.579 1.00 71.49  ? 142 LEU B C   1 
ATOM   4946  O  O   . LEU B 1 184 ? 118.758 90.519  166.560 1.00 76.08  ? 142 LEU B O   1 
ATOM   4947  C  CB  . LEU B 1 184 ? 116.567 92.327  166.787 1.00 69.02  ? 142 LEU B CB  1 
ATOM   4948  C  CG  . LEU B 1 184 ? 115.223 93.053  166.745 1.00 67.08  ? 142 LEU B CG  1 
ATOM   4949  C  CD1 . LEU B 1 184 ? 114.927 93.707  168.077 1.00 65.79  ? 142 LEU B CD1 1 
ATOM   4950  C  CD2 . LEU B 1 184 ? 115.216 94.082  165.642 1.00 65.65  ? 142 LEU B CD2 1 
ATOM   4951  N  N   . TYR B 1 185 ? 119.327 91.404  164.578 1.00 65.10  ? 143 TYR B N   1 
ATOM   4952  C  CA  . TYR B 1 185 ? 120.673 90.852  164.587 1.00 64.11  ? 143 TYR B CA  1 
ATOM   4953  C  C   . TYR B 1 185 ? 121.605 91.824  163.880 1.00 66.98  ? 143 TYR B C   1 
ATOM   4954  O  O   . TYR B 1 185 ? 121.173 92.641  163.065 1.00 73.16  ? 143 TYR B O   1 
ATOM   4955  C  CB  . TYR B 1 185 ? 120.724 89.482  163.907 1.00 68.65  ? 143 TYR B CB  1 
ATOM   4956  C  CG  . TYR B 1 185 ? 119.938 88.397  164.608 1.00 70.00  ? 143 TYR B CG  1 
ATOM   4957  C  CD1 . TYR B 1 185 ? 120.377 87.858  165.804 1.00 67.98  ? 143 TYR B CD1 1 
ATOM   4958  C  CD2 . TYR B 1 185 ? 118.762 87.906  164.065 1.00 71.89  ? 143 TYR B CD2 1 
ATOM   4959  C  CE1 . TYR B 1 185 ? 119.665 86.868  166.443 1.00 69.96  ? 143 TYR B CE1 1 
ATOM   4960  C  CE2 . TYR B 1 185 ? 118.046 86.914  164.696 1.00 66.56  ? 143 TYR B CE2 1 
ATOM   4961  C  CZ  . TYR B 1 185 ? 118.501 86.401  165.884 1.00 68.38  ? 143 TYR B CZ  1 
ATOM   4962  O  OH  . TYR B 1 185 ? 117.786 85.414  166.514 1.00 77.26  ? 143 TYR B OH  1 
ATOM   4963  N  N   . LEU B 1 186 ? 122.895 91.731  164.199 1.00 63.50  ? 144 LEU B N   1 
ATOM   4964  C  CA  . LEU B 1 186 ? 123.900 92.565  163.557 1.00 59.96  ? 144 LEU B CA  1 
ATOM   4965  C  C   . LEU B 1 186 ? 125.117 91.721  163.213 1.00 60.76  ? 144 LEU B C   1 
ATOM   4966  O  O   . LEU B 1 186 ? 125.407 90.725  163.878 1.00 65.74  ? 144 LEU B O   1 
ATOM   4967  C  CB  . LEU B 1 186 ? 124.305 93.758  164.436 1.00 55.35  ? 144 LEU B CB  1 
ATOM   4968  C  CG  . LEU B 1 186 ? 124.940 93.529  165.804 1.00 52.15  ? 144 LEU B CG  1 
ATOM   4969  C  CD1 . LEU B 1 186 ? 126.446 93.512  165.705 1.00 58.33  ? 144 LEU B CD1 1 
ATOM   4970  C  CD2 . LEU B 1 186 ? 124.501 94.618  166.753 1.00 58.25  ? 144 LEU B CD2 1 
ATOM   4971  N  N   . ASN B 1 187 ? 125.829 92.136  162.167 1.00 53.60  ? 145 ASN B N   1 
ATOM   4972  C  CA  . ASN B 1 187 ? 126.948 91.398  161.604 1.00 50.00  ? 145 ASN B CA  1 
ATOM   4973  C  C   . ASN B 1 187 ? 128.200 92.252  161.702 1.00 53.26  ? 145 ASN B C   1 
ATOM   4974  O  O   . ASN B 1 187 ? 128.215 93.385  161.212 1.00 64.12  ? 145 ASN B O   1 
ATOM   4975  C  CB  . ASN B 1 187 ? 126.678 91.053  160.141 1.00 48.20  ? 145 ASN B CB  1 
ATOM   4976  C  CG  . ASN B 1 187 ? 125.272 90.553  159.912 1.00 55.93  ? 145 ASN B CG  1 
ATOM   4977  O  OD1 . ASN B 1 187 ? 124.625 90.051  160.824 1.00 65.26  ? 145 ASN B OD1 1 
ATOM   4978  N  ND2 . ASN B 1 187 ? 124.787 90.699  158.688 1.00 55.25  ? 145 ASN B ND2 1 
ATOM   4979  N  N   . LEU B 1 188 ? 129.248 91.706  162.311 1.00 51.29  ? 146 LEU B N   1 
ATOM   4980  C  CA  . LEU B 1 188 ? 130.524 92.389  162.455 1.00 50.52  ? 146 LEU B CA  1 
ATOM   4981  C  C   . LEU B 1 188 ? 131.543 91.794  161.496 1.00 57.31  ? 146 LEU B C   1 
ATOM   4982  O  O   . LEU B 1 188 ? 131.519 90.595  161.211 1.00 69.07  ? 146 LEU B O   1 
ATOM   4983  C  CB  . LEU B 1 188 ? 131.055 92.282  163.885 1.00 43.85  ? 146 LEU B CB  1 
ATOM   4984  C  CG  . LEU B 1 188 ? 130.145 92.758  165.013 1.00 45.28  ? 146 LEU B CG  1 
ATOM   4985  C  CD1 . LEU B 1 188 ? 129.594 91.579  165.782 1.00 50.66  ? 146 LEU B CD1 1 
ATOM   4986  C  CD2 . LEU B 1 188 ? 130.905 93.677  165.934 1.00 53.76  ? 146 LEU B CD2 1 
ATOM   4987  N  N   . TYR B 1 189 ? 132.446 92.638  160.995 1.00 54.00  ? 147 TYR B N   1 
ATOM   4988  C  CA  . TYR B 1 189 ? 133.526 92.186  160.116 1.00 47.00  ? 147 TYR B CA  1 
ATOM   4989  C  C   . TYR B 1 189 ? 134.846 92.744  160.641 1.00 53.56  ? 147 TYR B C   1 
ATOM   4990  O  O   . TYR B 1 189 ? 135.291 93.808  160.211 1.00 56.47  ? 147 TYR B O   1 
ATOM   4991  C  CB  . TYR B 1 189 ? 133.269 92.612  158.680 1.00 51.26  ? 147 TYR B CB  1 
ATOM   4992  C  CG  . TYR B 1 189 ? 131.936 92.162  158.130 1.00 52.34  ? 147 TYR B CG  1 
ATOM   4993  C  CD1 . TYR B 1 189 ? 130.784 92.893  158.363 1.00 49.11  ? 147 TYR B CD1 1 
ATOM   4994  C  CD2 . TYR B 1 189 ? 131.832 91.010  157.369 1.00 55.68  ? 147 TYR B CD2 1 
ATOM   4995  C  CE1 . TYR B 1 189 ? 129.570 92.488  157.861 1.00 53.15  ? 147 TYR B CE1 1 
ATOM   4996  C  CE2 . TYR B 1 189 ? 130.621 90.598  156.862 1.00 53.64  ? 147 TYR B CE2 1 
ATOM   4997  C  CZ  . TYR B 1 189 ? 129.493 91.342  157.112 1.00 52.43  ? 147 TYR B CZ  1 
ATOM   4998  O  OH  . TYR B 1 189 ? 128.279 90.939  156.611 1.00 56.26  ? 147 TYR B OH  1 
ATOM   4999  N  N   . VAL B 1 190 ? 135.475 92.017  161.559 1.00 56.98  ? 148 VAL B N   1 
ATOM   5000  C  CA  . VAL B 1 190 ? 136.714 92.464  162.192 1.00 55.98  ? 148 VAL B CA  1 
ATOM   5001  C  C   . VAL B 1 190 ? 137.899 92.139  161.289 1.00 66.57  ? 148 VAL B C   1 
ATOM   5002  O  O   . VAL B 1 190 ? 138.081 90.977  160.906 1.00 72.26  ? 148 VAL B O   1 
ATOM   5003  C  CB  . VAL B 1 190 ? 136.889 91.819  163.574 1.00 54.70  ? 148 VAL B CB  1 
ATOM   5004  C  CG1 . VAL B 1 190 ? 138.010 92.496  164.334 1.00 57.87  ? 148 VAL B CG1 1 
ATOM   5005  C  CG2 . VAL B 1 190 ? 135.595 91.888  164.356 1.00 55.24  ? 148 VAL B CG2 1 
ATOM   5006  N  N   . PRO B 1 191 ? 138.726 93.112  160.930 1.00 65.30  ? 149 PRO B N   1 
ATOM   5007  C  CA  . PRO B 1 191 ? 139.889 92.828  160.086 1.00 64.69  ? 149 PRO B CA  1 
ATOM   5008  C  C   . PRO B 1 191 ? 141.025 92.216  160.894 1.00 72.90  ? 149 PRO B C   1 
ATOM   5009  O  O   . PRO B 1 191 ? 141.024 92.210  162.125 1.00 75.59  ? 149 PRO B O   1 
ATOM   5010  C  CB  . PRO B 1 191 ? 140.270 94.208  159.557 1.00 59.12  ? 149 PRO B CB  1 
ATOM   5011  C  CG  . PRO B 1 191 ? 139.897 95.114  160.664 1.00 60.88  ? 149 PRO B CG  1 
ATOM   5012  C  CD  . PRO B 1 191 ? 138.652 94.537  161.288 1.00 61.07  ? 149 PRO B CD  1 
ATOM   5013  N  N   . THR B 1 192 ? 142.010 91.696  160.169 1.00 80.80  ? 150 THR B N   1 
ATOM   5014  C  CA  . THR B 1 192 ? 143.184 91.099  160.795 1.00 77.29  ? 150 THR B CA  1 
ATOM   5015  C  C   . THR B 1 192 ? 144.466 91.566  160.115 1.00 77.78  ? 150 THR B C   1 
ATOM   5016  O  O   . THR B 1 192 ? 145.161 92.450  160.615 1.00 72.98  ? 150 THR B O   1 
ATOM   5017  C  CB  . THR B 1 192 ? 143.124 89.562  160.756 1.00 73.84  ? 150 THR B CB  1 
ATOM   5018  O  OG1 . THR B 1 192 ? 142.752 89.129  159.443 1.00 73.91  ? 150 THR B OG1 1 
ATOM   5019  C  CG2 . THR B 1 192 ? 142.111 89.043  161.762 1.00 71.50  ? 150 THR B CG2 1 
ATOM   5020  N  N   . SER B 1 199 ? 145.705 103.800 168.574 1.00 94.47  ? 174 SER B N   1 
ATOM   5021  C  CA  . SER B 1 199 ? 146.000 103.111 167.323 1.00 94.90  ? 174 SER B CA  1 
ATOM   5022  C  C   . SER B 1 199 ? 145.732 101.616 167.447 1.00 97.73  ? 174 SER B C   1 
ATOM   5023  O  O   . SER B 1 199 ? 145.331 100.969 166.479 1.00 96.73  ? 174 SER B O   1 
ATOM   5024  C  CB  . SER B 1 199 ? 147.452 103.352 166.906 1.00 93.28  ? 174 SER B CB  1 
ATOM   5025  O  OG  . SER B 1 199 ? 147.739 102.721 165.670 1.00 92.02  ? 174 SER B OG  1 
ATOM   5026  N  N   . GLY B 1 200 ? 145.959 101.074 168.646 1.00 96.14  ? 175 GLY B N   1 
ATOM   5027  C  CA  . GLY B 1 200 ? 145.728 99.654  168.860 1.00 92.42  ? 175 GLY B CA  1 
ATOM   5028  C  C   . GLY B 1 200 ? 144.281 99.256  168.643 1.00 92.73  ? 175 GLY B C   1 
ATOM   5029  O  O   . GLY B 1 200 ? 143.995 98.223  168.032 1.00 90.59  ? 175 GLY B O   1 
ATOM   5030  N  N   . LYS B 1 201 ? 143.351 100.064 169.142 1.00 88.00  ? 176 LYS B N   1 
ATOM   5031  C  CA  . LYS B 1 201 ? 141.938 99.828  168.906 1.00 88.25  ? 176 LYS B CA  1 
ATOM   5032  C  C   . LYS B 1 201 ? 141.562 100.243 167.489 1.00 88.15  ? 176 LYS B C   1 
ATOM   5033  O  O   . LYS B 1 201 ? 142.198 101.110 166.884 1.00 84.71  ? 176 LYS B O   1 
ATOM   5034  C  CB  . LYS B 1 201 ? 141.093 100.595 169.921 1.00 86.12  ? 176 LYS B CB  1 
ATOM   5035  C  CG  . LYS B 1 201 ? 141.115 100.006 171.319 1.00 84.32  ? 176 LYS B CG  1 
ATOM   5036  C  CD  . LYS B 1 201 ? 140.372 100.900 172.298 1.00 89.46  ? 176 LYS B CD  1 
ATOM   5037  C  CE  . LYS B 1 201 ? 139.829 100.107 173.471 1.00 88.54  ? 176 LYS B CE  1 
ATOM   5038  N  NZ  . LYS B 1 201 ? 138.895 100.922 174.294 1.00 86.25  ? 176 LYS B NZ  1 
ATOM   5039  N  N   . LYS B 1 202 ? 140.512 99.608  166.958 1.00 70.27  ? 177 LYS B N   1 
ATOM   5040  C  CA  . LYS B 1 202 ? 140.110 99.899  165.594 1.00 67.20  ? 177 LYS B CA  1 
ATOM   5041  C  C   . LYS B 1 202 ? 138.844 100.746 165.569 1.00 71.26  ? 177 LYS B C   1 
ATOM   5042  O  O   . LYS B 1 202 ? 138.013 100.660 166.477 1.00 70.70  ? 177 LYS B O   1 
ATOM   5043  C  CB  . LYS B 1 202 ? 139.858 98.607  164.813 1.00 67.49  ? 177 LYS B CB  1 
ATOM   5044  C  CG  . LYS B 1 202 ? 141.097 97.788  164.527 1.00 69.03  ? 177 LYS B CG  1 
ATOM   5045  C  CD  . LYS B 1 202 ? 140.718 96.397  164.057 1.00 69.44  ? 177 LYS B CD  1 
ATOM   5046  C  CE  . LYS B 1 202 ? 141.937 95.511  163.902 1.00 69.21  ? 177 LYS B CE  1 
ATOM   5047  N  NZ  . LYS B 1 202 ? 142.909 96.080  162.933 1.00 73.05  ? 177 LYS B NZ  1 
ATOM   5048  N  N   . PRO B 1 203 ? 138.683 101.579 164.546 1.00 66.97  ? 178 PRO B N   1 
ATOM   5049  C  CA  . PRO B 1 203 ? 137.433 102.325 164.389 1.00 59.94  ? 178 PRO B CA  1 
ATOM   5050  C  C   . PRO B 1 203 ? 136.281 101.409 164.013 1.00 60.31  ? 178 PRO B C   1 
ATOM   5051  O  O   . PRO B 1 203 ? 136.464 100.324 163.460 1.00 65.64  ? 178 PRO B O   1 
ATOM   5052  C  CB  . PRO B 1 203 ? 137.748 103.309 163.259 1.00 58.76  ? 178 PRO B CB  1 
ATOM   5053  C  CG  . PRO B 1 203 ? 139.235 103.380 163.220 1.00 58.70  ? 178 PRO B CG  1 
ATOM   5054  C  CD  . PRO B 1 203 ? 139.700 102.014 163.579 1.00 65.75  ? 178 PRO B CD  1 
ATOM   5055  N  N   . VAL B 1 204 ? 135.073 101.869 164.323 1.00 45.76  ? 179 VAL B N   1 
ATOM   5056  C  CA  . VAL B 1 204 ? 133.844 101.139 164.040 1.00 42.66  ? 179 VAL B CA  1 
ATOM   5057  C  C   . VAL B 1 204 ? 133.011 101.961 163.070 1.00 48.07  ? 179 VAL B C   1 
ATOM   5058  O  O   . VAL B 1 204 ? 132.922 103.184 163.204 1.00 61.04  ? 179 VAL B O   1 
ATOM   5059  C  CB  . VAL B 1 204 ? 133.048 100.848 165.328 1.00 39.47  ? 179 VAL B CB  1 
ATOM   5060  C  CG1 . VAL B 1 204 ? 131.863 99.953  165.031 1.00 44.93  ? 179 VAL B CG1 1 
ATOM   5061  C  CG2 . VAL B 1 204 ? 133.943 100.214 166.367 1.00 46.52  ? 179 VAL B CG2 1 
ATOM   5062  N  N   . MET B 1 205 ? 132.414 101.294 162.087 1.00 37.56  ? 180 MET B N   1 
ATOM   5063  C  CA  . MET B 1 205 ? 131.530 101.939 161.121 1.00 30.46  ? 180 MET B CA  1 
ATOM   5064  C  C   . MET B 1 205 ? 130.246 101.131 161.029 1.00 45.14  ? 180 MET B C   1 
ATOM   5065  O  O   . MET B 1 205 ? 130.234 100.045 160.443 1.00 66.26  ? 180 MET B O   1 
ATOM   5066  C  CB  . MET B 1 205 ? 132.193 102.057 159.751 1.00 33.48  ? 180 MET B CB  1 
ATOM   5067  C  CG  . MET B 1 205 ? 133.465 102.876 159.741 1.00 45.53  ? 180 MET B CG  1 
ATOM   5068  S  SD  . MET B 1 205 ? 134.166 103.038 158.094 1.00 60.75  ? 180 MET B SD  1 
ATOM   5069  C  CE  . MET B 1 205 ? 132.804 103.802 157.237 1.00 34.92  ? 180 MET B CE  1 
ATOM   5070  N  N   . LEU B 1 206 ? 129.176 101.645 161.624 1.00 35.86  ? 181 LEU B N   1 
ATOM   5071  C  CA  . LEU B 1 206 ? 127.862 101.035 161.509 1.00 27.85  ? 181 LEU B CA  1 
ATOM   5072  C  C   . LEU B 1 206 ? 127.195 101.507 160.226 1.00 27.24  ? 181 LEU B C   1 
ATOM   5073  O  O   . LEU B 1 206 ? 127.364 102.655 159.814 1.00 44.67  ? 181 LEU B O   1 
ATOM   5074  C  CB  . LEU B 1 206 ? 127.004 101.401 162.720 1.00 26.02  ? 181 LEU B CB  1 
ATOM   5075  C  CG  . LEU B 1 206 ? 125.637 100.744 162.890 1.00 36.21  ? 181 LEU B CG  1 
ATOM   5076  C  CD1 . LEU B 1 206 ? 125.774 99.376  163.506 1.00 45.87  ? 181 LEU B CD1 1 
ATOM   5077  C  CD2 . LEU B 1 206 ? 124.749 101.610 163.751 1.00 36.94  ? 181 LEU B CD2 1 
ATOM   5078  N  N   . PHE B 1 207 ? 126.463 100.612 159.578 1.00 32.60  ? 182 PHE B N   1 
ATOM   5079  C  CA  . PHE B 1 207 ? 125.764 100.937 158.343 1.00 37.43  ? 182 PHE B CA  1 
ATOM   5080  C  C   . PHE B 1 207 ? 124.264 100.882 158.588 1.00 44.54  ? 182 PHE B C   1 
ATOM   5081  O  O   . PHE B 1 207 ? 123.733 99.829  158.953 1.00 57.75  ? 182 PHE B O   1 
ATOM   5082  C  CB  . PHE B 1 207 ? 126.155 99.986  157.214 1.00 37.46  ? 182 PHE B CB  1 
ATOM   5083  C  CG  . PHE B 1 207 ? 125.561 100.355 155.887 1.00 31.67  ? 182 PHE B CG  1 
ATOM   5084  C  CD1 . PHE B 1 207 ? 126.069 101.409 155.158 1.00 44.96  ? 182 PHE B CD1 1 
ATOM   5085  C  CD2 . PHE B 1 207 ? 124.494 99.657  155.372 1.00 42.49  ? 182 PHE B CD2 1 
ATOM   5086  C  CE1 . PHE B 1 207 ? 125.524 101.756 153.943 1.00 47.45  ? 182 PHE B CE1 1 
ATOM   5087  C  CE2 . PHE B 1 207 ? 123.950 100.003 154.158 1.00 46.34  ? 182 PHE B CE2 1 
ATOM   5088  C  CZ  . PHE B 1 207 ? 124.466 101.054 153.446 1.00 42.29  ? 182 PHE B CZ  1 
ATOM   5089  N  N   . LEU B 1 208 ? 123.587 102.007 158.376 1.00 28.42  ? 183 LEU B N   1 
ATOM   5090  C  CA  . LEU B 1 208 ? 122.139 102.108 158.541 1.00 22.85  ? 183 LEU B CA  1 
ATOM   5091  C  C   . LEU B 1 208 ? 121.502 102.010 157.161 1.00 37.56  ? 183 LEU B C   1 
ATOM   5092  O  O   . LEU B 1 208 ? 121.328 103.017 156.473 1.00 49.44  ? 183 LEU B O   1 
ATOM   5093  C  CB  . LEU B 1 208 ? 121.766 103.409 159.239 1.00 27.31  ? 183 LEU B CB  1 
ATOM   5094  C  CG  . LEU B 1 208 ? 121.856 103.426 160.763 1.00 26.94  ? 183 LEU B CG  1 
ATOM   5095  C  CD1 . LEU B 1 208 ? 123.249 103.775 161.207 1.00 35.91  ? 183 LEU B CD1 1 
ATOM   5096  C  CD2 . LEU B 1 208 ? 120.878 104.421 161.323 1.00 39.82  ? 183 LEU B CD2 1 
ATOM   5097  N  N   . HIS B 1 209 ? 121.138 100.794 156.766 1.00 53.40  ? 184 HIS B N   1 
ATOM   5098  C  CA  . HIS B 1 209 ? 120.649 100.516 155.425 1.00 55.41  ? 184 HIS B CA  1 
ATOM   5099  C  C   . HIS B 1 209 ? 119.228 101.036 155.240 1.00 60.44  ? 184 HIS B C   1 
ATOM   5100  O  O   . HIS B 1 209 ? 118.635 101.646 156.132 1.00 72.27  ? 184 HIS B O   1 
ATOM   5101  C  CB  . HIS B 1 209 ? 120.689 99.017  155.157 1.00 56.72  ? 184 HIS B CB  1 
ATOM   5102  C  CG  . HIS B 1 209 ? 119.742 98.237  156.008 1.00 56.82  ? 184 HIS B CG  1 
ATOM   5103  N  ND1 . HIS B 1 209 ? 118.462 97.929  155.604 1.00 60.06  ? 184 HIS B ND1 1 
ATOM   5104  C  CD2 . HIS B 1 209 ? 119.879 97.720  157.251 1.00 63.88  ? 184 HIS B CD2 1 
ATOM   5105  C  CE1 . HIS B 1 209 ? 117.855 97.245  156.557 1.00 64.00  ? 184 HIS B CE1 1 
ATOM   5106  N  NE2 . HIS B 1 209 ? 118.693 97.106  157.568 1.00 69.60  ? 184 HIS B NE2 1 
ATOM   5107  N  N   . GLY B 1 210 ? 118.667 100.772 154.063 1.00 67.46  ? 185 GLY B N   1 
ATOM   5108  C  CA  . GLY B 1 210 ? 117.272 101.064 153.798 1.00 63.10  ? 185 GLY B CA  1 
ATOM   5109  C  C   . GLY B 1 210 ? 117.038 102.129 152.749 1.00 65.86  ? 185 GLY B C   1 
ATOM   5110  O  O   . GLY B 1 210 ? 117.142 103.323 153.038 1.00 63.37  ? 185 GLY B O   1 
ATOM   5111  N  N   . GLY B 1 211 ? 116.715 101.710 151.524 1.00 65.21  ? 186 GLY B N   1 
ATOM   5112  C  CA  . GLY B 1 211 ? 116.369 102.676 150.495 1.00 63.33  ? 186 GLY B CA  1 
ATOM   5113  C  C   . GLY B 1 211 ? 115.091 103.426 150.817 1.00 62.52  ? 186 GLY B C   1 
ATOM   5114  O  O   . GLY B 1 211 ? 115.013 104.643 150.635 1.00 66.89  ? 186 GLY B O   1 
ATOM   5115  N  N   . SER B 1 212 ? 114.072 102.709 151.284 1.00 56.63  ? 187 SER B N   1 
ATOM   5116  C  CA  . SER B 1 212 ? 112.896 103.320 151.886 1.00 52.66  ? 187 SER B CA  1 
ATOM   5117  C  C   . SER B 1 212 ? 112.730 102.725 153.274 1.00 63.84  ? 187 SER B C   1 
ATOM   5118  O  O   . SER B 1 212 ? 113.661 102.103 153.795 1.00 76.45  ? 187 SER B O   1 
ATOM   5119  C  CB  . SER B 1 212 ? 111.645 103.085 151.046 1.00 52.28  ? 187 SER B CB  1 
ATOM   5120  O  OG  . SER B 1 212 ? 111.041 101.853 151.379 1.00 62.84  ? 187 SER B OG  1 
ATOM   5121  N  N   . TYR B 1 213 ? 111.571 102.906 153.893 1.00 48.34  ? 188 TYR B N   1 
ATOM   5122  C  CA  . TYR B 1 213 ? 111.342 102.361 155.222 1.00 49.31  ? 188 TYR B CA  1 
ATOM   5123  C  C   . TYR B 1 213 ? 110.576 101.043 155.202 1.00 52.71  ? 188 TYR B C   1 
ATOM   5124  O  O   . TYR B 1 213 ? 110.177 100.559 156.264 1.00 52.55  ? 188 TYR B O   1 
ATOM   5125  C  CB  . TYR B 1 213 ? 110.608 103.382 156.085 1.00 54.61  ? 188 TYR B CB  1 
ATOM   5126  C  CG  . TYR B 1 213 ? 111.410 104.629 156.373 1.00 55.06  ? 188 TYR B CG  1 
ATOM   5127  C  CD1 . TYR B 1 213 ? 112.453 104.613 157.283 1.00 48.89  ? 188 TYR B CD1 1 
ATOM   5128  C  CD2 . TYR B 1 213 ? 111.116 105.825 155.740 1.00 54.39  ? 188 TYR B CD2 1 
ATOM   5129  C  CE1 . TYR B 1 213 ? 113.180 105.750 157.550 1.00 47.35  ? 188 TYR B CE1 1 
ATOM   5130  C  CE2 . TYR B 1 213 ? 111.838 106.966 156.001 1.00 50.71  ? 188 TYR B CE2 1 
ATOM   5131  C  CZ  . TYR B 1 213 ? 112.867 106.922 156.905 1.00 53.21  ? 188 TYR B CZ  1 
ATOM   5132  O  OH  . TYR B 1 213 ? 113.585 108.060 157.168 1.00 55.08  ? 188 TYR B OH  1 
ATOM   5133  N  N   . MET B 1 214 ? 110.363 100.451 154.026 1.00 69.96  ? 189 MET B N   1 
ATOM   5134  C  CA  . MET B 1 214 ? 109.595 99.218  153.906 1.00 69.96  ? 189 MET B CA  1 
ATOM   5135  C  C   . MET B 1 214 ? 110.432 98.004  153.540 1.00 71.15  ? 189 MET B C   1 
ATOM   5136  O  O   . MET B 1 214 ? 109.918 96.883  153.596 1.00 78.05  ? 189 MET B O   1 
ATOM   5137  C  CB  . MET B 1 214 ? 108.493 99.369  152.847 1.00 70.07  ? 189 MET B CB  1 
ATOM   5138  C  CG  . MET B 1 214 ? 107.638 100.610 152.959 1.00 72.75  ? 189 MET B CG  1 
ATOM   5139  S  SD  . MET B 1 214 ? 106.265 100.436 154.105 1.00 80.45  ? 189 MET B SD  1 
ATOM   5140  C  CE  . MET B 1 214 ? 106.153 102.115 154.701 1.00 71.22  ? 189 MET B CE  1 
ATOM   5141  N  N   . GLU B 1 215 ? 111.692 98.187  153.166 1.00 66.96  ? 190 GLU B N   1 
ATOM   5142  C  CA  . GLU B 1 215 ? 112.441 97.156  152.468 1.00 68.68  ? 190 GLU B CA  1 
ATOM   5143  C  C   . GLU B 1 215 ? 113.908 97.217  152.862 1.00 74.06  ? 190 GLU B C   1 
ATOM   5144  O  O   . GLU B 1 215 ? 114.388 98.209  153.414 1.00 71.18  ? 190 GLU B O   1 
ATOM   5145  C  CB  . GLU B 1 215 ? 112.199 97.293  150.952 1.00 61.60  ? 190 GLU B CB  1 
ATOM   5146  C  CG  . GLU B 1 215 ? 112.751 98.554  150.241 1.00 72.79  ? 190 GLU B CG  1 
ATOM   5147  C  CD  . GLU B 1 215 ? 114.240 98.829  150.378 1.00 78.45  ? 190 GLU B CD  1 
ATOM   5148  O  OE1 . GLU B 1 215 ? 115.027 97.881  150.538 1.00 82.32  ? 190 GLU B OE1 1 
ATOM   5149  O  OE2 . GLU B 1 215 ? 114.629 100.013 150.340 1.00 73.91  ? 190 GLU B OE2 1 
ATOM   5150  N  N   . GLY B 1 216 ? 114.623 96.153  152.536 1.00 67.26  ? 191 GLY B N   1 
ATOM   5151  C  CA  . GLY B 1 216 ? 116.056 96.089  152.711 1.00 64.11  ? 191 GLY B CA  1 
ATOM   5152  C  C   . GLY B 1 216 ? 116.450 95.202  153.877 1.00 66.90  ? 191 GLY B C   1 
ATOM   5153  O  O   . GLY B 1 216 ? 115.653 94.887  154.762 1.00 72.33  ? 191 GLY B O   1 
ATOM   5154  N  N   . THR B 1 217 ? 117.711 94.787  153.858 1.00 64.94  ? 192 THR B N   1 
ATOM   5155  C  CA  . THR B 1 217 ? 118.277 94.039  154.967 1.00 63.56  ? 192 THR B CA  1 
ATOM   5156  C  C   . THR B 1 217 ? 119.784 94.219  154.927 1.00 67.06  ? 192 THR B C   1 
ATOM   5157  O  O   . THR B 1 217 ? 120.355 94.585  153.897 1.00 73.72  ? 192 THR B O   1 
ATOM   5158  C  CB  . THR B 1 217 ? 117.889 92.560  154.909 1.00 68.72  ? 192 THR B CB  1 
ATOM   5159  O  OG1 . THR B 1 217 ? 118.064 91.970  156.201 1.00 76.30  ? 192 THR B OG1 1 
ATOM   5160  C  CG2 . THR B 1 217 ? 118.749 91.822  153.907 1.00 69.77  ? 192 THR B CG2 1 
ATOM   5161  N  N   . GLY B 1 218 ? 120.423 93.974  156.066 1.00 61.55  ? 193 GLY B N   1 
ATOM   5162  C  CA  . GLY B 1 218 ? 121.854 94.180  156.153 1.00 65.36  ? 193 GLY B CA  1 
ATOM   5163  C  C   . GLY B 1 218 ? 122.694 93.120  155.488 1.00 66.73  ? 193 GLY B C   1 
ATOM   5164  O  O   . GLY B 1 218 ? 123.903 93.314  155.338 1.00 72.56  ? 193 GLY B O   1 
ATOM   5165  N  N   . ASN B 1 219 ? 122.087 92.006  155.083 1.00 61.21  ? 194 ASN B N   1 
ATOM   5166  C  CA  . ASN B 1 219 ? 122.848 90.923  154.477 1.00 63.67  ? 194 ASN B CA  1 
ATOM   5167  C  C   . ASN B 1 219 ? 123.281 91.243  153.055 1.00 65.56  ? 194 ASN B C   1 
ATOM   5168  O  O   . ASN B 1 219 ? 124.232 90.629  152.560 1.00 73.37  ? 194 ASN B O   1 
ATOM   5169  C  CB  . ASN B 1 219 ? 122.026 89.638  154.489 1.00 68.54  ? 194 ASN B CB  1 
ATOM   5170  C  CG  . ASN B 1 219 ? 121.194 89.495  155.742 1.00 71.37  ? 194 ASN B CG  1 
ATOM   5171  O  OD1 . ASN B 1 219 ? 121.590 89.939  156.818 1.00 67.87  ? 194 ASN B OD1 1 
ATOM   5172  N  ND2 . ASN B 1 219 ? 120.031 88.873  155.610 1.00 74.19  ? 194 ASN B ND2 1 
ATOM   5173  N  N   . MET B 1 220 ? 122.611 92.183  152.387 1.00 65.13  ? 195 MET B N   1 
ATOM   5174  C  CA  . MET B 1 220 ? 122.953 92.487  151.003 1.00 70.77  ? 195 MET B CA  1 
ATOM   5175  C  C   . MET B 1 220 ? 124.326 93.133  150.888 1.00 70.30  ? 195 MET B C   1 
ATOM   5176  O  O   . MET B 1 220 ? 124.969 93.036  149.837 1.00 72.72  ? 195 MET B O   1 
ATOM   5177  C  CB  . MET B 1 220 ? 121.894 93.398  150.383 1.00 66.95  ? 195 MET B CB  1 
ATOM   5178  C  CG  . MET B 1 220 ? 120.508 93.217  150.962 1.00 70.13  ? 195 MET B CG  1 
ATOM   5179  S  SD  . MET B 1 220 ? 119.348 94.471  150.402 1.00 65.45  ? 195 MET B SD  1 
ATOM   5180  C  CE  . MET B 1 220 ? 118.859 93.789  148.826 1.00 66.51  ? 195 MET B CE  1 
ATOM   5181  N  N   . PHE B 1 221 ? 124.792 93.785  151.945 1.00 63.52  ? 196 PHE B N   1 
ATOM   5182  C  CA  . PHE B 1 221 ? 126.025 94.564  151.914 1.00 62.77  ? 196 PHE B CA  1 
ATOM   5183  C  C   . PHE B 1 221 ? 127.112 93.787  152.650 1.00 67.07  ? 196 PHE B C   1 
ATOM   5184  O  O   . PHE B 1 221 ? 127.264 93.899  153.866 1.00 73.00  ? 196 PHE B O   1 
ATOM   5185  C  CB  . PHE B 1 221 ? 125.800 95.934  152.529 1.00 63.43  ? 196 PHE B CB  1 
ATOM   5186  C  CG  . PHE B 1 221 ? 124.769 96.750  151.811 1.00 62.39  ? 196 PHE B CG  1 
ATOM   5187  C  CD1 . PHE B 1 221 ? 124.993 97.185  150.520 1.00 66.01  ? 196 PHE B CD1 1 
ATOM   5188  C  CD2 . PHE B 1 221 ? 123.575 97.072  152.424 1.00 61.37  ? 196 PHE B CD2 1 
ATOM   5189  C  CE1 . PHE B 1 221 ? 124.050 97.931  149.858 1.00 63.65  ? 196 PHE B CE1 1 
ATOM   5190  C  CE2 . PHE B 1 221 ? 122.627 97.817  151.764 1.00 62.93  ? 196 PHE B CE2 1 
ATOM   5191  C  CZ  . PHE B 1 221 ? 122.865 98.247  150.480 1.00 65.87  ? 196 PHE B CZ  1 
ATOM   5192  N  N   . ASP B 1 222 ? 127.878 93.001  151.894 1.00 66.24  ? 197 ASP B N   1 
ATOM   5193  C  CA  . ASP B 1 222 ? 128.980 92.220  152.450 1.00 65.95  ? 197 ASP B CA  1 
ATOM   5194  C  C   . ASP B 1 222 ? 130.130 93.177  152.743 1.00 65.09  ? 197 ASP B C   1 
ATOM   5195  O  O   . ASP B 1 222 ? 131.047 93.376  151.942 1.00 68.26  ? 197 ASP B O   1 
ATOM   5196  C  CB  . ASP B 1 222 ? 129.391 91.110  151.491 1.00 68.53  ? 197 ASP B CB  1 
ATOM   5197  C  CG  . ASP B 1 222 ? 130.394 90.152  152.099 1.00 69.91  ? 197 ASP B CG  1 
ATOM   5198  O  OD1 . ASP B 1 222 ? 130.321 89.911  153.321 1.00 74.48  ? 197 ASP B OD1 1 
ATOM   5199  O  OD2 . ASP B 1 222 ? 131.258 89.640  151.355 1.00 63.83  ? 197 ASP B OD2 1 
ATOM   5200  N  N   . GLY B 1 223 ? 130.069 93.789  153.919 1.00 62.56  ? 198 GLY B N   1 
ATOM   5201  C  CA  . GLY B 1 223 ? 131.070 94.759  154.309 1.00 63.80  ? 198 GLY B CA  1 
ATOM   5202  C  C   . GLY B 1 223 ? 132.357 94.129  154.791 1.00 65.78  ? 198 GLY B C   1 
ATOM   5203  O  O   . GLY B 1 223 ? 132.757 94.321  155.942 1.00 66.10  ? 198 GLY B O   1 
ATOM   5204  N  N   . SER B 1 224 ? 133.016 93.372  153.916 1.00 63.66  ? 199 SER B N   1 
ATOM   5205  C  CA  . SER B 1 224 ? 134.270 92.710  154.247 1.00 57.54  ? 199 SER B CA  1 
ATOM   5206  C  C   . SER B 1 224 ? 135.472 93.280  153.518 1.00 60.64  ? 199 SER B C   1 
ATOM   5207  O  O   . SER B 1 224 ? 136.577 93.236  154.057 1.00 65.10  ? 199 SER B O   1 
ATOM   5208  C  CB  . SER B 1 224 ? 134.179 91.213  153.941 1.00 57.66  ? 199 SER B CB  1 
ATOM   5209  O  OG  . SER B 1 224 ? 135.449 90.610  154.066 1.00 62.15  ? 199 SER B OG  1 
ATOM   5210  N  N   . VAL B 1 225 ? 135.291 93.792  152.299 1.00 59.02  ? 200 VAL B N   1 
ATOM   5211  C  CA  . VAL B 1 225 ? 136.389 94.460  151.609 1.00 58.20  ? 200 VAL B CA  1 
ATOM   5212  C  C   . VAL B 1 225 ? 136.704 95.787  152.278 1.00 59.55  ? 200 VAL B C   1 
ATOM   5213  O  O   . VAL B 1 225 ? 137.871 96.173  152.406 1.00 64.25  ? 200 VAL B O   1 
ATOM   5214  C  CB  . VAL B 1 225 ? 136.051 94.646  150.122 1.00 54.34  ? 200 VAL B CB  1 
ATOM   5215  C  CG1 . VAL B 1 225 ? 137.246 95.197  149.379 1.00 55.65  ? 200 VAL B CG1 1 
ATOM   5216  C  CG2 . VAL B 1 225 ? 135.611 93.335  149.523 1.00 58.91  ? 200 VAL B CG2 1 
ATOM   5217  N  N   . LEU B 1 226 ? 135.670 96.512  152.704 1.00 56.02  ? 201 LEU B N   1 
ATOM   5218  C  CA  . LEU B 1 226 ? 135.884 97.779  153.392 1.00 48.25  ? 201 LEU B CA  1 
ATOM   5219  C  C   . LEU B 1 226 ? 136.622 97.568  154.706 1.00 54.93  ? 201 LEU B C   1 
ATOM   5220  O  O   . LEU B 1 226 ? 137.490 98.365  155.075 1.00 57.23  ? 201 LEU B O   1 
ATOM   5221  C  CB  . LEU B 1 226 ? 134.544 98.471  153.626 1.00 47.18  ? 201 LEU B CB  1 
ATOM   5222  C  CG  . LEU B 1 226 ? 134.532 99.808  154.357 1.00 48.05  ? 201 LEU B CG  1 
ATOM   5223  C  CD1 . LEU B 1 226 ? 135.400 100.807 153.635 1.00 48.01  ? 201 LEU B CD1 1 
ATOM   5224  C  CD2 . LEU B 1 226 ? 133.116 100.318 154.458 1.00 48.81  ? 201 LEU B CD2 1 
ATOM   5225  N  N   . ALA B 1 227 ? 136.286 96.498  155.429 1.00 61.55  ? 202 ALA B N   1 
ATOM   5226  C  CA  . ALA B 1 227 ? 136.966 96.207  156.685 1.00 61.66  ? 202 ALA B CA  1 
ATOM   5227  C  C   . ALA B 1 227 ? 138.425 95.835  156.461 1.00 63.90  ? 202 ALA B C   1 
ATOM   5228  O  O   . ALA B 1 227 ? 139.306 96.282  157.203 1.00 65.17  ? 202 ALA B O   1 
ATOM   5229  C  CB  . ALA B 1 227 ? 136.240 95.086  157.422 1.00 60.50  ? 202 ALA B CB  1 
ATOM   5230  N  N   . ALA B 1 228 ? 138.701 95.012  155.448 1.00 61.68  ? 203 ALA B N   1 
ATOM   5231  C  CA  . ALA B 1 228 ? 140.062 94.545  155.212 1.00 60.82  ? 203 ALA B CA  1 
ATOM   5232  C  C   . ALA B 1 228 ? 140.946 95.619  154.597 1.00 63.59  ? 203 ALA B C   1 
ATOM   5233  O  O   . ALA B 1 228 ? 142.160 95.615  154.821 1.00 66.43  ? 203 ALA B O   1 
ATOM   5234  C  CB  . ALA B 1 228 ? 140.045 93.314  154.310 1.00 63.29  ? 203 ALA B CB  1 
ATOM   5235  N  N   . TYR B 1 229 ? 140.368 96.536  153.823 1.00 56.71  ? 204 TYR B N   1 
ATOM   5236  C  CA  . TYR B 1 229 ? 141.160 97.576  153.179 1.00 56.65  ? 204 TYR B CA  1 
ATOM   5237  C  C   . TYR B 1 229 ? 141.517 98.686  154.158 1.00 60.30  ? 204 TYR B C   1 
ATOM   5238  O  O   . TYR B 1 229 ? 142.695 98.930  154.436 1.00 69.07  ? 204 TYR B O   1 
ATOM   5239  C  CB  . TYR B 1 229 ? 140.398 98.142  151.980 1.00 50.74  ? 204 TYR B CB  1 
ATOM   5240  C  CG  . TYR B 1 229 ? 141.125 99.235  151.231 1.00 53.76  ? 204 TYR B CG  1 
ATOM   5241  C  CD1 . TYR B 1 229 ? 141.101 100.547 151.678 1.00 53.59  ? 204 TYR B CD1 1 
ATOM   5242  C  CD2 . TYR B 1 229 ? 141.822 98.958  150.066 1.00 57.94  ? 204 TYR B CD2 1 
ATOM   5243  C  CE1 . TYR B 1 229 ? 141.760 101.543 150.998 1.00 58.06  ? 204 TYR B CE1 1 
ATOM   5244  C  CE2 . TYR B 1 229 ? 142.482 99.952  149.377 1.00 59.56  ? 204 TYR B CE2 1 
ATOM   5245  C  CZ  . TYR B 1 229 ? 142.447 101.242 149.848 1.00 56.34  ? 204 TYR B CZ  1 
ATOM   5246  O  OH  . TYR B 1 229 ? 143.103 102.239 149.168 1.00 51.69  ? 204 TYR B OH  1 
ATOM   5247  N  N   . GLY B 1 230 ? 140.512 99.369  154.689 1.00 50.59  ? 205 GLY B N   1 
ATOM   5248  C  CA  . GLY B 1 230 ? 140.766 100.486 155.567 1.00 50.34  ? 205 GLY B CA  1 
ATOM   5249  C  C   . GLY B 1 230 ? 141.103 100.134 156.992 1.00 52.55  ? 205 GLY B C   1 
ATOM   5250  O  O   . GLY B 1 230 ? 141.374 101.037 157.786 1.00 57.56  ? 205 GLY B O   1 
ATOM   5251  N  N   . ASN B 1 231 ? 141.100 98.848  157.339 1.00 54.46  ? 206 ASN B N   1 
ATOM   5252  C  CA  . ASN B 1 231 ? 141.389 98.395  158.699 1.00 61.28  ? 206 ASN B CA  1 
ATOM   5253  C  C   . ASN B 1 231 ? 140.403 98.998  159.699 1.00 61.80  ? 206 ASN B C   1 
ATOM   5254  O  O   . ASN B 1 231 ? 140.786 99.601  160.703 1.00 61.37  ? 206 ASN B O   1 
ATOM   5255  C  CB  . ASN B 1 231 ? 142.837 98.709  159.086 1.00 59.61  ? 206 ASN B CB  1 
ATOM   5256  C  CG  . ASN B 1 231 ? 143.239 98.081  160.401 1.00 62.25  ? 206 ASN B CG  1 
ATOM   5257  O  OD1 . ASN B 1 231 ? 143.873 97.028  160.433 1.00 69.61  ? 206 ASN B OD1 1 
ATOM   5258  N  ND2 . ASN B 1 231 ? 142.874 98.730  161.500 1.00 58.80  ? 206 ASN B ND2 1 
ATOM   5259  N  N   . VAL B 1 232 ? 139.112 98.833  159.409 1.00 56.35  ? 207 VAL B N   1 
ATOM   5260  C  CA  . VAL B 1 232 ? 138.037 99.287  160.278 1.00 55.65  ? 207 VAL B CA  1 
ATOM   5261  C  C   . VAL B 1 232 ? 137.075 98.129  160.495 1.00 54.63  ? 207 VAL B C   1 
ATOM   5262  O  O   . VAL B 1 232 ? 137.055 97.158  159.738 1.00 62.75  ? 207 VAL B O   1 
ATOM   5263  C  CB  . VAL B 1 232 ? 137.287 100.507 159.704 1.00 46.45  ? 207 VAL B CB  1 
ATOM   5264  C  CG1 . VAL B 1 232 ? 138.253 101.627 159.394 1.00 52.06  ? 207 VAL B CG1 1 
ATOM   5265  C  CG2 . VAL B 1 232 ? 136.522 100.116 158.465 1.00 43.64  ? 207 VAL B CG2 1 
ATOM   5266  N  N   . ILE B 1 233 ? 136.276 98.237  161.547 1.00 50.38  ? 208 ILE B N   1 
ATOM   5267  C  CA  . ILE B 1 233 ? 135.304 97.212  161.907 1.00 44.39  ? 208 ILE B CA  1 
ATOM   5268  C  C   . ILE B 1 233 ? 133.952 97.652  161.371 1.00 45.12  ? 208 ILE B C   1 
ATOM   5269  O  O   . ILE B 1 233 ? 133.326 98.561  161.922 1.00 60.54  ? 208 ILE B O   1 
ATOM   5270  C  CB  . ILE B 1 233 ? 135.253 96.994  163.423 1.00 50.62  ? 208 ILE B CB  1 
ATOM   5271  C  CG1 . ILE B 1 233 ? 136.595 96.470  163.929 1.00 51.83  ? 208 ILE B CG1 1 
ATOM   5272  C  CG2 . ILE B 1 233 ? 134.131 96.044  163.788 1.00 49.90  ? 208 ILE B CG2 1 
ATOM   5273  C  CD1 . ILE B 1 233 ? 136.537 95.910  165.321 1.00 50.47  ? 208 ILE B CD1 1 
ATOM   5274  N  N   . VAL B 1 234 ? 133.488 97.015  160.305 1.00 40.57  ? 209 VAL B N   1 
ATOM   5275  C  CA  . VAL B 1 234 ? 132.210 97.360  159.696 1.00 42.34  ? 209 VAL B CA  1 
ATOM   5276  C  C   . VAL B 1 234 ? 131.117 96.501  160.315 1.00 50.50  ? 209 VAL B C   1 
ATOM   5277  O  O   . VAL B 1 234 ? 131.258 95.276  160.425 1.00 57.38  ? 209 VAL B O   1 
ATOM   5278  C  CB  . VAL B 1 234 ? 132.256 97.182  158.172 1.00 41.96  ? 209 VAL B CB  1 
ATOM   5279  C  CG1 . VAL B 1 234 ? 130.907 97.492  157.571 1.00 45.31  ? 209 VAL B CG1 1 
ATOM   5280  C  CG2 . VAL B 1 234 ? 133.305 98.086  157.581 1.00 44.20  ? 209 VAL B CG2 1 
ATOM   5281  N  N   . VAL B 1 235 ? 130.028 97.147  160.726 1.00 37.27  ? 210 VAL B N   1 
ATOM   5282  C  CA  . VAL B 1 235 ? 128.906 96.486  161.378 1.00 29.76  ? 210 VAL B CA  1 
ATOM   5283  C  C   . VAL B 1 235 ? 127.644 96.822  160.602 1.00 27.94  ? 210 VAL B C   1 
ATOM   5284  O  O   . VAL B 1 235 ? 127.262 97.993  160.518 1.00 41.26  ? 210 VAL B O   1 
ATOM   5285  C  CB  . VAL B 1 235 ? 128.759 96.924  162.843 1.00 31.92  ? 210 VAL B CB  1 
ATOM   5286  C  CG1 . VAL B 1 235 ? 127.587 96.221  163.485 1.00 30.40  ? 210 VAL B CG1 1 
ATOM   5287  C  CG2 . VAL B 1 235 ? 130.038 96.657  163.607 1.00 38.26  ? 210 VAL B CG2 1 
ATOM   5288  N  N   . THR B 1 236 ? 126.985 95.803  160.059 1.00 47.17  ? 211 THR B N   1 
ATOM   5289  C  CA  . THR B 1 236 ? 125.730 95.982  159.335 1.00 51.52  ? 211 THR B CA  1 
ATOM   5290  C  C   . THR B 1 236 ? 124.615 95.270  160.083 1.00 52.85  ? 211 THR B C   1 
ATOM   5291  O  O   . THR B 1 236 ? 124.732 94.084  160.393 1.00 56.23  ? 211 THR B O   1 
ATOM   5292  C  CB  . THR B 1 236 ? 125.825 95.453  157.903 1.00 54.37  ? 211 THR B CB  1 
ATOM   5293  O  OG1 . THR B 1 236 ? 125.586 94.043  157.896 1.00 51.21  ? 211 THR B OG1 1 
ATOM   5294  C  CG2 . THR B 1 236 ? 127.193 95.730  157.323 1.00 49.39  ? 211 THR B CG2 1 
ATOM   5295  N  N   . LEU B 1 237 ? 123.531 95.983  160.359 1.00 59.03  ? 212 LEU B N   1 
ATOM   5296  C  CA  . LEU B 1 237 ? 122.496 95.496  161.257 1.00 57.19  ? 212 LEU B CA  1 
ATOM   5297  C  C   . LEU B 1 237 ? 121.172 95.316  160.525 1.00 62.15  ? 212 LEU B C   1 
ATOM   5298  O  O   . LEU B 1 237 ? 121.008 95.714  159.370 1.00 68.10  ? 212 LEU B O   1 
ATOM   5299  C  CB  . LEU B 1 237 ? 122.306 96.453  162.438 1.00 60.49  ? 212 LEU B CB  1 
ATOM   5300  C  CG  . LEU B 1 237 ? 121.336 97.611  162.211 1.00 57.46  ? 212 LEU B CG  1 
ATOM   5301  C  CD1 . LEU B 1 237 ? 120.966 98.233  163.530 1.00 61.06  ? 212 LEU B CD1 1 
ATOM   5302  C  CD2 . LEU B 1 237 ? 121.934 98.652  161.291 1.00 48.61  ? 212 LEU B CD2 1 
ATOM   5303  N  N   . ASN B 1 238 ? 120.223 94.703  161.229 1.00 62.31  ? 213 ASN B N   1 
ATOM   5304  C  CA  . ASN B 1 238 ? 118.839 94.589  160.792 1.00 58.81  ? 213 ASN B CA  1 
ATOM   5305  C  C   . ASN B 1 238 ? 117.938 95.208  161.850 1.00 64.83  ? 213 ASN B C   1 
ATOM   5306  O  O   . ASN B 1 238 ? 118.119 94.958  163.046 1.00 67.69  ? 213 ASN B O   1 
ATOM   5307  C  CB  . ASN B 1 238 ? 118.448 93.131  160.562 1.00 56.10  ? 213 ASN B CB  1 
ATOM   5308  C  CG  . ASN B 1 238 ? 119.099 92.542  159.341 1.00 62.92  ? 213 ASN B CG  1 
ATOM   5309  O  OD1 . ASN B 1 238 ? 118.434 92.253  158.351 1.00 71.99  ? 213 ASN B OD1 1 
ATOM   5310  N  ND2 . ASN B 1 238 ? 120.408 92.356  159.401 1.00 65.03  ? 213 ASN B ND2 1 
ATOM   5311  N  N   . TYR B 1 239 ? 116.973 96.011  161.413 1.00 58.15  ? 214 TYR B N   1 
ATOM   5312  C  CA  . TYR B 1 239 ? 116.055 96.688  162.314 1.00 52.96  ? 214 TYR B CA  1 
ATOM   5313  C  C   . TYR B 1 239 ? 114.636 96.545  161.789 1.00 54.55  ? 214 TYR B C   1 
ATOM   5314  O  O   . TYR B 1 239 ? 114.416 96.312  160.600 1.00 57.70  ? 214 TYR B O   1 
ATOM   5315  C  CB  . TYR B 1 239 ? 116.414 98.169  162.479 1.00 55.25  ? 214 TYR B CB  1 
ATOM   5316  C  CG  . TYR B 1 239 ? 116.364 98.979  161.203 1.00 52.30  ? 214 TYR B CG  1 
ATOM   5317  C  CD1 . TYR B 1 239 ? 117.439 99.005  160.329 1.00 52.54  ? 214 TYR B CD1 1 
ATOM   5318  C  CD2 . TYR B 1 239 ? 115.248 99.734  160.884 1.00 53.70  ? 214 TYR B CD2 1 
ATOM   5319  C  CE1 . TYR B 1 239 ? 117.397 99.748  159.168 1.00 52.56  ? 214 TYR B CE1 1 
ATOM   5320  C  CE2 . TYR B 1 239 ? 115.199 100.480 159.726 1.00 54.37  ? 214 TYR B CE2 1 
ATOM   5321  C  CZ  . TYR B 1 239 ? 116.275 100.485 158.873 1.00 50.55  ? 214 TYR B CZ  1 
ATOM   5322  O  OH  . TYR B 1 239 ? 116.225 101.229 157.720 1.00 50.12  ? 214 TYR B OH  1 
ATOM   5323  N  N   . ARG B 1 240 ? 113.672 96.678  162.698 1.00 59.41  ? 215 ARG B N   1 
ATOM   5324  C  CA  . ARG B 1 240 ? 112.270 96.505  162.342 1.00 56.87  ? 215 ARG B CA  1 
ATOM   5325  C  C   . ARG B 1 240 ? 111.860 97.505  161.271 1.00 57.71  ? 215 ARG B C   1 
ATOM   5326  O  O   . ARG B 1 240 ? 112.146 98.699  161.377 1.00 61.03  ? 215 ARG B O   1 
ATOM   5327  C  CB  . ARG B 1 240 ? 111.395 96.663  163.580 1.00 52.86  ? 215 ARG B CB  1 
ATOM   5328  C  CG  . ARG B 1 240 ? 111.011 95.352  164.225 1.00 53.80  ? 215 ARG B CG  1 
ATOM   5329  C  CD  . ARG B 1 240 ? 110.217 95.588  165.485 1.00 58.21  ? 215 ARG B CD  1 
ATOM   5330  N  NE  . ARG B 1 240 ? 110.991 96.337  166.465 1.00 59.38  ? 215 ARG B NE  1 
ATOM   5331  C  CZ  . ARG B 1 240 ? 110.558 96.648  167.677 1.00 62.32  ? 215 ARG B CZ  1 
ATOM   5332  N  NH1 . ARG B 1 240 ? 109.355 96.291  168.093 1.00 63.18  ? 215 ARG B NH1 1 
ATOM   5333  N  NH2 . ARG B 1 240 ? 111.353 97.332  168.493 1.00 60.72  ? 215 ARG B NH2 1 
ATOM   5334  N  N   . LEU B 1 241 ? 111.173 97.012  160.245 1.00 62.41  ? 216 LEU B N   1 
ATOM   5335  C  CA  . LEU B 1 241 ? 110.904 97.772  159.036 1.00 59.83  ? 216 LEU B CA  1 
ATOM   5336  C  C   . LEU B 1 241 ? 109.410 97.864  158.772 1.00 69.80  ? 216 LEU B C   1 
ATOM   5337  O  O   . LEU B 1 241 ? 108.641 96.972  159.138 1.00 72.03  ? 216 LEU B O   1 
ATOM   5338  C  CB  . LEU B 1 241 ? 111.578 97.129  157.825 1.00 53.60  ? 216 LEU B CB  1 
ATOM   5339  C  CG  . LEU B 1 241 ? 113.095 97.217  157.756 1.00 58.70  ? 216 LEU B CG  1 
ATOM   5340  C  CD1 . LEU B 1 241 ? 113.627 96.139  156.847 1.00 62.71  ? 216 LEU B CD1 1 
ATOM   5341  C  CD2 . LEU B 1 241 ? 113.515 98.580  157.261 1.00 61.96  ? 216 LEU B CD2 1 
ATOM   5342  N  N   . GLY B 1 242 ? 109.013 98.950  158.121 1.00 69.14  ? 217 GLY B N   1 
ATOM   5343  C  CA  . GLY B 1 242 ? 107.655 99.048  157.614 1.00 65.42  ? 217 GLY B CA  1 
ATOM   5344  C  C   . GLY B 1 242 ? 106.630 99.111  158.724 1.00 69.41  ? 217 GLY B C   1 
ATOM   5345  O  O   . GLY B 1 242 ? 106.722 99.931  159.642 1.00 70.38  ? 217 GLY B O   1 
ATOM   5346  N  N   . VAL B 1 243 ? 105.634 98.229  158.638 1.00 65.18  ? 218 VAL B N   1 
ATOM   5347  C  CA  . VAL B 1 243 ? 104.482 98.313  159.526 1.00 61.58  ? 218 VAL B CA  1 
ATOM   5348  C  C   . VAL B 1 243 ? 104.866 97.968  160.957 1.00 65.15  ? 218 VAL B C   1 
ATOM   5349  O  O   . VAL B 1 243 ? 104.410 98.614  161.905 1.00 71.87  ? 218 VAL B O   1 
ATOM   5350  C  CB  . VAL B 1 243 ? 103.354 97.402  159.018 1.00 63.06  ? 218 VAL B CB  1 
ATOM   5351  C  CG1 . VAL B 1 243 ? 102.113 97.604  159.856 1.00 62.46  ? 218 VAL B CG1 1 
ATOM   5352  C  CG2 . VAL B 1 243 ? 103.071 97.678  157.554 1.00 68.97  ? 218 VAL B CG2 1 
ATOM   5353  N  N   . LEU B 1 244 ? 105.696 96.946  161.142 1.00 63.30  ? 219 LEU B N   1 
ATOM   5354  C  CA  . LEU B 1 244 ? 105.974 96.462  162.487 1.00 67.50  ? 219 LEU B CA  1 
ATOM   5355  C  C   . LEU B 1 244 ? 106.946 97.346  163.251 1.00 69.64  ? 219 LEU B C   1 
ATOM   5356  O  O   . LEU B 1 244 ? 107.049 97.212  164.473 1.00 73.40  ? 219 LEU B O   1 
ATOM   5357  C  CB  . LEU B 1 244 ? 106.526 95.040  162.430 1.00 66.70  ? 219 LEU B CB  1 
ATOM   5358  C  CG  . LEU B 1 244 ? 105.730 94.073  161.564 1.00 68.61  ? 219 LEU B CG  1 
ATOM   5359  C  CD1 . LEU B 1 244 ? 106.514 93.766  160.310 1.00 68.36  ? 219 LEU B CD1 1 
ATOM   5360  C  CD2 . LEU B 1 244 ? 105.413 92.809  162.330 1.00 70.29  ? 219 LEU B CD2 1 
ATOM   5361  N  N   . GLY B 1 245 ? 107.658 98.237  162.571 1.00 61.69  ? 220 GLY B N   1 
ATOM   5362  C  CA  . GLY B 1 245 ? 108.669 99.028  163.238 1.00 64.76  ? 220 GLY B CA  1 
ATOM   5363  C  C   . GLY B 1 245 ? 108.440 100.521 163.192 1.00 68.46  ? 220 GLY B C   1 
ATOM   5364  O  O   . GLY B 1 245 ? 109.196 101.281 163.800 1.00 73.13  ? 220 GLY B O   1 
ATOM   5365  N  N   . PHE B 1 246 ? 107.411 100.966 162.473 1.00 61.37  ? 221 PHE B N   1 
ATOM   5366  C  CA  . PHE B 1 246 ? 107.170 102.396 162.348 1.00 59.76  ? 221 PHE B CA  1 
ATOM   5367  C  C   . PHE B 1 246 ? 105.696 102.765 162.462 1.00 57.49  ? 221 PHE B C   1 
ATOM   5368  O  O   . PHE B 1 246 ? 105.356 103.941 162.289 1.00 59.41  ? 221 PHE B O   1 
ATOM   5369  C  CB  . PHE B 1 246 ? 107.736 102.916 161.024 1.00 58.89  ? 221 PHE B CB  1 
ATOM   5370  C  CG  . PHE B 1 246 ? 109.238 102.961 160.983 1.00 54.67  ? 221 PHE B CG  1 
ATOM   5371  C  CD1 . PHE B 1 246 ? 109.946 103.723 161.889 1.00 51.83  ? 221 PHE B CD1 1 
ATOM   5372  C  CD2 . PHE B 1 246 ? 109.939 102.249 160.032 1.00 57.89  ? 221 PHE B CD2 1 
ATOM   5373  C  CE1 . PHE B 1 246 ? 111.322 103.766 161.850 1.00 49.57  ? 221 PHE B CE1 1 
ATOM   5374  C  CE2 . PHE B 1 246 ? 111.315 102.292 159.990 1.00 60.02  ? 221 PHE B CE2 1 
ATOM   5375  C  CZ  . PHE B 1 246 ? 112.005 103.051 160.899 1.00 53.76  ? 221 PHE B CZ  1 
ATOM   5376  N  N   . LEU B 1 247 ? 104.815 101.811 162.748 1.00 66.85  ? 222 LEU B N   1 
ATOM   5377  C  CA  . LEU B 1 247 ? 103.402 102.120 162.916 1.00 71.94  ? 222 LEU B CA  1 
ATOM   5378  C  C   . LEU B 1 247 ? 103.190 102.984 164.150 1.00 77.53  ? 222 LEU B C   1 
ATOM   5379  O  O   . LEU B 1 247 ? 103.750 102.720 165.217 1.00 81.17  ? 222 LEU B O   1 
ATOM   5380  C  CB  . LEU B 1 247 ? 102.588 100.834 163.033 1.00 74.77  ? 222 LEU B CB  1 
ATOM   5381  C  CG  . LEU B 1 247 ? 101.093 100.947 163.326 1.00 75.11  ? 222 LEU B CG  1 
ATOM   5382  C  CD1 . LEU B 1 247 ? 100.315 100.058 162.381 1.00 75.08  ? 222 LEU B CD1 1 
ATOM   5383  C  CD2 . LEU B 1 247 ? 100.794 100.573 164.768 1.00 75.00  ? 222 LEU B CD2 1 
ATOM   5384  N  N   . SER B 1 248 ? 102.368 104.019 164.003 1.00 77.87  ? 223 SER B N   1 
ATOM   5385  C  CA  . SER B 1 248 ? 102.099 104.935 165.099 1.00 77.69  ? 223 SER B CA  1 
ATOM   5386  C  C   . SER B 1 248 ? 100.698 105.499 164.951 1.00 76.80  ? 223 SER B C   1 
ATOM   5387  O  O   . SER B 1 248 ? 100.119 105.503 163.863 1.00 80.60  ? 223 SER B O   1 
ATOM   5388  C  CB  . SER B 1 248 ? 103.115 106.076 165.147 1.00 79.72  ? 223 SER B CB  1 
ATOM   5389  O  OG  . SER B 1 248 ? 102.660 107.114 165.994 1.00 82.16  ? 223 SER B OG  1 
ATOM   5390  N  N   . THR B 1 249 ? 100.159 105.980 166.067 1.00 82.46  ? 224 THR B N   1 
ATOM   5391  C  CA  . THR B 1 249 ? 98.854  106.619 166.089 1.00 83.51  ? 224 THR B CA  1 
ATOM   5392  C  C   . THR B 1 249 ? 98.915  108.063 166.561 1.00 85.79  ? 224 THR B C   1 
ATOM   5393  O  O   . THR B 1 249 ? 97.894  108.757 166.513 1.00 85.70  ? 224 THR B O   1 
ATOM   5394  C  CB  . THR B 1 249 ? 97.886  105.836 166.986 1.00 85.28  ? 224 THR B CB  1 
ATOM   5395  O  OG1 . THR B 1 249 ? 98.330  105.904 168.345 1.00 83.86  ? 224 THR B OG1 1 
ATOM   5396  C  CG2 . THR B 1 249 ? 97.817  104.384 166.558 1.00 84.25  ? 224 THR B CG2 1 
ATOM   5397  N  N   . GLY B 1 250 ? 100.072 108.535 167.006 1.00 87.61  ? 225 GLY B N   1 
ATOM   5398  C  CA  . GLY B 1 250 ? 100.220 109.864 167.568 1.00 85.83  ? 225 GLY B CA  1 
ATOM   5399  C  C   . GLY B 1 250 ? 100.054 109.898 169.071 1.00 86.75  ? 225 GLY B C   1 
ATOM   5400  O  O   . GLY B 1 250 ? 100.804 110.586 169.765 1.00 85.60  ? 225 GLY B O   1 
ATOM   5401  N  N   . ASP B 1 251 ? 99.081  109.154 169.590 1.00 104.34 ? 226 ASP B N   1 
ATOM   5402  C  CA  . ASP B 1 251 ? 98.832  109.098 171.024 1.00 105.54 ? 226 ASP B CA  1 
ATOM   5403  C  C   . ASP B 1 251 ? 99.818  108.132 171.675 1.00 103.89 ? 226 ASP B C   1 
ATOM   5404  O  O   . ASP B 1 251 ? 100.774 107.664 171.052 1.00 103.80 ? 226 ASP B O   1 
ATOM   5405  C  CB  . ASP B 1 251 ? 97.383  108.703 171.294 1.00 104.61 ? 226 ASP B CB  1 
ATOM   5406  C  CG  . ASP B 1 251 ? 96.391  109.665 170.673 1.00 106.95 ? 226 ASP B CG  1 
ATOM   5407  O  OD1 . ASP B 1 251 ? 96.697  110.874 170.608 1.00 107.75 ? 226 ASP B OD1 1 
ATOM   5408  O  OD2 . ASP B 1 251 ? 95.307  109.212 170.251 1.00 105.86 ? 226 ASP B OD2 1 
ATOM   5409  N  N   . GLN B 1 252 ? 99.589  107.813 172.947 1.00 103.58 ? 227 GLN B N   1 
ATOM   5410  C  CA  . GLN B 1 252 ? 100.468 106.909 173.676 1.00 105.36 ? 227 GLN B CA  1 
ATOM   5411  C  C   . GLN B 1 252 ? 100.160 105.441 173.417 1.00 106.41 ? 227 GLN B C   1 
ATOM   5412  O  O   . GLN B 1 252 ? 100.875 104.578 173.936 1.00 105.52 ? 227 GLN B O   1 
ATOM   5413  C  CB  . GLN B 1 252 ? 100.387 107.192 175.177 1.00 105.18 ? 227 GLN B CB  1 
ATOM   5414  C  CG  . GLN B 1 252 ? 101.736 107.243 175.869 1.00 105.78 ? 227 GLN B CG  1 
ATOM   5415  C  CD  . GLN B 1 252 ? 102.389 108.606 175.768 1.00 107.41 ? 227 GLN B CD  1 
ATOM   5416  O  OE1 . GLN B 1 252 ? 101.871 109.507 175.109 1.00 107.01 ? 227 GLN B OE1 1 
ATOM   5417  N  NE2 . GLN B 1 252 ? 103.530 108.767 176.427 1.00 104.43 ? 227 GLN B NE2 1 
ATOM   5418  N  N   . ALA B 1 253 ? 99.115  105.136 172.644 1.00 102.03 ? 228 ALA B N   1 
ATOM   5419  C  CA  . ALA B 1 253 ? 98.842  103.748 172.290 1.00 101.65 ? 228 ALA B CA  1 
ATOM   5420  C  C   . ALA B 1 253 ? 99.976  103.163 171.461 1.00 99.41  ? 228 ALA B C   1 
ATOM   5421  O  O   . ALA B 1 253 ? 100.377 102.012 171.665 1.00 96.14  ? 228 ALA B O   1 
ATOM   5422  C  CB  . ALA B 1 253 ? 97.517  103.649 171.537 1.00 101.00 ? 228 ALA B CB  1 
ATOM   5423  N  N   . ALA B 1 254 ? 100.506 103.944 170.521 1.00 89.38  ? 229 ALA B N   1 
ATOM   5424  C  CA  . ALA B 1 254 ? 101.669 103.536 169.737 1.00 84.87  ? 229 ALA B CA  1 
ATOM   5425  C  C   . ALA B 1 254 ? 102.466 104.801 169.434 1.00 83.92  ? 229 ALA B C   1 
ATOM   5426  O  O   . ALA B 1 254 ? 102.091 105.575 168.550 1.00 85.35  ? 229 ALA B O   1 
ATOM   5427  C  CB  . ALA B 1 254 ? 101.256 102.810 168.465 1.00 84.11  ? 229 ALA B CB  1 
ATOM   5428  N  N   . LYS B 1 255 ? 103.550 105.009 170.182 1.00 80.50  ? 230 LYS B N   1 
ATOM   5429  C  CA  . LYS B 1 255 ? 104.366 106.203 169.990 1.00 81.86  ? 230 LYS B CA  1 
ATOM   5430  C  C   . LYS B 1 255 ? 104.988 106.235 168.600 1.00 81.62  ? 230 LYS B C   1 
ATOM   5431  O  O   . LYS B 1 255 ? 105.010 107.283 167.945 1.00 79.89  ? 230 LYS B O   1 
ATOM   5432  C  CB  . LYS B 1 255 ? 105.451 106.268 171.064 1.00 84.06  ? 230 LYS B CB  1 
ATOM   5433  C  CG  . LYS B 1 255 ? 105.013 106.914 172.365 1.00 80.60  ? 230 LYS B CG  1 
ATOM   5434  C  CD  . LYS B 1 255 ? 105.359 108.391 172.387 1.00 83.40  ? 230 LYS B CD  1 
ATOM   5435  C  CE  . LYS B 1 255 ? 105.703 108.852 173.792 1.00 86.43  ? 230 LYS B CE  1 
ATOM   5436  N  NZ  . LYS B 1 255 ? 106.164 110.267 173.821 1.00 83.95  ? 230 LYS B NZ  1 
ATOM   5437  N  N   . GLY B 1 256 ? 105.496 105.100 168.133 1.00 72.99  ? 231 GLY B N   1 
ATOM   5438  C  CA  . GLY B 1 256 ? 106.134 105.017 166.834 1.00 73.54  ? 231 GLY B CA  1 
ATOM   5439  C  C   . GLY B 1 256 ? 107.647 105.033 166.937 1.00 78.08  ? 231 GLY B C   1 
ATOM   5440  O  O   . GLY B 1 256 ? 108.236 105.055 168.022 1.00 81.05  ? 231 GLY B O   1 
ATOM   5441  N  N   . ASN B 1 257 ? 108.276 105.024 165.761 1.00 67.02  ? 232 ASN B N   1 
ATOM   5442  C  CA  . ASN B 1 257 ? 109.733 105.028 165.635 1.00 62.67  ? 232 ASN B CA  1 
ATOM   5443  C  C   . ASN B 1 257 ? 110.363 103.844 166.364 1.00 68.41  ? 232 ASN B C   1 
ATOM   5444  O  O   . ASN B 1 257 ? 111.324 103.993 167.120 1.00 73.10  ? 232 ASN B O   1 
ATOM   5445  C  CB  . ASN B 1 257 ? 110.332 106.342 166.138 1.00 58.71  ? 232 ASN B CB  1 
ATOM   5446  C  CG  . ASN B 1 257 ? 109.706 107.546 165.497 1.00 63.15  ? 232 ASN B CG  1 
ATOM   5447  O  OD1 . ASN B 1 257 ? 108.807 107.424 164.671 1.00 74.61  ? 232 ASN B OD1 1 
ATOM   5448  N  ND2 . ASN B 1 257 ? 110.180 108.726 165.869 1.00 62.95  ? 232 ASN B ND2 1 
ATOM   5449  N  N   . TYR B 1 258 ? 109.811 102.652 166.141 1.00 66.39  ? 233 TYR B N   1 
ATOM   5450  C  CA  . TYR B 1 258 ? 110.428 101.467 166.723 1.00 64.33  ? 233 TYR B CA  1 
ATOM   5451  C  C   . TYR B 1 258 ? 111.701 101.084 165.982 1.00 64.99  ? 233 TYR B C   1 
ATOM   5452  O  O   . TYR B 1 258 ? 112.611 100.501 166.579 1.00 71.46  ? 233 TYR B O   1 
ATOM   5453  C  CB  . TYR B 1 258 ? 109.440 100.304 166.738 1.00 65.36  ? 233 TYR B CB  1 
ATOM   5454  C  CG  . TYR B 1 258 ? 108.125 100.642 167.393 1.00 67.03  ? 233 TYR B CG  1 
ATOM   5455  C  CD1 . TYR B 1 258 ? 108.071 101.017 168.725 1.00 69.20  ? 233 TYR B CD1 1 
ATOM   5456  C  CD2 . TYR B 1 258 ? 106.941 100.591 166.679 1.00 66.84  ? 233 TYR B CD2 1 
ATOM   5457  C  CE1 . TYR B 1 258 ? 106.875 101.330 169.327 1.00 66.97  ? 233 TYR B CE1 1 
ATOM   5458  C  CE2 . TYR B 1 258 ? 105.740 100.903 167.271 1.00 68.41  ? 233 TYR B CE2 1 
ATOM   5459  C  CZ  . TYR B 1 258 ? 105.713 101.271 168.595 1.00 70.18  ? 233 TYR B CZ  1 
ATOM   5460  O  OH  . TYR B 1 258 ? 104.515 101.582 169.192 1.00 74.23  ? 233 TYR B OH  1 
ATOM   5461  N  N   . GLY B 1 259 ? 111.791 101.406 164.692 1.00 60.29  ? 234 GLY B N   1 
ATOM   5462  C  CA  . GLY B 1 259 ? 113.023 101.152 163.965 1.00 57.12  ? 234 GLY B CA  1 
ATOM   5463  C  C   . GLY B 1 259 ? 114.179 102.004 164.452 1.00 62.76  ? 234 GLY B C   1 
ATOM   5464  O  O   . GLY B 1 259 ? 115.302 101.514 164.602 1.00 67.20  ? 234 GLY B O   1 
ATOM   5465  N  N   . LEU B 1 260 ? 113.928 103.291 164.701 1.00 61.86  ? 235 LEU B N   1 
ATOM   5466  C  CA  . LEU B 1 260 ? 114.978 104.153 165.232 1.00 58.73  ? 235 LEU B CA  1 
ATOM   5467  C  C   . LEU B 1 260 ? 115.396 103.707 166.625 1.00 57.66  ? 235 LEU B C   1 
ATOM   5468  O  O   . LEU B 1 260 ? 116.581 103.755 166.974 1.00 62.32  ? 235 LEU B O   1 
ATOM   5469  C  CB  . LEU B 1 260 ? 114.511 105.607 165.254 1.00 56.49  ? 235 LEU B CB  1 
ATOM   5470  C  CG  . LEU B 1 260 ? 114.366 106.331 163.917 1.00 57.07  ? 235 LEU B CG  1 
ATOM   5471  C  CD1 . LEU B 1 260 ? 114.272 107.822 164.143 1.00 60.23  ? 235 LEU B CD1 1 
ATOM   5472  C  CD2 . LEU B 1 260 ? 115.522 106.013 163.007 1.00 60.39  ? 235 LEU B CD2 1 
ATOM   5473  N  N   . LEU B 1 261 ? 114.436 103.270 167.439 1.00 54.19  ? 236 LEU B N   1 
ATOM   5474  C  CA  . LEU B 1 261 ? 114.771 102.749 168.758 1.00 57.19  ? 236 LEU B CA  1 
ATOM   5475  C  C   . LEU B 1 261 ? 115.601 101.475 168.654 1.00 67.40  ? 236 LEU B C   1 
ATOM   5476  O  O   . LEU B 1 261 ? 116.527 101.267 169.444 1.00 74.95  ? 236 LEU B O   1 
ATOM   5477  C  CB  . LEU B 1 261 ? 113.496 102.508 169.560 1.00 60.03  ? 236 LEU B CB  1 
ATOM   5478  C  CG  . LEU B 1 261 ? 112.842 103.787 170.082 1.00 65.43  ? 236 LEU B CG  1 
ATOM   5479  C  CD1 . LEU B 1 261 ? 111.414 103.525 170.515 1.00 72.00  ? 236 LEU B CD1 1 
ATOM   5480  C  CD2 . LEU B 1 261 ? 113.652 104.366 171.226 1.00 64.72  ? 236 LEU B CD2 1 
ATOM   5481  N  N   . ASP B 1 262 ? 115.290 100.611 167.685 1.00 72.47  ? 237 ASP B N   1 
ATOM   5482  C  CA  . ASP B 1 262 ? 116.102 99.415  167.475 1.00 65.78  ? 237 ASP B CA  1 
ATOM   5483  C  C   . ASP B 1 262 ? 117.519 99.776  167.045 1.00 71.04  ? 237 ASP B C   1 
ATOM   5484  O  O   . ASP B 1 262 ? 118.492 99.168  167.507 1.00 76.88  ? 237 ASP B O   1 
ATOM   5485  C  CB  . ASP B 1 262 ? 115.443 98.507  166.439 1.00 63.19  ? 237 ASP B CB  1 
ATOM   5486  C  CG  . ASP B 1 262 ? 114.162 97.874  166.948 1.00 73.13  ? 237 ASP B CG  1 
ATOM   5487  O  OD1 . ASP B 1 262 ? 113.827 98.080  168.130 1.00 72.92  ? 237 ASP B OD1 1 
ATOM   5488  O  OD2 . ASP B 1 262 ? 113.486 97.168  166.170 1.00 75.00  ? 237 ASP B OD2 1 
ATOM   5489  N  N   . GLN B 1 263 ? 117.657 100.764 166.158 1.00 56.18  ? 238 GLN B N   1 
ATOM   5490  C  CA  . GLN B 1 263 ? 118.987 101.202 165.742 1.00 43.28  ? 238 GLN B CA  1 
ATOM   5491  C  C   . GLN B 1 263 ? 119.772 101.773 166.914 1.00 47.45  ? 238 GLN B C   1 
ATOM   5492  O  O   . GLN B 1 263 ? 120.975 101.522 167.051 1.00 55.87  ? 238 GLN B O   1 
ATOM   5493  C  CB  . GLN B 1 263 ? 118.878 102.236 164.627 1.00 37.58  ? 238 GLN B CB  1 
ATOM   5494  C  CG  . GLN B 1 263 ? 118.741 101.643 163.251 1.00 51.03  ? 238 GLN B CG  1 
ATOM   5495  C  CD  . GLN B 1 263 ? 118.178 102.630 162.264 1.00 51.23  ? 238 GLN B CD  1 
ATOM   5496  O  OE1 . GLN B 1 263 ? 117.803 103.738 162.630 1.00 50.92  ? 238 GLN B OE1 1 
ATOM   5497  N  NE2 . GLN B 1 263 ? 118.121 102.238 161.000 1.00 50.96  ? 238 GLN B NE2 1 
ATOM   5498  N  N   . ILE B 1 264 ? 119.110 102.553 167.767 1.00 51.40  ? 239 ILE B N   1 
ATOM   5499  C  CA  . ILE B 1 264 ? 119.784 103.117 168.931 1.00 50.02  ? 239 ILE B CA  1 
ATOM   5500  C  C   . ILE B 1 264 ? 120.175 102.016 169.909 1.00 55.05  ? 239 ILE B C   1 
ATOM   5501  O  O   . ILE B 1 264 ? 121.232 102.081 170.545 1.00 61.65  ? 239 ILE B O   1 
ATOM   5502  C  CB  . ILE B 1 264 ? 118.896 104.187 169.586 1.00 50.15  ? 239 ILE B CB  1 
ATOM   5503  C  CG1 . ILE B 1 264 ? 118.899 105.454 168.736 1.00 53.62  ? 239 ILE B CG1 1 
ATOM   5504  C  CG2 . ILE B 1 264 ? 119.375 104.501 170.981 1.00 52.54  ? 239 ILE B CG2 1 
ATOM   5505  C  CD1 . ILE B 1 264 ? 117.918 106.495 169.190 1.00 58.10  ? 239 ILE B CD1 1 
ATOM   5506  N  N   . GLN B 1 265 ? 119.342 100.982 170.040 1.00 59.31  ? 240 GLN B N   1 
ATOM   5507  C  CA  . GLN B 1 265 ? 119.710 99.849  170.882 1.00 58.50  ? 240 GLN B CA  1 
ATOM   5508  C  C   . GLN B 1 265 ? 120.929 99.125  170.326 1.00 60.90  ? 240 GLN B C   1 
ATOM   5509  O  O   . GLN B 1 265 ? 121.804 98.694  171.085 1.00 74.51  ? 240 GLN B O   1 
ATOM   5510  C  CB  . GLN B 1 265 ? 118.535 98.887  171.019 1.00 57.63  ? 240 GLN B CB  1 
ATOM   5511  C  CG  . GLN B 1 265 ? 118.885 97.593  171.719 1.00 60.20  ? 240 GLN B CG  1 
ATOM   5512  C  CD  . GLN B 1 265 ? 119.463 97.815  173.101 1.00 66.88  ? 240 GLN B CD  1 
ATOM   5513  O  OE1 . GLN B 1 265 ? 118.996 98.669  173.852 1.00 68.26  ? 240 GLN B OE1 1 
ATOM   5514  N  NE2 . GLN B 1 265 ? 120.485 97.042  173.444 1.00 64.89  ? 240 GLN B NE2 1 
ATOM   5515  N  N   . ALA B 1 266 ? 121.000 98.976  169.003 1.00 49.44  ? 241 ALA B N   1 
ATOM   5516  C  CA  . ALA B 1 266 ? 122.182 98.368  168.397 1.00 49.65  ? 241 ALA B CA  1 
ATOM   5517  C  C   . ALA B 1 266 ? 123.422 99.215  168.639 1.00 47.02  ? 241 ALA B C   1 
ATOM   5518  O  O   . ALA B 1 266 ? 124.507 98.683  168.899 1.00 54.73  ? 241 ALA B O   1 
ATOM   5519  C  CB  . ALA B 1 266 ? 121.964 98.161  166.902 1.00 47.59  ? 241 ALA B CB  1 
ATOM   5520  N  N   . LEU B 1 267 ? 123.284 100.537 168.547 1.00 51.87  ? 242 LEU B N   1 
ATOM   5521  C  CA  . LEU B 1 267 ? 124.410 101.414 168.851 1.00 50.71  ? 242 LEU B CA  1 
ATOM   5522  C  C   . LEU B 1 267 ? 124.834 101.279 170.308 1.00 51.83  ? 242 LEU B C   1 
ATOM   5523  O  O   . LEU B 1 267 ? 126.028 101.314 170.616 1.00 56.78  ? 242 LEU B O   1 
ATOM   5524  C  CB  . LEU B 1 267 ? 124.060 102.865 168.528 1.00 47.41  ? 242 LEU B CB  1 
ATOM   5525  C  CG  . LEU B 1 267 ? 124.338 103.311 167.095 1.00 44.41  ? 242 LEU B CG  1 
ATOM   5526  C  CD1 . LEU B 1 267 ? 123.699 104.652 166.830 1.00 51.78  ? 242 LEU B CD1 1 
ATOM   5527  C  CD2 . LEU B 1 267 ? 125.824 103.376 166.844 1.00 45.01  ? 242 LEU B CD2 1 
ATOM   5528  N  N   . ARG B 1 268 ? 123.870 101.137 171.219 1.00 52.26  ? 243 ARG B N   1 
ATOM   5529  C  CA  . ARG B 1 268 ? 124.205 100.940 172.627 1.00 54.80  ? 243 ARG B CA  1 
ATOM   5530  C  C   . ARG B 1 268 ? 124.952 99.630  172.839 1.00 56.32  ? 243 ARG B C   1 
ATOM   5531  O  O   . ARG B 1 268 ? 125.929 99.573  173.600 1.00 65.32  ? 243 ARG B O   1 
ATOM   5532  C  CB  . ARG B 1 268 ? 122.937 100.973 173.476 1.00 56.71  ? 243 ARG B CB  1 
ATOM   5533  C  CG  . ARG B 1 268 ? 123.062 101.815 174.727 1.00 61.85  ? 243 ARG B CG  1 
ATOM   5534  C  CD  . ARG B 1 268 ? 121.833 101.698 175.608 1.00 62.60  ? 243 ARG B CD  1 
ATOM   5535  N  NE  . ARG B 1 268 ? 120.618 102.158 174.947 1.00 57.88  ? 243 ARG B NE  1 
ATOM   5536  C  CZ  . ARG B 1 268 ? 120.305 103.432 174.755 1.00 64.50  ? 243 ARG B CZ  1 
ATOM   5537  N  NH1 . ARG B 1 268 ? 121.112 104.408 175.135 1.00 61.86  ? 243 ARG B NH1 1 
ATOM   5538  N  NH2 . ARG B 1 268 ? 119.150 103.734 174.171 1.00 64.27  ? 243 ARG B NH2 1 
ATOM   5539  N  N   . TRP B 1 269 ? 124.500 98.563  172.178 1.00 55.69  ? 244 TRP B N   1 
ATOM   5540  C  CA  . TRP B 1 269 ? 125.198 97.285  172.263 1.00 57.57  ? 244 TRP B CA  1 
ATOM   5541  C  C   . TRP B 1 269 ? 126.620 97.404  171.737 1.00 58.17  ? 244 TRP B C   1 
ATOM   5542  O  O   . TRP B 1 269 ? 127.558 96.867  172.334 1.00 60.40  ? 244 TRP B O   1 
ATOM   5543  C  CB  . TRP B 1 269 ? 124.432 96.216  171.488 1.00 57.10  ? 244 TRP B CB  1 
ATOM   5544  C  CG  . TRP B 1 269 ? 124.988 94.838  171.644 1.00 62.54  ? 244 TRP B CG  1 
ATOM   5545  C  CD1 . TRP B 1 269 ? 124.593 93.893  172.544 1.00 67.59  ? 244 TRP B CD1 1 
ATOM   5546  C  CD2 . TRP B 1 269 ? 126.036 94.242  170.874 1.00 60.26  ? 244 TRP B CD2 1 
ATOM   5547  N  NE1 . TRP B 1 269 ? 125.330 92.748  172.384 1.00 61.67  ? 244 TRP B NE1 1 
ATOM   5548  C  CE2 . TRP B 1 269 ? 126.224 92.937  171.364 1.00 62.38  ? 244 TRP B CE2 1 
ATOM   5549  C  CE3 . TRP B 1 269 ? 126.834 94.685  169.817 1.00 57.96  ? 244 TRP B CE3 1 
ATOM   5550  C  CZ2 . TRP B 1 269 ? 127.176 92.073  170.835 1.00 63.14  ? 244 TRP B CZ2 1 
ATOM   5551  C  CZ3 . TRP B 1 269 ? 127.778 93.825  169.295 1.00 60.03  ? 244 TRP B CZ3 1 
ATOM   5552  C  CH2 . TRP B 1 269 ? 127.941 92.535  169.804 1.00 61.46  ? 244 TRP B CH2 1 
ATOM   5553  N  N   . LEU B 1 270 ? 126.799 98.104  170.616 1.00 61.90  ? 245 LEU B N   1 
ATOM   5554  C  CA  . LEU B 1 270 ? 128.146 98.330  170.101 1.00 60.02  ? 245 LEU B CA  1 
ATOM   5555  C  C   . LEU B 1 270 ? 128.986 99.122  171.092 1.00 60.96  ? 245 LEU B C   1 
ATOM   5556  O  O   . LEU B 1 270 ? 130.149 98.789  171.336 1.00 60.45  ? 245 LEU B O   1 
ATOM   5557  C  CB  . LEU B 1 270 ? 128.082 99.055  168.759 1.00 55.76  ? 245 LEU B CB  1 
ATOM   5558  C  CG  . LEU B 1 270 ? 127.944 98.168  167.527 1.00 55.34  ? 245 LEU B CG  1 
ATOM   5559  C  CD1 . LEU B 1 270 ? 128.319 98.940  166.285 1.00 58.33  ? 245 LEU B CD1 1 
ATOM   5560  C  CD2 . LEU B 1 270 ? 128.814 96.940  167.672 1.00 60.85  ? 245 LEU B CD2 1 
ATOM   5561  N  N   . SER B 1 271 ? 128.407 100.165 171.686 1.00 66.54  ? 246 SER B N   1 
ATOM   5562  C  CA  . SER B 1 271 ? 129.157 101.012 172.605 1.00 66.41  ? 246 SER B CA  1 
ATOM   5563  C  C   . SER B 1 271 ? 129.635 100.227 173.816 1.00 63.75  ? 246 SER B C   1 
ATOM   5564  O  O   . SER B 1 271 ? 130.764 100.420 174.282 1.00 61.83  ? 246 SER B O   1 
ATOM   5565  C  CB  . SER B 1 271 ? 128.297 102.193 173.046 1.00 64.02  ? 246 SER B CB  1 
ATOM   5566  O  OG  . SER B 1 271 ? 128.864 102.834 174.173 1.00 70.40  ? 246 SER B OG  1 
ATOM   5567  N  N   . GLU B 1 272 ? 128.794 99.344  174.344 1.00 66.52  ? 247 GLU B N   1 
ATOM   5568  C  CA  . GLU B 1 272 ? 129.142 98.600  175.546 1.00 70.04  ? 247 GLU B CA  1 
ATOM   5569  C  C   . GLU B 1 272 ? 129.735 97.223  175.267 1.00 70.00  ? 247 GLU B C   1 
ATOM   5570  O  O   . GLU B 1 272 ? 130.034 96.497  176.219 1.00 65.33  ? 247 GLU B O   1 
ATOM   5571  C  CB  . GLU B 1 272 ? 127.914 98.458  176.451 1.00 69.27  ? 247 GLU B CB  1 
ATOM   5572  C  CG  . GLU B 1 272 ? 126.893 97.457  175.961 1.00 69.96  ? 247 GLU B CG  1 
ATOM   5573  C  CD  . GLU B 1 272 ? 125.694 97.360  176.878 1.00 73.56  ? 247 GLU B CD  1 
ATOM   5574  O  OE1 . GLU B 1 272 ? 125.347 98.377  177.515 1.00 74.31  ? 247 GLU B OE1 1 
ATOM   5575  O  OE2 . GLU B 1 272 ? 125.097 96.266  176.961 1.00 73.91  ? 247 GLU B OE2 1 
ATOM   5576  N  N   . ASN B 1 273 ? 129.925 96.842  174.000 1.00 71.70  ? 248 ASN B N   1 
ATOM   5577  C  CA  . ASN B 1 273 ? 130.415 95.504  173.698 1.00 66.93  ? 248 ASN B CA  1 
ATOM   5578  C  C   . ASN B 1 273 ? 131.481 95.429  172.613 1.00 69.52  ? 248 ASN B C   1 
ATOM   5579  O  O   . ASN B 1 273 ? 131.967 94.328  172.343 1.00 70.93  ? 248 ASN B O   1 
ATOM   5580  C  CB  . ASN B 1 273 ? 129.247 94.599  173.287 1.00 68.35  ? 248 ASN B CB  1 
ATOM   5581  C  CG  . ASN B 1 273 ? 128.709 93.789  174.437 1.00 71.04  ? 248 ASN B CG  1 
ATOM   5582  O  OD1 . ASN B 1 273 ? 129.070 92.627  174.612 1.00 76.08  ? 248 ASN B OD1 1 
ATOM   5583  N  ND2 . ASN B 1 273 ? 127.833 94.393  175.227 1.00 69.81  ? 248 ASN B ND2 1 
ATOM   5584  N  N   . ILE B 1 274 ? 131.858 96.539  171.977 1.00 66.46  ? 249 ILE B N   1 
ATOM   5585  C  CA  . ILE B 1 274 ? 132.785 96.447  170.853 1.00 65.71  ? 249 ILE B CA  1 
ATOM   5586  C  C   . ILE B 1 274 ? 134.236 96.379  171.302 1.00 73.25  ? 249 ILE B C   1 
ATOM   5587  O  O   . ILE B 1 274 ? 135.104 96.003  170.506 1.00 78.99  ? 249 ILE B O   1 
ATOM   5588  C  CB  . ILE B 1 274 ? 132.592 97.621  169.879 1.00 64.51  ? 249 ILE B CB  1 
ATOM   5589  C  CG1 . ILE B 1 274 ? 133.189 97.294  168.512 1.00 66.69  ? 249 ILE B CG1 1 
ATOM   5590  C  CG2 . ILE B 1 274 ? 133.217 98.881  170.435 1.00 69.46  ? 249 ILE B CG2 1 
ATOM   5591  C  CD1 . ILE B 1 274 ? 132.795 95.946  167.993 1.00 68.78  ? 249 ILE B CD1 1 
ATOM   5592  N  N   . ALA B 1 275 ? 134.531 96.723  172.556 1.00 74.73  ? 250 ALA B N   1 
ATOM   5593  C  CA  . ALA B 1 275 ? 135.907 96.634  173.029 1.00 72.93  ? 250 ALA B CA  1 
ATOM   5594  C  C   . ALA B 1 275 ? 136.403 95.195  173.036 1.00 76.05  ? 250 ALA B C   1 
ATOM   5595  O  O   . ALA B 1 275 ? 137.609 94.954  172.911 1.00 77.44  ? 250 ALA B O   1 
ATOM   5596  C  CB  . ALA B 1 275 ? 136.024 97.245  174.424 1.00 70.45  ? 250 ALA B CB  1 
ATOM   5597  N  N   . HIS B 1 276 ? 135.493 94.229  173.171 1.00 76.13  ? 251 HIS B N   1 
ATOM   5598  C  CA  . HIS B 1 276 ? 135.900 92.829  173.226 1.00 73.56  ? 251 HIS B CA  1 
ATOM   5599  C  C   . HIS B 1 276 ? 136.403 92.332  171.878 1.00 74.26  ? 251 HIS B C   1 
ATOM   5600  O  O   . HIS B 1 276 ? 137.275 91.458  171.831 1.00 80.66  ? 251 HIS B O   1 
ATOM   5601  C  CB  . HIS B 1 276 ? 134.739 91.960  173.708 1.00 72.30  ? 251 HIS B CB  1 
ATOM   5602  C  CG  . HIS B 1 276 ? 134.181 92.371  175.034 1.00 78.56  ? 251 HIS B CG  1 
ATOM   5603  N  ND1 . HIS B 1 276 ? 133.115 91.726  175.623 1.00 80.37  ? 251 HIS B ND1 1 
ATOM   5604  C  CD2 . HIS B 1 276 ? 134.540 93.358  175.888 1.00 75.95  ? 251 HIS B CD2 1 
ATOM   5605  C  CE1 . HIS B 1 276 ? 132.839 92.301  176.780 1.00 76.90  ? 251 HIS B CE1 1 
ATOM   5606  N  NE2 . HIS B 1 276 ? 133.689 93.294  176.964 1.00 77.60  ? 251 HIS B NE2 1 
ATOM   5607  N  N   . PHE B 1 277 ? 135.873 92.866  170.781 1.00 71.18  ? 252 PHE B N   1 
ATOM   5608  C  CA  . PHE B 1 277 ? 136.251 92.432  169.444 1.00 73.49  ? 252 PHE B CA  1 
ATOM   5609  C  C   . PHE B 1 277 ? 137.472 93.162  168.906 1.00 73.29  ? 252 PHE B C   1 
ATOM   5610  O  O   . PHE B 1 277 ? 137.881 92.898  167.771 1.00 74.89  ? 252 PHE B O   1 
ATOM   5611  C  CB  . PHE B 1 277 ? 135.083 92.620  168.475 1.00 64.16  ? 252 PHE B CB  1 
ATOM   5612  C  CG  . PHE B 1 277 ? 133.902 91.754  168.777 1.00 67.99  ? 252 PHE B CG  1 
ATOM   5613  C  CD1 . PHE B 1 277 ? 133.803 90.489  168.239 1.00 72.93  ? 252 PHE B CD1 1 
ATOM   5614  C  CD2 . PHE B 1 277 ? 132.888 92.206  169.598 1.00 72.00  ? 252 PHE B CD2 1 
ATOM   5615  C  CE1 . PHE B 1 277 ? 132.717 89.690  168.516 1.00 73.91  ? 252 PHE B CE1 1 
ATOM   5616  C  CE2 . PHE B 1 277 ? 131.799 91.410  169.877 1.00 72.75  ? 252 PHE B CE2 1 
ATOM   5617  C  CZ  . PHE B 1 277 ? 131.714 90.152  169.336 1.00 72.22  ? 252 PHE B CZ  1 
ATOM   5618  N  N   . GLY B 1 278 ? 138.057 94.068  169.681 1.00 72.17  ? 253 GLY B N   1 
ATOM   5619  C  CA  . GLY B 1 278 ? 139.201 94.835  169.246 1.00 73.95  ? 253 GLY B CA  1 
ATOM   5620  C  C   . GLY B 1 278 ? 138.883 96.239  168.785 1.00 73.07  ? 253 GLY B C   1 
ATOM   5621  O  O   . GLY B 1 278 ? 139.811 97.024  168.564 1.00 74.83  ? 253 GLY B O   1 
ATOM   5622  N  N   . GLY B 1 279 ? 137.607 96.581  168.641 1.00 71.67  ? 254 GLY B N   1 
ATOM   5623  C  CA  . GLY B 1 279 ? 137.236 97.900  168.186 1.00 74.39  ? 254 GLY B CA  1 
ATOM   5624  C  C   . GLY B 1 279 ? 137.352 98.951  169.267 1.00 75.82  ? 254 GLY B C   1 
ATOM   5625  O  O   . GLY B 1 279 ? 137.667 98.670  170.423 1.00 72.18  ? 254 GLY B O   1 
ATOM   5626  N  N   . ASP B 1 280 ? 137.089 100.193 168.869 1.00 75.05  ? 255 ASP B N   1 
ATOM   5627  C  CA  . ASP B 1 280 ? 137.168 101.334 169.767 1.00 74.74  ? 255 ASP B CA  1 
ATOM   5628  C  C   . ASP B 1 280 ? 135.770 101.842 170.071 1.00 74.07  ? 255 ASP B C   1 
ATOM   5629  O  O   . ASP B 1 280 ? 135.045 102.224 169.142 1.00 76.58  ? 255 ASP B O   1 
ATOM   5630  C  CB  . ASP B 1 280 ? 138.014 102.444 169.149 1.00 73.30  ? 255 ASP B CB  1 
ATOM   5631  C  CG  . ASP B 1 280 ? 138.699 103.306 170.191 1.00 78.61  ? 255 ASP B CG  1 
ATOM   5632  O  OD1 . ASP B 1 280 ? 138.100 103.541 171.260 1.00 75.77  ? 255 ASP B OD1 1 
ATOM   5633  O  OD2 . ASP B 1 280 ? 139.838 103.750 169.940 1.00 77.11  ? 255 ASP B OD2 1 
ATOM   5634  N  N   . PRO B 1 281 ? 135.343 101.871 171.333 1.00 74.15  ? 256 PRO B N   1 
ATOM   5635  C  CA  . PRO B 1 281 ? 134.041 102.451 171.672 1.00 72.14  ? 256 PRO B CA  1 
ATOM   5636  C  C   . PRO B 1 281 ? 134.006 103.970 171.651 1.00 76.88  ? 256 PRO B C   1 
ATOM   5637  O  O   . PRO B 1 281 ? 133.049 104.553 172.166 1.00 81.05  ? 256 PRO B O   1 
ATOM   5638  C  CB  . PRO B 1 281 ? 133.803 101.926 173.096 1.00 74.09  ? 256 PRO B CB  1 
ATOM   5639  C  CG  . PRO B 1 281 ? 135.162 101.761 173.653 1.00 76.26  ? 256 PRO B CG  1 
ATOM   5640  C  CD  . PRO B 1 281 ? 136.020 101.303 172.511 1.00 77.24  ? 256 PRO B CD  1 
ATOM   5641  N  N   . GLU B 1 282 ? 135.019 104.618 171.078 1.00 77.94  ? 257 GLU B N   1 
ATOM   5642  C  CA  . GLU B 1 282 ? 135.111 106.071 171.056 1.00 74.99  ? 257 GLU B CA  1 
ATOM   5643  C  C   . GLU B 1 282 ? 135.213 106.633 169.643 1.00 74.03  ? 257 GLU B C   1 
ATOM   5644  O  O   . GLU B 1 282 ? 135.419 107.841 169.485 1.00 78.25  ? 257 GLU B O   1 
ATOM   5645  C  CB  . GLU B 1 282 ? 136.310 106.533 171.889 1.00 76.80  ? 257 GLU B CB  1 
ATOM   5646  C  CG  . GLU B 1 282 ? 136.109 107.859 172.597 1.00 77.49  ? 257 GLU B CG  1 
ATOM   5647  C  CD  . GLU B 1 282 ? 135.347 107.715 173.896 1.00 81.95  ? 257 GLU B CD  1 
ATOM   5648  O  OE1 . GLU B 1 282 ? 135.158 106.568 174.351 1.00 82.65  ? 257 GLU B OE1 1 
ATOM   5649  O  OE2 . GLU B 1 282 ? 134.938 108.748 174.464 1.00 84.54  ? 257 GLU B OE2 1 
ATOM   5650  N  N   . ARG B 1 283 ? 135.078 105.799 168.614 1.00 66.61  ? 258 ARG B N   1 
ATOM   5651  C  CA  . ARG B 1 283 ? 135.208 106.254 167.233 1.00 74.02  ? 258 ARG B CA  1 
ATOM   5652  C  C   . ARG B 1 283 ? 134.143 105.618 166.352 1.00 71.73  ? 258 ARG B C   1 
ATOM   5653  O  O   . ARG B 1 283 ? 134.418 105.199 165.224 1.00 72.51  ? 258 ARG B O   1 
ATOM   5654  C  CB  . ARG B 1 283 ? 136.604 105.958 166.689 1.00 74.22  ? 258 ARG B CB  1 
ATOM   5655  C  CG  . ARG B 1 283 ? 137.685 106.870 167.244 1.00 73.24  ? 258 ARG B CG  1 
ATOM   5656  C  CD  . ARG B 1 283 ? 138.991 106.713 166.491 1.00 73.55  ? 258 ARG B CD  1 
ATOM   5657  N  NE  . ARG B 1 283 ? 139.818 105.654 167.053 1.00 73.83  ? 258 ARG B NE  1 
ATOM   5658  C  CZ  . ARG B 1 283 ? 141.046 105.368 166.645 1.00 74.97  ? 258 ARG B CZ  1 
ATOM   5659  N  NH1 . ARG B 1 283 ? 141.626 106.048 165.672 1.00 72.11  ? 258 ARG B NH1 1 
ATOM   5660  N  NH2 . ARG B 1 283 ? 141.707 104.374 167.228 1.00 77.60  ? 258 ARG B NH2 1 
ATOM   5661  N  N   . ILE B 1 284 ? 132.908 105.555 166.842 1.00 58.80  ? 259 ILE B N   1 
ATOM   5662  C  CA  . ILE B 1 284 ? 131.832 104.848 166.156 1.00 55.18  ? 259 ILE B CA  1 
ATOM   5663  C  C   . ILE B 1 284 ? 131.205 105.802 165.145 1.00 48.44  ? 259 ILE B C   1 
ATOM   5664  O  O   . ILE B 1 284 ? 130.406 106.664 165.500 1.00 54.21  ? 259 ILE B O   1 
ATOM   5665  C  CB  . ILE B 1 284 ? 130.791 104.312 167.139 1.00 51.90  ? 259 ILE B CB  1 
ATOM   5666  C  CG1 . ILE B 1 284 ? 131.441 103.370 168.150 1.00 51.93  ? 259 ILE B CG1 1 
ATOM   5667  C  CG2 . ILE B 1 284 ? 129.682 103.594 166.397 1.00 53.56  ? 259 ILE B CG2 1 
ATOM   5668  C  CD1 . ILE B 1 284 ? 130.483 102.851 169.190 1.00 55.67  ? 259 ILE B CD1 1 
ATOM   5669  N  N   . THR B 1 285 ? 131.569 105.644 163.878 1.00 45.82  ? 260 THR B N   1 
ATOM   5670  C  CA  . THR B 1 285 ? 130.879 106.319 162.793 1.00 47.14  ? 260 THR B CA  1 
ATOM   5671  C  C   . THR B 1 285 ? 129.621 105.543 162.434 1.00 51.67  ? 260 THR B C   1 
ATOM   5672  O  O   . THR B 1 285 ? 129.578 104.319 162.549 1.00 68.74  ? 260 THR B O   1 
ATOM   5673  C  CB  . THR B 1 285 ? 131.790 106.423 161.570 1.00 49.07  ? 260 THR B CB  1 
ATOM   5674  O  OG1 . THR B 1 285 ? 132.994 107.108 161.927 1.00 65.33  ? 260 THR B OG1 1 
ATOM   5675  C  CG2 . THR B 1 285 ? 131.118 107.171 160.445 1.00 40.44  ? 260 THR B CG2 1 
ATOM   5676  N  N   . ILE B 1 286 ? 128.581 106.262 162.024 1.00 36.49  ? 261 ILE B N   1 
ATOM   5677  C  CA  . ILE B 1 286 ? 127.394 105.661 161.429 1.00 28.10  ? 261 ILE B CA  1 
ATOM   5678  C  C   . ILE B 1 286 ? 127.210 106.275 160.054 1.00 27.61  ? 261 ILE B C   1 
ATOM   5679  O  O   . ILE B 1 286 ? 127.282 107.498 159.905 1.00 59.05  ? 261 ILE B O   1 
ATOM   5680  C  CB  . ILE B 1 286 ? 126.139 105.859 162.298 1.00 24.16  ? 261 ILE B CB  1 
ATOM   5681  C  CG1 . ILE B 1 286 ? 125.886 107.335 162.581 1.00 29.15  ? 261 ILE B CG1 1 
ATOM   5682  C  CG2 . ILE B 1 286 ? 126.276 105.115 163.601 1.00 41.60  ? 261 ILE B CG2 1 
ATOM   5683  C  CD1 . ILE B 1 286 ? 124.771 107.576 163.557 1.00 34.06  ? 261 ILE B CD1 1 
ATOM   5684  N  N   . PHE B 1 287 ? 127.007 105.434 159.046 1.00 20.57  ? 262 PHE B N   1 
ATOM   5685  C  CA  . PHE B 1 287 ? 126.825 105.940 157.696 1.00 29.64  ? 262 PHE B CA  1 
ATOM   5686  C  C   . PHE B 1 287 ? 125.751 105.144 156.981 1.00 29.91  ? 262 PHE B C   1 
ATOM   5687  O  O   . PHE B 1 287 ? 125.497 103.984 157.304 1.00 58.49  ? 262 PHE B O   1 
ATOM   5688  C  CB  . PHE B 1 287 ? 128.134 105.923 156.896 1.00 40.26  ? 262 PHE B CB  1 
ATOM   5689  C  CG  . PHE B 1 287 ? 128.580 104.567 156.441 1.00 36.34  ? 262 PHE B CG  1 
ATOM   5690  C  CD1 . PHE B 1 287 ? 128.975 103.608 157.347 1.00 42.35  ? 262 PHE B CD1 1 
ATOM   5691  C  CD2 . PHE B 1 287 ? 128.660 104.276 155.095 1.00 36.85  ? 262 PHE B CD2 1 
ATOM   5692  C  CE1 . PHE B 1 287 ? 129.407 102.375 156.921 1.00 40.79  ? 262 PHE B CE1 1 
ATOM   5693  C  CE2 . PHE B 1 287 ? 129.092 103.046 154.666 1.00 39.84  ? 262 PHE B CE2 1 
ATOM   5694  C  CZ  . PHE B 1 287 ? 129.466 102.095 155.579 1.00 42.66  ? 262 PHE B CZ  1 
ATOM   5695  N  N   . GLY B 1 288 ? 125.111 105.787 156.017 1.00 12.35  ? 263 GLY B N   1 
ATOM   5696  C  CA  . GLY B 1 288 ? 124.057 105.141 155.268 1.00 30.60  ? 263 GLY B CA  1 
ATOM   5697  C  C   . GLY B 1 288 ? 123.664 105.979 154.078 1.00 38.64  ? 263 GLY B C   1 
ATOM   5698  O  O   . GLY B 1 288 ? 123.914 107.186 154.036 1.00 45.55  ? 263 GLY B O   1 
ATOM   5699  N  N   . SER B 1 289 ? 123.045 105.319 153.107 1.00 40.47  ? 264 SER B N   1 
ATOM   5700  C  CA  . SER B 1 289 ? 122.593 105.962 151.887 1.00 37.09  ? 264 SER B CA  1 
ATOM   5701  C  C   . SER B 1 289 ? 121.099 105.742 151.725 1.00 47.95  ? 264 SER B C   1 
ATOM   5702  O  O   . SER B 1 289 ? 120.548 104.751 152.208 1.00 61.07  ? 264 SER B O   1 
ATOM   5703  C  CB  . SER B 1 289 ? 123.329 105.421 150.662 1.00 48.60  ? 264 SER B CB  1 
ATOM   5704  O  OG  . SER B 1 289 ? 122.485 105.420 149.525 1.00 54.13  ? 264 SER B OG  1 
ATOM   5705  N  N   . GLY B 1 290 ? 120.447 106.670 151.035 1.00 42.70  ? 265 GLY B N   1 
ATOM   5706  C  CA  . GLY B 1 290 ? 119.009 106.588 150.887 1.00 43.49  ? 265 GLY B CA  1 
ATOM   5707  C  C   . GLY B 1 290 ? 118.295 106.981 152.169 1.00 43.34  ? 265 GLY B C   1 
ATOM   5708  O  O   . GLY B 1 290 ? 118.786 107.784 152.960 1.00 45.36  ? 265 GLY B O   1 
ATOM   5709  N  N   . ALA B 1 291 ? 117.115 106.391 152.373 1.00 52.54  ? 266 ALA B N   1 
ATOM   5710  C  CA  . ALA B 1 291 ? 116.329 106.713 153.558 1.00 48.68  ? 266 ALA B CA  1 
ATOM   5711  C  C   . ALA B 1 291 ? 117.062 106.342 154.835 1.00 52.68  ? 266 ALA B C   1 
ATOM   5712  O  O   . ALA B 1 291 ? 116.833 106.960 155.879 1.00 66.28  ? 266 ALA B O   1 
ATOM   5713  C  CB  . ALA B 1 291 ? 114.975 106.012 153.508 1.00 51.01  ? 266 ALA B CB  1 
ATOM   5714  N  N   . GLY B 1 292 ? 117.947 105.349 154.777 1.00 39.37  ? 267 GLY B N   1 
ATOM   5715  C  CA  . GLY B 1 292 ? 118.769 105.046 155.935 1.00 32.13  ? 267 GLY B CA  1 
ATOM   5716  C  C   . GLY B 1 292 ? 119.579 106.243 156.387 1.00 44.72  ? 267 GLY B C   1 
ATOM   5717  O  O   . GLY B 1 292 ? 119.715 106.494 157.586 1.00 48.28  ? 267 GLY B O   1 
ATOM   5718  N  N   . ALA B 1 293 ? 120.107 107.013 155.430 1.00 45.89  ? 268 ALA B N   1 
ATOM   5719  C  CA  . ALA B 1 293 ? 120.812 108.246 155.768 1.00 35.35  ? 268 ALA B CA  1 
ATOM   5720  C  C   . ALA B 1 293 ? 119.906 109.207 156.517 1.00 36.87  ? 268 ALA B C   1 
ATOM   5721  O  O   . ALA B 1 293 ? 120.358 109.914 157.424 1.00 47.44  ? 268 ALA B O   1 
ATOM   5722  C  CB  . ALA B 1 293 ? 121.352 108.911 154.509 1.00 38.40  ? 268 ALA B CB  1 
ATOM   5723  N  N   . SER B 1 294 ? 118.624 109.250 156.153 1.00 31.65  ? 269 SER B N   1 
ATOM   5724  C  CA  . SER B 1 294 ? 117.673 110.044 156.919 1.00 22.79  ? 269 SER B CA  1 
ATOM   5725  C  C   . SER B 1 294 ? 117.697 109.632 158.381 1.00 33.53  ? 269 SER B C   1 
ATOM   5726  O  O   . SER B 1 294 ? 117.781 110.481 159.275 1.00 47.40  ? 269 SER B O   1 
ATOM   5727  C  CB  . SER B 1 294 ? 116.272 109.895 156.336 1.00 26.62  ? 269 SER B CB  1 
ATOM   5728  O  OG  . SER B 1 294 ? 116.134 110.659 155.152 1.00 44.54  ? 269 SER B OG  1 
ATOM   5729  N  N   . CYS B 1 295 ? 117.674 108.321 158.640 1.00 38.38  ? 270 CYS B N   1 
ATOM   5730  C  CA  . CYS B 1 295 ? 117.801 107.836 160.008 1.00 36.06  ? 270 CYS B CA  1 
ATOM   5731  C  C   . CYS B 1 295 ? 119.031 108.428 160.676 1.00 39.62  ? 270 CYS B C   1 
ATOM   5732  O  O   . CYS B 1 295 ? 118.955 108.916 161.809 1.00 46.55  ? 270 CYS B O   1 
ATOM   5733  C  CB  . CYS B 1 295 ? 117.863 106.309 160.024 1.00 29.66  ? 270 CYS B CB  1 
ATOM   5734  S  SG  . CYS B 1 295 ? 116.391 105.489 159.388 1.00 43.22  ? 270 CYS B SG  1 
ATOM   5735  N  N   . VAL B 1 296 ? 120.157 108.458 159.958 1.00 36.76  ? 271 VAL B N   1 
ATOM   5736  C  CA  . VAL B 1 296 ? 121.379 109.029 160.516 1.00 29.47  ? 271 VAL B CA  1 
ATOM   5737  C  C   . VAL B 1 296 ? 121.122 110.450 160.989 1.00 39.10  ? 271 VAL B C   1 
ATOM   5738  O  O   . VAL B 1 296 ? 121.426 110.806 162.133 1.00 54.50  ? 271 VAL B O   1 
ATOM   5739  C  CB  . VAL B 1 296 ? 122.517 108.983 159.483 1.00 19.97  ? 271 VAL B CB  1 
ATOM   5740  C  CG1 . VAL B 1 296 ? 123.670 109.833 159.948 1.00 18.51  ? 271 VAL B CG1 1 
ATOM   5741  C  CG2 . VAL B 1 296 ? 122.969 107.566 159.270 1.00 35.34  ? 271 VAL B CG2 1 
ATOM   5742  N  N   . ASN B 1 297 ? 120.505 111.269 160.136 1.00 35.73  ? 272 ASN B N   1 
ATOM   5743  C  CA  . ASN B 1 297 ? 120.211 112.635 160.546 1.00 32.76  ? 272 ASN B CA  1 
ATOM   5744  C  C   . ASN B 1 297 ? 119.236 112.650 161.712 1.00 39.67  ? 272 ASN B C   1 
ATOM   5745  O  O   . ASN B 1 297 ? 119.415 113.408 162.670 1.00 48.11  ? 272 ASN B O   1 
ATOM   5746  C  CB  . ASN B 1 297 ? 119.669 113.434 159.367 1.00 33.12  ? 272 ASN B CB  1 
ATOM   5747  C  CG  . ASN B 1 297 ? 120.765 113.970 158.487 1.00 44.53  ? 272 ASN B CG  1 
ATOM   5748  O  OD1 . ASN B 1 297 ? 121.084 115.153 158.530 1.00 54.81  ? 272 ASN B OD1 1 
ATOM   5749  N  ND2 . ASN B 1 297 ? 121.358 113.100 157.686 1.00 36.54  ? 272 ASN B ND2 1 
ATOM   5750  N  N   . LEU B 1 298 ? 118.218 111.791 161.669 1.00 35.45  ? 273 LEU B N   1 
ATOM   5751  C  CA  . LEU B 1 298 ? 117.288 111.730 162.786 1.00 32.79  ? 273 LEU B CA  1 
ATOM   5752  C  C   . LEU B 1 298 ? 117.948 111.177 164.037 1.00 37.16  ? 273 LEU B C   1 
ATOM   5753  O  O   . LEU B 1 298 ? 117.419 111.364 165.136 1.00 43.28  ? 273 LEU B O   1 
ATOM   5754  C  CB  . LEU B 1 298 ? 116.067 110.892 162.412 1.00 33.71  ? 273 LEU B CB  1 
ATOM   5755  C  CG  . LEU B 1 298 ? 115.266 111.400 161.217 1.00 25.87  ? 273 LEU B CG  1 
ATOM   5756  C  CD1 . LEU B 1 298 ? 114.343 110.326 160.708 1.00 32.34  ? 273 LEU B CD1 1 
ATOM   5757  C  CD2 . LEU B 1 298 ? 114.479 112.620 161.604 1.00 35.10  ? 273 LEU B CD2 1 
ATOM   5758  N  N   . LEU B 1 299 ? 119.088 110.502 163.897 1.00 42.30  ? 274 LEU B N   1 
ATOM   5759  C  CA  . LEU B 1 299 ? 119.850 110.053 165.050 1.00 43.24  ? 274 LEU B CA  1 
ATOM   5760  C  C   . LEU B 1 299 ? 120.775 111.130 165.591 1.00 42.30  ? 274 LEU B C   1 
ATOM   5761  O  O   . LEU B 1 299 ? 121.320 110.963 166.685 1.00 51.48  ? 274 LEU B O   1 
ATOM   5762  C  CB  . LEU B 1 299 ? 120.671 108.810 164.697 1.00 42.12  ? 274 LEU B CB  1 
ATOM   5763  C  CG  . LEU B 1 299 ? 119.908 107.498 164.543 1.00 30.42  ? 274 LEU B CG  1 
ATOM   5764  C  CD1 . LEU B 1 299 ? 120.872 106.341 164.463 1.00 36.32  ? 274 LEU B CD1 1 
ATOM   5765  C  CD2 . LEU B 1 299 ? 118.946 107.312 165.686 1.00 38.05  ? 274 LEU B CD2 1 
ATOM   5766  N  N   . ILE B 1 300 ? 120.964 112.220 164.854 1.00 40.78  ? 275 ILE B N   1 
ATOM   5767  C  CA  . ILE B 1 300 ? 121.794 113.314 165.336 1.00 43.11  ? 275 ILE B CA  1 
ATOM   5768  C  C   . ILE B 1 300 ? 121.011 114.236 166.266 1.00 53.55  ? 275 ILE B C   1 
ATOM   5769  O  O   . ILE B 1 300 ? 121.564 114.737 167.250 1.00 54.79  ? 275 ILE B O   1 
ATOM   5770  C  CB  . ILE B 1 300 ? 122.384 114.086 164.144 1.00 36.84  ? 275 ILE B CB  1 
ATOM   5771  C  CG1 . ILE B 1 300 ? 123.524 113.293 163.510 1.00 40.90  ? 275 ILE B CG1 1 
ATOM   5772  C  CG2 . ILE B 1 300 ? 122.881 115.447 164.568 1.00 42.66  ? 275 ILE B CG2 1 
ATOM   5773  C  CD1 . ILE B 1 300 ? 124.318 114.079 162.506 1.00 38.01  ? 275 ILE B CD1 1 
ATOM   5774  N  N   . LEU B 1 301 ? 119.726 114.442 165.997 1.00 56.05  ? 276 LEU B N   1 
ATOM   5775  C  CA  . LEU B 1 301 ? 118.888 115.350 166.766 1.00 54.09  ? 276 LEU B CA  1 
ATOM   5776  C  C   . LEU B 1 301 ? 118.220 114.683 167.961 1.00 56.30  ? 276 LEU B C   1 
ATOM   5777  O  O   . LEU B 1 301 ? 117.532 115.366 168.725 1.00 63.37  ? 276 LEU B O   1 
ATOM   5778  C  CB  . LEU B 1 301 ? 117.817 115.961 165.857 1.00 49.33  ? 276 LEU B CB  1 
ATOM   5779  C  CG  . LEU B 1 301 ? 118.218 116.155 164.394 1.00 43.77  ? 276 LEU B CG  1 
ATOM   5780  C  CD1 . LEU B 1 301 ? 117.015 116.520 163.557 1.00 43.04  ? 276 LEU B CD1 1 
ATOM   5781  C  CD2 . LEU B 1 301 ? 119.286 117.216 164.273 1.00 53.65  ? 276 LEU B CD2 1 
ATOM   5782  N  N   . SER B 1 302 ? 118.404 113.380 168.145 1.00 57.27  ? 277 SER B N   1 
ATOM   5783  C  CA  . SER B 1 302 ? 117.755 112.646 169.223 1.00 55.25  ? 277 SER B CA  1 
ATOM   5784  C  C   . SER B 1 302 ? 118.649 112.622 170.452 1.00 65.07  ? 277 SER B C   1 
ATOM   5785  O  O   . SER B 1 302 ? 119.843 112.325 170.350 1.00 68.73  ? 277 SER B O   1 
ATOM   5786  C  CB  . SER B 1 302 ? 117.438 111.218 168.785 1.00 63.83  ? 277 SER B CB  1 
ATOM   5787  O  OG  . SER B 1 302 ? 116.532 111.211 167.698 1.00 71.62  ? 277 SER B OG  1 
ATOM   5788  N  N   . HIS B 1 303 ? 118.070 112.924 171.614 1.00 81.21  ? 278 HIS B N   1 
ATOM   5789  C  CA  . HIS B 1 303 ? 118.838 112.880 172.850 1.00 80.39  ? 278 HIS B CA  1 
ATOM   5790  C  C   . HIS B 1 303 ? 119.072 111.461 173.346 1.00 83.54  ? 278 HIS B C   1 
ATOM   5791  O  O   . HIS B 1 303 ? 119.861 111.274 174.277 1.00 83.34  ? 278 HIS B O   1 
ATOM   5792  C  CB  . HIS B 1 303 ? 118.151 113.700 173.945 1.00 76.19  ? 278 HIS B CB  1 
ATOM   5793  C  CG  . HIS B 1 303 ? 116.678 113.460 174.055 1.00 82.13  ? 278 HIS B CG  1 
ATOM   5794  N  ND1 . HIS B 1 303 ? 115.770 113.974 173.156 1.00 84.16  ? 278 HIS B ND1 1 
ATOM   5795  C  CD2 . HIS B 1 303 ? 115.954 112.774 174.970 1.00 83.10  ? 278 HIS B CD2 1 
ATOM   5796  C  CE1 . HIS B 1 303 ? 114.550 113.609 173.507 1.00 83.58  ? 278 HIS B CE1 1 
ATOM   5797  N  NE2 . HIS B 1 303 ? 114.634 112.879 174.605 1.00 85.89  ? 278 HIS B NE2 1 
ATOM   5798  N  N   . HIS B 1 304 ? 118.408 110.466 172.756 1.00 77.85  ? 279 HIS B N   1 
ATOM   5799  C  CA  . HIS B 1 304 ? 118.676 109.081 173.126 1.00 74.26  ? 279 HIS B CA  1 
ATOM   5800  C  C   . HIS B 1 304 ? 120.098 108.680 172.763 1.00 74.85  ? 279 HIS B C   1 
ATOM   5801  O  O   . HIS B 1 304 ? 120.786 108.022 173.551 1.00 79.58  ? 279 HIS B O   1 
ATOM   5802  C  CB  . HIS B 1 304 ? 117.669 108.154 172.450 1.00 72.26  ? 279 HIS B CB  1 
ATOM   5803  C  CG  . HIS B 1 304 ? 116.305 108.200 173.060 1.00 75.33  ? 279 HIS B CG  1 
ATOM   5804  N  ND1 . HIS B 1 304 ? 115.454 107.117 173.060 1.00 78.46  ? 279 HIS B ND1 1 
ATOM   5805  C  CD2 . HIS B 1 304 ? 115.646 109.197 173.693 1.00 74.96  ? 279 HIS B CD2 1 
ATOM   5806  C  CE1 . HIS B 1 304 ? 114.328 107.446 173.666 1.00 76.57  ? 279 HIS B CE1 1 
ATOM   5807  N  NE2 . HIS B 1 304 ? 114.418 108.703 174.060 1.00 76.01  ? 279 HIS B NE2 1 
ATOM   5808  N  N   . SER B 1 305 ? 120.556 109.067 171.577 1.00 74.72  ? 280 SER B N   1 
ATOM   5809  C  CA  . SER B 1 305 ? 121.911 108.760 171.128 1.00 78.23  ? 280 SER B CA  1 
ATOM   5810  C  C   . SER B 1 305 ? 122.831 109.936 171.445 1.00 75.92  ? 280 SER B C   1 
ATOM   5811  O  O   . SER B 1 305 ? 123.310 110.653 170.566 1.00 69.76  ? 280 SER B O   1 
ATOM   5812  C  CB  . SER B 1 305 ? 121.914 108.437 169.640 1.00 75.81  ? 280 SER B CB  1 
ATOM   5813  O  OG  . SER B 1 305 ? 122.078 109.618 168.878 1.00 70.65  ? 280 SER B OG  1 
ATOM   5814  N  N   . GLU B 1 306 ? 123.074 110.126 172.742 1.00 86.82  ? 281 GLU B N   1 
ATOM   5815  C  CA  . GLU B 1 306 ? 123.877 111.262 173.177 1.00 90.02  ? 281 GLU B CA  1 
ATOM   5816  C  C   . GLU B 1 306 ? 125.364 110.999 172.975 1.00 90.86  ? 281 GLU B C   1 
ATOM   5817  O  O   . GLU B 1 306 ? 126.027 111.688 172.194 1.00 91.79  ? 281 GLU B O   1 
ATOM   5818  C  CB  . GLU B 1 306 ? 123.582 111.588 174.642 1.00 90.05  ? 281 GLU B CB  1 
ATOM   5819  C  CG  . GLU B 1 306 ? 124.340 112.799 175.162 1.00 89.97  ? 281 GLU B CG  1 
ATOM   5820  C  CD  . GLU B 1 306 ? 123.480 113.708 176.020 1.00 92.18  ? 281 GLU B CD  1 
ATOM   5821  O  OE1 . GLU B 1 306 ? 122.245 113.711 175.838 1.00 94.72  ? 281 GLU B OE1 1 
ATOM   5822  O  OE2 . GLU B 1 306 ? 124.040 114.421 176.877 1.00 91.85  ? 281 GLU B OE2 1 
ATOM   5823  N  N   . GLY B 1 307 ? 125.902 109.996 173.660 1.00 79.07  ? 282 GLY B N   1 
ATOM   5824  C  CA  . GLY B 1 307 ? 127.319 109.711 173.568 1.00 76.18  ? 282 GLY B CA  1 
ATOM   5825  C  C   . GLY B 1 307 ? 127.630 108.385 172.910 1.00 77.21  ? 282 GLY B C   1 
ATOM   5826  O  O   . GLY B 1 307 ? 128.748 107.876 173.027 1.00 79.54  ? 282 GLY B O   1 
ATOM   5827  N  N   . LEU B 1 308 ? 126.646 107.812 172.216 1.00 65.46  ? 283 LEU B N   1 
ATOM   5828  C  CA  . LEU B 1 308 ? 126.830 106.486 171.638 1.00 66.42  ? 283 LEU B CA  1 
ATOM   5829  C  C   . LEU B 1 308 ? 127.807 106.515 170.469 1.00 66.42  ? 283 LEU B C   1 
ATOM   5830  O  O   . LEU B 1 308 ? 128.660 105.630 170.348 1.00 68.62  ? 283 LEU B O   1 
ATOM   5831  C  CB  . LEU B 1 308 ? 125.483 105.917 171.203 1.00 63.91  ? 283 LEU B CB  1 
ATOM   5832  C  CG  . LEU B 1 308 ? 124.441 105.819 172.314 1.00 64.48  ? 283 LEU B CG  1 
ATOM   5833  C  CD1 . LEU B 1 308 ? 123.211 105.086 171.824 1.00 64.38  ? 283 LEU B CD1 1 
ATOM   5834  C  CD2 . LEU B 1 308 ? 125.024 105.132 173.534 1.00 65.68  ? 283 LEU B CD2 1 
ATOM   5835  N  N   . PHE B 1 309 ? 127.703 107.518 169.603 1.00 57.22  ? 284 PHE B N   1 
ATOM   5836  C  CA  . PHE B 1 309 ? 128.581 107.638 168.451 1.00 56.23  ? 284 PHE B CA  1 
ATOM   5837  C  C   . PHE B 1 309 ? 129.175 109.039 168.408 1.00 56.12  ? 284 PHE B C   1 
ATOM   5838  O  O   . PHE B 1 309 ? 128.788 109.926 169.171 1.00 64.91  ? 284 PHE B O   1 
ATOM   5839  C  CB  . PHE B 1 309 ? 127.843 107.316 167.147 1.00 52.90  ? 284 PHE B CB  1 
ATOM   5840  C  CG  . PHE B 1 309 ? 126.732 108.264 166.824 1.00 48.67  ? 284 PHE B CG  1 
ATOM   5841  C  CD1 . PHE B 1 309 ? 125.485 108.105 167.387 1.00 55.26  ? 284 PHE B CD1 1 
ATOM   5842  C  CD2 . PHE B 1 309 ? 126.931 109.302 165.940 1.00 46.79  ? 284 PHE B CD2 1 
ATOM   5843  C  CE1 . PHE B 1 309 ? 124.464 108.970 167.083 1.00 55.64  ? 284 PHE B CE1 1 
ATOM   5844  C  CE2 . PHE B 1 309 ? 125.914 110.169 165.634 1.00 49.25  ? 284 PHE B CE2 1 
ATOM   5845  C  CZ  . PHE B 1 309 ? 124.680 110.003 166.206 1.00 51.78  ? 284 PHE B CZ  1 
ATOM   5846  N  N   . GLN B 1 310 ? 130.134 109.234 167.505 1.00 48.93  ? 285 GLN B N   1 
ATOM   5847  C  CA  . GLN B 1 310 ? 130.879 110.484 167.440 1.00 46.50  ? 285 GLN B CA  1 
ATOM   5848  C  C   . GLN B 1 310 ? 130.913 111.139 166.069 1.00 49.49  ? 285 GLN B C   1 
ATOM   5849  O  O   . GLN B 1 310 ? 131.259 112.322 165.994 1.00 54.18  ? 285 GLN B O   1 
ATOM   5850  C  CB  . GLN B 1 310 ? 132.324 110.268 167.907 1.00 49.88  ? 285 GLN B CB  1 
ATOM   5851  C  CG  . GLN B 1 310 ? 132.469 110.099 169.403 1.00 57.04  ? 285 GLN B CG  1 
ATOM   5852  C  CD  . GLN B 1 310 ? 132.371 108.655 169.828 1.00 64.01  ? 285 GLN B CD  1 
ATOM   5853  O  OE1 . GLN B 1 310 ? 132.534 107.750 169.015 1.00 67.91  ? 285 GLN B OE1 1 
ATOM   5854  N  NE2 . GLN B 1 310 ? 132.105 108.428 171.108 1.00 59.80  ? 285 GLN B NE2 1 
ATOM   5855  N  N   . LYS B 1 311 ? 130.587 110.430 164.992 1.00 46.60  ? 286 LYS B N   1 
ATOM   5856  C  CA  . LYS B 1 311 ? 130.640 110.992 163.651 1.00 39.38  ? 286 LYS B CA  1 
ATOM   5857  C  C   . LYS B 1 311 ? 129.390 110.570 162.893 1.00 45.52  ? 286 LYS B C   1 
ATOM   5858  O  O   . LYS B 1 311 ? 128.504 109.911 163.439 1.00 58.67  ? 286 LYS B O   1 
ATOM   5859  C  CB  . LYS B 1 311 ? 131.907 110.550 162.915 1.00 38.17  ? 286 LYS B CB  1 
ATOM   5860  C  CG  . LYS B 1 311 ? 133.193 110.973 163.592 1.00 46.69  ? 286 LYS B CG  1 
ATOM   5861  C  CD  . LYS B 1 311 ? 134.317 110.010 163.282 1.00 52.17  ? 286 LYS B CD  1 
ATOM   5862  C  CE  . LYS B 1 311 ? 135.495 110.245 164.195 1.00 52.53  ? 286 LYS B CE  1 
ATOM   5863  N  NZ  . LYS B 1 311 ? 135.988 111.638 164.077 1.00 49.86  ? 286 LYS B NZ  1 
ATOM   5864  N  N   . ALA B 1 312 ? 129.315 110.962 161.624 1.00 32.66  ? 287 ALA B N   1 
ATOM   5865  C  CA  . ALA B 1 312 ? 128.198 110.579 160.776 1.00 24.80  ? 287 ALA B CA  1 
ATOM   5866  C  C   . ALA B 1 312 ? 128.582 110.817 159.327 1.00 28.09  ? 287 ALA B C   1 
ATOM   5867  O  O   . ALA B 1 312 ? 129.314 111.760 159.026 1.00 52.09  ? 287 ALA B O   1 
ATOM   5868  C  CB  . ALA B 1 312 ? 126.933 111.366 161.124 1.00 28.02  ? 287 ALA B CB  1 
ATOM   5869  N  N   . ILE B 1 313 ? 128.092 109.959 158.437 1.00 8.09   ? 288 ILE B N   1 
ATOM   5870  C  CA  . ILE B 1 313 ? 128.309 110.090 157.000 1.00 14.38  ? 288 ILE B CA  1 
ATOM   5871  C  C   . ILE B 1 313 ? 126.954 109.884 156.338 1.00 27.19  ? 288 ILE B C   1 
ATOM   5872  O  O   . ILE B 1 313 ? 126.533 108.745 156.120 1.00 48.92  ? 288 ILE B O   1 
ATOM   5873  C  CB  . ILE B 1 313 ? 129.334 109.087 156.463 1.00 25.45  ? 288 ILE B CB  1 
ATOM   5874  C  CG1 . ILE B 1 313 ? 130.662 109.200 157.205 1.00 40.32  ? 288 ILE B CG1 1 
ATOM   5875  C  CG2 . ILE B 1 313 ? 129.534 109.278 154.976 1.00 26.12  ? 288 ILE B CG2 1 
ATOM   5876  C  CD1 . ILE B 1 313 ? 131.632 108.095 156.870 1.00 35.44  ? 288 ILE B CD1 1 
ATOM   5877  N  N   . ALA B 1 314 ? 126.272 110.973 156.010 1.00 25.27  ? 289 ALA B N   1 
ATOM   5878  C  CA  . ALA B 1 314 ? 124.948 110.912 155.405 1.00 24.31  ? 289 ALA B CA  1 
ATOM   5879  C  C   . ALA B 1 314 ? 125.076 111.204 153.918 1.00 28.05  ? 289 ALA B C   1 
ATOM   5880  O  O   . ALA B 1 314 ? 125.324 112.346 153.527 1.00 52.96  ? 289 ALA B O   1 
ATOM   5881  C  CB  . ALA B 1 314 ? 124.005 111.905 156.075 1.00 30.36  ? 289 ALA B CB  1 
ATOM   5882  N  N   . GLN B 1 315 ? 124.892 110.184 153.088 1.00 26.95  ? 290 GLN B N   1 
ATOM   5883  C  CA  . GLN B 1 315 ? 125.020 110.325 151.645 1.00 36.69  ? 290 GLN B CA  1 
ATOM   5884  C  C   . GLN B 1 315 ? 123.664 110.140 150.981 1.00 35.53  ? 290 GLN B C   1 
ATOM   5885  O  O   . GLN B 1 315 ? 122.994 109.130 151.206 1.00 47.66  ? 290 GLN B O   1 
ATOM   5886  C  CB  . GLN B 1 315 ? 126.028 109.321 151.083 1.00 33.27  ? 290 GLN B CB  1 
ATOM   5887  C  CG  . GLN B 1 315 ? 125.956 107.939 151.692 1.00 38.70  ? 290 GLN B CG  1 
ATOM   5888  C  CD  . GLN B 1 315 ? 127.252 107.170 151.542 1.00 37.75  ? 290 GLN B CD  1 
ATOM   5889  O  OE1 . GLN B 1 315 ? 128.324 107.758 151.452 1.00 34.13  ? 290 GLN B OE1 1 
ATOM   5890  N  NE2 . GLN B 1 315 ? 127.157 105.849 151.513 1.00 39.45  ? 290 GLN B NE2 1 
ATOM   5891  N  N   . SER B 1 316 ? 123.271 111.117 150.163 1.00 32.39  ? 291 SER B N   1 
ATOM   5892  C  CA  . SER B 1 316 ? 122.014 111.082 149.415 1.00 28.57  ? 291 SER B CA  1 
ATOM   5893  C  C   . SER B 1 316 ? 120.811 110.928 150.339 1.00 34.57  ? 291 SER B C   1 
ATOM   5894  O  O   . SER B 1 316 ? 119.834 110.258 150.009 1.00 54.70  ? 291 SER B O   1 
ATOM   5895  C  CB  . SER B 1 316 ? 122.025 109.973 148.365 1.00 37.42  ? 291 SER B CB  1 
ATOM   5896  O  OG  . SER B 1 316 ? 123.128 110.106 147.495 1.00 46.13  ? 291 SER B OG  1 
ATOM   5897  N  N   . GLY B 1 317 ? 120.874 111.556 151.500 1.00 30.88  ? 292 GLY B N   1 
ATOM   5898  C  CA  . GLY B 1 317 ? 119.789 111.460 152.460 1.00 38.80  ? 292 GLY B CA  1 
ATOM   5899  C  C   . GLY B 1 317 ? 119.718 112.704 153.309 1.00 47.23  ? 292 GLY B C   1 
ATOM   5900  O  O   . GLY B 1 317 ? 120.716 113.404 153.503 1.00 56.31  ? 292 GLY B O   1 
ATOM   5901  N  N   . THR B 1 318 ? 118.521 112.989 153.811 1.00 44.53  ? 293 THR B N   1 
ATOM   5902  C  CA  . THR B 1 318 ? 118.310 114.144 154.666 1.00 36.29  ? 293 THR B CA  1 
ATOM   5903  C  C   . THR B 1 318 ? 117.103 113.872 155.550 1.00 44.54  ? 293 THR B C   1 
ATOM   5904  O  O   . THR B 1 318 ? 116.290 112.990 155.267 1.00 50.71  ? 293 THR B O   1 
ATOM   5905  C  CB  . THR B 1 318 ? 118.090 115.418 153.849 1.00 48.30  ? 293 THR B CB  1 
ATOM   5906  O  OG1 . THR B 1 318 ? 118.880 115.368 152.658 1.00 53.07  ? 293 THR B OG1 1 
ATOM   5907  C  CG2 . THR B 1 318 ? 118.517 116.627 154.649 1.00 49.94  ? 293 THR B CG2 1 
ATOM   5908  N  N   . ALA B 1 319 ? 117.000 114.632 156.634 1.00 39.61  ? 294 ALA B N   1 
ATOM   5909  C  CA  . ALA B 1 319 ? 115.847 114.563 157.516 1.00 40.93  ? 294 ALA B CA  1 
ATOM   5910  C  C   . ALA B 1 319 ? 114.831 115.659 157.246 1.00 45.65  ? 294 ALA B C   1 
ATOM   5911  O  O   . ALA B 1 319 ? 113.848 115.766 157.984 1.00 51.32  ? 294 ALA B O   1 
ATOM   5912  C  CB  . ALA B 1 319 ? 116.292 114.631 158.977 1.00 45.30  ? 294 ALA B CB  1 
ATOM   5913  N  N   . ILE B 1 320 ? 115.041 116.478 156.217 1.00 44.21  ? 295 ILE B N   1 
ATOM   5914  C  CA  . ILE B 1 320 ? 114.170 117.609 155.930 1.00 46.05  ? 295 ILE B CA  1 
ATOM   5915  C  C   . ILE B 1 320 ? 113.509 117.518 154.566 1.00 51.90  ? 295 ILE B C   1 
ATOM   5916  O  O   . ILE B 1 320 ? 112.774 118.434 154.190 1.00 53.51  ? 295 ILE B O   1 
ATOM   5917  C  CB  . ILE B 1 320 ? 114.924 118.947 156.065 1.00 40.64  ? 295 ILE B CB  1 
ATOM   5918  C  CG1 . ILE B 1 320 ? 115.819 119.187 154.858 1.00 39.91  ? 295 ILE B CG1 1 
ATOM   5919  C  CG2 . ILE B 1 320 ? 115.760 118.965 157.323 1.00 43.11  ? 295 ILE B CG2 1 
ATOM   5920  C  CD1 . ILE B 1 320 ? 116.653 120.432 154.980 1.00 44.38  ? 295 ILE B CD1 1 
ATOM   5921  N  N   . SER B 1 321 ? 113.735 116.445 153.813 1.00 46.60  ? 296 SER B N   1 
ATOM   5922  C  CA  . SER B 1 321 ? 113.097 116.304 152.516 1.00 45.11  ? 296 SER B CA  1 
ATOM   5923  C  C   . SER B 1 321 ? 111.642 115.879 152.695 1.00 56.46  ? 296 SER B C   1 
ATOM   5924  O  O   . SER B 1 321 ? 111.148 115.712 153.812 1.00 62.11  ? 296 SER B O   1 
ATOM   5925  C  CB  . SER B 1 321 ? 113.866 115.316 151.646 1.00 41.15  ? 296 SER B CB  1 
ATOM   5926  O  OG  . SER B 1 321 ? 114.242 114.174 152.387 1.00 54.76  ? 296 SER B OG  1 
ATOM   5927  N  N   . SER B 1 322 ? 110.938 115.714 151.574 1.00 48.88  ? 297 SER B N   1 
ATOM   5928  C  CA  . SER B 1 322 ? 109.510 115.419 151.635 1.00 42.55  ? 297 SER B CA  1 
ATOM   5929  C  C   . SER B 1 322 ? 109.243 114.025 152.185 1.00 40.46  ? 297 SER B C   1 
ATOM   5930  O  O   . SER B 1 322 ? 108.304 113.833 152.964 1.00 47.00  ? 297 SER B O   1 
ATOM   5931  C  CB  . SER B 1 322 ? 108.886 115.577 150.251 1.00 41.64  ? 297 SER B CB  1 
ATOM   5932  O  OG  . SER B 1 322 ? 109.779 115.157 149.236 1.00 41.41  ? 297 SER B OG  1 
ATOM   5933  N  N   . TRP B 1 323 ? 110.054 113.043 151.801 1.00 34.41  ? 298 TRP B N   1 
ATOM   5934  C  CA  . TRP B 1 323 ? 109.814 111.642 152.140 1.00 39.99  ? 298 TRP B CA  1 
ATOM   5935  C  C   . TRP B 1 323 ? 110.725 111.146 153.250 1.00 41.40  ? 298 TRP B C   1 
ATOM   5936  O  O   . TRP B 1 323 ? 111.184 110.004 153.210 1.00 50.50  ? 298 TRP B O   1 
ATOM   5937  C  CB  . TRP B 1 323 ? 109.972 110.764 150.905 1.00 39.94  ? 298 TRP B CB  1 
ATOM   5938  C  CG  . TRP B 1 323 ? 111.243 110.987 150.154 1.00 37.01  ? 298 TRP B CG  1 
ATOM   5939  C  CD1 . TRP B 1 323 ? 112.470 111.258 150.675 1.00 41.25  ? 298 TRP B CD1 1 
ATOM   5940  C  CD2 . TRP B 1 323 ? 111.411 110.950 148.738 1.00 39.26  ? 298 TRP B CD2 1 
ATOM   5941  N  NE1 . TRP B 1 323 ? 113.392 111.394 149.671 1.00 39.39  ? 298 TRP B NE1 1 
ATOM   5942  C  CE2 . TRP B 1 323 ? 112.762 111.210 148.470 1.00 36.17  ? 298 TRP B CE2 1 
ATOM   5943  C  CE3 . TRP B 1 323 ? 110.547 110.723 147.669 1.00 43.96  ? 298 TRP B CE3 1 
ATOM   5944  C  CZ2 . TRP B 1 323 ? 113.265 111.248 147.186 1.00 33.69  ? 298 TRP B CZ2 1 
ATOM   5945  C  CZ3 . TRP B 1 323 ? 111.051 110.762 146.397 1.00 39.56  ? 298 TRP B CZ3 1 
ATOM   5946  C  CH2 . TRP B 1 323 ? 112.396 111.021 146.163 1.00 30.77  ? 298 TRP B CH2 1 
ATOM   5947  N  N   . SER B 1 324 ? 111.015 111.974 154.248 1.00 41.09  ? 299 SER B N   1 
ATOM   5948  C  CA  . SER B 1 324 ? 111.892 111.567 155.334 1.00 41.08  ? 299 SER B CA  1 
ATOM   5949  C  C   . SER B 1 324 ? 111.186 111.406 156.666 1.00 44.87  ? 299 SER B C   1 
ATOM   5950  O  O   . SER B 1 324 ? 111.676 110.666 157.517 1.00 50.78  ? 299 SER B O   1 
ATOM   5951  C  CB  . SER B 1 324 ? 113.035 112.570 155.500 1.00 46.33  ? 299 SER B CB  1 
ATOM   5952  O  OG  . SER B 1 324 ? 114.177 112.145 154.780 1.00 52.02  ? 299 SER B OG  1 
ATOM   5953  N  N   . VAL B 1 325 ? 110.060 112.078 156.874 1.00 46.38  ? 300 VAL B N   1 
ATOM   5954  C  CA  . VAL B 1 325 ? 109.293 111.963 158.109 1.00 45.20  ? 300 VAL B CA  1 
ATOM   5955  C  C   . VAL B 1 325 ? 107.817 111.861 157.753 1.00 53.37  ? 300 VAL B C   1 
ATOM   5956  O  O   . VAL B 1 325 ? 107.339 112.539 156.838 1.00 55.42  ? 300 VAL B O   1 
ATOM   5957  C  CB  . VAL B 1 325 ? 109.555 113.153 159.055 1.00 38.52  ? 300 VAL B CB  1 
ATOM   5958  C  CG1 . VAL B 1 325 ? 108.649 113.087 160.263 1.00 48.68  ? 300 VAL B CG1 1 
ATOM   5959  C  CG2 . VAL B 1 325 ? 110.997 113.167 159.501 1.00 40.51  ? 300 VAL B CG2 1 
ATOM   5960  N  N   . ASN B 1 326 ? 107.097 111.000 158.467 1.00 61.98  ? 301 ASN B N   1 
ATOM   5961  C  CA  . ASN B 1 326 ? 105.656 110.853 158.302 1.00 59.53  ? 301 ASN B CA  1 
ATOM   5962  C  C   . ASN B 1 326 ? 104.962 111.840 159.231 1.00 64.55  ? 301 ASN B C   1 
ATOM   5963  O  O   . ASN B 1 326 ? 105.089 111.743 160.455 1.00 62.99  ? 301 ASN B O   1 
ATOM   5964  C  CB  . ASN B 1 326 ? 105.229 109.421 158.602 1.00 59.56  ? 301 ASN B CB  1 
ATOM   5965  C  CG  . ASN B 1 326 ? 103.765 109.185 158.339 1.00 60.36  ? 301 ASN B CG  1 
ATOM   5966  O  OD1 . ASN B 1 326 ? 103.094 110.010 157.722 1.00 63.42  ? 301 ASN B OD1 1 
ATOM   5967  N  ND2 . ASN B 1 326 ? 103.258 108.052 158.803 1.00 58.42  ? 301 ASN B ND2 1 
ATOM   5968  N  N   . TYR B 1 327 ? 104.223 112.786 158.654 1.00 65.39  ? 302 TYR B N   1 
ATOM   5969  C  CA  . TYR B 1 327 ? 103.615 113.865 159.420 1.00 63.70  ? 302 TYR B CA  1 
ATOM   5970  C  C   . TYR B 1 327 ? 102.161 113.607 159.785 1.00 67.11  ? 302 TYR B C   1 
ATOM   5971  O  O   . TYR B 1 327 ? 101.633 114.293 160.666 1.00 74.99  ? 302 TYR B O   1 
ATOM   5972  C  CB  . TYR B 1 327 ? 103.712 115.182 158.646 1.00 62.16  ? 302 TYR B CB  1 
ATOM   5973  C  CG  . TYR B 1 327 ? 105.046 115.865 158.796 1.00 63.14  ? 302 TYR B CG  1 
ATOM   5974  C  CD1 . TYR B 1 327 ? 105.533 116.206 160.046 1.00 66.05  ? 302 TYR B CD1 1 
ATOM   5975  C  CD2 . TYR B 1 327 ? 105.819 116.166 157.688 1.00 67.02  ? 302 TYR B CD2 1 
ATOM   5976  C  CE1 . TYR B 1 327 ? 106.750 116.828 160.190 1.00 69.34  ? 302 TYR B CE1 1 
ATOM   5977  C  CE2 . TYR B 1 327 ? 107.038 116.787 157.821 1.00 71.40  ? 302 TYR B CE2 1 
ATOM   5978  C  CZ  . TYR B 1 327 ? 107.499 117.116 159.074 1.00 74.56  ? 302 TYR B CZ  1 
ATOM   5979  O  OH  . TYR B 1 327 ? 108.717 117.738 159.209 1.00 75.16  ? 302 TYR B OH  1 
ATOM   5980  N  N   . GLN B 1 328 ? 101.501 112.654 159.135 1.00 67.77  ? 303 GLN B N   1 
ATOM   5981  C  CA  . GLN B 1 328 ? 100.118 112.295 159.448 1.00 70.25  ? 303 GLN B CA  1 
ATOM   5982  C  C   . GLN B 1 328 ? 100.022 110.782 159.566 1.00 70.54  ? 303 GLN B C   1 
ATOM   5983  O  O   . GLN B 1 328 ? 99.483  110.102 158.686 1.00 75.38  ? 303 GLN B O   1 
ATOM   5984  C  CB  . GLN B 1 328 ? 99.160  112.836 158.386 1.00 72.97  ? 303 GLN B CB  1 
ATOM   5985  C  CG  . GLN B 1 328 ? 99.723  112.819 156.981 1.00 73.74  ? 303 GLN B CG  1 
ATOM   5986  C  CD  . GLN B 1 328 ? 98.841  113.553 155.996 1.00 76.17  ? 303 GLN B CD  1 
ATOM   5987  O  OE1 . GLN B 1 328 ? 97.817  114.124 156.369 1.00 77.04  ? 303 GLN B OE1 1 
ATOM   5988  N  NE2 . GLN B 1 328 ? 99.235  113.545 154.728 1.00 76.76  ? 303 GLN B NE2 1 
ATOM   5989  N  N   . PRO B 1 329 ? 100.544 110.215 160.656 1.00 65.24  ? 304 PRO B N   1 
ATOM   5990  C  CA  . PRO B 1 329 ? 100.553 108.754 160.784 1.00 67.87  ? 304 PRO B CA  1 
ATOM   5991  C  C   . PRO B 1 329 ? 99.224  108.173 161.218 1.00 71.90  ? 304 PRO B C   1 
ATOM   5992  O  O   . PRO B 1 329 ? 98.967  106.993 160.941 1.00 70.54  ? 304 PRO B O   1 
ATOM   5993  C  CB  . PRO B 1 329 ? 101.625 108.512 161.848 1.00 65.53  ? 304 PRO B CB  1 
ATOM   5994  C  CG  . PRO B 1 329 ? 101.519 109.712 162.723 1.00 68.66  ? 304 PRO B CG  1 
ATOM   5995  C  CD  . PRO B 1 329 ? 101.105 110.872 161.848 1.00 66.33  ? 304 PRO B CD  1 
ATOM   5996  N  N   . LEU B 1 330 ? 98.379  108.957 161.890 1.00 80.56  ? 305 LEU B N   1 
ATOM   5997  C  CA  . LEU B 1 330 ? 97.106  108.434 162.371 1.00 77.79  ? 305 LEU B CA  1 
ATOM   5998  C  C   . LEU B 1 330 ? 96.208  108.018 161.216 1.00 79.37  ? 305 LEU B C   1 
ATOM   5999  O  O   . LEU B 1 330 ? 95.532  106.986 161.289 1.00 82.83  ? 305 LEU B O   1 
ATOM   6000  C  CB  . LEU B 1 330 ? 96.412  109.473 163.248 1.00 76.73  ? 305 LEU B CB  1 
ATOM   6001  C  CG  . LEU B 1 330 ? 95.172  108.995 164.006 1.00 80.88  ? 305 LEU B CG  1 
ATOM   6002  C  CD1 . LEU B 1 330 ? 95.389  107.622 164.618 1.00 79.12  ? 305 LEU B CD1 1 
ATOM   6003  C  CD2 . LEU B 1 330 ? 94.777  110.004 165.074 1.00 81.69  ? 305 LEU B CD2 1 
ATOM   6004  N  N   . LYS B 1 331 ? 96.196  108.803 160.137 1.00 72.01  ? 306 LYS B N   1 
ATOM   6005  C  CA  . LYS B 1 331 ? 95.356  108.478 158.989 1.00 74.14  ? 306 LYS B CA  1 
ATOM   6006  C  C   . LYS B 1 331 ? 95.734  107.129 158.390 1.00 73.74  ? 306 LYS B C   1 
ATOM   6007  O  O   . LYS B 1 331 ? 94.877  106.260 158.194 1.00 77.40  ? 306 LYS B O   1 
ATOM   6008  C  CB  . LYS B 1 331 ? 95.465  109.575 157.932 1.00 73.25  ? 306 LYS B CB  1 
ATOM   6009  C  CG  . LYS B 1 331 ? 94.744  109.245 156.640 1.00 75.75  ? 306 LYS B CG  1 
ATOM   6010  C  CD  . LYS B 1 331 ? 95.505  109.760 155.429 1.00 74.34  ? 306 LYS B CD  1 
ATOM   6011  C  CE  . LYS B 1 331 ? 95.447  111.272 155.319 1.00 75.04  ? 306 LYS B CE  1 
ATOM   6012  N  NZ  . LYS B 1 331 ? 95.787  111.730 153.944 1.00 72.95  ? 306 LYS B NZ  1 
ATOM   6013  N  N   . TYR B 1 332 ? 97.021  106.930 158.099 1.00 66.38  ? 307 TYR B N   1 
ATOM   6014  C  CA  . TYR B 1 332 ? 97.437  105.681 157.472 1.00 69.17  ? 307 TYR B CA  1 
ATOM   6015  C  C   . TYR B 1 332 ? 97.340  104.507 158.433 1.00 70.72  ? 307 TYR B C   1 
ATOM   6016  O  O   . TYR B 1 332 ? 97.039  103.386 158.009 1.00 74.79  ? 307 TYR B O   1 
ATOM   6017  C  CB  . TYR B 1 332 ? 98.851  105.814 156.918 1.00 66.86  ? 307 TYR B CB  1 
ATOM   6018  C  CG  . TYR B 1 332 ? 98.953  106.798 155.780 1.00 69.75  ? 307 TYR B CG  1 
ATOM   6019  C  CD1 . TYR B 1 332 ? 98.640  106.421 154.486 1.00 70.07  ? 307 TYR B CD1 1 
ATOM   6020  C  CD2 . TYR B 1 332 ? 99.351  108.105 156.001 1.00 69.29  ? 307 TYR B CD2 1 
ATOM   6021  C  CE1 . TYR B 1 332 ? 98.727  107.313 153.445 1.00 68.65  ? 307 TYR B CE1 1 
ATOM   6022  C  CE2 . TYR B 1 332 ? 99.442  109.004 154.967 1.00 70.30  ? 307 TYR B CE2 1 
ATOM   6023  C  CZ  . TYR B 1 332 ? 99.129  108.603 153.691 1.00 71.65  ? 307 TYR B CZ  1 
ATOM   6024  O  OH  . TYR B 1 332 ? 99.221  109.502 152.656 1.00 74.72  ? 307 TYR B OH  1 
ATOM   6025  N  N   . THR B 1 333 ? 97.574  104.737 159.726 1.00 75.93  ? 308 THR B N   1 
ATOM   6026  C  CA  . THR B 1 333 ? 97.360  103.672 160.697 1.00 72.96  ? 308 THR B CA  1 
ATOM   6027  C  C   . THR B 1 333 ? 95.901  103.236 160.716 1.00 74.04  ? 308 THR B C   1 
ATOM   6028  O  O   . THR B 1 333 ? 95.608  102.037 160.764 1.00 77.35  ? 308 THR B O   1 
ATOM   6029  C  CB  . THR B 1 333 ? 97.799  104.122 162.088 1.00 74.57  ? 308 THR B CB  1 
ATOM   6030  O  OG1 . THR B 1 333 ? 99.154  104.583 162.035 1.00 82.68  ? 308 THR B OG1 1 
ATOM   6031  C  CG2 . THR B 1 333 ? 97.703  102.969 163.068 1.00 71.83  ? 308 THR B CG2 1 
ATOM   6032  N  N   . ARG B 1 334 ? 94.970  104.194 160.671 1.00 82.06  ? 309 ARG B N   1 
ATOM   6033  C  CA  . ARG B 1 334 ? 93.553  103.844 160.651 1.00 80.97  ? 309 ARG B CA  1 
ATOM   6034  C  C   . ARG B 1 334 ? 93.167  103.139 159.355 1.00 80.10  ? 309 ARG B C   1 
ATOM   6035  O  O   . ARG B 1 334 ? 92.347  102.214 159.370 1.00 82.25  ? 309 ARG B O   1 
ATOM   6036  C  CB  . ARG B 1 334 ? 92.701  105.092 160.863 1.00 81.58  ? 309 ARG B CB  1 
ATOM   6037  C  CG  . ARG B 1 334 ? 92.246  105.280 162.299 1.00 79.82  ? 309 ARG B CG  1 
ATOM   6038  C  CD  . ARG B 1 334 ? 91.038  106.199 162.393 1.00 84.64  ? 309 ARG B CD  1 
ATOM   6039  N  NE  . ARG B 1 334 ? 91.324  107.538 161.892 1.00 88.62  ? 309 ARG B NE  1 
ATOM   6040  C  CZ  . ARG B 1 334 ? 90.961  107.988 160.699 1.00 88.07  ? 309 ARG B CZ  1 
ATOM   6041  N  NH1 . ARG B 1 334 ? 90.292  107.229 159.847 1.00 86.28  ? 309 ARG B NH1 1 
ATOM   6042  N  NH2 . ARG B 1 334 ? 91.283  109.230 160.348 1.00 83.28  ? 309 ARG B NH2 1 
ATOM   6043  N  N   . LEU B 1 335 ? 93.737  103.561 158.223 1.00 74.24  ? 310 LEU B N   1 
ATOM   6044  C  CA  . LEU B 1 335 ? 93.480  102.841 156.978 1.00 76.21  ? 310 LEU B CA  1 
ATOM   6045  C  C   . LEU B 1 335 ? 93.966  101.402 157.061 1.00 77.21  ? 310 LEU B C   1 
ATOM   6046  O  O   . LEU B 1 335 ? 93.270  100.478 156.623 1.00 83.26  ? 310 LEU B O   1 
ATOM   6047  C  CB  . LEU B 1 335 ? 94.129  103.543 155.785 1.00 76.31  ? 310 LEU B CB  1 
ATOM   6048  C  CG  . LEU B 1 335 ? 93.302  104.562 154.999 1.00 81.39  ? 310 LEU B CG  1 
ATOM   6049  C  CD1 . LEU B 1 335 ? 93.410  105.977 155.538 1.00 78.06  ? 310 LEU B CD1 1 
ATOM   6050  C  CD2 . LEU B 1 335 ? 93.685  104.504 153.526 1.00 78.62  ? 310 LEU B CD2 1 
ATOM   6051  N  N   . LEU B 1 336 ? 95.161  101.187 157.613 1.00 77.23  ? 311 LEU B N   1 
ATOM   6052  C  CA  . LEU B 1 336 ? 95.667  99.825  157.731 1.00 78.76  ? 311 LEU B CA  1 
ATOM   6053  C  C   . LEU B 1 336 ? 94.824  99.009  158.702 1.00 82.12  ? 311 LEU B C   1 
ATOM   6054  O  O   . LEU B 1 336 ? 94.589  97.818  158.477 1.00 84.89  ? 311 LEU B O   1 
ATOM   6055  C  CB  . LEU B 1 336 ? 97.130  99.830  158.167 1.00 77.96  ? 311 LEU B CB  1 
ATOM   6056  C  CG  . LEU B 1 336 ? 97.667  98.427  158.453 1.00 75.11  ? 311 LEU B CG  1 
ATOM   6057  C  CD1 . LEU B 1 336 ? 98.295  97.829  157.211 1.00 76.30  ? 311 LEU B CD1 1 
ATOM   6058  C  CD2 . LEU B 1 336 ? 98.651  98.428  159.598 1.00 76.18  ? 311 LEU B CD2 1 
ATOM   6059  N  N   . ALA B 1 337 ? 94.362  99.631  159.788 1.00 89.92  ? 312 ALA B N   1 
ATOM   6060  C  CA  . ALA B 1 337 ? 93.498  98.926  160.728 1.00 88.99  ? 312 ALA B CA  1 
ATOM   6061  C  C   . ALA B 1 337 ? 92.191  98.511  160.066 1.00 89.15  ? 312 ALA B C   1 
ATOM   6062  O  O   . ALA B 1 337 ? 91.713  97.388  160.266 1.00 90.53  ? 312 ALA B O   1 
ATOM   6063  C  CB  . ALA B 1 337 ? 93.229  99.802  161.950 1.00 88.86  ? 312 ALA B CB  1 
ATOM   6064  N  N   . ALA B 1 338 ? 91.599  99.404  159.271 1.00 90.23  ? 313 ALA B N   1 
ATOM   6065  C  CA  . ALA B 1 338 ? 90.374  99.061  158.557 1.00 92.15  ? 313 ALA B CA  1 
ATOM   6066  C  C   . ALA B 1 338 ? 90.618  97.955  157.539 1.00 92.12  ? 313 ALA B C   1 
ATOM   6067  O  O   . ALA B 1 338 ? 89.791  97.049  157.386 1.00 95.05  ? 313 ALA B O   1 
ATOM   6068  C  CB  . ALA B 1 338 ? 89.802  100.301 157.873 1.00 90.31  ? 313 ALA B CB  1 
ATOM   6069  N  N   . LYS B 1 339 ? 91.744  98.014  156.828 1.00 86.09  ? 314 LYS B N   1 
ATOM   6070  C  CA  . LYS B 1 339 ? 92.022  97.013  155.804 1.00 84.29  ? 314 LYS B CA  1 
ATOM   6071  C  C   . LYS B 1 339 ? 92.289  95.644  156.419 1.00 85.33  ? 314 LYS B C   1 
ATOM   6072  O  O   . LYS B 1 339 ? 91.838  94.623  155.888 1.00 86.51  ? 314 LYS B O   1 
ATOM   6073  C  CB  . LYS B 1 339 ? 93.206  97.455  154.946 1.00 83.12  ? 314 LYS B CB  1 
ATOM   6074  C  CG  . LYS B 1 339 ? 93.380  96.644  153.676 1.00 84.74  ? 314 LYS B CG  1 
ATOM   6075  C  CD  . LYS B 1 339 ? 93.873  97.509  152.530 1.00 85.52  ? 314 LYS B CD  1 
ATOM   6076  C  CE  . LYS B 1 339 ? 92.981  98.719  152.326 1.00 83.94  ? 314 LYS B CE  1 
ATOM   6077  N  NZ  . LYS B 1 339 ? 93.410  99.528  151.152 1.00 83.25  ? 314 LYS B NZ  1 
ATOM   6078  N  N   . VAL B 1 340 ? 93.021  95.603  157.533 1.00 95.43  ? 315 VAL B N   1 
ATOM   6079  C  CA  . VAL B 1 340 ? 93.395  94.327  158.137 1.00 97.06  ? 315 VAL B CA  1 
ATOM   6080  C  C   . VAL B 1 340 ? 92.161  93.586  158.632 1.00 99.27  ? 315 VAL B C   1 
ATOM   6081  O  O   . VAL B 1 340 ? 92.017  92.378  158.412 1.00 100.63 ? 315 VAL B O   1 
ATOM   6082  C  CB  . VAL B 1 340 ? 94.418  94.552  159.265 1.00 97.51  ? 315 VAL B CB  1 
ATOM   6083  C  CG1 . VAL B 1 340 ? 94.321  93.452  160.307 1.00 98.94  ? 315 VAL B CG1 1 
ATOM   6084  C  CG2 . VAL B 1 340 ? 95.821  94.620  158.698 1.00 96.17  ? 315 VAL B CG2 1 
ATOM   6085  N  N   . GLY B 1 341 ? 91.245  94.292  159.288 1.00 106.06 ? 316 GLY B N   1 
ATOM   6086  C  CA  . GLY B 1 341 ? 90.039  93.654  159.770 1.00 106.96 ? 316 GLY B CA  1 
ATOM   6087  C  C   . GLY B 1 341 ? 89.521  94.153  161.102 1.00 107.54 ? 316 GLY B C   1 
ATOM   6088  O  O   . GLY B 1 341 ? 88.477  93.686  161.566 1.00 109.79 ? 316 GLY B O   1 
ATOM   6089  N  N   . CYS B 1 342 ? 90.224  95.089  161.737 1.00 111.52 ? 317 CYS B N   1 
ATOM   6090  C  CA  . CYS B 1 342 ? 89.723  95.679  162.975 1.00 113.91 ? 317 CYS B CA  1 
ATOM   6091  C  C   . CYS B 1 342 ? 90.128  97.141  163.041 1.00 111.44 ? 317 CYS B C   1 
ATOM   6092  O  O   . CYS B 1 342 ? 91.320  97.458  163.074 1.00 113.71 ? 317 CYS B O   1 
ATOM   6093  C  CB  . CYS B 1 342 ? 90.225  94.917  164.206 1.00 116.49 ? 317 CYS B CB  1 
ATOM   6094  S  SG  . CYS B 1 342 ? 92.007  94.910  164.513 1.00 119.90 ? 317 CYS B SG  1 
ATOM   6095  N  N   . ASP B 1 343 ? 89.132  98.026  163.060 1.00 111.32 ? 318 ASP B N   1 
ATOM   6096  C  CA  . ASP B 1 343 ? 89.337  99.471  163.154 1.00 114.27 ? 318 ASP B CA  1 
ATOM   6097  C  C   . ASP B 1 343 ? 88.402  99.998  164.238 1.00 113.72 ? 318 ASP B C   1 
ATOM   6098  O  O   . ASP B 1 343 ? 87.273  100.406 163.953 1.00 112.58 ? 318 ASP B O   1 
ATOM   6099  C  CB  . ASP B 1 343 ? 89.086  100.149 161.811 1.00 112.93 ? 318 ASP B CB  1 
ATOM   6100  C  CG  . ASP B 1 343 ? 89.207  101.656 161.887 1.00 113.38 ? 318 ASP B CG  1 
ATOM   6101  O  OD1 . ASP B 1 343 ? 89.918  102.153 162.786 1.00 113.80 ? 318 ASP B OD1 1 
ATOM   6102  O  OD2 . ASP B 1 343 ? 88.588  102.344 161.049 1.00 110.25 ? 318 ASP B OD2 1 
ATOM   6103  N  N   . ARG B 1 344 ? 88.873  99.986  165.478 1.00 113.06 ? 319 ARG B N   1 
ATOM   6104  C  CA  . ARG B 1 344 ? 88.102  100.501 166.598 1.00 112.69 ? 319 ARG B CA  1 
ATOM   6105  C  C   . ARG B 1 344 ? 88.403  101.979 166.811 1.00 113.56 ? 319 ARG B C   1 
ATOM   6106  O  O   . ARG B 1 344 ? 89.495  102.461 166.502 1.00 113.48 ? 319 ARG B O   1 
ATOM   6107  C  CB  . ARG B 1 344 ? 88.410  99.713  167.871 1.00 113.82 ? 319 ARG B CB  1 
ATOM   6108  C  CG  . ARG B 1 344 ? 88.603  98.222  167.643 1.00 114.20 ? 319 ARG B CG  1 
ATOM   6109  C  CD  . ARG B 1 344 ? 87.277  97.520  167.404 1.00 114.09 ? 319 ARG B CD  1 
ATOM   6110  N  NE  . ARG B 1 344 ? 87.455  96.118  167.045 1.00 113.61 ? 319 ARG B NE  1 
ATOM   6111  C  CZ  . ARG B 1 344 ? 87.138  95.600  165.867 1.00 113.27 ? 319 ARG B CZ  1 
ATOM   6112  N  NH1 . ARG B 1 344 ? 86.616  96.341  164.904 1.00 112.91 ? 319 ARG B NH1 1 
ATOM   6113  N  NH2 . ARG B 1 344 ? 87.348  94.305  165.650 1.00 111.45 ? 319 ARG B NH2 1 
ATOM   6114  N  N   . GLU B 1 345 ? 87.412  102.699 167.342 1.00 128.55 ? 320 GLU B N   1 
ATOM   6115  C  CA  . GLU B 1 345 ? 87.586  104.127 167.587 1.00 128.81 ? 320 GLU B CA  1 
ATOM   6116  C  C   . GLU B 1 345 ? 88.662  104.392 168.630 1.00 128.58 ? 320 GLU B C   1 
ATOM   6117  O  O   . GLU B 1 345 ? 89.280  105.462 168.627 1.00 126.47 ? 320 GLU B O   1 
ATOM   6118  C  CB  . GLU B 1 345 ? 86.262  104.751 168.025 1.00 127.88 ? 320 GLU B CB  1 
ATOM   6119  C  CG  . GLU B 1 345 ? 85.759  104.248 169.369 1.00 128.73 ? 320 GLU B CG  1 
ATOM   6120  C  CD  . GLU B 1 345 ? 85.000  105.304 170.142 1.00 128.70 ? 320 GLU B CD  1 
ATOM   6121  O  OE1 . GLU B 1 345 ? 84.513  106.268 169.516 1.00 129.52 ? 320 GLU B OE1 1 
ATOM   6122  O  OE2 . GLU B 1 345 ? 84.892  105.172 171.379 1.00 127.78 ? 320 GLU B OE2 1 
ATOM   6123  N  N   . ASP B 1 346 ? 88.896  103.440 169.529 1.00 133.00 ? 321 ASP B N   1 
ATOM   6124  C  CA  . ASP B 1 346 ? 89.899  103.589 170.572 1.00 133.04 ? 321 ASP B CA  1 
ATOM   6125  C  C   . ASP B 1 346 ? 91.249  103.126 170.044 1.00 134.77 ? 321 ASP B C   1 
ATOM   6126  O  O   . ASP B 1 346 ? 91.378  102.001 169.550 1.00 134.74 ? 321 ASP B O   1 
ATOM   6127  C  CB  . ASP B 1 346 ? 89.507  102.786 171.812 1.00 133.12 ? 321 ASP B CB  1 
ATOM   6128  C  CG  . ASP B 1 346 ? 90.105  103.350 173.082 1.00 133.76 ? 321 ASP B CG  1 
ATOM   6129  O  OD1 . ASP B 1 346 ? 90.978  104.237 172.984 1.00 133.04 ? 321 ASP B OD1 1 
ATOM   6130  O  OD2 . ASP B 1 346 ? 89.706  102.904 174.179 1.00 133.17 ? 321 ASP B OD2 1 
ATOM   6131  N  N   . SER B 1 347 ? 92.252  104.001 170.143 1.00 125.94 ? 322 SER B N   1 
ATOM   6132  C  CA  . SER B 1 347 ? 93.571  103.674 169.610 1.00 125.08 ? 322 SER B CA  1 
ATOM   6133  C  C   . SER B 1 347 ? 94.194  102.498 170.352 1.00 123.54 ? 322 SER B C   1 
ATOM   6134  O  O   . SER B 1 347 ? 94.811  101.623 169.734 1.00 121.52 ? 322 SER B O   1 
ATOM   6135  C  CB  . SER B 1 347 ? 94.479  104.900 169.682 1.00 124.54 ? 322 SER B CB  1 
ATOM   6136  O  OG  . SER B 1 347 ? 93.823  106.047 169.171 1.00 123.04 ? 322 SER B OG  1 
ATOM   6137  N  N   . THR B 1 348 ? 94.045  102.463 171.679 1.00 122.84 ? 323 THR B N   1 
ATOM   6138  C  CA  . THR B 1 348 ? 94.627  101.377 172.461 1.00 123.66 ? 323 THR B CA  1 
ATOM   6139  C  C   . THR B 1 348 ? 94.012  100.034 172.088 1.00 125.64 ? 323 THR B C   1 
ATOM   6140  O  O   . THR B 1 348 ? 94.727  99.036  171.935 1.00 124.44 ? 323 THR B O   1 
ATOM   6141  C  CB  . THR B 1 348 ? 94.446  101.652 173.953 1.00 123.65 ? 323 THR B CB  1 
ATOM   6142  O  OG1 . THR B 1 348 ? 94.589  103.055 174.200 1.00 123.67 ? 323 THR B OG1 1 
ATOM   6143  C  CG2 . THR B 1 348 ? 95.487  100.896 174.760 1.00 123.29 ? 323 THR B CG2 1 
ATOM   6144  N  N   . GLU B 1 349 ? 92.687  99.991  171.929 1.00 130.48 ? 324 GLU B N   1 
ATOM   6145  C  CA  . GLU B 1 349 ? 92.033  98.754  171.519 1.00 129.52 ? 324 GLU B CA  1 
ATOM   6146  C  C   . GLU B 1 349 ? 92.463  98.342  170.117 1.00 129.40 ? 324 GLU B C   1 
ATOM   6147  O  O   . GLU B 1 349 ? 92.664  97.153  169.846 1.00 129.82 ? 324 GLU B O   1 
ATOM   6148  C  CB  . GLU B 1 349 ? 90.515  98.912  171.591 1.00 128.68 ? 324 GLU B CB  1 
ATOM   6149  C  CG  . GLU B 1 349 ? 89.994  99.278  172.974 1.00 129.54 ? 324 GLU B CG  1 
ATOM   6150  C  CD  . GLU B 1 349 ? 90.242  98.190  174.004 1.00 131.55 ? 324 GLU B CD  1 
ATOM   6151  O  OE1 . GLU B 1 349 ? 90.337  97.006  173.616 1.00 130.41 ? 324 GLU B OE1 1 
ATOM   6152  O  OE2 . GLU B 1 349 ? 90.341  98.520  175.204 1.00 131.57 ? 324 GLU B OE2 1 
ATOM   6153  N  N   . ALA B 1 350 ? 92.609  99.313  169.213 1.00 119.67 ? 325 ALA B N   1 
ATOM   6154  C  CA  . ALA B 1 350 ? 93.055  98.997  167.860 1.00 119.31 ? 325 ALA B CA  1 
ATOM   6155  C  C   . ALA B 1 350 ? 94.456  98.401  167.866 1.00 120.64 ? 325 ALA B C   1 
ATOM   6156  O  O   . ALA B 1 350 ? 94.723  97.415  167.169 1.00 119.00 ? 325 ALA B O   1 
ATOM   6157  C  CB  . ALA B 1 350 ? 93.008  100.251 166.989 1.00 119.13 ? 325 ALA B CB  1 
ATOM   6158  N  N   . VAL B 1 351 ? 95.363  98.978  168.656 1.00 116.14 ? 326 VAL B N   1 
ATOM   6159  C  CA  . VAL B 1 351 ? 96.725  98.455  168.724 1.00 112.36 ? 326 VAL B CA  1 
ATOM   6160  C  C   . VAL B 1 351 ? 96.736  97.071  169.363 1.00 113.93 ? 326 VAL B C   1 
ATOM   6161  O  O   . VAL B 1 351 ? 97.489  96.183  168.942 1.00 112.89 ? 326 VAL B O   1 
ATOM   6162  C  CB  . VAL B 1 351 ? 97.637  99.441  169.476 1.00 110.11 ? 326 VAL B CB  1 
ATOM   6163  C  CG1 . VAL B 1 351 ? 98.987  98.809  169.765 1.00 110.84 ? 326 VAL B CG1 1 
ATOM   6164  C  CG2 . VAL B 1 351 ? 97.811  100.711 168.669 1.00 111.03 ? 326 VAL B CG2 1 
ATOM   6165  N  N   . GLU B 1 352 ? 95.906  96.862  170.389 1.00 118.74 ? 327 GLU B N   1 
ATOM   6166  C  CA  . GLU B 1 352 ? 95.843  95.549  171.021 1.00 118.16 ? 327 GLU B CA  1 
ATOM   6167  C  C   . GLU B 1 352 ? 95.303  94.499  170.060 1.00 117.26 ? 327 GLU B C   1 
ATOM   6168  O  O   . GLU B 1 352 ? 95.731  93.339  170.093 1.00 115.25 ? 327 GLU B O   1 
ATOM   6169  C  CB  . GLU B 1 352 ? 94.991  95.614  172.287 1.00 117.90 ? 327 GLU B CB  1 
ATOM   6170  C  CG  . GLU B 1 352 ? 95.770  95.975  173.547 1.00 119.27 ? 327 GLU B CG  1 
ATOM   6171  C  CD  . GLU B 1 352 ? 96.959  95.063  173.798 1.00 119.23 ? 327 GLU B CD  1 
ATOM   6172  O  OE1 . GLU B 1 352 ? 96.904  93.876  173.414 1.00 119.62 ? 327 GLU B OE1 1 
ATOM   6173  O  OE2 . GLU B 1 352 ? 97.954  95.537  174.384 1.00 117.78 ? 327 GLU B OE2 1 
ATOM   6174  N  N   . CYS B 1 353 ? 94.350  94.878  169.206 1.00 119.33 ? 328 CYS B N   1 
ATOM   6175  C  CA  . CYS B 1 353 ? 93.893  93.956  168.171 1.00 118.25 ? 328 CYS B CA  1 
ATOM   6176  C  C   . CYS B 1 353 ? 94.991  93.688  167.151 1.00 118.83 ? 328 CYS B C   1 
ATOM   6177  O  O   . CYS B 1 353 ? 95.160  92.551  166.696 1.00 119.83 ? 328 CYS B O   1 
ATOM   6178  C  CB  . CYS B 1 353 ? 92.652  94.503  167.472 1.00 119.99 ? 328 CYS B CB  1 
ATOM   6179  S  SG  . CYS B 1 353 ? 92.203  93.544  166.003 1.00 133.58 ? 328 CYS B SG  1 
ATOM   6180  N  N   . LEU B 1 354 ? 95.741  94.725  166.774 1.00 104.91 ? 329 LEU B N   1 
ATOM   6181  C  CA  . LEU B 1 354 ? 96.805  94.552  165.791 1.00 104.35 ? 329 LEU B CA  1 
ATOM   6182  C  C   . LEU B 1 354 ? 97.880  93.604  166.303 1.00 103.89 ? 329 LEU B C   1 
ATOM   6183  O  O   . LEU B 1 354 ? 98.423  92.798  165.540 1.00 102.03 ? 329 LEU B O   1 
ATOM   6184  C  CB  . LEU B 1 354 ? 97.413  95.907  165.432 1.00 103.25 ? 329 LEU B CB  1 
ATOM   6185  C  CG  . LEU B 1 354 ? 96.654  96.726  164.392 1.00 103.92 ? 329 LEU B CG  1 
ATOM   6186  C  CD1 . LEU B 1 354 ? 96.965  98.198  164.557 1.00 102.74 ? 329 LEU B CD1 1 
ATOM   6187  C  CD2 . LEU B 1 354 ? 97.000  96.258  162.992 1.00 102.45 ? 329 LEU B CD2 1 
ATOM   6188  N  N   . ARG B 1 355 ? 98.202  93.689  167.596 1.00 93.60  ? 330 ARG B N   1 
ATOM   6189  C  CA  . ARG B 1 355 ? 99.230  92.818  168.158 1.00 92.25  ? 330 ARG B CA  1 
ATOM   6190  C  C   . ARG B 1 355 ? 98.840  91.348  168.063 1.00 94.10  ? 330 ARG B C   1 
ATOM   6191  O  O   . ARG B 1 355 ? 99.715  90.475  168.052 1.00 93.04  ? 330 ARG B O   1 
ATOM   6192  C  CB  . ARG B 1 355 ? 99.509  93.196  169.612 1.00 91.58  ? 330 ARG B CB  1 
ATOM   6193  C  CG  . ARG B 1 355 ? 100.132 94.565  169.781 1.00 92.73  ? 330 ARG B CG  1 
ATOM   6194  C  CD  . ARG B 1 355 ? 100.873 94.680  171.099 1.00 91.65  ? 330 ARG B CD  1 
ATOM   6195  N  NE  . ARG B 1 355 ? 100.873 96.051  171.592 1.00 90.92  ? 330 ARG B NE  1 
ATOM   6196  C  CZ  . ARG B 1 355 ? 101.590 96.477  172.621 1.00 91.32  ? 330 ARG B CZ  1 
ATOM   6197  N  NH1 . ARG B 1 355 ? 102.389 95.664  173.290 1.00 93.10  ? 330 ARG B NH1 1 
ATOM   6198  N  NH2 . ARG B 1 355 ? 101.503 97.752  172.987 1.00 90.41  ? 330 ARG B NH2 1 
ATOM   6199  N  N   . ARG B 1 356 ? 97.541  91.052  167.996 1.00 108.53 ? 331 ARG B N   1 
ATOM   6200  C  CA  . ARG B 1 356 ? 97.094  89.671  167.863 1.00 107.68 ? 331 ARG B CA  1 
ATOM   6201  C  C   . ARG B 1 356 ? 97.308  89.121  166.459 1.00 108.00 ? 331 ARG B C   1 
ATOM   6202  O  O   . ARG B 1 356 ? 97.426  87.902  166.298 1.00 107.97 ? 331 ARG B O   1 
ATOM   6203  C  CB  . ARG B 1 356 ? 95.618  89.556  168.241 1.00 107.79 ? 331 ARG B CB  1 
ATOM   6204  C  CG  . ARG B 1 356 ? 95.348  89.653  169.730 1.00 108.87 ? 331 ARG B CG  1 
ATOM   6205  C  CD  . ARG B 1 356 ? 93.855  89.653  170.017 1.00 109.61 ? 331 ARG B CD  1 
ATOM   6206  N  NE  . ARG B 1 356 ? 93.523  90.470  171.178 1.00 110.87 ? 331 ARG B NE  1 
ATOM   6207  C  CZ  . ARG B 1 356 ? 92.318  90.964  171.426 1.00 110.25 ? 331 ARG B CZ  1 
ATOM   6208  N  NH1 . ARG B 1 356 ? 91.300  90.743  170.611 1.00 109.83 ? 331 ARG B NH1 1 
ATOM   6209  N  NH2 . ARG B 1 356 ? 92.130  91.700  172.517 1.00 109.44 ? 331 ARG B NH2 1 
ATOM   6210  N  N   . LYS B 1 357 ? 97.355  89.982  165.446 1.00 103.84 ? 332 LYS B N   1 
ATOM   6211  C  CA  . LYS B 1 357 ? 97.501  89.522  164.075 1.00 100.46 ? 332 LYS B CA  1 
ATOM   6212  C  C   . LYS B 1 357 ? 98.905  88.975  163.836 1.00 102.97 ? 332 LYS B C   1 
ATOM   6213  O  O   . LYS B 1 357 ? 99.864  89.314  164.534 1.00 106.71 ? 332 LYS B O   1 
ATOM   6214  C  CB  . LYS B 1 357 ? 97.216  90.657  163.094 1.00 99.00  ? 332 LYS B CB  1 
ATOM   6215  C  CG  . LYS B 1 357 ? 95.805  90.664  162.547 1.00 100.19 ? 332 LYS B CG  1 
ATOM   6216  C  CD  . LYS B 1 357 ? 94.804  91.009  163.631 1.00 103.11 ? 332 LYS B CD  1 
ATOM   6217  C  CE  . LYS B 1 357 ? 93.419  91.231  163.054 1.00 102.59 ? 332 LYS B CE  1 
ATOM   6218  N  NZ  . LYS B 1 357 ? 92.437  91.577  164.115 1.00 104.32 ? 332 LYS B NZ  1 
ATOM   6219  N  N   . SER B 1 358 ? 99.014  88.110  162.833 1.00 93.04  ? 333 SER B N   1 
ATOM   6220  C  CA  . SER B 1 358 ? 100.306 87.560  162.462 1.00 93.98  ? 333 SER B CA  1 
ATOM   6221  C  C   . SER B 1 358 ? 101.161 88.623  161.780 1.00 94.78  ? 333 SER B C   1 
ATOM   6222  O  O   . SER B 1 358 ? 100.659 89.605  161.228 1.00 94.76  ? 333 SER B O   1 
ATOM   6223  C  CB  . SER B 1 358 ? 100.132 86.356  161.541 1.00 94.88  ? 333 SER B CB  1 
ATOM   6224  O  OG  . SER B 1 358 ? 99.166  86.622  160.540 1.00 96.02  ? 333 SER B OG  1 
ATOM   6225  N  N   . SER B 1 359 ? 102.478 88.416  161.828 1.00 95.51  ? 334 SER B N   1 
ATOM   6226  C  CA  . SER B 1 359 ? 103.401 89.357  161.205 1.00 92.90  ? 334 SER B CA  1 
ATOM   6227  C  C   . SER B 1 359 ? 103.290 89.362  159.688 1.00 92.70  ? 334 SER B C   1 
ATOM   6228  O  O   . SER B 1 359 ? 103.713 90.332  159.054 1.00 94.78  ? 334 SER B O   1 
ATOM   6229  C  CB  . SER B 1 359 ? 104.838 89.034  161.610 1.00 95.81  ? 334 SER B CB  1 
ATOM   6230  O  OG  . SER B 1 359 ? 105.274 87.823  161.019 1.00 96.31  ? 334 SER B OG  1 
ATOM   6231  N  N   . ARG B 1 360 ? 102.741 88.306  159.095 1.00 92.51  ? 335 ARG B N   1 
ATOM   6232  C  CA  . ARG B 1 360 ? 102.617 88.228  157.648 1.00 92.56  ? 335 ARG B CA  1 
ATOM   6233  C  C   . ARG B 1 360 ? 101.317 88.823  157.129 1.00 91.41  ? 335 ARG B C   1 
ATOM   6234  O  O   . ARG B 1 360 ? 101.259 89.227  155.962 1.00 90.99  ? 335 ARG B O   1 
ATOM   6235  C  CB  . ARG B 1 360 ? 102.730 86.771  157.190 1.00 91.89  ? 335 ARG B CB  1 
ATOM   6236  C  CG  . ARG B 1 360 ? 102.923 86.600  155.695 1.00 90.28  ? 335 ARG B CG  1 
ATOM   6237  C  CD  . ARG B 1 360 ? 104.334 86.152  155.370 1.00 93.31  ? 335 ARG B CD  1 
ATOM   6238  N  NE  . ARG B 1 360 ? 105.268 87.270  155.334 1.00 95.77  ? 335 ARG B NE  1 
ATOM   6239  C  CZ  . ARG B 1 360 ? 105.430 88.076  154.294 1.00 93.49  ? 335 ARG B CZ  1 
ATOM   6240  N  NH1 . ARG B 1 360 ? 104.721 87.928  153.187 1.00 93.88  ? 335 ARG B NH1 1 
ATOM   6241  N  NH2 . ARG B 1 360 ? 106.325 89.056  154.366 1.00 89.74  ? 335 ARG B NH2 1 
ATOM   6242  N  N   . GLU B 1 361 ? 100.276 88.887  157.958 1.00 94.31  ? 336 GLU B N   1 
ATOM   6243  C  CA  . GLU B 1 361 ? 98.999  89.410  157.488 1.00 95.83  ? 336 GLU B CA  1 
ATOM   6244  C  C   . GLU B 1 361 ? 99.075  90.908  157.224 1.00 96.81  ? 336 GLU B C   1 
ATOM   6245  O  O   . GLU B 1 361 ? 98.672  91.379  156.155 1.00 97.67  ? 336 GLU B O   1 
ATOM   6246  C  CB  . GLU B 1 361 ? 97.898  89.097  158.500 1.00 97.36  ? 336 GLU B CB  1 
ATOM   6247  C  CG  . GLU B 1 361 ? 96.500  89.407  157.995 1.00 98.96  ? 336 GLU B CG  1 
ATOM   6248  C  CD  . GLU B 1 361 ? 95.427  89.057  159.003 1.00 101.55 ? 336 GLU B CD  1 
ATOM   6249  O  OE1 . GLU B 1 361 ? 95.777  88.563  160.094 1.00 102.33 ? 336 GLU B OE1 1 
ATOM   6250  O  OE2 . GLU B 1 361 ? 94.235  89.275  158.704 1.00 100.35 ? 336 GLU B OE2 1 
ATOM   6251  N  N   . LEU B 1 362 ? 99.600  91.676  158.182 1.00 90.05  ? 337 LEU B N   1 
ATOM   6252  C  CA  . LEU B 1 362 ? 99.609  93.128  158.046 1.00 89.09  ? 337 LEU B CA  1 
ATOM   6253  C  C   . LEU B 1 362 ? 100.722 93.637  157.141 1.00 86.15  ? 337 LEU B C   1 
ATOM   6254  O  O   . LEU B 1 362 ? 100.645 94.777  156.672 1.00 85.10  ? 337 LEU B O   1 
ATOM   6255  C  CB  . LEU B 1 362 ? 99.712  93.790  159.422 1.00 84.01  ? 337 LEU B CB  1 
ATOM   6256  C  CG  . LEU B 1 362 ? 100.685 93.229  160.456 1.00 82.39  ? 337 LEU B CG  1 
ATOM   6257  C  CD1 . LEU B 1 362 ? 102.092 93.732  160.206 1.00 82.32  ? 337 LEU B CD1 1 
ATOM   6258  C  CD2 . LEU B 1 362 ? 100.227 93.610  161.849 1.00 84.02  ? 337 LEU B CD2 1 
ATOM   6259  N  N   . VAL B 1 363 ? 101.753 92.832  156.892 1.00 85.47  ? 338 VAL B N   1 
ATOM   6260  C  CA  . VAL B 1 363 ? 102.794 93.236  155.955 1.00 83.72  ? 338 VAL B CA  1 
ATOM   6261  C  C   . VAL B 1 363 ? 102.269 93.218  154.525 1.00 88.95  ? 338 VAL B C   1 
ATOM   6262  O  O   . VAL B 1 363 ? 102.543 94.130  153.737 1.00 90.68  ? 338 VAL B O   1 
ATOM   6263  C  CB  . VAL B 1 363 ? 104.030 92.337  156.120 1.00 83.80  ? 338 VAL B CB  1 
ATOM   6264  C  CG1 . VAL B 1 363 ? 104.846 92.313  154.844 1.00 85.86  ? 338 VAL B CG1 1 
ATOM   6265  C  CG2 . VAL B 1 363 ? 104.871 92.821  157.276 1.00 85.25  ? 338 VAL B CG2 1 
ATOM   6266  N  N   . ASP B 1 364 ? 101.500 92.187  154.168 1.00 100.88 ? 339 ASP B N   1 
ATOM   6267  C  CA  . ASP B 1 364 ? 101.080 92.009  152.782 1.00 99.63  ? 339 ASP B CA  1 
ATOM   6268  C  C   . ASP B 1 364 ? 100.072 93.056  152.325 1.00 100.34 ? 339 ASP B C   1 
ATOM   6269  O  O   . ASP B 1 364 ? 100.027 93.366  151.130 1.00 102.30 ? 339 ASP B O   1 
ATOM   6270  C  CB  . ASP B 1 364 ? 100.507 90.603  152.587 1.00 100.29 ? 339 ASP B CB  1 
ATOM   6271  C  CG  . ASP B 1 364 ? 101.515 89.510  152.910 1.00 101.66 ? 339 ASP B CG  1 
ATOM   6272  O  OD1 . ASP B 1 364 ? 102.597 89.830  153.446 1.00 100.03 ? 339 ASP B OD1 1 
ATOM   6273  O  OD2 . ASP B 1 364 ? 101.225 88.328  152.630 1.00 103.15 ? 339 ASP B OD2 1 
ATOM   6274  N  N   . GLN B 1 365 ? 99.266  93.605  153.232 1.00 95.73  ? 340 GLN B N   1 
ATOM   6275  C  CA  . GLN B 1 365 ? 98.318  94.639  152.843 1.00 94.12  ? 340 GLN B CA  1 
ATOM   6276  C  C   . GLN B 1 365 ? 99.060  95.876  152.358 1.00 96.67  ? 340 GLN B C   1 
ATOM   6277  O  O   . GLN B 1 365 ? 100.119 96.232  152.880 1.00 99.74  ? 340 GLN B O   1 
ATOM   6278  C  CB  . GLN B 1 365 ? 97.401  95.003  154.011 1.00 91.12  ? 340 GLN B CB  1 
ATOM   6279  C  CG  . GLN B 1 365 ? 96.122  94.185  154.080 1.00 95.08  ? 340 GLN B CG  1 
ATOM   6280  C  CD  . GLN B 1 365 ? 96.290  92.895  154.855 1.00 99.65  ? 340 GLN B CD  1 
ATOM   6281  O  OE1 . GLN B 1 365 ? 96.415  92.905  156.078 1.00 97.87  ? 340 GLN B OE1 1 
ATOM   6282  N  NE2 . GLN B 1 365 ? 96.293  91.773  154.145 1.00 99.56  ? 340 GLN B NE2 1 
ATOM   6283  N  N   . ASP B 1 366 ? 98.502  96.532  151.350 1.00 92.64  ? 341 ASP B N   1 
ATOM   6284  C  CA  . ASP B 1 366 ? 99.105  97.736  150.807 1.00 93.81  ? 341 ASP B CA  1 
ATOM   6285  C  C   . ASP B 1 366 ? 98.426  98.978  151.372 1.00 93.82  ? 341 ASP B C   1 
ATOM   6286  O  O   . ASP B 1 366 ? 97.225  98.973  151.657 1.00 95.35  ? 341 ASP B O   1 
ATOM   6287  C  CB  . ASP B 1 366 ? 99.107  97.684  149.268 1.00 96.16  ? 341 ASP B CB  1 
ATOM   6288  C  CG  . ASP B 1 366 ? 97.848  98.260  148.599 1.00 99.99  ? 341 ASP B CG  1 
ATOM   6289  O  OD1 . ASP B 1 366 ? 96.869  98.701  149.222 1.00 97.51  ? 341 ASP B OD1 1 
ATOM   6290  O  OD2 . ASP B 1 366 ? 97.825  98.215  147.355 1.00 101.32 ? 341 ASP B OD2 1 
ATOM   6291  N  N   . VAL B 1 367 ? 99.228  100.009 151.620 1.00 82.62  ? 342 VAL B N   1 
ATOM   6292  C  CA  . VAL B 1 367 ? 98.738  101.297 152.092 1.00 79.10  ? 342 VAL B CA  1 
ATOM   6293  C  C   . VAL B 1 367 ? 99.442  102.367 151.276 1.00 80.08  ? 342 VAL B C   1 
ATOM   6294  O  O   . VAL B 1 367 ? 100.579 102.742 151.579 1.00 83.05  ? 342 VAL B O   1 
ATOM   6295  C  CB  . VAL B 1 367 ? 98.990  101.488 153.598 1.00 79.93  ? 342 VAL B CB  1 
ATOM   6296  C  CG1 . VAL B 1 367 ? 98.572  102.879 154.032 1.00 81.84  ? 342 VAL B CG1 1 
ATOM   6297  C  CG2 . VAL B 1 367 ? 98.256  100.433 154.402 1.00 76.35  ? 342 VAL B CG2 1 
ATOM   6298  N  N   . GLN B 1 368 ? 98.787  102.853 150.231 1.00 79.10  ? 343 GLN B N   1 
ATOM   6299  C  CA  . GLN B 1 368 ? 99.437  103.751 149.289 1.00 81.69  ? 343 GLN B CA  1 
ATOM   6300  C  C   . GLN B 1 368 ? 99.448  105.169 149.838 1.00 82.80  ? 343 GLN B C   1 
ATOM   6301  O  O   . GLN B 1 368 ? 98.375  105.727 150.099 1.00 85.10  ? 343 GLN B O   1 
ATOM   6302  C  CB  . GLN B 1 368 ? 98.732  103.717 147.948 1.00 78.07  ? 343 GLN B CB  1 
ATOM   6303  C  CG  . GLN B 1 368 ? 99.682  103.609 146.780 1.00 78.58  ? 343 GLN B CG  1 
ATOM   6304  C  CD  . GLN B 1 368 ? 100.621 102.430 146.915 1.00 81.63  ? 343 GLN B CD  1 
ATOM   6305  O  OE1 . GLN B 1 368 ? 100.233 101.365 147.395 1.00 78.98  ? 343 GLN B OE1 1 
ATOM   6306  N  NE2 . GLN B 1 368 ? 101.868 102.616 146.496 1.00 81.06  ? 343 GLN B NE2 1 
ATOM   6307  N  N   . PRO B 1 369 ? 100.611 105.780 150.033 1.00 68.05  ? 344 PRO B N   1 
ATOM   6308  C  CA  . PRO B 1 369 ? 100.657 107.182 150.448 1.00 63.41  ? 344 PRO B CA  1 
ATOM   6309  C  C   . PRO B 1 369 ? 100.582 108.107 149.241 1.00 66.95  ? 344 PRO B C   1 
ATOM   6310  O  O   . PRO B 1 369 ? 100.655 107.681 148.089 1.00 67.45  ? 344 PRO B O   1 
ATOM   6311  C  CB  . PRO B 1 369 ? 102.016 107.284 151.139 1.00 62.81  ? 344 PRO B CB  1 
ATOM   6312  C  CG  . PRO B 1 369 ? 102.864 106.320 150.382 1.00 60.68  ? 344 PRO B CG  1 
ATOM   6313  C  CD  . PRO B 1 369 ? 101.958 105.191 149.947 1.00 66.13  ? 344 PRO B CD  1 
ATOM   6314  N  N   . ALA B 1 370 ? 100.439 109.398 149.527 1.00 59.59  ? 345 ALA B N   1 
ATOM   6315  C  CA  . ALA B 1 370 ? 100.481 110.386 148.462 1.00 59.56  ? 345 ALA B CA  1 
ATOM   6316  C  C   . ALA B 1 370 ? 101.845 110.354 147.781 1.00 63.93  ? 345 ALA B C   1 
ATOM   6317  O  O   . ALA B 1 370 ? 102.844 109.920 148.357 1.00 71.34  ? 345 ALA B O   1 
ATOM   6318  C  CB  . ALA B 1 370 ? 100.195 111.783 149.010 1.00 63.52  ? 345 ALA B CB  1 
ATOM   6319  N  N   . ARG B 1 371 ? 101.877 110.803 146.530 1.00 59.38  ? 346 ARG B N   1 
ATOM   6320  C  CA  . ARG B 1 371 ? 103.116 110.759 145.767 1.00 56.97  ? 346 ARG B CA  1 
ATOM   6321  C  C   . ARG B 1 371 ? 104.190 111.598 146.446 1.00 62.22  ? 346 ARG B C   1 
ATOM   6322  O  O   . ARG B 1 371 ? 103.907 112.653 147.018 1.00 65.50  ? 346 ARG B O   1 
ATOM   6323  C  CB  . ARG B 1 371 ? 102.879 111.253 144.344 1.00 58.51  ? 346 ARG B CB  1 
ATOM   6324  C  CG  . ARG B 1 371 ? 101.782 110.507 143.615 1.00 64.10  ? 346 ARG B CG  1 
ATOM   6325  C  CD  . ARG B 1 371 ? 102.085 110.394 142.136 1.00 63.92  ? 346 ARG B CD  1 
ATOM   6326  N  NE  . ARG B 1 371 ? 103.353 109.719 141.899 1.00 67.92  ? 346 ARG B NE  1 
ATOM   6327  C  CZ  . ARG B 1 371 ? 103.933 109.618 140.712 1.00 72.13  ? 346 ARG B CZ  1 
ATOM   6328  N  NH1 . ARG B 1 371 ? 103.382 110.138 139.627 1.00 68.22  ? 346 ARG B NH1 1 
ATOM   6329  N  NH2 . ARG B 1 371 ? 105.095 108.979 140.610 1.00 68.94  ? 346 ARG B NH2 1 
ATOM   6330  N  N   . TYR B 1 372 ? 105.429 111.107 146.394 1.00 58.67  ? 347 TYR B N   1 
ATOM   6331  C  CA  . TYR B 1 372 ? 106.577 111.758 147.023 1.00 50.55  ? 347 TYR B CA  1 
ATOM   6332  C  C   . TYR B 1 372 ? 106.378 111.931 148.526 1.00 58.22  ? 347 TYR B C   1 
ATOM   6333  O  O   . TYR B 1 372 ? 106.811 112.926 149.108 1.00 61.70  ? 347 TYR B O   1 
ATOM   6334  C  CB  . TYR B 1 372 ? 106.884 113.105 146.365 1.00 41.74  ? 347 TYR B CB  1 
ATOM   6335  C  CG  . TYR B 1 372 ? 106.834 113.065 144.859 1.00 48.27  ? 347 TYR B CG  1 
ATOM   6336  C  CD1 . TYR B 1 372 ? 107.434 112.037 144.154 1.00 55.20  ? 347 TYR B CD1 1 
ATOM   6337  C  CD2 . TYR B 1 372 ? 106.184 114.054 144.143 1.00 51.39  ? 347 TYR B CD2 1 
ATOM   6338  C  CE1 . TYR B 1 372 ? 107.389 111.995 142.777 1.00 55.35  ? 347 TYR B CE1 1 
ATOM   6339  C  CE2 . TYR B 1 372 ? 106.133 114.019 142.767 1.00 56.38  ? 347 TYR B CE2 1 
ATOM   6340  C  CZ  . TYR B 1 372 ? 106.737 112.988 142.089 1.00 54.57  ? 347 TYR B CZ  1 
ATOM   6341  O  OH  . TYR B 1 372 ? 106.689 112.948 140.717 1.00 53.57  ? 347 TYR B OH  1 
ATOM   6342  N  N   . HIS B 1 373 ? 105.714 110.967 149.161 1.00 49.30  ? 348 HIS B N   1 
ATOM   6343  C  CA  . HIS B 1 373 ? 105.563 110.924 150.608 1.00 39.12  ? 348 HIS B CA  1 
ATOM   6344  C  C   . HIS B 1 373 ? 105.669 109.472 151.050 1.00 47.69  ? 348 HIS B C   1 
ATOM   6345  O  O   . HIS B 1 373 ? 105.841 108.567 150.230 1.00 51.48  ? 348 HIS B O   1 
ATOM   6346  C  CB  . HIS B 1 373 ? 104.237 111.546 151.056 1.00 35.88  ? 348 HIS B CB  1 
ATOM   6347  C  CG  . HIS B 1 373 ? 104.219 113.042 151.006 1.00 47.58  ? 348 HIS B CG  1 
ATOM   6348  N  ND1 . HIS B 1 373 ? 104.214 113.748 149.823 1.00 54.44  ? 348 HIS B ND1 1 
ATOM   6349  C  CD2 . HIS B 1 373 ? 104.198 113.966 151.995 1.00 52.33  ? 348 HIS B CD2 1 
ATOM   6350  C  CE1 . HIS B 1 373 ? 104.194 115.042 150.084 1.00 51.83  ? 348 HIS B CE1 1 
ATOM   6351  N  NE2 . HIS B 1 373 ? 104.184 115.202 151.395 1.00 58.17  ? 348 HIS B NE2 1 
ATOM   6352  N  N   . ILE B 1 374 ? 105.569 109.241 152.356 1.00 52.30  ? 349 ILE B N   1 
ATOM   6353  C  CA  . ILE B 1 374 ? 105.634 107.892 152.902 1.00 53.36  ? 349 ILE B CA  1 
ATOM   6354  C  C   . ILE B 1 374 ? 104.445 107.663 153.822 1.00 57.28  ? 349 ILE B C   1 
ATOM   6355  O  O   . ILE B 1 374 ? 103.874 108.604 154.382 1.00 57.45  ? 349 ILE B O   1 
ATOM   6356  C  CB  . ILE B 1 374 ? 106.950 107.625 153.661 1.00 48.12  ? 349 ILE B CB  1 
ATOM   6357  C  CG1 . ILE B 1 374 ? 107.115 108.617 154.808 1.00 46.70  ? 349 ILE B CG1 1 
ATOM   6358  C  CG2 . ILE B 1 374 ? 108.130 107.683 152.717 1.00 51.64  ? 349 ILE B CG2 1 
ATOM   6359  C  CD1 . ILE B 1 374 ? 108.162 108.208 155.798 1.00 51.26  ? 349 ILE B CD1 1 
ATOM   6360  N  N   . ALA B 1 375 ? 104.078 106.393 153.978 1.00 64.13  ? 350 ALA B N   1 
ATOM   6361  C  CA  . ALA B 1 375 ? 102.976 106.012 154.853 1.00 62.56  ? 350 ALA B CA  1 
ATOM   6362  C  C   . ALA B 1 375 ? 103.475 105.684 156.256 1.00 63.46  ? 350 ALA B C   1 
ATOM   6363  O  O   . ALA B 1 375 ? 103.073 106.326 157.231 1.00 67.68  ? 350 ALA B O   1 
ATOM   6364  C  CB  . ALA B 1 375 ? 102.219 104.821 154.259 1.00 64.79  ? 350 ALA B CB  1 
ATOM   6365  N  N   . PHE B 1 376 ? 104.355 104.695 156.370 1.00 61.53  ? 351 PHE B N   1 
ATOM   6366  C  CA  . PHE B 1 376 ? 104.920 104.289 157.649 1.00 61.38  ? 351 PHE B CA  1 
ATOM   6367  C  C   . PHE B 1 376 ? 106.394 104.665 157.678 1.00 58.91  ? 351 PHE B C   1 
ATOM   6368  O  O   . PHE B 1 376 ? 107.174 104.203 156.841 1.00 67.66  ? 351 PHE B O   1 
ATOM   6369  C  CB  . PHE B 1 376 ? 104.741 102.788 157.872 1.00 61.65  ? 351 PHE B CB  1 
ATOM   6370  C  CG  . PHE B 1 376 ? 103.309 102.354 157.937 1.00 60.97  ? 351 PHE B CG  1 
ATOM   6371  C  CD1 . PHE B 1 376 ? 102.436 102.940 158.829 1.00 63.15  ? 351 PHE B CD1 1 
ATOM   6372  C  CD2 . PHE B 1 376 ? 102.838 101.362 157.102 1.00 62.86  ? 351 PHE B CD2 1 
ATOM   6373  C  CE1 . PHE B 1 376 ? 101.122 102.542 158.889 1.00 64.89  ? 351 PHE B CE1 1 
ATOM   6374  C  CE2 . PHE B 1 376 ? 101.525 100.963 157.159 1.00 66.80  ? 351 PHE B CE2 1 
ATOM   6375  C  CZ  . PHE B 1 376 ? 100.667 101.554 158.054 1.00 66.44  ? 351 PHE B CZ  1 
ATOM   6376  N  N   . GLY B 1 377 ? 106.770 105.492 158.643 1.00 44.84  ? 352 GLY B N   1 
ATOM   6377  C  CA  . GLY B 1 377 ? 108.125 105.967 158.762 1.00 45.56  ? 352 GLY B CA  1 
ATOM   6378  C  C   . GLY B 1 377 ? 108.311 106.707 160.066 1.00 55.36  ? 352 GLY B C   1 
ATOM   6379  O  O   . GLY B 1 377 ? 107.459 106.651 160.955 1.00 66.78  ? 352 GLY B O   1 
ATOM   6380  N  N   . PRO B 1 378 ? 109.429 107.410 160.214 1.00 41.67  ? 353 PRO B N   1 
ATOM   6381  C  CA  . PRO B 1 378 ? 109.674 108.136 161.461 1.00 35.82  ? 353 PRO B CA  1 
ATOM   6382  C  C   . PRO B 1 378 ? 108.594 109.175 161.710 1.00 42.06  ? 353 PRO B C   1 
ATOM   6383  O  O   . PRO B 1 378 ? 108.120 109.838 160.787 1.00 49.59  ? 353 PRO B O   1 
ATOM   6384  C  CB  . PRO B 1 378 ? 111.041 108.783 161.229 1.00 38.48  ? 353 PRO B CB  1 
ATOM   6385  C  CG  . PRO B 1 378 ? 111.666 107.963 160.167 1.00 43.40  ? 353 PRO B CG  1 
ATOM   6386  C  CD  . PRO B 1 378 ? 110.547 107.551 159.275 1.00 46.41  ? 353 PRO B CD  1 
ATOM   6387  N  N   . VAL B 1 379 ? 108.202 109.308 162.972 1.00 57.60  ? 354 VAL B N   1 
ATOM   6388  C  CA  . VAL B 1 379 ? 107.129 110.206 163.377 1.00 58.18  ? 354 VAL B CA  1 
ATOM   6389  C  C   . VAL B 1 379 ? 107.652 111.118 164.473 1.00 65.60  ? 354 VAL B C   1 
ATOM   6390  O  O   . VAL B 1 379 ? 108.300 110.652 165.415 1.00 71.93  ? 354 VAL B O   1 
ATOM   6391  C  CB  . VAL B 1 379 ? 105.892 109.436 163.871 1.00 62.81  ? 354 VAL B CB  1 
ATOM   6392  C  CG1 . VAL B 1 379 ? 104.737 110.386 164.077 1.00 65.11  ? 354 VAL B CG1 1 
ATOM   6393  C  CG2 . VAL B 1 379 ? 105.513 108.348 162.889 1.00 64.75  ? 354 VAL B CG2 1 
ATOM   6394  N  N   . VAL B 1 380 ? 107.376 112.413 164.349 1.00 65.73  ? 355 VAL B N   1 
ATOM   6395  C  CA  . VAL B 1 380 ? 107.711 113.356 165.408 1.00 65.53  ? 355 VAL B CA  1 
ATOM   6396  C  C   . VAL B 1 380 ? 106.803 113.101 166.606 1.00 68.74  ? 355 VAL B C   1 
ATOM   6397  O  O   . VAL B 1 380 ? 105.574 113.192 166.509 1.00 73.00  ? 355 VAL B O   1 
ATOM   6398  C  CB  . VAL B 1 380 ? 107.605 114.800 164.904 1.00 65.65  ? 355 VAL B CB  1 
ATOM   6399  C  CG1 . VAL B 1 380 ? 106.272 115.035 164.218 1.00 67.19  ? 355 VAL B CG1 1 
ATOM   6400  C  CG2 . VAL B 1 380 ? 107.769 115.762 166.057 1.00 65.36  ? 355 VAL B CG2 1 
ATOM   6401  N  N   . ASP B 1 381 ? 107.404 112.761 167.745 1.00 74.11  ? 356 ASP B N   1 
ATOM   6402  C  CA  . ASP B 1 381 ? 106.636 112.367 168.920 1.00 74.52  ? 356 ASP B CA  1 
ATOM   6403  C  C   . ASP B 1 381 ? 107.088 113.006 170.224 1.00 78.59  ? 356 ASP B C   1 
ATOM   6404  O  O   . ASP B 1 381 ? 106.310 113.003 171.185 1.00 81.31  ? 356 ASP B O   1 
ATOM   6405  C  CB  . ASP B 1 381 ? 106.666 110.840 169.090 1.00 77.81  ? 356 ASP B CB  1 
ATOM   6406  C  CG  . ASP B 1 381 ? 108.072 110.274 169.047 1.00 84.86  ? 356 ASP B CG  1 
ATOM   6407  O  OD1 . ASP B 1 381 ? 108.965 110.825 169.722 1.00 84.70  ? 356 ASP B OD1 1 
ATOM   6408  O  OD2 . ASP B 1 381 ? 108.287 109.269 168.340 1.00 82.87  ? 356 ASP B OD2 1 
ATOM   6409  N  N   . GLY B 1 382 ? 108.301 113.542 170.302 1.00 79.34  ? 357 GLY B N   1 
ATOM   6410  C  CA  . GLY B 1 382 ? 108.836 114.079 171.530 1.00 79.42  ? 357 GLY B CA  1 
ATOM   6411  C  C   . GLY B 1 382 ? 109.728 113.122 172.293 1.00 85.73  ? 357 GLY B C   1 
ATOM   6412  O  O   . GLY B 1 382 ? 110.499 113.566 173.150 1.00 86.57  ? 357 GLY B O   1 
ATOM   6413  N  N   . ASP B 1 383 ? 109.641 111.823 172.006 1.00 86.20  ? 358 ASP B N   1 
ATOM   6414  C  CA  . ASP B 1 383 ? 110.525 110.855 172.643 1.00 83.22  ? 358 ASP B CA  1 
ATOM   6415  C  C   . ASP B 1 383 ? 111.856 110.762 171.906 1.00 81.96  ? 358 ASP B C   1 
ATOM   6416  O  O   . ASP B 1 383 ? 112.905 111.121 172.449 1.00 80.24  ? 358 ASP B O   1 
ATOM   6417  C  CB  . ASP B 1 383 ? 109.846 109.484 172.706 1.00 82.08  ? 358 ASP B CB  1 
ATOM   6418  C  CG  . ASP B 1 383 ? 110.628 108.481 173.534 1.00 87.72  ? 358 ASP B CG  1 
ATOM   6419  O  OD1 . ASP B 1 383 ? 111.538 108.899 174.280 1.00 87.82  ? 358 ASP B OD1 1 
ATOM   6420  O  OD2 . ASP B 1 383 ? 110.333 107.272 173.439 1.00 88.01  ? 358 ASP B OD2 1 
ATOM   6421  N  N   . VAL B 1 384 ? 111.828 110.297 170.661 1.00 74.13  ? 359 VAL B N   1 
ATOM   6422  C  CA  . VAL B 1 384 ? 113.049 110.175 169.872 1.00 73.21  ? 359 VAL B CA  1 
ATOM   6423  C  C   . VAL B 1 384 ? 113.315 111.440 169.073 1.00 79.92  ? 359 VAL B C   1 
ATOM   6424  O  O   . VAL B 1 384 ? 114.410 112.001 169.127 1.00 89.43  ? 359 VAL B O   1 
ATOM   6425  C  CB  . VAL B 1 384 ? 112.974 108.938 168.953 1.00 77.44  ? 359 VAL B CB  1 
ATOM   6426  C  CG1 . VAL B 1 384 ? 114.294 108.746 168.230 1.00 76.08  ? 359 VAL B CG1 1 
ATOM   6427  C  CG2 . VAL B 1 384 ? 112.623 107.703 169.755 1.00 77.51  ? 359 VAL B CG2 1 
ATOM   6428  N  N   . VAL B 1 385 ? 112.324 111.913 168.327 1.00 75.13  ? 360 VAL B N   1 
ATOM   6429  C  CA  . VAL B 1 385 ? 112.423 113.163 167.586 1.00 78.23  ? 360 VAL B CA  1 
ATOM   6430  C  C   . VAL B 1 385 ? 111.563 114.195 168.314 1.00 75.39  ? 360 VAL B C   1 
ATOM   6431  O  O   . VAL B 1 385 ? 110.328 114.110 168.270 1.00 78.75  ? 360 VAL B O   1 
ATOM   6432  C  CB  . VAL B 1 385 ? 111.983 112.993 166.127 1.00 71.34  ? 360 VAL B CB  1 
ATOM   6433  C  CG1 . VAL B 1 385 ? 112.535 114.113 165.279 1.00 69.33  ? 360 VAL B CG1 1 
ATOM   6434  C  CG2 . VAL B 1 385 ? 112.442 111.653 165.593 1.00 68.03  ? 360 VAL B CG2 1 
ATOM   6435  N  N   . PRO B 1 386 ? 112.162 115.167 169.007 1.00 67.71  ? 361 PRO B N   1 
ATOM   6436  C  CA  . PRO B 1 386 ? 111.344 116.108 169.796 1.00 71.81  ? 361 PRO B CA  1 
ATOM   6437  C  C   . PRO B 1 386 ? 110.390 116.939 168.956 1.00 72.67  ? 361 PRO B C   1 
ATOM   6438  O  O   . PRO B 1 386 ? 109.186 116.971 169.236 1.00 75.66  ? 361 PRO B O   1 
ATOM   6439  C  CB  . PRO B 1 386 ? 112.400 116.975 170.495 1.00 77.69  ? 361 PRO B CB  1 
ATOM   6440  C  CG  . PRO B 1 386 ? 113.640 116.144 170.498 1.00 72.90  ? 361 PRO B CG  1 
ATOM   6441  C  CD  . PRO B 1 386 ? 113.603 115.357 169.232 1.00 66.20  ? 361 PRO B CD  1 
ATOM   6442  N  N   . ASP B 1 387 ? 110.896 117.624 167.937 1.00 76.31  ? 362 ASP B N   1 
ATOM   6443  C  CA  . ASP B 1 387 ? 110.086 118.412 167.021 1.00 77.83  ? 362 ASP B CA  1 
ATOM   6444  C  C   . ASP B 1 387 ? 110.394 117.958 165.601 1.00 78.37  ? 362 ASP B C   1 
ATOM   6445  O  O   . ASP B 1 387 ? 111.171 117.025 165.387 1.00 80.57  ? 362 ASP B O   1 
ATOM   6446  C  CB  . ASP B 1 387 ? 110.350 119.911 167.198 1.00 78.45  ? 362 ASP B CB  1 
ATOM   6447  C  CG  . ASP B 1 387 ? 109.188 120.763 166.741 1.00 81.94  ? 362 ASP B CG  1 
ATOM   6448  O  OD1 . ASP B 1 387 ? 108.202 120.195 166.228 1.00 81.77  ? 362 ASP B OD1 1 
ATOM   6449  O  OD2 . ASP B 1 387 ? 109.259 122.000 166.895 1.00 80.13  ? 362 ASP B OD2 1 
ATOM   6450  N  N   . ASP B 1 388 ? 109.779 118.609 164.623 1.00 70.40  ? 363 ASP B N   1 
ATOM   6451  C  CA  . ASP B 1 388 ? 110.083 118.276 163.242 1.00 68.10  ? 363 ASP B CA  1 
ATOM   6452  C  C   . ASP B 1 388 ? 111.539 118.625 162.944 1.00 65.14  ? 363 ASP B C   1 
ATOM   6453  O  O   . ASP B 1 388 ? 112.054 119.622 163.461 1.00 68.98  ? 363 ASP B O   1 
ATOM   6454  C  CB  . ASP B 1 388 ? 109.147 119.010 162.282 1.00 66.31  ? 363 ASP B CB  1 
ATOM   6455  C  CG  . ASP B 1 388 ? 109.181 120.504 162.465 1.00 69.71  ? 363 ASP B CG  1 
ATOM   6456  O  OD1 . ASP B 1 388 ? 109.507 120.953 163.581 1.00 74.42  ? 363 ASP B OD1 1 
ATOM   6457  O  OD2 . ASP B 1 388 ? 108.879 121.229 161.496 1.00 71.72  ? 363 ASP B OD2 1 
ATOM   6458  N  N   . PRO B 1 389 ? 112.234 117.821 162.139 1.00 58.65  ? 364 PRO B N   1 
ATOM   6459  C  CA  . PRO B 1 389 ? 113.681 118.023 161.974 1.00 58.90  ? 364 PRO B CA  1 
ATOM   6460  C  C   . PRO B 1 389 ? 114.060 119.378 161.410 1.00 63.76  ? 364 PRO B C   1 
ATOM   6461  O  O   . PRO B 1 389 ? 115.139 119.885 161.735 1.00 68.44  ? 364 PRO B O   1 
ATOM   6462  C  CB  . PRO B 1 389 ? 114.081 116.887 161.024 1.00 57.27  ? 364 PRO B CB  1 
ATOM   6463  C  CG  . PRO B 1 389 ? 113.009 115.874 161.174 1.00 62.79  ? 364 PRO B CG  1 
ATOM   6464  C  CD  . PRO B 1 389 ? 111.757 116.646 161.398 1.00 68.11  ? 364 PRO B CD  1 
ATOM   6465  N  N   . GLU B 1 390 ? 113.216 119.981 160.572 1.00 70.78  ? 365 GLU B N   1 
ATOM   6466  C  CA  . GLU B 1 390 ? 113.565 121.270 159.983 1.00 68.22  ? 365 GLU B CA  1 
ATOM   6467  C  C   . GLU B 1 390 ? 113.759 122.337 161.052 1.00 70.99  ? 365 GLU B C   1 
ATOM   6468  O  O   . GLU B 1 390 ? 114.709 123.124 160.987 1.00 73.75  ? 365 GLU B O   1 
ATOM   6469  C  CB  . GLU B 1 390 ? 112.489 121.697 158.988 1.00 70.84  ? 365 GLU B CB  1 
ATOM   6470  C  CG  . GLU B 1 390 ? 112.577 123.150 158.556 1.00 74.35  ? 365 GLU B CG  1 
ATOM   6471  C  CD  . GLU B 1 390 ? 113.714 123.412 157.592 1.00 79.76  ? 365 GLU B CD  1 
ATOM   6472  O  OE1 . GLU B 1 390 ? 114.848 123.649 158.055 1.00 78.04  ? 365 GLU B OE1 1 
ATOM   6473  O  OE2 . GLU B 1 390 ? 113.471 123.386 156.368 1.00 76.16  ? 365 GLU B OE2 1 
ATOM   6474  N  N   . ILE B 1 391 ? 112.871 122.379 162.045 1.00 73.79  ? 366 ILE B N   1 
ATOM   6475  C  CA  . ILE B 1 391 ? 112.994 123.360 163.119 1.00 70.28  ? 366 ILE B CA  1 
ATOM   6476  C  C   . ILE B 1 391 ? 114.168 123.029 164.033 1.00 71.66  ? 366 ILE B C   1 
ATOM   6477  O  O   . ILE B 1 391 ? 114.895 123.926 164.472 1.00 73.58  ? 366 ILE B O   1 
ATOM   6478  C  CB  . ILE B 1 391 ? 111.673 123.451 163.901 1.00 70.34  ? 366 ILE B CB  1 
ATOM   6479  C  CG1 . ILE B 1 391 ? 110.661 124.299 163.138 1.00 73.67  ? 366 ILE B CG1 1 
ATOM   6480  C  CG2 . ILE B 1 391 ? 111.903 124.030 165.283 1.00 68.73  ? 366 ILE B CG2 1 
ATOM   6481  C  CD1 . ILE B 1 391 ? 109.351 124.477 163.868 1.00 75.00  ? 366 ILE B CD1 1 
ATOM   6482  N  N   . LEU B 1 392 ? 114.379 121.743 164.326 1.00 72.19  ? 367 LEU B N   1 
ATOM   6483  C  CA  . LEU B 1 392 ? 115.372 121.360 165.326 1.00 69.25  ? 367 LEU B CA  1 
ATOM   6484  C  C   . LEU B 1 392 ? 116.773 121.808 164.935 1.00 69.09  ? 367 LEU B C   1 
ATOM   6485  O  O   . LEU B 1 392 ? 117.517 122.331 165.771 1.00 74.49  ? 367 LEU B O   1 
ATOM   6486  C  CB  . LEU B 1 392 ? 115.345 119.850 165.543 1.00 70.04  ? 367 LEU B CB  1 
ATOM   6487  C  CG  . LEU B 1 392 ? 114.321 119.330 166.548 1.00 70.89  ? 367 LEU B CG  1 
ATOM   6488  C  CD1 . LEU B 1 392 ? 114.495 117.842 166.745 1.00 71.97  ? 367 LEU B CD1 1 
ATOM   6489  C  CD2 . LEU B 1 392 ? 114.458 120.061 167.864 1.00 73.94  ? 367 LEU B CD2 1 
ATOM   6490  N  N   . MET B 1 393 ? 117.159 121.612 163.676 1.00 60.27  ? 368 MET B N   1 
ATOM   6491  C  CA  . MET B 1 393 ? 118.501 122.008 163.276 1.00 63.20  ? 368 MET B CA  1 
ATOM   6492  C  C   . MET B 1 393 ? 118.640 123.510 163.084 1.00 68.29  ? 368 MET B C   1 
ATOM   6493  O  O   . MET B 1 393 ? 119.769 124.000 162.985 1.00 73.71  ? 368 MET B O   1 
ATOM   6494  C  CB  . MET B 1 393 ? 118.927 121.281 161.997 1.00 61.45  ? 368 MET B CB  1 
ATOM   6495  C  CG  . MET B 1 393 ? 117.864 121.195 160.931 1.00 66.43  ? 368 MET B CG  1 
ATOM   6496  S  SD  . MET B 1 393 ? 118.343 120.107 159.580 1.00 77.05  ? 368 MET B SD  1 
ATOM   6497  C  CE  . MET B 1 393 ? 119.418 118.962 160.435 1.00 54.39  ? 368 MET B CE  1 
ATOM   6498  N  N   . GLN B 1 394 ? 117.535 124.253 163.025 1.00 64.95  ? 369 GLN B N   1 
ATOM   6499  C  CA  . GLN B 1 394 ? 117.637 125.708 163.009 1.00 64.21  ? 369 GLN B CA  1 
ATOM   6500  C  C   . GLN B 1 394 ? 118.123 126.231 164.354 1.00 64.72  ? 369 GLN B C   1 
ATOM   6501  O  O   . GLN B 1 394 ? 119.054 127.041 164.418 1.00 64.91  ? 369 GLN B O   1 
ATOM   6502  C  CB  . GLN B 1 394 ? 116.289 126.328 162.647 1.00 68.10  ? 369 GLN B CB  1 
ATOM   6503  C  CG  . GLN B 1 394 ? 115.838 126.053 161.229 1.00 68.33  ? 369 GLN B CG  1 
ATOM   6504  C  CD  . GLN B 1 394 ? 116.100 127.214 160.301 1.00 70.02  ? 369 GLN B CD  1 
ATOM   6505  O  OE1 . GLN B 1 394 ? 116.868 128.118 160.625 1.00 69.16  ? 369 GLN B OE1 1 
ATOM   6506  N  NE2 . GLN B 1 394 ? 115.459 127.200 159.139 1.00 68.82  ? 369 GLN B NE2 1 
ATOM   6507  N  N   . GLN B 1 395 ? 117.511 125.772 165.441 1.00 83.01  ? 370 GLN B N   1 
ATOM   6508  C  CA  . GLN B 1 395 ? 117.896 126.203 166.784 1.00 82.83  ? 370 GLN B CA  1 
ATOM   6509  C  C   . GLN B 1 395 ? 118.924 125.264 167.408 1.00 84.36  ? 370 GLN B C   1 
ATOM   6510  O  O   . GLN B 1 395 ? 118.781 124.833 168.549 1.00 84.91  ? 370 GLN B O   1 
ATOM   6511  C  CB  . GLN B 1 395 ? 116.657 126.310 167.661 1.00 82.36  ? 370 GLN B CB  1 
ATOM   6512  C  CG  . GLN B 1 395 ? 115.420 126.782 166.926 1.00 85.01  ? 370 GLN B CG  1 
ATOM   6513  C  CD  . GLN B 1 395 ? 114.146 126.222 167.520 1.00 87.58  ? 370 GLN B CD  1 
ATOM   6514  O  OE1 . GLN B 1 395 ? 114.179 125.282 168.311 1.00 87.39  ? 370 GLN B OE1 1 
ATOM   6515  N  NE2 . GLN B 1 395 ? 113.014 126.799 167.141 1.00 86.87  ? 370 GLN B NE2 1 
ATOM   6516  N  N   . GLY B 1 396 ? 119.979 124.963 166.654 1.00 87.92  ? 371 GLY B N   1 
ATOM   6517  C  CA  . GLY B 1 396 ? 121.133 124.221 167.129 1.00 85.79  ? 371 GLY B CA  1 
ATOM   6518  C  C   . GLY B 1 396 ? 120.896 123.088 168.105 1.00 86.66  ? 371 GLY B C   1 
ATOM   6519  O  O   . GLY B 1 396 ? 121.601 122.989 169.112 1.00 93.81  ? 371 GLY B O   1 
ATOM   6520  N  N   . GLU B 1 397 ? 119.924 122.225 167.830 1.00 81.44  ? 372 GLU B N   1 
ATOM   6521  C  CA  . GLU B 1 397 ? 119.625 121.110 168.731 1.00 83.32  ? 372 GLU B CA  1 
ATOM   6522  C  C   . GLU B 1 397 ? 120.390 119.847 168.349 1.00 84.56  ? 372 GLU B C   1 
ATOM   6523  O  O   . GLU B 1 397 ? 119.816 118.770 168.216 1.00 89.25  ? 372 GLU B O   1 
ATOM   6524  C  CB  . GLU B 1 397 ? 118.125 120.851 168.755 1.00 85.47  ? 372 GLU B CB  1 
ATOM   6525  C  CG  . GLU B 1 397 ? 117.295 122.080 169.063 1.00 88.42  ? 372 GLU B CG  1 
ATOM   6526  C  CD  . GLU B 1 397 ? 117.046 122.262 170.543 1.00 91.04  ? 372 GLU B CD  1 
ATOM   6527  O  OE1 . GLU B 1 397 ? 118.000 122.604 171.270 1.00 90.06  ? 372 GLU B OE1 1 
ATOM   6528  O  OE2 . GLU B 1 397 ? 115.893 122.067 170.980 1.00 91.51  ? 372 GLU B OE2 1 
ATOM   6529  N  N   . PHE B 1 398 ? 121.705 119.969 168.184 1.00 72.88  ? 373 PHE B N   1 
ATOM   6530  C  CA  . PHE B 1 398 ? 122.565 118.832 167.893 1.00 73.34  ? 373 PHE B CA  1 
ATOM   6531  C  C   . PHE B 1 398 ? 123.852 118.984 168.689 1.00 72.57  ? 373 PHE B C   1 
ATOM   6532  O  O   . PHE B 1 398 ? 124.156 120.055 169.218 1.00 80.01  ? 373 PHE B O   1 
ATOM   6533  C  CB  . PHE B 1 398 ? 122.846 118.690 166.389 1.00 74.29  ? 373 PHE B CB  1 
ATOM   6534  C  CG  . PHE B 1 398 ? 122.903 119.993 165.650 1.00 69.99  ? 373 PHE B CG  1 
ATOM   6535  C  CD1 . PHE B 1 398 ? 121.752 120.583 165.170 1.00 67.72  ? 373 PHE B CD1 1 
ATOM   6536  C  CD2 . PHE B 1 398 ? 124.111 120.618 165.420 1.00 72.94  ? 373 PHE B CD2 1 
ATOM   6537  C  CE1 . PHE B 1 398 ? 121.806 121.777 164.491 1.00 70.99  ? 373 PHE B CE1 1 
ATOM   6538  C  CE2 . PHE B 1 398 ? 124.167 121.810 164.740 1.00 72.90  ? 373 PHE B CE2 1 
ATOM   6539  C  CZ  . PHE B 1 398 ? 123.013 122.390 164.276 1.00 70.63  ? 373 PHE B CZ  1 
ATOM   6540  N  N   . LEU B 1 399 ? 124.614 117.899 168.776 1.00 71.45  ? 374 LEU B N   1 
ATOM   6541  C  CA  . LEU B 1 399 ? 125.681 117.775 169.759 1.00 76.27  ? 374 LEU B CA  1 
ATOM   6542  C  C   . LEU B 1 399 ? 127.058 117.677 169.109 1.00 83.53  ? 374 LEU B C   1 
ATOM   6543  O  O   . LEU B 1 399 ? 127.916 116.917 169.560 1.00 86.76  ? 374 LEU B O   1 
ATOM   6544  C  CB  . LEU B 1 399 ? 125.434 116.566 170.656 1.00 78.58  ? 374 LEU B CB  1 
ATOM   6545  C  CG  . LEU B 1 399 ? 124.782 116.809 172.015 1.00 80.39  ? 374 LEU B CG  1 
ATOM   6546  C  CD1 . LEU B 1 399 ? 124.173 115.525 172.544 1.00 82.52  ? 374 LEU B CD1 1 
ATOM   6547  C  CD2 . LEU B 1 399 ? 125.787 117.351 172.996 1.00 82.36  ? 374 LEU B CD2 1 
ATOM   6548  N  N   . ASN B 1 400 ? 127.293 118.452 168.049 1.00 80.62  ? 375 ASN B N   1 
ATOM   6549  C  CA  . ASN B 1 400 ? 128.619 118.594 167.441 1.00 81.94  ? 375 ASN B CA  1 
ATOM   6550  C  C   . ASN B 1 400 ? 129.151 117.250 166.929 1.00 83.38  ? 375 ASN B C   1 
ATOM   6551  O  O   . ASN B 1 400 ? 130.135 116.702 167.425 1.00 82.76  ? 375 ASN B O   1 
ATOM   6552  C  CB  . ASN B 1 400 ? 129.600 119.231 168.435 1.00 77.79  ? 375 ASN B CB  1 
ATOM   6553  C  CG  . ASN B 1 400 ? 130.885 119.696 167.779 1.00 81.12  ? 375 ASN B CG  1 
ATOM   6554  O  OD1 . ASN B 1 400 ? 131.807 118.911 167.568 1.00 83.83  ? 375 ASN B OD1 1 
ATOM   6555  N  ND2 . ASN B 1 400 ? 130.957 120.983 167.465 1.00 80.26  ? 375 ASN B ND2 1 
ATOM   6556  N  N   . TYR B 1 401 ? 128.463 116.730 165.915 1.00 62.66  ? 376 TYR B N   1 
ATOM   6557  C  CA  . TYR B 1 401 ? 128.881 115.518 165.221 1.00 52.84  ? 376 TYR B CA  1 
ATOM   6558  C  C   . TYR B 1 401 ? 129.506 115.881 163.881 1.00 60.61  ? 376 TYR B C   1 
ATOM   6559  O  O   . TYR B 1 401 ? 128.882 116.573 163.070 1.00 67.54  ? 376 TYR B O   1 
ATOM   6560  C  CB  . TYR B 1 401 ? 127.701 114.573 164.996 1.00 52.14  ? 376 TYR B CB  1 
ATOM   6561  C  CG  . TYR B 1 401 ? 127.007 114.115 166.253 1.00 55.26  ? 376 TYR B CG  1 
ATOM   6562  C  CD1 . TYR B 1 401 ? 127.623 113.242 167.128 1.00 61.20  ? 376 TYR B CD1 1 
ATOM   6563  C  CD2 . TYR B 1 401 ? 125.725 114.541 166.553 1.00 59.22  ? 376 TYR B CD2 1 
ATOM   6564  C  CE1 . TYR B 1 401 ? 126.990 112.816 168.272 1.00 59.91  ? 376 TYR B CE1 1 
ATOM   6565  C  CE2 . TYR B 1 401 ? 125.083 114.118 167.694 1.00 58.23  ? 376 TYR B CE2 1 
ATOM   6566  C  CZ  . TYR B 1 401 ? 125.721 113.256 168.549 1.00 59.64  ? 376 TYR B CZ  1 
ATOM   6567  O  OH  . TYR B 1 401 ? 125.086 112.831 169.690 1.00 65.41  ? 376 TYR B OH  1 
ATOM   6568  N  N   . ASP B 1 402 ? 130.726 115.403 163.645 1.00 62.74  ? 377 ASP B N   1 
ATOM   6569  C  CA  . ASP B 1 402 ? 131.382 115.623 162.363 1.00 58.65  ? 377 ASP B CA  1 
ATOM   6570  C  C   . ASP B 1 402 ? 130.575 114.970 161.251 1.00 56.69  ? 377 ASP B C   1 
ATOM   6571  O  O   . ASP B 1 402 ? 130.130 113.829 161.386 1.00 74.56  ? 377 ASP B O   1 
ATOM   6572  C  CB  . ASP B 1 402 ? 132.796 115.050 162.389 1.00 57.15  ? 377 ASP B CB  1 
ATOM   6573  C  CG  . ASP B 1 402 ? 133.635 115.628 163.503 1.00 67.92  ? 377 ASP B CG  1 
ATOM   6574  O  OD1 . ASP B 1 402 ? 133.129 116.505 164.231 1.00 74.93  ? 377 ASP B OD1 1 
ATOM   6575  O  OD2 . ASP B 1 402 ? 134.801 115.209 163.653 1.00 65.89  ? 377 ASP B OD2 1 
ATOM   6576  N  N   . MET B 1 403 ? 130.393 115.683 160.145 1.00 34.86  ? 378 MET B N   1 
ATOM   6577  C  CA  . MET B 1 403 ? 129.513 115.230 159.081 1.00 39.90  ? 378 MET B CA  1 
ATOM   6578  C  C   . MET B 1 403 ? 130.255 115.132 157.757 1.00 40.03  ? 378 MET B C   1 
ATOM   6579  O  O   . MET B 1 403 ? 131.134 115.941 157.456 1.00 55.18  ? 378 MET B O   1 
ATOM   6580  C  CB  . MET B 1 403 ? 128.319 116.169 158.918 1.00 41.75  ? 378 MET B CB  1 
ATOM   6581  C  CG  . MET B 1 403 ? 127.294 116.067 160.022 1.00 45.85  ? 378 MET B CG  1 
ATOM   6582  S  SD  . MET B 1 403 ? 125.616 116.169 159.381 1.00 69.00  ? 378 MET B SD  1 
ATOM   6583  C  CE  . MET B 1 403 ? 125.340 114.466 158.910 1.00 47.72  ? 378 MET B CE  1 
ATOM   6584  N  N   . LEU B 1 404 ? 129.872 114.141 156.956 1.00 17.96  ? 379 LEU B N   1 
ATOM   6585  C  CA  . LEU B 1 404 ? 130.367 113.975 155.590 1.00 21.07  ? 379 LEU B CA  1 
ATOM   6586  C  C   . LEU B 1 404 ? 129.149 113.770 154.696 1.00 33.93  ? 379 LEU B C   1 
ATOM   6587  O  O   . LEU B 1 404 ? 128.769 112.635 154.405 1.00 49.66  ? 379 LEU B O   1 
ATOM   6588  C  CB  . LEU B 1 404 ? 131.342 112.812 155.493 1.00 30.61  ? 379 LEU B CB  1 
ATOM   6589  C  CG  . LEU B 1 404 ? 132.354 112.808 154.350 1.00 25.73  ? 379 LEU B CG  1 
ATOM   6590  C  CD1 . LEU B 1 404 ? 133.551 111.968 154.729 1.00 34.66  ? 379 LEU B CD1 1 
ATOM   6591  C  CD2 . LEU B 1 404 ? 131.734 112.283 153.078 1.00 35.66  ? 379 LEU B CD2 1 
ATOM   6592  N  N   . ILE B 1 405 ? 128.557 114.866 154.245 1.00 16.34  ? 380 ILE B N   1 
ATOM   6593  C  CA  . ILE B 1 405 ? 127.338 114.821 153.460 1.00 13.48  ? 380 ILE B CA  1 
ATOM   6594  C  C   . ILE B 1 405 ? 127.705 114.852 151.987 1.00 29.71  ? 380 ILE B C   1 
ATOM   6595  O  O   . ILE B 1 405 ? 128.822 115.204 151.603 1.00 61.52  ? 380 ILE B O   1 
ATOM   6596  C  CB  . ILE B 1 405 ? 126.388 115.979 153.824 1.00 20.61  ? 380 ILE B CB  1 
ATOM   6597  C  CG1 . ILE B 1 405 ? 126.541 116.331 155.297 1.00 26.87  ? 380 ILE B CG1 1 
ATOM   6598  C  CG2 . ILE B 1 405 ? 124.951 115.603 153.547 1.00 31.64  ? 380 ILE B CG2 1 
ATOM   6599  C  CD1 . ILE B 1 405 ? 125.623 117.418 155.749 1.00 37.24  ? 380 ILE B CD1 1 
ATOM   6600  N  N   . GLY B 1 406 ? 126.761 114.471 151.140 1.00 17.89  ? 381 GLY B N   1 
ATOM   6601  C  CA  . GLY B 1 406 ? 127.039 114.480 149.719 1.00 32.98  ? 381 GLY B CA  1 
ATOM   6602  C  C   . GLY B 1 406 ? 125.827 114.088 148.912 1.00 35.10  ? 381 GLY B C   1 
ATOM   6603  O  O   . GLY B 1 406 ? 124.791 113.691 149.449 1.00 50.49  ? 381 GLY B O   1 
ATOM   6604  N  N   . VAL B 1 407 ? 125.982 114.213 147.598 1.00 42.76  ? 382 VAL B N   1 
ATOM   6605  C  CA  . VAL B 1 407 ? 124.933 113.923 146.631 1.00 24.28  ? 382 VAL B CA  1 
ATOM   6606  C  C   . VAL B 1 407 ? 125.576 113.380 145.360 1.00 45.98  ? 382 VAL B C   1 
ATOM   6607  O  O   . VAL B 1 407 ? 126.798 113.294 145.247 1.00 64.15  ? 382 VAL B O   1 
ATOM   6608  C  CB  . VAL B 1 407 ? 124.080 115.163 146.307 1.00 19.82  ? 382 VAL B CB  1 
ATOM   6609  C  CG1 . VAL B 1 407 ? 123.097 115.433 147.419 1.00 40.75  ? 382 VAL B CG1 1 
ATOM   6610  C  CG2 . VAL B 1 407 ? 124.971 116.355 146.085 1.00 24.90  ? 382 VAL B CG2 1 
ATOM   6611  N  N   . ASN B 1 408 ? 124.738 113.005 144.399 1.00 42.44  ? 383 ASN B N   1 
ATOM   6612  C  CA  . ASN B 1 408 ? 125.174 112.609 143.067 1.00 35.68  ? 383 ASN B CA  1 
ATOM   6613  C  C   . ASN B 1 408 ? 124.697 113.641 142.054 1.00 39.79  ? 383 ASN B C   1 
ATOM   6614  O  O   . ASN B 1 408 ? 123.934 114.552 142.381 1.00 49.64  ? 383 ASN B O   1 
ATOM   6615  C  CB  . ASN B 1 408 ? 124.642 111.219 142.708 1.00 31.08  ? 383 ASN B CB  1 
ATOM   6616  C  CG  . ASN B 1 408 ? 124.898 110.204 143.791 1.00 32.04  ? 383 ASN B CG  1 
ATOM   6617  O  OD1 . ASN B 1 408 ? 124.840 110.520 144.972 1.00 34.90  ? 383 ASN B OD1 1 
ATOM   6618  N  ND2 . ASN B 1 408 ? 125.177 108.974 143.395 1.00 37.54  ? 383 ASN B ND2 1 
ATOM   6619  N  N   . GLN B 1 409 ? 125.150 113.503 140.807 1.00 44.47  ? 384 GLN B N   1 
ATOM   6620  C  CA  . GLN B 1 409 ? 124.743 114.471 139.793 1.00 47.20  ? 384 GLN B CA  1 
ATOM   6621  C  C   . GLN B 1 409 ? 123.273 114.299 139.436 1.00 57.14  ? 384 GLN B C   1 
ATOM   6622  O  O   . GLN B 1 409 ? 122.484 115.245 139.531 1.00 70.87  ? 384 GLN B O   1 
ATOM   6623  C  CB  . GLN B 1 409 ? 125.616 114.369 138.539 1.00 50.60  ? 384 GLN B CB  1 
ATOM   6624  C  CG  . GLN B 1 409 ? 124.866 114.801 137.276 1.00 64.14  ? 384 GLN B CG  1 
ATOM   6625  C  CD  . GLN B 1 409 ? 125.749 114.993 136.061 1.00 66.54  ? 384 GLN B CD  1 
ATOM   6626  O  OE1 . GLN B 1 409 ? 126.368 116.039 135.892 1.00 69.89  ? 384 GLN B OE1 1 
ATOM   6627  N  NE2 . GLN B 1 409 ? 125.790 113.997 135.194 1.00 55.47  ? 384 GLN B NE2 1 
ATOM   6628  N  N   . GLY B 1 410 ? 122.886 113.104 139.008 1.00 44.09  ? 385 GLY B N   1 
ATOM   6629  C  CA  . GLY B 1 410 ? 121.496 112.876 138.678 1.00 47.36  ? 385 GLY B CA  1 
ATOM   6630  C  C   . GLY B 1 410 ? 120.897 111.720 139.442 1.00 47.50  ? 385 GLY B C   1 
ATOM   6631  O  O   . GLY B 1 410 ? 121.212 110.564 139.164 1.00 51.26  ? 385 GLY B O   1 
ATOM   6632  N  N   . GLU B 1 411 ? 120.003 112.015 140.383 1.00 49.00  ? 386 GLU B N   1 
ATOM   6633  C  CA  . GLU B 1 411 ? 119.391 110.985 141.204 1.00 44.63  ? 386 GLU B CA  1 
ATOM   6634  C  C   . GLU B 1 411 ? 117.921 110.763 140.904 1.00 47.76  ? 386 GLU B C   1 
ATOM   6635  O  O   . GLU B 1 411 ? 117.392 109.705 141.252 1.00 61.62  ? 386 GLU B O   1 
ATOM   6636  C  CB  . GLU B 1 411 ? 119.546 111.326 142.690 1.00 42.49  ? 386 GLU B CB  1 
ATOM   6637  C  CG  . GLU B 1 411 ? 120.724 112.218 142.978 1.00 47.38  ? 386 GLU B CG  1 
ATOM   6638  C  CD  . GLU B 1 411 ? 121.175 112.130 144.410 1.00 56.07  ? 386 GLU B CD  1 
ATOM   6639  O  OE1 . GLU B 1 411 ? 120.392 111.647 145.247 1.00 55.34  ? 386 GLU B OE1 1 
ATOM   6640  O  OE2 . GLU B 1 411 ? 122.315 112.539 144.699 1.00 61.82  ? 386 GLU B OE2 1 
ATOM   6641  N  N   . GLY B 1 412 ? 117.255 111.717 140.269 1.00 44.33  ? 387 GLY B N   1 
ATOM   6642  C  CA  . GLY B 1 412 ? 115.868 111.531 139.907 1.00 45.91  ? 387 GLY B CA  1 
ATOM   6643  C  C   . GLY B 1 412 ? 115.723 110.758 138.617 1.00 46.52  ? 387 GLY B C   1 
ATOM   6644  O  O   . GLY B 1 412 ? 114.847 111.056 137.803 1.00 53.13  ? 387 GLY B O   1 
ATOM   6645  N  N   . LEU B 1 413 ? 116.583 109.757 138.419 1.00 39.46  ? 388 LEU B N   1 
ATOM   6646  C  CA  . LEU B 1 413 ? 116.550 108.990 137.181 1.00 43.93  ? 388 LEU B CA  1 
ATOM   6647  C  C   . LEU B 1 413 ? 115.213 108.295 136.993 1.00 45.86  ? 388 LEU B C   1 
ATOM   6648  O  O   . LEU B 1 413 ? 114.824 107.993 135.860 1.00 56.15  ? 388 LEU B O   1 
ATOM   6649  C  CB  . LEU B 1 413 ? 117.684 107.971 137.164 1.00 47.59  ? 388 LEU B CB  1 
ATOM   6650  C  CG  . LEU B 1 413 ? 117.917 107.262 135.835 1.00 43.75  ? 388 LEU B CG  1 
ATOM   6651  C  CD1 . LEU B 1 413 ? 118.093 108.277 134.730 1.00 45.88  ? 388 LEU B CD1 1 
ATOM   6652  C  CD2 . LEU B 1 413 ? 119.124 106.360 135.925 1.00 47.84  ? 388 LEU B CD2 1 
ATOM   6653  N  N   . LYS B 1 414 ? 114.496 108.034 138.080 1.00 39.21  ? 389 LYS B N   1 
ATOM   6654  C  CA  . LYS B 1 414 ? 113.179 107.428 137.991 1.00 41.73  ? 389 LYS B CA  1 
ATOM   6655  C  C   . LYS B 1 414 ? 112.055 108.453 137.945 1.00 52.55  ? 389 LYS B C   1 
ATOM   6656  O  O   . LYS B 1 414 ? 110.894 108.066 137.777 1.00 59.80  ? 389 LYS B O   1 
ATOM   6657  C  CB  . LYS B 1 414 ? 112.968 106.470 139.162 1.00 47.01  ? 389 LYS B CB  1 
ATOM   6658  C  CG  . LYS B 1 414 ? 113.999 105.363 139.199 1.00 51.22  ? 389 LYS B CG  1 
ATOM   6659  C  CD  . LYS B 1 414 ? 113.542 104.201 140.047 1.00 57.95  ? 389 LYS B CD  1 
ATOM   6660  C  CE  . LYS B 1 414 ? 114.136 102.903 139.543 1.00 64.84  ? 389 LYS B CE  1 
ATOM   6661  N  NZ  . LYS B 1 414 ? 113.798 102.657 138.115 1.00 57.71  ? 389 LYS B NZ  1 
ATOM   6662  N  N   . PHE B 1 415 ? 112.363 109.742 138.099 1.00 48.73  ? 390 PHE B N   1 
ATOM   6663  C  CA  . PHE B 1 415 ? 111.371 110.770 137.807 1.00 40.87  ? 390 PHE B CA  1 
ATOM   6664  C  C   . PHE B 1 415 ? 111.023 110.772 136.327 1.00 48.92  ? 390 PHE B C   1 
ATOM   6665  O  O   . PHE B 1 415 ? 109.850 110.885 135.955 1.00 60.64  ? 390 PHE B O   1 
ATOM   6666  C  CB  . PHE B 1 415 ? 111.891 112.141 138.234 1.00 38.69  ? 390 PHE B CB  1 
ATOM   6667  C  CG  . PHE B 1 415 ? 110.882 113.245 138.104 1.00 42.72  ? 390 PHE B CG  1 
ATOM   6668  C  CD1 . PHE B 1 415 ? 109.597 113.089 138.579 1.00 49.02  ? 390 PHE B CD1 1 
ATOM   6669  C  CD2 . PHE B 1 415 ? 111.227 114.447 137.521 1.00 41.30  ? 390 PHE B CD2 1 
ATOM   6670  C  CE1 . PHE B 1 415 ? 108.678 114.108 138.467 1.00 46.47  ? 390 PHE B CE1 1 
ATOM   6671  C  CE2 . PHE B 1 415 ? 110.310 115.465 137.407 1.00 39.86  ? 390 PHE B CE2 1 
ATOM   6672  C  CZ  . PHE B 1 415 ? 109.037 115.295 137.879 1.00 42.15  ? 390 PHE B CZ  1 
ATOM   6673  N  N   . VAL B 1 416 ? 112.030 110.643 135.472 1.00 54.32  ? 391 VAL B N   1 
ATOM   6674  C  CA  . VAL B 1 416 ? 111.831 110.527 134.032 1.00 56.37  ? 391 VAL B CA  1 
ATOM   6675  C  C   . VAL B 1 416 ? 112.079 109.064 133.677 1.00 61.44  ? 391 VAL B C   1 
ATOM   6676  O  O   . VAL B 1 416 ? 113.203 108.635 133.415 1.00 57.72  ? 391 VAL B O   1 
ATOM   6677  C  CB  . VAL B 1 416 ? 112.725 111.489 133.253 1.00 52.96  ? 391 VAL B CB  1 
ATOM   6678  C  CG1 . VAL B 1 416 ? 112.188 112.889 133.382 1.00 54.92  ? 391 VAL B CG1 1 
ATOM   6679  C  CG2 . VAL B 1 416 ? 114.142 111.456 133.787 1.00 51.08  ? 391 VAL B CG2 1 
ATOM   6680  N  N   . GLU B 1 417 ? 111.007 108.283 133.677 1.00 76.13  ? 392 GLU B N   1 
ATOM   6681  C  CA  . GLU B 1 417 ? 111.062 106.869 133.330 1.00 76.27  ? 392 GLU B CA  1 
ATOM   6682  C  C   . GLU B 1 417 ? 110.133 106.505 132.188 1.00 79.06  ? 392 GLU B C   1 
ATOM   6683  O  O   . GLU B 1 417 ? 110.487 105.667 131.355 1.00 78.89  ? 392 GLU B O   1 
ATOM   6684  C  CB  . GLU B 1 417 ? 110.723 106.007 134.554 1.00 73.51  ? 392 GLU B CB  1 
ATOM   6685  N  N   . ASP B 1 418 ? 108.950 107.116 132.124 1.00 93.26  ? 393 ASP B N   1 
ATOM   6686  C  CA  . ASP B 1 418 ? 108.036 106.854 131.021 1.00 96.32  ? 393 ASP B CA  1 
ATOM   6687  C  C   . ASP B 1 418 ? 108.535 107.439 129.707 1.00 96.28  ? 393 ASP B C   1 
ATOM   6688  O  O   . ASP B 1 418 ? 108.025 107.070 128.645 1.00 95.21  ? 393 ASP B O   1 
ATOM   6689  C  CB  . ASP B 1 418 ? 106.649 107.410 131.344 1.00 94.11  ? 393 ASP B CB  1 
ATOM   6690  N  N   . SER B 1 419 ? 109.517 108.340 129.756 1.00 92.15  ? 394 SER B N   1 
ATOM   6691  C  CA  . SER B 1 419 ? 110.063 108.974 128.564 1.00 91.98  ? 394 SER B CA  1 
ATOM   6692  C  C   . SER B 1 419 ? 111.522 108.604 128.326 1.00 91.49  ? 394 SER B C   1 
ATOM   6693  O  O   . SER B 1 419 ? 112.221 109.303 127.588 1.00 93.29  ? 394 SER B O   1 
ATOM   6694  C  CB  . SER B 1 419 ? 109.919 110.491 128.659 1.00 87.98  ? 394 SER B CB  1 
ATOM   6695  O  OG  . SER B 1 419 ? 110.899 111.031 129.525 1.00 85.03  ? 394 SER B OG  1 
ATOM   6696  N  N   . ALA B 1 420 ? 111.997 107.525 128.940 1.00 93.09  ? 395 ALA B N   1 
ATOM   6697  C  CA  . ALA B 1 420 ? 113.366 107.068 128.748 1.00 95.29  ? 395 ALA B CA  1 
ATOM   6698  C  C   . ALA B 1 420 ? 113.512 106.121 127.565 1.00 97.07  ? 395 ALA B C   1 
ATOM   6699  O  O   . ALA B 1 420 ? 114.632 105.697 127.263 1.00 97.01  ? 395 ALA B O   1 
ATOM   6700  C  CB  . ALA B 1 420 ? 113.880 106.385 130.019 1.00 94.38  ? 395 ALA B CB  1 
ATOM   6701  N  N   . GLU B 1 421 ? 112.417 105.785 126.891 1.00 102.18 ? 396 GLU B N   1 
ATOM   6702  C  CA  . GLU B 1 421 ? 112.420 104.877 125.750 1.00 100.38 ? 396 GLU B CA  1 
ATOM   6703  C  C   . GLU B 1 421 ? 111.776 105.547 124.547 1.00 101.65 ? 396 GLU B C   1 
ATOM   6704  O  O   . GLU B 1 421 ? 110.912 104.983 123.872 1.00 99.40  ? 396 GLU B O   1 
ATOM   6705  C  CB  . GLU B 1 421 ? 111.708 103.570 126.087 1.00 97.87  ? 396 GLU B CB  1 
ATOM   6706  N  N   . SER B 1 422 ? 112.193 106.779 124.270 1.00 98.85  ? 397 SER B N   1 
ATOM   6707  C  CA  . SER B 1 422 ? 111.677 107.549 123.151 1.00 98.77  ? 397 SER B CA  1 
ATOM   6708  C  C   . SER B 1 422 ? 112.838 108.051 122.305 1.00 98.67  ? 397 SER B C   1 
ATOM   6709  O  O   . SER B 1 422 ? 113.969 108.182 122.779 1.00 95.00  ? 397 SER B O   1 
ATOM   6710  C  CB  . SER B 1 422 ? 110.819 108.729 123.628 1.00 94.76  ? 397 SER B CB  1 
ATOM   6711  O  OG  . SER B 1 422 ? 110.036 109.248 122.568 1.00 95.29  ? 397 SER B OG  1 
ATOM   6712  N  N   . GLU B 1 423 ? 112.546 108.313 121.029 1.00 100.11 ? 398 GLU B N   1 
ATOM   6713  C  CA  . GLU B 1 423 ? 113.571 108.826 120.126 1.00 99.95  ? 398 GLU B CA  1 
ATOM   6714  C  C   . GLU B 1 423 ? 114.064 110.193 120.581 1.00 103.23 ? 398 GLU B C   1 
ATOM   6715  O  O   . GLU B 1 423 ? 115.270 110.410 120.745 1.00 102.68 ? 398 GLU B O   1 
ATOM   6716  C  CB  . GLU B 1 423 ? 113.025 108.895 118.700 1.00 99.37  ? 398 GLU B CB  1 
ATOM   6717  N  N   . ASP B 1 424 ? 113.144 111.123 120.801 1.00 100.09 ? 399 ASP B N   1 
ATOM   6718  C  CA  . ASP B 1 424 ? 113.458 112.422 121.372 1.00 96.27  ? 399 ASP B CA  1 
ATOM   6719  C  C   . ASP B 1 424 ? 112.986 112.468 122.818 1.00 96.50  ? 399 ASP B C   1 
ATOM   6720  O  O   . ASP B 1 424 ? 112.283 111.576 123.299 1.00 99.49  ? 399 ASP B O   1 
ATOM   6721  C  CB  . ASP B 1 424 ? 112.819 113.552 120.557 1.00 94.41  ? 399 ASP B CB  1 
ATOM   6722  C  CG  . ASP B 1 424 ? 111.307 113.514 120.593 1.00 96.72  ? 399 ASP B CG  1 
ATOM   6723  O  OD1 . ASP B 1 424 ? 110.741 112.416 120.775 1.00 95.26  ? 399 ASP B OD1 1 
ATOM   6724  O  OD2 . ASP B 1 424 ? 110.682 114.583 120.436 1.00 99.54  ? 399 ASP B OD2 1 
ATOM   6725  N  N   . GLY B 1 425 ? 113.379 113.525 123.515 1.00 90.01  ? 400 GLY B N   1 
ATOM   6726  C  CA  . GLY B 1 425 ? 113.052 113.680 124.918 1.00 89.24  ? 400 GLY B CA  1 
ATOM   6727  C  C   . GLY B 1 425 ? 111.601 114.038 125.147 1.00 90.32  ? 400 GLY B C   1 
ATOM   6728  O  O   . GLY B 1 425 ? 110.717 113.719 124.345 1.00 93.56  ? 400 GLY B O   1 
ATOM   6729  N  N   . VAL B 1 426 ? 111.352 114.713 126.259 1.00 72.72  ? 401 VAL B N   1 
ATOM   6730  C  CA  . VAL B 1 426 ? 109.996 115.069 126.652 1.00 72.86  ? 401 VAL B CA  1 
ATOM   6731  C  C   . VAL B 1 426 ? 109.527 116.252 125.817 1.00 73.91  ? 401 VAL B C   1 
ATOM   6732  O  O   . VAL B 1 426 ? 110.224 117.268 125.712 1.00 79.08  ? 401 VAL B O   1 
ATOM   6733  C  CB  . VAL B 1 426 ? 109.940 115.391 128.151 1.00 75.15  ? 401 VAL B CB  1 
ATOM   6734  C  CG1 . VAL B 1 426 ? 108.546 115.810 128.550 1.00 73.53  ? 401 VAL B CG1 1 
ATOM   6735  C  CG2 . VAL B 1 426 ? 110.391 114.193 128.957 1.00 77.33  ? 401 VAL B CG2 1 
ATOM   6736  N  N   . SER B 1 427 ? 108.349 116.124 125.216 1.00 72.06  ? 402 SER B N   1 
ATOM   6737  C  CA  . SER B 1 427 ? 107.769 117.231 124.475 1.00 76.90  ? 402 SER B CA  1 
ATOM   6738  C  C   . SER B 1 427 ? 107.250 118.300 125.434 1.00 79.00  ? 402 SER B C   1 
ATOM   6739  O  O   . SER B 1 427 ? 107.053 118.058 126.627 1.00 86.45  ? 402 SER B O   1 
ATOM   6740  C  CB  . SER B 1 427 ? 106.642 116.737 123.572 1.00 78.83  ? 402 SER B CB  1 
ATOM   6741  O  OG  . SER B 1 427 ? 105.826 115.800 124.250 1.00 82.81  ? 402 SER B OG  1 
ATOM   6742  N  N   . ALA B 1 428 ? 107.026 119.500 124.893 1.00 66.09  ? 403 ALA B N   1 
ATOM   6743  C  CA  . ALA B 1 428 ? 106.633 120.630 125.730 1.00 65.05  ? 403 ALA B CA  1 
ATOM   6744  C  C   . ALA B 1 428 ? 105.290 120.385 126.404 1.00 68.81  ? 403 ALA B C   1 
ATOM   6745  O  O   . ALA B 1 428 ? 105.111 120.708 127.585 1.00 71.02  ? 403 ALA B O   1 
ATOM   6746  C  CB  . ALA B 1 428 ? 106.586 121.908 124.897 1.00 67.86  ? 403 ALA B CB  1 
ATOM   6747  N  N   . SER B 1 429 ? 104.334 119.814 125.667 1.00 73.47  ? 404 SER B N   1 
ATOM   6748  C  CA  . SER B 1 429 ? 103.036 119.497 126.251 1.00 73.06  ? 404 SER B CA  1 
ATOM   6749  C  C   . SER B 1 429 ? 103.165 118.499 127.392 1.00 70.93  ? 404 SER B C   1 
ATOM   6750  O  O   . SER B 1 429 ? 102.325 118.480 128.297 1.00 72.18  ? 404 SER B O   1 
ATOM   6751  C  CB  . SER B 1 429 ? 102.095 118.952 125.177 1.00 77.98  ? 404 SER B CB  1 
ATOM   6752  O  OG  . SER B 1 429 ? 101.981 119.854 124.091 1.00 80.21  ? 404 SER B OG  1 
ATOM   6753  N  N   . ALA B 1 430 ? 104.201 117.662 127.365 1.00 66.01  ? 405 ALA B N   1 
ATOM   6754  C  CA  . ALA B 1 430 ? 104.448 116.729 128.454 1.00 68.70  ? 405 ALA B CA  1 
ATOM   6755  C  C   . ALA B 1 430 ? 105.362 117.308 129.524 1.00 70.05  ? 405 ALA B C   1 
ATOM   6756  O  O   . ALA B 1 430 ? 105.207 116.974 130.703 1.00 70.69  ? 405 ALA B O   1 
ATOM   6757  C  CB  . ALA B 1 430 ? 105.047 115.431 127.910 1.00 63.46  ? 405 ALA B CB  1 
ATOM   6758  N  N   . PHE B 1 431 ? 106.302 118.176 129.146 1.00 62.30  ? 406 PHE B N   1 
ATOM   6759  C  CA  . PHE B 1 431 ? 107.154 118.829 130.135 1.00 48.39  ? 406 PHE B CA  1 
ATOM   6760  C  C   . PHE B 1 431 ? 106.329 119.697 131.076 1.00 52.61  ? 406 PHE B C   1 
ATOM   6761  O  O   . PHE B 1 431 ? 106.468 119.614 132.304 1.00 68.79  ? 406 PHE B O   1 
ATOM   6762  C  CB  . PHE B 1 431 ? 108.224 119.655 129.421 1.00 52.58  ? 406 PHE B CB  1 
ATOM   6763  C  CG  . PHE B 1 431 ? 109.067 120.497 130.335 1.00 58.80  ? 406 PHE B CG  1 
ATOM   6764  C  CD1 . PHE B 1 431 ? 110.164 119.960 130.979 1.00 59.43  ? 406 PHE B CD1 1 
ATOM   6765  C  CD2 . PHE B 1 431 ? 108.782 121.835 130.525 1.00 62.55  ? 406 PHE B CD2 1 
ATOM   6766  C  CE1 . PHE B 1 431 ? 110.944 120.736 131.810 1.00 54.17  ? 406 PHE B CE1 1 
ATOM   6767  C  CE2 . PHE B 1 431 ? 109.560 122.611 131.354 1.00 60.14  ? 406 PHE B CE2 1 
ATOM   6768  C  CZ  . PHE B 1 431 ? 110.642 122.060 131.996 1.00 56.14  ? 406 PHE B CZ  1 
ATOM   6769  N  N   . ASP B 1 432 ? 105.446 120.527 130.517 1.00 58.05  ? 407 ASP B N   1 
ATOM   6770  C  CA  . ASP B 1 432 ? 104.617 121.366 131.374 1.00 61.88  ? 407 ASP B CA  1 
ATOM   6771  C  C   . ASP B 1 432 ? 103.648 120.536 132.207 1.00 64.44  ? 407 ASP B C   1 
ATOM   6772  O  O   . ASP B 1 432 ? 103.352 120.895 133.351 1.00 65.35  ? 407 ASP B O   1 
ATOM   6773  C  CB  . ASP B 1 432 ? 103.932 122.456 130.526 1.00 64.83  ? 407 ASP B CB  1 
ATOM   6774  C  CG  . ASP B 1 432 ? 102.551 122.064 129.967 1.00 79.08  ? 407 ASP B CG  1 
ATOM   6775  O  OD1 . ASP B 1 432 ? 101.990 120.985 130.244 1.00 84.20  ? 407 ASP B OD1 1 
ATOM   6776  O  OD2 . ASP B 1 432 ? 102.003 122.892 129.208 1.00 78.65  ? 407 ASP B OD2 1 
ATOM   6777  N  N   . PHE B 1 433 ? 103.163 119.416 131.666 1.00 62.64  ? 408 PHE B N   1 
ATOM   6778  C  CA  . PHE B 1 433 ? 102.293 118.538 132.441 1.00 60.96  ? 408 PHE B CA  1 
ATOM   6779  C  C   . PHE B 1 433 ? 103.034 117.916 133.620 1.00 71.21  ? 408 PHE B C   1 
ATOM   6780  O  O   . PHE B 1 433 ? 102.493 117.846 134.730 1.00 75.99  ? 408 PHE B O   1 
ATOM   6781  C  CB  . PHE B 1 433 ? 101.709 117.451 131.542 1.00 58.26  ? 408 PHE B CB  1 
ATOM   6782  C  CG  . PHE B 1 433 ? 100.792 116.505 132.256 1.00 66.83  ? 408 PHE B CG  1 
ATOM   6783  C  CD1 . PHE B 1 433 ? 99.478  116.850 132.502 1.00 67.64  ? 408 PHE B CD1 1 
ATOM   6784  C  CD2 . PHE B 1 433 ? 101.244 115.268 132.679 1.00 68.05  ? 408 PHE B CD2 1 
ATOM   6785  C  CE1 . PHE B 1 433 ? 98.632  115.981 133.159 1.00 63.99  ? 408 PHE B CE1 1 
ATOM   6786  C  CE2 . PHE B 1 433 ? 100.401 114.396 133.336 1.00 66.22  ? 408 PHE B CE2 1 
ATOM   6787  C  CZ  . PHE B 1 433 ? 99.094  114.752 133.574 1.00 62.66  ? 408 PHE B CZ  1 
ATOM   6788  N  N   . THR B 1 434 ? 104.267 117.450 133.400 1.00 66.89  ? 409 THR B N   1 
ATOM   6789  C  CA  . THR B 1 434 ? 105.036 116.878 134.500 1.00 58.99  ? 409 THR B CA  1 
ATOM   6790  C  C   . THR B 1 434 ? 105.340 117.925 135.558 1.00 56.46  ? 409 THR B C   1 
ATOM   6791  O  O   . THR B 1 434 ? 105.276 117.636 136.756 1.00 65.45  ? 409 THR B O   1 
ATOM   6792  C  CB  . THR B 1 434 ? 106.334 116.252 133.997 1.00 52.50  ? 409 THR B CB  1 
ATOM   6793  O  OG1 . THR B 1 434 ? 107.094 117.234 133.286 1.00 63.66  ? 409 THR B OG1 1 
ATOM   6794  C  CG2 . THR B 1 434 ? 106.049 115.067 133.096 1.00 57.78  ? 409 THR B CG2 1 
ATOM   6795  N  N   . VAL B 1 435 ? 105.672 119.148 135.141 1.00 42.57  ? 410 VAL B N   1 
ATOM   6796  C  CA  . VAL B 1 435 ? 105.935 120.201 136.121 1.00 38.44  ? 410 VAL B CA  1 
ATOM   6797  C  C   . VAL B 1 435 ? 104.671 120.531 136.909 1.00 48.25  ? 410 VAL B C   1 
ATOM   6798  O  O   . VAL B 1 435 ? 104.719 120.750 138.127 1.00 58.80  ? 410 VAL B O   1 
ATOM   6799  C  CB  . VAL B 1 435 ? 106.522 121.445 135.435 1.00 36.23  ? 410 VAL B CB  1 
ATOM   6800  C  CG1 . VAL B 1 435 ? 106.553 122.602 136.397 1.00 41.12  ? 410 VAL B CG1 1 
ATOM   6801  C  CG2 . VAL B 1 435 ? 107.917 121.152 134.941 1.00 38.73  ? 410 VAL B CG2 1 
ATOM   6802  N  N   . SER B 1 436 ? 103.520 120.572 136.233 1.00 55.58  ? 411 SER B N   1 
ATOM   6803  C  CA  . SER B 1 436 ? 102.268 120.850 136.930 1.00 56.03  ? 411 SER B CA  1 
ATOM   6804  C  C   . SER B 1 436 ? 101.939 119.758 137.938 1.00 58.73  ? 411 SER B C   1 
ATOM   6805  O  O   . SER B 1 436 ? 101.506 120.050 139.058 1.00 64.29  ? 411 SER B O   1 
ATOM   6806  C  CB  . SER B 1 436 ? 101.130 121.006 135.927 1.00 65.34  ? 411 SER B CB  1 
ATOM   6807  O  OG  . SER B 1 436 ? 99.921  121.329 136.587 1.00 66.56  ? 411 SER B OG  1 
ATOM   6808  N  N   . ASN B 1 437 ? 102.129 118.493 137.559 1.00 57.70  ? 412 ASN B N   1 
ATOM   6809  C  CA  . ASN B 1 437 ? 101.900 117.401 138.502 1.00 60.92  ? 412 ASN B CA  1 
ATOM   6810  C  C   . ASN B 1 437 ? 102.876 117.469 139.671 1.00 65.13  ? 412 ASN B C   1 
ATOM   6811  O  O   . ASN B 1 437 ? 102.504 117.203 140.820 1.00 62.68  ? 412 ASN B O   1 
ATOM   6812  C  CB  . ASN B 1 437 ? 102.012 116.058 137.788 1.00 61.38  ? 412 ASN B CB  1 
ATOM   6813  C  CG  . ASN B 1 437 ? 100.665 115.467 137.457 1.00 73.57  ? 412 ASN B CG  1 
ATOM   6814  O  OD1 . ASN B 1 437 ? 100.142 114.635 138.196 1.00 76.95  ? 412 ASN B OD1 1 
ATOM   6815  N  ND2 . ASN B 1 437 ? 100.086 115.903 136.348 1.00 71.43  ? 412 ASN B ND2 1 
ATOM   6816  N  N   . PHE B 1 438 ? 104.132 117.812 139.389 1.00 59.35  ? 413 PHE B N   1 
ATOM   6817  C  CA  . PHE B 1 438 ? 105.128 118.003 140.436 1.00 47.38  ? 413 PHE B CA  1 
ATOM   6818  C  C   . PHE B 1 438 ? 104.654 119.030 141.455 1.00 49.15  ? 413 PHE B C   1 
ATOM   6819  O  O   . PHE B 1 438 ? 104.635 118.764 142.664 1.00 57.04  ? 413 PHE B O   1 
ATOM   6820  C  CB  . PHE B 1 438 ? 106.441 118.432 139.780 1.00 50.48  ? 413 PHE B CB  1 
ATOM   6821  C  CG  . PHE B 1 438 ? 107.564 118.675 140.734 1.00 52.05  ? 413 PHE B CG  1 
ATOM   6822  C  CD1 . PHE B 1 438 ? 108.405 117.647 141.104 1.00 56.45  ? 413 PHE B CD1 1 
ATOM   6823  C  CD2 . PHE B 1 438 ? 107.809 119.941 141.225 1.00 50.28  ? 413 PHE B CD2 1 
ATOM   6824  C  CE1 . PHE B 1 438 ? 109.447 117.871 141.966 1.00 55.07  ? 413 PHE B CE1 1 
ATOM   6825  C  CE2 . PHE B 1 438 ? 108.849 120.168 142.086 1.00 45.55  ? 413 PHE B CE2 1 
ATOM   6826  C  CZ  . PHE B 1 438 ? 109.669 119.132 142.455 1.00 49.73  ? 413 PHE B CZ  1 
ATOM   6827  N  N   . VAL B 1 439 ? 104.237 120.203 140.978 1.00 49.81  ? 414 VAL B N   1 
ATOM   6828  C  CA  . VAL B 1 439 ? 103.805 121.265 141.884 1.00 47.80  ? 414 VAL B CA  1 
ATOM   6829  C  C   . VAL B 1 439 ? 102.545 120.855 142.635 1.00 54.62  ? 414 VAL B C   1 
ATOM   6830  O  O   . VAL B 1 439 ? 102.393 121.148 143.826 1.00 59.56  ? 414 VAL B O   1 
ATOM   6831  C  CB  . VAL B 1 439 ? 103.601 122.582 141.115 1.00 47.14  ? 414 VAL B CB  1 
ATOM   6832  C  CG1 . VAL B 1 439 ? 103.162 123.676 142.059 1.00 48.92  ? 414 VAL B CG1 1 
ATOM   6833  C  CG2 . VAL B 1 439 ? 104.876 122.981 140.423 1.00 50.64  ? 414 VAL B CG2 1 
ATOM   6834  N  N   . ASP B 1 440 ? 101.617 120.177 141.954 1.00 63.26  ? 415 ASP B N   1 
ATOM   6835  C  CA  . ASP B 1 440 ? 100.387 119.750 142.613 1.00 63.57  ? 415 ASP B CA  1 
ATOM   6836  C  C   . ASP B 1 440 ? 100.672 118.774 143.746 1.00 70.31  ? 415 ASP B C   1 
ATOM   6837  O  O   . ASP B 1 440 ? 100.118 118.904 144.842 1.00 70.77  ? 415 ASP B O   1 
ATOM   6838  C  CB  . ASP B 1 440 ? 99.438  119.116 141.596 1.00 66.07  ? 415 ASP B CB  1 
ATOM   6839  C  CG  . ASP B 1 440 ? 98.812  120.133 140.669 1.00 75.93  ? 415 ASP B CG  1 
ATOM   6840  O  OD1 . ASP B 1 440 ? 99.271  121.294 140.660 1.00 79.54  ? 415 ASP B OD1 1 
ATOM   6841  O  OD2 . ASP B 1 440 ? 97.858  119.772 139.948 1.00 77.37  ? 415 ASP B OD2 1 
ATOM   6842  N  N   . ASN B 1 441 ? 101.541 117.790 143.502 1.00 64.98  ? 416 ASN B N   1 
ATOM   6843  C  CA  . ASN B 1 441 ? 101.805 116.769 144.507 1.00 56.71  ? 416 ASN B CA  1 
ATOM   6844  C  C   . ASN B 1 441 ? 102.666 117.287 145.647 1.00 62.66  ? 416 ASN B C   1 
ATOM   6845  O  O   . ASN B 1 441 ? 102.496 116.847 146.788 1.00 66.70  ? 416 ASN B O   1 
ATOM   6846  C  CB  . ASN B 1 441 ? 102.477 115.557 143.866 1.00 51.04  ? 416 ASN B CB  1 
ATOM   6847  C  CG  . ASN B 1 441 ? 101.623 114.917 142.801 1.00 61.92  ? 416 ASN B CG  1 
ATOM   6848  O  OD1 . ASN B 1 441 ? 102.115 114.539 141.741 1.00 68.94  ? 416 ASN B OD1 1 
ATOM   6849  N  ND2 . ASN B 1 441 ? 100.334 114.791 143.076 1.00 66.42  ? 416 ASN B ND2 1 
ATOM   6850  N  N   . LEU B 1 442 ? 103.585 118.212 145.373 1.00 57.47  ? 417 LEU B N   1 
ATOM   6851  C  CA  . LEU B 1 442 ? 104.536 118.598 146.407 1.00 49.64  ? 417 LEU B CA  1 
ATOM   6852  C  C   . LEU B 1 442 ? 104.117 119.840 147.184 1.00 50.39  ? 417 LEU B C   1 
ATOM   6853  O  O   . LEU B 1 442 ? 104.260 119.871 148.409 1.00 61.61  ? 417 LEU B O   1 
ATOM   6854  C  CB  . LEU B 1 442 ? 105.916 118.805 145.790 1.00 43.24  ? 417 LEU B CB  1 
ATOM   6855  C  CG  . LEU B 1 442 ? 106.824 117.620 146.084 1.00 47.46  ? 417 LEU B CG  1 
ATOM   6856  C  CD1 . LEU B 1 442 ? 107.994 117.582 145.136 1.00 54.14  ? 417 LEU B CD1 1 
ATOM   6857  C  CD2 . LEU B 1 442 ? 107.296 117.705 147.517 1.00 53.22  ? 417 LEU B CD2 1 
ATOM   6858  N  N   . TYR B 1 443 ? 103.609 120.870 146.511 1.00 50.71  ? 418 TYR B N   1 
ATOM   6859  C  CA  . TYR B 1 443 ? 103.200 122.097 147.189 1.00 52.54  ? 418 TYR B CA  1 
ATOM   6860  C  C   . TYR B 1 443 ? 101.692 122.160 147.401 1.00 56.14  ? 418 TYR B C   1 
ATOM   6861  O  O   . TYR B 1 443 ? 101.226 122.266 148.539 1.00 51.86  ? 418 TYR B O   1 
ATOM   6862  C  CB  . TYR B 1 443 ? 103.687 123.316 146.399 1.00 50.07  ? 418 TYR B CB  1 
ATOM   6863  C  CG  . TYR B 1 443 ? 105.189 123.446 146.382 1.00 48.99  ? 418 TYR B CG  1 
ATOM   6864  C  CD1 . TYR B 1 443 ? 105.859 124.078 147.414 1.00 51.65  ? 418 TYR B CD1 1 
ATOM   6865  C  CD2 . TYR B 1 443 ? 105.936 122.925 145.339 1.00 51.35  ? 418 TYR B CD2 1 
ATOM   6866  C  CE1 . TYR B 1 443 ? 107.226 124.192 147.406 1.00 50.74  ? 418 TYR B CE1 1 
ATOM   6867  C  CE2 . TYR B 1 443 ? 107.302 123.036 145.322 1.00 48.90  ? 418 TYR B CE2 1 
ATOM   6868  C  CZ  . TYR B 1 443 ? 107.942 123.670 146.359 1.00 49.16  ? 418 TYR B CZ  1 
ATOM   6869  O  OH  . TYR B 1 443 ? 109.311 123.785 146.352 1.00 46.65  ? 418 TYR B OH  1 
ATOM   6870  N  N   . GLY B 1 444 ? 100.919 122.090 146.321 1.00 82.81  ? 419 GLY B N   1 
ATOM   6871  C  CA  . GLY B 1 444 ? 99.470  122.073 146.432 1.00 83.27  ? 419 GLY B CA  1 
ATOM   6872  C  C   . GLY B 1 444 ? 98.871  123.306 147.070 1.00 87.77  ? 419 GLY B C   1 
ATOM   6873  O  O   . GLY B 1 444 ? 97.784  123.227 147.653 1.00 88.42  ? 419 GLY B O   1 
ATOM   6874  N  N   . TYR B 1 445 ? 99.544  124.449 146.970 1.00 98.92  ? 420 TYR B N   1 
ATOM   6875  C  CA  . TYR B 1 445 ? 99.035  125.684 147.551 1.00 95.31  ? 420 TYR B CA  1 
ATOM   6876  C  C   . TYR B 1 445 ? 98.050  126.329 146.586 1.00 98.58  ? 420 TYR B C   1 
ATOM   6877  O  O   . TYR B 1 445 ? 98.419  126.601 145.436 1.00 100.03 ? 420 TYR B O   1 
ATOM   6878  C  CB  . TYR B 1 445 ? 100.171 126.645 147.856 1.00 93.35  ? 420 TYR B CB  1 
ATOM   6879  N  N   . PRO B 1 446 ? 96.801  126.567 146.991 1.00 103.41 ? 421 PRO B N   1 
ATOM   6880  C  CA  . PRO B 1 446 ? 95.842  127.194 146.067 1.00 101.32 ? 421 PRO B CA  1 
ATOM   6881  C  C   . PRO B 1 446 ? 96.253  128.583 145.612 1.00 103.36 ? 421 PRO B C   1 
ATOM   6882  O  O   . PRO B 1 446 ? 95.961  128.961 144.470 1.00 100.02 ? 421 PRO B O   1 
ATOM   6883  C  CB  . PRO B 1 446 ? 94.542  127.232 146.884 1.00 102.13 ? 421 PRO B CB  1 
ATOM   6884  C  CG  . PRO B 1 446 ? 94.737  126.231 147.982 1.00 101.44 ? 421 PRO B CG  1 
ATOM   6885  C  CD  . PRO B 1 446 ? 96.197  126.260 148.296 1.00 102.30 ? 421 PRO B CD  1 
ATOM   6886  N  N   . GLU B 1 447 ? 96.922  129.356 146.469 1.00 106.72 ? 422 GLU B N   1 
ATOM   6887  C  CA  . GLU B 1 447 ? 97.283  130.727 146.119 1.00 104.93 ? 422 GLU B CA  1 
ATOM   6888  C  C   . GLU B 1 447 ? 98.501  130.761 145.204 1.00 106.95 ? 422 GLU B C   1 
ATOM   6889  O  O   . GLU B 1 447 ? 98.432  131.256 144.074 1.00 105.93 ? 422 GLU B O   1 
ATOM   6890  C  CB  . GLU B 1 447 ? 97.538  131.542 147.389 1.00 100.98 ? 422 GLU B CB  1 
ATOM   6891  N  N   . GLY B 1 448 ? 99.628  130.242 145.679 1.00 94.66  ? 423 GLY B N   1 
ATOM   6892  C  CA  . GLY B 1 448 ? 100.812 130.156 144.850 1.00 91.57  ? 423 GLY B CA  1 
ATOM   6893  C  C   . GLY B 1 448 ? 100.769 128.942 143.949 1.00 91.93  ? 423 GLY B C   1 
ATOM   6894  O  O   . GLY B 1 448 ? 101.495 127.968 144.170 1.00 94.63  ? 423 GLY B O   1 
ATOM   6895  N  N   . LYS B 1 449 ? 99.913  128.981 142.934 1.00 84.22  ? 424 LYS B N   1 
ATOM   6896  C  CA  . LYS B 1 449 ? 99.747  127.864 142.016 1.00 88.12  ? 424 LYS B CA  1 
ATOM   6897  C  C   . LYS B 1 449 ? 100.273 128.168 140.624 1.00 89.66  ? 424 LYS B C   1 
ATOM   6898  O  O   . LYS B 1 449 ? 101.050 127.384 140.072 1.00 88.67  ? 424 LYS B O   1 
ATOM   6899  C  CB  . LYS B 1 449 ? 98.266  127.465 141.937 1.00 87.33  ? 424 LYS B CB  1 
ATOM   6900  N  N   . ASP B 1 450 ? 99.869  129.294 140.037 1.00 80.63  ? 425 ASP B N   1 
ATOM   6901  C  CA  . ASP B 1 450 ? 100.311 129.654 138.699 1.00 77.03  ? 425 ASP B CA  1 
ATOM   6902  C  C   . ASP B 1 450 ? 101.491 130.613 138.692 1.00 76.27  ? 425 ASP B C   1 
ATOM   6903  O  O   . ASP B 1 450 ? 102.178 130.713 137.671 1.00 72.74  ? 425 ASP B O   1 
ATOM   6904  C  CB  . ASP B 1 450 ? 99.154  130.267 137.906 1.00 78.30  ? 425 ASP B CB  1 
ATOM   6905  C  CG  . ASP B 1 450 ? 98.502  129.268 136.975 1.00 81.72  ? 425 ASP B CG  1 
ATOM   6906  O  OD1 . ASP B 1 450 ? 99.210  128.354 136.506 1.00 80.58  ? 425 ASP B OD1 1 
ATOM   6907  O  OD2 . ASP B 1 450 ? 97.286  129.390 136.719 1.00 83.41  ? 425 ASP B OD2 1 
ATOM   6908  N  N   . VAL B 1 451 ? 101.731 131.331 139.789 1.00 65.47  ? 426 VAL B N   1 
ATOM   6909  C  CA  . VAL B 1 451 ? 102.970 132.089 139.908 1.00 55.34  ? 426 VAL B CA  1 
ATOM   6910  C  C   . VAL B 1 451 ? 104.146 131.145 140.101 1.00 61.59  ? 426 VAL B C   1 
ATOM   6911  O  O   . VAL B 1 451 ? 105.214 131.336 139.512 1.00 67.75  ? 426 VAL B O   1 
ATOM   6912  C  CB  . VAL B 1 451 ? 102.874 133.110 141.054 1.00 48.71  ? 426 VAL B CB  1 
ATOM   6913  C  CG1 . VAL B 1 451 ? 104.164 133.890 141.163 1.00 47.81  ? 426 VAL B CG1 1 
ATOM   6914  C  CG2 . VAL B 1 451 ? 101.702 134.046 140.831 1.00 58.34  ? 426 VAL B CG2 1 
ATOM   6915  N  N   . LEU B 1 452 ? 103.968 130.113 140.928 1.00 60.00  ? 427 LEU B N   1 
ATOM   6916  C  CA  . LEU B 1 452 ? 105.065 129.199 141.231 1.00 57.16  ? 427 LEU B CA  1 
ATOM   6917  C  C   . LEU B 1 452 ? 105.351 128.258 140.069 1.00 52.33  ? 427 LEU B C   1 
ATOM   6918  O  O   . LEU B 1 452 ? 106.517 128.006 139.739 1.00 56.16  ? 427 LEU B O   1 
ATOM   6919  C  CB  . LEU B 1 452 ? 104.743 128.405 142.493 1.00 56.86  ? 427 LEU B CB  1 
ATOM   6920  C  CG  . LEU B 1 452 ? 105.855 127.532 143.058 1.00 54.96  ? 427 LEU B CG  1 
ATOM   6921  C  CD1 . LEU B 1 452 ? 107.174 128.265 143.020 1.00 53.65  ? 427 LEU B CD1 1 
ATOM   6922  C  CD2 . LEU B 1 452 ? 105.509 127.136 144.471 1.00 59.84  ? 427 LEU B CD2 1 
ATOM   6923  N  N   . ARG B 1 453 ? 104.305 127.718 139.444 1.00 56.51  ? 428 ARG B N   1 
ATOM   6924  C  CA  . ARG B 1 453 ? 104.520 126.801 138.333 1.00 62.34  ? 428 ARG B CA  1 
ATOM   6925  C  C   . ARG B 1 453 ? 105.217 127.499 137.178 1.00 67.62  ? 428 ARG B C   1 
ATOM   6926  O  O   . ARG B 1 453 ? 106.112 126.929 136.549 1.00 69.66  ? 428 ARG B O   1 
ATOM   6927  C  CB  . ARG B 1 453 ? 103.196 126.201 137.873 1.00 61.42  ? 428 ARG B CB  1 
ATOM   6928  C  CG  . ARG B 1 453 ? 103.327 125.362 136.621 1.00 62.33  ? 428 ARG B CG  1 
ATOM   6929  C  CD  . ARG B 1 453 ? 102.094 124.515 136.374 1.00 69.20  ? 428 ARG B CD  1 
ATOM   6930  N  NE  . ARG B 1 453 ? 100.880 125.313 136.271 1.00 72.29  ? 428 ARG B NE  1 
ATOM   6931  C  CZ  . ARG B 1 453 ? 99.971  125.415 137.230 1.00 72.96  ? 428 ARG B CZ  1 
ATOM   6932  N  NH1 . ARG B 1 453 ? 100.117 124.793 138.389 1.00 68.97  ? 428 ARG B NH1 1 
ATOM   6933  N  NH2 . ARG B 1 453 ? 98.889  126.158 137.023 1.00 72.40  ? 428 ARG B NH2 1 
ATOM   6934  N  N   . GLU B 1 454 ? 104.833 128.743 136.895 1.00 63.77  ? 429 GLU B N   1 
ATOM   6935  C  CA  . GLU B 1 454 ? 105.460 129.473 135.801 1.00 52.91  ? 429 GLU B CA  1 
ATOM   6936  C  C   . GLU B 1 454 ? 106.931 129.750 136.078 1.00 51.36  ? 429 GLU B C   1 
ATOM   6937  O  O   . GLU B 1 454 ? 107.768 129.623 135.179 1.00 56.62  ? 429 GLU B O   1 
ATOM   6938  C  CB  . GLU B 1 454 ? 104.706 130.772 135.537 1.00 55.74  ? 429 GLU B CB  1 
ATOM   6939  C  CG  . GLU B 1 454 ? 103.604 130.621 134.511 1.00 67.20  ? 429 GLU B CG  1 
ATOM   6940  C  CD  . GLU B 1 454 ? 104.091 129.953 133.240 1.00 72.65  ? 429 GLU B CD  1 
ATOM   6941  O  OE1 . GLU B 1 454 ? 105.162 130.347 132.732 1.00 69.20  ? 429 GLU B OE1 1 
ATOM   6942  O  OE2 . GLU B 1 454 ? 103.405 129.030 132.751 1.00 73.45  ? 429 GLU B OE2 1 
ATOM   6943  N  N   . THR B 1 455 ? 107.277 130.116 137.313 1.00 41.95  ? 430 THR B N   1 
ATOM   6944  C  CA  . THR B 1 455 ? 108.671 130.451 137.578 1.00 41.36  ? 430 THR B CA  1 
ATOM   6945  C  C   . THR B 1 455 ? 109.551 129.210 137.653 1.00 47.78  ? 430 THR B C   1 
ATOM   6946  O  O   . THR B 1 455 ? 110.708 129.260 137.224 1.00 54.61  ? 430 THR B O   1 
ATOM   6947  C  CB  . THR B 1 455 ? 108.805 131.283 138.851 1.00 45.57  ? 430 THR B CB  1 
ATOM   6948  O  OG1 . THR B 1 455 ? 110.192 131.509 139.120 1.00 53.34  ? 430 THR B OG1 1 
ATOM   6949  C  CG2 . THR B 1 455 ? 108.208 130.575 140.018 1.00 47.43  ? 430 THR B CG2 1 
ATOM   6950  N  N   . ILE B 1 456 ? 109.040 128.083 138.165 1.00 45.86  ? 431 ILE B N   1 
ATOM   6951  C  CA  . ILE B 1 456 ? 109.862 126.872 138.118 1.00 36.93  ? 431 ILE B CA  1 
ATOM   6952  C  C   . ILE B 1 456 ? 109.809 126.188 136.763 1.00 32.06  ? 431 ILE B C   1 
ATOM   6953  O  O   . ILE B 1 456 ? 110.600 125.272 136.517 1.00 40.93  ? 431 ILE B O   1 
ATOM   6954  C  CB  . ILE B 1 456 ? 109.510 125.830 139.197 1.00 33.29  ? 431 ILE B CB  1 
ATOM   6955  C  CG1 . ILE B 1 456 ? 108.372 124.930 138.747 1.00 36.15  ? 431 ILE B CG1 1 
ATOM   6956  C  CG2 . ILE B 1 456 ? 109.160 126.497 140.503 1.00 46.14  ? 431 ILE B CG2 1 
ATOM   6957  C  CD1 . ILE B 1 456 ? 108.259 123.694 139.581 1.00 47.02  ? 431 ILE B CD1 1 
ATOM   6958  N  N   . LYS B 1 457 ? 108.894 126.594 135.881 1.00 43.93  ? 432 LYS B N   1 
ATOM   6959  C  CA  . LYS B 1 457 ? 109.013 126.226 134.476 1.00 48.18  ? 432 LYS B CA  1 
ATOM   6960  C  C   . LYS B 1 457 ? 110.092 127.046 133.789 1.00 48.65  ? 432 LYS B C   1 
ATOM   6961  O  O   . LYS B 1 457 ? 110.888 126.511 133.012 1.00 50.77  ? 432 LYS B O   1 
ATOM   6962  C  CB  . LYS B 1 457 ? 107.681 126.427 133.759 1.00 54.53  ? 432 LYS B CB  1 
ATOM   6963  C  CG  . LYS B 1 457 ? 106.810 125.201 133.647 1.00 55.44  ? 432 LYS B CG  1 
ATOM   6964  C  CD  . LYS B 1 457 ? 105.619 125.493 132.754 1.00 52.05  ? 432 LYS B CD  1 
ATOM   6965  C  CE  . LYS B 1 457 ? 104.385 124.764 133.228 1.00 59.01  ? 432 LYS B CE  1 
ATOM   6966  N  NZ  . LYS B 1 457 ? 103.157 125.285 132.576 1.00 59.50  ? 432 LYS B NZ  1 
ATOM   6967  N  N   . PHE B 1 458 ? 110.124 128.353 134.054 1.00 41.93  ? 433 PHE B N   1 
ATOM   6968  C  CA  . PHE B 1 458 ? 111.095 129.219 133.396 1.00 39.78  ? 433 PHE B CA  1 
ATOM   6969  C  C   . PHE B 1 458 ? 112.511 128.924 133.866 1.00 46.66  ? 433 PHE B C   1 
ATOM   6970  O  O   . PHE B 1 458 ? 113.454 128.966 133.069 1.00 58.79  ? 433 PHE B O   1 
ATOM   6971  C  CB  . PHE B 1 458 ? 110.754 130.687 133.643 1.00 35.60  ? 433 PHE B CB  1 
ATOM   6972  C  CG  . PHE B 1 458 ? 111.931 131.608 133.513 1.00 33.69  ? 433 PHE B CG  1 
ATOM   6973  C  CD1 . PHE B 1 458 ? 112.367 132.015 132.275 1.00 40.10  ? 433 PHE B CD1 1 
ATOM   6974  C  CD2 . PHE B 1 458 ? 112.605 132.059 134.629 1.00 48.17  ? 433 PHE B CD2 1 
ATOM   6975  C  CE1 . PHE B 1 458 ? 113.447 132.852 132.150 1.00 43.86  ? 433 PHE B CE1 1 
ATOM   6976  C  CE2 . PHE B 1 458 ? 113.689 132.895 134.507 1.00 45.19  ? 433 PHE B CE2 1 
ATOM   6977  C  CZ  . PHE B 1 458 ? 114.108 133.292 133.265 1.00 39.92  ? 433 PHE B CZ  1 
ATOM   6978  N  N   . MET B 1 459 ? 112.688 128.651 135.158 1.00 46.76  ? 434 MET B N   1 
ATOM   6979  C  CA  . MET B 1 459 ? 114.035 128.454 135.677 1.00 38.81  ? 434 MET B CA  1 
ATOM   6980  C  C   . MET B 1 459 ? 114.679 127.200 135.100 1.00 45.43  ? 434 MET B C   1 
ATOM   6981  O  O   . MET B 1 459 ? 115.869 127.207 134.769 1.00 47.96  ? 434 MET B O   1 
ATOM   6982  C  CB  . MET B 1 459 ? 114.005 128.396 137.201 1.00 35.29  ? 434 MET B CB  1 
ATOM   6983  C  CG  . MET B 1 459 ? 115.331 128.723 137.851 1.00 43.10  ? 434 MET B CG  1 
ATOM   6984  S  SD  . MET B 1 459 ? 115.743 130.473 137.771 1.00 71.55  ? 434 MET B SD  1 
ATOM   6985  C  CE  . MET B 1 459 ? 114.137 131.215 138.045 1.00 47.15  ? 434 MET B CE  1 
ATOM   6986  N  N   . TYR B 1 460 ? 113.918 126.119 134.973 1.00 47.73  ? 435 TYR B N   1 
ATOM   6987  C  CA  . TYR B 1 460 ? 114.457 124.843 134.500 1.00 47.41  ? 435 TYR B CA  1 
ATOM   6988  C  C   . TYR B 1 460 ? 114.151 124.628 133.020 1.00 49.55  ? 435 TYR B C   1 
ATOM   6989  O  O   . TYR B 1 460 ? 113.438 123.704 132.634 1.00 47.24  ? 435 TYR B O   1 
ATOM   6990  C  CB  . TYR B 1 460 ? 113.913 123.698 135.345 1.00 38.46  ? 435 TYR B CB  1 
ATOM   6991  C  CG  . TYR B 1 460 ? 114.501 123.657 136.728 1.00 36.44  ? 435 TYR B CG  1 
ATOM   6992  C  CD1 . TYR B 1 460 ? 115.710 123.032 136.968 1.00 43.85  ? 435 TYR B CD1 1 
ATOM   6993  C  CD2 . TYR B 1 460 ? 113.850 124.252 137.791 1.00 43.06  ? 435 TYR B CD2 1 
ATOM   6994  C  CE1 . TYR B 1 460 ? 116.251 122.999 138.227 1.00 41.27  ? 435 TYR B CE1 1 
ATOM   6995  C  CE2 . TYR B 1 460 ? 114.384 124.223 139.053 1.00 47.87  ? 435 TYR B CE2 1 
ATOM   6996  C  CZ  . TYR B 1 460 ? 115.584 123.597 139.265 1.00 47.40  ? 435 TYR B CZ  1 
ATOM   6997  O  OH  . TYR B 1 460 ? 116.115 123.567 140.530 1.00 52.46  ? 435 TYR B OH  1 
ATOM   6998  N  N   . THR B 1 461 ? 114.712 125.497 132.183 1.00 53.15  ? 436 THR B N   1 
ATOM   6999  C  CA  . THR B 1 461 ? 114.699 125.284 130.741 1.00 55.38  ? 436 THR B CA  1 
ATOM   7000  C  C   . THR B 1 461 ? 115.814 126.109 130.121 1.00 57.44  ? 436 THR B C   1 
ATOM   7001  O  O   . THR B 1 461 ? 115.939 127.300 130.414 1.00 63.67  ? 436 THR B O   1 
ATOM   7002  C  CB  . THR B 1 461 ? 113.348 125.656 130.119 1.00 51.79  ? 436 THR B CB  1 
ATOM   7003  O  OG1 . THR B 1 461 ? 113.486 125.737 128.697 1.00 56.41  ? 436 THR B OG1 1 
ATOM   7004  C  CG2 . THR B 1 461 ? 112.861 126.983 130.640 1.00 49.23  ? 436 THR B CG2 1 
ATOM   7005  N  N   . ASP B 1 462 ? 116.626 125.475 129.278 1.00 70.65  ? 437 ASP B N   1 
ATOM   7006  C  CA  . ASP B 1 462 ? 117.722 126.169 128.613 1.00 75.62  ? 437 ASP B CA  1 
ATOM   7007  C  C   . ASP B 1 462 ? 117.151 126.977 127.457 1.00 81.19  ? 437 ASP B C   1 
ATOM   7008  O  O   . ASP B 1 462 ? 116.736 126.411 126.442 1.00 86.44  ? 437 ASP B O   1 
ATOM   7009  C  CB  . ASP B 1 462 ? 118.770 125.176 128.123 1.00 72.29  ? 437 ASP B CB  1 
ATOM   7010  C  CG  . ASP B 1 462 ? 120.087 125.843 127.782 1.00 77.74  ? 437 ASP B CG  1 
ATOM   7011  O  OD1 . ASP B 1 462 ? 120.114 127.085 127.659 1.00 75.79  ? 437 ASP B OD1 1 
ATOM   7012  O  OD2 . ASP B 1 462 ? 121.097 125.125 127.635 1.00 83.15  ? 437 ASP B OD2 1 
ATOM   7013  N  N   . TRP B 1 463 ? 117.132 128.303 127.605 1.00 65.77  ? 438 TRP B N   1 
ATOM   7014  C  CA  . TRP B 1 463 ? 116.492 129.144 126.600 1.00 57.75  ? 438 TRP B CA  1 
ATOM   7015  C  C   . TRP B 1 463 ? 117.336 129.282 125.343 1.00 61.85  ? 438 TRP B C   1 
ATOM   7016  O  O   . TRP B 1 463 ? 116.791 129.521 124.260 1.00 69.72  ? 438 TRP B O   1 
ATOM   7017  C  CB  . TRP B 1 463 ? 116.187 130.516 127.187 1.00 61.07  ? 438 TRP B CB  1 
ATOM   7018  C  CG  . TRP B 1 463 ? 115.128 130.467 128.223 1.00 62.65  ? 438 TRP B CG  1 
ATOM   7019  C  CD1 . TRP B 1 463 ? 115.307 130.469 129.568 1.00 60.58  ? 438 TRP B CD1 1 
ATOM   7020  C  CD2 . TRP B 1 463 ? 113.716 130.402 128.003 1.00 64.56  ? 438 TRP B CD2 1 
ATOM   7021  N  NE1 . TRP B 1 463 ? 114.094 130.412 130.204 1.00 66.43  ? 438 TRP B NE1 1 
ATOM   7022  C  CE2 . TRP B 1 463 ? 113.101 130.372 129.263 1.00 64.01  ? 438 TRP B CE2 1 
ATOM   7023  C  CE3 . TRP B 1 463 ? 112.914 130.370 126.862 1.00 65.96  ? 438 TRP B CE3 1 
ATOM   7024  C  CZ2 . TRP B 1 463 ? 111.721 130.309 129.416 1.00 61.54  ? 438 TRP B CZ2 1 
ATOM   7025  C  CZ3 . TRP B 1 463 ? 111.544 130.309 127.017 1.00 63.22  ? 438 TRP B CZ3 1 
ATOM   7026  C  CH2 . TRP B 1 463 ? 110.962 130.279 128.284 1.00 58.96  ? 438 TRP B CH2 1 
ATOM   7027  N  N   . ALA B 1 464 ? 118.655 129.142 125.458 1.00 66.51  ? 439 ALA B N   1 
ATOM   7028  C  CA  . ALA B 1 464 ? 119.505 129.251 124.281 1.00 69.48  ? 439 ALA B CA  1 
ATOM   7029  C  C   . ALA B 1 464 ? 119.272 128.118 123.293 1.00 74.95  ? 439 ALA B C   1 
ATOM   7030  O  O   . ALA B 1 464 ? 119.558 128.282 122.104 1.00 73.06  ? 439 ALA B O   1 
ATOM   7031  C  CB  . ALA B 1 464 ? 120.975 129.280 124.694 1.00 69.78  ? 439 ALA B CB  1 
ATOM   7032  N  N   . ASP B 1 465 ? 118.769 126.976 123.756 1.00 86.84  ? 440 ASP B N   1 
ATOM   7033  C  CA  . ASP B 1 465 ? 118.573 125.807 122.914 1.00 81.57  ? 440 ASP B CA  1 
ATOM   7034  C  C   . ASP B 1 465 ? 117.172 125.309 123.301 1.00 76.16  ? 440 ASP B C   1 
ATOM   7035  O  O   . ASP B 1 465 ? 116.962 124.204 123.786 1.00 78.63  ? 440 ASP B O   1 
ATOM   7036  C  CB  . ASP B 1 465 ? 119.721 124.812 123.126 1.00 80.58  ? 440 ASP B CB  1 
ATOM   7037  C  CG  . ASP B 1 465 ? 119.445 123.408 122.583 1.00 88.62  ? 440 ASP B CG  1 
ATOM   7038  O  OD1 . ASP B 1 465 ? 118.351 123.128 122.062 1.00 88.37  ? 440 ASP B OD1 1 
ATOM   7039  O  OD2 . ASP B 1 465 ? 120.352 122.555 122.690 1.00 94.03  ? 440 ASP B OD2 1 
ATOM   7040  N  N   . ARG B 1 466 ? 116.191 126.210 123.205 1.00 68.94  ? 441 ARG B N   1 
ATOM   7041  C  CA  . ARG B 1 466 ? 114.897 125.994 123.850 1.00 71.27  ? 441 ARG B CA  1 
ATOM   7042  C  C   . ARG B 1 466 ? 114.184 124.752 123.327 1.00 74.47  ? 441 ARG B C   1 
ATOM   7043  O  O   . ARG B 1 466 ? 113.595 123.996 124.107 1.00 75.82  ? 441 ARG B O   1 
ATOM   7044  C  CB  . ARG B 1 466 ? 114.016 127.227 123.665 1.00 72.64  ? 441 ARG B CB  1 
ATOM   7045  C  CG  . ARG B 1 466 ? 112.563 127.025 124.036 1.00 70.54  ? 441 ARG B CG  1 
ATOM   7046  C  CD  . ARG B 1 466 ? 111.813 128.349 124.029 1.00 74.51  ? 441 ARG B CD  1 
ATOM   7047  N  NE  . ARG B 1 466 ? 111.957 129.070 122.769 1.00 77.62  ? 441 ARG B NE  1 
ATOM   7048  C  CZ  . ARG B 1 466 ? 112.696 130.160 122.598 1.00 80.90  ? 441 ARG B CZ  1 
ATOM   7049  N  NH1 . ARG B 1 466 ? 113.381 130.696 123.594 1.00 78.77  ? 441 ARG B NH1 1 
ATOM   7050  N  NH2 . ARG B 1 466 ? 112.748 130.726 121.396 1.00 82.40  ? 441 ARG B NH2 1 
ATOM   7051  N  N   . ASP B 1 467 ? 114.218 124.521 122.017 1.00 86.13  ? 442 ASP B N   1 
ATOM   7052  C  CA  . ASP B 1 467 ? 113.385 123.500 121.383 1.00 83.79  ? 442 ASP B CA  1 
ATOM   7053  C  C   . ASP B 1 467 ? 114.137 122.199 121.132 1.00 86.55  ? 442 ASP B C   1 
ATOM   7054  O  O   . ASP B 1 467 ? 113.917 121.541 120.111 1.00 86.50  ? 442 ASP B O   1 
ATOM   7055  C  CB  . ASP B 1 467 ? 112.801 124.036 120.081 1.00 79.74  ? 442 ASP B CB  1 
ATOM   7056  N  N   . ASN B 1 468 ? 115.031 121.801 122.041 1.00 88.07  ? 443 ASN B N   1 
ATOM   7057  C  CA  . ASN B 1 468 ? 115.810 120.584 121.824 1.00 86.28  ? 443 ASN B CA  1 
ATOM   7058  C  C   . ASN B 1 468 ? 114.943 119.337 121.911 1.00 91.81  ? 443 ASN B C   1 
ATOM   7059  O  O   . ASN B 1 468 ? 115.065 118.431 121.079 1.00 97.13  ? 443 ASN B O   1 
ATOM   7060  C  CB  . ASN B 1 468 ? 116.949 120.494 122.833 1.00 82.74  ? 443 ASN B CB  1 
ATOM   7061  C  CG  . ASN B 1 468 ? 118.050 119.561 122.380 1.00 89.57  ? 443 ASN B CG  1 
ATOM   7062  O  OD1 . ASN B 1 468 ? 117.798 118.407 122.038 1.00 92.45  ? 443 ASN B OD1 1 
ATOM   7063  N  ND2 . ASN B 1 468 ? 119.280 120.056 122.377 1.00 89.41  ? 443 ASN B ND2 1 
ATOM   7064  N  N   . GLY B 1 469 ? 114.068 119.266 122.907 1.00 86.72  ? 444 GLY B N   1 
ATOM   7065  C  CA  . GLY B 1 469 ? 113.327 118.047 123.153 1.00 85.24  ? 444 GLY B CA  1 
ATOM   7066  C  C   . GLY B 1 469 ? 114.095 117.111 124.059 1.00 86.37  ? 444 GLY B C   1 
ATOM   7067  O  O   . GLY B 1 469 ? 113.598 116.712 125.115 1.00 89.67  ? 444 GLY B O   1 
ATOM   7068  N  N   . GLU B 1 470 ? 115.319 116.758 123.661 1.00 85.39  ? 445 GLU B N   1 
ATOM   7069  C  CA  . GLU B 1 470 ? 116.154 115.918 124.512 1.00 84.31  ? 445 GLU B CA  1 
ATOM   7070  C  C   . GLU B 1 470 ? 116.699 116.693 125.704 1.00 89.85  ? 445 GLU B C   1 
ATOM   7071  O  O   . GLU B 1 470 ? 116.875 116.118 126.783 1.00 91.53  ? 445 GLU B O   1 
ATOM   7072  C  CB  . GLU B 1 470 ? 117.297 115.313 123.699 1.00 82.66  ? 445 GLU B CB  1 
ATOM   7073  C  CG  . GLU B 1 470 ? 117.894 114.061 124.315 1.00 86.86  ? 445 GLU B CG  1 
ATOM   7074  C  CD  . GLU B 1 470 ? 118.936 114.371 125.370 1.00 93.34  ? 445 GLU B CD  1 
ATOM   7075  O  OE1 . GLU B 1 470 ? 119.443 115.512 125.388 1.00 90.16  ? 445 GLU B OE1 1 
ATOM   7076  O  OE2 . GLU B 1 470 ? 119.246 113.478 126.185 1.00 94.26  ? 445 GLU B OE2 1 
ATOM   7077  N  N   . MET B 1 471 ? 116.974 117.986 125.543 1.00 90.76  ? 446 MET B N   1 
ATOM   7078  C  CA  . MET B 1 471 ? 117.390 118.787 126.687 1.00 85.89  ? 446 MET B CA  1 
ATOM   7079  C  C   . MET B 1 471 ? 116.124 119.274 127.385 1.00 84.65  ? 446 MET B C   1 
ATOM   7080  O  O   . MET B 1 471 ? 115.927 120.469 127.620 1.00 88.62  ? 446 MET B O   1 
ATOM   7081  C  CB  . MET B 1 471 ? 118.310 119.933 126.243 1.00 86.16  ? 446 MET B CB  1 
ATOM   7082  C  CG  . MET B 1 471 ? 118.741 120.912 127.332 1.00 86.98  ? 446 MET B CG  1 
ATOM   7083  S  SD  . MET B 1 471 ? 120.303 121.733 126.977 1.00 97.58  ? 446 MET B SD  1 
ATOM   7084  C  CE  . MET B 1 471 ? 121.183 120.432 126.120 1.00 89.10  ? 446 MET B CE  1 
ATOM   7085  N  N   . ARG B 1 472 ? 115.226 118.336 127.667 1.00 69.32  ? 447 ARG B N   1 
ATOM   7086  C  CA  . ARG B 1 472 ? 114.102 118.573 128.557 1.00 68.52  ? 447 ARG B CA  1 
ATOM   7087  C  C   . ARG B 1 472 ? 114.067 117.432 129.561 1.00 78.09  ? 447 ARG B C   1 
ATOM   7088  O  O   . ARG B 1 472 ? 113.705 117.625 130.724 1.00 81.63  ? 447 ARG B O   1 
ATOM   7089  C  CB  . ARG B 1 472 ? 112.794 118.675 127.777 1.00 67.12  ? 447 ARG B CB  1 
ATOM   7090  C  CG  . ARG B 1 472 ? 112.139 120.038 127.860 1.00 69.49  ? 447 ARG B CG  1 
ATOM   7091  C  CD  . ARG B 1 472 ? 111.086 120.211 126.782 1.00 74.59  ? 447 ARG B CD  1 
ATOM   7092  N  NE  . ARG B 1 472 ? 111.672 120.588 125.503 1.00 76.32  ? 447 ARG B NE  1 
ATOM   7093  C  CZ  . ARG B 1 472 ? 111.013 120.607 124.354 1.00 71.53  ? 447 ARG B CZ  1 
ATOM   7094  N  NH1 . ARG B 1 472 ? 109.742 120.256 124.281 1.00 66.79  ? 447 ARG B NH1 1 
ATOM   7095  N  NH2 . ARG B 1 472 ? 111.646 120.988 123.249 1.00 74.41  ? 447 ARG B NH2 1 
ATOM   7096  N  N   . ARG B 1 473 ? 114.486 116.244 129.121 1.00 77.65  ? 448 ARG B N   1 
ATOM   7097  C  CA  . ARG B 1 473 ? 114.698 115.144 130.054 1.00 71.66  ? 448 ARG B CA  1 
ATOM   7098  C  C   . ARG B 1 473 ? 115.792 115.485 131.051 1.00 75.27  ? 448 ARG B C   1 
ATOM   7099  O  O   . ARG B 1 473 ? 115.651 115.230 132.254 1.00 83.63  ? 448 ARG B O   1 
ATOM   7100  C  CB  . ARG B 1 473 ? 115.059 113.874 129.292 1.00 67.74  ? 448 ARG B CB  1 
ATOM   7101  C  CG  . ARG B 1 473 ? 113.875 113.054 128.849 1.00 75.27  ? 448 ARG B CG  1 
ATOM   7102  C  CD  . ARG B 1 473 ? 114.242 111.589 128.815 1.00 77.72  ? 448 ARG B CD  1 
ATOM   7103  N  NE  . ARG B 1 473 ? 115.616 111.401 128.369 1.00 78.19  ? 448 ARG B NE  1 
ATOM   7104  C  CZ  . ARG B 1 473 ? 115.970 111.186 127.111 1.00 80.98  ? 448 ARG B CZ  1 
ATOM   7105  N  NH1 . ARG B 1 473 ? 115.071 111.111 126.144 1.00 82.68  ? 448 ARG B NH1 1 
ATOM   7106  N  NH2 . ARG B 1 473 ? 117.258 111.041 126.816 1.00 74.57  ? 448 ARG B NH2 1 
ATOM   7107  N  N   . LYS B 1 474 ? 116.891 116.067 130.569 1.00 67.76  ? 449 LYS B N   1 
ATOM   7108  C  CA  . LYS B 1 474 ? 117.976 116.448 131.462 1.00 65.86  ? 449 LYS B CA  1 
ATOM   7109  C  C   . LYS B 1 474 ? 117.506 117.472 132.482 1.00 70.68  ? 449 LYS B C   1 
ATOM   7110  O  O   . LYS B 1 474 ? 117.834 117.369 133.668 1.00 75.70  ? 449 LYS B O   1 
ATOM   7111  C  CB  . LYS B 1 474 ? 119.150 116.997 130.658 1.00 69.76  ? 449 LYS B CB  1 
ATOM   7112  C  CG  . LYS B 1 474 ? 119.722 116.018 129.657 1.00 71.93  ? 449 LYS B CG  1 
ATOM   7113  C  CD  . LYS B 1 474 ? 120.677 115.048 130.315 1.00 71.73  ? 449 LYS B CD  1 
ATOM   7114  C  CE  . LYS B 1 474 ? 121.230 114.064 129.300 1.00 76.78  ? 449 LYS B CE  1 
ATOM   7115  N  NZ  . LYS B 1 474 ? 121.633 114.742 128.040 1.00 74.42  ? 449 LYS B NZ  1 
ATOM   7116  N  N   . THR B 1 475 ? 116.717 118.455 132.049 1.00 55.48  ? 450 THR B N   1 
ATOM   7117  C  CA  . THR B 1 475 ? 116.272 119.487 132.978 1.00 50.61  ? 450 THR B CA  1 
ATOM   7118  C  C   . THR B 1 475 ? 115.216 118.961 133.944 1.00 57.42  ? 450 THR B C   1 
ATOM   7119  O  O   . THR B 1 475 ? 115.172 119.389 135.097 1.00 60.08  ? 450 THR B O   1 
ATOM   7120  C  CB  . THR B 1 475 ? 115.750 120.700 132.216 1.00 54.91  ? 450 THR B CB  1 
ATOM   7121  O  OG1 . THR B 1 475 ? 114.636 120.313 131.406 1.00 69.44  ? 450 THR B OG1 1 
ATOM   7122  C  CG2 . THR B 1 475 ? 116.843 121.267 131.335 1.00 61.33  ? 450 THR B CG2 1 
ATOM   7123  N  N   . LEU B 1 476 ? 114.365 118.029 133.510 1.00 58.75  ? 451 LEU B N   1 
ATOM   7124  C  CA  . LEU B 1 476 ? 113.419 117.415 134.440 1.00 54.33  ? 451 LEU B CA  1 
ATOM   7125  C  C   . LEU B 1 476 ? 114.145 116.600 135.504 1.00 54.15  ? 451 LEU B C   1 
ATOM   7126  O  O   . LEU B 1 476 ? 113.831 116.690 136.701 1.00 64.77  ? 451 LEU B O   1 
ATOM   7127  C  CB  . LEU B 1 476 ? 112.435 116.532 133.676 1.00 54.13  ? 451 LEU B CB  1 
ATOM   7128  C  CG  . LEU B 1 476 ? 111.142 117.175 133.188 1.00 52.66  ? 451 LEU B CG  1 
ATOM   7129  C  CD1 . LEU B 1 476 ? 110.206 116.111 132.661 1.00 54.75  ? 451 LEU B CD1 1 
ATOM   7130  C  CD2 . LEU B 1 476 ? 110.490 117.953 134.311 1.00 53.97  ? 451 LEU B CD2 1 
ATOM   7131  N  N   . LEU B 1 477 ? 115.118 115.791 135.082 1.00 48.54  ? 452 LEU B N   1 
ATOM   7132  C  CA  . LEU B 1 477 ? 115.905 115.022 136.036 1.00 44.78  ? 452 LEU B CA  1 
ATOM   7133  C  C   . LEU B 1 477 ? 116.658 115.945 136.985 1.00 50.33  ? 452 LEU B C   1 
ATOM   7134  O  O   . LEU B 1 477 ? 116.728 115.686 138.194 1.00 49.93  ? 452 LEU B O   1 
ATOM   7135  C  CB  . LEU B 1 477 ? 116.862 114.099 135.284 1.00 41.02  ? 452 LEU B CB  1 
ATOM   7136  C  CG  . LEU B 1 477 ? 118.178 113.714 135.950 1.00 53.31  ? 452 LEU B CG  1 
ATOM   7137  C  CD1 . LEU B 1 477 ? 117.932 112.775 137.103 1.00 51.87  ? 452 LEU B CD1 1 
ATOM   7138  C  CD2 . LEU B 1 477 ? 119.108 113.073 134.941 1.00 59.73  ? 452 LEU B CD2 1 
ATOM   7139  N  N   . ALA B 1 478 ? 117.207 117.041 136.461 1.00 51.30  ? 453 ALA B N   1 
ATOM   7140  C  CA  . ALA B 1 478 ? 117.898 118.001 137.309 1.00 47.86  ? 453 ALA B CA  1 
ATOM   7141  C  C   . ALA B 1 478 ? 116.936 118.689 138.266 1.00 43.99  ? 453 ALA B C   1 
ATOM   7142  O  O   . ALA B 1 478 ? 117.305 118.997 139.398 1.00 57.82  ? 453 ALA B O   1 
ATOM   7143  C  CB  . ALA B 1 478 ? 118.629 119.029 136.451 1.00 48.19  ? 453 ALA B CB  1 
ATOM   7144  N  N   . LEU B 1 479 ? 115.699 118.937 137.834 1.00 33.11  ? 454 LEU B N   1 
ATOM   7145  C  CA  . LEU B 1 479 ? 114.718 119.564 138.714 1.00 40.59  ? 454 LEU B CA  1 
ATOM   7146  C  C   . LEU B 1 479 ? 114.387 118.658 139.889 1.00 37.21  ? 454 LEU B C   1 
ATOM   7147  O  O   . LEU B 1 479 ? 114.361 119.101 141.044 1.00 44.06  ? 454 LEU B O   1 
ATOM   7148  C  CB  . LEU B 1 479 ? 113.457 119.911 137.922 1.00 45.09  ? 454 LEU B CB  1 
ATOM   7149  C  CG  . LEU B 1 479 ? 112.099 119.943 138.622 1.00 34.67  ? 454 LEU B CG  1 
ATOM   7150  C  CD1 . LEU B 1 479 ? 112.050 121.010 139.685 1.00 41.01  ? 454 LEU B CD1 1 
ATOM   7151  C  CD2 . LEU B 1 479 ? 111.001 120.172 137.605 1.00 40.41  ? 454 LEU B CD2 1 
ATOM   7152  N  N   . PHE B 1 480 ? 114.139 117.379 139.614 1.00 37.41  ? 455 PHE B N   1 
ATOM   7153  C  CA  . PHE B 1 480 ? 113.854 116.459 140.711 1.00 26.78  ? 455 PHE B CA  1 
ATOM   7154  C  C   . PHE B 1 480 ? 115.055 116.312 141.637 1.00 36.28  ? 455 PHE B C   1 
ATOM   7155  O  O   . PHE B 1 480 ? 114.910 116.359 142.867 1.00 44.69  ? 455 PHE B O   1 
ATOM   7156  C  CB  . PHE B 1 480 ? 113.429 115.099 140.178 1.00 27.85  ? 455 PHE B CB  1 
ATOM   7157  C  CG  . PHE B 1 480 ? 112.653 114.292 141.167 1.00 32.87  ? 455 PHE B CG  1 
ATOM   7158  C  CD1 . PHE B 1 480 ? 111.586 114.848 141.841 1.00 34.84  ? 455 PHE B CD1 1 
ATOM   7159  C  CD2 . PHE B 1 480 ? 112.998 112.984 141.437 1.00 35.80  ? 455 PHE B CD2 1 
ATOM   7160  C  CE1 . PHE B 1 480 ? 110.871 114.110 142.754 1.00 41.92  ? 455 PHE B CE1 1 
ATOM   7161  C  CE2 . PHE B 1 480 ? 112.286 112.245 142.349 1.00 37.52  ? 455 PHE B CE2 1 
ATOM   7162  C  CZ  . PHE B 1 480 ? 111.221 112.809 143.009 1.00 35.37  ? 455 PHE B CZ  1 
ATOM   7163  N  N   . THR B 1 481 ? 116.253 116.152 141.068 1.00 35.20  ? 456 THR B N   1 
ATOM   7164  C  CA  . THR B 1 481 ? 117.447 116.019 141.894 1.00 25.48  ? 456 THR B CA  1 
ATOM   7165  C  C   . THR B 1 481 ? 117.660 117.253 142.756 1.00 31.11  ? 456 THR B C   1 
ATOM   7166  O  O   . THR B 1 481 ? 117.978 117.142 143.944 1.00 43.57  ? 456 THR B O   1 
ATOM   7167  C  CB  . THR B 1 481 ? 118.667 115.776 141.012 1.00 29.09  ? 456 THR B CB  1 
ATOM   7168  O  OG1 . THR B 1 481 ? 118.646 114.430 140.534 1.00 36.45  ? 456 THR B OG1 1 
ATOM   7169  C  CG2 . THR B 1 481 ? 119.941 116.008 141.791 1.00 29.64  ? 456 THR B CG2 1 
ATOM   7170  N  N   . ASP B 1 482 ? 117.479 118.440 142.178 1.00 31.60  ? 457 ASP B N   1 
ATOM   7171  C  CA  . ASP B 1 482 ? 117.704 119.671 142.918 1.00 24.41  ? 457 ASP B CA  1 
ATOM   7172  C  C   . ASP B 1 482 ? 116.690 119.842 144.033 1.00 31.63  ? 457 ASP B C   1 
ATOM   7173  O  O   . ASP B 1 482 ? 117.048 120.270 145.133 1.00 50.20  ? 457 ASP B O   1 
ATOM   7174  C  CB  . ASP B 1 482 ? 117.663 120.866 141.973 1.00 23.80  ? 457 ASP B CB  1 
ATOM   7175  C  CG  . ASP B 1 482 ? 118.917 120.990 141.149 1.00 42.93  ? 457 ASP B CG  1 
ATOM   7176  O  OD1 . ASP B 1 482 ? 120.011 120.773 141.701 1.00 56.82  ? 457 ASP B OD1 1 
ATOM   7177  O  OD2 . ASP B 1 482 ? 118.815 121.302 139.948 1.00 44.18  ? 457 ASP B OD2 1 
ATOM   7178  N  N   . HIS B 1 483 ? 115.419 119.527 143.784 1.00 22.77  ? 458 HIS B N   1 
ATOM   7179  C  CA  . HIS B 1 483 ? 114.442 119.740 144.845 1.00 27.09  ? 458 HIS B CA  1 
ATOM   7180  C  C   . HIS B 1 483 ? 114.614 118.733 145.968 1.00 39.61  ? 458 HIS B C   1 
ATOM   7181  O  O   . HIS B 1 483 ? 114.611 119.103 147.146 1.00 52.25  ? 458 HIS B O   1 
ATOM   7182  C  CB  . HIS B 1 483 ? 113.016 119.678 144.322 1.00 34.93  ? 458 HIS B CB  1 
ATOM   7183  C  CG  . HIS B 1 483 ? 112.003 120.046 145.359 1.00 31.49  ? 458 HIS B CG  1 
ATOM   7184  N  ND1 . HIS B 1 483 ? 110.670 119.720 145.257 1.00 40.58  ? 458 HIS B ND1 1 
ATOM   7185  C  CD2 . HIS B 1 483 ? 112.138 120.712 146.529 1.00 36.34  ? 458 HIS B CD2 1 
ATOM   7186  C  CE1 . HIS B 1 483 ? 110.026 120.173 146.316 1.00 42.00  ? 458 HIS B CE1 1 
ATOM   7187  N  NE2 . HIS B 1 483 ? 110.894 120.779 147.104 1.00 37.37  ? 458 HIS B NE2 1 
ATOM   7188  N  N   . GLN B 1 484 ? 114.758 117.454 145.632 1.00 40.48  ? 459 GLN B N   1 
ATOM   7189  C  CA  . GLN B 1 484 ? 114.652 116.437 146.669 1.00 24.54  ? 459 GLN B CA  1 
ATOM   7190  C  C   . GLN B 1 484 ? 115.974 116.105 147.342 1.00 34.50  ? 459 GLN B C   1 
ATOM   7191  O  O   . GLN B 1 484 ? 115.976 115.756 148.526 1.00 52.35  ? 459 GLN B O   1 
ATOM   7192  C  CB  . GLN B 1 484 ? 114.039 115.167 146.090 1.00 19.85  ? 459 GLN B CB  1 
ATOM   7193  C  CG  . GLN B 1 484 ? 112.631 115.366 145.590 1.00 29.09  ? 459 GLN B CG  1 
ATOM   7194  C  CD  . GLN B 1 484 ? 111.604 115.182 146.676 1.00 37.03  ? 459 GLN B CD  1 
ATOM   7195  O  OE1 . GLN B 1 484 ? 111.161 116.142 147.300 1.00 37.39  ? 459 GLN B OE1 1 
ATOM   7196  N  NE2 . GLN B 1 484 ? 111.218 113.941 146.911 1.00 51.73  ? 459 GLN B NE2 1 
ATOM   7197  N  N   . TRP B 1 485 ? 117.095 116.207 146.640 1.00 32.56  ? 460 TRP B N   1 
ATOM   7198  C  CA  . TRP B 1 485 ? 118.354 115.717 147.185 1.00 24.93  ? 460 TRP B CA  1 
ATOM   7199  C  C   . TRP B 1 485 ? 119.426 116.779 147.343 1.00 28.71  ? 460 TRP B C   1 
ATOM   7200  O  O   . TRP B 1 485 ? 120.196 116.716 148.299 1.00 43.64  ? 460 TRP B O   1 
ATOM   7201  C  CB  . TRP B 1 485 ? 118.901 114.591 146.309 1.00 18.99  ? 460 TRP B CB  1 
ATOM   7202  C  CG  . TRP B 1 485 ? 118.278 113.272 146.585 1.00 29.58  ? 460 TRP B CG  1 
ATOM   7203  C  CD1 . TRP B 1 485 ? 118.485 112.483 147.672 1.00 39.58  ? 460 TRP B CD1 1 
ATOM   7204  C  CD2 . TRP B 1 485 ? 117.347 112.577 145.754 1.00 27.44  ? 460 TRP B CD2 1 
ATOM   7205  N  NE1 . TRP B 1 485 ? 117.738 111.338 147.572 1.00 34.17  ? 460 TRP B NE1 1 
ATOM   7206  C  CE2 . TRP B 1 485 ? 117.030 111.374 146.400 1.00 34.12  ? 460 TRP B CE2 1 
ATOM   7207  C  CE3 . TRP B 1 485 ? 116.749 112.858 144.527 1.00 26.65  ? 460 TRP B CE3 1 
ATOM   7208  C  CZ2 . TRP B 1 485 ? 116.149 110.455 145.861 1.00 33.66  ? 460 TRP B CZ2 1 
ATOM   7209  C  CZ3 . TRP B 1 485 ? 115.875 111.948 143.997 1.00 23.27  ? 460 TRP B CZ3 1 
ATOM   7210  C  CH2 . TRP B 1 485 ? 115.579 110.763 144.661 1.00 33.98  ? 460 TRP B CH2 1 
ATOM   7211  N  N   . VAL B 1 486 ? 119.519 117.746 146.433 1.00 18.03  ? 461 VAL B N   1 
ATOM   7212  C  CA  . VAL B 1 486 ? 120.618 118.704 146.505 1.00 24.43  ? 461 VAL B CA  1 
ATOM   7213  C  C   . VAL B 1 486 ? 120.268 119.869 147.420 1.00 29.82  ? 461 VAL B C   1 
ATOM   7214  O  O   . VAL B 1 486 ? 121.069 120.262 148.274 1.00 47.99  ? 461 VAL B O   1 
ATOM   7215  C  CB  . VAL B 1 486 ? 121.012 119.187 145.100 1.00 21.97  ? 461 VAL B CB  1 
ATOM   7216  C  CG1 . VAL B 1 486 ? 121.868 120.430 145.197 1.00 10.73  ? 461 VAL B CG1 1 
ATOM   7217  C  CG2 . VAL B 1 486 ? 121.762 118.097 144.366 1.00 21.81  ? 461 VAL B CG2 1 
ATOM   7218  N  N   . ALA B 1 487 ? 119.084 120.453 147.254 1.00 24.81  ? 462 ALA B N   1 
ATOM   7219  C  CA  . ALA B 1 487 ? 118.707 121.580 148.105 1.00 25.46  ? 462 ALA B CA  1 
ATOM   7220  C  C   . ALA B 1 487 ? 118.621 121.204 149.579 1.00 35.09  ? 462 ALA B C   1 
ATOM   7221  O  O   . ALA B 1 487 ? 119.172 121.947 150.410 1.00 42.17  ? 462 ALA B O   1 
ATOM   7222  C  CB  . ALA B 1 487 ? 117.401 122.201 147.604 1.00 22.58  ? 462 ALA B CB  1 
ATOM   7223  N  N   . PRO B 1 488 ? 117.955 120.113 149.984 1.00 29.71  ? 463 PRO B N   1 
ATOM   7224  C  CA  . PRO B 1 488 ? 118.000 119.742 151.407 1.00 26.87  ? 463 PRO B CA  1 
ATOM   7225  C  C   . PRO B 1 488 ? 119.395 119.424 151.909 1.00 41.72  ? 463 PRO B C   1 
ATOM   7226  O  O   . PRO B 1 488 ? 119.719 119.750 153.056 1.00 46.50  ? 463 PRO B O   1 
ATOM   7227  C  CB  . PRO B 1 488 ? 117.081 118.518 151.472 1.00 28.89  ? 463 PRO B CB  1 
ATOM   7228  C  CG  . PRO B 1 488 ? 116.180 118.674 150.327 1.00 30.77  ? 463 PRO B CG  1 
ATOM   7229  C  CD  . PRO B 1 488 ? 117.040 119.230 149.246 1.00 28.72  ? 463 PRO B CD  1 
ATOM   7230  N  N   . ALA B 1 489 ? 120.235 118.791 151.088 1.00 45.92  ? 464 ALA B N   1 
ATOM   7231  C  CA  . ALA B 1 489 ? 121.591 118.484 151.529 1.00 31.52  ? 464 ALA B CA  1 
ATOM   7232  C  C   . ALA B 1 489 ? 122.389 119.755 151.774 1.00 38.07  ? 464 ALA B C   1 
ATOM   7233  O  O   . ALA B 1 489 ? 123.099 119.867 152.778 1.00 49.05  ? 464 ALA B O   1 
ATOM   7234  C  CB  . ALA B 1 489 ? 122.296 117.597 150.507 1.00 20.23  ? 464 ALA B CB  1 
ATOM   7235  N  N   . VAL B 1 490 ? 122.274 120.735 150.878 1.00 29.84  ? 465 VAL B N   1 
ATOM   7236  C  CA  . VAL B 1 490 ? 122.990 121.989 151.080 1.00 23.83  ? 465 VAL B CA  1 
ATOM   7237  C  C   . VAL B 1 490 ? 122.425 122.742 152.277 1.00 31.29  ? 465 VAL B C   1 
ATOM   7238  O  O   . VAL B 1 490 ? 123.172 123.357 153.045 1.00 45.49  ? 465 VAL B O   1 
ATOM   7239  C  CB  . VAL B 1 490 ? 122.959 122.840 149.801 1.00 15.33  ? 465 VAL B CB  1 
ATOM   7240  C  CG1 . VAL B 1 490 ? 123.631 124.163 150.045 1.00 29.71  ? 465 VAL B CG1 1 
ATOM   7241  C  CG2 . VAL B 1 490 ? 123.658 122.113 148.676 1.00 14.64  ? 465 VAL B CG2 1 
ATOM   7242  N  N   . ALA B 1 491 ? 121.105 122.696 152.470 1.00 33.64  ? 466 ALA B N   1 
ATOM   7243  C  CA  . ALA B 1 491 ? 120.506 123.382 153.611 1.00 32.23  ? 466 ALA B CA  1 
ATOM   7244  C  C   . ALA B 1 491 ? 120.981 122.782 154.928 1.00 36.02  ? 466 ALA B C   1 
ATOM   7245  O  O   . ALA B 1 491 ? 121.338 123.511 155.860 1.00 46.38  ? 466 ALA B O   1 
ATOM   7246  C  CB  . ALA B 1 491 ? 118.983 123.330 153.515 1.00 37.73  ? 466 ALA B CB  1 
ATOM   7247  N  N   . THR B 1 492 ? 121.007 121.450 155.023 1.00 36.77  ? 467 THR B N   1 
ATOM   7248  C  CA  . THR B 1 492 ? 121.458 120.826 156.263 1.00 33.20  ? 467 THR B CA  1 
ATOM   7249  C  C   . THR B 1 492 ? 122.962 120.982 156.456 1.00 35.27  ? 467 THR B C   1 
ATOM   7250  O  O   . THR B 1 492 ? 123.423 121.104 157.595 1.00 49.25  ? 467 THR B O   1 
ATOM   7251  C  CB  . THR B 1 492 ? 121.051 119.351 156.312 1.00 36.14  ? 467 THR B CB  1 
ATOM   7252  O  OG1 . THR B 1 492 ? 121.434 118.795 157.572 1.00 43.39  ? 467 THR B OG1 1 
ATOM   7253  C  CG2 . THR B 1 492 ? 121.711 118.557 155.221 1.00 40.18  ? 467 THR B CG2 1 
ATOM   7254  N  N   . ALA B 1 493 ? 123.739 121.019 155.372 1.00 30.44  ? 468 ALA B N   1 
ATOM   7255  C  CA  . ALA B 1 493 ? 125.164 121.287 155.510 1.00 34.68  ? 468 ALA B CA  1 
ATOM   7256  C  C   . ALA B 1 493 ? 125.413 122.697 156.030 1.00 40.15  ? 468 ALA B C   1 
ATOM   7257  O  O   . ALA B 1 493 ? 126.268 122.898 156.899 1.00 48.00  ? 468 ALA B O   1 
ATOM   7258  C  CB  . ALA B 1 493 ? 125.871 121.068 154.175 1.00 25.86  ? 468 ALA B CB  1 
ATOM   7259  N  N   . LYS B 1 494 ? 124.679 123.686 155.516 1.00 39.82  ? 469 LYS B N   1 
ATOM   7260  C  CA  . LYS B 1 494 ? 124.806 125.043 156.039 1.00 32.97  ? 469 LYS B CA  1 
ATOM   7261  C  C   . LYS B 1 494 ? 124.379 125.112 157.497 1.00 45.58  ? 469 LYS B C   1 
ATOM   7262  O  O   . LYS B 1 494 ? 125.034 125.771 158.311 1.00 56.09  ? 469 LYS B O   1 
ATOM   7263  C  CB  . LYS B 1 494 ? 123.975 126.017 155.209 1.00 34.74  ? 469 LYS B CB  1 
ATOM   7264  C  CG  . LYS B 1 494 ? 124.553 126.348 153.858 1.00 42.08  ? 469 LYS B CG  1 
ATOM   7265  C  CD  . LYS B 1 494 ? 123.885 127.576 153.271 1.00 46.01  ? 469 LYS B CD  1 
ATOM   7266  C  CE  . LYS B 1 494 ? 122.380 127.501 153.413 1.00 52.89  ? 469 LYS B CE  1 
ATOM   7267  N  NZ  . LYS B 1 494 ? 121.700 128.609 152.695 1.00 51.87  ? 469 LYS B NZ  1 
ATOM   7268  N  N   . LEU B 1 495 ? 123.277 124.445 157.845 1.00 44.48  ? 470 LEU B N   1 
ATOM   7269  C  CA  . LEU B 1 495 ? 122.782 124.503 159.216 1.00 39.25  ? 470 LEU B CA  1 
ATOM   7270  C  C   . LEU B 1 495 ? 123.764 123.866 160.189 1.00 49.90  ? 470 LEU B C   1 
ATOM   7271  O  O   . LEU B 1 495 ? 123.942 124.358 161.308 1.00 56.99  ? 470 LEU B O   1 
ATOM   7272  C  CB  . LEU B 1 495 ? 121.418 123.827 159.311 1.00 38.81  ? 470 LEU B CB  1 
ATOM   7273  C  CG  . LEU B 1 495 ? 120.201 124.747 159.266 1.00 50.18  ? 470 LEU B CG  1 
ATOM   7274  C  CD1 . LEU B 1 495 ? 120.376 125.837 158.225 1.00 50.28  ? 470 LEU B CD1 1 
ATOM   7275  C  CD2 . LEU B 1 495 ? 118.956 123.942 158.974 1.00 53.53  ? 470 LEU B CD2 1 
ATOM   7276  N  N   . HIS B 1 496 ? 124.403 122.765 159.791 1.00 52.01  ? 471 HIS B N   1 
ATOM   7277  C  CA  . HIS B 1 496 ? 125.393 122.144 160.664 1.00 45.29  ? 471 HIS B CA  1 
ATOM   7278  C  C   . HIS B 1 496 ? 126.671 122.969 160.733 1.00 51.21  ? 471 HIS B C   1 
ATOM   7279  O  O   . HIS B 1 496 ? 127.251 123.131 161.811 1.00 58.39  ? 471 HIS B O   1 
ATOM   7280  C  CB  . HIS B 1 496 ? 125.693 120.726 160.190 1.00 40.87  ? 471 HIS B CB  1 
ATOM   7281  C  CG  . HIS B 1 496 ? 124.754 119.703 160.738 1.00 44.21  ? 471 HIS B CG  1 
ATOM   7282  N  ND1 . HIS B 1 496 ? 123.423 119.653 160.386 1.00 55.55  ? 471 HIS B ND1 1 
ATOM   7283  C  CD2 . HIS B 1 496 ? 124.946 118.697 161.622 1.00 53.08  ? 471 HIS B CD2 1 
ATOM   7284  C  CE1 . HIS B 1 496 ? 122.838 118.657 161.025 1.00 57.90  ? 471 HIS B CE1 1 
ATOM   7285  N  NE2 . HIS B 1 496 ? 123.740 118.061 161.782 1.00 60.64  ? 471 HIS B NE2 1 
ATOM   7286  N  N   . ALA B 1 497 ? 127.127 123.501 159.597 1.00 47.96  ? 472 ALA B N   1 
ATOM   7287  C  CA  . ALA B 1 497 ? 128.361 124.275 159.590 1.00 46.17  ? 472 ALA B CA  1 
ATOM   7288  C  C   . ALA B 1 497 ? 128.205 125.630 160.263 1.00 56.54  ? 472 ALA B C   1 
ATOM   7289  O  O   . ALA B 1 497 ? 129.210 126.232 160.651 1.00 65.03  ? 472 ALA B O   1 
ATOM   7290  C  CB  . ALA B 1 497 ? 128.856 124.464 158.159 1.00 47.61  ? 472 ALA B CB  1 
ATOM   7291  N  N   . ASP B 1 498 ? 126.976 126.125 160.411 1.00 63.53  ? 473 ASP B N   1 
ATOM   7292  C  CA  . ASP B 1 498 ? 126.761 127.417 161.050 1.00 62.81  ? 473 ASP B CA  1 
ATOM   7293  C  C   . ASP B 1 498 ? 126.949 127.370 162.558 1.00 65.49  ? 473 ASP B C   1 
ATOM   7294  O  O   . ASP B 1 498 ? 127.041 128.431 163.182 1.00 69.96  ? 473 ASP B O   1 
ATOM   7295  C  CB  . ASP B 1 498 ? 125.362 127.939 160.731 1.00 59.32  ? 473 ASP B CB  1 
ATOM   7296  C  CG  . ASP B 1 498 ? 125.338 128.817 159.505 1.00 62.95  ? 473 ASP B CG  1 
ATOM   7297  O  OD1 . ASP B 1 498 ? 126.401 128.973 158.872 1.00 60.49  ? 473 ASP B OD1 1 
ATOM   7298  O  OD2 . ASP B 1 498 ? 124.260 129.352 159.173 1.00 67.36  ? 473 ASP B OD2 1 
ATOM   7299  N  N   . TYR B 1 499 ? 127.001 126.183 163.157 1.00 67.74  ? 474 TYR B N   1 
ATOM   7300  C  CA  . TYR B 1 499 ? 127.192 126.038 164.593 1.00 70.05  ? 474 TYR B CA  1 
ATOM   7301  C  C   . TYR B 1 499 ? 128.555 125.442 164.923 1.00 71.25  ? 474 TYR B C   1 
ATOM   7302  O  O   . TYR B 1 499 ? 128.724 124.794 165.957 1.00 73.42  ? 474 TYR B O   1 
ATOM   7303  C  CB  . TYR B 1 499 ? 126.074 125.196 165.201 1.00 68.86  ? 474 TYR B CB  1 
ATOM   7304  C  CG  . TYR B 1 499 ? 124.745 125.908 165.244 1.00 71.77  ? 474 TYR B CG  1 
ATOM   7305  C  CD1 . TYR B 1 499 ? 123.998 126.091 164.092 1.00 71.48  ? 474 TYR B CD1 1 
ATOM   7306  C  CD2 . TYR B 1 499 ? 124.241 126.405 166.434 1.00 73.39  ? 474 TYR B CD2 1 
ATOM   7307  C  CE1 . TYR B 1 499 ? 122.788 126.742 164.125 1.00 72.72  ? 474 TYR B CE1 1 
ATOM   7308  C  CE2 . TYR B 1 499 ? 123.031 127.059 166.475 1.00 73.80  ? 474 TYR B CE2 1 
ATOM   7309  C  CZ  . TYR B 1 499 ? 122.308 127.223 165.317 1.00 75.10  ? 474 TYR B CZ  1 
ATOM   7310  O  OH  . TYR B 1 499 ? 121.098 127.874 165.350 1.00 77.78  ? 474 TYR B OH  1 
ATOM   7311  N  N   . GLN B 1 500 ? 129.530 125.655 164.040 1.00 79.24  ? 475 GLN B N   1 
ATOM   7312  C  CA  . GLN B 1 500 ? 130.915 125.242 164.253 1.00 82.16  ? 475 GLN B CA  1 
ATOM   7313  C  C   . GLN B 1 500 ? 131.014 123.739 164.518 1.00 84.32  ? 475 GLN B C   1 
ATOM   7314  O  O   . GLN B 1 500 ? 131.440 123.291 165.583 1.00 91.96  ? 475 GLN B O   1 
ATOM   7315  C  CB  . GLN B 1 500 ? 131.557 126.050 165.385 1.00 85.23  ? 475 GLN B CB  1 
ATOM   7316  C  CG  . GLN B 1 500 ? 131.250 127.542 165.347 1.00 86.24  ? 475 GLN B CG  1 
ATOM   7317  C  CD  . GLN B 1 500 ? 131.900 128.251 164.173 1.00 89.80  ? 475 GLN B CD  1 
ATOM   7318  O  OE1 . GLN B 1 500 ? 132.837 127.739 163.561 1.00 94.08  ? 475 GLN B OE1 1 
ATOM   7319  N  NE2 . GLN B 1 500 ? 131.405 129.441 163.855 1.00 85.65  ? 475 GLN B NE2 1 
ATOM   7320  N  N   . SER B 1 501 ? 130.597 122.961 163.521 1.00 62.17  ? 476 SER B N   1 
ATOM   7321  C  CA  . SER B 1 501 ? 130.786 121.520 163.518 1.00 61.07  ? 476 SER B CA  1 
ATOM   7322  C  C   . SER B 1 501 ? 131.239 121.129 162.117 1.00 62.35  ? 476 SER B C   1 
ATOM   7323  O  O   . SER B 1 501 ? 130.579 121.500 161.133 1.00 67.74  ? 476 SER B O   1 
ATOM   7324  C  CB  . SER B 1 501 ? 129.506 120.773 163.902 1.00 54.91  ? 476 SER B CB  1 
ATOM   7325  O  OG  . SER B 1 501 ? 128.745 120.451 162.756 1.00 63.10  ? 476 SER B OG  1 
ATOM   7326  N  N   . PRO B 1 502 ? 132.346 120.403 161.978 1.00 56.32  ? 477 PRO B N   1 
ATOM   7327  C  CA  . PRO B 1 502 ? 132.918 120.179 160.646 1.00 55.76  ? 477 PRO B CA  1 
ATOM   7328  C  C   . PRO B 1 502 ? 131.936 119.486 159.717 1.00 53.32  ? 477 PRO B C   1 
ATOM   7329  O  O   . PRO B 1 502 ? 131.229 118.559 160.112 1.00 66.32  ? 477 PRO B O   1 
ATOM   7330  C  CB  . PRO B 1 502 ? 134.139 119.297 160.929 1.00 56.04  ? 477 PRO B CB  1 
ATOM   7331  C  CG  . PRO B 1 502 ? 134.450 119.519 162.369 1.00 50.37  ? 477 PRO B CG  1 
ATOM   7332  C  CD  . PRO B 1 502 ? 133.138 119.759 163.037 1.00 52.44  ? 477 PRO B CD  1 
ATOM   7333  N  N   . VAL B 1 503 ? 131.888 119.953 158.474 1.00 33.66  ? 478 VAL B N   1 
ATOM   7334  C  CA  . VAL B 1 503 ? 131.058 119.357 157.436 1.00 33.68  ? 478 VAL B CA  1 
ATOM   7335  C  C   . VAL B 1 503 ? 131.894 119.236 156.175 1.00 36.09  ? 478 VAL B C   1 
ATOM   7336  O  O   . VAL B 1 503 ? 132.510 120.213 155.742 1.00 58.61  ? 478 VAL B O   1 
ATOM   7337  C  CB  . VAL B 1 503 ? 129.793 120.185 157.154 1.00 37.01  ? 478 VAL B CB  1 
ATOM   7338  C  CG1 . VAL B 1 503 ? 128.992 119.546 156.042 1.00 36.90  ? 478 VAL B CG1 1 
ATOM   7339  C  CG2 . VAL B 1 503 ? 128.951 120.315 158.400 1.00 43.11  ? 478 VAL B CG2 1 
ATOM   7340  N  N   . TYR B 1 504 ? 131.916 118.047 155.587 1.00 31.33  ? 479 TYR B N   1 
ATOM   7341  C  CA  . TYR B 1 504 ? 132.594 117.820 154.319 1.00 34.26  ? 479 TYR B CA  1 
ATOM   7342  C  C   . TYR B 1 504 ? 131.548 117.450 153.281 1.00 40.06  ? 479 TYR B C   1 
ATOM   7343  O  O   . TYR B 1 504 ? 130.818 116.472 153.457 1.00 61.58  ? 479 TYR B O   1 
ATOM   7344  C  CB  . TYR B 1 504 ? 133.647 116.721 154.449 1.00 37.80  ? 479 TYR B CB  1 
ATOM   7345  C  CG  . TYR B 1 504 ? 134.812 117.102 155.325 1.00 36.84  ? 479 TYR B CG  1 
ATOM   7346  C  CD1 . TYR B 1 504 ? 134.714 117.050 156.702 1.00 41.73  ? 479 TYR B CD1 1 
ATOM   7347  C  CD2 . TYR B 1 504 ? 136.008 117.516 154.772 1.00 40.09  ? 479 TYR B CD2 1 
ATOM   7348  C  CE1 . TYR B 1 504 ? 135.774 117.402 157.504 1.00 42.12  ? 479 TYR B CE1 1 
ATOM   7349  C  CE2 . TYR B 1 504 ? 137.072 117.870 155.564 1.00 40.29  ? 479 TYR B CE2 1 
ATOM   7350  C  CZ  . TYR B 1 504 ? 136.951 117.812 156.928 1.00 43.06  ? 479 TYR B CZ  1 
ATOM   7351  O  OH  . TYR B 1 504 ? 138.013 118.164 157.723 1.00 43.28  ? 479 TYR B OH  1 
ATOM   7352  N  N   . PHE B 1 505 ? 131.481 118.217 152.203 1.00 12.27  ? 480 PHE B N   1 
ATOM   7353  C  CA  . PHE B 1 505 ? 130.485 118.013 151.162 1.00 12.60  ? 480 PHE B CA  1 
ATOM   7354  C  C   . PHE B 1 505 ? 131.138 117.332 149.970 1.00 29.15  ? 480 PHE B C   1 
ATOM   7355  O  O   . PHE B 1 505 ? 132.219 117.738 149.539 1.00 52.46  ? 480 PHE B O   1 
ATOM   7356  C  CB  . PHE B 1 505 ? 129.868 119.345 150.744 1.00 21.48  ? 480 PHE B CB  1 
ATOM   7357  C  CG  . PHE B 1 505 ? 128.549 119.214 150.046 1.00 23.13  ? 480 PHE B CG  1 
ATOM   7358  C  CD1 . PHE B 1 505 ? 128.491 119.026 148.682 1.00 32.16  ? 480 PHE B CD1 1 
ATOM   7359  C  CD2 . PHE B 1 505 ? 127.371 119.292 150.751 1.00 28.41  ? 480 PHE B CD2 1 
ATOM   7360  C  CE1 . PHE B 1 505 ? 127.286 118.911 148.038 1.00 32.79  ? 480 PHE B CE1 1 
ATOM   7361  C  CE2 . PHE B 1 505 ? 126.164 119.176 150.109 1.00 37.67  ? 480 PHE B CE2 1 
ATOM   7362  C  CZ  . PHE B 1 505 ? 126.123 118.987 148.751 1.00 32.41  ? 480 PHE B CZ  1 
ATOM   7363  N  N   . TYR B 1 506 ? 130.492 116.295 149.448 1.00 27.37  ? 481 TYR B N   1 
ATOM   7364  C  CA  . TYR B 1 506 ? 131.013 115.582 148.292 1.00 17.64  ? 481 TYR B CA  1 
ATOM   7365  C  C   . TYR B 1 506 ? 129.933 115.418 147.235 1.00 25.79  ? 481 TYR B C   1 
ATOM   7366  O  O   . TYR B 1 506 ? 128.741 115.319 147.541 1.00 53.47  ? 481 TYR B O   1 
ATOM   7367  C  CB  . TYR B 1 506 ? 131.581 114.208 148.677 1.00 28.84  ? 481 TYR B CB  1 
ATOM   7368  C  CG  . TYR B 1 506 ? 130.590 113.068 148.665 1.00 37.36  ? 481 TYR B CG  1 
ATOM   7369  C  CD1 . TYR B 1 506 ? 130.344 112.345 147.508 1.00 45.67  ? 481 TYR B CD1 1 
ATOM   7370  C  CD2 . TYR B 1 506 ? 129.926 112.694 149.819 1.00 29.99  ? 481 TYR B CD2 1 
ATOM   7371  C  CE1 . TYR B 1 506 ? 129.448 111.309 147.496 1.00 47.21  ? 481 TYR B CE1 1 
ATOM   7372  C  CE2 . TYR B 1 506 ? 129.029 111.655 149.815 1.00 29.75  ? 481 TYR B CE2 1 
ATOM   7373  C  CZ  . TYR B 1 506 ? 128.794 110.968 148.650 1.00 42.95  ? 481 TYR B CZ  1 
ATOM   7374  O  OH  . TYR B 1 506 ? 127.900 109.928 148.636 1.00 53.91  ? 481 TYR B OH  1 
ATOM   7375  N  N   . THR B 1 507 ? 130.368 115.378 145.981 1.00 31.33  ? 482 THR B N   1 
ATOM   7376  C  CA  . THR B 1 507 ? 129.480 115.159 144.852 1.00 32.62  ? 482 THR B CA  1 
ATOM   7377  C  C   . THR B 1 507 ? 130.051 114.049 143.988 1.00 39.39  ? 482 THR B C   1 
ATOM   7378  O  O   . THR B 1 507 ? 131.212 114.113 143.580 1.00 56.51  ? 482 THR B O   1 
ATOM   7379  C  CB  . THR B 1 507 ? 129.308 116.430 144.033 1.00 31.56  ? 482 THR B CB  1 
ATOM   7380  O  OG1 . THR B 1 507 ? 128.850 117.477 144.891 1.00 50.32  ? 482 THR B OG1 1 
ATOM   7381  C  CG2 . THR B 1 507 ? 128.285 116.211 142.965 1.00 31.20  ? 482 THR B CG2 1 
ATOM   7382  N  N   . PHE B 1 508 ? 129.236 113.040 143.714 1.00 38.64  ? 483 PHE B N   1 
ATOM   7383  C  CA  . PHE B 1 508 ? 129.662 111.856 142.984 1.00 33.08  ? 483 PHE B CA  1 
ATOM   7384  C  C   . PHE B 1 508 ? 129.183 111.954 141.545 1.00 39.96  ? 483 PHE B C   1 
ATOM   7385  O  O   . PHE B 1 508 ? 128.021 112.285 141.297 1.00 58.09  ? 483 PHE B O   1 
ATOM   7386  C  CB  . PHE B 1 508 ? 129.110 110.595 143.642 1.00 33.38  ? 483 PHE B CB  1 
ATOM   7387  C  CG  . PHE B 1 508 ? 129.993 109.400 143.494 1.00 39.47  ? 483 PHE B CG  1 
ATOM   7388  C  CD1 . PHE B 1 508 ? 131.187 109.325 144.175 1.00 41.83  ? 483 PHE B CD1 1 
ATOM   7389  C  CD2 . PHE B 1 508 ? 129.626 108.350 142.682 1.00 48.53  ? 483 PHE B CD2 1 
ATOM   7390  C  CE1 . PHE B 1 508 ? 132.000 108.232 144.043 1.00 47.19  ? 483 PHE B CE1 1 
ATOM   7391  C  CE2 . PHE B 1 508 ? 130.436 107.255 142.551 1.00 47.65  ? 483 PHE B CE2 1 
ATOM   7392  C  CZ  . PHE B 1 508 ? 131.625 107.197 143.229 1.00 50.75  ? 483 PHE B CZ  1 
ATOM   7393  N  N   . TYR B 1 509 ? 130.073 111.672 140.604 1.00 50.38  ? 484 TYR B N   1 
ATOM   7394  C  CA  . TYR B 1 509 ? 129.751 111.770 139.186 1.00 55.42  ? 484 TYR B CA  1 
ATOM   7395  C  C   . TYR B 1 509 ? 129.940 110.470 138.425 1.00 58.05  ? 484 TYR B C   1 
ATOM   7396  O  O   . TYR B 1 509 ? 129.104 110.128 137.588 1.00 63.31  ? 484 TYR B O   1 
ATOM   7397  C  CB  . TYR B 1 509 ? 130.602 112.862 138.537 1.00 55.99  ? 484 TYR B CB  1 
ATOM   7398  C  CG  . TYR B 1 509 ? 129.959 114.221 138.580 1.00 56.49  ? 484 TYR B CG  1 
ATOM   7399  C  CD1 . TYR B 1 509 ? 129.978 114.981 139.733 1.00 59.46  ? 484 TYR B CD1 1 
ATOM   7400  C  CD2 . TYR B 1 509 ? 129.333 114.745 137.467 1.00 55.34  ? 484 TYR B CD2 1 
ATOM   7401  C  CE1 . TYR B 1 509 ? 129.394 116.223 139.775 1.00 56.80  ? 484 TYR B CE1 1 
ATOM   7402  C  CE2 . TYR B 1 509 ? 128.750 115.985 137.503 1.00 56.90  ? 484 TYR B CE2 1 
ATOM   7403  C  CZ  . TYR B 1 509 ? 128.778 116.720 138.659 1.00 58.05  ? 484 TYR B CZ  1 
ATOM   7404  O  OH  . TYR B 1 509 ? 128.189 117.962 138.695 1.00 62.52  ? 484 TYR B OH  1 
ATOM   7405  N  N   . HIS B 1 510 ? 131.020 109.743 138.679 1.00 68.03  ? 485 HIS B N   1 
ATOM   7406  C  CA  . HIS B 1 510 ? 131.283 108.513 137.950 1.00 70.10  ? 485 HIS B CA  1 
ATOM   7407  C  C   . HIS B 1 510 ? 130.299 107.436 138.393 1.00 72.58  ? 485 HIS B C   1 
ATOM   7408  O  O   . HIS B 1 510 ? 130.026 107.279 139.585 1.00 70.30  ? 485 HIS B O   1 
ATOM   7409  C  CB  . HIS B 1 510 ? 132.726 108.074 138.203 1.00 71.02  ? 485 HIS B CB  1 
ATOM   7410  C  CG  . HIS B 1 510 ? 133.062 106.705 137.696 1.00 69.49  ? 485 HIS B CG  1 
ATOM   7411  N  ND1 . HIS B 1 510 ? 132.313 106.049 136.744 1.00 67.64  ? 485 HIS B ND1 1 
ATOM   7412  C  CD2 . HIS B 1 510 ? 134.074 105.867 138.018 1.00 70.98  ? 485 HIS B CD2 1 
ATOM   7413  C  CE1 . HIS B 1 510 ? 132.848 104.867 136.501 1.00 70.78  ? 485 HIS B CE1 1 
ATOM   7414  N  NE2 . HIS B 1 510 ? 133.918 104.731 137.262 1.00 73.38  ? 485 HIS B NE2 1 
ATOM   7415  N  N   . HIS B 1 511 ? 129.763 106.692 137.429 1.00 79.21  ? 486 HIS B N   1 
ATOM   7416  C  CA  . HIS B 1 511 ? 128.873 105.575 137.708 1.00 79.56  ? 486 HIS B CA  1 
ATOM   7417  C  C   . HIS B 1 511 ? 129.309 104.365 136.899 1.00 83.25  ? 486 HIS B C   1 
ATOM   7418  O  O   . HIS B 1 511 ? 129.845 104.496 135.797 1.00 84.34  ? 486 HIS B O   1 
ATOM   7419  C  CB  . HIS B 1 511 ? 127.422 105.910 137.377 1.00 75.77  ? 486 HIS B CB  1 
ATOM   7420  C  CG  . HIS B 1 511 ? 127.097 105.806 135.921 1.00 80.02  ? 486 HIS B CG  1 
ATOM   7421  N  ND1 . HIS B 1 511 ? 127.829 106.450 134.948 1.00 83.61  ? 486 HIS B ND1 1 
ATOM   7422  C  CD2 . HIS B 1 511 ? 126.120 105.131 135.271 1.00 80.62  ? 486 HIS B CD2 1 
ATOM   7423  C  CE1 . HIS B 1 511 ? 127.316 106.177 133.761 1.00 85.00  ? 486 HIS B CE1 1 
ATOM   7424  N  NE2 . HIS B 1 511 ? 126.277 105.379 133.930 1.00 85.53  ? 486 HIS B NE2 1 
ATOM   7425  N  N   . CYS B 1 512 ? 129.078 103.183 137.460 1.00 98.91  ? 487 CYS B N   1 
ATOM   7426  C  CA  . CYS B 1 512 ? 129.439 101.952 136.772 1.00 96.29  ? 487 CYS B CA  1 
ATOM   7427  C  C   . CYS B 1 512 ? 128.581 101.768 135.528 1.00 94.46  ? 487 CYS B C   1 
ATOM   7428  O  O   . CYS B 1 512 ? 127.370 101.997 135.549 1.00 98.14  ? 487 CYS B O   1 
ATOM   7429  C  CB  . CYS B 1 512 ? 129.275 100.757 137.708 1.00 97.02  ? 487 CYS B CB  1 
ATOM   7430  S  SG  . CYS B 1 512 ? 127.835 100.868 138.793 1.00 107.76 ? 487 CYS B SG  1 
ATOM   7431  N  N   . GLN B 1 513 ? 129.216 101.348 134.438 1.00 93.63  ? 488 GLN B N   1 
ATOM   7432  C  CA  . GLN B 1 513 ? 128.519 101.155 133.168 1.00 98.55  ? 488 GLN B CA  1 
ATOM   7433  C  C   . GLN B 1 513 ? 127.678 99.888  133.250 1.00 98.61  ? 488 GLN B C   1 
ATOM   7434  O  O   . GLN B 1 513 ? 128.189 98.776  133.109 1.00 99.25  ? 488 GLN B O   1 
ATOM   7435  C  CB  . GLN B 1 513 ? 129.520 101.081 132.019 1.00 99.27  ? 488 GLN B CB  1 
ATOM   7436  C  CG  . GLN B 1 513 ? 129.866 102.430 131.399 1.00 98.70  ? 488 GLN B CG  1 
ATOM   7437  C  CD  . GLN B 1 513 ? 128.715 103.038 130.619 1.00 98.60  ? 488 GLN B CD  1 
ATOM   7438  O  OE1 . GLN B 1 513 ? 127.856 103.714 131.184 1.00 95.12  ? 488 GLN B OE1 1 
ATOM   7439  N  NE2 . GLN B 1 513 ? 128.702 102.813 129.311 1.00 99.81  ? 488 GLN B NE2 1 
ATOM   7440  N  N   . ALA B 1 514 ? 126.377 100.050 133.477 1.00 98.65  ? 489 ALA B N   1 
ATOM   7441  C  CA  . ALA B 1 514 ? 125.470 98.916  133.588 1.00 98.12  ? 489 ALA B CA  1 
ATOM   7442  C  C   . ALA B 1 514 ? 125.051 98.448  132.195 1.00 102.07 ? 489 ALA B C   1 
ATOM   7443  O  O   . ALA B 1 514 ? 125.631 98.837  131.178 1.00 101.18 ? 489 ALA B O   1 
ATOM   7444  C  CB  . ALA B 1 514 ? 124.269 99.280  134.453 1.00 94.83  ? 489 ALA B CB  1 
ATOM   7445  N  N   . GLU B 1 515 ? 124.038 97.585  132.141 1.00 106.54 ? 490 GLU B N   1 
ATOM   7446  C  CA  . GLU B 1 515 ? 123.501 97.080  130.884 1.00 107.58 ? 490 GLU B CA  1 
ATOM   7447  C  C   . GLU B 1 515 ? 122.228 97.803  130.464 1.00 106.09 ? 490 GLU B C   1 
ATOM   7448  O  O   . GLU B 1 515 ? 122.137 98.298  129.337 1.00 102.08 ? 490 GLU B O   1 
ATOM   7449  C  CB  . GLU B 1 515 ? 123.231 95.574  130.992 1.00 101.36 ? 490 GLU B CB  1 
ATOM   7450  N  N   . GLY B 1 516 ? 121.242 97.870  131.350 1.00 101.58 ? 491 GLY B N   1 
ATOM   7451  C  CA  . GLY B 1 516 ? 119.977 98.510  131.071 1.00 100.63 ? 491 GLY B CA  1 
ATOM   7452  C  C   . GLY B 1 516 ? 119.919 99.985  131.393 1.00 102.37 ? 491 GLY B C   1 
ATOM   7453  O  O   . GLY B 1 516 ? 118.831 100.569 131.361 1.00 104.71 ? 491 GLY B O   1 
ATOM   7454  N  N   . ARG B 1 517 ? 121.050 100.607 131.709 1.00 89.28  ? 492 ARG B N   1 
ATOM   7455  C  CA  . ARG B 1 517 ? 120.972 102.028 132.019 1.00 88.60  ? 492 ARG B CA  1 
ATOM   7456  C  C   . ARG B 1 517 ? 121.212 102.863 130.765 1.00 90.32  ? 492 ARG B C   1 
ATOM   7457  O  O   . ARG B 1 517 ? 122.115 102.560 129.980 1.00 90.90  ? 492 ARG B O   1 
ATOM   7458  C  CB  . ARG B 1 517 ? 121.990 102.404 133.088 1.00 86.72  ? 492 ARG B CB  1 
ATOM   7459  C  CG  . ARG B 1 517 ? 121.657 101.846 134.457 1.00 89.53  ? 492 ARG B CG  1 
ATOM   7460  C  CD  . ARG B 1 517 ? 120.930 102.874 135.296 1.00 87.84  ? 492 ARG B CD  1 
ATOM   7461  N  NE  . ARG B 1 517 ? 121.813 103.969 135.671 1.00 87.85  ? 492 ARG B NE  1 
ATOM   7462  C  CZ  . ARG B 1 517 ? 122.701 103.908 136.653 1.00 86.95  ? 492 ARG B CZ  1 
ATOM   7463  N  NH1 . ARG B 1 517 ? 122.834 102.822 137.396 1.00 85.94  ? 492 ARG B NH1 1 
ATOM   7464  N  NH2 . ARG B 1 517 ? 123.470 104.963 136.898 1.00 85.51  ? 492 ARG B NH2 1 
ATOM   7465  N  N   . PRO B 1 518 ? 120.411 103.910 130.572 1.00 93.60  ? 493 PRO B N   1 
ATOM   7466  C  CA  . PRO B 1 518 ? 120.537 104.727 129.361 1.00 92.30  ? 493 PRO B CA  1 
ATOM   7467  C  C   . PRO B 1 518 ? 121.893 105.409 129.279 1.00 92.52  ? 493 PRO B C   1 
ATOM   7468  O  O   . PRO B 1 518 ? 122.533 105.697 130.292 1.00 93.51  ? 493 PRO B O   1 
ATOM   7469  C  CB  . PRO B 1 518 ? 119.407 105.752 129.505 1.00 89.64  ? 493 PRO B CB  1 
ATOM   7470  C  CG  . PRO B 1 518 ? 118.454 105.145 130.480 1.00 93.07  ? 493 PRO B CG  1 
ATOM   7471  C  CD  . PRO B 1 518 ? 119.291 104.345 131.422 1.00 91.39  ? 493 PRO B CD  1 
ATOM   7472  N  N   . GLU B 1 519 ? 122.334 105.655 128.043 1.00 91.24  ? 494 GLU B N   1 
ATOM   7473  C  CA  . GLU B 1 519 ? 123.625 106.301 127.832 1.00 89.52  ? 494 GLU B CA  1 
ATOM   7474  C  C   . GLU B 1 519 ? 123.627 107.726 128.371 1.00 90.25  ? 494 GLU B C   1 
ATOM   7475  O  O   . GLU B 1 519 ? 124.637 108.192 128.911 1.00 89.26  ? 494 GLU B O   1 
ATOM   7476  C  CB  . GLU B 1 519 ? 123.979 106.289 126.346 1.00 90.44  ? 494 GLU B CB  1 
ATOM   7477  N  N   . TRP B 1 520 ? 122.507 108.437 128.227 1.00 91.17  ? 495 TRP B N   1 
ATOM   7478  C  CA  . TRP B 1 520 ? 122.426 109.809 128.715 1.00 91.13  ? 495 TRP B CA  1 
ATOM   7479  C  C   . TRP B 1 520 ? 122.408 109.888 130.234 1.00 91.63  ? 495 TRP B C   1 
ATOM   7480  O  O   . TRP B 1 520 ? 122.713 110.949 130.789 1.00 90.48  ? 495 TRP B O   1 
ATOM   7481  C  CB  . TRP B 1 520 ? 121.180 110.493 128.155 1.00 89.50  ? 495 TRP B CB  1 
ATOM   7482  C  CG  . TRP B 1 520 ? 119.898 109.916 128.674 1.00 91.08  ? 495 TRP B CG  1 
ATOM   7483  C  CD1 . TRP B 1 520 ? 119.173 108.905 128.119 1.00 91.52  ? 495 TRP B CD1 1 
ATOM   7484  C  CD2 . TRP B 1 520 ? 119.191 110.316 129.853 1.00 90.78  ? 495 TRP B CD2 1 
ATOM   7485  N  NE1 . TRP B 1 520 ? 118.057 108.650 128.878 1.00 89.99  ? 495 TRP B NE1 1 
ATOM   7486  C  CE2 . TRP B 1 520 ? 118.047 109.503 129.949 1.00 93.21  ? 495 TRP B CE2 1 
ATOM   7487  C  CE3 . TRP B 1 520 ? 119.416 111.282 130.836 1.00 88.22  ? 495 TRP B CE3 1 
ATOM   7488  C  CZ2 . TRP B 1 520 ? 117.130 109.627 130.989 1.00 93.41  ? 495 TRP B CZ2 1 
ATOM   7489  C  CZ3 . TRP B 1 520 ? 118.505 111.402 131.865 1.00 89.63  ? 495 TRP B CZ3 1 
ATOM   7490  C  CH2 . TRP B 1 520 ? 117.377 110.581 131.934 1.00 91.09  ? 495 TRP B CH2 1 
ATOM   7491  N  N   . ALA B 1 521 ? 122.057 108.801 130.916 1.00 91.75  ? 496 ALA B N   1 
ATOM   7492  C  CA  . ALA B 1 521 ? 121.924 108.826 132.364 1.00 90.75  ? 496 ALA B CA  1 
ATOM   7493  C  C   . ALA B 1 521 ? 123.288 108.999 133.027 1.00 89.13  ? 496 ALA B C   1 
ATOM   7494  O  O   . ALA B 1 521 ? 124.340 108.941 132.385 1.00 87.89  ? 496 ALA B O   1 
ATOM   7495  C  CB  . ALA B 1 521 ? 121.249 107.550 132.863 1.00 89.80  ? 496 ALA B CB  1 
ATOM   7496  N  N   . ASP B 1 522 ? 123.256 109.217 134.338 1.00 77.07  ? 497 ASP B N   1 
ATOM   7497  C  CA  . ASP B 1 522 ? 124.466 109.417 135.119 1.00 72.16  ? 497 ASP B CA  1 
ATOM   7498  C  C   . ASP B 1 522 ? 124.303 108.708 136.459 1.00 75.89  ? 497 ASP B C   1 
ATOM   7499  O  O   . ASP B 1 522 ? 123.422 107.861 136.632 1.00 79.87  ? 497 ASP B O   1 
ATOM   7500  C  CB  . ASP B 1 522 ? 124.767 110.908 135.288 1.00 67.14  ? 497 ASP B CB  1 
ATOM   7501  C  CG  . ASP B 1 522 ? 126.220 111.165 135.570 1.00 77.44  ? 497 ASP B CG  1 
ATOM   7502  O  OD1 . ASP B 1 522 ? 126.613 111.066 136.748 1.00 82.92  ? 497 ASP B OD1 1 
ATOM   7503  O  OD2 . ASP B 1 522 ? 126.969 111.464 134.618 1.00 81.72  ? 497 ASP B OD2 1 
ATOM   7504  N  N   . ALA B 1 523 ? 125.168 109.054 137.412 1.00 51.66  ? 498 ALA B N   1 
ATOM   7505  C  CA  . ALA B 1 523 ? 125.190 108.380 138.703 1.00 51.43  ? 498 ALA B CA  1 
ATOM   7506  C  C   . ALA B 1 523 ? 123.877 108.584 139.437 1.00 53.33  ? 498 ALA B C   1 
ATOM   7507  O  O   . ALA B 1 523 ? 123.621 109.665 139.972 1.00 61.25  ? 498 ALA B O   1 
ATOM   7508  C  CB  . ALA B 1 523 ? 126.353 108.890 139.550 1.00 48.32  ? 498 ALA B CB  1 
ATOM   7509  N  N   . ALA B 1 524 ? 123.050 107.548 139.482 1.00 52.72  ? 499 ALA B N   1 
ATOM   7510  C  CA  . ALA B 1 524 ? 121.711 107.654 140.034 1.00 51.92  ? 499 ALA B CA  1 
ATOM   7511  C  C   . ALA B 1 524 ? 121.749 107.430 141.542 1.00 53.85  ? 499 ALA B C   1 
ATOM   7512  O  O   . ALA B 1 524 ? 122.816 107.321 142.149 1.00 60.56  ? 499 ALA B O   1 
ATOM   7513  C  CB  . ALA B 1 524 ? 120.776 106.676 139.332 1.00 51.37  ? 499 ALA B CB  1 
ATOM   7514  N  N   . HIS B 1 525 ? 120.575 107.369 142.163 1.00 45.41  ? 500 HIS B N   1 
ATOM   7515  C  CA  . HIS B 1 525 ? 120.499 107.202 143.606 1.00 42.77  ? 500 HIS B CA  1 
ATOM   7516  C  C   . HIS B 1 525 ? 121.113 105.872 144.014 1.00 54.59  ? 500 HIS B C   1 
ATOM   7517  O  O   . HIS B 1 525 ? 120.814 104.830 143.428 1.00 61.04  ? 500 HIS B O   1 
ATOM   7518  C  CB  . HIS B 1 525 ? 119.045 107.279 144.063 1.00 41.18  ? 500 HIS B CB  1 
ATOM   7519  C  CG  . HIS B 1 525 ? 118.874 107.307 145.548 1.00 48.24  ? 500 HIS B CG  1 
ATOM   7520  N  ND1 . HIS B 1 525 ? 117.638 107.360 146.151 1.00 51.58  ? 500 HIS B ND1 1 
ATOM   7521  C  CD2 . HIS B 1 525 ? 119.781 107.296 146.552 1.00 49.84  ? 500 HIS B CD2 1 
ATOM   7522  C  CE1 . HIS B 1 525 ? 117.789 107.375 147.462 1.00 50.44  ? 500 HIS B CE1 1 
ATOM   7523  N  NE2 . HIS B 1 525 ? 119.081 107.336 147.732 1.00 44.94  ? 500 HIS B NE2 1 
ATOM   7524  N  N   . GLY B 1 526 ? 121.979 105.911 145.020 1.00 54.89  ? 501 GLY B N   1 
ATOM   7525  C  CA  . GLY B 1 526 ? 122.590 104.693 145.501 1.00 53.12  ? 501 GLY B CA  1 
ATOM   7526  C  C   . GLY B 1 526 ? 123.632 104.103 144.585 1.00 55.96  ? 501 GLY B C   1 
ATOM   7527  O  O   . GLY B 1 526 ? 123.933 102.915 144.696 1.00 62.16  ? 501 GLY B O   1 
ATOM   7528  N  N   . ASP B 1 527 ? 124.190 104.894 143.675 1.00 57.78  ? 502 ASP B N   1 
ATOM   7529  C  CA  . ASP B 1 527 ? 125.265 104.427 142.813 1.00 52.63  ? 502 ASP B CA  1 
ATOM   7530  C  C   . ASP B 1 527 ? 126.642 104.682 143.401 1.00 56.55  ? 502 ASP B C   1 
ATOM   7531  O  O   . ASP B 1 527 ? 127.642 104.360 142.756 1.00 67.09  ? 502 ASP B O   1 
ATOM   7532  C  CB  . ASP B 1 527 ? 125.167 105.081 141.434 1.00 51.52  ? 502 ASP B CB  1 
ATOM   7533  C  CG  . ASP B 1 527 ? 124.609 104.143 140.389 1.00 61.26  ? 502 ASP B CG  1 
ATOM   7534  O  OD1 . ASP B 1 527 ? 124.592 102.922 140.637 1.00 69.19  ? 502 ASP B OD1 1 
ATOM   7535  O  OD2 . ASP B 1 527 ? 124.187 104.622 139.319 1.00 68.58  ? 502 ASP B OD2 1 
ATOM   7536  N  N   . GLU B 1 528 ? 126.721 105.261 144.593 1.00 50.30  ? 503 GLU B N   1 
ATOM   7537  C  CA  . GLU B 1 528 ? 127.981 105.368 145.310 1.00 49.23  ? 503 GLU B CA  1 
ATOM   7538  C  C   . GLU B 1 528 ? 128.186 104.229 146.290 1.00 55.86  ? 503 GLU B C   1 
ATOM   7539  O  O   . GLU B 1 528 ? 129.193 104.220 147.001 1.00 65.41  ? 503 GLU B O   1 
ATOM   7540  C  CB  . GLU B 1 528 ? 128.065 106.699 146.058 1.00 47.96  ? 503 GLU B CB  1 
ATOM   7541  C  CG  . GLU B 1 528 ? 127.089 106.828 147.208 1.00 55.28  ? 503 GLU B CG  1 
ATOM   7542  C  CD  . GLU B 1 528 ? 126.013 107.864 146.944 1.00 63.80  ? 503 GLU B CD  1 
ATOM   7543  O  OE1 . GLU B 1 528 ? 125.557 107.970 145.788 1.00 61.77  ? 503 GLU B OE1 1 
ATOM   7544  O  OE2 . GLU B 1 528 ? 125.627 108.577 147.893 1.00 60.54  ? 503 GLU B OE2 1 
ATOM   7545  N  N   . LEU B 1 529 ? 127.258 103.281 146.352 1.00 57.16  ? 504 LEU B N   1 
ATOM   7546  C  CA  . LEU B 1 529 ? 127.324 102.158 147.278 1.00 57.37  ? 504 LEU B CA  1 
ATOM   7547  C  C   . LEU B 1 529 ? 128.285 101.065 146.818 1.00 59.32  ? 504 LEU B C   1 
ATOM   7548  O  O   . LEU B 1 529 ? 128.964 100.471 147.664 1.00 67.01  ? 504 LEU B O   1 
ATOM   7549  C  CB  . LEU B 1 529 ? 125.931 101.573 147.501 1.00 57.96  ? 504 LEU B CB  1 
ATOM   7550  C  CG  . LEU B 1 529 ? 125.185 102.175 148.686 1.00 62.14  ? 504 LEU B CG  1 
ATOM   7551  C  CD1 . LEU B 1 529 ? 123.896 101.427 148.937 1.00 63.86  ? 504 LEU B CD1 1 
ATOM   7552  C  CD2 . LEU B 1 529 ? 126.064 102.159 149.920 1.00 58.37  ? 504 LEU B CD2 1 
ATOM   7553  N  N   . PRO B 1 530 ? 128.365 100.733 145.523 1.00 58.41  ? 505 PRO B N   1 
ATOM   7554  C  CA  . PRO B 1 530 ? 129.404 99.776  145.109 1.00 57.08  ? 505 PRO B CA  1 
ATOM   7555  C  C   . PRO B 1 530 ? 130.808 100.234 145.445 1.00 59.99  ? 505 PRO B C   1 
ATOM   7556  O  O   . PRO B 1 530 ? 131.654 99.409  145.808 1.00 72.17  ? 505 PRO B O   1 
ATOM   7557  C  CB  . PRO B 1 530 ? 129.195 99.666  143.595 1.00 59.72  ? 505 PRO B CB  1 
ATOM   7558  C  CG  . PRO B 1 530 ? 127.789 100.002 143.387 1.00 59.47  ? 505 PRO B CG  1 
ATOM   7559  C  CD  . PRO B 1 530 ? 127.431 101.018 144.419 1.00 61.35  ? 505 PRO B CD  1 
ATOM   7560  N  N   . TYR B 1 531 ? 131.083 101.533 145.338 1.00 50.77  ? 506 TYR B N   1 
ATOM   7561  C  CA  . TYR B 1 531 ? 132.436 102.023 145.567 1.00 53.87  ? 506 TYR B CA  1 
ATOM   7562  C  C   . TYR B 1 531 ? 132.778 102.081 147.050 1.00 58.76  ? 506 TYR B C   1 
ATOM   7563  O  O   . TYR B 1 531 ? 133.909 101.772 147.437 1.00 67.23  ? 506 TYR B O   1 
ATOM   7564  C  CB  . TYR B 1 531 ? 132.605 103.393 144.916 1.00 53.15  ? 506 TYR B CB  1 
ATOM   7565  C  CG  . TYR B 1 531 ? 132.345 103.361 143.433 1.00 53.83  ? 506 TYR B CG  1 
ATOM   7566  C  CD1 . TYR B 1 531 ? 133.312 102.917 142.555 1.00 56.99  ? 506 TYR B CD1 1 
ATOM   7567  C  CD2 . TYR B 1 531 ? 131.125 103.749 142.916 1.00 60.19  ? 506 TYR B CD2 1 
ATOM   7568  C  CE1 . TYR B 1 531 ? 133.077 102.875 141.203 1.00 62.35  ? 506 TYR B CE1 1 
ATOM   7569  C  CE2 . TYR B 1 531 ? 130.881 103.709 141.565 1.00 61.55  ? 506 TYR B CE2 1 
ATOM   7570  C  CZ  . TYR B 1 531 ? 131.861 103.271 140.714 1.00 61.76  ? 506 TYR B CZ  1 
ATOM   7571  O  OH  . TYR B 1 531 ? 131.624 103.229 139.363 1.00 62.16  ? 506 TYR B OH  1 
ATOM   7572  N  N   . VAL B 1 532 ? 131.822 102.466 147.894 1.00 43.45  ? 507 VAL B N   1 
ATOM   7573  C  CA  . VAL B 1 532 ? 132.098 102.559 149.323 1.00 37.38  ? 507 VAL B CA  1 
ATOM   7574  C  C   . VAL B 1 532 ? 132.352 101.179 149.913 1.00 51.13  ? 507 VAL B C   1 
ATOM   7575  O  O   . VAL B 1 532 ? 133.181 101.020 150.816 1.00 61.62  ? 507 VAL B O   1 
ATOM   7576  C  CB  . VAL B 1 532 ? 130.950 103.283 150.044 1.00 44.21  ? 507 VAL B CB  1 
ATOM   7577  C  CG1 . VAL B 1 532 ? 131.139 103.208 151.540 1.00 46.57  ? 507 VAL B CG1 1 
ATOM   7578  C  CG2 . VAL B 1 532 ? 130.897 104.722 149.607 1.00 55.03  ? 507 VAL B CG2 1 
ATOM   7579  N  N   . PHE B 1 533 ? 131.653 100.161 149.422 1.00 50.52  ? 508 PHE B N   1 
ATOM   7580  C  CA  . PHE B 1 533 ? 131.770 98.819  149.974 1.00 46.34  ? 508 PHE B CA  1 
ATOM   7581  C  C   . PHE B 1 533 ? 132.764 97.942  149.227 1.00 54.01  ? 508 PHE B C   1 
ATOM   7582  O  O   . PHE B 1 533 ? 132.879 96.756  149.548 1.00 63.20  ? 508 PHE B O   1 
ATOM   7583  C  CB  . PHE B 1 533 ? 130.402 98.141  150.000 1.00 45.35  ? 508 PHE B CB  1 
ATOM   7584  C  CG  . PHE B 1 533 ? 129.645 98.385  151.265 1.00 51.85  ? 508 PHE B CG  1 
ATOM   7585  C  CD1 . PHE B 1 533 ? 130.085 97.851  152.458 1.00 57.26  ? 508 PHE B CD1 1 
ATOM   7586  C  CD2 . PHE B 1 533 ? 128.507 99.159  151.266 1.00 52.33  ? 508 PHE B CD2 1 
ATOM   7587  C  CE1 . PHE B 1 533 ? 129.401 98.078  153.624 1.00 54.72  ? 508 PHE B CE1 1 
ATOM   7588  C  CE2 . PHE B 1 533 ? 127.821 99.387  152.431 1.00 56.98  ? 508 PHE B CE2 1 
ATOM   7589  C  CZ  . PHE B 1 533 ? 128.269 98.845  153.611 1.00 57.98  ? 508 PHE B CZ  1 
ATOM   7590  N  N   . GLY B 1 534 ? 133.479 98.486  148.250 1.00 57.40  ? 509 GLY B N   1 
ATOM   7591  C  CA  . GLY B 1 534 ? 134.514 97.735  147.561 1.00 53.26  ? 509 GLY B CA  1 
ATOM   7592  C  C   . GLY B 1 534 ? 134.029 96.573  146.724 1.00 60.74  ? 509 GLY B C   1 
ATOM   7593  O  O   . GLY B 1 534 ? 134.698 95.535  146.670 1.00 71.84  ? 509 GLY B O   1 
ATOM   7594  N  N   . VAL B 1 535 ? 132.873 96.715  146.076 1.00 58.69  ? 510 VAL B N   1 
ATOM   7595  C  CA  . VAL B 1 535 ? 132.442 95.706  145.108 1.00 58.61  ? 510 VAL B CA  1 
ATOM   7596  C  C   . VAL B 1 535 ? 133.400 95.599  143.930 1.00 67.63  ? 510 VAL B C   1 
ATOM   7597  O  O   . VAL B 1 535 ? 133.705 94.472  143.514 1.00 72.93  ? 510 VAL B O   1 
ATOM   7598  C  CB  . VAL B 1 535 ? 130.989 95.961  144.689 1.00 54.35  ? 510 VAL B CB  1 
ATOM   7599  C  CG1 . VAL B 1 535 ? 130.676 95.245  143.397 1.00 63.03  ? 510 VAL B CG1 1 
ATOM   7600  C  CG2 . VAL B 1 535 ? 130.048 95.500  145.778 1.00 58.42  ? 510 VAL B CG2 1 
ATOM   7601  N  N   . PRO B 1 536 ? 133.906 96.691  143.337 1.00 66.65  ? 511 PRO B N   1 
ATOM   7602  C  CA  . PRO B 1 536 ? 134.805 96.529  142.183 1.00 69.77  ? 511 PRO B CA  1 
ATOM   7603  C  C   . PRO B 1 536 ? 136.060 95.728  142.482 1.00 72.58  ? 511 PRO B C   1 
ATOM   7604  O  O   . PRO B 1 536 ? 136.635 95.134  141.563 1.00 75.58  ? 511 PRO B O   1 
ATOM   7605  C  CB  . PRO B 1 536 ? 135.145 97.975  141.804 1.00 65.79  ? 511 PRO B CB  1 
ATOM   7606  C  CG  . PRO B 1 536 ? 134.005 98.752  142.276 1.00 65.98  ? 511 PRO B CG  1 
ATOM   7607  C  CD  . PRO B 1 536 ? 133.599 98.114  143.561 1.00 69.80  ? 511 PRO B CD  1 
ATOM   7608  N  N   . MET B 1 537 ? 136.506 95.692  143.733 1.00 66.79  ? 512 MET B N   1 
ATOM   7609  C  CA  . MET B 1 537 ? 137.709 94.953  144.084 1.00 66.71  ? 512 MET B CA  1 
ATOM   7610  C  C   . MET B 1 537 ? 137.445 93.472  144.323 1.00 69.54  ? 512 MET B C   1 
ATOM   7611  O  O   . MET B 1 537 ? 138.376 92.742  144.677 1.00 73.80  ? 512 MET B O   1 
ATOM   7612  C  CB  . MET B 1 537 ? 138.365 95.581  145.314 1.00 62.30  ? 512 MET B CB  1 
ATOM   7613  C  CG  . MET B 1 537 ? 139.351 96.676  144.961 1.00 67.32  ? 512 MET B CG  1 
ATOM   7614  S  SD  . MET B 1 537 ? 139.388 98.024  146.148 1.00 81.46  ? 512 MET B SD  1 
ATOM   7615  C  CE  . MET B 1 537 ? 140.086 97.190  147.562 1.00 71.98  ? 512 MET B CE  1 
ATOM   7616  N  N   . VAL B 1 538 ? 136.207 93.017  144.151 1.00 66.50  ? 513 VAL B N   1 
ATOM   7617  C  CA  . VAL B 1 538 ? 135.877 91.599  144.236 1.00 69.01  ? 513 VAL B CA  1 
ATOM   7618  C  C   . VAL B 1 538 ? 135.284 91.157  142.906 1.00 70.02  ? 513 VAL B C   1 
ATOM   7619  O  O   . VAL B 1 538 ? 135.447 90.005  142.487 1.00 72.97  ? 513 VAL B O   1 
ATOM   7620  C  CB  . VAL B 1 538 ? 134.917 91.329  145.410 1.00 68.80  ? 513 VAL B CB  1 
ATOM   7621  C  CG1 . VAL B 1 538 ? 134.090 90.079  145.173 1.00 66.51  ? 513 VAL B CG1 1 
ATOM   7622  C  CG2 . VAL B 1 538 ? 135.706 91.193  146.694 1.00 70.04  ? 513 VAL B CG2 1 
ATOM   7623  N  N   . GLY B 1 539 ? 134.633 92.077  142.214 1.00 78.56  ? 514 GLY B N   1 
ATOM   7624  C  CA  . GLY B 1 539 ? 134.021 91.800  140.932 1.00 81.38  ? 514 GLY B CA  1 
ATOM   7625  C  C   . GLY B 1 539 ? 132.512 91.914  140.995 1.00 82.58  ? 514 GLY B C   1 
ATOM   7626  O  O   . GLY B 1 539 ? 131.921 92.210  142.031 1.00 83.89  ? 514 GLY B O   1 
ATOM   7627  N  N   . ALA B 1 540 ? 131.893 91.666  139.845 1.00 82.08  ? 515 ALA B N   1 
ATOM   7628  C  CA  . ALA B 1 540 ? 130.446 91.769  139.743 1.00 81.11  ? 515 ALA B CA  1 
ATOM   7629  C  C   . ALA B 1 540 ? 129.765 90.739  140.633 1.00 82.62  ? 515 ALA B C   1 
ATOM   7630  O  O   . ALA B 1 540 ? 130.219 89.599  140.755 1.00 86.05  ? 515 ALA B O   1 
ATOM   7631  C  CB  . ALA B 1 540 ? 130.005 91.576  138.295 1.00 80.26  ? 515 ALA B CB  1 
ATOM   7632  N  N   . THR B 1 541 ? 128.673 91.151  141.260 1.00 83.18  ? 516 THR B N   1 
ATOM   7633  C  CA  . THR B 1 541 ? 127.826 90.265  142.042 1.00 84.88  ? 516 THR B CA  1 
ATOM   7634  C  C   . THR B 1 541 ? 126.425 90.257  141.435 1.00 84.36  ? 516 THR B C   1 
ATOM   7635  O  O   . THR B 1 541 ? 126.178 90.849  140.382 1.00 85.37  ? 516 THR B O   1 
ATOM   7636  C  CB  . THR B 1 541 ? 127.807 90.689  143.512 1.00 88.11  ? 516 THR B CB  1 
ATOM   7637  O  OG1 . THR B 1 541 ? 127.354 92.042  143.617 1.00 88.34  ? 516 THR B OG1 1 
ATOM   7638  C  CG2 . THR B 1 541 ? 129.195 90.580  144.112 1.00 83.17  ? 516 THR B CG2 1 
ATOM   7639  N  N   . ASP B 1 542 ? 125.503 89.568  142.107 1.00 83.76  ? 517 ASP B N   1 
ATOM   7640  C  CA  . ASP B 1 542 ? 124.130 89.511  141.618 1.00 84.93  ? 517 ASP B CA  1 
ATOM   7641  C  C   . ASP B 1 542 ? 123.455 90.874  141.691 1.00 87.78  ? 517 ASP B C   1 
ATOM   7642  O  O   . ASP B 1 542 ? 122.682 91.238  140.798 1.00 87.89  ? 517 ASP B O   1 
ATOM   7643  C  CB  . ASP B 1 542 ? 123.336 88.472  142.406 1.00 84.40  ? 517 ASP B CB  1 
ATOM   7644  C  CG  . ASP B 1 542 ? 123.718 88.436  143.868 1.00 86.41  ? 517 ASP B CG  1 
ATOM   7645  O  OD1 . ASP B 1 542 ? 124.663 89.155  144.253 1.00 83.26  ? 517 ASP B OD1 1 
ATOM   7646  O  OD2 . ASP B 1 542 ? 123.077 87.685  144.632 1.00 87.60  ? 517 ASP B OD2 1 
ATOM   7647  N  N   . LEU B 1 543 ? 123.725 91.639  142.749 1.00 82.77  ? 518 LEU B N   1 
ATOM   7648  C  CA  . LEU B 1 543 ? 123.082 92.940  142.897 1.00 78.22  ? 518 LEU B CA  1 
ATOM   7649  C  C   . LEU B 1 543 ? 123.671 93.977  141.953 1.00 77.89  ? 518 LEU B C   1 
ATOM   7650  O  O   . LEU B 1 543 ? 122.976 94.922  141.566 1.00 78.20  ? 518 LEU B O   1 
ATOM   7651  C  CB  . LEU B 1 543 ? 123.201 93.420  144.340 1.00 77.39  ? 518 LEU B CB  1 
ATOM   7652  C  CG  . LEU B 1 543 ? 122.096 92.964  145.287 1.00 74.62  ? 518 LEU B CG  1 
ATOM   7653  C  CD1 . LEU B 1 543 ? 122.423 93.357  146.714 1.00 75.24  ? 518 LEU B CD1 1 
ATOM   7654  C  CD2 . LEU B 1 543 ? 120.770 93.560  144.863 1.00 73.71  ? 518 LEU B CD2 1 
ATOM   7655  N  N   . PHE B 1 544 ? 124.943 93.835  141.581 1.00 80.79  ? 519 PHE B N   1 
ATOM   7656  C  CA  . PHE B 1 544 ? 125.632 94.798  140.723 1.00 82.20  ? 519 PHE B CA  1 
ATOM   7657  C  C   . PHE B 1 544 ? 126.167 94.071  139.497 1.00 85.98  ? 519 PHE B C   1 
ATOM   7658  O  O   . PHE B 1 544 ? 127.297 93.559  139.508 1.00 87.39  ? 519 PHE B O   1 
ATOM   7659  C  CB  . PHE B 1 544 ? 126.752 95.507  141.479 1.00 78.76  ? 519 PHE B CB  1 
ATOM   7660  C  CG  . PHE B 1 544 ? 126.326 96.066  142.804 1.00 78.70  ? 519 PHE B CG  1 
ATOM   7661  C  CD1 . PHE B 1 544 ? 125.647 97.267  142.875 1.00 78.28  ? 519 PHE B CD1 1 
ATOM   7662  C  CD2 . PHE B 1 544 ? 126.603 95.392  143.977 1.00 81.11  ? 519 PHE B CD2 1 
ATOM   7663  C  CE1 . PHE B 1 544 ? 125.253 97.785  144.094 1.00 79.99  ? 519 PHE B CE1 1 
ATOM   7664  C  CE2 . PHE B 1 544 ? 126.210 95.907  145.199 1.00 79.13  ? 519 PHE B CE2 1 
ATOM   7665  C  CZ  . PHE B 1 544 ? 125.536 97.104  145.257 1.00 79.01  ? 519 PHE B CZ  1 
ATOM   7666  N  N   . PRO B 1 545 ? 125.392 94.004  138.416 1.00 95.93  ? 520 PRO B N   1 
ATOM   7667  C  CA  . PRO B 1 545 ? 125.785 93.215  137.239 1.00 95.31  ? 520 PRO B CA  1 
ATOM   7668  C  C   . PRO B 1 545 ? 126.677 93.925  136.226 1.00 96.47  ? 520 PRO B C   1 
ATOM   7669  O  O   . PRO B 1 545 ? 126.962 93.336  135.179 1.00 97.19  ? 520 PRO B O   1 
ATOM   7670  C  CB  . PRO B 1 545 ? 124.424 92.878  136.618 1.00 92.59  ? 520 PRO B CB  1 
ATOM   7671  C  CG  . PRO B 1 545 ? 123.575 94.046  136.944 1.00 94.84  ? 520 PRO B CG  1 
ATOM   7672  C  CD  . PRO B 1 545 ? 124.023 94.535  138.298 1.00 92.71  ? 520 PRO B CD  1 
ATOM   7673  N  N   . CYS B 1 546 ? 127.147 95.143  136.499 1.00 105.45 ? 521 CYS B N   1 
ATOM   7674  C  CA  . CYS B 1 546 ? 128.135 95.788  135.649 1.00 104.87 ? 521 CYS B CA  1 
ATOM   7675  C  C   . CYS B 1 546 ? 129.428 94.983  135.645 1.00 105.95 ? 521 CYS B C   1 
ATOM   7676  O  O   . CYS B 1 546 ? 129.595 94.031  136.414 1.00 106.08 ? 521 CYS B O   1 
ATOM   7677  C  CB  . CYS B 1 546 ? 128.439 97.198  136.156 1.00 105.88 ? 521 CYS B CB  1 
ATOM   7678  S  SG  . CYS B 1 546 ? 127.013 98.187  136.598 1.00 118.81 ? 521 CYS B SG  1 
ATOM   7679  N  N   . ASN B 1 547 ? 130.371 95.366  134.786 1.00 104.55 ? 522 ASN B N   1 
ATOM   7680  C  CA  . ASN B 1 547 ? 131.739 94.930  135.019 1.00 103.97 ? 522 ASN B CA  1 
ATOM   7681  C  C   . ASN B 1 547 ? 132.431 96.148  135.604 1.00 102.25 ? 522 ASN B C   1 
ATOM   7682  O  O   . ASN B 1 547 ? 131.954 97.274  135.430 1.00 102.88 ? 522 ASN B O   1 
ATOM   7683  C  CB  . ASN B 1 547 ? 132.549 94.485  133.800 1.00 102.59 ? 522 ASN B CB  1 
ATOM   7684  C  CG  . ASN B 1 547 ? 132.393 95.373  132.588 1.00 105.03 ? 522 ASN B CG  1 
ATOM   7685  O  OD1 . ASN B 1 547 ? 132.397 96.598  132.706 1.00 102.31 ? 522 ASN B OD1 1 
ATOM   7686  N  ND2 . ASN B 1 547 ? 132.378 94.777  131.403 1.00 108.25 ? 522 ASN B ND2 1 
ATOM   7687  N  N   . PHE B 1 548 ? 133.543 95.937  136.282 1.00 84.78  ? 523 PHE B N   1 
ATOM   7688  C  CA  . PHE B 1 548 ? 134.327 97.035  136.818 1.00 84.57  ? 523 PHE B CA  1 
ATOM   7689  C  C   . PHE B 1 548 ? 135.728 97.025  136.225 1.00 84.37  ? 523 PHE B C   1 
ATOM   7690  O  O   . PHE B 1 548 ? 136.497 96.085  136.448 1.00 85.97  ? 523 PHE B O   1 
ATOM   7691  C  CB  . PHE B 1 548 ? 134.368 96.949  138.341 1.00 87.49  ? 523 PHE B CB  1 
ATOM   7692  C  CG  . PHE B 1 548 ? 133.013 97.049  138.981 1.00 85.87  ? 523 PHE B CG  1 
ATOM   7693  C  CD1 . PHE B 1 548 ? 132.453 98.286  139.229 1.00 85.60  ? 523 PHE B CD1 1 
ATOM   7694  C  CD2 . PHE B 1 548 ? 132.292 95.916  139.313 1.00 85.79  ? 523 PHE B CD2 1 
ATOM   7695  C  CE1 . PHE B 1 548 ? 131.217 98.394  139.812 1.00 84.61  ? 523 PHE B CE1 1 
ATOM   7696  C  CE2 . PHE B 1 548 ? 131.048 96.021  139.895 1.00 88.41  ? 523 PHE B CE2 1 
ATOM   7697  C  CZ  . PHE B 1 548 ? 130.512 97.264  140.144 1.00 87.54  ? 523 PHE B CZ  1 
ATOM   7698  N  N   . SER B 1 549 ? 136.063 98.084  135.498 1.00 79.52  ? 524 SER B N   1 
ATOM   7699  C  CA  . SER B 1 549 ? 137.359 98.190  134.844 1.00 81.48  ? 524 SER B CA  1 
ATOM   7700  C  C   . SER B 1 549 ? 138.408 98.633  135.864 1.00 83.71  ? 524 SER B C   1 
ATOM   7701  O  O   . SER B 1 549 ? 138.187 98.599  137.076 1.00 88.67  ? 524 SER B O   1 
ATOM   7702  C  CB  . SER B 1 549 ? 137.267 99.143  133.661 1.00 80.55  ? 524 SER B CB  1 
ATOM   7703  O  OG  . SER B 1 549 ? 137.037 100.460 134.111 1.00 79.06  ? 524 SER B OG  1 
ATOM   7704  N  N   . LYS B 1 550 ? 139.583 99.037  135.378 1.00 79.93  ? 525 LYS B N   1 
ATOM   7705  C  CA  . LYS B 1 550 ? 140.619 99.542  136.273 1.00 80.34  ? 525 LYS B CA  1 
ATOM   7706  C  C   . LYS B 1 550 ? 140.248 100.899 136.855 1.00 84.99  ? 525 LYS B C   1 
ATOM   7707  O  O   . LYS B 1 550 ? 140.611 101.207 137.999 1.00 86.91  ? 525 LYS B O   1 
ATOM   7708  C  CB  . LYS B 1 550 ? 141.950 99.637  135.530 1.00 79.15  ? 525 LYS B CB  1 
ATOM   7709  N  N   . ASN B 1 551 ? 139.540 101.725 136.081 1.00 76.43  ? 526 ASN B N   1 
ATOM   7710  C  CA  . ASN B 1 551 ? 139.113 103.026 136.581 1.00 76.34  ? 526 ASN B CA  1 
ATOM   7711  C  C   . ASN B 1 551 ? 138.190 102.877 137.780 1.00 76.05  ? 526 ASN B C   1 
ATOM   7712  O  O   . ASN B 1 551 ? 138.321 103.606 138.770 1.00 77.16  ? 526 ASN B O   1 
ATOM   7713  C  CB  . ASN B 1 551 ? 138.419 103.813 135.471 1.00 75.70  ? 526 ASN B CB  1 
ATOM   7714  C  CG  . ASN B 1 551 ? 139.364 104.731 134.732 1.00 78.76  ? 526 ASN B CG  1 
ATOM   7715  O  OD1 . ASN B 1 551 ? 140.293 105.286 135.318 1.00 78.08  ? 526 ASN B OD1 1 
ATOM   7716  N  ND2 . ASN B 1 551 ? 139.133 104.900 133.437 1.00 78.40  ? 526 ASN B ND2 1 
ATOM   7717  N  N   . ASP B 1 552 ? 137.248 101.936 137.708 1.00 66.50  ? 527 ASP B N   1 
ATOM   7718  C  CA  . ASP B 1 552 ? 136.334 101.728 138.823 1.00 63.34  ? 527 ASP B CA  1 
ATOM   7719  C  C   . ASP B 1 552 ? 137.074 101.238 140.057 1.00 67.82  ? 527 ASP B C   1 
ATOM   7720  O  O   . ASP B 1 552 ? 136.744 101.631 141.178 1.00 75.20  ? 527 ASP B O   1 
ATOM   7721  C  CB  . ASP B 1 552 ? 135.235 100.748 138.429 1.00 69.19  ? 527 ASP B CB  1 
ATOM   7722  C  CG  . ASP B 1 552 ? 134.178 101.388 137.561 1.00 74.17  ? 527 ASP B CG  1 
ATOM   7723  O  OD1 . ASP B 1 552 ? 134.504 102.366 136.860 1.00 74.51  ? 527 ASP B OD1 1 
ATOM   7724  O  OD2 . ASP B 1 552 ? 133.022 100.918 137.579 1.00 79.21  ? 527 ASP B OD2 1 
ATOM   7725  N  N   . VAL B 1 553 ? 138.077 100.378 139.874 1.00 70.31  ? 528 VAL B N   1 
ATOM   7726  C  CA  . VAL B 1 553 ? 138.855 99.906  141.016 1.00 71.00  ? 528 VAL B CA  1 
ATOM   7727  C  C   . VAL B 1 553 ? 139.622 101.057 141.651 1.00 70.95  ? 528 VAL B C   1 
ATOM   7728  O  O   . VAL B 1 553 ? 139.672 101.187 142.881 1.00 75.08  ? 528 VAL B O   1 
ATOM   7729  C  CB  . VAL B 1 553 ? 139.792 98.762  140.592 1.00 71.86  ? 528 VAL B CB  1 
ATOM   7730  C  CG1 . VAL B 1 553 ? 140.796 98.468  141.689 1.00 71.02  ? 528 VAL B CG1 1 
ATOM   7731  C  CG2 . VAL B 1 553 ? 138.986 97.520  140.262 1.00 72.37  ? 528 VAL B CG2 1 
ATOM   7732  N  N   . MET B 1 554 ? 140.227 101.917 140.827 1.00 69.20  ? 529 MET B N   1 
ATOM   7733  C  CA  . MET B 1 554 ? 140.939 103.071 141.369 1.00 71.28  ? 529 MET B CA  1 
ATOM   7734  C  C   . MET B 1 554 ? 139.998 103.989 142.139 1.00 72.29  ? 529 MET B C   1 
ATOM   7735  O  O   . MET B 1 554 ? 140.325 104.447 143.242 1.00 71.12  ? 529 MET B O   1 
ATOM   7736  C  CB  . MET B 1 554 ? 141.630 103.837 140.241 1.00 70.48  ? 529 MET B CB  1 
ATOM   7737  C  CG  . MET B 1 554 ? 142.110 105.226 140.630 1.00 73.45  ? 529 MET B CG  1 
ATOM   7738  S  SD  . MET B 1 554 ? 140.964 106.537 140.153 1.00 95.20  ? 529 MET B SD  1 
ATOM   7739  C  CE  . MET B 1 554 ? 141.683 107.086 138.609 1.00 78.81  ? 529 MET B CE  1 
ATOM   7740  N  N   . LEU B 1 555 ? 138.819 104.265 141.575 1.00 67.46  ? 530 LEU B N   1 
ATOM   7741  C  CA  . LEU B 1 555 ? 137.873 105.146 142.252 1.00 64.85  ? 530 LEU B CA  1 
ATOM   7742  C  C   . LEU B 1 555 ? 137.356 104.525 143.542 1.00 64.22  ? 530 LEU B C   1 
ATOM   7743  O  O   . LEU B 1 555 ? 137.167 105.229 144.539 1.00 68.99  ? 530 LEU B O   1 
ATOM   7744  C  CB  . LEU B 1 555 ? 136.709 105.494 141.332 1.00 58.64  ? 530 LEU B CB  1 
ATOM   7745  C  CG  . LEU B 1 555 ? 135.965 106.719 141.851 1.00 53.51  ? 530 LEU B CG  1 
ATOM   7746  C  CD1 . LEU B 1 555 ? 136.868 107.928 141.777 1.00 62.02  ? 530 LEU B CD1 1 
ATOM   7747  C  CD2 . LEU B 1 555 ? 134.695 106.957 141.082 1.00 57.59  ? 530 LEU B CD2 1 
ATOM   7748  N  N   . SER B 1 556 ? 137.097 103.217 143.538 1.00 55.41  ? 531 SER B N   1 
ATOM   7749  C  CA  . SER B 1 556 ? 136.656 102.557 144.759 1.00 48.78  ? 531 SER B CA  1 
ATOM   7750  C  C   . SER B 1 556 ? 137.728 102.628 145.831 1.00 49.28  ? 531 SER B C   1 
ATOM   7751  O  O   . SER B 1 556 ? 137.425 102.864 147.005 1.00 53.05  ? 531 SER B O   1 
ATOM   7752  C  CB  . SER B 1 556 ? 136.285 101.106 144.472 1.00 54.09  ? 531 SER B CB  1 
ATOM   7753  O  OG  . SER B 1 556 ? 136.268 100.357 145.671 1.00 55.76  ? 531 SER B OG  1 
ATOM   7754  N  N   . ALA B 1 557 ? 138.991 102.434 145.449 1.00 58.83  ? 532 ALA B N   1 
ATOM   7755  C  CA  . ALA B 1 557 ? 140.072 102.572 146.417 1.00 61.67  ? 532 ALA B CA  1 
ATOM   7756  C  C   . ALA B 1 557 ? 140.125 103.984 146.980 1.00 68.09  ? 532 ALA B C   1 
ATOM   7757  O  O   . ALA B 1 557 ? 140.283 104.170 148.191 1.00 71.52  ? 532 ALA B O   1 
ATOM   7758  C  CB  . ALA B 1 557 ? 141.406 102.199 145.775 1.00 60.92  ? 532 ALA B CB  1 
ATOM   7759  N  N   . VAL B 1 558 ? 139.971 104.993 146.120 1.00 63.89  ? 533 VAL B N   1 
ATOM   7760  C  CA  . VAL B 1 558 ? 140.033 106.380 146.581 1.00 56.67  ? 533 VAL B CA  1 
ATOM   7761  C  C   . VAL B 1 558 ? 138.892 106.677 147.550 1.00 59.32  ? 533 VAL B C   1 
ATOM   7762  O  O   . VAL B 1 558 ? 139.098 107.256 148.626 1.00 63.64  ? 533 VAL B O   1 
ATOM   7763  C  CB  . VAL B 1 558 ? 140.017 107.340 145.380 1.00 54.96  ? 533 VAL B CB  1 
ATOM   7764  C  CG1 . VAL B 1 558 ? 139.441 108.679 145.782 1.00 58.47  ? 533 VAL B CG1 1 
ATOM   7765  C  CG2 . VAL B 1 558 ? 141.415 107.505 144.828 1.00 62.78  ? 533 VAL B CG2 1 
ATOM   7766  N  N   . VAL B 1 559 ? 137.672 106.283 147.184 1.00 51.19  ? 534 VAL B N   1 
ATOM   7767  C  CA  . VAL B 1 559 ? 136.507 106.584 148.009 1.00 42.20  ? 534 VAL B CA  1 
ATOM   7768  C  C   . VAL B 1 559 ? 136.586 105.848 149.339 1.00 46.08  ? 534 VAL B C   1 
ATOM   7769  O  O   . VAL B 1 559 ? 136.272 106.409 150.396 1.00 50.97  ? 534 VAL B O   1 
ATOM   7770  C  CB  . VAL B 1 559 ? 135.218 106.247 147.243 1.00 36.45  ? 534 VAL B CB  1 
ATOM   7771  C  CG1 . VAL B 1 559 ? 134.077 106.035 148.197 1.00 48.09  ? 534 VAL B CG1 1 
ATOM   7772  C  CG2 . VAL B 1 559 ? 134.886 107.357 146.278 1.00 42.64  ? 534 VAL B CG2 1 
ATOM   7773  N  N   . MET B 1 560 ? 137.007 104.585 149.313 1.00 52.81  ? 535 MET B N   1 
ATOM   7774  C  CA  . MET B 1 560 ? 137.160 103.832 150.549 1.00 52.73  ? 535 MET B CA  1 
ATOM   7775  C  C   . MET B 1 560 ? 138.242 104.436 151.432 1.00 57.01  ? 535 MET B C   1 
ATOM   7776  O  O   . MET B 1 560 ? 138.102 104.466 152.660 1.00 62.71  ? 535 MET B O   1 
ATOM   7777  C  CB  . MET B 1 560 ? 137.461 102.373 150.219 1.00 46.44  ? 535 MET B CB  1 
ATOM   7778  C  CG  . MET B 1 560 ? 136.221 101.517 150.176 1.00 51.71  ? 535 MET B CG  1 
ATOM   7779  S  SD  . MET B 1 560 ? 136.444 99.939  149.353 1.00 68.05  ? 535 MET B SD  1 
ATOM   7780  C  CE  . MET B 1 560 ? 138.144 99.599  149.740 1.00 61.39  ? 535 MET B CE  1 
ATOM   7781  N  N   . THR B 1 561 ? 139.325 104.936 150.829 1.00 56.10  ? 536 THR B N   1 
ATOM   7782  C  CA  . THR B 1 561 ? 140.346 105.618 151.615 1.00 54.67  ? 536 THR B CA  1 
ATOM   7783  C  C   . THR B 1 561 ? 139.782 106.861 152.285 1.00 60.36  ? 536 THR B C   1 
ATOM   7784  O  O   . THR B 1 561 ? 140.048 107.111 153.464 1.00 67.49  ? 536 THR B O   1 
ATOM   7785  C  CB  . THR B 1 561 ? 141.535 105.994 150.736 1.00 56.24  ? 536 THR B CB  1 
ATOM   7786  O  OG1 . THR B 1 561 ? 142.080 104.815 150.136 1.00 69.69  ? 536 THR B OG1 1 
ATOM   7787  C  CG2 . THR B 1 561 ? 142.604 106.660 151.571 1.00 51.98  ? 536 THR B CG2 1 
ATOM   7788  N  N   . TYR B 1 562 ? 138.992 107.648 151.552 1.00 49.13  ? 537 TYR B N   1 
ATOM   7789  C  CA  . TYR B 1 562 ? 138.392 108.844 152.141 1.00 47.62  ? 537 TYR B CA  1 
ATOM   7790  C  C   . TYR B 1 562 ? 137.483 108.480 153.309 1.00 50.31  ? 537 TYR B C   1 
ATOM   7791  O  O   . TYR B 1 562 ? 137.573 109.068 154.395 1.00 57.90  ? 537 TYR B O   1 
ATOM   7792  C  CB  . TYR B 1 562 ? 137.611 109.619 151.081 1.00 49.87  ? 537 TYR B CB  1 
ATOM   7793  C  CG  . TYR B 1 562 ? 138.455 110.551 150.250 1.00 49.90  ? 537 TYR B CG  1 
ATOM   7794  C  CD1 . TYR B 1 562 ? 139.527 111.224 150.804 1.00 52.12  ? 537 TYR B CD1 1 
ATOM   7795  C  CD2 . TYR B 1 562 ? 138.179 110.755 148.909 1.00 49.89  ? 537 TYR B CD2 1 
ATOM   7796  C  CE1 . TYR B 1 562 ? 140.300 112.073 150.050 1.00 49.88  ? 537 TYR B CE1 1 
ATOM   7797  C  CE2 . TYR B 1 562 ? 138.947 111.601 148.147 1.00 47.95  ? 537 TYR B CE2 1 
ATOM   7798  C  CZ  . TYR B 1 562 ? 140.006 112.257 148.723 1.00 51.06  ? 537 TYR B CZ  1 
ATOM   7799  O  OH  . TYR B 1 562 ? 140.779 113.105 147.971 1.00 63.55  ? 537 TYR B OH  1 
ATOM   7800  N  N   . TRP B 1 563 ? 136.606 107.497 153.103 1.00 38.50  ? 538 TRP B N   1 
ATOM   7801  C  CA  . TRP B 1 563 ? 135.660 107.111 154.145 1.00 40.11  ? 538 TRP B CA  1 
ATOM   7802  C  C   . TRP B 1 563 ? 136.378 106.582 155.380 1.00 46.78  ? 538 TRP B C   1 
ATOM   7803  O  O   . TRP B 1 563 ? 136.043 106.952 156.511 1.00 57.79  ? 538 TRP B O   1 
ATOM   7804  C  CB  . TRP B 1 563 ? 134.692 106.060 153.605 1.00 42.62  ? 538 TRP B CB  1 
ATOM   7805  C  CG  . TRP B 1 563 ? 133.422 106.588 152.993 1.00 41.56  ? 538 TRP B CG  1 
ATOM   7806  C  CD1 . TRP B 1 563 ? 132.168 106.112 153.209 1.00 41.93  ? 538 TRP B CD1 1 
ATOM   7807  C  CD2 . TRP B 1 563 ? 133.283 107.660 152.047 1.00 45.92  ? 538 TRP B CD2 1 
ATOM   7808  N  NE1 . TRP B 1 563 ? 131.256 106.823 152.475 1.00 50.00  ? 538 TRP B NE1 1 
ATOM   7809  C  CE2 . TRP B 1 563 ? 131.916 107.778 151.752 1.00 41.00  ? 538 TRP B CE2 1 
ATOM   7810  C  CE3 . TRP B 1 563 ? 134.179 108.533 151.428 1.00 46.81  ? 538 TRP B CE3 1 
ATOM   7811  C  CZ2 . TRP B 1 563 ? 131.427 108.728 150.870 1.00 34.86  ? 538 TRP B CZ2 1 
ATOM   7812  C  CZ3 . TRP B 1 563 ? 133.688 109.475 150.554 1.00 39.78  ? 538 TRP B CZ3 1 
ATOM   7813  C  CH2 . TRP B 1 563 ? 132.328 109.565 150.282 1.00 36.58  ? 538 TRP B CH2 1 
ATOM   7814  N  N   . THR B 1 564 ? 137.377 105.718 155.187 1.00 44.21  ? 539 THR B N   1 
ATOM   7815  C  CA  . THR B 1 564 ? 138.071 105.142 156.331 1.00 44.15  ? 539 THR B CA  1 
ATOM   7816  C  C   . THR B 1 564 ? 138.942 106.169 157.041 1.00 53.34  ? 539 THR B C   1 
ATOM   7817  O  O   . THR B 1 564 ? 139.079 106.110 158.267 1.00 55.59  ? 539 THR B O   1 
ATOM   7818  C  CB  . THR B 1 564 ? 138.900 103.942 155.890 1.00 50.24  ? 539 THR B CB  1 
ATOM   7819  O  OG1 . THR B 1 564 ? 139.741 104.318 154.796 1.00 62.50  ? 539 THR B OG1 1 
ATOM   7820  C  CG2 . THR B 1 564 ? 137.987 102.820 155.448 1.00 48.80  ? 539 THR B CG2 1 
ATOM   7821  N  N   . ASN B 1 565 ? 139.525 107.122 156.309 1.00 59.25  ? 540 ASN B N   1 
ATOM   7822  C  CA  . ASN B 1 565 ? 140.226 108.219 156.967 1.00 58.92  ? 540 ASN B CA  1 
ATOM   7823  C  C   . ASN B 1 565 ? 139.271 109.033 157.826 1.00 62.76  ? 540 ASN B C   1 
ATOM   7824  O  O   . ASN B 1 565 ? 139.608 109.416 158.954 1.00 65.71  ? 540 ASN B O   1 
ATOM   7825  C  CB  . ASN B 1 565 ? 140.897 109.115 155.931 1.00 56.76  ? 540 ASN B CB  1 
ATOM   7826  C  CG  . ASN B 1 565 ? 142.106 108.474 155.306 1.00 64.81  ? 540 ASN B CG  1 
ATOM   7827  O  OD1 . ASN B 1 565 ? 142.575 107.437 155.764 1.00 70.79  ? 540 ASN B OD1 1 
ATOM   7828  N  ND2 . ASN B 1 565 ? 142.626 109.090 154.254 1.00 66.61  ? 540 ASN B ND2 1 
ATOM   7829  N  N   . PHE B 1 566 ? 138.072 109.310 157.306 1.00 50.74  ? 541 PHE B N   1 
ATOM   7830  C  CA  . PHE B 1 566 ? 137.084 110.029 158.101 1.00 45.47  ? 541 PHE B CA  1 
ATOM   7831  C  C   . PHE B 1 566 ? 136.721 109.248 159.355 1.00 50.80  ? 541 PHE B C   1 
ATOM   7832  O  O   . PHE B 1 566 ? 136.582 109.826 160.437 1.00 58.01  ? 541 PHE B O   1 
ATOM   7833  C  CB  . PHE B 1 566 ? 135.834 110.308 157.272 1.00 44.30  ? 541 PHE B CB  1 
ATOM   7834  C  CG  . PHE B 1 566 ? 134.813 111.133 157.989 1.00 43.12  ? 541 PHE B CG  1 
ATOM   7835  C  CD1 . PHE B 1 566 ? 134.905 112.508 158.001 1.00 43.61  ? 541 PHE B CD1 1 
ATOM   7836  C  CD2 . PHE B 1 566 ? 133.768 110.533 158.659 1.00 44.25  ? 541 PHE B CD2 1 
ATOM   7837  C  CE1 . PHE B 1 566 ? 133.975 113.266 158.661 1.00 41.46  ? 541 PHE B CE1 1 
ATOM   7838  C  CE2 . PHE B 1 566 ? 132.837 111.288 159.323 1.00 47.58  ? 541 PHE B CE2 1 
ATOM   7839  C  CZ  . PHE B 1 566 ? 132.940 112.656 159.323 1.00 47.62  ? 541 PHE B CZ  1 
ATOM   7840  N  N   . ALA B 1 567 ? 136.560 107.932 159.227 1.00 47.06  ? 542 ALA B N   1 
ATOM   7841  C  CA  . ALA B 1 567 ? 136.263 107.117 160.399 1.00 39.88  ? 542 ALA B CA  1 
ATOM   7842  C  C   . ALA B 1 567 ? 137.398 107.176 161.411 1.00 49.69  ? 542 ALA B C   1 
ATOM   7843  O  O   . ALA B 1 567 ? 137.157 107.241 162.621 1.00 57.27  ? 542 ALA B O   1 
ATOM   7844  C  CB  . ALA B 1 567 ? 135.994 105.673 159.986 1.00 44.49  ? 542 ALA B CB  1 
ATOM   7845  N  N   . LYS B 1 568 ? 138.643 107.152 160.933 1.00 54.98  ? 543 LYS B N   1 
ATOM   7846  C  CA  . LYS B 1 568 ? 139.788 107.126 161.839 1.00 52.93  ? 543 LYS B CA  1 
ATOM   7847  C  C   . LYS B 1 568 ? 139.943 108.442 162.590 1.00 55.66  ? 543 LYS B C   1 
ATOM   7848  O  O   . LYS B 1 568 ? 140.098 108.450 163.815 1.00 58.85  ? 543 LYS B O   1 
ATOM   7849  C  CB  . LYS B 1 568 ? 141.066 106.809 161.063 1.00 55.59  ? 543 LYS B CB  1 
ATOM   7850  C  CG  . LYS B 1 568 ? 141.195 105.368 160.615 1.00 58.50  ? 543 LYS B CG  1 
ATOM   7851  C  CD  . LYS B 1 568 ? 142.371 105.204 159.677 1.00 57.09  ? 543 LYS B CD  1 
ATOM   7852  C  CE  . LYS B 1 568 ? 142.366 103.841 159.032 1.00 53.02  ? 543 LYS B CE  1 
ATOM   7853  N  NZ  . LYS B 1 568 ? 143.267 103.798 157.854 1.00 56.30  ? 543 LYS B NZ  1 
ATOM   7854  N  N   . THR B 1 569 ? 139.903 109.571 161.876 1.00 66.04  ? 544 THR B N   1 
ATOM   7855  C  CA  . THR B 1 569 ? 140.275 110.843 162.482 1.00 63.42  ? 544 THR B CA  1 
ATOM   7856  C  C   . THR B 1 569 ? 139.300 111.989 162.249 1.00 64.50  ? 544 THR B C   1 
ATOM   7857  O  O   . THR B 1 569 ? 139.590 113.110 162.678 1.00 66.85  ? 544 THR B O   1 
ATOM   7858  C  CB  . THR B 1 569 ? 141.654 111.284 161.982 1.00 63.02  ? 544 THR B CB  1 
ATOM   7859  O  OG1 . THR B 1 569 ? 142.054 112.469 162.679 1.00 74.27  ? 544 THR B OG1 1 
ATOM   7860  C  CG2 . THR B 1 569 ? 141.596 111.586 160.504 1.00 59.17  ? 544 THR B CG2 1 
ATOM   7861  N  N   . GLY B 1 570 ? 138.171 111.758 161.588 1.00 64.23  ? 545 GLY B N   1 
ATOM   7862  C  CA  . GLY B 1 570 ? 137.254 112.850 161.328 1.00 63.10  ? 545 GLY B CA  1 
ATOM   7863  C  C   . GLY B 1 570 ? 137.738 113.847 160.303 1.00 65.75  ? 545 GLY B C   1 
ATOM   7864  O  O   . GLY B 1 570 ? 137.260 114.982 160.283 1.00 69.38  ? 545 GLY B O   1 
ATOM   7865  N  N   . ASP B 1 571 ? 138.673 113.453 159.451 1.00 65.93  ? 546 ASP B N   1 
ATOM   7866  C  CA  . ASP B 1 571 ? 139.256 114.320 158.440 1.00 65.27  ? 546 ASP B CA  1 
ATOM   7867  C  C   . ASP B 1 571 ? 139.721 113.453 157.278 1.00 73.45  ? 546 ASP B C   1 
ATOM   7868  O  O   . ASP B 1 571 ? 140.644 112.649 157.442 1.00 85.56  ? 546 ASP B O   1 
ATOM   7869  C  CB  . ASP B 1 571 ? 140.416 115.120 159.033 1.00 67.71  ? 546 ASP B CB  1 
ATOM   7870  C  CG  . ASP B 1 571 ? 140.839 116.277 158.159 1.00 75.99  ? 546 ASP B CG  1 
ATOM   7871  O  OD1 . ASP B 1 571 ? 140.246 116.457 157.077 1.00 79.79  ? 546 ASP B OD1 1 
ATOM   7872  O  OD2 . ASP B 1 571 ? 141.766 117.013 158.557 1.00 80.13  ? 546 ASP B OD2 1 
ATOM   7873  N  N   . PRO B 1 572 ? 139.124 113.586 156.094 1.00 59.07  ? 547 PRO B N   1 
ATOM   7874  C  CA  . PRO B 1 572 ? 139.381 112.614 155.023 1.00 63.78  ? 547 PRO B CA  1 
ATOM   7875  C  C   . PRO B 1 572 ? 140.777 112.677 154.422 1.00 70.15  ? 547 PRO B C   1 
ATOM   7876  O  O   . PRO B 1 572 ? 141.041 112.016 153.414 1.00 72.04  ? 547 PRO B O   1 
ATOM   7877  C  CB  . PRO B 1 572 ? 138.322 112.971 153.974 1.00 53.83  ? 547 PRO B CB  1 
ATOM   7878  C  CG  . PRO B 1 572 ? 137.288 113.717 154.711 1.00 54.41  ? 547 PRO B CG  1 
ATOM   7879  C  CD  . PRO B 1 572 ? 138.026 114.494 155.743 1.00 57.34  ? 547 PRO B CD  1 
ATOM   7880  N  N   . ASN B 1 573 ? 141.682 113.454 155.013 1.00 74.38  ? 548 ASN B N   1 
ATOM   7881  C  CA  . ASN B 1 573 ? 143.017 113.609 154.459 1.00 75.08  ? 548 ASN B CA  1 
ATOM   7882  C  C   . ASN B 1 573 ? 144.140 113.085 155.340 1.00 75.79  ? 548 ASN B C   1 
ATOM   7883  O  O   . ASN B 1 573 ? 145.199 112.741 154.806 1.00 77.60  ? 548 ASN B O   1 
ATOM   7884  C  CB  . ASN B 1 573 ? 143.300 115.088 154.157 1.00 72.96  ? 548 ASN B CB  1 
ATOM   7885  C  CG  . ASN B 1 573 ? 142.154 115.761 153.450 1.00 69.69  ? 548 ASN B CG  1 
ATOM   7886  O  OD1 . ASN B 1 573 ? 141.471 116.610 154.020 1.00 66.24  ? 548 ASN B OD1 1 
ATOM   7887  N  ND2 . ASN B 1 573 ? 141.933 115.385 152.198 1.00 70.74  ? 548 ASN B ND2 1 
ATOM   7888  N  N   . GLN B 1 574 ? 143.951 113.013 156.653 1.00 78.65  ? 549 GLN B N   1 
ATOM   7889  C  CA  . GLN B 1 574 ? 145.097 112.879 157.544 1.00 83.52  ? 549 GLN B CA  1 
ATOM   7890  C  C   . GLN B 1 574 ? 145.789 111.517 157.469 1.00 90.06  ? 549 GLN B C   1 
ATOM   7891  O  O   . GLN B 1 574 ? 146.935 111.448 157.005 1.00 89.13  ? 549 GLN B O   1 
ATOM   7892  C  CB  . GLN B 1 574 ? 144.676 113.184 158.985 1.00 75.69  ? 549 GLN B CB  1 
ATOM   7893  N  N   . PRO B 1 575 ? 145.153 110.412 157.898 1.00 83.97  ? 550 PRO B N   1 
ATOM   7894  C  CA  . PRO B 1 575 ? 145.934 109.201 158.196 1.00 77.97  ? 550 PRO B CA  1 
ATOM   7895  C  C   . PRO B 1 575 ? 146.589 108.552 156.987 1.00 79.90  ? 550 PRO B C   1 
ATOM   7896  O  O   . PRO B 1 575 ? 147.807 108.355 156.975 1.00 82.14  ? 550 PRO B O   1 
ATOM   7897  C  CB  . PRO B 1 575 ? 144.899 108.258 158.829 1.00 72.87  ? 550 PRO B CB  1 
ATOM   7898  C  CG  . PRO B 1 575 ? 143.652 109.072 159.002 1.00 77.54  ? 550 PRO B CG  1 
ATOM   7899  C  CD  . PRO B 1 575 ? 143.712 110.137 157.971 1.00 76.48  ? 550 PRO B CD  1 
ATOM   7900  N  N   . VAL B 1 576 ? 145.807 108.222 155.966 1.00 83.26  ? 551 VAL B N   1 
ATOM   7901  C  CA  . VAL B 1 576 ? 146.300 107.468 154.821 1.00 82.09  ? 551 VAL B CA  1 
ATOM   7902  C  C   . VAL B 1 576 ? 146.314 108.399 153.611 1.00 82.19  ? 551 VAL B C   1 
ATOM   7903  O  O   . VAL B 1 576 ? 145.246 108.743 153.083 1.00 84.94  ? 551 VAL B O   1 
ATOM   7904  C  CB  . VAL B 1 576 ? 145.446 106.223 154.551 1.00 80.35  ? 551 VAL B CB  1 
ATOM   7905  C  CG1 . VAL B 1 576 ? 145.951 105.497 153.317 1.00 78.46  ? 551 VAL B CG1 1 
ATOM   7906  C  CG2 . VAL B 1 576 ? 145.457 105.305 155.756 1.00 77.64  ? 551 VAL B CG2 1 
ATOM   7907  N  N   . PRO B 1 577 ? 147.479 108.827 153.137 1.00 82.64  ? 552 PRO B N   1 
ATOM   7908  C  CA  . PRO B 1 577 ? 147.523 109.616 151.904 1.00 81.67  ? 552 PRO B CA  1 
ATOM   7909  C  C   . PRO B 1 577 ? 147.101 108.780 150.709 1.00 81.27  ? 552 PRO B C   1 
ATOM   7910  O  O   . PRO B 1 577 ? 147.188 107.550 150.718 1.00 84.80  ? 552 PRO B O   1 
ATOM   7911  C  CB  . PRO B 1 577 ? 148.994 110.034 151.800 1.00 80.82  ? 552 PRO B CB  1 
ATOM   7912  C  CG  . PRO B 1 577 ? 149.732 109.010 152.594 1.00 79.94  ? 552 PRO B CG  1 
ATOM   7913  C  CD  . PRO B 1 577 ? 148.817 108.630 153.718 1.00 81.43  ? 552 PRO B CD  1 
ATOM   7914  N  N   . GLN B 1 578 ? 146.624 109.465 149.677 1.00 75.89  ? 553 GLN B N   1 
ATOM   7915  C  CA  . GLN B 1 578 ? 146.153 108.794 148.472 1.00 78.43  ? 553 GLN B CA  1 
ATOM   7916  C  C   . GLN B 1 578 ? 147.291 108.081 147.749 1.00 79.25  ? 553 GLN B C   1 
ATOM   7917  O  O   . GLN B 1 578 ? 147.478 108.256 146.546 1.00 81.54  ? 553 GLN B O   1 
ATOM   7918  C  CB  . GLN B 1 578 ? 145.487 109.796 147.533 1.00 80.60  ? 553 GLN B CB  1 
ATOM   7919  C  CG  . GLN B 1 578 ? 144.242 110.436 148.107 1.00 77.93  ? 553 GLN B CG  1 
ATOM   7920  C  CD  . GLN B 1 578 ? 143.203 109.420 148.507 1.00 77.19  ? 553 GLN B CD  1 
ATOM   7921  O  OE1 . GLN B 1 578 ? 142.713 108.656 147.677 1.00 78.90  ? 553 GLN B OE1 1 
ATOM   7922  N  NE2 . GLN B 1 578 ? 142.854 109.407 149.784 1.00 75.72  ? 553 GLN B NE2 1 
ATOM   7923  N  N   . ARG B 1 589 ? 145.638 111.961 140.180 1.00 88.45  ? 564 ARG B N   1 
ATOM   7924  C  CA  . ARG B 1 589 ? 144.849 113.182 140.268 1.00 88.90  ? 564 ARG B CA  1 
ATOM   7925  C  C   . ARG B 1 589 ? 144.410 113.455 141.699 1.00 92.69  ? 564 ARG B C   1 
ATOM   7926  O  O   . ARG B 1 589 ? 144.106 114.591 142.060 1.00 92.63  ? 564 ARG B O   1 
ATOM   7927  C  CB  . ARG B 1 589 ? 143.623 113.095 139.361 1.00 84.66  ? 564 ARG B CB  1 
ATOM   7928  C  CG  . ARG B 1 589 ? 143.946 113.113 137.881 1.00 88.10  ? 564 ARG B CG  1 
ATOM   7929  C  CD  . ARG B 1 589 ? 142.963 112.270 137.091 1.00 91.83  ? 564 ARG B CD  1 
ATOM   7930  N  NE  . ARG B 1 589 ? 142.848 112.726 135.712 1.00 92.48  ? 564 ARG B NE  1 
ATOM   7931  C  CZ  . ARG B 1 589 ? 142.385 111.986 134.714 1.00 91.45  ? 564 ARG B CZ  1 
ATOM   7932  N  NH1 . ARG B 1 589 ? 141.986 110.739 134.905 1.00 89.70  ? 564 ARG B NH1 1 
ATOM   7933  N  NH2 . ARG B 1 589 ? 142.320 112.510 133.494 1.00 90.57  ? 564 ARG B NH2 1 
ATOM   7934  N  N   . PHE B 1 590 ? 144.387 112.406 142.513 1.00 88.82  ? 565 PHE B N   1 
ATOM   7935  C  CA  . PHE B 1 590 ? 143.845 112.482 143.861 1.00 89.43  ? 565 PHE B CA  1 
ATOM   7936  C  C   . PHE B 1 590 ? 144.888 112.825 144.917 1.00 87.27  ? 565 PHE B C   1 
ATOM   7937  O  O   . PHE B 1 590 ? 144.541 112.908 146.098 1.00 86.43  ? 565 PHE B O   1 
ATOM   7938  C  CB  . PHE B 1 590 ? 143.164 111.160 144.220 1.00 88.93  ? 565 PHE B CB  1 
ATOM   7939  C  CG  . PHE B 1 590 ? 141.749 111.057 143.730 1.00 91.80  ? 565 PHE B CG  1 
ATOM   7940  C  CD1 . PHE B 1 590 ? 140.729 111.742 144.366 1.00 87.61  ? 565 PHE B CD1 1 
ATOM   7941  C  CD2 . PHE B 1 590 ? 141.439 110.280 142.628 1.00 87.31  ? 565 PHE B CD2 1 
ATOM   7942  C  CE1 . PHE B 1 590 ? 139.428 111.645 143.920 1.00 83.52  ? 565 PHE B CE1 1 
ATOM   7943  C  CE2 . PHE B 1 590 ? 140.138 110.184 142.176 1.00 87.49  ? 565 PHE B CE2 1 
ATOM   7944  C  CZ  . PHE B 1 590 ? 139.133 110.868 142.823 1.00 86.18  ? 565 PHE B CZ  1 
ATOM   7945  N  N   . GLU B 1 591 ? 146.147 113.025 144.532 1.00 89.05  ? 566 GLU B N   1 
ATOM   7946  C  CA  . GLU B 1 591 ? 147.178 113.356 145.507 1.00 89.55  ? 566 GLU B CA  1 
ATOM   7947  C  C   . GLU B 1 591 ? 147.298 114.851 145.759 1.00 89.38  ? 566 GLU B C   1 
ATOM   7948  O  O   . GLU B 1 591 ? 147.628 115.257 146.879 1.00 90.62  ? 566 GLU B O   1 
ATOM   7949  C  CB  . GLU B 1 591 ? 148.536 112.812 145.055 1.00 90.54  ? 566 GLU B CB  1 
ATOM   7950  C  CG  . GLU B 1 591 ? 148.534 111.343 144.670 1.00 89.97  ? 566 GLU B CG  1 
ATOM   7951  C  CD  . GLU B 1 591 ? 148.339 111.133 143.182 1.00 91.57  ? 566 GLU B CD  1 
ATOM   7952  O  OE1 . GLU B 1 591 ? 147.793 112.039 142.521 1.00 92.55  ? 566 GLU B OE1 1 
ATOM   7953  O  OE2 . GLU B 1 591 ? 148.734 110.063 142.674 1.00 90.88  ? 566 GLU B OE2 1 
ATOM   7954  N  N   . GLU B 1 592 ? 147.043 115.680 144.747 1.00 89.28  ? 567 GLU B N   1 
ATOM   7955  C  CA  . GLU B 1 592 ? 147.186 117.123 144.891 1.00 93.48  ? 567 GLU B CA  1 
ATOM   7956  C  C   . GLU B 1 592 ? 145.949 117.798 145.466 1.00 94.32  ? 567 GLU B C   1 
ATOM   7957  O  O   . GLU B 1 592 ? 146.023 118.978 145.826 1.00 90.65  ? 567 GLU B O   1 
ATOM   7958  C  CB  . GLU B 1 592 ? 147.523 117.753 143.537 1.00 91.57  ? 567 GLU B CB  1 
ATOM   7959  N  N   . VAL B 1 593 ? 144.828 117.090 145.568 1.00 88.83  ? 568 VAL B N   1 
ATOM   7960  C  CA  . VAL B 1 593 ? 143.572 117.677 146.019 1.00 82.05  ? 568 VAL B CA  1 
ATOM   7961  C  C   . VAL B 1 593 ? 143.480 117.562 147.533 1.00 78.99  ? 568 VAL B C   1 
ATOM   7962  O  O   . VAL B 1 593 ? 143.651 116.476 148.098 1.00 78.93  ? 568 VAL B O   1 
ATOM   7963  C  CB  . VAL B 1 593 ? 142.372 117.000 145.337 1.00 78.38  ? 568 VAL B CB  1 
ATOM   7964  C  CG1 . VAL B 1 593 ? 142.279 117.436 143.889 1.00 80.04  ? 568 VAL B CG1 1 
ATOM   7965  C  CG2 . VAL B 1 593 ? 142.492 115.493 145.419 1.00 75.88  ? 568 VAL B CG2 1 
ATOM   7966  N  N   . VAL B 1 594 ? 143.218 118.685 148.193 1.00 69.16  ? 569 VAL B N   1 
ATOM   7967  C  CA  . VAL B 1 594 ? 143.021 118.727 149.636 1.00 70.22  ? 569 VAL B CA  1 
ATOM   7968  C  C   . VAL B 1 594 ? 141.556 119.038 149.890 1.00 71.57  ? 569 VAL B C   1 
ATOM   7969  O  O   . VAL B 1 594 ? 141.063 120.104 149.502 1.00 74.11  ? 569 VAL B O   1 
ATOM   7970  C  CB  . VAL B 1 594 ? 143.931 119.766 150.304 1.00 68.58  ? 569 VAL B CB  1 
ATOM   7971  C  CG1 . VAL B 1 594 ? 143.805 119.684 151.812 1.00 66.83  ? 569 VAL B CG1 1 
ATOM   7972  C  CG2 . VAL B 1 594 ? 145.368 119.554 149.879 1.00 71.43  ? 569 VAL B CG2 1 
ATOM   7973  N  N   . TRP B 1 595 ? 140.859 118.111 150.537 1.00 56.10  ? 570 TRP B N   1 
ATOM   7974  C  CA  . TRP B 1 595 ? 139.448 118.307 150.828 1.00 49.53  ? 570 TRP B CA  1 
ATOM   7975  C  C   . TRP B 1 595 ? 139.286 119.334 151.940 1.00 55.38  ? 570 TRP B C   1 
ATOM   7976  O  O   . TRP B 1 595 ? 139.915 119.224 152.996 1.00 54.34  ? 570 TRP B O   1 
ATOM   7977  C  CB  . TRP B 1 595 ? 138.811 116.981 151.222 1.00 52.04  ? 570 TRP B CB  1 
ATOM   7978  C  CG  . TRP B 1 595 ? 137.344 116.933 151.007 1.00 50.71  ? 570 TRP B CG  1 
ATOM   7979  C  CD1 . TRP B 1 595 ? 136.517 117.986 150.778 1.00 52.07  ? 570 TRP B CD1 1 
ATOM   7980  C  CD2 . TRP B 1 595 ? 136.519 115.766 151.001 1.00 46.22  ? 570 TRP B CD2 1 
ATOM   7981  N  NE1 . TRP B 1 595 ? 135.228 117.550 150.632 1.00 50.22  ? 570 TRP B NE1 1 
ATOM   7982  C  CE2 . TRP B 1 595 ? 135.205 116.188 150.764 1.00 46.78  ? 570 TRP B CE2 1 
ATOM   7983  C  CE3 . TRP B 1 595 ? 136.766 114.406 151.173 1.00 51.07  ? 570 TRP B CE3 1 
ATOM   7984  C  CZ2 . TRP B 1 595 ? 134.144 115.302 150.696 1.00 51.02  ? 570 TRP B CZ2 1 
ATOM   7985  C  CZ3 . TRP B 1 595 ? 135.712 113.530 151.104 1.00 50.79  ? 570 TRP B CZ3 1 
ATOM   7986  C  CH2 . TRP B 1 595 ? 134.419 113.978 150.868 1.00 48.96  ? 570 TRP B CH2 1 
ATOM   7987  N  N   . SER B 1 596 ? 138.435 120.330 151.706 1.00 58.99  ? 571 SER B N   1 
ATOM   7988  C  CA  . SER B 1 596 ? 138.274 121.459 152.608 1.00 57.70  ? 571 SER B CA  1 
ATOM   7989  C  C   . SER B 1 596 ? 136.891 121.451 153.244 1.00 55.33  ? 571 SER B C   1 
ATOM   7990  O  O   . SER B 1 596 ? 135.926 120.942 152.669 1.00 58.86  ? 571 SER B O   1 
ATOM   7991  C  CB  . SER B 1 596 ? 138.489 122.781 151.872 1.00 54.48  ? 571 SER B CB  1 
ATOM   7992  O  OG  . SER B 1 596 ? 139.819 122.890 151.401 1.00 61.43  ? 571 SER B OG  1 
ATOM   7993  N  N   . LYS B 1 597 ? 136.808 122.030 154.438 1.00 44.81  ? 572 LYS B N   1 
ATOM   7994  C  CA  . LYS B 1 597 ? 135.549 122.081 155.165 1.00 42.08  ? 572 LYS B CA  1 
ATOM   7995  C  C   . LYS B 1 597 ? 134.512 122.885 154.393 1.00 47.11  ? 572 LYS B C   1 
ATOM   7996  O  O   . LYS B 1 597 ? 134.826 123.874 153.729 1.00 59.15  ? 572 LYS B O   1 
ATOM   7997  C  CB  . LYS B 1 597 ? 135.752 122.706 156.543 1.00 39.74  ? 572 LYS B CB  1 
ATOM   7998  C  CG  . LYS B 1 597 ? 136.612 121.898 157.487 1.00 48.85  ? 572 LYS B CG  1 
ATOM   7999  C  CD  . LYS B 1 597 ? 136.113 122.049 158.911 1.00 51.15  ? 572 LYS B CD  1 
ATOM   8000  C  CE  . LYS B 1 597 ? 137.227 121.871 159.921 1.00 50.54  ? 572 LYS B CE  1 
ATOM   8001  N  NZ  . LYS B 1 597 ? 136.882 122.502 161.223 1.00 50.90  ? 572 LYS B NZ  1 
ATOM   8002  N  N   . PHE B 1 598 ? 133.261 122.453 154.492 1.00 39.01  ? 573 PHE B N   1 
ATOM   8003  C  CA  . PHE B 1 598 ? 132.144 123.154 153.867 1.00 39.35  ? 573 PHE B CA  1 
ATOM   8004  C  C   . PHE B 1 598 ? 131.786 124.346 154.741 1.00 47.90  ? 573 PHE B C   1 
ATOM   8005  O  O   . PHE B 1 598 ? 131.063 124.213 155.729 1.00 50.33  ? 573 PHE B O   1 
ATOM   8006  C  CB  . PHE B 1 598 ? 130.959 122.213 153.692 1.00 45.71  ? 573 PHE B CB  1 
ATOM   8007  C  CG  . PHE B 1 598 ? 129.759 122.846 153.053 1.00 39.12  ? 573 PHE B CG  1 
ATOM   8008  C  CD1 . PHE B 1 598 ? 128.786 123.448 153.821 1.00 34.64  ? 573 PHE B CD1 1 
ATOM   8009  C  CD2 . PHE B 1 598 ? 129.593 122.814 151.689 1.00 43.66  ? 573 PHE B CD2 1 
ATOM   8010  C  CE1 . PHE B 1 598 ? 127.685 124.016 153.237 1.00 37.88  ? 573 PHE B CE1 1 
ATOM   8011  C  CE2 . PHE B 1 598 ? 128.491 123.381 151.104 1.00 40.24  ? 573 PHE B CE2 1 
ATOM   8012  C  CZ  . PHE B 1 598 ? 127.538 123.984 151.880 1.00 42.20  ? 573 PHE B CZ  1 
ATOM   8013  N  N   . ASN B 1 599 ? 132.301 125.518 154.387 1.00 60.77  ? 574 ASN B N   1 
ATOM   8014  C  CA  . ASN B 1 599 ? 131.962 126.746 155.090 1.00 61.10  ? 574 ASN B CA  1 
ATOM   8015  C  C   . ASN B 1 599 ? 130.727 127.371 154.459 1.00 59.89  ? 574 ASN B C   1 
ATOM   8016  O  O   . ASN B 1 599 ? 130.542 127.314 153.242 1.00 61.00  ? 574 ASN B O   1 
ATOM   8017  C  CB  . ASN B 1 599 ? 133.130 127.732 155.056 1.00 55.88  ? 574 ASN B CB  1 
ATOM   8018  N  N   . SER B 1 600 ? 129.876 127.961 155.298 1.00 59.53  ? 575 SER B N   1 
ATOM   8019  C  CA  . SER B 1 600 ? 128.647 128.559 154.792 1.00 57.56  ? 575 SER B CA  1 
ATOM   8020  C  C   . SER B 1 600 ? 128.938 129.727 153.860 1.00 64.00  ? 575 SER B C   1 
ATOM   8021  O  O   . SER B 1 600 ? 128.248 129.911 152.851 1.00 69.06  ? 575 SER B O   1 
ATOM   8022  C  CB  . SER B 1 600 ? 127.769 129.009 155.956 1.00 58.16  ? 575 SER B CB  1 
ATOM   8023  O  OG  . SER B 1 600 ? 126.650 129.738 155.491 1.00 62.41  ? 575 SER B OG  1 
ATOM   8024  N  N   . LYS B 1 601 ? 129.953 130.532 154.182 1.00 71.06  ? 576 LYS B N   1 
ATOM   8025  C  CA  . LYS B 1 601 ? 130.264 131.707 153.373 1.00 68.44  ? 576 LYS B CA  1 
ATOM   8026  C  C   . LYS B 1 601 ? 130.758 131.313 151.987 1.00 65.33  ? 576 LYS B C   1 
ATOM   8027  O  O   . LYS B 1 601 ? 130.284 131.842 150.975 1.00 63.33  ? 576 LYS B O   1 
ATOM   8028  C  CB  . LYS B 1 601 ? 131.299 132.571 154.090 1.00 71.09  ? 576 LYS B CB  1 
ATOM   8029  C  CG  . LYS B 1 601 ? 130.994 132.800 155.561 1.00 73.33  ? 576 LYS B CG  1 
ATOM   8030  C  CD  . LYS B 1 601 ? 132.262 132.790 156.400 1.00 74.02  ? 576 LYS B CD  1 
ATOM   8031  C  CE  . LYS B 1 601 ? 133.343 133.662 155.782 1.00 73.39  ? 576 LYS B CE  1 
ATOM   8032  N  NZ  . LYS B 1 601 ? 134.705 133.122 156.040 1.00 72.64  ? 576 LYS B NZ  1 
ATOM   8033  N  N   . GLU B 1 602 ? 131.715 130.392 151.920 1.00 65.39  ? 577 GLU B N   1 
ATOM   8034  C  CA  . GLU B 1 602 ? 132.201 129.837 150.661 1.00 66.46  ? 577 GLU B CA  1 
ATOM   8035  C  C   . GLU B 1 602 ? 131.976 128.332 150.704 1.00 72.20  ? 577 GLU B C   1 
ATOM   8036  O  O   . GLU B 1 602 ? 132.655 127.620 151.450 1.00 76.55  ? 577 GLU B O   1 
ATOM   8037  C  CB  . GLU B 1 602 ? 133.674 130.166 150.442 1.00 66.78  ? 577 GLU B CB  1 
ATOM   8038  C  CG  . GLU B 1 602 ? 134.270 129.476 149.235 1.00 67.89  ? 577 GLU B CG  1 
ATOM   8039  C  CD  . GLU B 1 602 ? 135.685 129.929 148.941 1.00 75.15  ? 577 GLU B CD  1 
ATOM   8040  O  OE1 . GLU B 1 602 ? 136.211 130.770 149.699 1.00 74.84  ? 577 GLU B OE1 1 
ATOM   8041  O  OE2 . GLU B 1 602 ? 136.271 129.443 147.951 1.00 76.74  ? 577 GLU B OE2 1 
ATOM   8042  N  N   . LYS B 1 603 ? 131.031 127.848 149.900 1.00 56.03  ? 578 LYS B N   1 
ATOM   8043  C  CA  . LYS B 1 603 ? 130.560 126.468 150.002 1.00 52.39  ? 578 LYS B CA  1 
ATOM   8044  C  C   . LYS B 1 603 ? 131.507 125.530 149.255 1.00 54.86  ? 578 LYS B C   1 
ATOM   8045  O  O   . LYS B 1 603 ? 131.196 124.975 148.201 1.00 56.51  ? 578 LYS B O   1 
ATOM   8046  C  CB  . LYS B 1 603 ? 129.136 126.364 149.479 1.00 57.82  ? 578 LYS B CB  1 
ATOM   8047  C  CG  . LYS B 1 603 ? 128.177 127.355 150.119 1.00 55.90  ? 578 LYS B CG  1 
ATOM   8048  C  CD  . LYS B 1 603 ? 126.769 127.188 149.580 1.00 55.02  ? 578 LYS B CD  1 
ATOM   8049  C  CE  . LYS B 1 603 ? 125.925 128.398 149.896 1.00 46.94  ? 578 LYS B CE  1 
ATOM   8050  N  NZ  . LYS B 1 603 ? 126.269 128.941 151.231 1.00 52.91  ? 578 LYS B NZ  1 
ATOM   8051  N  N   . GLN B 1 604 ? 132.685 125.341 149.842 1.00 61.90  ? 579 GLN B N   1 
ATOM   8052  C  CA  . GLN B 1 604 ? 133.688 124.468 149.251 1.00 58.65  ? 579 GLN B CA  1 
ATOM   8053  C  C   . GLN B 1 604 ? 133.268 123.008 149.346 1.00 56.81  ? 579 GLN B C   1 
ATOM   8054  O  O   . GLN B 1 604 ? 132.650 122.584 150.324 1.00 63.95  ? 579 GLN B O   1 
ATOM   8055  C  CB  . GLN B 1 604 ? 135.031 124.668 149.943 1.00 56.68  ? 579 GLN B CB  1 
ATOM   8056  C  CG  . GLN B 1 604 ? 136.015 125.487 149.146 1.00 56.74  ? 579 GLN B CG  1 
ATOM   8057  C  CD  . GLN B 1 604 ? 136.985 126.226 150.029 1.00 63.00  ? 579 GLN B CD  1 
ATOM   8058  O  OE1 . GLN B 1 604 ? 136.825 126.264 151.248 1.00 63.37  ? 579 GLN B OE1 1 
ATOM   8059  N  NE2 . GLN B 1 604 ? 138.000 126.824 149.421 1.00 66.24  ? 579 GLN B NE2 1 
ATOM   8060  N  N   . TYR B 1 605 ? 133.619 122.235 148.324 1.00 38.10  ? 580 TYR B N   1 
ATOM   8061  C  CA  . TYR B 1 605 ? 133.297 120.817 148.286 1.00 33.75  ? 580 TYR B CA  1 
ATOM   8062  C  C   . TYR B 1 605 ? 134.268 120.128 147.341 1.00 46.29  ? 580 TYR B C   1 
ATOM   8063  O  O   . TYR B 1 605 ? 134.969 120.775 146.563 1.00 68.32  ? 580 TYR B O   1 
ATOM   8064  C  CB  . TYR B 1 605 ? 131.847 120.587 147.857 1.00 41.42  ? 580 TYR B CB  1 
ATOM   8065  C  CG  . TYR B 1 605 ? 131.575 120.774 146.383 1.00 30.64  ? 580 TYR B CG  1 
ATOM   8066  C  CD1 . TYR B 1 605 ? 131.751 119.734 145.487 1.00 38.75  ? 580 TYR B CD1 1 
ATOM   8067  C  CD2 . TYR B 1 605 ? 131.119 121.980 145.894 1.00 38.26  ? 580 TYR B CD2 1 
ATOM   8068  C  CE1 . TYR B 1 605 ? 131.498 119.896 144.150 1.00 43.44  ? 580 TYR B CE1 1 
ATOM   8069  C  CE2 . TYR B 1 605 ? 130.862 122.151 144.555 1.00 47.32  ? 580 TYR B CE2 1 
ATOM   8070  C  CZ  . TYR B 1 605 ? 131.054 121.104 143.688 1.00 46.07  ? 580 TYR B CZ  1 
ATOM   8071  O  OH  . TYR B 1 605 ? 130.800 121.265 142.348 1.00 48.06  ? 580 TYR B OH  1 
ATOM   8072  N  N   . LEU B 1 606 ? 134.302 118.802 147.420 1.00 37.15  ? 581 LEU B N   1 
ATOM   8073  C  CA  . LEU B 1 606 ? 135.112 117.984 146.529 1.00 38.34  ? 581 LEU B CA  1 
ATOM   8074  C  C   . LEU B 1 606 ? 134.215 117.330 145.493 1.00 34.42  ? 581 LEU B C   1 
ATOM   8075  O  O   . LEU B 1 606 ? 133.076 116.968 145.790 1.00 50.74  ? 581 LEU B O   1 
ATOM   8076  C  CB  . LEU B 1 606 ? 135.878 116.913 147.305 1.00 42.87  ? 581 LEU B CB  1 
ATOM   8077  C  CG  . LEU B 1 606 ? 137.135 116.353 146.640 1.00 47.31  ? 581 LEU B CG  1 
ATOM   8078  C  CD1 . LEU B 1 606 ? 138.210 116.116 147.670 1.00 53.29  ? 581 LEU B CD1 1 
ATOM   8079  C  CD2 . LEU B 1 606 ? 136.837 115.074 145.906 1.00 43.05  ? 581 LEU B CD2 1 
ATOM   8080  N  N   . HIS B 1 607 ? 134.730 117.173 144.283 1.00 41.03  ? 582 HIS B N   1 
ATOM   8081  C  CA  . HIS B 1 607 ? 133.969 116.630 143.165 1.00 45.21  ? 582 HIS B CA  1 
ATOM   8082  C  C   . HIS B 1 607 ? 134.552 115.258 142.844 1.00 49.11  ? 582 HIS B C   1 
ATOM   8083  O  O   . HIS B 1 607 ? 135.405 115.120 141.969 1.00 63.57  ? 582 HIS B O   1 
ATOM   8084  C  CB  . HIS B 1 607 ? 134.040 117.594 141.983 1.00 52.65  ? 582 HIS B CB  1 
ATOM   8085  C  CG  . HIS B 1 607 ? 133.568 117.021 140.686 1.00 55.05  ? 582 HIS B CG  1 
ATOM   8086  N  ND1 . HIS B 1 607 ? 134.269 116.057 139.996 1.00 62.15  ? 582 HIS B ND1 1 
ATOM   8087  C  CD2 . HIS B 1 607 ? 132.482 117.306 139.933 1.00 55.56  ? 582 HIS B CD2 1 
ATOM   8088  C  CE1 . HIS B 1 607 ? 133.625 115.758 138.883 1.00 60.96  ? 582 HIS B CE1 1 
ATOM   8089  N  NE2 . HIS B 1 607 ? 132.537 116.503 138.820 1.00 61.82  ? 582 HIS B NE2 1 
ATOM   8090  N  N   . ILE B 1 608 ? 134.080 114.237 143.559 1.00 41.06  ? 583 ILE B N   1 
ATOM   8091  C  CA  . ILE B 1 608 ? 134.623 112.895 143.397 1.00 42.38  ? 583 ILE B CA  1 
ATOM   8092  C  C   . ILE B 1 608 ? 134.298 112.382 142.002 1.00 43.93  ? 583 ILE B C   1 
ATOM   8093  O  O   . ILE B 1 608 ? 133.164 112.500 141.526 1.00 47.65  ? 583 ILE B O   1 
ATOM   8094  C  CB  . ILE B 1 608 ? 134.077 111.954 144.479 1.00 41.16  ? 583 ILE B CB  1 
ATOM   8095  C  CG1 . ILE B 1 608 ? 134.436 112.472 145.868 1.00 41.04  ? 583 ILE B CG1 1 
ATOM   8096  C  CG2 . ILE B 1 608 ? 134.631 110.564 144.295 1.00 35.75  ? 583 ILE B CG2 1 
ATOM   8097  C  CD1 . ILE B 1 608 ? 133.876 111.644 146.987 1.00 32.10  ? 583 ILE B CD1 1 
ATOM   8098  N  N   . GLY B 1 609 ? 135.299 111.820 141.338 1.00 63.44  ? 584 GLY B N   1 
ATOM   8099  C  CA  . GLY B 1 609 ? 135.118 111.322 139.993 1.00 68.09  ? 584 GLY B CA  1 
ATOM   8100  C  C   . GLY B 1 609 ? 136.461 110.990 139.378 1.00 73.63  ? 584 GLY B C   1 
ATOM   8101  O  O   . GLY B 1 609 ? 137.491 110.989 140.055 1.00 71.49  ? 584 GLY B O   1 
ATOM   8102  N  N   . LEU B 1 610 ? 136.429 110.707 138.075 1.00 79.38  ? 585 LEU B N   1 
ATOM   8103  C  CA  . LEU B 1 610 ? 137.666 110.397 137.369 1.00 76.12  ? 585 LEU B CA  1 
ATOM   8104  C  C   . LEU B 1 610 ? 138.586 111.607 137.288 1.00 77.97  ? 585 LEU B C   1 
ATOM   8105  O  O   . LEU B 1 610 ? 139.804 111.449 137.165 1.00 84.36  ? 585 LEU B O   1 
ATOM   8106  C  CB  . LEU B 1 610 ? 137.353 109.869 135.972 1.00 72.90  ? 585 LEU B CB  1 
ATOM   8107  C  CG  . LEU B 1 610 ? 136.550 108.570 135.939 1.00 73.22  ? 585 LEU B CG  1 
ATOM   8108  C  CD1 . LEU B 1 610 ? 136.150 108.221 134.519 1.00 76.01  ? 585 LEU B CD1 1 
ATOM   8109  C  CD2 . LEU B 1 610 ? 137.342 107.441 136.567 1.00 73.29  ? 585 LEU B CD2 1 
ATOM   8110  N  N   . LYS B 1 611 ? 138.030 112.816 137.363 1.00 68.07  ? 586 LYS B N   1 
ATOM   8111  C  CA  . LYS B 1 611 ? 138.803 114.056 137.305 1.00 70.67  ? 586 LYS B CA  1 
ATOM   8112  C  C   . LYS B 1 611 ? 138.422 114.911 138.505 1.00 71.26  ? 586 LYS B C   1 
ATOM   8113  O  O   . LYS B 1 611 ? 137.704 115.911 138.369 1.00 76.64  ? 586 LYS B O   1 
ATOM   8114  C  CB  . LYS B 1 611 ? 138.561 114.798 135.991 1.00 70.41  ? 586 LYS B CB  1 
ATOM   8115  N  N   . PRO B 1 612 ? 138.893 114.552 139.695 1.00 64.09  ? 587 PRO B N   1 
ATOM   8116  C  CA  . PRO B 1 612 ? 138.466 115.260 140.904 1.00 65.35  ? 587 PRO B CA  1 
ATOM   8117  C  C   . PRO B 1 612 ? 138.969 116.691 140.944 1.00 61.44  ? 587 PRO B C   1 
ATOM   8118  O  O   . PRO B 1 612 ? 140.001 117.031 140.361 1.00 68.47  ? 587 PRO B O   1 
ATOM   8119  C  CB  . PRO B 1 612 ? 139.087 114.432 142.030 1.00 63.93  ? 587 PRO B CB  1 
ATOM   8120  C  CG  . PRO B 1 612 ? 140.289 113.833 141.404 1.00 65.90  ? 587 PRO B CG  1 
ATOM   8121  C  CD  . PRO B 1 612 ? 139.891 113.514 139.994 1.00 66.29  ? 587 PRO B CD  1 
ATOM   8122  N  N   . ARG B 1 613 ? 138.220 117.531 141.651 1.00 60.01  ? 588 ARG B N   1 
ATOM   8123  C  CA  . ARG B 1 613 ? 138.592 118.923 141.847 1.00 66.02  ? 588 ARG B CA  1 
ATOM   8124  C  C   . ARG B 1 613 ? 137.826 119.462 143.044 1.00 64.63  ? 588 ARG B C   1 
ATOM   8125  O  O   . ARG B 1 613 ? 136.682 119.076 143.287 1.00 69.34  ? 588 ARG B O   1 
ATOM   8126  C  CB  . ARG B 1 613 ? 138.303 119.761 140.596 1.00 67.09  ? 588 ARG B CB  1 
ATOM   8127  C  CG  . ARG B 1 613 ? 138.745 121.208 140.709 1.00 71.06  ? 588 ARG B CG  1 
ATOM   8128  C  CD  . ARG B 1 613 ? 138.655 121.950 139.383 1.00 71.14  ? 588 ARG B CD  1 
ATOM   8129  N  NE  . ARG B 1 613 ? 137.993 123.243 139.527 1.00 69.78  ? 588 ARG B NE  1 
ATOM   8130  C  CZ  . ARG B 1 613 ? 138.498 124.281 140.182 1.00 71.59  ? 588 ARG B CZ  1 
ATOM   8131  N  NH1 . ARG B 1 613 ? 139.692 124.230 140.748 1.00 68.58  ? 588 ARG B NH1 1 
ATOM   8132  N  NH2 . ARG B 1 613 ? 137.785 125.400 140.272 1.00 70.69  ? 588 ARG B NH2 1 
ATOM   8133  N  N   . VAL B 1 614 ? 138.469 120.348 143.799 1.00 46.14  ? 589 VAL B N   1 
ATOM   8134  C  CA  . VAL B 1 614 ? 137.830 121.009 144.929 1.00 37.79  ? 589 VAL B CA  1 
ATOM   8135  C  C   . VAL B 1 614 ? 137.163 122.266 144.383 1.00 42.09  ? 589 VAL B C   1 
ATOM   8136  O  O   . VAL B 1 614 ? 137.819 123.279 144.145 1.00 62.03  ? 589 VAL B O   1 
ATOM   8137  C  CB  . VAL B 1 614 ? 138.828 121.327 146.041 1.00 47.50  ? 589 VAL B CB  1 
ATOM   8138  C  CG1 . VAL B 1 614 ? 138.127 121.996 147.203 1.00 51.05  ? 589 VAL B CG1 1 
ATOM   8139  C  CG2 . VAL B 1 614 ? 139.513 120.062 146.500 1.00 56.18  ? 589 VAL B CG2 1 
ATOM   8140  N  N   . ARG B 1 615 ? 135.853 122.202 144.193 1.00 46.19  ? 590 ARG B N   1 
ATOM   8141  C  CA  . ARG B 1 615 ? 135.123 123.283 143.551 1.00 53.70  ? 590 ARG B CA  1 
ATOM   8142  C  C   . ARG B 1 615 ? 134.665 124.294 144.598 1.00 63.00  ? 590 ARG B C   1 
ATOM   8143  O  O   . ARG B 1 615 ? 135.110 124.274 145.748 1.00 63.41  ? 590 ARG B O   1 
ATOM   8144  C  CB  . ARG B 1 615 ? 133.965 122.721 142.735 1.00 57.28  ? 590 ARG B CB  1 
ATOM   8145  C  CG  . ARG B 1 615 ? 134.399 121.702 141.700 1.00 64.06  ? 590 ARG B CG  1 
ATOM   8146  C  CD  . ARG B 1 615 ? 134.772 122.370 140.394 1.00 65.88  ? 590 ARG B CD  1 
ATOM   8147  N  NE  . ARG B 1 615 ? 133.710 122.254 139.404 1.00 75.03  ? 590 ARG B NE  1 
ATOM   8148  C  CZ  . ARG B 1 615 ? 133.673 121.330 138.454 1.00 77.00  ? 590 ARG B CZ  1 
ATOM   8149  N  NH1 . ARG B 1 615 ? 134.634 120.430 138.327 1.00 73.55  ? 590 ARG B NH1 1 
ATOM   8150  N  NH2 . ARG B 1 615 ? 132.647 121.310 137.607 1.00 71.79  ? 590 ARG B NH2 1 
ATOM   8151  N  N   . ASP B 1 616 ? 133.770 125.198 144.211 1.00 70.72  ? 591 ASP B N   1 
ATOM   8152  C  CA  . ASP B 1 616 ? 133.471 126.371 145.022 1.00 67.93  ? 591 ASP B CA  1 
ATOM   8153  C  C   . ASP B 1 616 ? 132.001 126.535 145.369 1.00 69.98  ? 591 ASP B C   1 
ATOM   8154  O  O   . ASP B 1 616 ? 131.688 127.001 146.464 1.00 73.04  ? 591 ASP B O   1 
ATOM   8155  C  CB  . ASP B 1 616 ? 133.962 127.633 144.304 1.00 71.39  ? 591 ASP B CB  1 
ATOM   8156  C  CG  . ASP B 1 616 ? 134.641 128.607 145.240 1.00 74.70  ? 591 ASP B CG  1 
ATOM   8157  O  OD1 . ASP B 1 616 ? 133.947 129.183 146.101 1.00 75.76  ? 591 ASP B OD1 1 
ATOM   8158  O  OD2 . ASP B 1 616 ? 135.870 128.789 145.119 1.00 75.22  ? 591 ASP B OD2 1 
ATOM   8159  N  N   . ASN B 1 617 ? 131.086 126.188 144.468 1.00 68.11  ? 592 ASN B N   1 
ATOM   8160  C  CA  . ASN B 1 617 ? 129.660 126.364 144.737 1.00 65.65  ? 592 ASN B CA  1 
ATOM   8161  C  C   . ASN B 1 617 ? 128.883 125.403 143.857 1.00 64.78  ? 592 ASN B C   1 
ATOM   8162  O  O   . ASN B 1 617 ? 128.880 125.558 142.632 1.00 66.09  ? 592 ASN B O   1 
ATOM   8163  C  CB  . ASN B 1 617 ? 129.225 127.803 144.476 1.00 62.46  ? 592 ASN B CB  1 
ATOM   8164  C  CG  . ASN B 1 617 ? 129.095 128.609 145.745 1.00 65.01  ? 592 ASN B CG  1 
ATOM   8165  O  OD1 . ASN B 1 617 ? 128.542 128.138 146.733 1.00 66.83  ? 592 ASN B OD1 1 
ATOM   8166  N  ND2 . ASN B 1 617 ? 129.604 129.832 145.726 1.00 63.40  ? 592 ASN B ND2 1 
ATOM   8167  N  N   . TYR B 1 618 ? 128.226 124.423 144.469 1.00 45.72  ? 593 TYR B N   1 
ATOM   8168  C  CA  . TYR B 1 618 ? 127.494 123.417 143.709 1.00 48.98  ? 593 TYR B CA  1 
ATOM   8169  C  C   . TYR B 1 618 ? 126.138 123.979 143.316 1.00 49.17  ? 593 TYR B C   1 
ATOM   8170  O  O   . TYR B 1 618 ? 125.270 124.168 144.173 1.00 58.21  ? 593 TYR B O   1 
ATOM   8171  C  CB  . TYR B 1 618 ? 127.322 122.135 144.514 1.00 43.20  ? 593 TYR B CB  1 
ATOM   8172  C  CG  . TYR B 1 618 ? 126.823 120.994 143.667 1.00 36.29  ? 593 TYR B CG  1 
ATOM   8173  C  CD1 . TYR B 1 618 ? 127.226 120.866 142.350 1.00 45.41  ? 593 TYR B CD1 1 
ATOM   8174  C  CD2 . TYR B 1 618 ? 125.938 120.062 144.170 1.00 36.75  ? 593 TYR B CD2 1 
ATOM   8175  C  CE1 . TYR B 1 618 ? 126.776 119.837 141.565 1.00 47.11  ? 593 TYR B CE1 1 
ATOM   8176  C  CE2 . TYR B 1 618 ? 125.480 119.029 143.388 1.00 50.09  ? 593 TYR B CE2 1 
ATOM   8177  C  CZ  . TYR B 1 618 ? 125.905 118.923 142.085 1.00 48.17  ? 593 TYR B CZ  1 
ATOM   8178  O  OH  . TYR B 1 618 ? 125.458 117.898 141.291 1.00 51.99  ? 593 TYR B OH  1 
ATOM   8179  N  N   . ARG B 1 619 ? 125.953 124.231 142.023 1.00 39.26  ? 594 ARG B N   1 
ATOM   8180  C  CA  . ARG B 1 619 ? 124.683 124.693 141.475 1.00 37.30  ? 594 ARG B CA  1 
ATOM   8181  C  C   . ARG B 1 619 ? 124.119 125.841 142.305 1.00 45.00  ? 594 ARG B C   1 
ATOM   8182  O  O   . ARG B 1 619 ? 123.029 125.759 142.867 1.00 56.87  ? 594 ARG B O   1 
ATOM   8183  C  CB  . ARG B 1 619 ? 123.685 123.540 141.390 1.00 32.85  ? 594 ARG B CB  1 
ATOM   8184  C  CG  . ARG B 1 619 ? 123.892 122.645 140.200 1.00 33.29  ? 594 ARG B CG  1 
ATOM   8185  C  CD  . ARG B 1 619 ? 123.044 121.400 140.306 1.00 38.14  ? 594 ARG B CD  1 
ATOM   8186  N  NE  . ARG B 1 619 ? 122.640 120.930 138.990 1.00 42.47  ? 594 ARG B NE  1 
ATOM   8187  C  CZ  . ARG B 1 619 ? 121.602 121.408 138.322 1.00 49.68  ? 594 ARG B CZ  1 
ATOM   8188  N  NH1 . ARG B 1 619 ? 120.824 122.344 138.835 1.00 45.27  ? 594 ARG B NH1 1 
ATOM   8189  N  NH2 . ARG B 1 619 ? 121.339 120.936 137.107 1.00 58.64  ? 594 ARG B NH2 1 
ATOM   8190  N  N   . ALA B 1 620 ? 124.899 126.919 142.387 1.00 42.89  ? 595 ALA B N   1 
ATOM   8191  C  CA  . ALA B 1 620 ? 124.527 128.028 143.258 1.00 40.62  ? 595 ALA B CA  1 
ATOM   8192  C  C   . ALA B 1 620 ? 123.190 128.622 142.850 1.00 39.79  ? 595 ALA B C   1 
ATOM   8193  O  O   . ALA B 1 620 ? 122.367 128.964 143.706 1.00 44.10  ? 595 ALA B O   1 
ATOM   8194  C  CB  . ALA B 1 620 ? 125.616 129.097 143.241 1.00 46.24  ? 595 ALA B CB  1 
ATOM   8195  N  N   . ASN B 1 621 ? 122.949 128.728 141.544 1.00 45.99  ? 596 ASN B N   1 
ATOM   8196  C  CA  . ASN B 1 621 ? 121.726 129.356 141.060 1.00 51.27  ? 596 ASN B CA  1 
ATOM   8197  C  C   . ASN B 1 621 ? 120.491 128.581 141.502 1.00 56.86  ? 596 ASN B C   1 
ATOM   8198  O  O   . ASN B 1 621 ? 119.580 129.144 142.116 1.00 60.40  ? 596 ASN B O   1 
ATOM   8199  C  CB  . ASN B 1 621 ? 121.782 129.468 139.538 1.00 48.81  ? 596 ASN B CB  1 
ATOM   8200  C  CG  . ASN B 1 621 ? 120.757 130.424 138.989 1.00 54.66  ? 596 ASN B CG  1 
ATOM   8201  O  OD1 . ASN B 1 621 ? 120.114 131.158 139.734 1.00 64.91  ? 596 ASN B OD1 1 
ATOM   8202  N  ND2 . ASN B 1 621 ? 120.597 130.423 137.673 1.00 58.39  ? 596 ASN B ND2 1 
ATOM   8203  N  N   . LYS B 1 622 ? 120.457 127.275 141.232 1.00 38.48  ? 597 LYS B N   1 
ATOM   8204  C  CA  . LYS B 1 622 ? 119.257 126.496 141.528 1.00 30.26  ? 597 LYS B CA  1 
ATOM   8205  C  C   . LYS B 1 622 ? 119.086 126.269 143.024 1.00 27.40  ? 597 LYS B C   1 
ATOM   8206  O  O   . LYS B 1 622 ? 117.961 126.285 143.535 1.00 43.66  ? 597 LYS B O   1 
ATOM   8207  C  CB  . LYS B 1 622 ? 119.306 125.168 140.786 1.00 37.54  ? 597 LYS B CB  1 
ATOM   8208  C  CG  . LYS B 1 622 ? 119.628 125.310 139.319 1.00 42.39  ? 597 LYS B CG  1 
ATOM   8209  C  CD  . LYS B 1 622 ? 118.614 126.178 138.616 1.00 39.01  ? 597 LYS B CD  1 
ATOM   8210  C  CE  . LYS B 1 622 ? 118.914 126.259 137.135 1.00 40.69  ? 597 LYS B CE  1 
ATOM   8211  N  NZ  . LYS B 1 622 ? 118.062 127.269 136.457 1.00 52.73  ? 597 LYS B NZ  1 
ATOM   8212  N  N   . VAL B 1 623 ? 120.185 126.048 143.744 1.00 31.03  ? 598 VAL B N   1 
ATOM   8213  C  CA  . VAL B 1 623 ? 120.096 125.886 145.191 1.00 38.30  ? 598 VAL B CA  1 
ATOM   8214  C  C   . VAL B 1 623 ? 119.575 127.162 145.838 1.00 45.98  ? 598 VAL B C   1 
ATOM   8215  O  O   . VAL B 1 623 ? 118.720 127.119 146.732 1.00 49.87  ? 598 VAL B O   1 
ATOM   8216  C  CB  . VAL B 1 623 ? 121.461 125.472 145.762 1.00 33.44  ? 598 VAL B CB  1 
ATOM   8217  C  CG1 . VAL B 1 623 ? 121.448 125.555 147.268 1.00 28.07  ? 598 VAL B CG1 1 
ATOM   8218  C  CG2 . VAL B 1 623 ? 121.811 124.076 145.306 1.00 32.84  ? 598 VAL B CG2 1 
ATOM   8219  N  N   . ALA B 1 624 ? 120.078 128.319 145.399 1.00 40.26  ? 599 ALA B N   1 
ATOM   8220  C  CA  . ALA B 1 624 ? 119.565 129.583 145.913 1.00 35.54  ? 599 ALA B CA  1 
ATOM   8221  C  C   . ALA B 1 624 ? 118.114 129.801 145.513 1.00 38.22  ? 599 ALA B C   1 
ATOM   8222  O  O   . ALA B 1 624 ? 117.348 130.396 146.274 1.00 34.37  ? 599 ALA B O   1 
ATOM   8223  C  CB  . ALA B 1 624 ? 120.430 130.738 145.424 1.00 42.27  ? 599 ALA B CB  1 
ATOM   8224  N  N   . PHE B 1 625 ? 117.724 129.332 144.328 1.00 34.32  ? 600 PHE B N   1 
ATOM   8225  C  CA  . PHE B 1 625 ? 116.323 129.379 143.927 1.00 27.22  ? 600 PHE B CA  1 
ATOM   8226  C  C   . PHE B 1 625 ? 115.450 128.616 144.913 1.00 33.66  ? 600 PHE B C   1 
ATOM   8227  O  O   . PHE B 1 625 ? 114.438 129.134 145.395 1.00 41.45  ? 600 PHE B O   1 
ATOM   8228  C  CB  . PHE B 1 625 ? 116.183 128.808 142.513 1.00 27.29  ? 600 PHE B CB  1 
ATOM   8229  C  CG  . PHE B 1 625 ? 114.767 128.649 142.044 1.00 22.82  ? 600 PHE B CG  1 
ATOM   8230  C  CD1 . PHE B 1 625 ? 113.785 129.545 142.407 1.00 27.50  ? 600 PHE B CD1 1 
ATOM   8231  C  CD2 . PHE B 1 625 ? 114.424 127.604 141.220 1.00 29.57  ? 600 PHE B CD2 1 
ATOM   8232  C  CE1 . PHE B 1 625 ? 112.493 129.390 141.966 1.00 22.75  ? 600 PHE B CE1 1 
ATOM   8233  C  CE2 . PHE B 1 625 ? 113.135 127.448 140.782 1.00 33.30  ? 600 PHE B CE2 1 
ATOM   8234  C  CZ  . PHE B 1 625 ? 112.171 128.341 141.156 1.00 24.67  ? 600 PHE B CZ  1 
ATOM   8235  N  N   . TRP B 1 626 ? 115.838 127.385 145.238 1.00 39.16  ? 601 TRP B N   1 
ATOM   8236  C  CA  . TRP B 1 626 ? 114.987 126.551 146.080 1.00 30.85  ? 601 TRP B CA  1 
ATOM   8237  C  C   . TRP B 1 626 ? 115.022 126.966 147.543 1.00 34.34  ? 601 TRP B C   1 
ATOM   8238  O  O   . TRP B 1 626 ? 114.053 126.724 148.268 1.00 38.36  ? 601 TRP B O   1 
ATOM   8239  C  CB  . TRP B 1 626 ? 115.377 125.081 145.948 1.00 19.19  ? 601 TRP B CB  1 
ATOM   8240  C  CG  . TRP B 1 626 ? 114.988 124.501 144.646 1.00 15.05  ? 601 TRP B CG  1 
ATOM   8241  C  CD1 . TRP B 1 626 ? 115.819 124.092 143.658 1.00 35.35  ? 601 TRP B CD1 1 
ATOM   8242  C  CD2 . TRP B 1 626 ? 113.660 124.274 144.175 1.00 19.08  ? 601 TRP B CD2 1 
ATOM   8243  N  NE1 . TRP B 1 626 ? 115.095 123.618 142.597 1.00 32.98  ? 601 TRP B NE1 1 
ATOM   8244  C  CE2 . TRP B 1 626 ? 113.764 123.719 142.892 1.00 24.87  ? 601 TRP B CE2 1 
ATOM   8245  C  CE3 . TRP B 1 626 ? 112.391 124.484 144.715 1.00 29.36  ? 601 TRP B CE3 1 
ATOM   8246  C  CZ2 . TRP B 1 626 ? 112.654 123.372 142.141 1.00 37.61  ? 601 TRP B CZ2 1 
ATOM   8247  C  CZ3 . TRP B 1 626 ? 111.291 124.139 143.967 1.00 37.46  ? 601 TRP B CZ3 1 
ATOM   8248  C  CH2 . TRP B 1 626 ? 111.428 123.588 142.695 1.00 41.50  ? 601 TRP B CH2 1 
ATOM   8249  N  N   . LEU B 1 627 ? 116.109 127.580 148.002 1.00 35.82  ? 602 LEU B N   1 
ATOM   8250  C  CA  . LEU B 1 627 ? 116.203 127.941 149.410 1.00 32.61  ? 602 LEU B CA  1 
ATOM   8251  C  C   . LEU B 1 627 ? 115.776 129.369 149.714 1.00 43.80  ? 602 LEU B C   1 
ATOM   8252  O  O   . LEU B 1 627 ? 115.327 129.636 150.832 1.00 45.82  ? 602 LEU B O   1 
ATOM   8253  C  CB  . LEU B 1 627 ? 117.633 127.743 149.920 1.00 32.70  ? 602 LEU B CB  1 
ATOM   8254  C  CG  . LEU B 1 627 ? 118.239 126.346 149.833 1.00 33.84  ? 602 LEU B CG  1 
ATOM   8255  C  CD1 . LEU B 1 627 ? 119.677 126.395 150.284 1.00 33.01  ? 602 LEU B CD1 1 
ATOM   8256  C  CD2 . LEU B 1 627 ? 117.455 125.365 150.671 1.00 33.63  ? 602 LEU B CD2 1 
ATOM   8257  N  N   . GLU B 1 628 ? 115.892 130.297 148.761 1.00 48.39  ? 603 GLU B N   1 
ATOM   8258  C  CA  . GLU B 1 628 ? 115.721 131.711 149.058 1.00 46.68  ? 603 GLU B CA  1 
ATOM   8259  C  C   . GLU B 1 628 ? 114.703 132.437 148.190 1.00 46.29  ? 603 GLU B C   1 
ATOM   8260  O  O   . GLU B 1 628 ? 114.376 133.585 148.505 1.00 50.54  ? 603 GLU B O   1 
ATOM   8261  C  CB  . GLU B 1 628 ? 117.067 132.440 148.947 1.00 42.77  ? 603 GLU B CB  1 
ATOM   8262  C  CG  . GLU B 1 628 ? 118.138 131.859 149.850 1.00 46.81  ? 603 GLU B CG  1 
ATOM   8263  C  CD  . GLU B 1 628 ? 119.437 132.626 149.792 1.00 59.27  ? 603 GLU B CD  1 
ATOM   8264  O  OE1 . GLU B 1 628 ? 119.391 133.866 149.660 1.00 58.21  ? 603 GLU B OE1 1 
ATOM   8265  O  OE2 . GLU B 1 628 ? 120.506 131.988 149.883 1.00 61.88  ? 603 GLU B OE2 1 
ATOM   8266  N  N   . LEU B 1 629 ? 114.195 131.828 147.124 1.00 39.12  ? 604 LEU B N   1 
ATOM   8267  C  CA  . LEU B 1 629 ? 113.141 132.440 146.324 1.00 28.23  ? 604 LEU B CA  1 
ATOM   8268  C  C   . LEU B 1 629 ? 111.811 131.716 146.424 1.00 41.63  ? 604 LEU B C   1 
ATOM   8269  O  O   . LEU B 1 629 ? 110.777 132.366 146.572 1.00 57.79  ? 604 LEU B O   1 
ATOM   8270  C  CB  . LEU B 1 629 ? 113.556 132.517 144.854 1.00 28.58  ? 604 LEU B CB  1 
ATOM   8271  C  CG  . LEU B 1 629 ? 112.453 133.015 143.922 1.00 28.17  ? 604 LEU B CG  1 
ATOM   8272  C  CD1 . LEU B 1 629 ? 112.050 134.418 144.306 1.00 42.83  ? 604 LEU B CD1 1 
ATOM   8273  C  CD2 . LEU B 1 629 ? 112.886 132.960 142.475 1.00 37.92  ? 604 LEU B CD2 1 
ATOM   8274  N  N   . VAL B 1 630 ? 111.808 130.383 146.345 1.00 37.86  ? 605 VAL B N   1 
ATOM   8275  C  CA  . VAL B 1 630 ? 110.553 129.637 146.461 1.00 26.88  ? 605 VAL B CA  1 
ATOM   8276  C  C   . VAL B 1 630 ? 109.817 129.941 147.759 1.00 42.26  ? 605 VAL B C   1 
ATOM   8277  O  O   . VAL B 1 630 ? 108.584 130.064 147.727 1.00 54.53  ? 605 VAL B O   1 
ATOM   8278  C  CB  . VAL B 1 630 ? 110.806 128.140 146.243 1.00 31.69  ? 605 VAL B CB  1 
ATOM   8279  C  CG1 . VAL B 1 630 ? 109.649 127.328 146.767 1.00 44.83  ? 605 VAL B CG1 1 
ATOM   8280  C  CG2 . VAL B 1 630 ? 110.999 127.863 144.777 1.00 34.73  ? 605 VAL B CG2 1 
ATOM   8281  N  N   . PRO B 1 631 ? 110.471 130.073 148.918 1.00 51.10  ? 606 PRO B N   1 
ATOM   8282  C  CA  . PRO B 1 631 ? 109.728 130.481 150.120 1.00 57.31  ? 606 PRO B CA  1 
ATOM   8283  C  C   . PRO B 1 631 ? 109.020 131.820 149.990 1.00 62.94  ? 606 PRO B C   1 
ATOM   8284  O  O   . PRO B 1 631 ? 108.064 132.067 150.735 1.00 66.50  ? 606 PRO B O   1 
ATOM   8285  C  CB  . PRO B 1 631 ? 110.816 130.532 151.197 1.00 54.68  ? 606 PRO B CB  1 
ATOM   8286  C  CG  . PRO B 1 631 ? 111.786 129.524 150.768 1.00 51.19  ? 606 PRO B CG  1 
ATOM   8287  C  CD  . PRO B 1 631 ? 111.821 129.599 149.270 1.00 54.50  ? 606 PRO B CD  1 
ATOM   8288  N  N   . HIS B 1 632 ? 109.450 132.691 149.080 1.00 54.95  ? 607 HIS B N   1 
ATOM   8289  C  CA  . HIS B 1 632 ? 108.802 133.984 148.903 1.00 51.32  ? 607 HIS B CA  1 
ATOM   8290  C  C   . HIS B 1 632 ? 107.589 133.927 147.987 1.00 51.86  ? 607 HIS B C   1 
ATOM   8291  O  O   . HIS B 1 632 ? 106.951 134.962 147.776 1.00 61.28  ? 607 HIS B O   1 
ATOM   8292  C  CB  . HIS B 1 632 ? 109.796 135.007 148.354 1.00 55.58  ? 607 HIS B CB  1 
ATOM   8293  C  CG  . HIS B 1 632 ? 110.901 135.343 149.304 1.00 64.49  ? 607 HIS B CG  1 
ATOM   8294  N  ND1 . HIS B 1 632 ? 112.017 136.055 148.924 1.00 67.22  ? 607 HIS B ND1 1 
ATOM   8295  C  CD2 . HIS B 1 632 ? 111.060 135.065 150.619 1.00 59.83  ? 607 HIS B CD2 1 
ATOM   8296  C  CE1 . HIS B 1 632 ? 112.819 136.199 149.964 1.00 69.00  ? 607 HIS B CE1 1 
ATOM   8297  N  NE2 . HIS B 1 632 ? 112.261 135.608 151.005 1.00 68.19  ? 607 HIS B NE2 1 
ATOM   8298  N  N   . LEU B 1 633 ? 107.257 132.768 147.434 1.00 41.70  ? 608 LEU B N   1 
ATOM   8299  C  CA  . LEU B 1 633 ? 106.088 132.655 146.569 1.00 45.22  ? 608 LEU B CA  1 
ATOM   8300  C  C   . LEU B 1 633 ? 105.042 131.725 147.175 1.00 52.02  ? 608 LEU B C   1 
ATOM   8301  O  O   . LEU B 1 633 ? 105.376 130.725 147.811 1.00 51.48  ? 608 LEU B O   1 
ATOM   8302  C  CB  . LEU B 1 633 ? 106.489 132.159 145.181 1.00 38.57  ? 608 LEU B CB  1 
ATOM   8303  C  CG  . LEU B 1 633 ? 107.839 132.626 144.641 1.00 36.28  ? 608 LEU B CG  1 
ATOM   8304  C  CD1 . LEU B 1 633 ? 108.115 131.963 143.316 1.00 36.55  ? 608 LEU B CD1 1 
ATOM   8305  C  CD2 . LEU B 1 633 ? 107.876 134.132 144.494 1.00 43.31  ? 608 LEU B CD2 1 
ATOM   8306  N  N   . ALA C 2 106 ? 89.793  142.180 76.385  1.00 154.04 ? 83  ALA C N   1 
ATOM   8307  C  CA  . ALA C 2 106 ? 90.297  141.912 75.043  1.00 154.69 ? 83  ALA C CA  1 
ATOM   8308  C  C   . ALA C 2 106 ? 91.799  141.654 75.072  1.00 155.19 ? 83  ALA C C   1 
ATOM   8309  O  O   . ALA C 2 106 ? 92.468  141.705 74.040  1.00 154.65 ? 83  ALA C O   1 
ATOM   8310  C  CB  . ALA C 2 106 ? 89.973  143.070 74.113  1.00 153.54 ? 83  ALA C CB  1 
ATOM   8311  N  N   . GLY C 2 107 ? 92.324  141.376 76.263  1.00 154.38 ? 84  GLY C N   1 
ATOM   8312  C  CA  . GLY C 2 107 ? 93.738  141.105 76.439  1.00 153.63 ? 84  GLY C CA  1 
ATOM   8313  C  C   . GLY C 2 107 ? 94.098  139.677 76.095  1.00 153.60 ? 84  GLY C C   1 
ATOM   8314  O  O   . GLY C 2 107 ? 93.498  139.050 75.213  1.00 154.27 ? 84  GLY C O   1 
ATOM   8315  N  N   . THR C 2 108 ? 95.094  139.147 76.805  1.00 153.56 ? 85  THR C N   1 
ATOM   8316  C  CA  . THR C 2 108 ? 95.552  137.775 76.595  1.00 154.84 ? 85  THR C CA  1 
ATOM   8317  C  C   . THR C 2 108 ? 94.527  136.829 77.215  1.00 155.18 ? 85  THR C C   1 
ATOM   8318  O  O   . THR C 2 108 ? 94.664  136.352 78.345  1.00 155.06 ? 85  THR C O   1 
ATOM   8319  C  CB  . THR C 2 108 ? 96.940  137.574 77.187  1.00 154.56 ? 85  THR C CB  1 
ATOM   8320  O  OG1 . THR C 2 108 ? 97.784  138.665 76.802  1.00 153.33 ? 85  THR C OG1 1 
ATOM   8321  C  CG2 . THR C 2 108 ? 97.549  136.277 76.685  1.00 153.53 ? 85  THR C CG2 1 
ATOM   8322  N  N   . THR C 2 109 ? 93.474  136.555 76.449  1.00 159.59 ? 86  THR C N   1 
ATOM   8323  C  CA  . THR C 2 109 ? 92.393  135.709 76.935  1.00 160.01 ? 86  THR C CA  1 
ATOM   8324  C  C   . THR C 2 109 ? 92.850  134.257 77.018  1.00 160.38 ? 86  THR C C   1 
ATOM   8325  O  O   . THR C 2 109 ? 93.387  133.707 76.052  1.00 160.34 ? 86  THR C O   1 
ATOM   8326  C  CB  . THR C 2 109 ? 91.174  135.830 76.020  1.00 159.88 ? 86  THR C CB  1 
ATOM   8327  O  OG1 . THR C 2 109 ? 90.593  137.132 76.166  1.00 159.34 ? 86  THR C OG1 1 
ATOM   8328  C  CG2 . THR C 2 109 ? 90.132  134.779 76.372  1.00 158.33 ? 86  THR C CG2 1 
ATOM   8329  N  N   . TYR C 2 110 ? 92.629  133.636 78.173  1.00 158.43 ? 87  TYR C N   1 
ATOM   8330  C  CA  . TYR C 2 110 ? 93.030  132.259 78.421  1.00 158.48 ? 87  TYR C CA  1 
ATOM   8331  C  C   . TYR C 2 110 ? 91.791  131.384 78.553  1.00 158.72 ? 87  TYR C C   1 
ATOM   8332  O  O   . TYR C 2 110 ? 90.844  131.743 79.261  1.00 157.54 ? 87  TYR C O   1 
ATOM   8333  C  CB  . TYR C 2 110 ? 93.894  132.161 79.680  1.00 157.08 ? 87  TYR C CB  1 
ATOM   8334  C  CG  . TYR C 2 110 ? 95.377  132.164 79.391  1.00 156.97 ? 87  TYR C CG  1 
ATOM   8335  C  CD1 . TYR C 2 110 ? 96.009  133.307 78.924  1.00 156.81 ? 87  TYR C CD1 1 
ATOM   8336  C  CD2 . TYR C 2 110 ? 96.143  131.024 79.581  1.00 157.37 ? 87  TYR C CD2 1 
ATOM   8337  C  CE1 . TYR C 2 110 ? 97.364  133.314 78.658  1.00 157.58 ? 87  TYR C CE1 1 
ATOM   8338  C  CE2 . TYR C 2 110 ? 97.497  131.021 79.318  1.00 157.41 ? 87  TYR C CE2 1 
ATOM   8339  C  CZ  . TYR C 2 110 ? 98.102  132.168 78.856  1.00 157.95 ? 87  TYR C CZ  1 
ATOM   8340  O  OH  . TYR C 2 110 ? 99.450  132.167 78.593  1.00 157.57 ? 87  TYR C OH  1 
ATOM   8341  N  N   . ILE C 2 111 ? 91.805  130.238 77.876  1.00 163.23 ? 88  ILE C N   1 
ATOM   8342  C  CA  . ILE C 2 111 ? 90.652  129.349 77.789  1.00 162.88 ? 88  ILE C CA  1 
ATOM   8343  C  C   . ILE C 2 111 ? 90.843  128.195 78.761  1.00 161.66 ? 88  ILE C C   1 
ATOM   8344  O  O   . ILE C 2 111 ? 91.888  127.532 78.755  1.00 160.37 ? 88  ILE C O   1 
ATOM   8345  C  CB  . ILE C 2 111 ? 90.466  128.823 76.355  1.00 162.62 ? 88  ILE C CB  1 
ATOM   8346  C  CG1 . ILE C 2 111 ? 90.124  129.967 75.400  1.00 161.96 ? 88  ILE C CG1 1 
ATOM   8347  C  CG2 . ILE C 2 111 ? 89.393  127.742 76.314  1.00 161.56 ? 88  ILE C CG2 1 
ATOM   8348  C  CD1 . ILE C 2 111 ? 88.667  130.344 75.388  1.00 160.78 ? 88  ILE C CD1 1 
ATOM   8349  N  N   . PHE C 2 112 ? 89.837  127.954 79.596  1.00 162.54 ? 89  PHE C N   1 
ATOM   8350  C  CA  . PHE C 2 112 ? 89.808  126.769 80.439  1.00 163.47 ? 89  PHE C CA  1 
ATOM   8351  C  C   . PHE C 2 112 ? 89.130  125.631 79.691  1.00 163.51 ? 89  PHE C C   1 
ATOM   8352  O  O   . PHE C 2 112 ? 88.194  125.851 78.918  1.00 163.76 ? 89  PHE C O   1 
ATOM   8353  C  CB  . PHE C 2 112 ? 89.077  127.050 81.753  1.00 163.09 ? 89  PHE C CB  1 
ATOM   8354  C  CG  . PHE C 2 112 ? 89.937  127.706 82.792  1.00 162.69 ? 89  PHE C CG  1 
ATOM   8355  C  CD1 . PHE C 2 112 ? 90.198  129.062 82.736  1.00 162.03 ? 89  PHE C CD1 1 
ATOM   8356  C  CD2 . PHE C 2 112 ? 90.490  126.964 83.819  1.00 161.80 ? 89  PHE C CD2 1 
ATOM   8357  C  CE1 . PHE C 2 112 ? 90.991  129.667 83.686  1.00 161.63 ? 89  PHE C CE1 1 
ATOM   8358  C  CE2 . PHE C 2 112 ? 91.283  127.564 84.773  1.00 162.12 ? 89  PHE C CE2 1 
ATOM   8359  C  CZ  . PHE C 2 112 ? 91.535  128.918 84.705  1.00 162.12 ? 89  PHE C CZ  1 
ATOM   8360  N  N   . SER C 2 113 ? 89.608  124.411 79.926  1.00 162.59 ? 90  SER C N   1 
ATOM   8361  C  CA  . SER C 2 113 ? 89.130  123.259 79.172  1.00 162.24 ? 90  SER C CA  1 
ATOM   8362  C  C   . SER C 2 113 ? 88.623  122.159 80.094  1.00 162.09 ? 90  SER C C   1 
ATOM   8363  O  O   . SER C 2 113 ? 88.432  122.382 81.294  1.00 160.73 ? 90  SER C O   1 
ATOM   8364  C  CB  . SER C 2 113 ? 90.237  122.719 78.265  1.00 161.43 ? 90  SER C CB  1 
ATOM   8365  O  OG  . SER C 2 113 ? 89.784  121.605 77.517  1.00 161.25 ? 90  SER C OG  1 
ATOM   8366  N  N   . LYS C 2 114 ? 88.391  120.976 79.530  1.00 162.99 ? 91  LYS C N   1 
ATOM   8367  C  CA  . LYS C 2 114 ? 87.858  119.858 80.297  1.00 162.55 ? 91  LYS C CA  1 
ATOM   8368  C  C   . LYS C 2 114 ? 88.792  119.488 81.443  1.00 162.74 ? 91  LYS C C   1 
ATOM   8369  O  O   . LYS C 2 114 ? 90.017  119.590 81.331  1.00 162.41 ? 91  LYS C O   1 
ATOM   8370  C  CB  . LYS C 2 114 ? 87.645  118.650 79.383  1.00 162.11 ? 91  LYS C CB  1 
ATOM   8371  C  CG  . LYS C 2 114 ? 88.865  118.284 78.550  1.00 161.53 ? 91  LYS C CG  1 
ATOM   8372  C  CD  . LYS C 2 114 ? 88.576  117.115 77.623  1.00 160.74 ? 91  LYS C CD  1 
ATOM   8373  C  CE  . LYS C 2 114 ? 89.684  116.935 76.596  1.00 160.54 ? 91  LYS C CE  1 
ATOM   8374  N  NZ  . LYS C 2 114 ? 90.988  116.594 77.227  1.00 160.70 ? 91  LYS C NZ  1 
ATOM   8375  N  N   . GLY C 2 115 ? 88.201  119.062 82.555  1.00 165.85 ? 92  GLY C N   1 
ATOM   8376  C  CA  . GLY C 2 115 ? 88.965  118.696 83.729  1.00 165.33 ? 92  GLY C CA  1 
ATOM   8377  C  C   . GLY C 2 115 ? 89.227  119.873 84.643  1.00 166.07 ? 92  GLY C C   1 
ATOM   8378  O  O   . GLY C 2 115 ? 88.636  119.971 85.723  1.00 165.54 ? 92  GLY C O   1 
ATOM   8379  N  N   . GLY C 2 116 ? 90.104  120.771 84.224  1.00 166.94 ? 93  GLY C N   1 
ATOM   8380  C  CA  . GLY C 2 116 ? 90.415  121.950 85.001  1.00 166.43 ? 93  GLY C CA  1 
ATOM   8381  C  C   . GLY C 2 116 ? 91.797  122.466 84.659  1.00 165.88 ? 93  GLY C C   1 
ATOM   8382  O  O   . GLY C 2 116 ? 92.452  121.988 83.737  1.00 164.82 ? 93  GLY C O   1 
ATOM   8383  N  N   . GLY C 2 117 ? 92.223  123.460 85.428  1.00 163.46 ? 94  GLY C N   1 
ATOM   8384  C  CA  . GLY C 2 117 ? 93.534  124.052 85.235  1.00 162.84 ? 94  GLY C CA  1 
ATOM   8385  C  C   . GLY C 2 117 ? 93.775  125.134 86.263  1.00 163.01 ? 94  GLY C C   1 
ATOM   8386  O  O   . GLY C 2 117 ? 92.889  125.490 87.048  1.00 163.00 ? 94  GLY C O   1 
ATOM   8387  N  N   . GLN C 2 118 ? 94.997  125.662 86.245  1.00 156.84 ? 95  GLN C N   1 
ATOM   8388  C  CA  . GLN C 2 118 ? 95.405  126.639 87.242  1.00 156.15 ? 95  GLN C CA  1 
ATOM   8389  C  C   . GLN C 2 118 ? 96.655  127.373 86.775  1.00 155.90 ? 95  GLN C C   1 
ATOM   8390  O  O   . GLN C 2 118 ? 97.565  126.772 86.185  1.00 156.06 ? 95  GLN C O   1 
ATOM   8391  C  CB  . GLN C 2 118 ? 95.657  125.961 88.594  1.00 155.50 ? 95  GLN C CB  1 
ATOM   8392  C  CG  . GLN C 2 118 ? 96.294  126.851 89.637  1.00 154.42 ? 95  GLN C CG  1 
ATOM   8393  C  CD  . GLN C 2 118 ? 96.310  126.206 91.002  1.00 155.90 ? 95  GLN C CD  1 
ATOM   8394  O  OE1 . GLN C 2 118 ? 95.315  125.627 91.437  1.00 156.24 ? 95  GLN C OE1 1 
ATOM   8395  N  NE2 . GLN C 2 118 ? 97.443  126.297 91.686  1.00 155.33 ? 95  GLN C NE2 1 
ATOM   8396  N  N   . ILE C 2 119 ? 96.680  128.677 87.045  1.00 145.76 ? 96  ILE C N   1 
ATOM   8397  C  CA  . ILE C 2 119 ? 97.829  129.539 86.788  1.00 145.90 ? 96  ILE C CA  1 
ATOM   8398  C  C   . ILE C 2 119 ? 98.341  130.044 88.129  1.00 146.41 ? 96  ILE C C   1 
ATOM   8399  O  O   . ILE C 2 119 ? 97.556  130.511 88.962  1.00 144.33 ? 96  ILE C O   1 
ATOM   8400  C  CB  . ILE C 2 119 ? 97.464  130.718 85.869  1.00 145.66 ? 96  ILE C CB  1 
ATOM   8401  C  CG1 . ILE C 2 119 ? 96.762  130.231 84.602  1.00 145.12 ? 96  ILE C CG1 1 
ATOM   8402  C  CG2 . ILE C 2 119 ? 98.711  131.508 85.502  1.00 145.31 ? 96  ILE C CG2 1 
ATOM   8403  C  CD1 . ILE C 2 119 ? 97.478  129.117 83.900  1.00 146.08 ? 96  ILE C CD1 1 
ATOM   8404  N  N   . THR C 2 120 ? 99.650  129.953 88.339  1.00 144.18 ? 97  THR C N   1 
ATOM   8405  C  CA  . THR C 2 120 ? 100.270 130.343 89.598  1.00 142.54 ? 97  THR C CA  1 
ATOM   8406  C  C   . THR C 2 120 ? 101.330 131.403 89.346  1.00 142.10 ? 97  THR C C   1 
ATOM   8407  O  O   . THR C 2 120 ? 102.234 131.200 88.531  1.00 141.62 ? 97  THR C O   1 
ATOM   8408  C  CB  . THR C 2 120 ? 100.898 129.135 90.299  1.00 141.70 ? 97  THR C CB  1 
ATOM   8409  O  OG1 . THR C 2 120 ? 99.878  128.184 90.625  1.00 142.54 ? 97  THR C OG1 1 
ATOM   8410  C  CG2 . THR C 2 120 ? 101.604 129.567 91.570  1.00 139.34 ? 97  THR C CG2 1 
ATOM   8411  N  N   . TYR C 2 121 ? 101.217 132.528 90.045  1.00 127.74 ? 98  TYR C N   1 
ATOM   8412  C  CA  . TYR C 2 121 ? 102.239 133.567 90.051  1.00 124.82 ? 98  TYR C CA  1 
ATOM   8413  C  C   . TYR C 2 121 ? 102.880 133.582 91.431  1.00 123.85 ? 98  TYR C C   1 
ATOM   8414  O  O   . TYR C 2 121 ? 102.189 133.782 92.434  1.00 124.36 ? 98  TYR C O   1 
ATOM   8415  C  CB  . TYR C 2 121 ? 101.642 134.934 89.713  1.00 122.53 ? 98  TYR C CB  1 
ATOM   8416  C  CG  . TYR C 2 121 ? 102.642 136.074 89.637  1.00 122.38 ? 98  TYR C CG  1 
ATOM   8417  C  CD1 . TYR C 2 121 ? 104.008 135.834 89.553  1.00 122.13 ? 98  TYR C CD1 1 
ATOM   8418  C  CD2 . TYR C 2 121 ? 102.214 137.394 89.642  1.00 124.46 ? 98  TYR C CD2 1 
ATOM   8419  C  CE1 . TYR C 2 121 ? 104.913 136.873 89.484  1.00 123.27 ? 98  TYR C CE1 1 
ATOM   8420  C  CE2 . TYR C 2 121 ? 103.113 138.438 89.571  1.00 124.55 ? 98  TYR C CE2 1 
ATOM   8421  C  CZ  . TYR C 2 121 ? 104.460 138.172 89.492  1.00 123.51 ? 98  TYR C CZ  1 
ATOM   8422  O  OH  . TYR C 2 121 ? 105.360 139.208 89.422  1.00 122.28 ? 98  TYR C OH  1 
ATOM   8423  N  N   . LYS C 2 122 ? 104.191 133.371 91.479  1.00 116.57 ? 99  LYS C N   1 
ATOM   8424  C  CA  . LYS C 2 122 ? 104.939 133.339 92.728  1.00 116.49 ? 99  LYS C CA  1 
ATOM   8425  C  C   . LYS C 2 122 ? 105.871 134.541 92.776  1.00 118.91 ? 99  LYS C C   1 
ATOM   8426  O  O   . LYS C 2 122 ? 106.720 134.709 91.894  1.00 120.86 ? 99  LYS C O   1 
ATOM   8427  C  CB  . LYS C 2 122 ? 105.729 132.038 92.857  1.00 116.09 ? 99  LYS C CB  1 
ATOM   8428  C  CG  . LYS C 2 122 ? 106.608 131.966 94.092  1.00 117.09 ? 99  LYS C CG  1 
ATOM   8429  C  CD  . LYS C 2 122 ? 107.213 130.582 94.254  1.00 117.83 ? 99  LYS C CD  1 
ATOM   8430  C  CE  . LYS C 2 122 ? 107.885 130.430 95.609  1.00 118.61 ? 99  LYS C CE  1 
ATOM   8431  N  NZ  . LYS C 2 122 ? 108.525 129.096 95.769  1.00 117.17 ? 99  LYS C NZ  1 
ATOM   8432  N  N   . TRP C 2 123 ? 105.708 135.372 93.800  1.00 110.25 ? 100 TRP C N   1 
ATOM   8433  C  CA  . TRP C 2 123 ? 106.600 136.500 93.991  1.00 107.55 ? 100 TRP C CA  1 
ATOM   8434  C  C   . TRP C 2 123 ? 107.979 136.012 94.427  1.00 107.98 ? 100 TRP C C   1 
ATOM   8435  O  O   . TRP C 2 123 ? 108.103 134.955 95.051  1.00 104.12 ? 100 TRP C O   1 
ATOM   8436  C  CB  . TRP C 2 123 ? 106.041 137.452 95.042  1.00 105.27 ? 100 TRP C CB  1 
ATOM   8437  C  CG  . TRP C 2 123 ? 105.208 138.551 94.488  1.00 102.66 ? 100 TRP C CG  1 
ATOM   8438  C  CD1 . TRP C 2 123 ? 105.653 139.702 93.916  1.00 105.91 ? 100 TRP C CD1 1 
ATOM   8439  C  CD2 . TRP C 2 123 ? 103.779 138.616 94.466  1.00 101.94 ? 100 TRP C CD2 1 
ATOM   8440  N  NE1 . TRP C 2 123 ? 104.591 140.480 93.533  1.00 107.92 ? 100 TRP C NE1 1 
ATOM   8441  C  CE2 . TRP C 2 123 ? 103.428 139.834 93.860  1.00 104.45 ? 100 TRP C CE2 1 
ATOM   8442  C  CE3 . TRP C 2 123 ? 102.764 137.762 94.897  1.00 103.18 ? 100 TRP C CE3 1 
ATOM   8443  C  CZ2 . TRP C 2 123 ? 102.106 140.220 93.674  1.00 105.49 ? 100 TRP C CZ2 1 
ATOM   8444  C  CZ3 . TRP C 2 123 ? 101.453 138.147 94.711  1.00 104.35 ? 100 TRP C CZ3 1 
ATOM   8445  C  CH2 . TRP C 2 123 ? 101.135 139.364 94.105  1.00 105.06 ? 100 TRP C CH2 1 
ATOM   8446  N  N   . PRO C 2 124 ? 109.031 136.756 94.102  1.00 113.74 ? 101 PRO C N   1 
ATOM   8447  C  CA  . PRO C 2 124 ? 110.351 136.445 94.650  1.00 115.04 ? 101 PRO C CA  1 
ATOM   8448  C  C   . PRO C 2 124 ? 110.326 136.534 96.164  1.00 115.54 ? 101 PRO C C   1 
ATOM   8449  O  O   . PRO C 2 124 ? 109.683 137.432 96.727  1.00 115.93 ? 101 PRO C O   1 
ATOM   8450  C  CB  . PRO C 2 124 ? 111.257 137.524 94.039  1.00 112.92 ? 101 PRO C CB  1 
ATOM   8451  C  CG  . PRO C 2 124 ? 110.331 138.599 93.579  1.00 111.24 ? 101 PRO C CG  1 
ATOM   8452  C  CD  . PRO C 2 124 ? 109.063 137.914 93.196  1.00 110.30 ? 101 PRO C CD  1 
ATOM   8453  N  N   . PRO C 2 125 ? 111.013 135.624 96.859  1.00 114.84 ? 102 PRO C N   1 
ATOM   8454  C  CA  . PRO C 2 125 ? 110.903 135.594 98.327  1.00 112.75 ? 102 PRO C CA  1 
ATOM   8455  C  C   . PRO C 2 125 ? 111.328 136.883 99.004  1.00 111.00 ? 102 PRO C C   1 
ATOM   8456  O  O   . PRO C 2 125 ? 110.835 137.184 100.098 1.00 111.32 ? 102 PRO C O   1 
ATOM   8457  C  CB  . PRO C 2 125 ? 111.814 134.422 98.717  1.00 112.71 ? 102 PRO C CB  1 
ATOM   8458  C  CG  . PRO C 2 125 ? 111.848 133.557 97.501  1.00 111.81 ? 102 PRO C CG  1 
ATOM   8459  C  CD  . PRO C 2 125 ? 111.816 134.505 96.341  1.00 112.25 ? 102 PRO C CD  1 
ATOM   8460  N  N   . ASN C 2 126 ? 112.221 137.655 98.395  1.00 107.29 ? 103 ASN C N   1 
ATOM   8461  C  CA  . ASN C 2 126 ? 112.688 138.900 98.987  1.00 110.82 ? 103 ASN C CA  1 
ATOM   8462  C  C   . ASN C 2 126 ? 111.870 140.112 98.563  1.00 111.21 ? 103 ASN C C   1 
ATOM   8463  O  O   . ASN C 2 126 ? 112.142 141.220 99.037  1.00 108.36 ? 103 ASN C O   1 
ATOM   8464  C  CB  . ASN C 2 126 ? 114.161 139.129 98.636  1.00 110.38 ? 103 ASN C CB  1 
ATOM   8465  C  CG  . ASN C 2 126 ? 114.861 140.032 99.628  1.00 111.26 ? 103 ASN C CG  1 
ATOM   8466  O  OD1 . ASN C 2 126 ? 115.207 139.612 100.730 1.00 111.73 ? 103 ASN C OD1 1 
ATOM   8467  N  ND2 . ASN C 2 126 ? 115.080 141.281 99.237  1.00 110.07 ? 103 ASN C ND2 1 
ATOM   8468  N  N   . ASP C 2 127 ? 110.880 139.938 97.692  1.00 110.61 ? 104 ASP C N   1 
ATOM   8469  C  CA  . ASP C 2 127 ? 110.095 141.060 97.189  1.00 109.79 ? 104 ASP C CA  1 
ATOM   8470  C  C   . ASP C 2 127 ? 108.612 140.696 97.243  1.00 109.10 ? 104 ASP C C   1 
ATOM   8471  O  O   . ASP C 2 127 ? 107.867 140.848 96.274  1.00 109.40 ? 104 ASP C O   1 
ATOM   8472  C  CB  . ASP C 2 127 ? 110.550 141.432 95.776  1.00 110.53 ? 104 ASP C CB  1 
ATOM   8473  C  CG  . ASP C 2 127 ? 109.881 142.695 95.237  1.00 113.40 ? 104 ASP C CG  1 
ATOM   8474  O  OD1 . ASP C 2 127 ? 108.934 143.216 95.862  1.00 111.90 ? 104 ASP C OD1 1 
ATOM   8475  O  OD2 . ASP C 2 127 ? 110.304 143.164 94.160  1.00 114.13 ? 104 ASP C OD2 1 
ATOM   8476  N  N   . ARG C 2 128 ? 108.170 140.176 98.384  1.00 97.45  ? 105 ARG C N   1 
ATOM   8477  C  CA  . ARG C 2 128 ? 106.751 139.930 98.598  1.00 94.50  ? 105 ARG C CA  1 
ATOM   8478  C  C   . ARG C 2 128 ? 106.103 141.199 99.127  1.00 96.29  ? 105 ARG C C   1 
ATOM   8479  O  O   . ARG C 2 128 ? 106.434 141.631 100.238 1.00 100.71 ? 105 ARG C O   1 
ATOM   8480  C  CB  . ARG C 2 128 ? 106.541 138.793 99.580  1.00 96.38  ? 105 ARG C CB  1 
ATOM   8481  C  CG  . ARG C 2 128 ? 107.055 137.448 99.109  1.00 96.02  ? 105 ARG C CG  1 
ATOM   8482  C  CD  . ARG C 2 128 ? 106.250 136.322 99.733  1.00 98.88  ? 105 ARG C CD  1 
ATOM   8483  N  NE  . ARG C 2 128 ? 106.948 135.044 99.676  1.00 98.34  ? 105 ARG C NE  1 
ATOM   8484  C  CZ  . ARG C 2 128 ? 107.724 134.573 100.641 1.00 98.40  ? 105 ARG C CZ  1 
ATOM   8485  N  NH1 . ARG C 2 128 ? 107.933 135.255 101.755 1.00 96.91  ? 105 ARG C NH1 1 
ATOM   8486  N  NH2 . ARG C 2 128 ? 108.305 133.386 100.485 1.00 97.81  ? 105 ARG C NH2 1 
ATOM   8487  N  N   . PRO C 2 129 ? 105.183 141.819 98.390  1.00 85.58  ? 106 PRO C N   1 
ATOM   8488  C  CA  . PRO C 2 129 ? 104.661 143.123 98.806  1.00 84.44  ? 106 PRO C CA  1 
ATOM   8489  C  C   . PRO C 2 129 ? 103.477 143.017 99.753  1.00 85.69  ? 106 PRO C C   1 
ATOM   8490  O  O   . PRO C 2 129 ? 102.622 142.139 99.633  1.00 86.78  ? 106 PRO C O   1 
ATOM   8491  C  CB  . PRO C 2 129 ? 104.235 143.748 97.471  1.00 81.71  ? 106 PRO C CB  1 
ATOM   8492  C  CG  . PRO C 2 129 ? 103.795 142.580 96.662  1.00 86.34  ? 106 PRO C CG  1 
ATOM   8493  C  CD  . PRO C 2 129 ? 104.634 141.395 97.092  1.00 89.26  ? 106 PRO C CD  1 
ATOM   8494  N  N   . SER C 2 130 ? 103.438 143.937 100.712 1.00 76.53  ? 107 SER C N   1 
ATOM   8495  C  CA  . SER C 2 130 ? 102.302 144.105 101.609 1.00 69.61  ? 107 SER C CA  1 
ATOM   8496  C  C   . SER C 2 130 ? 101.691 145.468 101.333 1.00 73.17  ? 107 SER C C   1 
ATOM   8497  O  O   . SER C 2 130 ? 102.377 146.489 101.435 1.00 78.58  ? 107 SER C O   1 
ATOM   8498  C  CB  . SER C 2 130 ? 102.731 143.986 103.069 1.00 70.44  ? 107 SER C CB  1 
ATOM   8499  O  OG  . SER C 2 130 ? 103.631 142.909 103.239 1.00 78.53  ? 107 SER C OG  1 
ATOM   8500  N  N   . THR C 2 131 ? 100.408 145.487 100.991 1.00 77.18  ? 108 THR C N   1 
ATOM   8501  C  CA  . THR C 2 131 ? 99.753  146.687 100.494 1.00 79.39  ? 108 THR C CA  1 
ATOM   8502  C  C   . THR C 2 131 ? 98.576  147.064 101.379 1.00 79.10  ? 108 THR C C   1 
ATOM   8503  O  O   . THR C 2 131 ? 97.801  146.203 101.801 1.00 78.20  ? 108 THR C O   1 
ATOM   8504  C  CB  . THR C 2 131 ? 99.265  146.490 99.060  1.00 84.45  ? 108 THR C CB  1 
ATOM   8505  O  OG1 . THR C 2 131 ? 98.770  145.155 98.903  1.00 85.86  ? 108 THR C OG1 1 
ATOM   8506  C  CG2 . THR C 2 131 ? 100.398 146.723 98.078  1.00 85.65  ? 108 THR C CG2 1 
ATOM   8507  N  N   . ARG C 2 132 ? 98.449  148.361 101.652 1.00 87.97  ? 109 ARG C N   1 
ATOM   8508  C  CA  . ARG C 2 132 ? 97.289  148.863 102.373 1.00 85.39  ? 109 ARG C CA  1 
ATOM   8509  C  C   . ARG C 2 132 ? 96.057  148.933 101.485 1.00 90.96  ? 109 ARG C C   1 
ATOM   8510  O  O   . ARG C 2 132 ? 94.932  148.832 101.985 1.00 94.71  ? 109 ARG C O   1 
ATOM   8511  C  CB  . ARG C 2 132 ? 97.590  150.242 102.957 1.00 83.97  ? 109 ARG C CB  1 
ATOM   8512  C  CG  . ARG C 2 132 ? 96.596  150.701 104.002 1.00 87.23  ? 109 ARG C CG  1 
ATOM   8513  C  CD  . ARG C 2 132 ? 97.100  151.929 104.733 1.00 91.63  ? 109 ARG C CD  1 
ATOM   8514  N  NE  . ARG C 2 132 ? 97.211  151.702 106.168 1.00 95.33  ? 109 ARG C NE  1 
ATOM   8515  C  CZ  . ARG C 2 132 ? 98.358  151.614 106.827 1.00 92.04  ? 109 ARG C CZ  1 
ATOM   8516  N  NH1 . ARG C 2 132 ? 99.521  151.723 106.207 1.00 89.35  ? 109 ARG C NH1 1 
ATOM   8517  N  NH2 . ARG C 2 132 ? 98.338  151.416 108.142 1.00 89.48  ? 109 ARG C NH2 1 
ATOM   8518  N  N   . ALA C 2 133 ? 96.243  149.106 100.179 1.00 101.73 ? 110 ALA C N   1 
ATOM   8519  C  CA  . ALA C 2 133 ? 95.147  149.173 99.225  1.00 99.25  ? 110 ALA C CA  1 
ATOM   8520  C  C   . ALA C 2 133 ? 95.435  148.241 98.058  1.00 101.79 ? 110 ALA C C   1 
ATOM   8521  O  O   . ALA C 2 133 ? 96.591  148.064 97.664  1.00 104.25 ? 110 ALA C O   1 
ATOM   8522  C  CB  . ALA C 2 133 ? 94.936  150.600 98.717  1.00 96.64  ? 110 ALA C CB  1 
ATOM   8523  N  N   . ASP C 2 134 ? 94.379  147.647 97.511  1.00 107.40 ? 111 ASP C N   1 
ATOM   8524  C  CA  . ASP C 2 134 ? 94.503  146.674 96.435  1.00 106.36 ? 111 ASP C CA  1 
ATOM   8525  C  C   . ASP C 2 134 ? 93.487  146.964 95.340  1.00 107.91 ? 111 ASP C C   1 
ATOM   8526  O  O   . ASP C 2 134 ? 92.411  147.512 95.596  1.00 106.16 ? 111 ASP C O   1 
ATOM   8527  C  CB  . ASP C 2 134 ? 94.304  145.244 96.949  1.00 106.49 ? 111 ASP C CB  1 
ATOM   8528  C  CG  . ASP C 2 134 ? 95.097  144.962 98.206  1.00 108.62 ? 111 ASP C CG  1 
ATOM   8529  O  OD1 . ASP C 2 134 ? 96.342  145.033 98.150  1.00 110.51 ? 111 ASP C OD1 1 
ATOM   8530  O  OD2 . ASP C 2 134 ? 94.476  144.670 99.250  1.00 108.43 ? 111 ASP C OD2 1 
ATOM   8531  N  N   . ARG C 2 135 ? 93.836  146.574 94.115  1.00 122.33 ? 112 ARG C N   1 
ATOM   8532  C  CA  . ARG C 2 135 ? 92.954  146.726 92.964  1.00 122.74 ? 112 ARG C CA  1 
ATOM   8533  C  C   . ARG C 2 135 ? 93.009  145.450 92.138  1.00 123.07 ? 112 ARG C C   1 
ATOM   8534  O  O   . ARG C 2 135 ? 94.079  145.070 91.654  1.00 120.47 ? 112 ARG C O   1 
ATOM   8535  C  CB  . ARG C 2 135 ? 93.354  147.935 92.116  1.00 121.92 ? 112 ARG C CB  1 
ATOM   8536  C  CG  . ARG C 2 135 ? 92.783  149.249 92.616  1.00 122.23 ? 112 ARG C CG  1 
ATOM   8537  C  CD  . ARG C 2 135 ? 93.546  150.431 92.046  1.00 122.10 ? 112 ARG C CD  1 
ATOM   8538  N  NE  . ARG C 2 135 ? 94.914  150.492 92.544  1.00 125.73 ? 112 ARG C NE  1 
ATOM   8539  C  CZ  . ARG C 2 135 ? 95.280  151.099 93.665  1.00 125.63 ? 112 ARG C CZ  1 
ATOM   8540  N  NH1 . ARG C 2 135 ? 94.400  151.713 94.438  1.00 124.37 ? 112 ARG C NH1 1 
ATOM   8541  N  NH2 . ARG C 2 135 ? 96.563  151.089 94.018  1.00 123.51 ? 112 ARG C NH2 1 
ATOM   8542  N  N   . LEU C 2 136 ? 91.860  144.796 91.973  1.00 125.65 ? 113 LEU C N   1 
ATOM   8543  C  CA  . LEU C 2 136 ? 91.763  143.524 91.261  1.00 125.26 ? 113 LEU C CA  1 
ATOM   8544  C  C   . LEU C 2 136 ? 90.742  143.670 90.140  1.00 124.67 ? 113 LEU C C   1 
ATOM   8545  O  O   . LEU C 2 136 ? 89.549  143.843 90.404  1.00 123.39 ? 113 LEU C O   1 
ATOM   8546  C  CB  . LEU C 2 136 ? 91.367  142.394 92.211  1.00 123.98 ? 113 LEU C CB  1 
ATOM   8547  C  CG  . LEU C 2 136 ? 91.228  140.998 91.605  1.00 124.02 ? 113 LEU C CG  1 
ATOM   8548  C  CD1 . LEU C 2 136 ? 92.582  140.321 91.510  1.00 124.33 ? 113 LEU C CD1 1 
ATOM   8549  C  CD2 . LEU C 2 136 ? 90.262  140.156 92.418  1.00 124.67 ? 113 LEU C CD2 1 
ATOM   8550  N  N   . ALA C 2 137 ? 91.203  143.590 88.895  1.00 136.65 ? 114 ALA C N   1 
ATOM   8551  C  CA  . ALA C 2 137 ? 90.348  143.735 87.726  1.00 137.90 ? 114 ALA C CA  1 
ATOM   8552  C  C   . ALA C 2 137 ? 90.457  142.500 86.847  1.00 138.88 ? 114 ALA C C   1 
ATOM   8553  O  O   . ALA C 2 137 ? 91.554  141.976 86.634  1.00 137.03 ? 114 ALA C O   1 
ATOM   8554  C  CB  . ALA C 2 137 ? 90.724  144.977 86.915  1.00 137.60 ? 114 ALA C CB  1 
ATOM   8555  N  N   . ILE C 2 138 ? 89.320  142.040 86.332  1.00 145.65 ? 115 ILE C N   1 
ATOM   8556  C  CA  . ILE C 2 138 ? 89.314  140.901 85.417  1.00 144.71 ? 115 ILE C CA  1 
ATOM   8557  C  C   . ILE C 2 138 ? 88.026  140.921 84.609  1.00 145.96 ? 115 ILE C C   1 
ATOM   8558  O  O   . ILE C 2 138 ? 86.951  141.216 85.134  1.00 145.24 ? 115 ILE C O   1 
ATOM   8559  C  CB  . ILE C 2 138 ? 89.503  139.563 86.176  1.00 143.21 ? 115 ILE C CB  1 
ATOM   8560  C  CG1 . ILE C 2 138 ? 89.888  138.437 85.214  1.00 144.13 ? 115 ILE C CG1 1 
ATOM   8561  C  CG2 . ILE C 2 138 ? 88.273  139.188 86.975  1.00 143.88 ? 115 ILE C CG2 1 
ATOM   8562  C  CD1 . ILE C 2 138 ? 91.190  138.618 84.520  1.00 144.73 ? 115 ILE C CD1 1 
ATOM   8563  N  N   . GLY C 2 139 ? 88.146  140.624 83.319  1.00 157.25 ? 116 GLY C N   1 
ATOM   8564  C  CA  . GLY C 2 139 ? 86.998  140.337 82.482  1.00 156.92 ? 116 GLY C CA  1 
ATOM   8565  C  C   . GLY C 2 139 ? 86.886  138.831 82.331  1.00 156.47 ? 116 GLY C C   1 
ATOM   8566  O  O   . GLY C 2 139 ? 87.892  138.132 82.235  1.00 155.55 ? 116 GLY C O   1 
ATOM   8567  N  N   . PHE C 2 140 ? 85.655  138.337 82.329  1.00 162.70 ? 117 PHE C N   1 
ATOM   8568  C  CA  . PHE C 2 140 ? 85.450  136.900 82.309  1.00 163.62 ? 117 PHE C CA  1 
ATOM   8569  C  C   . PHE C 2 140 ? 84.147  136.569 81.600  1.00 164.52 ? 117 PHE C C   1 
ATOM   8570  O  O   . PHE C 2 140 ? 83.261  137.416 81.443  1.00 163.49 ? 117 PHE C O   1 
ATOM   8571  C  CB  . PHE C 2 140 ? 85.453  136.320 83.725  1.00 162.07 ? 117 PHE C CB  1 
ATOM   8572  C  CG  . PHE C 2 140 ? 84.119  136.368 84.398  1.00 162.35 ? 117 PHE C CG  1 
ATOM   8573  C  CD1 . PHE C 2 140 ? 83.540  137.581 84.724  1.00 161.62 ? 117 PHE C CD1 1 
ATOM   8574  C  CD2 . PHE C 2 140 ? 83.448  135.201 84.715  1.00 163.06 ? 117 PHE C CD2 1 
ATOM   8575  C  CE1 . PHE C 2 140 ? 82.315  137.628 85.346  1.00 162.75 ? 117 PHE C CE1 1 
ATOM   8576  C  CE2 . PHE C 2 140 ? 82.219  135.243 85.339  1.00 164.03 ? 117 PHE C CE2 1 
ATOM   8577  C  CZ  . PHE C 2 140 ? 81.653  136.458 85.656  1.00 163.99 ? 117 PHE C CZ  1 
ATOM   8578  N  N   . SER C 2 141 ? 84.054  135.313 81.173  1.00 167.29 ? 118 SER C N   1 
ATOM   8579  C  CA  . SER C 2 141 ? 82.871  134.810 80.482  1.00 166.03 ? 118 SER C CA  1 
ATOM   8580  C  C   . SER C 2 141 ? 82.746  133.325 80.791  1.00 165.91 ? 118 SER C C   1 
ATOM   8581  O  O   . SER C 2 141 ? 83.585  132.529 80.357  1.00 165.32 ? 118 SER C O   1 
ATOM   8582  C  CB  . SER C 2 141 ? 82.969  135.052 78.979  1.00 165.46 ? 118 SER C CB  1 
ATOM   8583  O  OG  . SER C 2 141 ? 84.255  134.710 78.496  1.00 165.10 ? 118 SER C OG  1 
ATOM   8584  N  N   . THR C 2 142 ? 81.715  132.963 81.550  1.00 167.60 ? 119 THR C N   1 
ATOM   8585  C  CA  . THR C 2 142 ? 81.454  131.570 81.883  1.00 168.41 ? 119 THR C CA  1 
ATOM   8586  C  C   . THR C 2 142 ? 80.017  131.447 82.364  1.00 168.55 ? 119 THR C C   1 
ATOM   8587  O  O   . THR C 2 142 ? 79.362  132.441 82.690  1.00 166.92 ? 119 THR C O   1 
ATOM   8588  C  CB  . THR C 2 142 ? 82.424  131.043 82.946  1.00 168.05 ? 119 THR C CB  1 
ATOM   8589  O  OG1 . THR C 2 142 ? 82.420  129.610 82.926  1.00 167.27 ? 119 THR C OG1 1 
ATOM   8590  C  CG2 . THR C 2 142 ? 82.016  131.524 84.333  1.00 167.93 ? 119 THR C CG2 1 
ATOM   8591  N  N   . VAL C 2 143 ? 79.537  130.205 82.404  1.00 169.05 ? 120 VAL C N   1 
ATOM   8592  C  CA  . VAL C 2 143 ? 78.175  129.897 82.813  1.00 168.27 ? 120 VAL C CA  1 
ATOM   8593  C  C   . VAL C 2 143 ? 78.137  129.036 84.068  1.00 167.74 ? 120 VAL C C   1 
ATOM   8594  O  O   . VAL C 2 143 ? 77.079  128.519 84.427  1.00 167.83 ? 120 VAL C O   1 
ATOM   8595  C  CB  . VAL C 2 143 ? 77.390  129.226 81.668  1.00 167.70 ? 120 VAL C CB  1 
ATOM   8596  C  CG1 . VAL C 2 143 ? 77.216  130.193 80.505  1.00 166.62 ? 120 VAL C CG1 1 
ATOM   8597  C  CG2 . VAL C 2 143 ? 78.096  127.959 81.213  1.00 166.63 ? 120 VAL C CG2 1 
ATOM   8598  N  N   . GLN C 2 144 ? 79.271  128.866 84.742  1.00 163.58 ? 121 GLN C N   1 
ATOM   8599  C  CA  . GLN C 2 144 ? 79.300  128.078 85.965  1.00 163.22 ? 121 GLN C CA  1 
ATOM   8600  C  C   . GLN C 2 144 ? 78.505  128.771 87.063  1.00 164.24 ? 121 GLN C C   1 
ATOM   8601  O  O   . GLN C 2 144 ? 78.531  129.998 87.194  1.00 165.25 ? 121 GLN C O   1 
ATOM   8602  C  CB  . GLN C 2 144 ? 80.739  127.854 86.424  1.00 162.68 ? 121 GLN C CB  1 
ATOM   8603  C  CG  . GLN C 2 144 ? 81.450  126.718 85.713  1.00 163.03 ? 121 GLN C CG  1 
ATOM   8604  C  CD  . GLN C 2 144 ? 82.506  126.062 86.581  1.00 163.84 ? 121 GLN C CD  1 
ATOM   8605  O  OE1 . GLN C 2 144 ? 82.921  126.617 87.597  1.00 163.83 ? 121 GLN C OE1 1 
ATOM   8606  N  NE2 . GLN C 2 144 ? 82.945  124.873 86.184  1.00 163.56 ? 121 GLN C NE2 1 
ATOM   8607  N  N   . LYS C 2 145 ? 77.781  127.976 87.850  1.00 161.89 ? 122 LYS C N   1 
ATOM   8608  C  CA  . LYS C 2 145 ? 77.002  128.523 88.952  1.00 162.02 ? 122 LYS C CA  1 
ATOM   8609  C  C   . LYS C 2 145 ? 77.824  128.676 90.226  1.00 161.67 ? 122 LYS C C   1 
ATOM   8610  O  O   . LYS C 2 145 ? 77.432  129.442 91.113  1.00 161.75 ? 122 LYS C O   1 
ATOM   8611  C  CB  . LYS C 2 145 ? 75.781  127.639 89.216  1.00 162.56 ? 122 LYS C CB  1 
ATOM   8612  C  CG  . LYS C 2 145 ? 74.588  128.373 89.806  1.00 162.89 ? 122 LYS C CG  1 
ATOM   8613  C  CD  . LYS C 2 145 ? 73.347  127.493 89.799  1.00 161.71 ? 122 LYS C CD  1 
ATOM   8614  C  CE  . LYS C 2 145 ? 72.170  128.184 90.470  1.00 161.52 ? 122 LYS C CE  1 
ATOM   8615  N  NZ  . LYS C 2 145 ? 72.385  128.358 91.934  1.00 161.75 ? 122 LYS C NZ  1 
ATOM   8616  N  N   . GLU C 2 146 ? 78.947  127.968 90.333  1.00 161.53 ? 123 GLU C N   1 
ATOM   8617  C  CA  . GLU C 2 146 ? 79.847  128.072 91.474  1.00 163.18 ? 123 GLU C CA  1 
ATOM   8618  C  C   . GLU C 2 146 ? 81.277  127.949 90.975  1.00 163.47 ? 123 GLU C C   1 
ATOM   8619  O  O   . GLU C 2 146 ? 81.611  126.973 90.296  1.00 162.97 ? 123 GLU C O   1 
ATOM   8620  C  CB  . GLU C 2 146 ? 79.563  126.982 92.514  1.00 162.29 ? 123 GLU C CB  1 
ATOM   8621  C  CG  . GLU C 2 146 ? 78.298  127.190 93.323  1.00 162.12 ? 123 GLU C CG  1 
ATOM   8622  C  CD  . GLU C 2 146 ? 78.468  128.237 94.403  1.00 162.92 ? 123 GLU C CD  1 
ATOM   8623  O  OE1 . GLU C 2 146 ? 79.625  128.582 94.724  1.00 162.98 ? 123 GLU C OE1 1 
ATOM   8624  O  OE2 . GLU C 2 146 ? 77.443  128.710 94.937  1.00 162.56 ? 123 GLU C OE2 1 
ATOM   8625  N  N   . ALA C 2 147 ? 82.119  128.925 91.311  1.00 157.02 ? 124 ALA C N   1 
ATOM   8626  C  CA  . ALA C 2 147 ? 83.502  128.884 90.854  1.00 155.98 ? 124 ALA C CA  1 
ATOM   8627  C  C   . ALA C 2 147 ? 84.359  129.771 91.742  1.00 155.81 ? 124 ALA C C   1 
ATOM   8628  O  O   . ALA C 2 147 ? 83.851  130.601 92.496  1.00 155.26 ? 124 ALA C O   1 
ATOM   8629  C  CB  . ALA C 2 147 ? 83.623  129.319 89.389  1.00 155.40 ? 124 ALA C CB  1 
ATOM   8630  N  N   . VAL C 2 148 ? 85.672  129.581 91.640  1.00 147.64 ? 125 VAL C N   1 
ATOM   8631  C  CA  . VAL C 2 148 ? 86.659  130.448 92.275  1.00 145.28 ? 125 VAL C CA  1 
ATOM   8632  C  C   . VAL C 2 148 ? 87.633  130.892 91.195  1.00 145.32 ? 125 VAL C C   1 
ATOM   8633  O  O   . VAL C 2 148 ? 88.354  130.061 90.630  1.00 144.48 ? 125 VAL C O   1 
ATOM   8634  C  CB  . VAL C 2 148 ? 87.403  129.740 93.419  1.00 144.94 ? 125 VAL C CB  1 
ATOM   8635  C  CG1 . VAL C 2 148 ? 88.560  130.594 93.907  1.00 144.58 ? 125 VAL C CG1 1 
ATOM   8636  C  CG2 . VAL C 2 148 ? 86.449  129.426 94.559  1.00 145.39 ? 125 VAL C CG2 1 
ATOM   8637  N  N   . LEU C 2 149 ? 87.659  132.193 90.906  1.00 140.32 ? 126 LEU C N   1 
ATOM   8638  C  CA  . LEU C 2 149 ? 88.445  132.699 89.786  1.00 139.16 ? 126 LEU C CA  1 
ATOM   8639  C  C   . LEU C 2 149 ? 89.874  133.035 90.201  1.00 139.70 ? 126 LEU C C   1 
ATOM   8640  O  O   . LEU C 2 149 ? 90.832  132.466 89.668  1.00 139.20 ? 126 LEU C O   1 
ATOM   8641  C  CB  . LEU C 2 149 ? 87.757  133.927 89.180  1.00 137.79 ? 126 LEU C CB  1 
ATOM   8642  C  CG  . LEU C 2 149 ? 86.352  133.704 88.616  1.00 139.55 ? 126 LEU C CG  1 
ATOM   8643  C  CD1 . LEU C 2 149 ? 85.286  134.043 89.648  1.00 139.29 ? 126 LEU C CD1 1 
ATOM   8644  C  CD2 . LEU C 2 149 ? 86.147  134.516 87.346  1.00 140.20 ? 126 LEU C CD2 1 
ATOM   8645  N  N   . VAL C 2 150 ? 90.032  133.955 91.150  1.00 132.68 ? 127 VAL C N   1 
ATOM   8646  C  CA  . VAL C 2 150 ? 91.341  134.406 91.607  1.00 131.21 ? 127 VAL C CA  1 
ATOM   8647  C  C   . VAL C 2 150 ? 91.396  134.276 93.121  1.00 129.38 ? 127 VAL C C   1 
ATOM   8648  O  O   . VAL C 2 150 ? 90.473  134.707 93.820  1.00 127.99 ? 127 VAL C O   1 
ATOM   8649  C  CB  . VAL C 2 150 ? 91.630  135.857 91.179  1.00 130.17 ? 127 VAL C CB  1 
ATOM   8650  C  CG1 . VAL C 2 150 ? 92.949  136.329 91.763  1.00 129.59 ? 127 VAL C CG1 1 
ATOM   8651  C  CG2 . VAL C 2 150 ? 91.646  135.971 89.665  1.00 129.80 ? 127 VAL C CG2 1 
ATOM   8652  N  N   . ARG C 2 151 ? 92.476  133.682 93.624  1.00 122.65 ? 128 ARG C N   1 
ATOM   8653  C  CA  . ARG C 2 151 ? 92.695  133.514 95.055  1.00 122.58 ? 128 ARG C CA  1 
ATOM   8654  C  C   . ARG C 2 151 ? 94.112  133.959 95.378  1.00 123.99 ? 128 ARG C C   1 
ATOM   8655  O  O   . ARG C 2 151 ? 95.075  133.360 94.891  1.00 125.46 ? 128 ARG C O   1 
ATOM   8656  C  CB  . ARG C 2 151 ? 92.478  132.058 95.475  1.00 123.25 ? 128 ARG C CB  1 
ATOM   8657  C  CG  . ARG C 2 151 ? 93.022  131.710 96.845  1.00 121.22 ? 128 ARG C CG  1 
ATOM   8658  C  CD  . ARG C 2 151 ? 92.207  132.368 97.933  1.00 121.85 ? 128 ARG C CD  1 
ATOM   8659  N  NE  . ARG C 2 151 ? 92.363  131.692 99.213  1.00 123.54 ? 128 ARG C NE  1 
ATOM   8660  C  CZ  . ARG C 2 151 ? 91.362  131.164 99.904  1.00 123.89 ? 128 ARG C CZ  1 
ATOM   8661  N  NH1 . ARG C 2 151 ? 90.116  131.217 99.464  1.00 122.57 ? 128 ARG C NH1 1 
ATOM   8662  N  NH2 . ARG C 2 151 ? 91.618  130.570 101.066 1.00 123.95 ? 128 ARG C NH2 1 
ATOM   8663  N  N   . VAL C 2 152 ? 94.239  135.002 96.192  1.00 111.80 ? 129 VAL C N   1 
ATOM   8664  C  CA  . VAL C 2 152 ? 95.531  135.560 96.573  1.00 109.08 ? 129 VAL C CA  1 
ATOM   8665  C  C   . VAL C 2 152 ? 95.820  135.162 98.012  1.00 110.10 ? 129 VAL C C   1 
ATOM   8666  O  O   . VAL C 2 152 ? 94.996  135.396 98.904  1.00 110.47 ? 129 VAL C O   1 
ATOM   8667  C  CB  . VAL C 2 152 ? 95.556  137.088 96.412  1.00 108.26 ? 129 VAL C CB  1 
ATOM   8668  C  CG1 . VAL C 2 152 ? 96.947  137.620 96.694  1.00 109.62 ? 129 VAL C CG1 1 
ATOM   8669  C  CG2 . VAL C 2 152 ? 95.107  137.476 95.020  1.00 110.64 ? 129 VAL C CG2 1 
ATOM   8670  N  N   . ASP C 2 153 ? 96.987  134.569 98.237  1.00 108.90 ? 130 ASP C N   1 
ATOM   8671  C  CA  . ASP C 2 153 ? 97.362  134.061 99.546  1.00 108.81 ? 130 ASP C CA  1 
ATOM   8672  C  C   . ASP C 2 153 ? 98.575  134.808 100.080 1.00 106.98 ? 130 ASP C C   1 
ATOM   8673  O  O   . ASP C 2 153 ? 99.370  135.376 99.328  1.00 109.75 ? 130 ASP C O   1 
ATOM   8674  C  CB  . ASP C 2 153 ? 97.669  132.558 99.496  1.00 111.48 ? 130 ASP C CB  1 
ATOM   8675  C  CG  . ASP C 2 153 ? 96.423  131.703 99.600  1.00 113.27 ? 130 ASP C CG  1 
ATOM   8676  O  OD1 . ASP C 2 153 ? 95.607  131.944 100.513 1.00 113.31 ? 130 ASP C OD1 1 
ATOM   8677  O  OD2 . ASP C 2 153 ? 96.262  130.784 98.770  1.00 111.75 ? 130 ASP C OD2 1 
ATOM   8678  N  N   . SER C 2 154 ? 98.707  134.794 101.399 1.00 99.85  ? 131 SER C N   1 
ATOM   8679  C  CA  . SER C 2 154 ? 99.879  135.333 102.065 1.00 101.28 ? 131 SER C CA  1 
ATOM   8680  C  C   . SER C 2 154 ? 100.970 134.266 102.085 1.00 101.06 ? 131 SER C C   1 
ATOM   8681  O  O   . SER C 2 154 ? 100.888 133.250 101.390 1.00 102.25 ? 131 SER C O   1 
ATOM   8682  C  CB  . SER C 2 154 ? 99.513  135.813 103.465 1.00 100.43 ? 131 SER C CB  1 
ATOM   8683  O  OG  . SER C 2 154 ? 98.508  134.993 104.033 1.00 98.94  ? 131 SER C OG  1 
ATOM   8684  N  N   . SER C 2 155 ? 102.011 134.484 102.878 1.00 98.77  ? 132 SER C N   1 
ATOM   8685  C  CA  . SER C 2 155 ? 103.084 133.509 103.001 1.00 99.35  ? 132 SER C CA  1 
ATOM   8686  C  C   . SER C 2 155 ? 102.633 132.382 103.928 1.00 101.17 ? 132 SER C C   1 
ATOM   8687  O  O   . SER C 2 155 ? 101.448 132.232 104.235 1.00 97.92  ? 132 SER C O   1 
ATOM   8688  C  CB  . SER C 2 155 ? 104.361 134.184 103.488 1.00 99.89  ? 132 SER C CB  1 
ATOM   8689  O  OG  . SER C 2 155 ? 105.505 133.529 102.973 1.00 98.19  ? 132 SER C OG  1 
ATOM   8690  N  N   . SER C 2 156 ? 103.580 131.562 104.375 1.00 108.23 ? 133 SER C N   1 
ATOM   8691  C  CA  . SER C 2 156 ? 103.245 130.423 105.219 1.00 108.86 ? 133 SER C CA  1 
ATOM   8692  C  C   . SER C 2 156 ? 102.765 130.888 106.589 1.00 109.41 ? 133 SER C C   1 
ATOM   8693  O  O   . SER C 2 156 ? 103.417 131.706 107.245 1.00 107.85 ? 133 SER C O   1 
ATOM   8694  C  CB  . SER C 2 156 ? 104.456 129.506 105.368 1.00 108.52 ? 133 SER C CB  1 
ATOM   8695  O  OG  . SER C 2 156 ? 105.567 130.216 105.884 1.00 107.77 ? 133 SER C OG  1 
ATOM   8696  N  N   . GLY C 2 157 ? 101.627 130.359 107.022 1.00 104.51 ? 134 GLY C N   1 
ATOM   8697  C  CA  . GLY C 2 157 ? 101.092 130.615 108.350 1.00 104.87 ? 134 GLY C CA  1 
ATOM   8698  C  C   . GLY C 2 157 ? 100.107 131.759 108.475 1.00 102.71 ? 134 GLY C C   1 
ATOM   8699  O  O   . GLY C 2 157 ? 99.132  131.657 109.221 1.00 102.61 ? 134 GLY C O   1 
ATOM   8700  N  N   . LEU C 2 158 ? 100.349 132.854 107.761 1.00 96.99  ? 135 LEU C N   1 
ATOM   8701  C  CA  . LEU C 2 158 ? 99.484  134.020 107.863 1.00 96.32  ? 135 LEU C CA  1 
ATOM   8702  C  C   . LEU C 2 158 ? 98.116  133.737 107.256 1.00 96.74  ? 135 LEU C C   1 
ATOM   8703  O  O   . LEU C 2 158 ? 98.001  133.076 106.221 1.00 99.25  ? 135 LEU C O   1 
ATOM   8704  C  CB  . LEU C 2 158 ? 100.135 135.217 107.174 1.00 95.71  ? 135 LEU C CB  1 
ATOM   8705  C  CG  . LEU C 2 158 ? 101.344 135.793 107.907 1.00 90.84  ? 135 LEU C CG  1 
ATOM   8706  C  CD1 . LEU C 2 158 ? 102.438 136.181 106.934 1.00 88.81  ? 135 LEU C CD1 1 
ATOM   8707  C  CD2 . LEU C 2 158 ? 100.919 136.981 108.736 1.00 90.63  ? 135 LEU C CD2 1 
ATOM   8708  N  N   . GLY C 2 159 ? 97.075  134.248 107.908 1.00 93.91  ? 136 GLY C N   1 
ATOM   8709  C  CA  . GLY C 2 159 ? 95.712  134.005 107.480 1.00 94.46  ? 136 GLY C CA  1 
ATOM   8710  C  C   . GLY C 2 159 ? 95.149  135.097 106.594 1.00 97.53  ? 136 GLY C C   1 
ATOM   8711  O  O   . GLY C 2 159 ? 93.930  135.228 106.455 1.00 97.36  ? 136 GLY C O   1 
ATOM   8712  N  N   . ASP C 2 160 ? 96.030  135.892 105.996 1.00 95.04  ? 137 ASP C N   1 
ATOM   8713  C  CA  . ASP C 2 160 ? 95.609  136.997 105.148 1.00 93.28  ? 137 ASP C CA  1 
ATOM   8714  C  C   . ASP C 2 160 ? 95.376  136.494 103.730 1.00 95.96  ? 137 ASP C C   1 
ATOM   8715  O  O   . ASP C 2 160 ? 96.266  135.882 103.132 1.00 94.96  ? 137 ASP C O   1 
ATOM   8716  C  CB  . ASP C 2 160 ? 96.675  138.090 105.153 1.00 91.90  ? 137 ASP C CB  1 
ATOM   8717  C  CG  . ASP C 2 160 ? 96.532  139.031 106.327 1.00 94.47  ? 137 ASP C CG  1 
ATOM   8718  O  OD1 . ASP C 2 160 ? 95.390  139.390 106.647 1.00 93.84  ? 137 ASP C OD1 1 
ATOM   8719  O  OD2 . ASP C 2 160 ? 97.555  139.414 106.931 1.00 96.64  ? 137 ASP C OD2 1 
ATOM   8720  N  N   . TYR C 2 161 ? 94.185  136.746 103.186 1.00 105.42 ? 138 TYR C N   1 
ATOM   8721  C  CA  . TYR C 2 161 ? 93.895  136.236 101.850 1.00 104.77 ? 138 TYR C CA  1 
ATOM   8722  C  C   . TYR C 2 161 ? 92.812  137.076 101.190 1.00 105.44 ? 138 TYR C C   1 
ATOM   8723  O  O   . TYR C 2 161 ? 92.078  137.810 101.851 1.00 106.05 ? 138 TYR C O   1 
ATOM   8724  C  CB  . TYR C 2 161 ? 93.501  134.751 101.892 1.00 102.56 ? 138 TYR C CB  1 
ATOM   8725  C  CG  . TYR C 2 161 ? 92.114  134.438 102.429 1.00 104.64 ? 138 TYR C CG  1 
ATOM   8726  C  CD1 . TYR C 2 161 ? 90.976  134.644 101.660 1.00 106.42 ? 138 TYR C CD1 1 
ATOM   8727  C  CD2 . TYR C 2 161 ? 91.955  133.874 103.686 1.00 106.34 ? 138 TYR C CD2 1 
ATOM   8728  C  CE1 . TYR C 2 161 ? 89.720  134.344 102.147 1.00 107.96 ? 138 TYR C CE1 1 
ATOM   8729  C  CE2 . TYR C 2 161 ? 90.702  133.570 104.181 1.00 108.42 ? 138 TYR C CE2 1 
ATOM   8730  C  CZ  . TYR C 2 161 ? 89.590  133.805 103.407 1.00 109.14 ? 138 TYR C CZ  1 
ATOM   8731  O  OH  . TYR C 2 161 ? 88.342  133.500 103.895 1.00 105.89 ? 138 TYR C OH  1 
ATOM   8732  N  N   . LEU C 2 162 ? 92.725  136.947 99.867  1.00 108.96 ? 139 LEU C N   1 
ATOM   8733  C  CA  . LEU C 2 162 ? 91.734  137.647 99.060  1.00 107.63 ? 139 LEU C CA  1 
ATOM   8734  C  C   . LEU C 2 162 ? 91.321  136.739 97.914  1.00 110.95 ? 139 LEU C C   1 
ATOM   8735  O  O   . LEU C 2 162 ? 92.180  136.238 97.184  1.00 111.05 ? 139 LEU C O   1 
ATOM   8736  C  CB  . LEU C 2 162 ? 92.292  138.966 98.516  1.00 106.35 ? 139 LEU C CB  1 
ATOM   8737  C  CG  . LEU C 2 162 ? 91.562  139.611 97.337  1.00 107.78 ? 139 LEU C CG  1 
ATOM   8738  C  CD1 . LEU C 2 162 ? 90.382  140.420 97.821  1.00 108.47 ? 139 LEU C CD1 1 
ATOM   8739  C  CD2 . LEU C 2 162 ? 92.506  140.483 96.534  1.00 109.32 ? 139 LEU C CD2 1 
ATOM   8740  N  N   . GLU C 2 163 ? 90.014  136.530 97.751  1.00 132.22 ? 140 GLU C N   1 
ATOM   8741  C  CA  . GLU C 2 163 ? 89.504  135.597 96.758  1.00 131.92 ? 140 GLU C CA  1 
ATOM   8742  C  C   . GLU C 2 163 ? 88.313  136.204 96.034  1.00 131.34 ? 140 GLU C C   1 
ATOM   8743  O  O   . GLU C 2 163 ? 87.464  136.853 96.650  1.00 129.66 ? 140 GLU C O   1 
ATOM   8744  C  CB  . GLU C 2 163 ? 89.101  134.270 97.415  1.00 131.43 ? 140 GLU C CB  1 
ATOM   8745  C  CG  . GLU C 2 163 ? 88.059  133.469 96.653  1.00 133.07 ? 140 GLU C CG  1 
ATOM   8746  C  CD  . GLU C 2 163 ? 87.212  132.605 97.567  1.00 134.87 ? 140 GLU C CD  1 
ATOM   8747  O  OE1 . GLU C 2 163 ? 87.127  132.918 98.773  1.00 132.84 ? 140 GLU C OE1 1 
ATOM   8748  O  OE2 . GLU C 2 163 ? 86.631  131.612 97.081  1.00 135.28 ? 140 GLU C OE2 1 
ATOM   8749  N  N   . LEU C 2 164 ? 88.262  136.002 94.722  1.00 138.17 ? 141 LEU C N   1 
ATOM   8750  C  CA  . LEU C 2 164 ? 87.109  136.358 93.908  1.00 139.50 ? 141 LEU C CA  1 
ATOM   8751  C  C   . LEU C 2 164 ? 86.408  135.073 93.493  1.00 142.09 ? 141 LEU C C   1 
ATOM   8752  O  O   . LEU C 2 164 ? 87.048  134.163 92.956  1.00 143.01 ? 141 LEU C O   1 
ATOM   8753  C  CB  . LEU C 2 164 ? 87.535  137.165 92.681  1.00 138.51 ? 141 LEU C CB  1 
ATOM   8754  C  CG  . LEU C 2 164 ? 86.462  137.523 91.652  1.00 141.31 ? 141 LEU C CG  1 
ATOM   8755  C  CD1 . LEU C 2 164 ? 85.258  138.143 92.329  1.00 141.64 ? 141 LEU C CD1 1 
ATOM   8756  C  CD2 . LEU C 2 164 ? 87.027  138.465 90.599  1.00 140.46 ? 141 LEU C CD2 1 
ATOM   8757  N  N   . HIS C 2 165 ? 85.104  134.984 93.753  1.00 145.37 ? 142 HIS C N   1 
ATOM   8758  C  CA  . HIS C 2 165 ? 84.413  133.730 93.503  1.00 144.36 ? 142 HIS C CA  1 
ATOM   8759  C  C   . HIS C 2 165 ? 82.953  133.988 93.167  1.00 146.64 ? 142 HIS C C   1 
ATOM   8760  O  O   . HIS C 2 165 ? 82.373  135.002 93.562  1.00 145.52 ? 142 HIS C O   1 
ATOM   8761  C  CB  . HIS C 2 165 ? 84.519  132.785 94.706  1.00 144.19 ? 142 HIS C CB  1 
ATOM   8762  C  CG  . HIS C 2 165 ? 83.789  133.266 95.921  1.00 144.89 ? 142 HIS C CG  1 
ATOM   8763  N  ND1 . HIS C 2 165 ? 82.676  132.626 96.421  1.00 145.03 ? 142 HIS C ND1 1 
ATOM   8764  C  CD2 . HIS C 2 165 ? 84.011  134.325 96.734  1.00 144.62 ? 142 HIS C CD2 1 
ATOM   8765  C  CE1 . HIS C 2 165 ? 82.245  133.268 97.492  1.00 144.68 ? 142 HIS C CE1 1 
ATOM   8766  N  NE2 . HIS C 2 165 ? 83.038  134.304 97.703  1.00 144.80 ? 142 HIS C NE2 1 
ATOM   8767  N  N   . ILE C 2 166 ? 82.368  133.040 92.442  1.00 159.70 ? 143 ILE C N   1 
ATOM   8768  C  CA  . ILE C 2 166 ? 80.964  133.062 92.054  1.00 158.19 ? 143 ILE C CA  1 
ATOM   8769  C  C   . ILE C 2 166 ? 80.229  132.049 92.919  1.00 156.90 ? 143 ILE C C   1 
ATOM   8770  O  O   . ILE C 2 166 ? 80.504  130.843 92.849  1.00 156.69 ? 143 ILE C O   1 
ATOM   8771  C  CB  . ILE C 2 166 ? 80.785  132.743 90.563  1.00 157.28 ? 143 ILE C CB  1 
ATOM   8772  C  CG1 . ILE C 2 166 ? 81.226  133.926 89.703  1.00 157.85 ? 143 ILE C CG1 1 
ATOM   8773  C  CG2 . ILE C 2 166 ? 79.345  132.383 90.266  1.00 157.42 ? 143 ILE C CG2 1 
ATOM   8774  C  CD1 . ILE C 2 166 ? 80.934  133.739 88.233  1.00 157.82 ? 143 ILE C CD1 1 
ATOM   8775  N  N   . HIS C 2 167 ? 79.300  132.542 93.733  1.00 159.98 ? 144 HIS C N   1 
ATOM   8776  C  CA  . HIS C 2 167 ? 78.473  131.722 94.608  1.00 161.82 ? 144 HIS C CA  1 
ATOM   8777  C  C   . HIS C 2 167 ? 77.023  131.861 94.166  1.00 163.27 ? 144 HIS C C   1 
ATOM   8778  O  O   . HIS C 2 167 ? 76.487  132.974 94.133  1.00 162.89 ? 144 HIS C O   1 
ATOM   8779  C  CB  . HIS C 2 167 ? 78.641  132.148 96.068  1.00 161.83 ? 144 HIS C CB  1 
ATOM   8780  C  CG  . HIS C 2 167 ? 77.799  131.370 97.031  1.00 162.46 ? 144 HIS C CG  1 
ATOM   8781  N  ND1 . HIS C 2 167 ? 78.067  130.060 97.365  1.00 163.09 ? 144 HIS C ND1 1 
ATOM   8782  C  CD2 . HIS C 2 167 ? 76.700  131.721 97.739  1.00 161.23 ? 144 HIS C CD2 1 
ATOM   8783  C  CE1 . HIS C 2 167 ? 77.168  129.637 98.234  1.00 161.70 ? 144 HIS C CE1 1 
ATOM   8784  N  NE2 . HIS C 2 167 ? 76.326  130.626 98.478  1.00 161.83 ? 144 HIS C NE2 1 
ATOM   8785  N  N   . GLN C 2 168 ? 76.399  130.732 93.819  1.00 165.43 ? 145 GLN C N   1 
ATOM   8786  C  CA  . GLN C 2 168 ? 75.010  130.699 93.350  1.00 164.84 ? 145 GLN C CA  1 
ATOM   8787  C  C   . GLN C 2 168 ? 74.804  131.623 92.152  1.00 164.70 ? 145 GLN C C   1 
ATOM   8788  O  O   . GLN C 2 168 ? 73.739  132.218 91.973  1.00 163.54 ? 145 GLN C O   1 
ATOM   8789  C  CB  . GLN C 2 168 ? 74.035  131.052 94.475  1.00 164.99 ? 145 GLN C CB  1 
ATOM   8790  C  CG  . GLN C 2 168 ? 74.146  130.180 95.710  1.00 164.29 ? 145 GLN C CG  1 
ATOM   8791  C  CD  . GLN C 2 168 ? 73.178  130.603 96.798  1.00 164.62 ? 145 GLN C CD  1 
ATOM   8792  O  OE1 . GLN C 2 168 ? 72.340  131.480 96.591  1.00 164.60 ? 145 GLN C OE1 1 
ATOM   8793  N  NE2 . GLN C 2 168 ? 73.287  129.978 97.964  1.00 164.73 ? 145 GLN C NE2 1 
ATOM   8794  N  N   . GLY C 2 169 ? 75.837  131.748 91.322  1.00 166.19 ? 146 GLY C N   1 
ATOM   8795  C  CA  . GLY C 2 169 ? 75.797  132.595 90.155  1.00 166.47 ? 146 GLY C CA  1 
ATOM   8796  C  C   . GLY C 2 169 ? 76.212  134.032 90.402  1.00 168.03 ? 146 GLY C C   1 
ATOM   8797  O  O   . GLY C 2 169 ? 76.549  134.741 89.448  1.00 167.33 ? 146 GLY C O   1 
ATOM   8798  N  N   . LYS C 2 170 ? 76.203  134.477 91.656  1.00 164.41 ? 147 LYS C N   1 
ATOM   8799  C  CA  . LYS C 2 170 ? 76.535  135.860 91.974  1.00 163.47 ? 147 LYS C CA  1 
ATOM   8800  C  C   . LYS C 2 170 ? 78.027  135.995 92.245  1.00 162.44 ? 147 LYS C C   1 
ATOM   8801  O  O   . LYS C 2 170 ? 78.593  135.234 93.033  1.00 161.27 ? 147 LYS C O   1 
ATOM   8802  C  CB  . LYS C 2 170 ? 75.731  136.331 93.183  1.00 162.38 ? 147 LYS C CB  1 
ATOM   8803  C  CG  . LYS C 2 170 ? 74.234  136.121 93.040  1.00 162.20 ? 147 LYS C CG  1 
ATOM   8804  C  CD  . LYS C 2 170 ? 73.726  136.677 91.721  1.00 161.90 ? 147 LYS C CD  1 
ATOM   8805  C  CE  . LYS C 2 170 ? 72.525  135.893 91.231  1.00 161.85 ? 147 LYS C CE  1 
ATOM   8806  N  NZ  . LYS C 2 170 ? 72.798  134.429 91.252  1.00 161.51 ? 147 LYS C NZ  1 
ATOM   8807  N  N   . ILE C 2 171 ? 78.662  136.965 91.594  1.00 155.85 ? 148 ILE C N   1 
ATOM   8808  C  CA  . ILE C 2 171 ? 80.090  137.194 91.777  1.00 154.73 ? 148 ILE C CA  1 
ATOM   8809  C  C   . ILE C 2 171 ? 80.306  138.009 93.045  1.00 155.00 ? 148 ILE C C   1 
ATOM   8810  O  O   . ILE C 2 171 ? 79.491  138.871 93.397  1.00 154.94 ? 148 ILE C O   1 
ATOM   8811  C  CB  . ILE C 2 171 ? 80.690  137.886 90.539  1.00 153.76 ? 148 ILE C CB  1 
ATOM   8812  C  CG1 . ILE C 2 171 ? 82.201  137.662 90.483  1.00 153.81 ? 148 ILE C CG1 1 
ATOM   8813  C  CG2 . ILE C 2 171 ? 80.367  139.372 90.527  1.00 153.34 ? 148 ILE C CG2 1 
ATOM   8814  C  CD1 . ILE C 2 171 ? 82.797  137.870 89.110  1.00 153.63 ? 148 ILE C CD1 1 
ATOM   8815  N  N   . GLY C 2 172 ? 81.394  137.721 93.755  1.00 143.65 ? 149 GLY C N   1 
ATOM   8816  C  CA  . GLY C 2 172 ? 81.673  138.409 95.000  1.00 141.91 ? 149 GLY C CA  1 
ATOM   8817  C  C   . GLY C 2 172 ? 83.101  138.197 95.438  1.00 142.40 ? 149 GLY C C   1 
ATOM   8818  O  O   . GLY C 2 172 ? 83.724  137.177 95.121  1.00 142.50 ? 149 GLY C O   1 
ATOM   8819  N  N   . VAL C 2 173 ? 83.615  139.162 96.196  1.00 136.75 ? 150 VAL C N   1 
ATOM   8820  C  CA  . VAL C 2 173 ? 84.986  139.150 96.690  1.00 136.92 ? 150 VAL C CA  1 
ATOM   8821  C  C   . VAL C 2 173 ? 84.955  138.931 98.196  1.00 135.08 ? 150 VAL C C   1 
ATOM   8822  O  O   . VAL C 2 173 ? 84.253  139.645 98.924  1.00 134.22 ? 150 VAL C O   1 
ATOM   8823  C  CB  . VAL C 2 173 ? 85.723  140.453 96.337  1.00 136.69 ? 150 VAL C CB  1 
ATOM   8824  C  CG1 . VAL C 2 173 ? 86.798  140.751 97.366  1.00 135.67 ? 150 VAL C CG1 1 
ATOM   8825  C  CG2 . VAL C 2 173 ? 86.332  140.352 94.952  1.00 135.38 ? 150 VAL C CG2 1 
ATOM   8826  N  N   . LYS C 2 174 ? 85.719  137.946 98.657  1.00 125.16 ? 151 LYS C N   1 
ATOM   8827  C  CA  . LYS C 2 174 ? 85.820  137.592 100.065 1.00 126.08 ? 151 LYS C CA  1 
ATOM   8828  C  C   . LYS C 2 174 ? 87.281  137.716 100.474 1.00 128.29 ? 151 LYS C C   1 
ATOM   8829  O  O   . LYS C 2 174 ? 88.143  137.037 99.908  1.00 127.62 ? 151 LYS C O   1 
ATOM   8830  C  CB  . LYS C 2 174 ? 85.306  136.168 100.289 1.00 126.06 ? 151 LYS C CB  1 
ATOM   8831  C  CG  . LYS C 2 174 ? 84.730  135.898 101.660 1.00 126.10 ? 151 LYS C CG  1 
ATOM   8832  C  CD  . LYS C 2 174 ? 84.130  134.503 101.742 1.00 126.69 ? 151 LYS C CD  1 
ATOM   8833  C  CE  . LYS C 2 174 ? 85.187  133.436 101.508 1.00 126.56 ? 151 LYS C CE  1 
ATOM   8834  N  NZ  . LYS C 2 174 ? 84.655  132.062 101.723 1.00 126.68 ? 151 LYS C NZ  1 
ATOM   8835  N  N   . PHE C 2 175 ? 87.568  138.587 101.441 1.00 115.83 ? 152 PHE C N   1 
ATOM   8836  C  CA  . PHE C 2 175 ? 88.939  138.787 101.887 1.00 109.33 ? 152 PHE C CA  1 
ATOM   8837  C  C   . PHE C 2 175 ? 89.016  138.786 103.405 1.00 108.40 ? 152 PHE C C   1 
ATOM   8838  O  O   . PHE C 2 175 ? 88.099  139.235 104.098 1.00 108.89 ? 152 PHE C O   1 
ATOM   8839  C  CB  . PHE C 2 175 ? 89.541  140.091 101.336 1.00 109.63 ? 152 PHE C CB  1 
ATOM   8840  C  CG  . PHE C 2 175 ? 88.805  141.334 101.748 1.00 108.65 ? 152 PHE C CG  1 
ATOM   8841  C  CD1 . PHE C 2 175 ? 89.153  142.012 102.901 1.00 108.70 ? 152 PHE C CD1 1 
ATOM   8842  C  CD2 . PHE C 2 175 ? 87.782  141.838 100.969 1.00 110.67 ? 152 PHE C CD2 1 
ATOM   8843  C  CE1 . PHE C 2 175 ? 88.485  143.157 103.276 1.00 109.88 ? 152 PHE C CE1 1 
ATOM   8844  C  CE2 . PHE C 2 175 ? 87.111  142.984 101.341 1.00 110.62 ? 152 PHE C CE2 1 
ATOM   8845  C  CZ  . PHE C 2 175 ? 87.464  143.643 102.496 1.00 109.82 ? 152 PHE C CZ  1 
ATOM   8846  N  N   . ASN C 2 176 ? 90.135  138.275 103.908 1.00 103.76 ? 153 ASN C N   1 
ATOM   8847  C  CA  . ASN C 2 176 ? 90.444  138.252 105.330 1.00 103.60 ? 153 ASN C CA  1 
ATOM   8848  C  C   . ASN C 2 176 ? 91.744  139.010 105.540 1.00 105.56 ? 153 ASN C C   1 
ATOM   8849  O  O   . ASN C 2 176 ? 92.801  138.581 105.059 1.00 104.27 ? 153 ASN C O   1 
ATOM   8850  C  CB  . ASN C 2 176 ? 90.565  136.817 105.842 1.00 104.96 ? 153 ASN C CB  1 
ATOM   8851  C  CG  . ASN C 2 176 ? 90.447  136.725 107.346 1.00 105.38 ? 153 ASN C CG  1 
ATOM   8852  O  OD1 . ASN C 2 176 ? 89.475  137.197 107.935 1.00 104.19 ? 153 ASN C OD1 1 
ATOM   8853  N  ND2 . ASN C 2 176 ? 91.439  136.110 107.979 1.00 105.78 ? 153 ASN C ND2 1 
ATOM   8854  N  N   . VAL C 2 177 ? 91.660  140.136 106.250 1.00 98.64  ? 154 VAL C N   1 
ATOM   8855  C  CA  . VAL C 2 177 ? 92.810  140.983 106.539 1.00 95.32  ? 154 VAL C CA  1 
ATOM   8856  C  C   . VAL C 2 177 ? 93.292  140.842 107.971 1.00 94.88  ? 154 VAL C C   1 
ATOM   8857  O  O   . VAL C 2 177 ? 94.285  141.483 108.342 1.00 94.42  ? 154 VAL C O   1 
ATOM   8858  C  CB  . VAL C 2 177 ? 92.515  142.459 106.219 1.00 92.01  ? 154 VAL C CB  1 
ATOM   8859  C  CG1 . VAL C 2 177 ? 92.463  142.667 104.719 1.00 92.00  ? 154 VAL C CG1 1 
ATOM   8860  C  CG2 . VAL C 2 177 ? 91.215  142.889 106.867 1.00 93.23  ? 154 VAL C CG2 1 
ATOM   8861  N  N   . GLY C 2 178 ? 92.639  140.014 108.785 1.00 99.18  ? 155 GLY C N   1 
ATOM   8862  C  CA  . GLY C 2 178 ? 93.142  139.726 110.114 1.00 97.11  ? 155 GLY C CA  1 
ATOM   8863  C  C   . GLY C 2 178 ? 92.110  139.696 111.223 1.00 98.84  ? 155 GLY C C   1 
ATOM   8864  O  O   . GLY C 2 178 ? 92.255  138.928 112.178 1.00 97.45  ? 155 GLY C O   1 
ATOM   8865  N  N   . THR C 2 179 ? 91.067  140.520 111.123 1.00 111.74 ? 156 THR C N   1 
ATOM   8866  C  CA  . THR C 2 179 ? 90.044  140.558 112.164 1.00 112.23 ? 156 THR C CA  1 
ATOM   8867  C  C   . THR C 2 179 ? 88.907  139.589 111.867 1.00 113.75 ? 156 THR C C   1 
ATOM   8868  O  O   . THR C 2 179 ? 88.666  138.645 112.627 1.00 112.90 ? 156 THR C O   1 
ATOM   8869  C  CB  . THR C 2 179 ? 89.478  141.974 112.309 1.00 111.18 ? 156 THR C CB  1 
ATOM   8870  O  OG1 . THR C 2 179 ? 88.412  142.157 111.371 1.00 111.21 ? 156 THR C OG1 1 
ATOM   8871  C  CG2 . THR C 2 179 ? 90.542  142.995 112.035 1.00 109.33 ? 156 THR C CG2 1 
ATOM   8872  N  N   . ASP C 2 180 ? 88.207  139.812 110.760 1.00 122.99 ? 157 ASP C N   1 
ATOM   8873  C  CA  . ASP C 2 180 ? 87.070  138.992 110.382 1.00 121.99 ? 157 ASP C CA  1 
ATOM   8874  C  C   . ASP C 2 180 ? 87.026  138.903 108.867 1.00 120.80 ? 157 ASP C C   1 
ATOM   8875  O  O   . ASP C 2 180 ? 87.518  139.785 108.159 1.00 120.30 ? 157 ASP C O   1 
ATOM   8876  C  CB  . ASP C 2 180 ? 85.754  139.564 110.925 1.00 121.67 ? 157 ASP C CB  1 
ATOM   8877  C  CG  . ASP C 2 180 ? 85.658  139.477 112.437 1.00 123.66 ? 157 ASP C CG  1 
ATOM   8878  O  OD1 . ASP C 2 180 ? 85.679  138.349 112.973 1.00 123.21 ? 157 ASP C OD1 1 
ATOM   8879  O  OD2 . ASP C 2 180 ? 85.563  140.537 113.090 1.00 123.52 ? 157 ASP C OD2 1 
ATOM   8880  N  N   . ASP C 2 181 ? 86.428  137.825 108.375 1.00 115.16 ? 158 ASP C N   1 
ATOM   8881  C  CA  . ASP C 2 181 ? 86.298  137.624 106.941 1.00 115.38 ? 158 ASP C CA  1 
ATOM   8882  C  C   . ASP C 2 181 ? 85.208  138.547 106.411 1.00 115.83 ? 158 ASP C C   1 
ATOM   8883  O  O   . ASP C 2 181 ? 84.039  138.408 106.785 1.00 116.05 ? 158 ASP C O   1 
ATOM   8884  C  CB  . ASP C 2 181 ? 85.970  136.165 106.641 1.00 113.85 ? 158 ASP C CB  1 
ATOM   8885  C  CG  . ASP C 2 181 ? 86.332  135.769 105.231 1.00 115.21 ? 158 ASP C CG  1 
ATOM   8886  O  OD1 . ASP C 2 181 ? 86.072  136.568 104.311 1.00 117.07 ? 158 ASP C OD1 1 
ATOM   8887  O  OD2 . ASP C 2 181 ? 86.899  134.673 105.044 1.00 113.53 ? 158 ASP C OD2 1 
ATOM   8888  N  N   . ILE C 2 182 ? 85.582  139.489 105.548 1.00 117.93 ? 159 ILE C N   1 
ATOM   8889  C  CA  . ILE C 2 182 ? 84.650  140.459 104.988 1.00 117.90 ? 159 ILE C CA  1 
ATOM   8890  C  C   . ILE C 2 182 ? 84.389  140.088 103.537 1.00 119.68 ? 159 ILE C C   1 
ATOM   8891  O  O   . ILE C 2 182 ? 85.331  139.912 102.754 1.00 120.05 ? 159 ILE C O   1 
ATOM   8892  C  CB  . ILE C 2 182 ? 85.186  141.896 105.104 1.00 118.77 ? 159 ILE C CB  1 
ATOM   8893  C  CG1 . ILE C 2 182 ? 85.318  142.300 106.573 1.00 118.61 ? 159 ILE C CG1 1 
ATOM   8894  C  CG2 . ILE C 2 182 ? 84.271  142.864 104.374 1.00 118.70 ? 159 ILE C CG2 1 
ATOM   8895  C  CD1 . ILE C 2 182 ? 86.705  142.758 106.961 1.00 118.33 ? 159 ILE C CD1 1 
ATOM   8896  N  N   . ALA C 2 183 ? 83.114  139.968 103.181 1.00 129.42 ? 160 ALA C N   1 
ATOM   8897  C  CA  . ALA C 2 183 ? 82.700  139.604 101.834 1.00 128.76 ? 160 ALA C CA  1 
ATOM   8898  C  C   . ALA C 2 183 ? 81.754  140.663 101.291 1.00 128.65 ? 160 ALA C C   1 
ATOM   8899  O  O   . ALA C 2 183 ? 80.793  141.050 101.964 1.00 126.40 ? 160 ALA C O   1 
ATOM   8900  C  CB  . ALA C 2 183 ? 82.021  138.233 101.815 1.00 126.94 ? 160 ALA C CB  1 
ATOM   8901  N  N   . ILE C 2 184 ? 82.032  141.129 100.078 1.00 138.39 ? 161 ILE C N   1 
ATOM   8902  C  CA  . ILE C 2 184 ? 81.152  142.036 99.354  1.00 138.89 ? 161 ILE C CA  1 
ATOM   8903  C  C   . ILE C 2 184 ? 80.788  141.356 98.043  1.00 139.68 ? 161 ILE C C   1 
ATOM   8904  O  O   . ILE C 2 184 ? 81.672  141.022 97.244  1.00 138.97 ? 161 ILE C O   1 
ATOM   8905  C  CB  . ILE C 2 184 ? 81.805  143.407 99.119  1.00 138.74 ? 161 ILE C CB  1 
ATOM   8906  C  CG1 . ILE C 2 184 ? 81.006  144.217 98.099  1.00 138.84 ? 161 ILE C CG1 1 
ATOM   8907  C  CG2 . ILE C 2 184 ? 83.255  143.250 98.684  1.00 138.98 ? 161 ILE C CG2 1 
ATOM   8908  C  CD1 . ILE C 2 184 ? 81.424  145.664 98.020  1.00 137.75 ? 161 ILE C CD1 1 
ATOM   8909  N  N   . GLU C 2 185 ? 79.495  141.134 97.828  1.00 152.51 ? 162 GLU C N   1 
ATOM   8910  C  CA  . GLU C 2 185 ? 79.031  140.318 96.717  1.00 153.01 ? 162 GLU C CA  1 
ATOM   8911  C  C   . GLU C 2 185 ? 77.995  141.074 95.902  1.00 153.73 ? 162 GLU C C   1 
ATOM   8912  O  O   . GLU C 2 185 ? 77.100  141.717 96.459  1.00 153.26 ? 162 GLU C O   1 
ATOM   8913  C  CB  . GLU C 2 185 ? 78.439  138.995 97.220  1.00 152.38 ? 162 GLU C CB  1 
ATOM   8914  C  CG  . GLU C 2 185 ? 78.092  138.008 96.120  1.00 153.17 ? 162 GLU C CG  1 
ATOM   8915  C  CD  . GLU C 2 185 ? 77.498  136.721 96.657  1.00 153.72 ? 162 GLU C CD  1 
ATOM   8916  O  OE1 . GLU C 2 185 ? 76.984  136.732 97.796  1.00 153.68 ? 162 GLU C OE1 1 
ATOM   8917  O  OE2 . GLU C 2 185 ? 77.544  135.699 95.940  1.00 153.77 ? 162 GLU C OE2 1 
ATOM   8918  N  N   . GLU C 2 186 ? 78.122  140.988 94.581  1.00 158.77 ? 163 GLU C N   1 
ATOM   8919  C  CA  . GLU C 2 186 ? 77.128  141.531 93.662  1.00 158.70 ? 163 GLU C CA  1 
ATOM   8920  C  C   . GLU C 2 186 ? 76.067  140.461 93.437  1.00 158.23 ? 163 GLU C C   1 
ATOM   8921  O  O   . GLU C 2 186 ? 76.316  139.462 92.755  1.00 157.01 ? 163 GLU C O   1 
ATOM   8922  C  CB  . GLU C 2 186 ? 77.778  141.959 92.349  1.00 158.50 ? 163 GLU C CB  1 
ATOM   8923  C  CG  . GLU C 2 186 ? 76.807  142.105 91.185  1.00 159.03 ? 163 GLU C CG  1 
ATOM   8924  C  CD  . GLU C 2 186 ? 75.825  143.243 91.380  1.00 160.20 ? 163 GLU C CD  1 
ATOM   8925  O  OE1 . GLU C 2 186 ? 76.274  144.387 91.599  1.00 160.29 ? 163 GLU C OE1 1 
ATOM   8926  O  OE2 . GLU C 2 186 ? 74.602  142.993 91.315  1.00 159.99 ? 163 GLU C OE2 1 
ATOM   8927  N  N   . SER C 2 187 ? 74.887  140.661 94.025  1.00 163.17 ? 164 SER C N   1 
ATOM   8928  C  CA  . SER C 2 187 ? 73.807  139.692 93.935  1.00 163.72 ? 164 SER C CA  1 
ATOM   8929  C  C   . SER C 2 187 ? 72.585  140.190 93.182  1.00 164.23 ? 164 SER C C   1 
ATOM   8930  O  O   . SER C 2 187 ? 71.748  139.367 92.797  1.00 163.16 ? 164 SER C O   1 
ATOM   8931  C  CB  . SER C 2 187 ? 73.366  139.246 95.338  1.00 162.30 ? 164 SER C CB  1 
ATOM   8932  O  OG  . SER C 2 187 ? 72.193  138.453 95.273  1.00 161.86 ? 164 SER C OG  1 
ATOM   8933  N  N   . ASN C 2 188 ? 72.455  141.494 92.961  1.00 163.30 ? 165 ASN C N   1 
ATOM   8934  C  CA  . ASN C 2 188 ? 71.272  142.051 92.304  1.00 162.66 ? 165 ASN C CA  1 
ATOM   8935  C  C   . ASN C 2 188 ? 71.460  142.153 90.793  1.00 162.75 ? 165 ASN C C   1 
ATOM   8936  O  O   . ASN C 2 188 ? 71.228  143.200 90.190  1.00 162.06 ? 165 ASN C O   1 
ATOM   8937  C  CB  . ASN C 2 188 ? 70.941  143.409 92.909  1.00 162.35 ? 165 ASN C CB  1 
ATOM   8938  C  CG  . ASN C 2 188 ? 70.781  143.352 94.417  1.00 162.04 ? 165 ASN C CG  1 
ATOM   8939  O  OD1 . ASN C 2 188 ? 69.759  142.894 94.928  1.00 161.53 ? 165 ASN C OD1 1 
ATOM   8940  N  ND2 . ASN C 2 188 ? 71.794  143.819 95.137  1.00 161.38 ? 165 ASN C ND2 1 
ATOM   8941  N  N   . ALA C 2 189 ? 71.870  141.048 90.174  1.00 168.14 ? 166 ALA C N   1 
ATOM   8942  C  CA  . ALA C 2 189 ? 72.051  140.971 88.729  1.00 167.69 ? 166 ALA C CA  1 
ATOM   8943  C  C   . ALA C 2 189 ? 72.310  139.518 88.358  1.00 168.20 ? 166 ALA C C   1 
ATOM   8944  O  O   . ALA C 2 189 ? 72.607  138.680 89.213  1.00 167.32 ? 166 ALA C O   1 
ATOM   8945  C  CB  . ALA C 2 189 ? 73.198  141.862 88.244  1.00 165.84 ? 166 ALA C CB  1 
ATOM   8946  N  N   . ILE C 2 190 ? 72.191  139.232 87.064  1.00 171.28 ? 167 ILE C N   1 
ATOM   8947  C  CA  . ILE C 2 190 ? 72.558  137.942 86.491  1.00 171.15 ? 167 ILE C CA  1 
ATOM   8948  C  C   . ILE C 2 190 ? 73.799  138.166 85.643  1.00 170.92 ? 167 ILE C C   1 
ATOM   8949  O  O   . ILE C 2 190 ? 73.775  138.959 84.694  1.00 170.10 ? 167 ILE C O   1 
ATOM   8950  C  CB  . ILE C 2 190 ? 71.416  137.340 85.659  1.00 169.90 ? 167 ILE C CB  1 
ATOM   8951  N  N   . ILE C 2 191 ? 74.884  137.472 85.981  1.00 169.61 ? 168 ILE C N   1 
ATOM   8952  C  CA  . ILE C 2 191 ? 76.183  137.778 85.396  1.00 169.37 ? 168 ILE C CA  1 
ATOM   8953  C  C   . ILE C 2 191 ? 76.727  136.562 84.656  1.00 169.90 ? 168 ILE C C   1 
ATOM   8954  O  O   . ILE C 2 191 ? 77.451  136.698 83.663  1.00 168.87 ? 168 ILE C O   1 
ATOM   8955  C  CB  . ILE C 2 191 ? 77.152  138.270 86.490  1.00 168.87 ? 168 ILE C CB  1 
ATOM   8956  C  CG1 . ILE C 2 191 ? 78.606  138.216 86.027  1.00 168.80 ? 168 ILE C CG1 1 
ATOM   8957  C  CG2 . ILE C 2 191 ? 76.974  137.456 87.761  1.00 167.37 ? 168 ILE C CG2 1 
ATOM   8958  C  CD1 . ILE C 2 191 ? 79.556  138.874 86.997  1.00 168.26 ? 168 ILE C CD1 1 
ATOM   8959  N  N   . ASN C 2 192 ? 76.354  135.367 85.103  1.00 172.61 ? 169 ASN C N   1 
ATOM   8960  C  CA  . ASN C 2 192 ? 76.815  134.136 84.459  1.00 172.02 ? 169 ASN C CA  1 
ATOM   8961  C  C   . ASN C 2 192 ? 75.873  133.702 83.339  1.00 171.59 ? 169 ASN C C   1 
ATOM   8962  O  O   . ASN C 2 192 ? 75.401  132.566 83.295  1.00 170.96 ? 169 ASN C O   1 
ATOM   8963  C  CB  . ASN C 2 192 ? 76.979  133.033 85.499  1.00 171.72 ? 169 ASN C CB  1 
ATOM   8964  C  CG  . ASN C 2 192 ? 75.711  132.782 86.291  1.00 171.65 ? 169 ASN C CG  1 
ATOM   8965  O  OD1 . ASN C 2 192 ? 74.797  133.605 86.302  1.00 171.00 ? 169 ASN C OD1 1 
ATOM   8966  N  ND2 . ASN C 2 192 ? 75.651  131.636 86.958  1.00 170.76 ? 169 ASN C ND2 1 
ATOM   8967  N  N   . ASP C 2 193 ? 75.600  134.617 82.411  1.00 169.46 ? 170 ASP C N   1 
ATOM   8968  C  CA  . ASP C 2 193 ? 74.725  134.349 81.279  1.00 168.64 ? 170 ASP C CA  1 
ATOM   8969  C  C   . ASP C 2 193 ? 75.494  134.060 79.997  1.00 168.68 ? 170 ASP C C   1 
ATOM   8970  O  O   . ASP C 2 193 ? 74.894  134.033 78.919  1.00 168.76 ? 170 ASP C O   1 
ATOM   8971  C  CB  . ASP C 2 193 ? 73.765  135.523 81.063  1.00 167.98 ? 170 ASP C CB  1 
ATOM   8972  C  CG  . ASP C 2 193 ? 74.485  136.847 80.874  1.00 168.44 ? 170 ASP C CG  1 
ATOM   8973  O  OD1 . ASP C 2 193 ? 75.731  136.852 80.787  1.00 168.88 ? 170 ASP C OD1 1 
ATOM   8974  O  OD2 . ASP C 2 193 ? 73.799  137.888 80.815  1.00 168.22 ? 170 ASP C OD2 1 
ATOM   8975  N  N   . GLY C 2 194 ? 76.807  133.850 80.089  1.00 167.29 ? 171 GLY C N   1 
ATOM   8976  C  CA  . GLY C 2 194 ? 77.627  133.570 78.932  1.00 166.55 ? 171 GLY C CA  1 
ATOM   8977  C  C   . GLY C 2 194 ? 78.198  134.787 78.239  1.00 166.59 ? 171 GLY C C   1 
ATOM   8978  O  O   . GLY C 2 194 ? 79.014  134.630 77.322  1.00 165.84 ? 171 GLY C O   1 
ATOM   8979  N  N   . LYS C 2 195 ? 77.801  135.990 78.642  1.00 168.02 ? 172 LYS C N   1 
ATOM   8980  C  CA  . LYS C 2 195 ? 78.335  137.201 78.045  1.00 167.98 ? 172 LYS C CA  1 
ATOM   8981  C  C   . LYS C 2 195 ? 79.690  137.549 78.658  1.00 168.95 ? 172 LYS C C   1 
ATOM   8982  O  O   . LYS C 2 195 ? 80.120  136.977 79.664  1.00 168.36 ? 172 LYS C O   1 
ATOM   8983  C  CB  . LYS C 2 195 ? 77.357  138.362 78.221  1.00 167.29 ? 172 LYS C CB  1 
ATOM   8984  C  CG  . LYS C 2 195 ? 76.020  138.155 77.531  1.00 167.27 ? 172 LYS C CG  1 
ATOM   8985  C  CD  . LYS C 2 195 ? 76.172  138.167 76.017  1.00 167.15 ? 172 LYS C CD  1 
ATOM   8986  C  CE  . LYS C 2 195 ? 74.833  137.974 75.324  1.00 167.16 ? 172 LYS C CE  1 
ATOM   8987  N  NZ  . LYS C 2 195 ? 74.236  136.646 75.632  1.00 167.58 ? 172 LYS C NZ  1 
ATOM   8988  N  N   . TYR C 2 196 ? 80.369  138.505 78.031  1.00 167.20 ? 173 TYR C N   1 
ATOM   8989  C  CA  . TYR C 2 196 ? 81.667  138.977 78.499  1.00 166.10 ? 173 TYR C CA  1 
ATOM   8990  C  C   . TYR C 2 196 ? 81.438  140.087 79.518  1.00 165.78 ? 173 TYR C C   1 
ATOM   8991  O  O   . TYR C 2 196 ? 81.067  141.207 79.154  1.00 164.99 ? 173 TYR C O   1 
ATOM   8992  C  CB  . TYR C 2 196 ? 82.512  139.467 77.325  1.00 165.52 ? 173 TYR C CB  1 
ATOM   8993  C  CG  . TYR C 2 196 ? 83.900  139.937 77.701  1.00 165.28 ? 173 TYR C CG  1 
ATOM   8994  C  CD1 . TYR C 2 196 ? 84.127  141.247 78.104  1.00 165.07 ? 173 TYR C CD1 1 
ATOM   8995  C  CD2 . TYR C 2 196 ? 84.985  139.073 77.640  1.00 165.38 ? 173 TYR C CD2 1 
ATOM   8996  C  CE1 . TYR C 2 196 ? 85.392  141.680 78.445  1.00 165.54 ? 173 TYR C CE1 1 
ATOM   8997  C  CE2 . TYR C 2 196 ? 86.255  139.497 77.977  1.00 165.94 ? 173 TYR C CE2 1 
ATOM   8998  C  CZ  . TYR C 2 196 ? 86.453  140.802 78.379  1.00 166.79 ? 173 TYR C CZ  1 
ATOM   8999  O  OH  . TYR C 2 196 ? 87.716  141.232 78.718  1.00 166.32 ? 173 TYR C OH  1 
ATOM   9000  N  N   . HIS C 2 197 ? 81.660  139.779 80.791  1.00 163.84 ? 174 HIS C N   1 
ATOM   9001  C  CA  . HIS C 2 197 ? 81.521  140.752 81.862  1.00 163.52 ? 174 HIS C CA  1 
ATOM   9002  C  C   . HIS C 2 197 ? 82.897  141.212 82.320  1.00 163.57 ? 174 HIS C C   1 
ATOM   9003  O  O   . HIS C 2 197 ? 83.912  140.579 82.029  1.00 163.34 ? 174 HIS C O   1 
ATOM   9004  C  CB  . HIS C 2 197 ? 80.745  140.164 83.045  1.00 163.37 ? 174 HIS C CB  1 
ATOM   9005  C  CG  . HIS C 2 197 ? 79.365  139.705 82.695  1.00 164.03 ? 174 HIS C CG  1 
ATOM   9006  N  ND1 . HIS C 2 197 ? 78.231  140.373 83.103  1.00 164.08 ? 174 HIS C ND1 1 
ATOM   9007  C  CD2 . HIS C 2 197 ? 78.936  138.643 81.974  1.00 163.04 ? 174 HIS C CD2 1 
ATOM   9008  C  CE1 . HIS C 2 197 ? 77.163  139.741 82.651  1.00 162.94 ? 174 HIS C CE1 1 
ATOM   9009  N  NE2 . HIS C 2 197 ? 77.563  138.687 81.963  1.00 162.53 ? 174 HIS C NE2 1 
ATOM   9010  N  N   . VAL C 2 198 ? 82.925  142.336 83.031  1.00 155.29 ? 175 VAL C N   1 
ATOM   9011  C  CA  . VAL C 2 198 ? 84.152  142.869 83.610  1.00 154.26 ? 175 VAL C CA  1 
ATOM   9012  C  C   . VAL C 2 198 ? 83.867  143.258 85.053  1.00 153.59 ? 175 VAL C C   1 
ATOM   9013  O  O   . VAL C 2 198 ? 82.846  143.894 85.340  1.00 152.61 ? 175 VAL C O   1 
ATOM   9014  C  CB  . VAL C 2 198 ? 84.698  144.068 82.807  1.00 153.40 ? 175 VAL C CB  1 
ATOM   9015  C  CG1 . VAL C 2 198 ? 83.644  145.157 82.660  1.00 153.11 ? 175 VAL C CG1 1 
ATOM   9016  C  CG2 . VAL C 2 198 ? 85.958  144.619 83.456  1.00 152.50 ? 175 VAL C CG2 1 
ATOM   9017  N  N   . VAL C 2 199 ? 84.754  142.860 85.961  1.00 145.60 ? 176 VAL C N   1 
ATOM   9018  C  CA  . VAL C 2 199 ? 84.594  143.115 87.385  1.00 145.36 ? 176 VAL C CA  1 
ATOM   9019  C  C   . VAL C 2 199 ? 85.858  143.782 87.913  1.00 144.11 ? 176 VAL C C   1 
ATOM   9020  O  O   . VAL C 2 199 ? 86.978  143.329 87.637  1.00 142.44 ? 176 VAL C O   1 
ATOM   9021  C  CB  . VAL C 2 199 ? 84.270  141.824 88.164  1.00 144.21 ? 176 VAL C CB  1 
ATOM   9022  C  CG1 . VAL C 2 199 ? 85.332  140.775 87.944  1.00 143.25 ? 176 VAL C CG1 1 
ATOM   9023  C  CG2 . VAL C 2 199 ? 84.133  142.120 89.637  1.00 143.00 ? 176 VAL C CG2 1 
ATOM   9024  N  N   . ARG C 2 200 ? 85.669  144.878 88.647  1.00 135.65 ? 177 ARG C N   1 
ATOM   9025  C  CA  . ARG C 2 200 ? 86.744  145.636 89.268  1.00 135.03 ? 177 ARG C CA  1 
ATOM   9026  C  C   . ARG C 2 200 ? 86.460  145.755 90.757  1.00 135.49 ? 177 ARG C C   1 
ATOM   9027  O  O   . ARG C 2 200 ? 85.365  146.166 91.154  1.00 134.62 ? 177 ARG C O   1 
ATOM   9028  C  CB  . ARG C 2 200 ? 86.871  147.029 88.646  1.00 134.30 ? 177 ARG C CB  1 
ATOM   9029  C  CG  . ARG C 2 200 ? 87.859  147.117 87.502  1.00 134.09 ? 177 ARG C CG  1 
ATOM   9030  C  CD  . ARG C 2 200 ? 87.175  146.878 86.168  1.00 135.45 ? 177 ARG C CD  1 
ATOM   9031  N  NE  . ARG C 2 200 ? 85.986  147.708 86.014  1.00 135.35 ? 177 ARG C NE  1 
ATOM   9032  C  CZ  . ARG C 2 200 ? 86.003  148.972 85.617  1.00 134.67 ? 177 ARG C CZ  1 
ATOM   9033  N  NH1 . ARG C 2 200 ? 87.134  149.587 85.315  1.00 134.67 ? 177 ARG C NH1 1 
ATOM   9034  N  NH2 . ARG C 2 200 ? 84.855  149.637 85.521  1.00 134.00 ? 177 ARG C NH2 1 
ATOM   9035  N  N   . PHE C 2 201 ? 87.450  145.415 91.576  1.00 122.32 ? 178 PHE C N   1 
ATOM   9036  C  CA  . PHE C 2 201 ? 87.326  145.464 93.026  1.00 119.20 ? 178 PHE C CA  1 
ATOM   9037  C  C   . PHE C 2 201 ? 88.447  146.327 93.577  1.00 119.46 ? 178 PHE C C   1 
ATOM   9038  O  O   . PHE C 2 201 ? 89.623  146.068 93.303  1.00 118.37 ? 178 PHE C O   1 
ATOM   9039  C  CB  . PHE C 2 201 ? 87.380  144.057 93.625  1.00 119.08 ? 178 PHE C CB  1 
ATOM   9040  C  CG  . PHE C 2 201 ? 87.610  144.038 95.104  1.00 119.52 ? 178 PHE C CG  1 
ATOM   9041  C  CD1 . PHE C 2 201 ? 86.624  144.463 95.973  1.00 119.83 ? 178 PHE C CD1 1 
ATOM   9042  C  CD2 . PHE C 2 201 ? 88.808  143.589 95.626  1.00 118.35 ? 178 PHE C CD2 1 
ATOM   9043  C  CE1 . PHE C 2 201 ? 86.829  144.446 97.333  1.00 119.40 ? 178 PHE C CE1 1 
ATOM   9044  C  CE2 . PHE C 2 201 ? 89.017  143.569 96.986  1.00 117.82 ? 178 PHE C CE2 1 
ATOM   9045  C  CZ  . PHE C 2 201 ? 88.026  143.998 97.841  1.00 118.67 ? 178 PHE C CZ  1 
ATOM   9046  N  N   . THR C 2 202 ? 88.086  147.354 94.344  1.00 119.96 ? 179 THR C N   1 
ATOM   9047  C  CA  . THR C 2 202 ? 89.054  148.240 94.979  1.00 119.15 ? 179 THR C CA  1 
ATOM   9048  C  C   . THR C 2 202 ? 88.898  148.132 96.487  1.00 119.06 ? 179 THR C C   1 
ATOM   9049  O  O   . THR C 2 202 ? 87.818  148.397 97.025  1.00 120.28 ? 179 THR C O   1 
ATOM   9050  C  CB  . THR C 2 202 ? 88.871  149.691 94.530  1.00 119.19 ? 179 THR C CB  1 
ATOM   9051  O  OG1 . THR C 2 202 ? 87.803  150.293 95.272  1.00 118.75 ? 179 THR C OG1 1 
ATOM   9052  C  CG2 . THR C 2 202 ? 88.555  149.756 93.042  1.00 119.71 ? 179 THR C CG2 1 
ATOM   9053  N  N   . ARG C 2 203 ? 89.975  147.758 97.166  1.00 106.04 ? 180 ARG C N   1 
ATOM   9054  C  CA  . ARG C 2 203 ? 89.993  147.617 98.614  1.00 103.85 ? 180 ARG C CA  1 
ATOM   9055  C  C   . ARG C 2 203 ? 90.899  148.690 99.192  1.00 106.22 ? 180 ARG C C   1 
ATOM   9056  O  O   . ARG C 2 203 ? 92.050  148.823 98.767  1.00 108.56 ? 180 ARG C O   1 
ATOM   9057  C  CB  . ARG C 2 203 ? 90.489  146.231 99.012  1.00 104.02 ? 180 ARG C CB  1 
ATOM   9058  C  CG  . ARG C 2 203 ? 90.458  145.957 100.492 1.00 105.21 ? 180 ARG C CG  1 
ATOM   9059  C  CD  . ARG C 2 203 ? 90.999  144.560 100.770 1.00 107.51 ? 180 ARG C CD  1 
ATOM   9060  N  NE  . ARG C 2 203 ? 92.440  144.528 101.006 1.00 103.46 ? 180 ARG C NE  1 
ATOM   9061  C  CZ  . ARG C 2 203 ? 93.103  145.295 101.863 1.00 102.74 ? 180 ARG C CZ  1 
ATOM   9062  N  NH1 . ARG C 2 203 ? 92.479  146.116 102.692 1.00 104.39 ? 180 ARG C NH1 1 
ATOM   9063  N  NH2 . ARG C 2 203 ? 94.428  145.216 101.909 1.00 102.36 ? 180 ARG C NH2 1 
ATOM   9064  N  N   . SER C 2 204 ? 90.383  149.453 100.153 1.00 110.21 ? 181 SER C N   1 
ATOM   9065  C  CA  . SER C 2 204 ? 91.168  150.455 100.867 1.00 110.07 ? 181 SER C CA  1 
ATOM   9066  C  C   . SER C 2 204 ? 90.990  150.198 102.356 1.00 109.57 ? 181 SER C C   1 
ATOM   9067  O  O   . SER C 2 204 ? 89.940  150.519 102.923 1.00 112.37 ? 181 SER C O   1 
ATOM   9068  C  CB  . SER C 2 204 ? 90.736  151.872 100.492 1.00 108.09 ? 181 SER C CB  1 
ATOM   9069  O  OG  . SER C 2 204 ? 89.344  151.930 100.238 1.00 108.48 ? 181 SER C OG  1 
ATOM   9070  N  N   . GLY C 2 205 ? 92.005  149.611 102.979 1.00 103.80 ? 182 GLY C N   1 
ATOM   9071  C  CA  . GLY C 2 205 ? 91.881  149.230 104.375 1.00 103.25 ? 182 GLY C CA  1 
ATOM   9072  C  C   . GLY C 2 205 ? 90.732  148.262 104.560 1.00 103.75 ? 182 GLY C C   1 
ATOM   9073  O  O   . GLY C 2 205 ? 90.625  147.246 103.865 1.00 104.21 ? 182 GLY C O   1 
ATOM   9074  N  N   . GLY C 2 206 ? 89.849  148.580 105.502 1.00 112.93 ? 183 GLY C N   1 
ATOM   9075  C  CA  . GLY C 2 206 ? 88.658  147.787 105.708 1.00 113.39 ? 183 GLY C CA  1 
ATOM   9076  C  C   . GLY C 2 206 ? 87.509  148.100 104.782 1.00 114.98 ? 183 GLY C C   1 
ATOM   9077  O  O   . GLY C 2 206 ? 86.548  147.330 104.724 1.00 114.26 ? 183 GLY C O   1 
ATOM   9078  N  N   . ASN C 2 207 ? 87.578  149.209 104.050 1.00 118.95 ? 184 ASN C N   1 
ATOM   9079  C  CA  . ASN C 2 207 ? 86.513  149.565 103.125 1.00 117.27 ? 184 ASN C CA  1 
ATOM   9080  C  C   . ASN C 2 207 ? 86.694  148.835 101.801 1.00 119.02 ? 184 ASN C C   1 
ATOM   9081  O  O   . ASN C 2 207 ? 87.814  148.685 101.305 1.00 120.83 ? 184 ASN C O   1 
ATOM   9082  C  CB  . ASN C 2 207 ? 86.486  151.074 102.888 1.00 116.62 ? 184 ASN C CB  1 
ATOM   9083  C  CG  . ASN C 2 207 ? 86.430  151.866 104.177 1.00 118.75 ? 184 ASN C CG  1 
ATOM   9084  O  OD1 . ASN C 2 207 ? 85.995  151.362 105.212 1.00 116.80 ? 184 ASN C OD1 1 
ATOM   9085  N  ND2 . ASN C 2 207 ? 86.865  153.119 104.118 1.00 120.97 ? 184 ASN C ND2 1 
ATOM   9086  N  N   . ALA C 2 208 ? 85.584  148.379 101.226 1.00 126.21 ? 185 ALA C N   1 
ATOM   9087  C  CA  . ALA C 2 208 ? 85.629  147.640 99.975  1.00 125.67 ? 185 ALA C CA  1 
ATOM   9088  C  C   . ALA C 2 208 ? 84.658  148.250 98.976  1.00 127.67 ? 185 ALA C C   1 
ATOM   9089  O  O   . ALA C 2 208 ? 83.617  148.793 99.351  1.00 128.53 ? 185 ALA C O   1 
ATOM   9090  C  CB  . ALA C 2 208 ? 85.300  146.159 100.187 1.00 125.08 ? 185 ALA C CB  1 
ATOM   9091  N  N   . THR C 2 209 ? 85.007  148.152 97.695  1.00 129.09 ? 186 THR C N   1 
ATOM   9092  C  CA  . THR C 2 209 ? 84.153  148.644 96.624  1.00 128.14 ? 186 THR C CA  1 
ATOM   9093  C  C   . THR C 2 209 ? 84.197  147.654 95.472  1.00 128.87 ? 186 THR C C   1 
ATOM   9094  O  O   . THR C 2 209 ? 85.277  147.214 95.069  1.00 128.09 ? 186 THR C O   1 
ATOM   9095  C  CB  . THR C 2 209 ? 84.596  150.033 96.154  1.00 126.63 ? 186 THR C CB  1 
ATOM   9096  O  OG1 . THR C 2 209 ? 84.386  150.982 97.206  1.00 126.57 ? 186 THR C OG1 1 
ATOM   9097  C  CG2 . THR C 2 209 ? 83.808  150.464 94.931  1.00 127.86 ? 186 THR C CG2 1 
ATOM   9098  N  N   . LEU C 2 210 ? 83.023  147.308 94.951  1.00 136.28 ? 187 LEU C N   1 
ATOM   9099  C  CA  . LEU C 2 210 ? 82.885  146.337 93.877  1.00 135.17 ? 187 LEU C CA  1 
ATOM   9100  C  C   . LEU C 2 210 ? 82.100  146.966 92.736  1.00 136.25 ? 187 LEU C C   1 
ATOM   9101  O  O   . LEU C 2 210 ? 81.119  147.676 92.968  1.00 135.32 ? 187 LEU C O   1 
ATOM   9102  C  CB  . LEU C 2 210 ? 82.172  145.074 94.372  1.00 133.28 ? 187 LEU C CB  1 
ATOM   9103  C  CG  . LEU C 2 210 ? 82.154  143.849 93.460  1.00 134.53 ? 187 LEU C CG  1 
ATOM   9104  C  CD1 . LEU C 2 210 ? 83.406  143.801 92.615  1.00 134.18 ? 187 LEU C CD1 1 
ATOM   9105  C  CD2 . LEU C 2 210 ? 82.012  142.577 94.273  1.00 136.78 ? 187 LEU C CD2 1 
ATOM   9106  N  N   . GLN C 2 211 ? 82.534  146.713 91.502  1.00 143.06 ? 188 GLN C N   1 
ATOM   9107  C  CA  . GLN C 2 211 ? 81.811  147.176 90.327  1.00 142.94 ? 188 GLN C CA  1 
ATOM   9108  C  C   . GLN C 2 211 ? 81.849  146.093 89.263  1.00 143.54 ? 188 GLN C C   1 
ATOM   9109  O  O   . GLN C 2 211 ? 82.868  145.422 89.084  1.00 142.10 ? 188 GLN C O   1 
ATOM   9110  C  CB  . GLN C 2 211 ? 82.402  148.477 89.770  1.00 141.67 ? 188 GLN C CB  1 
ATOM   9111  C  CG  . GLN C 2 211 ? 81.485  149.204 88.799  1.00 141.82 ? 188 GLN C CG  1 
ATOM   9112  C  CD  . GLN C 2 211 ? 82.193  150.312 88.046  1.00 142.28 ? 188 GLN C CD  1 
ATOM   9113  O  OE1 . GLN C 2 211 ? 83.233  150.090 87.426  1.00 142.36 ? 188 GLN C OE1 1 
ATOM   9114  N  NE2 . GLN C 2 211 ? 81.635  151.515 88.101  1.00 141.67 ? 188 GLN C NE2 1 
ATOM   9115  N  N   . VAL C 2 212 ? 80.729  145.920 88.568  1.00 151.73 ? 189 VAL C N   1 
ATOM   9116  C  CA  . VAL C 2 212 ? 80.604  144.934 87.503  1.00 151.15 ? 189 VAL C CA  1 
ATOM   9117  C  C   . VAL C 2 212 ? 79.982  145.605 86.286  1.00 152.42 ? 189 VAL C C   1 
ATOM   9118  O  O   . VAL C 2 212 ? 78.914  146.221 86.389  1.00 151.51 ? 189 VAL C O   1 
ATOM   9119  C  CB  . VAL C 2 212 ? 79.775  143.716 87.953  1.00 151.35 ? 189 VAL C CB  1 
ATOM   9120  C  CG1 . VAL C 2 212 ? 80.601  142.833 88.867  1.00 150.92 ? 189 VAL C CG1 1 
ATOM   9121  C  CG2 . VAL C 2 212 ? 78.536  144.175 88.695  1.00 151.09 ? 189 VAL C CG2 1 
ATOM   9122  N  N   . ASP C 2 213 ? 80.655  145.488 85.139  1.00 155.16 ? 190 ASP C N   1 
ATOM   9123  C  CA  . ASP C 2 213 ? 80.204  146.084 83.886  1.00 154.52 ? 190 ASP C CA  1 
ATOM   9124  C  C   . ASP C 2 213 ? 79.952  147.577 84.044  1.00 153.51 ? 190 ASP C C   1 
ATOM   9125  O  O   . ASP C 2 213 ? 80.892  148.359 84.218  1.00 152.12 ? 190 ASP C O   1 
ATOM   9126  C  CB  . ASP C 2 213 ? 78.942  145.379 83.381  1.00 154.43 ? 190 ASP C CB  1 
ATOM   9127  C  CG  . ASP C 2 213 ? 79.203  143.944 82.968  1.00 154.55 ? 190 ASP C CG  1 
ATOM   9128  O  OD1 . ASP C 2 213 ? 80.198  143.704 82.254  1.00 154.32 ? 190 ASP C OD1 1 
ATOM   9129  O  OD2 . ASP C 2 213 ? 78.417  143.057 83.361  1.00 154.17 ? 190 ASP C OD2 1 
ATOM   9130  N  N   . SER C 2 214 ? 78.683  147.980 83.984  1.00 161.30 ? 191 SER C N   1 
ATOM   9131  C  CA  . SER C 2 214 ? 78.291  149.368 84.194  1.00 161.95 ? 191 SER C CA  1 
ATOM   9132  C  C   . SER C 2 214 ? 77.262  149.510 85.307  1.00 162.40 ? 191 SER C C   1 
ATOM   9133  O  O   . SER C 2 214 ? 76.760  150.616 85.538  1.00 161.80 ? 191 SER C O   1 
ATOM   9134  C  CB  . SER C 2 214 ? 77.749  149.975 82.895  1.00 162.11 ? 191 SER C CB  1 
ATOM   9135  O  OG  . SER C 2 214 ? 76.719  149.171 82.345  1.00 161.54 ? 191 SER C OG  1 
ATOM   9136  N  N   . TRP C 2 215 ? 76.935  148.421 85.997  1.00 163.12 ? 192 TRP C N   1 
ATOM   9137  C  CA  . TRP C 2 215 ? 75.996  148.484 87.102  1.00 162.78 ? 192 TRP C CA  1 
ATOM   9138  C  C   . TRP C 2 215 ? 76.577  149.322 88.240  1.00 163.64 ? 192 TRP C C   1 
ATOM   9139  O  O   . TRP C 2 215 ? 77.797  149.385 88.413  1.00 163.64 ? 192 TRP C O   1 
ATOM   9140  C  CB  . TRP C 2 215 ? 75.661  147.076 87.587  1.00 161.83 ? 192 TRP C CB  1 
ATOM   9141  C  CG  . TRP C 2 215 ? 74.815  146.312 86.611  1.00 162.65 ? 192 TRP C CG  1 
ATOM   9142  C  CD1 . TRP C 2 215 ? 73.687  146.758 85.986  1.00 162.54 ? 192 TRP C CD1 1 
ATOM   9143  C  CD2 . TRP C 2 215 ? 75.042  144.983 86.124  1.00 163.76 ? 192 TRP C CD2 1 
ATOM   9144  N  NE1 . TRP C 2 215 ? 73.189  145.785 85.154  1.00 162.46 ? 192 TRP C NE1 1 
ATOM   9145  C  CE2 . TRP C 2 215 ? 74.004  144.686 85.220  1.00 163.76 ? 192 TRP C CE2 1 
ATOM   9146  C  CE3 . TRP C 2 215 ? 76.018  144.014 86.370  1.00 163.42 ? 192 TRP C CE3 1 
ATOM   9147  C  CZ2 . TRP C 2 215 ? 73.915  143.462 84.561  1.00 163.40 ? 192 TRP C CZ2 1 
ATOM   9148  C  CZ3 . TRP C 2 215 ? 75.928  142.798 85.716  1.00 162.57 ? 192 TRP C CZ3 1 
ATOM   9149  C  CH2 . TRP C 2 215 ? 74.885  142.534 84.823  1.00 163.16 ? 192 TRP C CH2 1 
ATOM   9150  N  N   . PRO C 2 216 ? 75.723  149.986 89.023  1.00 157.30 ? 193 PRO C N   1 
ATOM   9151  C  CA  . PRO C 2 216 ? 76.227  150.912 90.044  1.00 156.24 ? 193 PRO C CA  1 
ATOM   9152  C  C   . PRO C 2 216 ? 77.107  150.207 91.065  1.00 156.72 ? 193 PRO C C   1 
ATOM   9153  O  O   . PRO C 2 216 ? 76.936  149.021 91.357  1.00 156.11 ? 193 PRO C O   1 
ATOM   9154  C  CB  . PRO C 2 216 ? 74.949  151.462 90.691  1.00 155.38 ? 193 PRO C CB  1 
ATOM   9155  C  CG  . PRO C 2 216 ? 73.877  150.486 90.331  1.00 154.54 ? 193 PRO C CG  1 
ATOM   9156  C  CD  . PRO C 2 216 ? 74.252  149.959 88.984  1.00 155.24 ? 193 PRO C CD  1 
ATOM   9157  N  N   . VAL C 2 217 ? 78.072  150.959 91.597  1.00 149.85 ? 194 VAL C N   1 
ATOM   9158  C  CA  . VAL C 2 217 ? 79.061  150.387 92.499  1.00 149.13 ? 194 VAL C CA  1 
ATOM   9159  C  C   . VAL C 2 217 ? 78.403  149.958 93.805  1.00 148.78 ? 194 VAL C C   1 
ATOM   9160  O  O   . VAL C 2 217 ? 77.398  150.530 94.247  1.00 146.99 ? 194 VAL C O   1 
ATOM   9161  C  CB  . VAL C 2 217 ? 80.200  151.390 92.760  1.00 147.62 ? 194 VAL C CB  1 
ATOM   9162  C  CG1 . VAL C 2 217 ? 81.015  151.608 91.498  1.00 146.80 ? 194 VAL C CG1 1 
ATOM   9163  C  CG2 . VAL C 2 217 ? 79.642  152.706 93.274  1.00 147.20 ? 194 VAL C CG2 1 
ATOM   9164  N  N   . ILE C 2 218 ? 78.979  148.932 94.423  1.00 148.78 ? 195 ILE C N   1 
ATOM   9165  C  CA  . ILE C 2 218 ? 78.583  148.456 95.742  1.00 148.05 ? 195 ILE C CA  1 
ATOM   9166  C  C   . ILE C 2 218 ? 79.699  148.807 96.713  1.00 146.97 ? 195 ILE C C   1 
ATOM   9167  O  O   . ILE C 2 218 ? 80.869  148.504 96.456  1.00 147.61 ? 195 ILE C O   1 
ATOM   9168  C  CB  . ILE C 2 218 ? 78.316  146.942 95.742  1.00 147.33 ? 195 ILE C CB  1 
ATOM   9169  C  CG1 . ILE C 2 218 ? 77.257  146.583 94.701  1.00 147.75 ? 195 ILE C CG1 1 
ATOM   9170  C  CG2 . ILE C 2 218 ? 77.888  146.475 97.124  1.00 145.04 ? 195 ILE C CG2 1 
ATOM   9171  C  CD1 . ILE C 2 218 ? 76.907  145.115 94.679  1.00 146.46 ? 195 ILE C CD1 1 
ATOM   9172  N  N   . GLU C 2 219 ? 79.343  149.448 97.819  1.00 150.49 ? 196 GLU C N   1 
ATOM   9173  C  CA  . GLU C 2 219 ? 80.302  149.832 98.842  1.00 150.48 ? 196 GLU C CA  1 
ATOM   9174  C  C   . GLU C 2 219 ? 80.041  149.034 100.113 1.00 151.48 ? 196 GLU C C   1 
ATOM   9175  O  O   . GLU C 2 219 ? 78.887  148.777 100.470 1.00 152.15 ? 196 GLU C O   1 
ATOM   9176  C  CB  . GLU C 2 219 ? 80.231  151.336 99.127  1.00 149.65 ? 196 GLU C CB  1 
ATOM   9177  C  CG  . GLU C 2 219 ? 78.953  151.806 99.812  1.00 150.45 ? 196 GLU C CG  1 
ATOM   9178  C  CD  . GLU C 2 219 ? 77.761  151.833 98.878  1.00 152.15 ? 196 GLU C CD  1 
ATOM   9179  O  OE1 . GLU C 2 219 ? 77.968  151.793 97.648  1.00 151.95 ? 196 GLU C OE1 1 
ATOM   9180  O  OE2 . GLU C 2 219 ? 76.616  151.891 99.374  1.00 152.27 ? 196 GLU C OE2 1 
ATOM   9181  N  N   . ARG C 2 220 ? 81.117  148.619 100.779 1.00 141.21 ? 197 ARG C N   1 
ATOM   9182  C  CA  . ARG C 2 220 ? 81.024  147.858 102.017 1.00 140.42 ? 197 ARG C CA  1 
ATOM   9183  C  C   . ARG C 2 220 ? 81.908  148.516 103.064 1.00 139.47 ? 197 ARG C C   1 
ATOM   9184  O  O   . ARG C 2 220 ? 83.108  148.718 102.831 1.00 141.13 ? 197 ARG C O   1 
ATOM   9185  C  CB  . ARG C 2 220 ? 81.431  146.396 101.808 1.00 139.90 ? 197 ARG C CB  1 
ATOM   9186  C  CG  . ARG C 2 220 ? 81.435  145.575 103.085 1.00 138.96 ? 197 ARG C CG  1 
ATOM   9187  C  CD  . ARG C 2 220 ? 80.023  145.363 103.600 1.00 138.14 ? 197 ARG C CD  1 
ATOM   9188  N  NE  . ARG C 2 220 ? 80.006  144.817 104.953 1.00 141.02 ? 197 ARG C NE  1 
ATOM   9189  C  CZ  . ARG C 2 220 ? 79.914  143.526 105.241 1.00 142.45 ? 197 ARG C CZ  1 
ATOM   9190  N  NH1 . ARG C 2 220 ? 79.830  142.610 104.291 1.00 140.94 ? 197 ARG C NH1 1 
ATOM   9191  N  NH2 . ARG C 2 220 ? 79.903  143.146 106.515 1.00 141.30 ? 197 ARG C NH2 1 
ATOM   9192  N  N   . TYR C 2 221 ? 81.311  148.843 104.209 1.00 136.18 ? 198 TYR C N   1 
ATOM   9193  C  CA  . TYR C 2 221 ? 81.986  149.514 105.319 1.00 136.75 ? 198 TYR C CA  1 
ATOM   9194  C  C   . TYR C 2 221 ? 81.711  148.716 106.586 1.00 137.35 ? 198 TYR C C   1 
ATOM   9195  O  O   . TYR C 2 221 ? 80.812  149.060 107.366 1.00 137.94 ? 198 TYR C O   1 
ATOM   9196  C  CB  . TYR C 2 221 ? 81.508  150.960 105.473 1.00 135.70 ? 198 TYR C CB  1 
ATOM   9197  C  CG  . TYR C 2 221 ? 81.895  151.886 104.341 1.00 135.30 ? 198 TYR C CG  1 
ATOM   9198  C  CD1 . TYR C 2 221 ? 81.332  151.749 103.079 1.00 134.60 ? 198 TYR C CD1 1 
ATOM   9199  C  CD2 . TYR C 2 221 ? 82.812  152.908 104.539 1.00 136.00 ? 198 TYR C CD2 1 
ATOM   9200  C  CE1 . TYR C 2 221 ? 81.681  152.593 102.048 1.00 136.48 ? 198 TYR C CE1 1 
ATOM   9201  C  CE2 . TYR C 2 221 ? 83.165  153.759 103.512 1.00 137.05 ? 198 TYR C CE2 1 
ATOM   9202  C  CZ  . TYR C 2 221 ? 82.596  153.596 102.268 1.00 137.67 ? 198 TYR C CZ  1 
ATOM   9203  O  OH  . TYR C 2 221 ? 82.942  154.439 101.237 1.00 137.61 ? 198 TYR C OH  1 
ATOM   9204  N  N   . PRO C 2 222 ? 82.457  147.636 106.817 1.00 134.56 ? 199 PRO C N   1 
ATOM   9205  C  CA  . PRO C 2 222 ? 82.207  146.811 108.006 1.00 134.41 ? 199 PRO C CA  1 
ATOM   9206  C  C   . PRO C 2 222 ? 82.428  147.596 109.290 1.00 135.11 ? 199 PRO C C   1 
ATOM   9207  O  O   . PRO C 2 222 ? 83.284  148.480 109.368 1.00 134.32 ? 199 PRO C O   1 
ATOM   9208  C  CB  . PRO C 2 222 ? 83.217  145.665 107.865 1.00 132.00 ? 199 PRO C CB  1 
ATOM   9209  C  CG  . PRO C 2 222 ? 84.260  146.180 106.934 1.00 134.15 ? 199 PRO C CG  1 
ATOM   9210  C  CD  . PRO C 2 222 ? 83.560  147.112 105.997 1.00 133.77 ? 199 PRO C CD  1 
ATOM   9211  N  N   . ALA C 2 223 ? 81.634  147.263 110.303 1.00 136.16 ? 200 ALA C N   1 
ATOM   9212  C  CA  . ALA C 2 223 ? 81.638  148.001 111.555 1.00 135.73 ? 200 ALA C CA  1 
ATOM   9213  C  C   . ALA C 2 223 ? 82.816  147.589 112.433 1.00 135.27 ? 200 ALA C C   1 
ATOM   9214  O  O   . ALA C 2 223 ? 83.399  146.514 112.278 1.00 133.77 ? 200 ALA C O   1 
ATOM   9215  C  CB  . ALA C 2 223 ? 80.325  147.786 112.309 1.00 134.47 ? 200 ALA C CB  1 
ATOM   9216  N  N   . GLY C 2 224 ? 83.154  148.471 113.372 1.00 136.27 ? 201 GLY C N   1 
ATOM   9217  C  CA  . GLY C 2 224 ? 84.235  148.220 114.302 1.00 134.82 ? 201 GLY C CA  1 
ATOM   9218  C  C   . GLY C 2 224 ? 85.589  148.616 113.747 1.00 135.49 ? 201 GLY C C   1 
ATOM   9219  O  O   . GLY C 2 224 ? 85.736  149.059 112.607 1.00 135.33 ? 201 GLY C O   1 
ATOM   9220  N  N   . ARG C 2 225 ? 86.635  148.546 114.598 1.00 126.45 ? 232 ARG C N   1 
ATOM   9221  C  CA  . ARG C 2 225 ? 88.028  148.860 114.143 1.00 125.53 ? 232 ARG C CA  1 
ATOM   9222  C  C   . ARG C 2 225 ? 88.518  147.601 113.441 1.00 124.99 ? 232 ARG C C   1 
ATOM   9223  O  O   . ARG C 2 225 ? 88.408  146.535 114.061 1.00 123.47 ? 232 ARG C O   1 
ATOM   9224  C  CB  . ARG C 2 225 ? 88.992  149.265 115.270 1.00 124.57 ? 232 ARG C CB  1 
ATOM   9225  C  CG  . ARG C 2 225 ? 90.173  150.145 114.853 1.00 125.44 ? 232 ARG C CG  1 
ATOM   9226  C  CD  . ARG C 2 225 ? 91.501  150.217 115.646 1.00 126.46 ? 232 ARG C CD  1 
ATOM   9227  N  NE  . ARG C 2 225 ? 92.684  149.564 115.043 1.00 126.96 ? 232 ARG C NE  1 
ATOM   9228  C  CZ  . ARG C 2 225 ? 93.806  149.140 115.653 1.00 124.77 ? 232 ARG C CZ  1 
ATOM   9229  N  NH1 . ARG C 2 225 ? 94.760  148.553 114.943 1.00 124.73 ? 232 ARG C NH1 1 
ATOM   9230  N  NH2 . ARG C 2 225 ? 93.986  149.321 116.953 1.00 123.43 ? 232 ARG C NH2 1 
ATOM   9231  N  N   . GLN C 2 226 ? 89.028  147.762 112.216 1.00 117.24 ? 233 GLN C N   1 
ATOM   9232  C  CA  . GLN C 2 226 ? 89.455  146.705 111.312 1.00 115.80 ? 233 GLN C CA  1 
ATOM   9233  C  C   . GLN C 2 226 ? 90.916  146.891 110.934 1.00 115.40 ? 233 GLN C C   1 
ATOM   9234  O  O   . GLN C 2 226 ? 91.362  148.011 110.668 1.00 115.67 ? 233 GLN C O   1 
ATOM   9235  C  CB  . GLN C 2 226 ? 88.592  146.686 110.047 1.00 114.98 ? 233 GLN C CB  1 
ATOM   9236  C  CG  . GLN C 2 226 ? 87.097  146.749 110.311 1.00 117.05 ? 233 GLN C CG  1 
ATOM   9237  C  CD  . GLN C 2 226 ? 86.545  145.445 110.847 1.00 119.27 ? 233 GLN C CD  1 
ATOM   9238  O  OE1 . GLN C 2 226 ? 86.582  145.191 112.050 1.00 117.77 ? 233 GLN C OE1 1 
ATOM   9239  N  NE2 . GLN C 2 226 ? 86.030  144.610 109.954 1.00 118.58 ? 233 GLN C NE2 1 
ATOM   9240  N  N   . LEU C 2 227 ? 91.656  145.785 110.917 1.00 95.67  ? 234 LEU C N   1 
ATOM   9241  C  CA  . LEU C 2 227 ? 93.020  145.808 110.413 1.00 93.91  ? 234 LEU C CA  1 
ATOM   9242  C  C   . LEU C 2 227 ? 93.014  146.158 108.931 1.00 96.19  ? 234 LEU C C   1 
ATOM   9243  O  O   . LEU C 2 227 ? 92.101  145.793 108.187 1.00 100.12 ? 234 LEU C O   1 
ATOM   9244  C  CB  . LEU C 2 227 ? 93.697  144.458 110.636 1.00 92.85  ? 234 LEU C CB  1 
ATOM   9245  C  CG  . LEU C 2 227 ? 93.885  144.035 112.092 1.00 91.92  ? 234 LEU C CG  1 
ATOM   9246  C  CD1 . LEU C 2 227 ? 94.631  142.718 112.180 1.00 93.25  ? 234 LEU C CD1 1 
ATOM   9247  C  CD2 . LEU C 2 227 ? 94.609  145.112 112.861 1.00 93.88  ? 234 LEU C CD2 1 
ATOM   9248  N  N   . THR C 2 228 ? 94.048  146.876 108.502 1.00 84.80  ? 235 THR C N   1 
ATOM   9249  C  CA  . THR C 2 228 ? 94.065  147.462 107.173 1.00 84.25  ? 235 THR C CA  1 
ATOM   9250  C  C   . THR C 2 228 ? 95.122  146.880 106.248 1.00 86.27  ? 235 THR C C   1 
ATOM   9251  O  O   . THR C 2 228 ? 95.051  147.118 105.039 1.00 90.24  ? 235 THR C O   1 
ATOM   9252  C  CB  . THR C 2 228 ? 94.278  148.979 107.275 1.00 84.48  ? 235 THR C CB  1 
ATOM   9253  O  OG1 . THR C 2 228 ? 95.360  149.249 108.174 1.00 81.47  ? 235 THR C OG1 1 
ATOM   9254  C  CG2 . THR C 2 228 ? 93.025  149.656 107.796 1.00 86.73  ? 235 THR C CG2 1 
ATOM   9255  N  N   . ILE C 2 229 ? 96.085  146.122 106.765 1.00 75.55  ? 236 ILE C N   1 
ATOM   9256  C  CA  . ILE C 2 229 ? 97.276  145.750 106.010 1.00 71.46  ? 236 ILE C CA  1 
ATOM   9257  C  C   . ILE C 2 229 ? 97.179  144.291 105.587 1.00 74.54  ? 236 ILE C C   1 
ATOM   9258  O  O   . ILE C 2 229 ? 97.057  143.394 106.430 1.00 75.88  ? 236 ILE C O   1 
ATOM   9259  C  CB  . ILE C 2 229 ? 98.554  146.006 106.818 1.00 66.55  ? 236 ILE C CB  1 
ATOM   9260  C  CG1 . ILE C 2 229 ? 98.713  147.499 107.067 1.00 68.19  ? 236 ILE C CG1 1 
ATOM   9261  C  CG2 . ILE C 2 229 ? 99.758  145.487 106.075 1.00 70.80  ? 236 ILE C CG2 1 
ATOM   9262  C  CD1 . ILE C 2 229 ? 98.922  148.289 105.810 1.00 72.57  ? 236 ILE C CD1 1 
ATOM   9263  N  N   . PHE C 2 230 ? 97.250  144.065 104.278 1.00 82.95  ? 237 PHE C N   1 
ATOM   9264  C  CA  . PHE C 2 230 ? 97.340  142.735 103.684 1.00 79.22  ? 237 PHE C CA  1 
ATOM   9265  C  C   . PHE C 2 230 ? 98.800  142.300 103.736 1.00 78.99  ? 237 PHE C C   1 
ATOM   9266  O  O   . PHE C 2 230 ? 99.636  142.834 103.003 1.00 85.31  ? 237 PHE C O   1 
ATOM   9267  C  CB  . PHE C 2 230 ? 96.818  142.793 102.251 1.00 82.68  ? 237 PHE C CB  1 
ATOM   9268  C  CG  . PHE C 2 230 ? 96.521  141.458 101.636 1.00 79.96  ? 237 PHE C CG  1 
ATOM   9269  C  CD1 . PHE C 2 230 ? 97.523  140.536 101.414 1.00 82.41  ? 237 PHE C CD1 1 
ATOM   9270  C  CD2 . PHE C 2 230 ? 95.238  141.147 101.233 1.00 80.19  ? 237 PHE C CD2 1 
ATOM   9271  C  CE1 . PHE C 2 230 ? 97.247  139.324 100.830 1.00 85.14  ? 237 PHE C CE1 1 
ATOM   9272  C  CE2 . PHE C 2 230 ? 94.959  139.936 100.649 1.00 82.69  ? 237 PHE C CE2 1 
ATOM   9273  C  CZ  . PHE C 2 230 ? 95.965  139.024 100.448 1.00 84.75  ? 237 PHE C CZ  1 
ATOM   9274  N  N   . ASN C 2 231 ? 99.113  141.330 104.590 1.00 72.61  ? 238 ASN C N   1 
ATOM   9275  C  CA  . ASN C 2 231 ? 100.493 141.066 104.978 1.00 77.61  ? 238 ASN C CA  1 
ATOM   9276  C  C   . ASN C 2 231 ? 101.132 140.014 104.079 1.00 78.40  ? 238 ASN C C   1 
ATOM   9277  O  O   . ASN C 2 231 ? 100.689 138.862 104.050 1.00 77.43  ? 238 ASN C O   1 
ATOM   9278  C  CB  . ASN C 2 231 ? 100.561 140.623 106.437 1.00 76.24  ? 238 ASN C CB  1 
ATOM   9279  C  CG  . ASN C 2 231 ? 100.193 141.731 107.395 1.00 76.74  ? 238 ASN C CG  1 
ATOM   9280  O  OD1 . ASN C 2 231 ? 99.056  141.814 107.859 1.00 79.88  ? 238 ASN C OD1 1 
ATOM   9281  N  ND2 . ASN C 2 231 ? 101.153 142.598 107.693 1.00 71.59  ? 238 ASN C ND2 1 
ATOM   9282  N  N   . SER C 2 232 ? 102.180 140.418 103.359 1.00 89.98  ? 239 SER C N   1 
ATOM   9283  C  CA  . SER C 2 232 ? 103.120 139.517 102.692 1.00 86.76  ? 239 SER C CA  1 
ATOM   9284  C  C   . SER C 2 232 ? 102.412 138.586 101.702 1.00 89.40  ? 239 SER C C   1 
ATOM   9285  O  O   . SER C 2 232 ? 102.370 137.367 101.868 1.00 90.27  ? 239 SER C O   1 
ATOM   9286  C  CB  . SER C 2 232 ? 103.916 138.713 103.724 1.00 85.33  ? 239 SER C CB  1 
ATOM   9287  O  OG  . SER C 2 232 ? 104.736 137.752 103.088 1.00 86.89  ? 239 SER C OG  1 
ATOM   9288  N  N   . GLN C 2 233 ? 101.853 139.198 100.661 1.00 92.80  ? 240 GLN C N   1 
ATOM   9289  C  CA  . GLN C 2 233 ? 101.297 138.422 99.561  1.00 90.91  ? 240 GLN C CA  1 
ATOM   9290  C  C   . GLN C 2 233 ? 102.382 137.556 98.936  1.00 94.19  ? 240 GLN C C   1 
ATOM   9291  O  O   . GLN C 2 233 ? 103.507 138.010 98.715  1.00 96.57  ? 240 GLN C O   1 
ATOM   9292  C  CB  . GLN C 2 233 ? 100.693 139.345 98.504  1.00 90.74  ? 240 GLN C CB  1 
ATOM   9293  C  CG  . GLN C 2 233 ? 99.982  140.553 99.063  1.00 90.29  ? 240 GLN C CG  1 
ATOM   9294  C  CD  . GLN C 2 233 ? 99.426  141.449 97.982  1.00 94.48  ? 240 GLN C CD  1 
ATOM   9295  O  OE1 . GLN C 2 233 ? 99.587  141.176 96.796  1.00 101.13 ? 240 GLN C OE1 1 
ATOM   9296  N  NE2 . GLN C 2 233 ? 98.768  142.527 98.386  1.00 89.09  ? 240 GLN C NE2 1 
ATOM   9297  N  N   . ALA C 2 234 ? 102.048 136.298 98.656  1.00 104.26 ? 241 ALA C N   1 
ATOM   9298  C  CA  . ALA C 2 234 ? 103.029 135.348 98.149  1.00 102.40 ? 241 ALA C CA  1 
ATOM   9299  C  C   . ALA C 2 234 ? 102.659 134.776 96.791  1.00 104.37 ? 241 ALA C C   1 
ATOM   9300  O  O   . ALA C 2 234 ? 103.506 134.738 95.892  1.00 103.49 ? 241 ALA C O   1 
ATOM   9301  C  CB  . ALA C 2 234 ? 103.223 134.207 99.158  1.00 101.23 ? 241 ALA C CB  1 
ATOM   9302  N  N   . THR C 2 235 ? 101.422 134.318 96.613  1.00 117.35 ? 242 THR C N   1 
ATOM   9303  C  CA  . THR C 2 235 ? 101.040 133.630 95.389  1.00 118.43 ? 242 THR C CA  1 
ATOM   9304  C  C   . THR C 2 235 ? 99.688  134.117 94.893  1.00 116.51 ? 242 THR C C   1 
ATOM   9305  O  O   . THR C 2 235 ? 98.760  134.324 95.679  1.00 114.44 ? 242 THR C O   1 
ATOM   9306  C  CB  . THR C 2 235 ? 100.985 132.111 95.593  1.00 117.98 ? 242 THR C CB  1 
ATOM   9307  O  OG1 . THR C 2 235 ? 100.470 131.820 96.897  1.00 117.29 ? 242 THR C OG1 1 
ATOM   9308  C  CG2 . THR C 2 235 ? 102.370 131.502 95.448  1.00 116.95 ? 242 THR C CG2 1 
ATOM   9309  N  N   . ILE C 2 236 ? 99.595  134.291 93.578  1.00 123.55 ? 243 ILE C N   1 
ATOM   9310  C  CA  . ILE C 2 236 ? 98.338  134.552 92.888  1.00 124.28 ? 243 ILE C CA  1 
ATOM   9311  C  C   . ILE C 2 236 ? 97.900  133.262 92.216  1.00 127.50 ? 243 ILE C C   1 
ATOM   9312  O  O   . ILE C 2 236 ? 98.671  132.657 91.460  1.00 129.03 ? 243 ILE C O   1 
ATOM   9313  C  CB  . ILE C 2 236 ? 98.486  135.681 91.855  1.00 124.18 ? 243 ILE C CB  1 
ATOM   9314  C  CG1 . ILE C 2 236 ? 98.918  136.981 92.530  1.00 126.32 ? 243 ILE C CG1 1 
ATOM   9315  C  CG2 . ILE C 2 236 ? 97.183  135.883 91.102  1.00 123.22 ? 243 ILE C CG2 1 
ATOM   9316  C  CD1 . ILE C 2 236 ? 98.865  138.181 91.610  1.00 124.68 ? 243 ILE C CD1 1 
ATOM   9317  N  N   . ILE C 2 237 ? 96.670  132.838 92.488  1.00 137.14 ? 244 ILE C N   1 
ATOM   9318  C  CA  . ILE C 2 237 ? 96.127  131.589 91.969  1.00 135.82 ? 244 ILE C CA  1 
ATOM   9319  C  C   . ILE C 2 237 ? 94.936  131.916 91.082  1.00 136.33 ? 244 ILE C C   1 
ATOM   9320  O  O   . ILE C 2 237 ? 93.992  132.581 91.524  1.00 136.45 ? 244 ILE C O   1 
ATOM   9321  C  CB  . ILE C 2 237 ? 95.719  130.634 93.104  1.00 133.47 ? 244 ILE C CB  1 
ATOM   9322  C  CG1 . ILE C 2 237 ? 96.958  130.094 93.815  1.00 133.37 ? 244 ILE C CG1 1 
ATOM   9323  C  CG2 . ILE C 2 237 ? 94.879  129.494 92.562  1.00 134.94 ? 244 ILE C CG2 1 
ATOM   9324  C  CD1 . ILE C 2 237 ? 97.963  129.465 92.886  1.00 134.40 ? 244 ILE C CD1 1 
ATOM   9325  N  N   . ILE C 2 238 ? 94.975  131.441 89.841  1.00 143.21 ? 245 ILE C N   1 
ATOM   9326  C  CA  . ILE C 2 238 ? 93.935  131.697 88.853  1.00 143.44 ? 245 ILE C CA  1 
ATOM   9327  C  C   . ILE C 2 238 ? 93.329  130.361 88.457  1.00 143.31 ? 245 ILE C C   1 
ATOM   9328  O  O   . ILE C 2 238 ? 94.051  129.453 88.024  1.00 142.87 ? 245 ILE C O   1 
ATOM   9329  C  CB  . ILE C 2 238 ? 94.487  132.424 87.618  1.00 142.50 ? 245 ILE C CB  1 
ATOM   9330  C  CG1 . ILE C 2 238 ? 95.436  133.546 88.033  1.00 141.20 ? 245 ILE C CG1 1 
ATOM   9331  C  CG2 . ILE C 2 238 ? 93.355  132.976 86.778  1.00 142.07 ? 245 ILE C CG2 1 
ATOM   9332  C  CD1 . ILE C 2 238 ? 96.310  134.037 86.906  1.00 141.58 ? 245 ILE C CD1 1 
ATOM   9333  N  N   . GLY C 2 239 ? 92.006  130.243 88.592  1.00 153.48 ? 246 GLY C N   1 
ATOM   9334  C  CA  . GLY C 2 239 ? 91.268  129.053 88.203  1.00 155.14 ? 246 GLY C CA  1 
ATOM   9335  C  C   . GLY C 2 239 ? 90.575  128.358 89.359  1.00 155.73 ? 246 GLY C C   1 
ATOM   9336  O  O   . GLY C 2 239 ? 89.501  127.777 89.172  1.00 155.49 ? 246 GLY C O   1 
ATOM   9337  N  N   . GLY C 2 240 ? 91.164  128.412 90.548  1.00 157.68 ? 247 GLY C N   1 
ATOM   9338  C  CA  . GLY C 2 240 ? 90.580  127.748 91.700  1.00 156.94 ? 247 GLY C CA  1 
ATOM   9339  C  C   . GLY C 2 240 ? 90.579  126.237 91.614  1.00 157.69 ? 247 GLY C C   1 
ATOM   9340  O  O   . GLY C 2 240 ? 89.604  125.597 92.027  1.00 157.00 ? 247 GLY C O   1 
ATOM   9341  N  N   . LYS C 2 241 ? 91.649  125.648 91.076  1.00 157.25 ? 248 LYS C N   1 
ATOM   9342  C  CA  . LYS C 2 241 ? 91.749  124.193 91.042  1.00 157.17 ? 248 LYS C CA  1 
ATOM   9343  C  C   . LYS C 2 241 ? 91.942  123.625 92.442  1.00 156.79 ? 248 LYS C C   1 
ATOM   9344  O  O   . LYS C 2 241 ? 91.268  122.665 92.834  1.00 155.17 ? 248 LYS C O   1 
ATOM   9345  C  CB  . LYS C 2 241 ? 92.898  123.768 90.128  1.00 157.23 ? 248 LYS C CB  1 
ATOM   9346  C  CG  . LYS C 2 241 ? 92.954  122.273 89.853  1.00 157.13 ? 248 LYS C CG  1 
ATOM   9347  C  CD  . LYS C 2 241 ? 94.237  121.896 89.130  1.00 156.92 ? 248 LYS C CD  1 
ATOM   9348  C  CE  . LYS C 2 241 ? 94.078  120.598 88.358  1.00 156.46 ? 248 LYS C CE  1 
ATOM   9349  N  NZ  . LYS C 2 241 ? 93.092  120.736 87.252  1.00 156.10 ? 248 LYS C NZ  1 
ATOM   9350  N  N   . GLU C 2 242 ? 92.859  124.210 93.212  1.00 155.48 ? 249 GLU C N   1 
ATOM   9351  C  CA  . GLU C 2 242 ? 93.146  123.723 94.555  1.00 154.95 ? 249 GLU C CA  1 
ATOM   9352  C  C   . GLU C 2 242 ? 92.092  124.140 95.571  1.00 155.48 ? 249 GLU C C   1 
ATOM   9353  O  O   . GLU C 2 242 ? 92.036  123.556 96.659  1.00 154.47 ? 249 GLU C O   1 
ATOM   9354  C  CB  . GLU C 2 242 ? 94.523  124.217 95.003  1.00 153.82 ? 249 GLU C CB  1 
ATOM   9355  C  CG  . GLU C 2 242 ? 95.663  123.752 94.111  1.00 153.66 ? 249 GLU C CG  1 
ATOM   9356  C  CD  . GLU C 2 242 ? 96.926  124.568 94.305  1.00 154.95 ? 249 GLU C CD  1 
ATOM   9357  O  OE1 . GLU C 2 242 ? 96.828  125.710 94.800  1.00 156.16 ? 249 GLU C OE1 1 
ATOM   9358  O  OE2 . GLU C 2 242 ? 98.017  124.068 93.961  1.00 154.89 ? 249 GLU C OE2 1 
ATOM   9359  N  N   . GLN C 2 243 ? 91.261  125.132 95.245  1.00 155.73 ? 250 GLN C N   1 
ATOM   9360  C  CA  . GLN C 2 243 ? 90.236  125.578 96.183  1.00 155.12 ? 250 GLN C CA  1 
ATOM   9361  C  C   . GLN C 2 243 ? 89.074  124.596 96.259  1.00 153.47 ? 250 GLN C C   1 
ATOM   9362  O  O   . GLN C 2 243 ? 88.388  124.528 97.285  1.00 153.02 ? 250 GLN C O   1 
ATOM   9363  C  CB  . GLN C 2 243 ? 89.731  126.967 95.793  1.00 153.36 ? 250 GLN C CB  1 
ATOM   9364  C  CG  . GLN C 2 243 ? 90.544  128.106 96.378  1.00 152.42 ? 250 GLN C CG  1 
ATOM   9365  C  CD  . GLN C 2 243 ? 92.029  127.938 96.141  1.00 154.06 ? 250 GLN C CD  1 
ATOM   9366  O  OE1 . GLN C 2 243 ? 92.473  127.764 95.007  1.00 153.38 ? 250 GLN C OE1 1 
ATOM   9367  N  NE2 . GLN C 2 243 ? 92.808  127.979 97.216  1.00 153.83 ? 250 GLN C NE2 1 
ATOM   9368  N  N   . GLY C 2 244 ? 88.838  123.837 95.196  1.00 155.62 ? 251 GLY C N   1 
ATOM   9369  C  CA  . GLY C 2 244 ? 87.753  122.875 95.151  1.00 157.33 ? 251 GLY C CA  1 
ATOM   9370  C  C   . GLY C 2 244 ? 86.683  123.176 94.127  1.00 158.28 ? 251 GLY C C   1 
ATOM   9371  O  O   . GLY C 2 244 ? 85.796  122.334 93.916  1.00 158.23 ? 251 GLY C O   1 
ATOM   9372  N  N   . GLN C 2 245 ? 86.717  124.341 93.479  1.00 158.10 ? 252 GLN C N   1 
ATOM   9373  C  CA  . GLN C 2 245 ? 85.753  124.710 92.444  1.00 158.10 ? 252 GLN C CA  1 
ATOM   9374  C  C   . GLN C 2 245 ? 86.517  124.996 91.158  1.00 157.73 ? 252 GLN C C   1 
ATOM   9375  O  O   . GLN C 2 245 ? 86.963  126.131 90.929  1.00 158.14 ? 252 GLN C O   1 
ATOM   9376  C  CB  . GLN C 2 245 ? 84.918  125.915 92.871  1.00 156.83 ? 252 GLN C CB  1 
ATOM   9377  C  CG  . GLN C 2 245 ? 83.868  125.606 93.928  1.00 156.48 ? 252 GLN C CG  1 
ATOM   9378  C  CD  . GLN C 2 245 ? 84.431  125.608 95.337  1.00 156.46 ? 252 GLN C CD  1 
ATOM   9379  O  OE1 . GLN C 2 245 ? 85.643  125.683 95.534  1.00 156.19 ? 252 GLN C OE1 1 
ATOM   9380  N  NE2 . GLN C 2 245 ? 83.550  125.528 96.326  1.00 156.13 ? 252 GLN C NE2 1 
ATOM   9381  N  N   . PRO C 2 246 ? 86.698  123.998 90.295  1.00 161.03 ? 253 PRO C N   1 
ATOM   9382  C  CA  . PRO C 2 246 ? 87.396  124.238 89.027  1.00 161.38 ? 253 PRO C CA  1 
ATOM   9383  C  C   . PRO C 2 246 ? 86.613  125.197 88.144  1.00 161.73 ? 253 PRO C C   1 
ATOM   9384  O  O   . PRO C 2 246 ? 85.389  125.306 88.238  1.00 161.35 ? 253 PRO C O   1 
ATOM   9385  C  CB  . PRO C 2 246 ? 87.488  122.843 88.397  1.00 160.78 ? 253 PRO C CB  1 
ATOM   9386  C  CG  . PRO C 2 246 ? 87.257  121.885 89.528  1.00 160.44 ? 253 PRO C CG  1 
ATOM   9387  C  CD  . PRO C 2 246 ? 86.329  122.584 90.467  1.00 160.11 ? 253 PRO C CD  1 
ATOM   9388  N  N   . PHE C 2 247 ? 87.339  125.903 87.285  1.00 161.79 ? 254 PHE C N   1 
ATOM   9389  C  CA  . PHE C 2 247 ? 86.764  126.931 86.431  1.00 161.74 ? 254 PHE C CA  1 
ATOM   9390  C  C   . PHE C 2 247 ? 86.695  126.444 84.991  1.00 162.53 ? 254 PHE C C   1 
ATOM   9391  O  O   . PHE C 2 247 ? 87.637  125.823 84.487  1.00 161.95 ? 254 PHE C O   1 
ATOM   9392  C  CB  . PHE C 2 247 ? 87.581  128.223 86.506  1.00 159.91 ? 254 PHE C CB  1 
ATOM   9393  C  CG  . PHE C 2 247 ? 86.905  129.400 85.875  1.00 159.72 ? 254 PHE C CG  1 
ATOM   9394  C  CD1 . PHE C 2 247 ? 85.832  130.012 86.497  1.00 159.49 ? 254 PHE C CD1 1 
ATOM   9395  C  CD2 . PHE C 2 247 ? 87.340  129.895 84.658  1.00 160.35 ? 254 PHE C CD2 1 
ATOM   9396  C  CE1 . PHE C 2 247 ? 85.207  131.098 85.920  1.00 160.41 ? 254 PHE C CE1 1 
ATOM   9397  C  CE2 . PHE C 2 247 ? 86.719  130.979 84.074  1.00 161.03 ? 254 PHE C CE2 1 
ATOM   9398  C  CZ  . PHE C 2 247 ? 85.650  131.582 84.706  1.00 160.72 ? 254 PHE C CZ  1 
ATOM   9399  N  N   . GLN C 2 248 ? 85.572  126.724 84.335  1.00 161.90 ? 255 GLN C N   1 
ATOM   9400  C  CA  . GLN C 2 248 ? 85.362  126.377 82.930  1.00 160.56 ? 255 GLN C CA  1 
ATOM   9401  C  C   . GLN C 2 248 ? 84.819  127.617 82.226  1.00 160.83 ? 255 GLN C C   1 
ATOM   9402  O  O   . GLN C 2 248 ? 83.616  127.889 82.276  1.00 160.30 ? 255 GLN C O   1 
ATOM   9403  C  CB  . GLN C 2 248 ? 84.412  125.193 82.791  1.00 160.43 ? 255 GLN C CB  1 
ATOM   9404  C  CG  . GLN C 2 248 ? 84.479  124.498 81.442  1.00 161.23 ? 255 GLN C CG  1 
ATOM   9405  C  CD  . GLN C 2 248 ? 83.604  123.262 81.381  1.00 160.70 ? 255 GLN C CD  1 
ATOM   9406  O  OE1 . GLN C 2 248 ? 82.592  123.169 82.074  1.00 160.12 ? 255 GLN C OE1 1 
ATOM   9407  N  NE2 . GLN C 2 248 ? 83.993  122.303 80.550  1.00 160.44 ? 255 GLN C NE2 1 
ATOM   9408  N  N   . GLY C 2 249 ? 85.706  128.365 81.573  1.00 160.21 ? 256 GLY C N   1 
ATOM   9409  C  CA  . GLY C 2 249 ? 85.315  129.589 80.902  1.00 159.71 ? 256 GLY C CA  1 
ATOM   9410  C  C   . GLY C 2 249 ? 86.484  130.343 80.303  1.00 159.28 ? 256 GLY C C   1 
ATOM   9411  O  O   . GLY C 2 249 ? 87.492  129.738 79.927  1.00 158.12 ? 256 GLY C O   1 
ATOM   9412  N  N   . GLN C 2 250 ? 86.359  131.666 80.204  1.00 162.13 ? 257 GLN C N   1 
ATOM   9413  C  CA  . GLN C 2 250 ? 87.392  132.514 79.624  1.00 163.02 ? 257 GLN C CA  1 
ATOM   9414  C  C   . GLN C 2 250 ? 87.690  133.676 80.561  1.00 162.96 ? 257 GLN C C   1 
ATOM   9415  O  O   . GLN C 2 250 ? 86.772  134.260 81.146  1.00 162.86 ? 257 GLN C O   1 
ATOM   9416  C  CB  . GLN C 2 250 ? 86.961  133.054 78.256  1.00 162.74 ? 257 GLN C CB  1 
ATOM   9417  C  CG  . GLN C 2 250 ? 86.246  132.036 77.385  1.00 162.83 ? 257 GLN C CG  1 
ATOM   9418  C  CD  . GLN C 2 250 ? 85.958  132.554 75.991  1.00 162.75 ? 257 GLN C CD  1 
ATOM   9419  O  OE1 . GLN C 2 250 ? 86.012  133.757 75.738  1.00 163.02 ? 257 GLN C OE1 1 
ATOM   9420  N  NE2 . GLN C 2 250 ? 85.637  131.644 75.078  1.00 162.39 ? 257 GLN C NE2 1 
ATOM   9421  N  N   . LEU C 2 251 ? 88.975  134.015 80.686  1.00 157.51 ? 258 LEU C N   1 
ATOM   9422  C  CA  . LEU C 2 251 ? 89.434  135.121 81.515  1.00 156.50 ? 258 LEU C CA  1 
ATOM   9423  C  C   . LEU C 2 251 ? 90.352  136.020 80.699  1.00 157.08 ? 258 LEU C C   1 
ATOM   9424  O  O   . LEU C 2 251 ? 91.052  135.556 79.796  1.00 156.97 ? 258 LEU C O   1 
ATOM   9425  C  CB  . LEU C 2 251 ? 90.181  134.620 82.758  1.00 155.80 ? 258 LEU C CB  1 
ATOM   9426  C  CG  . LEU C 2 251 ? 89.459  133.596 83.633  1.00 156.67 ? 258 LEU C CG  1 
ATOM   9427  C  CD1 . LEU C 2 251 ? 90.403  133.034 84.674  1.00 156.04 ? 258 LEU C CD1 1 
ATOM   9428  C  CD2 . LEU C 2 251 ? 88.254  134.222 84.299  1.00 156.89 ? 258 LEU C CD2 1 
ATOM   9429  N  N   . SER C 2 252 ? 90.355  137.312 81.032  1.00 157.07 ? 259 SER C N   1 
ATOM   9430  C  CA  . SER C 2 252 ? 91.141  138.292 80.292  1.00 156.78 ? 259 SER C CA  1 
ATOM   9431  C  C   . SER C 2 252 ? 91.486  139.475 81.187  1.00 155.90 ? 259 SER C C   1 
ATOM   9432  O  O   . SER C 2 252 ? 90.611  140.030 81.860  1.00 156.36 ? 259 SER C O   1 
ATOM   9433  C  CB  . SER C 2 252 ? 90.380  138.783 79.053  1.00 157.62 ? 259 SER C CB  1 
ATOM   9434  O  OG  . SER C 2 252 ? 89.858  137.702 78.298  1.00 159.18 ? 259 SER C OG  1 
ATOM   9435  N  N   . GLY C 2 253 ? 92.758  139.868 81.175  1.00 141.84 ? 260 GLY C N   1 
ATOM   9436  C  CA  . GLY C 2 253 ? 93.196  141.074 81.854  1.00 141.80 ? 260 GLY C CA  1 
ATOM   9437  C  C   . GLY C 2 253 ? 93.170  141.056 83.371  1.00 142.36 ? 260 GLY C C   1 
ATOM   9438  O  O   . GLY C 2 253 ? 92.365  141.758 83.989  1.00 141.79 ? 260 GLY C O   1 
ATOM   9439  N  N   . LEU C 2 254 ? 94.041  140.259 83.985  1.00 138.68 ? 261 LEU C N   1 
ATOM   9440  C  CA  . LEU C 2 254 ? 94.234  140.299 85.433  1.00 137.52 ? 261 LEU C CA  1 
ATOM   9441  C  C   . LEU C 2 254 ? 95.223  141.401 85.775  1.00 137.51 ? 261 LEU C C   1 
ATOM   9442  O  O   . LEU C 2 254 ? 96.437  141.186 85.788  1.00 136.21 ? 261 LEU C O   1 
ATOM   9443  C  CB  . LEU C 2 254 ? 94.714  138.953 85.960  1.00 137.20 ? 261 LEU C CB  1 
ATOM   9444  C  CG  . LEU C 2 254 ? 94.213  138.550 87.350  1.00 138.44 ? 261 LEU C CG  1 
ATOM   9445  C  CD1 . LEU C 2 254 ? 92.752  138.881 87.571  1.00 137.96 ? 261 LEU C CD1 1 
ATOM   9446  C  CD2 . LEU C 2 254 ? 94.460  137.075 87.584  1.00 137.75 ? 261 LEU C CD2 1 
ATOM   9447  N  N   . TYR C 2 255 ? 94.698  142.586 86.061  1.00 132.35 ? 262 TYR C N   1 
ATOM   9448  C  CA  . TYR C 2 255 ? 95.486  143.703 86.556  1.00 130.66 ? 262 TYR C CA  1 
ATOM   9449  C  C   . TYR C 2 255 ? 95.437  143.680 88.076  1.00 132.38 ? 262 TYR C C   1 
ATOM   9450  O  O   . TYR C 2 255 ? 94.352  143.724 88.665  1.00 132.64 ? 262 TYR C O   1 
ATOM   9451  C  CB  . TYR C 2 255 ? 94.950  145.029 86.018  1.00 129.38 ? 262 TYR C CB  1 
ATOM   9452  C  CG  . TYR C 2 255 ? 95.436  146.243 86.772  1.00 131.04 ? 262 TYR C CG  1 
ATOM   9453  C  CD1 . TYR C 2 255 ? 96.752  146.668 86.672  1.00 130.69 ? 262 TYR C CD1 1 
ATOM   9454  C  CD2 . TYR C 2 255 ? 94.574  146.969 87.584  1.00 132.41 ? 262 TYR C CD2 1 
ATOM   9455  C  CE1 . TYR C 2 255 ? 97.197  147.780 87.358  1.00 131.16 ? 262 TYR C CE1 1 
ATOM   9456  C  CE2 . TYR C 2 255 ? 95.011  148.083 88.276  1.00 133.04 ? 262 TYR C CE2 1 
ATOM   9457  C  CZ  . TYR C 2 255 ? 96.326  148.483 88.159  1.00 132.70 ? 262 TYR C CZ  1 
ATOM   9458  O  OH  . TYR C 2 255 ? 96.785  149.588 88.838  1.00 130.66 ? 262 TYR C OH  1 
ATOM   9459  N  N   . TYR C 2 256 ? 96.609  143.604 88.706  1.00 125.19 ? 263 TYR C N   1 
ATOM   9460  C  CA  . TYR C 2 256 ? 96.713  143.543 90.165  1.00 122.18 ? 263 TYR C CA  1 
ATOM   9461  C  C   . TYR C 2 256 ? 97.917  144.386 90.580  1.00 122.04 ? 263 TYR C C   1 
ATOM   9462  O  O   . TYR C 2 256 ? 99.051  143.901 90.585  1.00 123.00 ? 263 TYR C O   1 
ATOM   9463  C  CB  . TYR C 2 256 ? 96.837  142.105 90.647  1.00 122.68 ? 263 TYR C CB  1 
ATOM   9464  C  CG  . TYR C 2 256 ? 96.755  141.958 92.146  1.00 124.80 ? 263 TYR C CG  1 
ATOM   9465  C  CD1 . TYR C 2 256 ? 97.891  142.047 92.937  1.00 124.69 ? 263 TYR C CD1 1 
ATOM   9466  C  CD2 . TYR C 2 256 ? 95.539  141.732 92.771  1.00 124.29 ? 263 TYR C CD2 1 
ATOM   9467  C  CE1 . TYR C 2 256 ? 97.815  141.915 94.305  1.00 124.01 ? 263 TYR C CE1 1 
ATOM   9468  C  CE2 . TYR C 2 256 ? 95.455  141.597 94.139  1.00 123.56 ? 263 TYR C CE2 1 
ATOM   9469  C  CZ  . TYR C 2 256 ? 96.595  141.690 94.899  1.00 124.22 ? 263 TYR C CZ  1 
ATOM   9470  O  OH  . TYR C 2 256 ? 96.514  141.558 96.262  1.00 124.74 ? 263 TYR C OH  1 
ATOM   9471  N  N   . ASN C 2 257 ? 97.656  145.649 90.923  1.00 119.24 ? 264 ASN C N   1 
ATOM   9472  C  CA  . ASN C 2 257 ? 98.687  146.566 91.412  1.00 121.37 ? 264 ASN C CA  1 
ATOM   9473  C  C   . ASN C 2 257 ? 99.853  146.676 90.431  1.00 122.92 ? 264 ASN C C   1 
ATOM   9474  O  O   . ASN C 2 257 ? 101.018 146.740 90.827  1.00 122.76 ? 264 ASN C O   1 
ATOM   9475  C  CB  . ASN C 2 257 ? 99.182  146.149 92.797  1.00 121.32 ? 264 ASN C CB  1 
ATOM   9476  C  CG  . ASN C 2 257 ? 98.104  146.250 93.854  1.00 121.31 ? 264 ASN C CG  1 
ATOM   9477  O  OD1 . ASN C 2 257 ? 97.157  147.024 93.719  1.00 122.85 ? 264 ASN C OD1 1 
ATOM   9478  N  ND2 . ASN C 2 257 ? 98.241  145.466 94.915  1.00 118.12 ? 264 ASN C ND2 1 
ATOM   9479  N  N   . GLY C 2 258 ? 99.537  146.698 89.140  1.00 127.13 ? 265 GLY C N   1 
ATOM   9480  C  CA  . GLY C 2 258 ? 100.548 146.855 88.116  1.00 125.73 ? 265 GLY C CA  1 
ATOM   9481  C  C   . GLY C 2 258 ? 101.264 145.590 87.707  1.00 125.64 ? 265 GLY C C   1 
ATOM   9482  O  O   . GLY C 2 258 ? 102.268 145.674 86.991  1.00 126.69 ? 265 GLY C O   1 
ATOM   9483  N  N   . LEU C 2 259 ? 100.788 144.424 88.132  1.00 125.77 ? 266 LEU C N   1 
ATOM   9484  C  CA  . LEU C 2 259 ? 101.399 143.143 87.784  1.00 126.39 ? 266 LEU C CA  1 
ATOM   9485  C  C   . LEU C 2 259 ? 100.372 142.326 87.006  1.00 128.26 ? 266 LEU C C   1 
ATOM   9486  O  O   . LEU C 2 259 ? 99.626  141.534 87.585  1.00 128.43 ? 266 LEU C O   1 
ATOM   9487  C  CB  . LEU C 2 259 ? 101.874 142.406 89.030  1.00 125.36 ? 266 LEU C CB  1 
ATOM   9488  C  CG  . LEU C 2 259 ? 102.902 143.144 89.887  1.00 125.00 ? 266 LEU C CG  1 
ATOM   9489  C  CD1 . LEU C 2 259 ? 103.438 142.235 90.974  1.00 123.97 ? 266 LEU C CD1 1 
ATOM   9490  C  CD2 . LEU C 2 259 ? 104.036 143.681 89.029  1.00 125.72 ? 266 LEU C CD2 1 
ATOM   9491  N  N   . LYS C 2 260 ? 100.341 142.518 85.690  1.00 135.89 ? 267 LYS C N   1 
ATOM   9492  C  CA  . LYS C 2 260 ? 99.409  141.797 84.825  1.00 134.81 ? 267 LYS C CA  1 
ATOM   9493  C  C   . LYS C 2 260 ? 99.935  140.382 84.626  1.00 134.34 ? 267 LYS C C   1 
ATOM   9494  O  O   . LYS C 2 260 ? 100.816 140.142 83.797  1.00 135.25 ? 267 LYS C O   1 
ATOM   9495  C  CB  . LYS C 2 260 ? 99.236  142.523 83.497  1.00 133.45 ? 267 LYS C CB  1 
ATOM   9496  C  CG  . LYS C 2 260 ? 98.579  143.886 83.625  1.00 133.62 ? 267 LYS C CG  1 
ATOM   9497  C  CD  . LYS C 2 260 ? 98.086  144.390 82.281  1.00 133.55 ? 267 LYS C CD  1 
ATOM   9498  C  CE  . LYS C 2 260 ? 97.157  145.581 82.447  1.00 133.87 ? 267 LYS C CE  1 
ATOM   9499  N  NZ  . LYS C 2 260 ? 96.634  146.067 81.140  1.00 133.91 ? 267 LYS C NZ  1 
ATOM   9500  N  N   . VAL C 2 261 ? 99.393  139.437 85.396  1.00 135.41 ? 268 VAL C N   1 
ATOM   9501  C  CA  . VAL C 2 261 ? 99.884  138.064 85.342  1.00 137.06 ? 268 VAL C CA  1 
ATOM   9502  C  C   . VAL C 2 261 ? 99.493  137.397 84.027  1.00 139.50 ? 268 VAL C C   1 
ATOM   9503  O  O   . VAL C 2 261 ? 100.284 136.651 83.439  1.00 139.35 ? 268 VAL C O   1 
ATOM   9504  C  CB  . VAL C 2 261 ? 99.382  137.271 86.562  1.00 137.08 ? 268 VAL C CB  1 
ATOM   9505  C  CG1 . VAL C 2 261 ? 97.887  137.419 86.708  1.00 137.04 ? 268 VAL C CG1 1 
ATOM   9506  C  CG2 . VAL C 2 261 ? 99.771  135.806 86.448  1.00 137.80 ? 268 VAL C CG2 1 
ATOM   9507  N  N   . LEU C 2 262 ? 98.273  137.650 83.543  1.00 143.20 ? 269 LEU C N   1 
ATOM   9508  C  CA  . LEU C 2 262 ? 97.855  137.060 82.275  1.00 141.71 ? 269 LEU C CA  1 
ATOM   9509  C  C   . LEU C 2 262 ? 98.680  137.589 81.110  1.00 141.45 ? 269 LEU C C   1 
ATOM   9510  O  O   . LEU C 2 262 ? 98.896  136.868 80.130  1.00 141.26 ? 269 LEU C O   1 
ATOM   9511  C  CB  . LEU C 2 262 ? 96.368  137.319 82.032  1.00 141.21 ? 269 LEU C CB  1 
ATOM   9512  C  CG  . LEU C 2 262 ? 95.397  136.413 82.789  1.00 141.48 ? 269 LEU C CG  1 
ATOM   9513  C  CD1 . LEU C 2 262 ? 93.957  136.779 82.471  1.00 141.02 ? 269 LEU C CD1 1 
ATOM   9514  C  CD2 . LEU C 2 262 ? 95.665  134.956 82.459  1.00 141.53 ? 269 LEU C CD2 1 
ATOM   9515  N  N   . ASN C 2 263 ? 99.141  138.838 81.195  1.00 144.19 ? 270 ASN C N   1 
ATOM   9516  C  CA  . ASN C 2 263 ? 99.998  139.384 80.149  1.00 144.30 ? 270 ASN C CA  1 
ATOM   9517  C  C   . ASN C 2 263 ? 101.315 138.622 80.061  1.00 145.01 ? 270 ASN C C   1 
ATOM   9518  O  O   . ASN C 2 263 ? 101.795 138.321 78.962  1.00 143.59 ? 270 ASN C O   1 
ATOM   9519  C  CB  . ASN C 2 263 ? 100.250 140.869 80.405  1.00 142.95 ? 270 ASN C CB  1 
ATOM   9520  C  CG  . ASN C 2 263 ? 101.042 141.525 79.296  1.00 143.33 ? 270 ASN C CG  1 
ATOM   9521  O  OD1 . ASN C 2 263 ? 100.967 141.116 78.138  1.00 145.23 ? 270 ASN C OD1 1 
ATOM   9522  N  ND2 . ASN C 2 263 ? 101.808 142.553 79.645  1.00 142.12 ? 270 ASN C ND2 1 
ATOM   9523  N  N   . MET C 2 264 ? 101.915 138.303 81.209  1.00 146.50 ? 271 MET C N   1 
ATOM   9524  C  CA  . MET C 2 264 ? 103.169 137.562 81.238  1.00 145.26 ? 271 MET C CA  1 
ATOM   9525  C  C   . MET C 2 264 ? 102.980 136.061 81.076  1.00 145.42 ? 271 MET C C   1 
ATOM   9526  O  O   . MET C 2 264 ? 103.963 135.355 80.827  1.00 145.52 ? 271 MET C O   1 
ATOM   9527  C  CB  . MET C 2 264 ? 103.915 137.838 82.546  1.00 144.84 ? 271 MET C CB  1 
ATOM   9528  C  CG  . MET C 2 264 ? 104.671 139.154 82.571  1.00 145.83 ? 271 MET C CG  1 
ATOM   9529  S  SD  . MET C 2 264 ? 105.418 139.489 84.178  1.00 147.12 ? 271 MET C SD  1 
ATOM   9530  C  CE  . MET C 2 264 ? 104.659 141.058 84.589  1.00 144.49 ? 271 MET C CE  1 
ATOM   9531  N  N   . ALA C 2 265 ? 101.752 135.558 81.218  1.00 147.42 ? 272 ALA C N   1 
ATOM   9532  C  CA  . ALA C 2 265 ? 101.520 134.123 81.098  1.00 147.42 ? 272 ALA C CA  1 
ATOM   9533  C  C   . ALA C 2 265 ? 101.856 133.623 79.700  1.00 147.94 ? 272 ALA C C   1 
ATOM   9534  O  O   . ALA C 2 265 ? 102.452 132.551 79.541  1.00 147.20 ? 272 ALA C O   1 
ATOM   9535  C  CB  . ALA C 2 265 ? 100.071 133.795 81.454  1.00 146.51 ? 272 ALA C CB  1 
ATOM   9536  N  N   . ALA C 2 266 ? 101.479 134.383 78.672  1.00 154.33 ? 273 ALA C N   1 
ATOM   9537  C  CA  . ALA C 2 266 ? 101.806 134.007 77.303  1.00 154.40 ? 273 ALA C CA  1 
ATOM   9538  C  C   . ALA C 2 266 ? 103.279 134.201 76.975  1.00 154.73 ? 273 ALA C C   1 
ATOM   9539  O  O   . ALA C 2 266 ? 103.744 133.665 75.964  1.00 154.78 ? 273 ALA C O   1 
ATOM   9540  C  CB  . ALA C 2 266 ? 100.951 134.807 76.321  1.00 153.59 ? 273 ALA C CB  1 
ATOM   9541  N  N   . GLU C 2 267 ? 104.018 134.940 77.798  1.00 151.93 ? 274 GLU C N   1 
ATOM   9542  C  CA  . GLU C 2 267 ? 105.425 135.217 77.547  1.00 150.98 ? 274 GLU C CA  1 
ATOM   9543  C  C   . GLU C 2 267 ? 106.352 134.170 78.148  1.00 150.31 ? 274 GLU C C   1 
ATOM   9544  O  O   . GLU C 2 267 ? 107.574 134.334 78.071  1.00 150.22 ? 274 GLU C O   1 
ATOM   9545  C  CB  . GLU C 2 267 ? 105.793 136.602 78.087  1.00 149.35 ? 274 GLU C CB  1 
ATOM   9546  C  CG  . GLU C 2 267 ? 104.836 137.705 77.662  1.00 149.73 ? 274 GLU C CG  1 
ATOM   9547  C  CD  . GLU C 2 267 ? 104.652 137.773 76.158  1.00 151.51 ? 274 GLU C CD  1 
ATOM   9548  O  OE1 . GLU C 2 267 ? 105.668 137.745 75.431  1.00 152.08 ? 274 GLU C OE1 1 
ATOM   9549  O  OE2 . GLU C 2 267 ? 103.492 137.852 75.702  1.00 151.07 ? 274 GLU C OE2 1 
ATOM   9550  N  N   . ASN C 2 268 ? 105.801 133.107 78.740  1.00 149.41 ? 275 ASN C N   1 
ATOM   9551  C  CA  . ASN C 2 268 ? 106.587 132.024 79.334  1.00 150.14 ? 275 ASN C CA  1 
ATOM   9552  C  C   . ASN C 2 268 ? 107.556 132.559 80.387  1.00 150.50 ? 275 ASN C C   1 
ATOM   9553  O  O   . ASN C 2 268 ? 108.745 132.231 80.400  1.00 150.81 ? 275 ASN C O   1 
ATOM   9554  C  CB  . ASN C 2 268 ? 107.328 131.226 78.257  1.00 150.80 ? 275 ASN C CB  1 
ATOM   9555  C  CG  . ASN C 2 268 ? 107.692 129.825 78.714  1.00 150.42 ? 275 ASN C CG  1 
ATOM   9556  O  OD1 . ASN C 2 268 ? 107.661 129.520 79.907  1.00 149.83 ? 275 ASN C OD1 1 
ATOM   9557  N  ND2 . ASN C 2 268 ? 108.041 128.965 77.765  1.00 149.87 ? 275 ASN C ND2 1 
ATOM   9558  N  N   . ASP C 2 269 ? 107.035 133.402 81.274  1.00 149.78 ? 276 ASP C N   1 
ATOM   9559  C  CA  . ASP C 2 269 ? 107.844 133.949 82.353  1.00 150.61 ? 276 ASP C CA  1 
ATOM   9560  C  C   . ASP C 2 269 ? 108.257 132.847 83.324  1.00 150.80 ? 276 ASP C C   1 
ATOM   9561  O  O   . ASP C 2 269 ? 107.547 131.856 83.517  1.00 151.66 ? 276 ASP C O   1 
ATOM   9562  C  CB  . ASP C 2 269 ? 107.076 135.042 83.094  1.00 150.32 ? 276 ASP C CB  1 
ATOM   9563  C  CG  . ASP C 2 269 ? 107.872 135.645 84.233  1.00 149.93 ? 276 ASP C CG  1 
ATOM   9564  O  OD1 . ASP C 2 269 ? 109.055 135.986 84.017  1.00 148.78 ? 276 ASP C OD1 1 
ATOM   9565  O  OD2 . ASP C 2 269 ? 107.319 135.770 85.346  1.00 148.42 ? 276 ASP C OD2 1 
ATOM   9566  N  N   . ALA C 2 270 ? 109.431 133.029 83.935  1.00 146.27 ? 277 ALA C N   1 
ATOM   9567  C  CA  . ALA C 2 270 ? 109.960 132.016 84.842  1.00 146.13 ? 277 ALA C CA  1 
ATOM   9568  C  C   . ALA C 2 270 ? 109.062 131.828 86.059  1.00 146.78 ? 277 ALA C C   1 
ATOM   9569  O  O   . ALA C 2 270 ? 108.864 130.700 86.524  1.00 145.66 ? 277 ALA C O   1 
ATOM   9570  C  CB  . ALA C 2 270 ? 111.378 132.391 85.274  1.00 144.79 ? 277 ALA C CB  1 
ATOM   9571  N  N   . ASN C 2 271 ? 108.512 132.919 86.590  1.00 144.23 ? 278 ASN C N   1 
ATOM   9572  C  CA  . ASN C 2 271 ? 107.721 132.854 87.813  1.00 143.33 ? 278 ASN C CA  1 
ATOM   9573  C  C   . ASN C 2 271 ? 106.307 132.332 87.592  1.00 142.47 ? 278 ASN C C   1 
ATOM   9574  O  O   . ASN C 2 271 ? 105.649 131.955 88.568  1.00 142.05 ? 278 ASN C O   1 
ATOM   9575  C  CB  . ASN C 2 271 ? 107.655 134.236 88.465  1.00 142.60 ? 278 ASN C CB  1 
ATOM   9576  C  CG  . ASN C 2 271 ? 109.023 134.773 88.832  1.00 142.00 ? 278 ASN C CG  1 
ATOM   9577  O  OD1 . ASN C 2 271 ? 109.943 134.010 89.127  1.00 142.20 ? 278 ASN C OD1 1 
ATOM   9578  N  ND2 . ASN C 2 271 ? 109.166 136.093 88.813  1.00 141.16 ? 278 ASN C ND2 1 
ATOM   9579  N  N   . ILE C 2 272 ? 105.829 132.292 86.353  1.00 143.39 ? 279 ILE C N   1 
ATOM   9580  C  CA  . ILE C 2 272 ? 104.466 131.864 86.058  1.00 143.30 ? 279 ILE C CA  1 
ATOM   9581  C  C   . ILE C 2 272 ? 104.457 130.363 85.815  1.00 144.44 ? 279 ILE C C   1 
ATOM   9582  O  O   . ILE C 2 272 ? 105.300 129.837 85.078  1.00 144.93 ? 279 ILE C O   1 
ATOM   9583  C  CB  . ILE C 2 272 ? 103.902 132.621 84.844  1.00 143.66 ? 279 ILE C CB  1 
ATOM   9584  C  CG1 . ILE C 2 272 ? 104.181 134.118 84.971  1.00 142.53 ? 279 ILE C CG1 1 
ATOM   9585  C  CG2 . ILE C 2 272 ? 102.412 132.366 84.705  1.00 143.72 ? 279 ILE C CG2 1 
ATOM   9586  C  CD1 . ILE C 2 272 ? 103.575 134.747 86.200  1.00 144.20 ? 279 ILE C CD1 1 
ATOM   9587  N  N   . ALA C 2 273 ? 103.505 129.671 86.436  1.00 150.45 ? 280 ALA C N   1 
ATOM   9588  C  CA  . ALA C 2 273 ? 103.352 128.229 86.298  1.00 150.95 ? 280 ALA C CA  1 
ATOM   9589  C  C   . ALA C 2 273 ? 101.965 127.917 85.755  1.00 152.10 ? 280 ALA C C   1 
ATOM   9590  O  O   . ALA C 2 273 ? 100.968 128.468 86.234  1.00 152.15 ? 280 ALA C O   1 
ATOM   9591  C  CB  . ALA C 2 273 ? 103.569 127.519 87.637  1.00 149.27 ? 280 ALA C CB  1 
ATOM   9592  N  N   . ILE C 2 274 ? 101.910 127.036 84.760  1.00 154.63 ? 281 ILE C N   1 
ATOM   9593  C  CA  . ILE C 2 274 ? 100.667 126.606 84.128  1.00 153.99 ? 281 ILE C CA  1 
ATOM   9594  C  C   . ILE C 2 274 ? 100.514 125.115 84.383  1.00 153.23 ? 281 ILE C C   1 
ATOM   9595  O  O   . ILE C 2 274 ? 101.329 124.317 83.902  1.00 152.77 ? 281 ILE C O   1 
ATOM   9596  C  CB  . ILE C 2 274 ? 100.659 126.899 82.616  1.00 153.89 ? 281 ILE C CB  1 
ATOM   9597  C  CG1 . ILE C 2 274 ? 101.262 128.275 82.303  1.00 152.73 ? 281 ILE C CG1 1 
ATOM   9598  C  CG2 . ILE C 2 274 ? 99.261  126.742 82.036  1.00 152.96 ? 281 ILE C CG2 1 
ATOM   9599  C  CD1 . ILE C 2 274 ? 102.755 128.260 82.004  1.00 150.96 ? 281 ILE C CD1 1 
ATOM   9600  N  N   . VAL C 2 275 ? 99.482  124.731 85.134  1.00 157.32 ? 282 VAL C N   1 
ATOM   9601  C  CA  . VAL C 2 275 ? 99.240  123.320 85.419  1.00 158.60 ? 282 VAL C CA  1 
ATOM   9602  C  C   . VAL C 2 275 ? 97.777  123.015 85.142  1.00 158.88 ? 282 VAL C C   1 
ATOM   9603  O  O   . VAL C 2 275 ? 96.890  123.579 85.791  1.00 158.13 ? 282 VAL C O   1 
ATOM   9604  C  CB  . VAL C 2 275 ? 99.606  122.947 86.865  1.00 157.53 ? 282 VAL C CB  1 
ATOM   9605  C  CG1 . VAL C 2 275 ? 98.987  121.608 87.238  1.00 156.57 ? 282 VAL C CG1 1 
ATOM   9606  C  CG2 . VAL C 2 275 ? 101.117 122.901 87.031  1.00 157.01 ? 282 VAL C CG2 1 
ATOM   9607  N  N   . GLY C 2 276 ? 97.524  122.114 84.196  1.00 165.45 ? 283 GLY C N   1 
ATOM   9608  C  CA  . GLY C 2 276 ? 96.180  121.694 83.877  1.00 164.36 ? 283 GLY C CA  1 
ATOM   9609  C  C   . GLY C 2 276 ? 95.906  121.851 82.401  1.00 164.65 ? 283 GLY C C   1 
ATOM   9610  O  O   . GLY C 2 276 ? 96.827  121.920 81.580  1.00 164.51 ? 283 GLY C O   1 
ATOM   9611  N  N   . ASN C 2 277 ? 94.618  121.911 82.062  1.00 163.91 ? 284 ASN C N   1 
ATOM   9612  C  CA  . ASN C 2 277 ? 94.171  122.054 80.683  1.00 164.25 ? 284 ASN C CA  1 
ATOM   9613  C  C   . ASN C 2 277 ? 93.871  123.504 80.318  1.00 164.32 ? 284 ASN C C   1 
ATOM   9614  O  O   . ASN C 2 277 ? 92.991  123.767 79.492  1.00 163.63 ? 284 ASN C O   1 
ATOM   9615  C  CB  . ASN C 2 277 ? 92.946  121.176 80.430  1.00 163.43 ? 284 ASN C CB  1 
ATOM   9616  C  CG  . ASN C 2 277 ? 93.301  119.710 80.285  1.00 162.53 ? 284 ASN C CG  1 
ATOM   9617  O  OD1 . ASN C 2 277 ? 94.351  119.365 79.742  1.00 161.37 ? 284 ASN C OD1 1 
ATOM   9618  N  ND2 . ASN C 2 277 ? 92.426  118.837 80.770  1.00 162.62 ? 284 ASN C ND2 1 
ATOM   9619  N  N   . VAL C 2 278 ? 94.580  124.454 80.926  1.00 164.72 ? 285 VAL C N   1 
ATOM   9620  C  CA  . VAL C 2 278 ? 94.428  125.853 80.552  1.00 164.24 ? 285 VAL C CA  1 
ATOM   9621  C  C   . VAL C 2 278 ? 94.989  126.055 79.152  1.00 163.96 ? 285 VAL C C   1 
ATOM   9622  O  O   . VAL C 2 278 ? 96.098  125.602 78.839  1.00 162.87 ? 285 VAL C O   1 
ATOM   9623  C  CB  . VAL C 2 278 ? 95.128  126.767 81.569  1.00 163.80 ? 285 VAL C CB  1 
ATOM   9624  C  CG1 . VAL C 2 278 ? 94.930  128.223 81.197  1.00 162.85 ? 285 VAL C CG1 1 
ATOM   9625  C  CG2 . VAL C 2 278 ? 94.604  126.506 82.964  1.00 162.90 ? 285 VAL C CG2 1 
ATOM   9626  N  N   . ARG C 2 279 ? 94.225  126.731 78.301  1.00 161.63 ? 286 ARG C N   1 
ATOM   9627  C  CA  . ARG C 2 279 ? 94.621  126.950 76.920  1.00 161.27 ? 286 ARG C CA  1 
ATOM   9628  C  C   . ARG C 2 279 ? 94.556  128.433 76.589  1.00 160.87 ? 286 ARG C C   1 
ATOM   9629  O  O   . ARG C 2 279 ? 93.777  129.191 77.172  1.00 161.48 ? 286 ARG C O   1 
ATOM   9630  C  CB  . ARG C 2 279 ? 93.741  126.153 75.950  1.00 161.78 ? 286 ARG C CB  1 
ATOM   9631  C  CG  . ARG C 2 279 ? 93.823  124.645 76.135  1.00 161.38 ? 286 ARG C CG  1 
ATOM   9632  C  CD  . ARG C 2 279 ? 93.383  123.912 74.881  1.00 160.58 ? 286 ARG C CD  1 
ATOM   9633  N  NE  . ARG C 2 279 ? 94.183  124.298 73.723  1.00 161.31 ? 286 ARG C NE  1 
ATOM   9634  C  CZ  . ARG C 2 279 ? 93.766  125.111 72.762  1.00 161.17 ? 286 ARG C CZ  1 
ATOM   9635  N  NH1 . ARG C 2 279 ? 92.554  125.639 72.780  1.00 161.06 ? 286 ARG C NH1 1 
ATOM   9636  N  NH2 . ARG C 2 279 ? 94.589  125.405 71.760  1.00 160.34 ? 286 ARG C NH2 1 
ATOM   9637  N  N   . LEU C 2 280 ? 95.393  128.838 75.639  1.00 159.78 ? 287 LEU C N   1 
ATOM   9638  C  CA  . LEU C 2 280 ? 95.497  130.224 75.206  1.00 160.50 ? 287 LEU C CA  1 
ATOM   9639  C  C   . LEU C 2 280 ? 95.069  130.326 73.750  1.00 162.16 ? 287 LEU C C   1 
ATOM   9640  O  O   . LEU C 2 280 ? 95.491  129.516 72.918  1.00 161.88 ? 287 LEU C O   1 
ATOM   9641  C  CB  . LEU C 2 280 ? 96.927  130.745 75.381  1.00 160.37 ? 287 LEU C CB  1 
ATOM   9642  C  CG  . LEU C 2 280 ? 97.329  131.965 74.551  1.00 160.56 ? 287 LEU C CG  1 
ATOM   9643  C  CD1 . LEU C 2 280 ? 96.539  133.195 74.973  1.00 159.96 ? 287 LEU C CD1 1 
ATOM   9644  C  CD2 . LEU C 2 280 ? 98.825  132.217 74.654  1.00 160.21 ? 287 LEU C CD2 1 
ATOM   9645  N  N   . VAL C 2 281 ? 94.229  131.318 73.447  1.00 167.32 ? 288 VAL C N   1 
ATOM   9646  C  CA  . VAL C 2 281 ? 93.788  131.524 72.074  1.00 167.14 ? 288 VAL C CA  1 
ATOM   9647  C  C   . VAL C 2 281 ? 94.970  131.954 71.212  1.00 166.88 ? 288 VAL C C   1 
ATOM   9648  O  O   . VAL C 2 281 ? 95.930  132.575 71.689  1.00 166.36 ? 288 VAL C O   1 
ATOM   9649  C  CB  . VAL C 2 281 ? 92.643  132.554 72.012  1.00 165.77 ? 288 VAL C CB  1 
ATOM   9650  C  CG1 . VAL C 2 281 ? 91.638  132.295 73.117  1.00 164.82 ? 288 VAL C CG1 1 
ATOM   9651  C  CG2 . VAL C 2 281 ? 93.182  133.975 72.106  1.00 165.33 ? 288 VAL C CG2 1 
ATOM   9652  N  N   . GLY C 2 282 ? 94.911  131.601 69.933  1.00 162.33 ? 289 GLY C N   1 
ATOM   9653  C  CA  . GLY C 2 282 ? 95.969  131.938 69.000  1.00 161.13 ? 289 GLY C CA  1 
ATOM   9654  C  C   . GLY C 2 282 ? 97.274  131.210 69.263  1.00 161.10 ? 289 GLY C C   1 
ATOM   9655  O  O   . GLY C 2 282 ? 97.408  130.481 70.246  1.00 160.54 ? 289 GLY C O   1 
ATOM   9656  N  N   . ALA D 2 106 ? 139.902 121.663 200.592 1.00 178.28 ? 83  ALA D N   1 
ATOM   9657  C  CA  . ALA D 2 106 ? 140.294 122.752 199.706 1.00 178.62 ? 83  ALA D CA  1 
ATOM   9658  C  C   . ALA D 2 106 ? 141.276 122.268 198.646 1.00 179.81 ? 83  ALA D C   1 
ATOM   9659  O  O   . ALA D 2 106 ? 142.220 121.538 198.946 1.00 179.20 ? 83  ALA D O   1 
ATOM   9660  C  CB  . ALA D 2 106 ? 140.898 123.895 200.507 1.00 177.72 ? 83  ALA D CB  1 
ATOM   9661  N  N   . GLY D 2 107 ? 141.044 122.675 197.406 1.00 186.75 ? 84  GLY D N   1 
ATOM   9662  C  CA  . GLY D 2 107 ? 141.900 122.322 196.291 1.00 186.57 ? 84  GLY D CA  1 
ATOM   9663  C  C   . GLY D 2 107 ? 142.984 123.349 196.049 1.00 186.64 ? 84  GLY D C   1 
ATOM   9664  O  O   . GLY D 2 107 ? 143.441 124.037 196.967 1.00 186.18 ? 84  GLY D O   1 
ATOM   9665  N  N   . THR D 2 108 ? 143.400 123.457 194.788 1.00 186.14 ? 85  THR D N   1 
ATOM   9666  C  CA  . THR D 2 108 ? 144.425 124.424 194.416 1.00 186.01 ? 85  THR D CA  1 
ATOM   9667  C  C   . THR D 2 108 ? 143.852 125.834 194.463 1.00 186.46 ? 85  THR D C   1 
ATOM   9668  O  O   . THR D 2 108 ? 143.278 126.315 193.481 1.00 186.04 ? 85  THR D O   1 
ATOM   9669  C  CB  . THR D 2 108 ? 144.980 124.119 193.024 1.00 184.60 ? 85  THR D CB  1 
ATOM   9670  O  OG1 . THR D 2 108 ? 145.345 122.735 192.947 1.00 183.02 ? 85  THR D OG1 1 
ATOM   9671  C  CG2 . THR D 2 108 ? 146.205 124.972 192.750 1.00 184.85 ? 85  THR D CG2 1 
ATOM   9672  N  N   . THR D 2 109 ? 144.007 126.502 195.602 1.00 190.64 ? 86  THR D N   1 
ATOM   9673  C  CA  . THR D 2 109 ? 143.406 127.811 195.810 1.00 190.97 ? 86  THR D CA  1 
ATOM   9674  C  C   . THR D 2 109 ? 144.166 128.889 195.045 1.00 190.72 ? 86  THR D C   1 
ATOM   9675  O  O   . THR D 2 109 ? 145.398 128.868 194.962 1.00 189.81 ? 86  THR D O   1 
ATOM   9676  C  CB  . THR D 2 109 ? 143.373 128.145 197.303 1.00 190.18 ? 86  THR D CB  1 
ATOM   9677  O  OG1 . THR D 2 109 ? 142.668 127.114 198.006 1.00 189.52 ? 86  THR D OG1 1 
ATOM   9678  C  CG2 . THR D 2 109 ? 142.674 129.477 197.549 1.00 189.55 ? 86  THR D CG2 1 
ATOM   9679  N  N   . TYR D 2 110 ? 143.416 129.826 194.474 1.00 188.54 ? 87  TYR D N   1 
ATOM   9680  C  CA  . TYR D 2 110 ? 143.959 131.004 193.816 1.00 187.89 ? 87  TYR D CA  1 
ATOM   9681  C  C   . TYR D 2 110 ? 143.403 132.252 194.486 1.00 187.79 ? 87  TYR D C   1 
ATOM   9682  O  O   . TYR D 2 110 ? 142.268 132.254 194.974 1.00 186.76 ? 87  TYR D O   1 
ATOM   9683  C  CB  . TYR D 2 110 ? 143.625 131.013 192.322 1.00 187.12 ? 87  TYR D CB  1 
ATOM   9684  C  CG  . TYR D 2 110 ? 144.661 130.323 191.468 1.00 187.19 ? 87  TYR D CG  1 
ATOM   9685  C  CD1 . TYR D 2 110 ? 145.046 129.016 191.731 1.00 186.88 ? 87  TYR D CD1 1 
ATOM   9686  C  CD2 . TYR D 2 110 ? 145.258 130.980 190.402 1.00 187.21 ? 87  TYR D CD2 1 
ATOM   9687  C  CE1 . TYR D 2 110 ? 145.993 128.382 190.953 1.00 187.29 ? 87  TYR D CE1 1 
ATOM   9688  C  CE2 . TYR D 2 110 ? 146.208 130.353 189.619 1.00 187.54 ? 87  TYR D CE2 1 
ATOM   9689  C  CZ  . TYR D 2 110 ? 146.572 129.055 189.900 1.00 187.61 ? 87  TYR D CZ  1 
ATOM   9690  O  OH  . TYR D 2 110 ? 147.516 128.426 189.124 1.00 187.19 ? 87  TYR D OH  1 
ATOM   9691  N  N   . ILE D 2 111 ? 144.211 133.308 194.514 1.00 189.84 ? 88  ILE D N   1 
ATOM   9692  C  CA  . ILE D 2 111 ? 143.866 134.561 195.176 1.00 189.81 ? 88  ILE D CA  1 
ATOM   9693  C  C   . ILE D 2 111 ? 143.859 135.678 194.141 1.00 188.69 ? 88  ILE D C   1 
ATOM   9694  O  O   . ILE D 2 111 ? 144.793 135.799 193.339 1.00 188.52 ? 88  ILE D O   1 
ATOM   9695  C  CB  . ILE D 2 111 ? 144.839 134.875 196.326 1.00 189.59 ? 88  ILE D CB  1 
ATOM   9696  C  CG1 . ILE D 2 111 ? 146.289 134.702 195.870 1.00 188.47 ? 88  ILE D CG1 1 
ATOM   9697  C  CG2 . ILE D 2 111 ? 144.549 133.991 197.524 1.00 188.67 ? 88  ILE D CG2 1 
ATOM   9698  C  CD1 . ILE D 2 111 ? 147.301 134.892 196.977 1.00 187.73 ? 88  ILE D CD1 1 
ATOM   9699  N  N   . PHE D 2 112 ? 142.802 136.484 194.153 1.00 185.37 ? 89  PHE D N   1 
ATOM   9700  C  CA  . PHE D 2 112 ? 142.680 137.632 193.266 1.00 186.01 ? 89  PHE D CA  1 
ATOM   9701  C  C   . PHE D 2 112 ? 142.990 138.899 194.049 1.00 185.90 ? 89  PHE D C   1 
ATOM   9702  O  O   . PHE D 2 112 ? 142.350 139.176 195.068 1.00 185.74 ? 89  PHE D O   1 
ATOM   9703  C  CB  . PHE D 2 112 ? 141.279 137.706 192.659 1.00 186.36 ? 89  PHE D CB  1 
ATOM   9704  C  CG  . PHE D 2 112 ? 141.091 136.811 191.468 1.00 186.54 ? 89  PHE D CG  1 
ATOM   9705  C  CD1 . PHE D 2 112 ? 140.871 135.455 191.634 1.00 186.04 ? 89  PHE D CD1 1 
ATOM   9706  C  CD2 . PHE D 2 112 ? 141.140 137.326 190.183 1.00 185.69 ? 89  PHE D CD2 1 
ATOM   9707  C  CE1 . PHE D 2 112 ? 140.703 134.628 190.544 1.00 186.08 ? 89  PHE D CE1 1 
ATOM   9708  C  CE2 . PHE D 2 112 ? 140.972 136.505 189.088 1.00 185.54 ? 89  PHE D CE2 1 
ATOM   9709  C  CZ  . PHE D 2 112 ? 140.753 135.154 189.267 1.00 186.46 ? 89  PHE D CZ  1 
ATOM   9710  N  N   . SER D 2 113 ? 143.965 139.664 193.570 1.00 187.14 ? 90  SER D N   1 
ATOM   9711  C  CA  . SER D 2 113 ? 144.477 140.820 194.284 1.00 187.20 ? 90  SER D CA  1 
ATOM   9712  C  C   . SER D 2 113 ? 143.780 142.092 193.801 1.00 187.81 ? 90  SER D C   1 
ATOM   9713  O  O   . SER D 2 113 ? 142.796 142.046 193.056 1.00 187.45 ? 90  SER D O   1 
ATOM   9714  C  CB  . SER D 2 113 ? 145.996 140.905 194.117 1.00 186.40 ? 90  SER D CB  1 
ATOM   9715  O  OG  . SER D 2 113 ? 146.585 141.660 195.161 1.00 184.87 ? 90  SER D OG  1 
ATOM   9716  N  N   . LYS D 2 114 ? 144.293 143.240 194.241 1.00 188.31 ? 91  LYS D N   1 
ATOM   9717  C  CA  . LYS D 2 114 ? 143.716 144.527 193.874 1.00 187.31 ? 91  LYS D CA  1 
ATOM   9718  C  C   . LYS D 2 114 ? 143.716 144.708 192.362 1.00 187.07 ? 91  LYS D C   1 
ATOM   9719  O  O   . LYS D 2 114 ? 144.688 144.376 191.678 1.00 187.27 ? 91  LYS D O   1 
ATOM   9720  C  CB  . LYS D 2 114 ? 144.501 145.659 194.537 1.00 186.61 ? 91  LYS D CB  1 
ATOM   9721  C  CG  . LYS D 2 114 ? 146.004 145.424 194.557 1.00 186.44 ? 91  LYS D CG  1 
ATOM   9722  C  CD  . LYS D 2 114 ? 146.756 146.625 195.095 1.00 185.80 ? 91  LYS D CD  1 
ATOM   9723  C  CE  . LYS D 2 114 ? 148.228 146.304 195.290 1.00 185.44 ? 91  LYS D CE  1 
ATOM   9724  N  NZ  . LYS D 2 114 ? 148.900 145.946 194.011 1.00 185.30 ? 91  LYS D NZ  1 
ATOM   9725  N  N   . GLY D 2 115 ? 142.611 145.235 191.841 1.00 185.13 ? 92  GLY D N   1 
ATOM   9726  C  CA  . GLY D 2 115 ? 142.456 145.399 190.410 1.00 185.15 ? 92  GLY D CA  1 
ATOM   9727  C  C   . GLY D 2 115 ? 141.969 144.131 189.740 1.00 185.54 ? 92  GLY D C   1 
ATOM   9728  O  O   . GLY D 2 115 ? 141.295 144.180 188.707 1.00 184.81 ? 92  GLY D O   1 
ATOM   9729  N  N   . GLY D 2 116 ? 142.306 142.988 190.327 1.00 186.97 ? 93  GLY D N   1 
ATOM   9730  C  CA  . GLY D 2 116 ? 141.876 141.715 189.803 1.00 186.73 ? 93  GLY D CA  1 
ATOM   9731  C  C   . GLY D 2 116 ? 142.690 141.259 188.607 1.00 186.72 ? 93  GLY D C   1 
ATOM   9732  O  O   . GLY D 2 116 ? 143.776 141.761 188.303 1.00 185.83 ? 93  GLY D O   1 
ATOM   9733  N  N   . GLY D 2 117 ? 142.131 140.273 187.919 1.00 187.09 ? 94  GLY D N   1 
ATOM   9734  C  CA  . GLY D 2 117 ? 142.766 139.703 186.747 1.00 186.68 ? 94  GLY D CA  1 
ATOM   9735  C  C   . GLY D 2 117 ? 141.842 138.682 186.125 1.00 186.93 ? 94  GLY D C   1 
ATOM   9736  O  O   . GLY D 2 117 ? 140.732 138.438 186.609 1.00 186.87 ? 94  GLY D O   1 
ATOM   9737  N  N   . GLN D 2 118 ? 142.313 138.085 185.034 1.00 182.30 ? 95  GLN D N   1 
ATOM   9738  C  CA  . GLN D 2 118 ? 141.522 137.093 184.322 1.00 181.70 ? 95  GLN D CA  1 
ATOM   9739  C  C   . GLN D 2 118 ? 142.391 135.910 183.929 1.00 181.14 ? 95  GLN D C   1 
ATOM   9740  O  O   . GLN D 2 118 ? 143.500 136.085 183.413 1.00 180.65 ? 95  GLN D O   1 
ATOM   9741  C  CB  . GLN D 2 118 ? 140.860 137.697 183.080 1.00 181.13 ? 95  GLN D CB  1 
ATOM   9742  C  CG  . GLN D 2 118 ? 139.607 138.496 183.389 1.00 180.67 ? 95  GLN D CG  1 
ATOM   9743  C  CD  . GLN D 2 118 ? 138.818 138.846 182.147 1.00 181.12 ? 95  GLN D CD  1 
ATOM   9744  O  OE1 . GLN D 2 118 ? 137.790 139.519 182.218 1.00 180.58 ? 95  GLN D OE1 1 
ATOM   9745  N  NE2 . GLN D 2 118 ? 139.292 138.383 180.996 1.00 181.40 ? 95  GLN D NE2 1 
ATOM   9746  N  N   . ILE D 2 119 ? 141.873 134.711 184.167 1.00 175.10 ? 96  ILE D N   1 
ATOM   9747  C  CA  . ILE D 2 119 ? 142.526 133.473 183.769 1.00 174.62 ? 96  ILE D CA  1 
ATOM   9748  C  C   . ILE D 2 119 ? 141.599 132.753 182.793 1.00 175.81 ? 96  ILE D C   1 
ATOM   9749  O  O   . ILE D 2 119 ? 140.382 132.670 183.017 1.00 174.58 ? 96  ILE D O   1 
ATOM   9750  C  CB  . ILE D 2 119 ? 142.903 132.613 184.993 1.00 174.49 ? 96  ILE D CB  1 
ATOM   9751  C  CG1 . ILE D 2 119 ? 144.038 131.646 184.653 1.00 175.17 ? 96  ILE D CG1 1 
ATOM   9752  C  CG2 . ILE D 2 119 ? 141.711 131.892 185.575 1.00 174.13 ? 96  ILE D CG2 1 
ATOM   9753  C  CD1 . ILE D 2 119 ? 144.424 130.730 185.796 1.00 174.87 ? 96  ILE D CD1 1 
ATOM   9754  N  N   . THR D 2 120 ? 142.170 132.288 181.684 1.00 169.67 ? 97  THR D N   1 
ATOM   9755  C  CA  . THR D 2 120 ? 141.415 131.918 180.496 1.00 168.39 ? 97  THR D CA  1 
ATOM   9756  C  C   . THR D 2 120 ? 141.841 130.537 180.030 1.00 167.35 ? 97  THR D C   1 
ATOM   9757  O  O   . THR D 2 120 ? 143.034 130.298 179.814 1.00 166.37 ? 97  THR D O   1 
ATOM   9758  C  CB  . THR D 2 120 ? 141.661 132.921 179.364 1.00 166.94 ? 97  THR D CB  1 
ATOM   9759  O  OG1 . THR D 2 120 ? 141.145 134.204 179.730 1.00 166.75 ? 97  THR D OG1 1 
ATOM   9760  C  CG2 . THR D 2 120 ? 140.987 132.455 178.084 1.00 166.49 ? 97  THR D CG2 1 
ATOM   9761  N  N   . TYR D 2 121 ? 140.877 129.639 179.845 1.00 157.23 ? 98  TYR D N   1 
ATOM   9762  C  CA  . TYR D 2 121 ? 141.154 128.361 179.200 1.00 156.45 ? 98  TYR D CA  1 
ATOM   9763  C  C   . TYR D 2 121 ? 140.357 128.286 177.907 1.00 156.06 ? 98  TYR D C   1 
ATOM   9764  O  O   . TYR D 2 121 ? 139.124 128.363 177.927 1.00 156.80 ? 98  TYR D O   1 
ATOM   9765  C  CB  . TYR D 2 121 ? 140.829 127.179 180.111 1.00 155.60 ? 98  TYR D CB  1 
ATOM   9766  C  CG  . TYR D 2 121 ? 140.753 125.857 179.380 1.00 155.11 ? 98  TYR D CG  1 
ATOM   9767  C  CD1 . TYR D 2 121 ? 141.893 125.269 178.851 1.00 155.84 ? 98  TYR D CD1 1 
ATOM   9768  C  CD2 . TYR D 2 121 ? 139.545 125.192 179.226 1.00 154.17 ? 98  TYR D CD2 1 
ATOM   9769  C  CE1 . TYR D 2 121 ? 141.833 124.063 178.185 1.00 155.26 ? 98  TYR D CE1 1 
ATOM   9770  C  CE2 . TYR D 2 121 ? 139.477 123.984 178.562 1.00 154.50 ? 98  TYR D CE2 1 
ATOM   9771  C  CZ  . TYR D 2 121 ? 140.624 123.425 178.045 1.00 154.31 ? 98  TYR D CZ  1 
ATOM   9772  O  OH  . TYR D 2 121 ? 140.565 122.223 177.382 1.00 154.67 ? 98  TYR D OH  1 
ATOM   9773  N  N   . LYS D 2 122 ? 141.061 128.130 176.792 1.00 148.29 ? 99  LYS D N   1 
ATOM   9774  C  CA  . LYS D 2 122 ? 140.464 128.153 175.466 1.00 147.93 ? 99  LYS D CA  1 
ATOM   9775  C  C   . LYS D 2 122 ? 140.560 126.769 174.844 1.00 149.12 ? 99  LYS D C   1 
ATOM   9776  O  O   . LYS D 2 122 ? 141.652 126.200 174.751 1.00 150.30 ? 99  LYS D O   1 
ATOM   9777  C  CB  . LYS D 2 122 ? 141.161 129.185 174.577 1.00 147.20 ? 99  LYS D CB  1 
ATOM   9778  C  CG  . LYS D 2 122 ? 140.620 129.265 173.163 1.00 147.70 ? 99  LYS D CG  1 
ATOM   9779  C  CD  . LYS D 2 122 ? 141.153 130.495 172.446 1.00 148.53 ? 99  LYS D CD  1 
ATOM   9780  C  CE  . LYS D 2 122 ? 140.562 130.623 171.051 1.00 148.88 ? 99  LYS D CE  1 
ATOM   9781  N  NZ  . LYS D 2 122 ? 140.707 132.004 170.514 1.00 148.35 ? 99  LYS D NZ  1 
ATOM   9782  N  N   . TRP D 2 123 ? 139.418 126.231 174.428 1.00 138.86 ? 100 TRP D N   1 
ATOM   9783  C  CA  . TRP D 2 123 ? 139.410 124.950 173.749 1.00 137.55 ? 100 TRP D CA  1 
ATOM   9784  C  C   . TRP D 2 123 ? 140.062 125.087 172.375 1.00 138.59 ? 100 TRP D C   1 
ATOM   9785  O  O   . TRP D 2 123 ? 140.001 126.151 171.755 1.00 137.29 ? 100 TRP D O   1 
ATOM   9786  C  CB  . TRP D 2 123 ? 137.984 124.435 173.589 1.00 137.23 ? 100 TRP D CB  1 
ATOM   9787  C  CG  . TRP D 2 123 ? 137.433 123.743 174.796 1.00 137.74 ? 100 TRP D CG  1 
ATOM   9788  C  CD1 . TRP D 2 123 ? 137.694 122.469 175.198 1.00 138.11 ? 100 TRP D CD1 1 
ATOM   9789  C  CD2 . TRP D 2 123 ? 136.501 124.279 175.742 1.00 136.93 ? 100 TRP D CD2 1 
ATOM   9790  N  NE1 . TRP D 2 123 ? 136.993 122.181 176.342 1.00 137.93 ? 100 TRP D NE1 1 
ATOM   9791  C  CE2 . TRP D 2 123 ? 136.253 123.277 176.697 1.00 136.86 ? 100 TRP D CE2 1 
ATOM   9792  C  CE3 . TRP D 2 123 ? 135.858 125.512 175.877 1.00 136.31 ? 100 TRP D CE3 1 
ATOM   9793  C  CZ2 . TRP D 2 123 ? 135.390 123.467 177.770 1.00 136.94 ? 100 TRP D CZ2 1 
ATOM   9794  C  CZ3 . TRP D 2 123 ? 135.003 125.699 176.945 1.00 136.03 ? 100 TRP D CZ3 1 
ATOM   9795  C  CH2 . TRP D 2 123 ? 134.776 124.683 177.877 1.00 136.61 ? 100 TRP D CH2 1 
ATOM   9796  N  N   . PRO D 2 124 ? 140.705 124.029 171.885 1.00 146.24 ? 101 PRO D N   1 
ATOM   9797  C  CA  . PRO D 2 124 ? 141.219 124.066 170.520 1.00 147.92 ? 101 PRO D CA  1 
ATOM   9798  C  C   . PRO D 2 124 ? 140.084 124.239 169.533 1.00 147.71 ? 101 PRO D C   1 
ATOM   9799  O  O   . PRO D 2 124 ? 138.961 123.751 169.759 1.00 146.99 ? 101 PRO D O   1 
ATOM   9800  C  CB  . PRO D 2 124 ? 141.908 122.702 170.363 1.00 145.13 ? 101 PRO D CB  1 
ATOM   9801  C  CG  . PRO D 2 124 ? 141.380 121.854 171.467 1.00 143.38 ? 101 PRO D CG  1 
ATOM   9802  C  CD  . PRO D 2 124 ? 141.040 122.778 172.582 1.00 143.72 ? 101 PRO D CD  1 
ATOM   9803  N  N   . PRO D 2 125 ? 140.328 124.935 168.420 1.00 142.63 ? 102 PRO D N   1 
ATOM   9804  C  CA  . PRO D 2 125 ? 139.224 125.265 167.503 1.00 141.05 ? 102 PRO D CA  1 
ATOM   9805  C  C   . PRO D 2 125 ? 138.524 124.053 166.918 1.00 141.05 ? 102 PRO D C   1 
ATOM   9806  O  O   . PRO D 2 125 ? 137.396 124.187 166.428 1.00 141.39 ? 102 PRO D O   1 
ATOM   9807  C  CB  . PRO D 2 125 ? 139.913 126.093 166.410 1.00 141.19 ? 102 PRO D CB  1 
ATOM   9808  C  CG  . PRO D 2 125 ? 141.148 126.625 167.060 1.00 140.68 ? 102 PRO D CG  1 
ATOM   9809  C  CD  . PRO D 2 125 ? 141.597 125.548 167.998 1.00 140.58 ? 102 PRO D CD  1 
ATOM   9810  N  N   . ASN D 2 126 ? 139.150 122.879 166.944 1.00 141.72 ? 103 ASN D N   1 
ATOM   9811  C  CA  . ASN D 2 126 ? 138.521 121.671 166.430 1.00 142.82 ? 103 ASN D CA  1 
ATOM   9812  C  C   . ASN D 2 126 ? 137.777 120.888 167.506 1.00 143.16 ? 103 ASN D C   1 
ATOM   9813  O  O   . ASN D 2 126 ? 136.871 120.114 167.176 1.00 143.04 ? 103 ASN D O   1 
ATOM   9814  C  CB  . ASN D 2 126 ? 139.583 120.789 165.756 1.00 142.50 ? 103 ASN D CB  1 
ATOM   9815  C  CG  . ASN D 2 126 ? 139.220 119.316 165.756 1.00 143.28 ? 103 ASN D CG  1 
ATOM   9816  O  OD1 . ASN D 2 126 ? 139.479 118.600 166.722 1.00 143.12 ? 103 ASN D OD1 1 
ATOM   9817  N  ND2 . ASN D 2 126 ? 138.614 118.858 164.667 1.00 142.24 ? 103 ASN D ND2 1 
ATOM   9818  N  N   . ASP D 2 127 ? 138.106 121.098 168.778 1.00 141.28 ? 104 ASP D N   1 
ATOM   9819  C  CA  . ASP D 2 127 ? 137.555 120.318 169.881 1.00 141.21 ? 104 ASP D CA  1 
ATOM   9820  C  C   . ASP D 2 127 ? 136.686 121.159 170.812 1.00 139.95 ? 104 ASP D C   1 
ATOM   9821  O  O   . ASP D 2 127 ? 136.779 121.047 172.035 1.00 139.21 ? 104 ASP D O   1 
ATOM   9822  C  CB  . ASP D 2 127 ? 138.674 119.647 170.674 1.00 141.96 ? 104 ASP D CB  1 
ATOM   9823  C  CG  . ASP D 2 127 ? 139.163 118.370 170.025 1.00 141.70 ? 104 ASP D CG  1 
ATOM   9824  O  OD1 . ASP D 2 127 ? 138.419 117.797 169.202 1.00 141.32 ? 104 ASP D OD1 1 
ATOM   9825  O  OD2 . ASP D 2 127 ? 140.296 117.942 170.331 1.00 141.18 ? 104 ASP D OD2 1 
ATOM   9826  N  N   . ARG D 2 128 ? 135.839 122.016 170.251 1.00 130.43 ? 105 ARG D N   1 
ATOM   9827  C  CA  . ARG D 2 128 ? 134.908 122.791 171.065 1.00 129.25 ? 105 ARG D CA  1 
ATOM   9828  C  C   . ARG D 2 128 ? 133.745 121.906 171.497 1.00 128.63 ? 105 ARG D C   1 
ATOM   9829  O  O   . ARG D 2 128 ? 133.051 121.353 170.637 1.00 129.84 ? 105 ARG D O   1 
ATOM   9830  C  CB  . ARG D 2 128 ? 134.389 123.993 170.288 1.00 128.51 ? 105 ARG D CB  1 
ATOM   9831  C  CG  . ARG D 2 128 ? 135.473 124.889 169.715 1.00 127.52 ? 105 ARG D CG  1 
ATOM   9832  C  CD  . ARG D 2 128 ? 134.858 126.097 169.029 1.00 129.19 ? 105 ARG D CD  1 
ATOM   9833  N  NE  . ARG D 2 128 ? 135.838 126.873 168.280 1.00 130.84 ? 105 ARG D NE  1 
ATOM   9834  C  CZ  . ARG D 2 128 ? 135.947 126.863 166.959 1.00 131.46 ? 105 ARG D CZ  1 
ATOM   9835  N  NH1 . ARG D 2 128 ? 135.154 126.119 166.205 1.00 127.71 ? 105 ARG D NH1 1 
ATOM   9836  N  NH2 . ARG D 2 128 ? 136.877 127.617 166.378 1.00 131.29 ? 105 ARG D NH2 1 
ATOM   9837  N  N   . PRO D 2 129 ? 133.500 121.738 172.796 1.00 121.07 ? 106 PRO D N   1 
ATOM   9838  C  CA  . PRO D 2 129 ? 132.422 120.841 173.233 1.00 119.82 ? 106 PRO D CA  1 
ATOM   9839  C  C   . PRO D 2 129 ? 131.067 121.526 173.311 1.00 119.99 ? 106 PRO D C   1 
ATOM   9840  O  O   . PRO D 2 129 ? 130.924 122.631 173.836 1.00 120.53 ? 106 PRO D O   1 
ATOM   9841  C  CB  . PRO D 2 129 ? 132.860 120.401 174.638 1.00 118.76 ? 106 PRO D CB  1 
ATOM   9842  C  CG  . PRO D 2 129 ? 133.989 121.254 175.021 1.00 123.43 ? 106 PRO D CG  1 
ATOM   9843  C  CD  . PRO D 2 129 ? 134.480 122.028 173.854 1.00 124.53 ? 106 PRO D CD  1 
ATOM   9844  N  N   . SER D 2 130 ? 130.059 120.838 172.781 1.00 109.75 ? 107 SER D N   1 
ATOM   9845  C  CA  . SER D 2 130 ? 128.660 121.173 173.000 1.00 105.26 ? 107 SER D CA  1 
ATOM   9846  C  C   . SER D 2 130 ? 128.062 120.115 173.912 1.00 107.62 ? 107 SER D C   1 
ATOM   9847  O  O   . SER D 2 130 ? 128.345 118.924 173.755 1.00 113.90 ? 107 SER D O   1 
ATOM   9848  C  CB  . SER D 2 130 ? 127.887 121.236 171.683 1.00 102.13 ? 107 SER D CB  1 
ATOM   9849  O  OG  . SER D 2 130 ? 128.665 121.842 170.668 1.00 109.06 ? 107 SER D OG  1 
ATOM   9850  N  N   . THR D 2 131 ? 127.258 120.543 174.880 1.00 109.39 ? 108 THR D N   1 
ATOM   9851  C  CA  . THR D 2 131 ? 126.797 119.633 175.918 1.00 110.84 ? 108 THR D CA  1 
ATOM   9852  C  C   . THR D 2 131 ? 125.371 119.960 176.336 1.00 109.33 ? 108 THR D C   1 
ATOM   9853  O  O   . THR D 2 131 ? 125.014 121.127 176.507 1.00 109.28 ? 108 THR D O   1 
ATOM   9854  C  CB  . THR D 2 131 ? 127.734 119.678 177.132 1.00 113.03 ? 108 THR D CB  1 
ATOM   9855  O  OG1 . THR D 2 131 ? 127.152 118.951 178.221 1.00 114.64 ? 108 THR D OG1 1 
ATOM   9856  C  CG2 . THR D 2 131 ? 128.017 121.110 177.549 1.00 112.14 ? 108 THR D CG2 1 
ATOM   9857  N  N   . ARG D 2 132 ? 124.561 118.912 176.493 1.00 108.26 ? 109 ARG D N   1 
ATOM   9858  C  CA  . ARG D 2 132 ? 123.176 119.097 176.907 1.00 108.33 ? 109 ARG D CA  1 
ATOM   9859  C  C   . ARG D 2 132 ? 123.078 119.427 178.389 1.00 113.22 ? 109 ARG D C   1 
ATOM   9860  O  O   . ARG D 2 132 ? 122.252 120.253 178.793 1.00 112.53 ? 109 ARG D O   1 
ATOM   9861  C  CB  . ARG D 2 132 ? 122.362 117.845 176.591 1.00 107.82 ? 109 ARG D CB  1 
ATOM   9862  C  CG  . ARG D 2 132 ? 120.884 118.102 176.382 1.00 108.74 ? 109 ARG D CG  1 
ATOM   9863  C  CD  . ARG D 2 132 ? 120.203 116.894 175.770 1.00 111.83 ? 109 ARG D CD  1 
ATOM   9864  N  NE  . ARG D 2 132 ? 119.301 117.269 174.689 1.00 112.99 ? 109 ARG D NE  1 
ATOM   9865  C  CZ  . ARG D 2 132 ? 119.527 117.022 173.407 1.00 109.29 ? 109 ARG D CZ  1 
ATOM   9866  N  NH1 . ARG D 2 132 ? 120.621 116.397 173.006 1.00 107.92 ? 109 ARG D NH1 1 
ATOM   9867  N  NH2 . ARG D 2 132 ? 118.634 117.412 172.503 1.00 109.63 ? 109 ARG D NH2 1 
ATOM   9868  N  N   . ALA D 2 133 ? 123.903 118.788 179.213 1.00 128.02 ? 110 ALA D N   1 
ATOM   9869  C  CA  . ALA D 2 133 ? 123.874 118.961 180.660 1.00 125.61 ? 110 ALA D CA  1 
ATOM   9870  C  C   . ALA D 2 133 ? 125.170 119.619 181.110 1.00 125.99 ? 110 ALA D C   1 
ATOM   9871  O  O   . ALA D 2 133 ? 126.260 119.114 180.820 1.00 125.58 ? 110 ALA D O   1 
ATOM   9872  C  CB  . ALA D 2 133 ? 123.675 117.621 181.366 1.00 123.07 ? 110 ALA D CB  1 
ATOM   9873  N  N   . ASP D 2 134 ? 125.050 120.732 181.825 1.00 140.37 ? 111 ASP D N   1 
ATOM   9874  C  CA  . ASP D 2 134 ? 126.196 121.482 182.319 1.00 141.10 ? 111 ASP D CA  1 
ATOM   9875  C  C   . ASP D 2 134 ? 126.302 121.309 183.826 1.00 141.26 ? 111 ASP D C   1 
ATOM   9876  O  O   . ASP D 2 134 ? 125.296 121.397 184.539 1.00 139.14 ? 111 ASP D O   1 
ATOM   9877  C  CB  . ASP D 2 134 ? 126.075 122.967 181.967 1.00 141.76 ? 111 ASP D CB  1 
ATOM   9878  C  CG  . ASP D 2 134 ? 125.687 123.194 180.522 1.00 141.25 ? 111 ASP D CG  1 
ATOM   9879  O  OD1 . ASP D 2 134 ? 126.078 122.374 179.669 1.00 141.62 ? 111 ASP D OD1 1 
ATOM   9880  O  OD2 . ASP D 2 134 ? 124.996 124.193 180.238 1.00 141.29 ? 111 ASP D OD2 1 
ATOM   9881  N  N   . ARG D 2 135 ? 127.517 121.059 184.306 1.00 152.89 ? 112 ARG D N   1 
ATOM   9882  C  CA  . ARG D 2 135 ? 127.789 120.911 185.728 1.00 152.72 ? 112 ARG D CA  1 
ATOM   9883  C  C   . ARG D 2 135 ? 128.886 121.884 186.131 1.00 152.37 ? 112 ARG D C   1 
ATOM   9884  O  O   . ARG D 2 135 ? 129.931 121.955 185.477 1.00 150.38 ? 112 ARG D O   1 
ATOM   9885  C  CB  . ARG D 2 135 ? 128.200 119.478 186.066 1.00 152.41 ? 112 ARG D CB  1 
ATOM   9886  C  CG  . ARG D 2 135 ? 127.032 118.558 186.374 1.00 151.71 ? 112 ARG D CG  1 
ATOM   9887  C  CD  . ARG D 2 135 ? 126.570 117.821 185.130 1.00 151.62 ? 112 ARG D CD  1 
ATOM   9888  N  NE  . ARG D 2 135 ? 127.650 117.059 184.514 1.00 153.42 ? 112 ARG D NE  1 
ATOM   9889  C  CZ  . ARG D 2 135 ? 128.141 115.925 184.994 1.00 153.16 ? 112 ARG D CZ  1 
ATOM   9890  N  NH1 . ARG D 2 135 ? 127.667 115.380 186.102 1.00 152.07 ? 112 ARG D NH1 1 
ATOM   9891  N  NH2 . ARG D 2 135 ? 129.131 115.320 184.344 1.00 151.92 ? 112 ARG D NH2 1 
ATOM   9892  N  N   . LEU D 2 136 ? 128.644 122.628 187.206 1.00 161.89 ? 113 LEU D N   1 
ATOM   9893  C  CA  . LEU D 2 136 ? 129.604 123.578 187.743 1.00 162.14 ? 113 LEU D CA  1 
ATOM   9894  C  C   . LEU D 2 136 ? 129.739 123.354 189.241 1.00 162.65 ? 113 LEU D C   1 
ATOM   9895  O  O   . LEU D 2 136 ? 128.773 122.991 189.915 1.00 162.36 ? 113 LEU D O   1 
ATOM   9896  C  CB  . LEU D 2 136 ? 129.174 125.023 187.466 1.00 161.45 ? 113 LEU D CB  1 
ATOM   9897  C  CG  . LEU D 2 136 ? 130.236 126.104 187.651 1.00 161.14 ? 113 LEU D CG  1 
ATOM   9898  C  CD1 . LEU D 2 136 ? 131.239 126.057 186.513 1.00 161.35 ? 113 LEU D CD1 1 
ATOM   9899  C  CD2 . LEU D 2 136 ? 129.585 127.472 187.744 1.00 161.03 ? 113 LEU D CD2 1 
ATOM   9900  N  N   . ALA D 2 137 ? 130.946 123.572 189.759 1.00 172.64 ? 114 ALA D N   1 
ATOM   9901  C  CA  . ALA D 2 137 ? 131.201 123.411 191.185 1.00 172.48 ? 114 ALA D CA  1 
ATOM   9902  C  C   . ALA D 2 137 ? 132.502 124.115 191.530 1.00 173.19 ? 114 ALA D C   1 
ATOM   9903  O  O   . ALA D 2 137 ? 133.518 123.896 190.864 1.00 173.68 ? 114 ALA D O   1 
ATOM   9904  C  CB  . ALA D 2 137 ? 131.275 121.930 191.573 1.00 171.67 ? 114 ALA D CB  1 
ATOM   9905  N  N   . ILE D 2 138 ? 132.471 124.950 192.566 1.00 178.92 ? 115 ILE D N   1 
ATOM   9906  C  CA  . ILE D 2 138 ? 133.657 125.701 192.966 1.00 178.80 ? 115 ILE D CA  1 
ATOM   9907  C  C   . ILE D 2 138 ? 133.466 126.187 194.397 1.00 179.25 ? 115 ILE D C   1 
ATOM   9908  O  O   . ILE D 2 138 ? 132.352 126.516 194.810 1.00 178.98 ? 115 ILE D O   1 
ATOM   9909  C  CB  . ILE D 2 138 ? 133.929 126.873 191.991 1.00 177.89 ? 115 ILE D CB  1 
ATOM   9910  C  CG1 . ILE D 2 138 ? 135.253 127.564 192.323 1.00 177.84 ? 115 ILE D CG1 1 
ATOM   9911  C  CG2 . ILE D 2 138 ? 132.776 127.866 192.001 1.00 177.48 ? 115 ILE D CG2 1 
ATOM   9912  C  CD1 . ILE D 2 138 ? 135.507 128.818 191.522 1.00 177.70 ? 115 ILE D CD1 1 
ATOM   9913  N  N   . GLY D 2 139 ? 134.559 126.220 195.155 1.00 183.05 ? 116 GLY D N   1 
ATOM   9914  C  CA  . GLY D 2 139 ? 134.572 126.852 196.458 1.00 182.79 ? 116 GLY D CA  1 
ATOM   9915  C  C   . GLY D 2 139 ? 135.166 128.243 196.345 1.00 182.84 ? 116 GLY D C   1 
ATOM   9916  O  O   . GLY D 2 139 ? 136.023 128.498 195.505 1.00 182.67 ? 116 GLY D O   1 
ATOM   9917  N  N   . PHE D 2 140 ? 134.700 129.150 197.198 1.00 186.71 ? 117 PHE D N   1 
ATOM   9918  C  CA  . PHE D 2 140 ? 135.164 130.525 197.127 1.00 187.56 ? 117 PHE D CA  1 
ATOM   9919  C  C   . PHE D 2 140 ? 135.034 131.188 198.489 1.00 187.89 ? 117 PHE D C   1 
ATOM   9920  O  O   . PHE D 2 140 ? 134.327 130.707 199.379 1.00 187.15 ? 117 PHE D O   1 
ATOM   9921  C  CB  . PHE D 2 140 ? 134.393 131.324 196.072 1.00 186.50 ? 117 PHE D CB  1 
ATOM   9922  C  CG  . PHE D 2 140 ? 133.117 131.920 196.580 1.00 186.13 ? 117 PHE D CG  1 
ATOM   9923  C  CD1 . PHE D 2 140 ? 132.047 131.113 196.916 1.00 185.94 ? 117 PHE D CD1 1 
ATOM   9924  C  CD2 . PHE D 2 140 ? 132.988 133.291 196.718 1.00 185.96 ? 117 PHE D CD2 1 
ATOM   9925  C  CE1 . PHE D 2 140 ? 130.871 131.661 197.383 1.00 186.69 ? 117 PHE D CE1 1 
ATOM   9926  C  CE2 . PHE D 2 140 ? 131.814 133.846 197.184 1.00 186.58 ? 117 PHE D CE2 1 
ATOM   9927  C  CZ  . PHE D 2 140 ? 130.754 133.030 197.517 1.00 187.14 ? 117 PHE D CZ  1 
ATOM   9928  N  N   . SER D 2 141 ? 135.743 132.304 198.634 1.00 187.92 ? 118 SER D N   1 
ATOM   9929  C  CA  . SER D 2 141 ? 135.687 133.122 199.840 1.00 186.35 ? 118 SER D CA  1 
ATOM   9930  C  C   . SER D 2 141 ? 135.969 134.563 199.445 1.00 186.74 ? 118 SER D C   1 
ATOM   9931  O  O   . SER D 2 141 ? 137.071 134.877 198.981 1.00 186.76 ? 118 SER D O   1 
ATOM   9932  C  CB  . SER D 2 141 ? 136.690 132.638 200.889 1.00 185.45 ? 118 SER D CB  1 
ATOM   9933  O  OG  . SER D 2 141 ? 138.020 132.761 200.422 1.00 185.28 ? 118 SER D OG  1 
ATOM   9934  N  N   . THR D 2 142 ? 134.964 135.420 199.608 1.00 186.04 ? 119 THR D N   1 
ATOM   9935  C  CA  . THR D 2 142 ? 135.085 136.842 199.314 1.00 186.27 ? 119 THR D CA  1 
ATOM   9936  C  C   . THR D 2 142 ? 133.930 137.566 199.991 1.00 186.91 ? 119 THR D C   1 
ATOM   9937  O  O   . THR D 2 142 ? 132.967 136.948 200.453 1.00 186.15 ? 119 THR D O   1 
ATOM   9938  C  CB  . THR D 2 142 ? 135.090 137.115 197.807 1.00 185.59 ? 119 THR D CB  1 
ATOM   9939  O  OG1 . THR D 2 142 ? 135.646 138.412 197.559 1.00 184.28 ? 119 THR D OG1 1 
ATOM   9940  C  CG2 . THR D 2 142 ? 133.674 137.066 197.255 1.00 185.65 ? 119 THR D CG2 1 
ATOM   9941  N  N   . VAL D 2 143 ? 134.039 138.891 200.041 1.00 189.48 ? 120 VAL D N   1 
ATOM   9942  C  CA  . VAL D 2 143 ? 133.036 139.740 200.667 1.00 188.79 ? 120 VAL D CA  1 
ATOM   9943  C  C   . VAL D 2 143 ? 132.445 140.736 199.671 1.00 188.53 ? 120 VAL D C   1 
ATOM   9944  O  O   . VAL D 2 143 ? 131.799 141.699 200.066 1.00 188.04 ? 120 VAL D O   1 
ATOM   9945  C  CB  . VAL D 2 143 ? 133.616 140.464 201.896 1.00 187.65 ? 120 VAL D CB  1 
ATOM   9946  C  CG1 . VAL D 2 143 ? 133.979 139.461 202.976 1.00 187.13 ? 120 VAL D CG1 1 
ATOM   9947  C  CG2 . VAL D 2 143 ? 134.829 141.291 201.497 1.00 186.93 ? 120 VAL D CG2 1 
ATOM   9948  N  N   . GLN D 2 144 ? 132.661 140.510 198.378 1.00 186.85 ? 121 GLN D N   1 
ATOM   9949  C  CA  . GLN D 2 144 ? 132.188 141.440 197.367 1.00 186.10 ? 121 GLN D CA  1 
ATOM   9950  C  C   . GLN D 2 144 ? 130.668 141.383 197.239 1.00 186.56 ? 121 GLN D C   1 
ATOM   9951  O  O   . GLN D 2 144 ? 130.015 140.410 197.627 1.00 186.88 ? 121 GLN D O   1 
ATOM   9952  C  CB  . GLN D 2 144 ? 132.836 141.142 196.016 1.00 185.00 ? 121 GLN D CB  1 
ATOM   9953  C  CG  . GLN D 2 144 ? 134.274 141.609 195.908 1.00 185.07 ? 121 GLN D CG  1 
ATOM   9954  C  CD  . GLN D 2 144 ? 134.790 141.558 194.487 1.00 185.55 ? 121 GLN D CD  1 
ATOM   9955  O  OE1 . GLN D 2 144 ? 134.539 140.600 193.761 1.00 185.98 ? 121 GLN D OE1 1 
ATOM   9956  N  NE2 . GLN D 2 144 ? 135.510 142.596 194.081 1.00 185.59 ? 121 GLN D NE2 1 
ATOM   9957  N  N   . LYS D 2 145 ? 130.107 142.457 196.686 1.00 183.59 ? 122 LYS D N   1 
ATOM   9958  C  CA  . LYS D 2 145 ? 128.673 142.570 196.465 1.00 183.37 ? 122 LYS D CA  1 
ATOM   9959  C  C   . LYS D 2 145 ? 128.281 142.558 194.997 1.00 183.78 ? 122 LYS D C   1 
ATOM   9960  O  O   . LYS D 2 145 ? 127.214 142.039 194.662 1.00 183.72 ? 122 LYS D O   1 
ATOM   9961  C  CB  . LYS D 2 145 ? 128.139 143.855 197.114 1.00 182.82 ? 122 LYS D CB  1 
ATOM   9962  C  CG  . LYS D 2 145 ? 126.627 143.997 197.093 1.00 183.00 ? 122 LYS D CG  1 
ATOM   9963  C  CD  . LYS D 2 145 ? 126.185 145.208 197.900 1.00 182.91 ? 122 LYS D CD  1 
ATOM   9964  C  CE  . LYS D 2 145 ? 124.723 145.536 197.656 1.00 182.85 ? 122 LYS D CE  1 
ATOM   9965  N  NZ  . LYS D 2 145 ? 124.489 146.022 196.268 1.00 182.98 ? 122 LYS D NZ  1 
ATOM   9966  N  N   . GLU D 2 146 ? 129.114 143.110 194.115 1.00 184.75 ? 123 GLU D N   1 
ATOM   9967  C  CA  . GLU D 2 146 ? 128.841 143.147 192.681 1.00 184.79 ? 123 GLU D CA  1 
ATOM   9968  C  C   . GLU D 2 146 ? 130.068 142.630 191.944 1.00 184.10 ? 123 GLU D C   1 
ATOM   9969  O  O   . GLU D 2 146 ? 131.080 143.333 191.850 1.00 183.91 ? 123 GLU D O   1 
ATOM   9970  C  CB  . GLU D 2 146 ? 128.487 144.563 192.223 1.00 183.50 ? 123 GLU D CB  1 
ATOM   9971  C  CG  . GLU D 2 146 ? 127.351 145.203 193.002 1.00 183.25 ? 123 GLU D CG  1 
ATOM   9972  C  CD  . GLU D 2 146 ? 126.008 144.579 192.688 1.00 183.73 ? 123 GLU D CD  1 
ATOM   9973  O  OE1 . GLU D 2 146 ? 125.828 144.098 191.549 1.00 184.01 ? 123 GLU D OE1 1 
ATOM   9974  O  OE2 . GLU D 2 146 ? 125.134 144.564 193.579 1.00 183.47 ? 123 GLU D OE2 1 
ATOM   9975  N  N   . ALA D 2 147 ? 129.980 141.411 191.418 1.00 181.87 ? 124 ALA D N   1 
ATOM   9976  C  CA  . ALA D 2 147 ? 131.097 140.819 190.695 1.00 182.13 ? 124 ALA D CA  1 
ATOM   9977  C  C   . ALA D 2 147 ? 130.579 139.709 189.793 1.00 182.67 ? 124 ALA D C   1 
ATOM   9978  O  O   . ALA D 2 147 ? 129.451 139.236 189.946 1.00 181.96 ? 124 ALA D O   1 
ATOM   9979  C  CB  . ALA D 2 147 ? 132.162 140.276 191.652 1.00 181.58 ? 124 ALA D CB  1 
ATOM   9980  N  N   . VAL D 2 148 ? 131.424 139.303 188.848 1.00 179.20 ? 125 VAL D N   1 
ATOM   9981  C  CA  . VAL D 2 148 ? 131.163 138.159 187.982 1.00 177.54 ? 125 VAL D CA  1 
ATOM   9982  C  C   . VAL D 2 148 ? 132.369 137.230 188.047 1.00 177.18 ? 125 VAL D C   1 
ATOM   9983  O  O   . VAL D 2 148 ? 133.507 137.667 187.846 1.00 176.35 ? 125 VAL D O   1 
ATOM   9984  C  CB  . VAL D 2 148 ? 130.870 138.592 186.533 1.00 176.82 ? 125 VAL D CB  1 
ATOM   9985  C  CG1 . VAL D 2 148 ? 129.458 139.135 186.424 1.00 176.58 ? 125 VAL D CG1 1 
ATOM   9986  C  CG2 . VAL D 2 148 ? 131.862 139.646 186.080 1.00 176.78 ? 125 VAL D CG2 1 
ATOM   9987  N  N   . LEU D 2 149 ? 132.121 135.952 188.338 1.00 169.68 ? 126 LEU D N   1 
ATOM   9988  C  CA  . LEU D 2 149 ? 133.188 134.992 188.605 1.00 169.73 ? 126 LEU D CA  1 
ATOM   9989  C  C   . LEU D 2 149 ? 133.485 134.095 187.408 1.00 170.17 ? 126 LEU D C   1 
ATOM   9990  O  O   . LEU D 2 149 ? 134.624 134.044 186.934 1.00 169.50 ? 126 LEU D O   1 
ATOM   9991  C  CB  . LEU D 2 149 ? 132.822 134.138 189.826 1.00 168.83 ? 126 LEU D CB  1 
ATOM   9992  C  CG  . LEU D 2 149 ? 133.166 134.714 191.199 1.00 169.37 ? 126 LEU D CG  1 
ATOM   9993  C  CD1 . LEU D 2 149 ? 132.147 135.763 191.620 1.00 169.65 ? 126 LEU D CD1 1 
ATOM   9994  C  CD2 . LEU D 2 149 ? 133.254 133.600 192.231 1.00 169.31 ? 126 LEU D CD2 1 
ATOM   9995  N  N   . VAL D 2 150 ? 132.479 133.379 186.912 1.00 162.96 ? 127 VAL D N   1 
ATOM   9996  C  CA  . VAL D 2 150 ? 132.657 132.373 185.872 1.00 161.87 ? 127 VAL D CA  1 
ATOM   9997  C  C   . VAL D 2 150 ? 131.891 132.809 184.632 1.00 161.95 ? 127 VAL D C   1 
ATOM   9998  O  O   . VAL D 2 150 ? 130.701 133.133 184.713 1.00 160.34 ? 127 VAL D O   1 
ATOM   9999  C  CB  . VAL D 2 150 ? 132.191 130.985 186.343 1.00 161.48 ? 127 VAL D CB  1 
ATOM   10000 C  CG1 . VAL D 2 150 ? 132.835 129.903 185.507 1.00 161.60 ? 127 VAL D CG1 1 
ATOM   10001 C  CG2 . VAL D 2 150 ? 132.539 130.786 187.805 1.00 162.06 ? 127 VAL D CG2 1 
ATOM   10002 N  N   . ARG D 2 151 ? 132.577 132.818 183.491 1.00 155.61 ? 128 ARG D N   1 
ATOM   10003 C  CA  . ARG D 2 151 ? 131.990 133.212 182.216 1.00 154.91 ? 128 ARG D CA  1 
ATOM   10004 C  C   . ARG D 2 151 ? 132.285 132.137 181.185 1.00 156.12 ? 128 ARG D C   1 
ATOM   10005 O  O   . ARG D 2 151 ? 133.453 131.839 180.913 1.00 156.59 ? 128 ARG D O   1 
ATOM   10006 C  CB  . ARG D 2 151 ? 132.536 134.565 181.752 1.00 154.44 ? 128 ARG D CB  1 
ATOM   10007 C  CG  . ARG D 2 151 ? 132.134 134.951 180.337 1.00 153.38 ? 128 ARG D CG  1 
ATOM   10008 C  CD  . ARG D 2 151 ? 130.631 135.094 180.233 1.00 154.98 ? 128 ARG D CD  1 
ATOM   10009 N  NE  . ARG D 2 151 ? 130.176 135.400 178.882 1.00 156.00 ? 128 ARG D NE  1 
ATOM   10010 C  CZ  . ARG D 2 151 ? 129.718 136.584 178.499 1.00 155.54 ? 128 ARG D CZ  1 
ATOM   10011 N  NH1 . ARG D 2 151 ? 129.632 137.598 179.344 1.00 155.58 ? 128 ARG D NH1 1 
ATOM   10012 N  NH2 . ARG D 2 151 ? 129.329 136.753 177.239 1.00 155.22 ? 128 ARG D NH2 1 
ATOM   10013 N  N   . VAL D 2 152 ? 131.231 131.562 180.610 1.00 146.89 ? 129 VAL D N   1 
ATOM   10014 C  CA  . VAL D 2 152 ? 131.346 130.572 179.547 1.00 145.24 ? 129 VAL D CA  1 
ATOM   10015 C  C   . VAL D 2 152 ? 130.687 131.146 178.304 1.00 144.93 ? 129 VAL D C   1 
ATOM   10016 O  O   . VAL D 2 152 ? 129.515 131.537 178.342 1.00 144.32 ? 129 VAL D O   1 
ATOM   10017 C  CB  . VAL D 2 152 ? 130.697 129.233 179.940 1.00 142.71 ? 129 VAL D CB  1 
ATOM   10018 C  CG1 . VAL D 2 152 ? 131.155 128.132 179.004 1.00 143.66 ? 129 VAL D CG1 1 
ATOM   10019 C  CG2 . VAL D 2 152 ? 131.023 128.887 181.377 1.00 143.20 ? 129 VAL D CG2 1 
ATOM   10020 N  N   . ASP D 2 153 ? 131.436 131.196 177.207 1.00 140.68 ? 130 ASP D N   1 
ATOM   10021 C  CA  . ASP D 2 153 ? 130.964 131.793 175.970 1.00 140.82 ? 130 ASP D CA  1 
ATOM   10022 C  C   . ASP D 2 153 ? 131.021 130.782 174.835 1.00 140.76 ? 130 ASP D C   1 
ATOM   10023 O  O   . ASP D 2 153 ? 131.669 129.738 174.931 1.00 141.63 ? 130 ASP D O   1 
ATOM   10024 C  CB  . ASP D 2 153 ? 131.790 133.030 175.593 1.00 141.67 ? 130 ASP D CB  1 
ATOM   10025 C  CG  . ASP D 2 153 ? 131.188 134.316 176.117 1.00 142.78 ? 130 ASP D CG  1 
ATOM   10026 O  OD1 . ASP D 2 153 ? 129.991 134.312 176.470 1.00 144.33 ? 130 ASP D OD1 1 
ATOM   10027 O  OD2 . ASP D 2 153 ? 131.911 135.333 176.167 1.00 141.93 ? 130 ASP D OD2 1 
ATOM   10028 N  N   . SER D 2 154 ? 130.332 131.115 173.750 1.00 128.30 ? 131 SER D N   1 
ATOM   10029 C  CA  . SER D 2 154 ? 130.374 130.337 172.526 1.00 127.61 ? 131 SER D CA  1 
ATOM   10030 C  C   . SER D 2 154 ? 131.282 131.027 171.514 1.00 127.28 ? 131 SER D C   1 
ATOM   10031 O  O   . SER D 2 154 ? 131.884 132.068 171.787 1.00 127.76 ? 131 SER D O   1 
ATOM   10032 C  CB  . SER D 2 154 ? 128.964 130.151 171.968 1.00 127.14 ? 131 SER D CB  1 
ATOM   10033 O  OG  . SER D 2 154 ? 128.110 129.596 172.949 1.00 129.65 ? 131 SER D OG  1 
ATOM   10034 N  N   . SER D 2 155 ? 131.374 130.444 170.325 1.00 124.15 ? 132 SER D N   1 
ATOM   10035 C  CA  . SER D 2 155 ? 132.160 131.037 169.253 1.00 125.22 ? 132 SER D CA  1 
ATOM   10036 C  C   . SER D 2 155 ? 131.399 132.233 168.680 1.00 124.91 ? 132 SER D C   1 
ATOM   10037 O  O   . SER D 2 155 ? 130.367 132.657 169.209 1.00 122.65 ? 132 SER D O   1 
ATOM   10038 C  CB  . SER D 2 155 ? 132.487 129.991 168.191 1.00 121.11 ? 132 SER D CB  1 
ATOM   10039 O  OG  . SER D 2 155 ? 133.623 129.229 168.560 1.00 117.19 ? 132 SER D OG  1 
ATOM   10040 N  N   . SER D 2 156 ? 131.909 132.798 167.589 1.00 122.97 ? 133 SER D N   1 
ATOM   10041 C  CA  . SER D 2 156 ? 131.309 133.995 167.018 1.00 122.93 ? 133 SER D CA  1 
ATOM   10042 C  C   . SER D 2 156 ? 129.878 133.730 166.568 1.00 124.59 ? 133 SER D C   1 
ATOM   10043 O  O   . SER D 2 156 ? 129.572 132.681 165.995 1.00 124.31 ? 133 SER D O   1 
ATOM   10044 C  CB  . SER D 2 156 ? 132.145 134.492 165.839 1.00 122.90 ? 133 SER D CB  1 
ATOM   10045 O  OG  . SER D 2 156 ? 132.039 133.613 164.734 1.00 122.52 ? 133 SER D OG  1 
ATOM   10046 N  N   . GLY D 2 157 ? 129.005 134.685 166.833 1.00 125.01 ? 134 GLY D N   1 
ATOM   10047 C  CA  . GLY D 2 157 ? 127.614 134.620 166.395 1.00 122.99 ? 134 GLY D CA  1 
ATOM   10048 C  C   . GLY D 2 157 ? 126.617 134.010 167.357 1.00 122.14 ? 134 GLY D C   1 
ATOM   10049 O  O   . GLY D 2 157 ? 125.566 134.594 167.616 1.00 121.26 ? 134 GLY D O   1 
ATOM   10050 N  N   . LEU D 2 158 ? 126.931 132.834 167.890 1.00 118.99 ? 135 LEU D N   1 
ATOM   10051 C  CA  . LEU D 2 158 ? 125.999 132.133 168.762 1.00 118.11 ? 135 LEU D CA  1 
ATOM   10052 C  C   . LEU D 2 158 ? 125.811 132.893 170.068 1.00 117.36 ? 135 LEU D C   1 
ATOM   10053 O  O   . LEU D 2 158 ? 126.771 133.394 170.660 1.00 118.88 ? 135 LEU D O   1 
ATOM   10054 C  CB  . LEU D 2 158 ? 126.501 130.715 169.035 1.00 117.91 ? 135 LEU D CB  1 
ATOM   10055 C  CG  . LEU D 2 158 ? 127.187 130.031 167.849 1.00 116.62 ? 135 LEU D CG  1 
ATOM   10056 C  CD1 . LEU D 2 158 ? 127.811 128.712 168.264 1.00 112.76 ? 135 LEU D CD1 1 
ATOM   10057 C  CD2 . LEU D 2 158 ? 126.208 129.823 166.710 1.00 115.63 ? 135 LEU D CD2 1 
ATOM   10058 N  N   . GLY D 2 159 ? 124.562 132.978 170.516 1.00 118.20 ? 136 GLY D N   1 
ATOM   10059 C  CA  . GLY D 2 159 ? 124.199 133.703 171.714 1.00 119.16 ? 136 GLY D CA  1 
ATOM   10060 C  C   . GLY D 2 159 ? 124.246 132.906 172.998 1.00 119.43 ? 136 GLY D C   1 
ATOM   10061 O  O   . GLY D 2 159 ? 123.819 133.412 174.041 1.00 117.77 ? 136 GLY D O   1 
ATOM   10062 N  N   . ASP D 2 160 ? 124.749 131.676 172.958 1.00 124.10 ? 137 ASP D N   1 
ATOM   10063 C  CA  . ASP D 2 160 ? 124.777 130.832 174.145 1.00 124.98 ? 137 ASP D CA  1 
ATOM   10064 C  C   . ASP D 2 160 ? 125.818 131.347 175.130 1.00 125.74 ? 137 ASP D C   1 
ATOM   10065 O  O   . ASP D 2 160 ? 126.957 131.631 174.745 1.00 124.05 ? 137 ASP D O   1 
ATOM   10066 C  CB  . ASP D 2 160 ? 125.101 129.393 173.751 1.00 123.61 ? 137 ASP D CB  1 
ATOM   10067 C  CG  . ASP D 2 160 ? 123.892 128.641 173.256 1.00 123.05 ? 137 ASP D CG  1 
ATOM   10068 O  OD1 . ASP D 2 160 ? 122.793 128.894 173.774 1.00 121.56 ? 137 ASP D OD1 1 
ATOM   10069 O  OD2 . ASP D 2 160 ? 124.039 127.796 172.349 1.00 124.20 ? 137 ASP D OD2 1 
ATOM   10070 N  N   . TYR D 2 161 ? 125.440 131.464 176.403 1.00 139.69 ? 138 TYR D N   1 
ATOM   10071 C  CA  . TYR D 2 161 ? 126.423 131.826 177.420 1.00 140.34 ? 138 TYR D CA  1 
ATOM   10072 C  C   . TYR D 2 161 ? 125.913 131.416 178.794 1.00 140.34 ? 138 TYR D C   1 
ATOM   10073 O  O   . TYR D 2 161 ? 124.728 131.140 178.984 1.00 138.18 ? 138 TYR D O   1 
ATOM   10074 C  CB  . TYR D 2 161 ? 126.766 133.322 177.380 1.00 139.84 ? 138 TYR D CB  1 
ATOM   10075 C  CG  . TYR D 2 161 ? 125.638 134.268 177.734 1.00 141.27 ? 138 TYR D CG  1 
ATOM   10076 C  CD1 . TYR D 2 161 ? 125.385 134.620 179.055 1.00 140.86 ? 138 TYR D CD1 1 
ATOM   10077 C  CD2 . TYR D 2 161 ? 124.845 134.833 176.743 1.00 140.83 ? 138 TYR D CD2 1 
ATOM   10078 C  CE1 . TYR D 2 161 ? 124.362 135.492 179.378 1.00 139.58 ? 138 TYR D CE1 1 
ATOM   10079 C  CE2 . TYR D 2 161 ? 123.822 135.706 177.057 1.00 140.97 ? 138 TYR D CE2 1 
ATOM   10080 C  CZ  . TYR D 2 161 ? 123.584 136.031 178.374 1.00 141.13 ? 138 TYR D CZ  1 
ATOM   10081 O  OH  . TYR D 2 161 ? 122.565 136.899 178.687 1.00 141.25 ? 138 TYR D OH  1 
ATOM   10082 N  N   . LEU D 2 162 ? 126.837 131.373 179.752 1.00 145.80 ? 139 LEU D N   1 
ATOM   10083 C  CA  . LEU D 2 162 ? 126.522 131.038 181.133 1.00 145.05 ? 139 LEU D CA  1 
ATOM   10084 C  C   . LEU D 2 162 ? 127.339 131.930 182.057 1.00 146.47 ? 139 LEU D C   1 
ATOM   10085 O  O   . LEU D 2 162 ? 128.544 132.103 181.857 1.00 145.67 ? 139 LEU D O   1 
ATOM   10086 C  CB  . LEU D 2 162 ? 126.805 129.559 181.428 1.00 145.16 ? 139 LEU D CB  1 
ATOM   10087 C  CG  . LEU D 2 162 ? 127.148 129.174 182.868 1.00 146.52 ? 139 LEU D CG  1 
ATOM   10088 C  CD1 . LEU D 2 162 ? 125.894 129.142 183.728 1.00 146.95 ? 139 LEU D CD1 1 
ATOM   10089 C  CD2 . LEU D 2 162 ? 127.857 127.830 182.908 1.00 145.45 ? 139 LEU D CD2 1 
ATOM   10090 N  N   . GLU D 2 163 ? 126.678 132.485 183.071 1.00 157.32 ? 140 GLU D N   1 
ATOM   10091 C  CA  . GLU D 2 163 ? 127.266 133.473 183.961 1.00 157.00 ? 140 GLU D CA  1 
ATOM   10092 C  C   . GLU D 2 163 ? 127.038 133.068 185.407 1.00 156.78 ? 140 GLU D C   1 
ATOM   10093 O  O   . GLU D 2 163 ? 125.933 132.663 185.777 1.00 156.38 ? 140 GLU D O   1 
ATOM   10094 C  CB  . GLU D 2 163 ? 126.642 134.859 183.735 1.00 157.03 ? 140 GLU D CB  1 
ATOM   10095 C  CG  . GLU D 2 163 ? 127.016 135.558 182.438 1.00 156.88 ? 140 GLU D CG  1 
ATOM   10096 C  CD  . GLU D 2 163 ? 128.402 136.173 182.461 1.00 157.01 ? 140 GLU D CD  1 
ATOM   10097 O  OE1 . GLU D 2 163 ? 129.222 135.801 183.326 1.00 156.16 ? 140 GLU D OE1 1 
ATOM   10098 O  OE2 . GLU D 2 163 ? 128.664 137.050 181.613 1.00 157.67 ? 140 GLU D OE2 1 
ATOM   10099 N  N   . LEU D 2 164 ? 128.082 133.193 186.222 1.00 165.06 ? 141 LEU D N   1 
ATOM   10100 C  CA  . LEU D 2 164 ? 127.967 133.131 187.673 1.00 166.78 ? 141 LEU D CA  1 
ATOM   10101 C  C   . LEU D 2 164 ? 128.337 134.504 188.213 1.00 168.15 ? 141 LEU D C   1 
ATOM   10102 O  O   . LEU D 2 164 ? 129.415 135.024 187.903 1.00 167.14 ? 141 LEU D O   1 
ATOM   10103 C  CB  . LEU D 2 164 ? 128.868 132.044 188.263 1.00 165.94 ? 141 LEU D CB  1 
ATOM   10104 C  CG  . LEU D 2 164 ? 129.008 132.032 189.787 1.00 166.72 ? 141 LEU D CG  1 
ATOM   10105 C  CD1 . LEU D 2 164 ? 127.657 131.842 190.444 1.00 166.08 ? 141 LEU D CD1 1 
ATOM   10106 C  CD2 . LEU D 2 164 ? 129.964 130.945 190.238 1.00 166.06 ? 141 LEU D CD2 1 
ATOM   10107 N  N   . HIS D 2 165 ? 127.444 135.099 189.000 1.00 174.36 ? 142 HIS D N   1 
ATOM   10108 C  CA  . HIS D 2 165 ? 127.632 136.480 189.413 1.00 173.43 ? 142 HIS D CA  1 
ATOM   10109 C  C   . HIS D 2 165 ? 127.075 136.687 190.812 1.00 174.59 ? 142 HIS D C   1 
ATOM   10110 O  O   . HIS D 2 165 ? 126.090 136.058 191.209 1.00 173.82 ? 142 HIS D O   1 
ATOM   10111 C  CB  . HIS D 2 165 ? 126.954 137.445 188.436 1.00 173.21 ? 142 HIS D CB  1 
ATOM   10112 C  CG  . HIS D 2 165 ? 125.459 137.381 188.468 1.00 173.41 ? 142 HIS D CG  1 
ATOM   10113 N  ND1 . HIS D 2 165 ? 124.755 136.252 188.110 1.00 173.09 ? 142 HIS D ND1 1 
ATOM   10114 C  CD2 . HIS D 2 165 ? 124.534 138.307 188.816 1.00 173.43 ? 142 HIS D CD2 1 
ATOM   10115 C  CE1 . HIS D 2 165 ? 123.461 136.484 188.237 1.00 172.96 ? 142 HIS D CE1 1 
ATOM   10116 N  NE2 . HIS D 2 165 ? 123.300 137.723 188.663 1.00 173.12 ? 142 HIS D NE2 1 
ATOM   10117 N  N   . ILE D 2 166 ? 127.708 137.596 191.545 1.00 181.06 ? 143 ILE D N   1 
ATOM   10118 C  CA  . ILE D 2 166 ? 127.242 138.035 192.853 1.00 180.45 ? 143 ILE D CA  1 
ATOM   10119 C  C   . ILE D 2 166 ? 126.686 139.440 192.675 1.00 179.64 ? 143 ILE D C   1 
ATOM   10120 O  O   . ILE D 2 166 ? 127.431 140.381 192.375 1.00 179.03 ? 143 ILE D O   1 
ATOM   10121 C  CB  . ILE D 2 166 ? 128.361 138.005 193.902 1.00 179.88 ? 143 ILE D CB  1 
ATOM   10122 C  CG1 . ILE D 2 166 ? 129.149 136.697 193.803 1.00 179.19 ? 143 ILE D CG1 1 
ATOM   10123 C  CG2 . ILE D 2 166 ? 127.784 138.173 195.298 1.00 179.53 ? 143 ILE D CG2 1 
ATOM   10124 C  CD1 . ILE D 2 166 ? 130.269 136.580 194.813 1.00 178.93 ? 143 ILE D CD1 1 
ATOM   10125 N  N   . HIS D 2 167 ? 125.374 139.579 192.849 1.00 183.09 ? 144 HIS D N   1 
ATOM   10126 C  CA  . HIS D 2 167 ? 124.683 140.852 192.706 1.00 184.13 ? 144 HIS D CA  1 
ATOM   10127 C  C   . HIS D 2 167 ? 123.867 141.109 193.963 1.00 184.94 ? 144 HIS D C   1 
ATOM   10128 O  O   . HIS D 2 167 ? 123.116 140.233 194.406 1.00 184.63 ? 144 HIS D O   1 
ATOM   10129 C  CB  . HIS D 2 167 ? 123.777 140.853 191.469 1.00 183.99 ? 144 HIS D CB  1 
ATOM   10130 C  CG  . HIS D 2 167 ? 122.864 142.036 191.388 1.00 184.59 ? 144 HIS D CG  1 
ATOM   10131 N  ND1 . HIS D 2 167 ? 123.309 143.332 191.533 1.00 184.41 ? 144 HIS D ND1 1 
ATOM   10132 C  CD2 . HIS D 2 167 ? 121.529 142.119 191.173 1.00 183.82 ? 144 HIS D CD2 1 
ATOM   10133 C  CE1 . HIS D 2 167 ? 122.288 144.163 191.412 1.00 183.57 ? 144 HIS D CE1 1 
ATOM   10134 N  NE2 . HIS D 2 167 ? 121.197 143.452 191.194 1.00 183.86 ? 144 HIS D NE2 1 
ATOM   10135 N  N   . GLN D 2 168 ? 124.022 142.305 194.534 1.00 184.30 ? 145 GLN D N   1 
ATOM   10136 C  CA  . GLN D 2 168 ? 123.324 142.701 195.758 1.00 183.41 ? 145 GLN D CA  1 
ATOM   10137 C  C   . GLN D 2 168 ? 123.572 141.716 196.896 1.00 183.11 ? 145 GLN D C   1 
ATOM   10138 O  O   . GLN D 2 168 ? 122.694 141.479 197.730 1.00 182.65 ? 145 GLN D O   1 
ATOM   10139 C  CB  . GLN D 2 168 ? 121.821 142.868 195.514 1.00 183.40 ? 145 GLN D CB  1 
ATOM   10140 C  CG  . GLN D 2 168 ? 121.454 144.142 194.773 1.00 183.21 ? 145 GLN D CG  1 
ATOM   10141 C  CD  . GLN D 2 168 ? 119.959 144.289 194.571 1.00 183.19 ? 145 GLN D CD  1 
ATOM   10142 O  OE1 . GLN D 2 168 ? 119.180 143.413 194.947 1.00 183.04 ? 145 GLN D OE1 1 
ATOM   10143 N  NE2 . GLN D 2 168 ? 119.550 145.404 193.976 1.00 182.94 ? 145 GLN D NE2 1 
ATOM   10144 N  N   . GLY D 2 169 ? 124.768 141.132 196.937 1.00 182.29 ? 146 GLY D N   1 
ATOM   10145 C  CA  . GLY D 2 169 ? 125.114 140.171 197.961 1.00 182.43 ? 146 GLY D CA  1 
ATOM   10146 C  C   . GLY D 2 169 ? 124.574 138.777 197.742 1.00 183.57 ? 146 GLY D C   1 
ATOM   10147 O  O   . GLY D 2 169 ? 124.807 137.902 198.586 1.00 182.34 ? 146 GLY D O   1 
ATOM   10148 N  N   . LYS D 2 170 ? 123.864 138.537 196.643 1.00 186.35 ? 147 LYS D N   1 
ATOM   10149 C  CA  . LYS D 2 170 ? 123.281 137.238 196.340 1.00 185.24 ? 147 LYS D CA  1 
ATOM   10150 C  C   . LYS D 2 170 ? 124.037 136.608 195.178 1.00 184.84 ? 147 LYS D C   1 
ATOM   10151 O  O   . LYS D 2 170 ? 124.253 137.257 194.150 1.00 183.58 ? 147 LYS D O   1 
ATOM   10152 C  CB  . LYS D 2 170 ? 121.796 137.368 195.996 1.00 183.35 ? 147 LYS D CB  1 
ATOM   10153 C  CG  . LYS D 2 170 ? 121.005 138.238 196.955 1.00 183.47 ? 147 LYS D CG  1 
ATOM   10154 C  CD  . LYS D 2 170 ? 120.920 137.612 198.336 1.00 184.07 ? 147 LYS D CD  1 
ATOM   10155 C  CE  . LYS D 2 170 ? 120.201 138.530 199.313 1.00 183.32 ? 147 LYS D CE  1 
ATOM   10156 N  NZ  . LYS D 2 170 ? 120.897 139.837 199.465 1.00 182.90 ? 147 LYS D NZ  1 
ATOM   10157 N  N   . ILE D 2 171 ? 124.438 135.354 195.346 1.00 181.99 ? 148 ILE D N   1 
ATOM   10158 C  CA  . ILE D 2 171 ? 125.158 134.622 194.312 1.00 181.26 ? 148 ILE D CA  1 
ATOM   10159 C  C   . ILE D 2 171 ? 124.145 133.886 193.445 1.00 181.18 ? 148 ILE D C   1 
ATOM   10160 O  O   . ILE D 2 171 ? 123.184 133.298 193.956 1.00 180.98 ? 148 ILE D O   1 
ATOM   10161 C  CB  . ILE D 2 171 ? 126.180 133.653 194.935 1.00 180.54 ? 148 ILE D CB  1 
ATOM   10162 C  CG1 . ILE D 2 171 ? 126.986 132.943 193.847 1.00 179.99 ? 148 ILE D CG1 1 
ATOM   10163 C  CG2 . ILE D 2 171 ? 125.498 132.650 195.858 1.00 179.72 ? 148 ILE D CG2 1 
ATOM   10164 C  CD1 . ILE D 2 171 ? 128.244 132.280 194.360 1.00 179.83 ? 148 ILE D CD1 1 
ATOM   10165 N  N   . GLY D 2 172 ? 124.339 133.939 192.128 1.00 172.98 ? 149 GLY D N   1 
ATOM   10166 C  CA  . GLY D 2 172 ? 123.381 133.328 191.226 1.00 172.07 ? 149 GLY D CA  1 
ATOM   10167 C  C   . GLY D 2 172 ? 123.996 133.030 189.878 1.00 172.49 ? 149 GLY D C   1 
ATOM   10168 O  O   . GLY D 2 172 ? 125.102 133.470 189.554 1.00 172.80 ? 149 GLY D O   1 
ATOM   10169 N  N   . VAL D 2 173 ? 123.249 132.261 189.090 1.00 166.74 ? 150 VAL D N   1 
ATOM   10170 C  CA  . VAL D 2 173 ? 123.676 131.818 187.769 1.00 166.08 ? 150 VAL D CA  1 
ATOM   10171 C  C   . VAL D 2 173 ? 122.611 132.208 186.755 1.00 164.69 ? 150 VAL D C   1 
ATOM   10172 O  O   . VAL D 2 173 ? 121.416 131.986 186.982 1.00 164.14 ? 150 VAL D O   1 
ATOM   10173 C  CB  . VAL D 2 173 ? 123.933 130.299 187.725 1.00 165.16 ? 150 VAL D CB  1 
ATOM   10174 C  CG1 . VAL D 2 173 ? 125.270 129.973 188.366 1.00 164.96 ? 150 VAL D CG1 1 
ATOM   10175 C  CG2 . VAL D 2 173 ? 122.809 129.546 188.419 1.00 164.68 ? 150 VAL D CG2 1 
ATOM   10176 N  N   . LYS D 2 174 ? 123.047 132.789 185.641 1.00 155.31 ? 151 LYS D N   1 
ATOM   10177 C  CA  . LYS D 2 174 ? 122.164 133.186 184.550 1.00 155.12 ? 151 LYS D CA  1 
ATOM   10178 C  C   . LYS D 2 174 ? 122.717 132.628 183.249 1.00 156.57 ? 151 LYS D C   1 
ATOM   10179 O  O   . LYS D 2 174 ? 123.852 132.934 182.874 1.00 157.06 ? 151 LYS D O   1 
ATOM   10180 C  CB  . LYS D 2 174 ? 122.034 134.709 184.474 1.00 155.42 ? 151 LYS D CB  1 
ATOM   10181 C  CG  . LYS D 2 174 ? 121.384 135.217 183.199 1.00 155.92 ? 151 LYS D CG  1 
ATOM   10182 C  CD  . LYS D 2 174 ? 121.295 136.735 183.205 1.00 156.09 ? 151 LYS D CD  1 
ATOM   10183 C  CE  . LYS D 2 174 ? 122.636 137.363 183.554 1.00 156.08 ? 151 LYS D CE  1 
ATOM   10184 N  NZ  . LYS D 2 174 ? 122.594 138.849 183.483 1.00 155.85 ? 151 LYS D NZ  1 
ATOM   10185 N  N   . PHE D 2 175 ? 121.923 131.815 182.563 1.00 148.68 ? 152 PHE D N   1 
ATOM   10186 C  CA  . PHE D 2 175 ? 122.361 131.184 181.327 1.00 146.64 ? 152 PHE D CA  1 
ATOM   10187 C  C   . PHE D 2 175 ? 121.378 131.476 180.204 1.00 146.15 ? 152 PHE D C   1 
ATOM   10188 O  O   . PHE D 2 175 ? 120.162 131.508 180.416 1.00 145.64 ? 152 PHE D O   1 
ATOM   10189 C  CB  . PHE D 2 175 ? 122.532 129.665 181.495 1.00 146.67 ? 152 PHE D CB  1 
ATOM   10190 C  CG  . PHE D 2 175 ? 121.330 128.972 182.072 1.00 146.52 ? 152 PHE D CG  1 
ATOM   10191 C  CD1 . PHE D 2 175 ? 120.309 128.526 181.252 1.00 146.65 ? 152 PHE D CD1 1 
ATOM   10192 C  CD2 . PHE D 2 175 ? 121.230 128.753 183.433 1.00 146.78 ? 152 PHE D CD2 1 
ATOM   10193 C  CE1 . PHE D 2 175 ? 119.207 127.885 181.780 1.00 146.67 ? 152 PHE D CE1 1 
ATOM   10194 C  CE2 . PHE D 2 175 ? 120.130 128.113 183.967 1.00 147.48 ? 152 PHE D CE2 1 
ATOM   10195 C  CZ  . PHE D 2 175 ? 119.118 127.679 183.139 1.00 146.92 ? 152 PHE D CZ  1 
ATOM   10196 N  N   . ASN D 2 176 ? 121.922 131.713 179.015 1.00 135.83 ? 153 ASN D N   1 
ATOM   10197 C  CA  . ASN D 2 176 ? 121.148 131.836 177.787 1.00 136.36 ? 153 ASN D CA  1 
ATOM   10198 C  C   . ASN D 2 176 ? 121.481 130.634 176.913 1.00 137.06 ? 153 ASN D C   1 
ATOM   10199 O  O   . ASN D 2 176 ? 122.618 130.499 176.438 1.00 136.17 ? 153 ASN D O   1 
ATOM   10200 C  CB  . ASN D 2 176 ? 121.452 133.143 177.062 1.00 136.65 ? 153 ASN D CB  1 
ATOM   10201 C  CG  . ASN D 2 176 ? 120.475 133.424 175.939 1.00 136.25 ? 153 ASN D CG  1 
ATOM   10202 O  OD1 . ASN D 2 176 ? 119.322 132.993 175.983 1.00 134.37 ? 153 ASN D OD1 1 
ATOM   10203 N  ND2 . ASN D 2 176 ? 120.931 134.146 174.923 1.00 136.24 ? 153 ASN D ND2 1 
ATOM   10204 N  N   . VAL D 2 177 ? 120.488 129.762 176.719 1.00 129.16 ? 154 VAL D N   1 
ATOM   10205 C  CA  . VAL D 2 177 ? 120.628 128.573 175.891 1.00 125.61 ? 154 VAL D CA  1 
ATOM   10206 C  C   . VAL D 2 177 ? 119.998 128.744 174.519 1.00 126.44 ? 154 VAL D C   1 
ATOM   10207 O  O   . VAL D 2 177 ? 120.109 127.842 173.678 1.00 127.44 ? 154 VAL D O   1 
ATOM   10208 C  CB  . VAL D 2 177 ? 120.036 127.337 176.596 1.00 123.59 ? 154 VAL D CB  1 
ATOM   10209 C  CG1 . VAL D 2 177 ? 120.874 126.973 177.804 1.00 124.91 ? 154 VAL D CG1 1 
ATOM   10210 C  CG2 . VAL D 2 177 ? 118.598 127.602 177.003 1.00 124.80 ? 154 VAL D CG2 1 
ATOM   10211 N  N   . GLY D 2 178 ? 119.352 129.879 174.260 1.00 129.12 ? 155 GLY D N   1 
ATOM   10212 C  CA  . GLY D 2 178 ? 118.781 130.150 172.956 1.00 127.14 ? 155 GLY D CA  1 
ATOM   10213 C  C   . GLY D 2 178 ? 117.407 130.785 172.997 1.00 128.47 ? 155 GLY D C   1 
ATOM   10214 O  O   . GLY D 2 178 ? 117.084 131.618 172.145 1.00 127.69 ? 155 GLY D O   1 
ATOM   10215 N  N   . THR D 2 179 ? 116.585 130.409 173.977 1.00 140.51 ? 156 THR D N   1 
ATOM   10216 C  CA  . THR D 2 179 ? 115.260 131.010 174.095 1.00 140.10 ? 156 THR D CA  1 
ATOM   10217 C  C   . THR D 2 179 ? 115.326 132.349 174.819 1.00 141.48 ? 156 THR D C   1 
ATOM   10218 O  O   . THR D 2 179 ? 115.012 133.396 174.243 1.00 142.15 ? 156 THR D O   1 
ATOM   10219 C  CB  . THR D 2 179 ? 114.305 130.062 174.828 1.00 139.52 ? 156 THR D CB  1 
ATOM   10220 O  OG1 . THR D 2 179 ? 115.018 129.356 175.851 1.00 139.52 ? 156 THR D OG1 1 
ATOM   10221 C  CG2 . THR D 2 179 ? 113.685 129.068 173.862 1.00 139.47 ? 156 THR D CG2 1 
ATOM   10222 N  N   . ASP D 2 180 ? 115.746 132.330 176.081 1.00 144.87 ? 157 ASP D N   1 
ATOM   10223 C  CA  . ASP D 2 180 ? 115.787 133.529 176.905 1.00 145.16 ? 157 ASP D CA  1 
ATOM   10224 C  C   . ASP D 2 180 ? 116.781 133.302 178.033 1.00 145.48 ? 157 ASP D C   1 
ATOM   10225 O  O   . ASP D 2 180 ? 117.199 132.173 178.303 1.00 145.13 ? 157 ASP D O   1 
ATOM   10226 C  CB  . ASP D 2 180 ? 114.402 133.875 177.462 1.00 144.61 ? 157 ASP D CB  1 
ATOM   10227 C  CG  . ASP D 2 180 ? 113.582 134.719 176.506 1.00 145.00 ? 157 ASP D CG  1 
ATOM   10228 O  OD1 . ASP D 2 180 ? 114.115 135.724 175.991 1.00 144.52 ? 157 ASP D OD1 1 
ATOM   10229 O  OD2 . ASP D 2 180 ? 112.406 134.375 176.265 1.00 144.87 ? 157 ASP D OD2 1 
ATOM   10230 N  N   . ASP D 2 181 ? 117.160 134.395 178.688 1.00 147.22 ? 158 ASP D N   1 
ATOM   10231 C  CA  . ASP D 2 181 ? 118.016 134.302 179.862 1.00 147.35 ? 158 ASP D CA  1 
ATOM   10232 C  C   . ASP D 2 181 ? 117.238 133.702 181.025 1.00 147.24 ? 158 ASP D C   1 
ATOM   10233 O  O   . ASP D 2 181 ? 116.119 134.132 181.323 1.00 146.66 ? 158 ASP D O   1 
ATOM   10234 C  CB  . ASP D 2 181 ? 118.547 135.683 180.241 1.00 145.56 ? 158 ASP D CB  1 
ATOM   10235 C  CG  . ASP D 2 181 ? 119.714 136.117 179.380 1.00 145.81 ? 158 ASP D CG  1 
ATOM   10236 O  OD1 . ASP D 2 181 ? 120.698 135.356 179.283 1.00 146.48 ? 158 ASP D OD1 1 
ATOM   10237 O  OD2 . ASP D 2 181 ? 119.650 137.221 178.801 1.00 145.77 ? 158 ASP D OD2 1 
ATOM   10238 N  N   . ILE D 2 182 ? 117.826 132.707 181.684 1.00 152.66 ? 159 ILE D N   1 
ATOM   10239 C  CA  . ILE D 2 182 ? 117.238 132.086 182.865 1.00 153.50 ? 159 ILE D CA  1 
ATOM   10240 C  C   . ILE D 2 182 ? 118.201 132.293 184.023 1.00 154.46 ? 159 ILE D C   1 
ATOM   10241 O  O   . ILE D 2 182 ? 119.375 131.914 183.931 1.00 153.28 ? 159 ILE D O   1 
ATOM   10242 C  CB  . ILE D 2 182 ? 116.952 130.593 182.648 1.00 153.39 ? 159 ILE D CB  1 
ATOM   10243 C  CG1 . ILE D 2 182 ? 116.028 130.398 181.445 1.00 153.35 ? 159 ILE D CG1 1 
ATOM   10244 C  CG2 . ILE D 2 182 ? 116.341 129.983 183.899 1.00 153.59 ? 159 ILE D CG2 1 
ATOM   10245 C  CD1 . ILE D 2 182 ? 115.734 128.950 181.132 1.00 154.03 ? 159 ILE D CD1 1 
ATOM   10246 N  N   . ALA D 2 183 ? 117.708 132.891 185.105 1.00 161.70 ? 160 ALA D N   1 
ATOM   10247 C  CA  . ALA D 2 183 ? 118.528 133.247 186.256 1.00 160.59 ? 160 ALA D CA  1 
ATOM   10248 C  C   . ALA D 2 183 ? 117.966 132.605 187.515 1.00 160.38 ? 160 ALA D C   1 
ATOM   10249 O  O   . ALA D 2 183 ? 116.754 132.639 187.749 1.00 159.27 ? 160 ALA D O   1 
ATOM   10250 C  CB  . ALA D 2 183 ? 118.603 134.766 186.428 1.00 160.02 ? 160 ALA D CB  1 
ATOM   10251 N  N   . ILE D 2 184 ? 118.852 132.023 188.319 1.00 168.52 ? 161 ILE D N   1 
ATOM   10252 C  CA  . ILE D 2 184 ? 118.506 131.451 189.614 1.00 169.21 ? 161 ILE D CA  1 
ATOM   10253 C  C   . ILE D 2 184 ? 119.526 131.932 190.635 1.00 170.47 ? 161 ILE D C   1 
ATOM   10254 O  O   . ILE D 2 184 ? 120.735 131.795 190.418 1.00 170.23 ? 161 ILE D O   1 
ATOM   10255 C  CB  . ILE D 2 184 ? 118.458 129.913 189.568 1.00 169.40 ? 161 ILE D CB  1 
ATOM   10256 C  CG1 . ILE D 2 184 ? 117.103 129.457 189.034 1.00 169.30 ? 161 ILE D CG1 1 
ATOM   10257 C  CG2 . ILE D 2 184 ? 118.726 129.316 190.941 1.00 169.56 ? 161 ILE D CG2 1 
ATOM   10258 C  CD1 . ILE D 2 184 ? 115.971 129.656 190.019 1.00 168.63 ? 161 ILE D CD1 1 
ATOM   10259 N  N   . GLU D 2 185 ? 119.042 132.480 191.748 1.00 180.43 ? 162 GLU D N   1 
ATOM   10260 C  CA  . GLU D 2 185 ? 119.895 133.119 192.737 1.00 179.98 ? 162 GLU D CA  1 
ATOM   10261 C  C   . GLU D 2 185 ? 119.573 132.594 194.129 1.00 180.34 ? 162 GLU D C   1 
ATOM   10262 O  O   . GLU D 2 185 ? 118.437 132.208 194.418 1.00 180.27 ? 162 GLU D O   1 
ATOM   10263 C  CB  . GLU D 2 185 ? 119.724 134.641 192.705 1.00 178.50 ? 162 GLU D CB  1 
ATOM   10264 C  CG  . GLU D 2 185 ? 120.981 135.423 193.022 1.00 179.51 ? 162 GLU D CG  1 
ATOM   10265 C  CD  . GLU D 2 185 ? 121.129 136.654 192.150 1.00 180.26 ? 162 GLU D CD  1 
ATOM   10266 O  OE1 . GLU D 2 185 ? 120.418 136.746 191.127 1.00 179.83 ? 162 GLU D OE1 1 
ATOM   10267 O  OE2 . GLU D 2 185 ? 121.953 137.530 192.489 1.00 180.08 ? 162 GLU D OE2 1 
ATOM   10268 N  N   . GLU D 2 186 ? 120.590 132.586 194.993 1.00 186.26 ? 163 GLU D N   1 
ATOM   10269 C  CA  . GLU D 2 186 ? 120.420 132.223 196.400 1.00 186.62 ? 163 GLU D CA  1 
ATOM   10270 C  C   . GLU D 2 186 ? 119.965 133.473 197.149 1.00 186.71 ? 163 GLU D C   1 
ATOM   10271 O  O   . GLU D 2 186 ? 120.718 134.119 197.882 1.00 186.11 ? 163 GLU D O   1 
ATOM   10272 C  CB  . GLU D 2 186 ? 121.713 131.652 196.973 1.00 186.16 ? 163 GLU D CB  1 
ATOM   10273 C  CG  . GLU D 2 186 ? 121.613 131.173 198.419 1.00 186.06 ? 163 GLU D CG  1 
ATOM   10274 C  CD  . GLU D 2 186 ? 120.767 129.923 198.569 1.00 186.22 ? 163 GLU D CD  1 
ATOM   10275 O  OE1 . GLU D 2 186 ? 120.920 128.996 197.746 1.00 186.30 ? 163 GLU D OE1 1 
ATOM   10276 O  OE2 . GLU D 2 186 ? 119.948 129.867 199.510 1.00 186.14 ? 163 GLU D OE2 1 
ATOM   10277 N  N   . SER D 2 187 ? 118.694 133.824 196.941 1.00 186.39 ? 164 SER D N   1 
ATOM   10278 C  CA  . SER D 2 187 ? 118.173 135.076 197.478 1.00 185.66 ? 164 SER D CA  1 
ATOM   10279 C  C   . SER D 2 187 ? 117.989 135.007 198.989 1.00 186.02 ? 164 SER D C   1 
ATOM   10280 O  O   . SER D 2 187 ? 118.259 135.984 199.697 1.00 185.94 ? 164 SER D O   1 
ATOM   10281 C  CB  . SER D 2 187 ? 116.853 135.430 196.794 1.00 184.26 ? 164 SER D CB  1 
ATOM   10282 O  OG  . SER D 2 187 ? 116.346 136.665 197.269 1.00 183.98 ? 164 SER D OG  1 
ATOM   10283 N  N   . ASN D 2 188 ? 117.534 133.868 199.502 1.00 187.34 ? 165 ASN D N   1 
ATOM   10284 C  CA  . ASN D 2 188 ? 117.205 133.742 200.922 1.00 187.20 ? 165 ASN D CA  1 
ATOM   10285 C  C   . ASN D 2 188 ? 118.423 133.359 201.759 1.00 187.03 ? 165 ASN D C   1 
ATOM   10286 O  O   . ASN D 2 188 ? 118.385 132.410 202.542 1.00 186.52 ? 165 ASN D O   1 
ATOM   10287 C  CB  . ASN D 2 188 ? 116.079 132.731 201.099 1.00 186.80 ? 165 ASN D CB  1 
ATOM   10288 C  CG  . ASN D 2 188 ? 114.831 133.108 200.325 1.00 186.56 ? 165 ASN D CG  1 
ATOM   10289 O  OD1 . ASN D 2 188 ? 114.094 134.012 200.716 1.00 186.72 ? 165 ASN D OD1 1 
ATOM   10290 N  ND2 . ASN D 2 188 ? 114.588 132.415 199.219 1.00 186.22 ? 165 ASN D ND2 1 
ATOM   10291 N  N   . ALA D 2 189 ? 119.508 134.116 201.608 1.00 188.78 ? 166 ALA D N   1 
ATOM   10292 C  CA  . ALA D 2 189 ? 120.736 133.901 202.364 1.00 188.26 ? 166 ALA D CA  1 
ATOM   10293 C  C   . ALA D 2 189 ? 121.694 135.045 202.060 1.00 188.85 ? 166 ALA D C   1 
ATOM   10294 O  O   . ALA D 2 189 ? 121.480 135.833 201.135 1.00 188.62 ? 166 ALA D O   1 
ATOM   10295 C  CB  . ALA D 2 189 ? 121.387 132.555 202.033 1.00 187.51 ? 166 ALA D CB  1 
ATOM   10296 N  N   . ILE D 2 190 ? 122.753 135.127 202.862 1.00 190.99 ? 167 ILE D N   1 
ATOM   10297 C  CA  . ILE D 2 190 ? 123.860 136.050 202.642 1.00 191.49 ? 167 ILE D CA  1 
ATOM   10298 C  C   . ILE D 2 190 ? 125.144 135.234 202.649 1.00 190.96 ? 167 ILE D C   1 
ATOM   10299 O  O   . ILE D 2 190 ? 125.361 134.422 203.556 1.00 189.78 ? 167 ILE D O   1 
ATOM   10300 C  CB  . ILE D 2 190 ? 123.902 137.162 203.706 1.00 190.88 ? 167 ILE D CB  1 
ATOM   10301 C  CG1 . ILE D 2 190 ? 122.625 138.003 203.645 1.00 189.77 ? 167 ILE D CG1 1 
ATOM   10302 C  CG2 . ILE D 2 190 ? 125.128 138.042 203.511 1.00 189.42 ? 167 ILE D CG2 1 
ATOM   10303 C  CD1 . ILE D 2 190 ? 122.545 139.073 204.709 1.00 188.89 ? 167 ILE D CD1 1 
ATOM   10304 N  N   . ILE D 2 191 ? 125.989 135.444 201.641 1.00 190.44 ? 168 ILE D N   1 
ATOM   10305 C  CA  . ILE D 2 191 ? 127.099 134.532 201.395 1.00 190.01 ? 168 ILE D CA  1 
ATOM   10306 C  C   . ILE D 2 191 ? 128.440 135.253 201.491 1.00 189.96 ? 168 ILE D C   1 
ATOM   10307 O  O   . ILE D 2 191 ? 129.461 134.641 201.821 1.00 189.64 ? 168 ILE D O   1 
ATOM   10308 C  CB  . ILE D 2 191 ? 126.929 133.845 200.026 1.00 189.35 ? 168 ILE D CB  1 
ATOM   10309 C  CG1 . ILE D 2 191 ? 127.992 132.766 199.819 1.00 189.29 ? 168 ILE D CG1 1 
ATOM   10310 C  CG2 . ILE D 2 191 ? 126.967 134.869 198.899 1.00 188.00 ? 168 ILE D CG2 1 
ATOM   10311 C  CD1 . ILE D 2 191 ? 127.662 131.804 198.704 1.00 188.68 ? 168 ILE D CD1 1 
ATOM   10312 N  N   . ASN D 2 192 ? 128.450 136.559 201.228 1.00 191.10 ? 169 ASN D N   1 
ATOM   10313 C  CA  . ASN D 2 192 ? 129.708 137.297 201.196 1.00 190.38 ? 169 ASN D CA  1 
ATOM   10314 C  C   . ASN D 2 192 ? 130.155 137.704 202.597 1.00 190.78 ? 169 ASN D C   1 
ATOM   10315 O  O   . ASN D 2 192 ? 130.440 138.879 202.851 1.00 191.02 ? 169 ASN D O   1 
ATOM   10316 C  CB  . ASN D 2 192 ? 129.581 138.524 200.288 1.00 190.07 ? 169 ASN D CB  1 
ATOM   10317 C  CG  . ASN D 2 192 ? 128.513 139.493 200.757 1.00 190.74 ? 169 ASN D CG  1 
ATOM   10318 O  OD1 . ASN D 2 192 ? 127.578 139.113 201.463 1.00 190.86 ? 169 ASN D OD1 1 
ATOM   10319 N  ND2 . ASN D 2 192 ? 128.649 140.756 200.369 1.00 189.83 ? 169 ASN D ND2 1 
ATOM   10320 N  N   . ASP D 2 193 ? 130.238 136.736 203.507 1.00 190.11 ? 170 ASP D N   1 
ATOM   10321 C  CA  . ASP D 2 193 ? 130.641 136.982 204.885 1.00 189.40 ? 170 ASP D CA  1 
ATOM   10322 C  C   . ASP D 2 193 ? 132.102 136.636 205.145 1.00 188.93 ? 170 ASP D C   1 
ATOM   10323 O  O   . ASP D 2 193 ? 132.533 136.646 206.302 1.00 188.27 ? 170 ASP D O   1 
ATOM   10324 C  CB  . ASP D 2 193 ? 129.742 136.200 205.845 1.00 188.61 ? 170 ASP D CB  1 
ATOM   10325 C  CG  . ASP D 2 193 ? 129.973 134.704 205.771 1.00 189.12 ? 170 ASP D CG  1 
ATOM   10326 O  OD1 . ASP D 2 193 ? 130.180 134.189 204.652 1.00 190.20 ? 170 ASP D OD1 1 
ATOM   10327 O  OD2 . ASP D 2 193 ? 129.946 134.043 206.829 1.00 188.64 ? 170 ASP D OD2 1 
ATOM   10328 N  N   . GLY D 2 194 ? 132.870 136.329 204.102 1.00 188.01 ? 171 GLY D N   1 
ATOM   10329 C  CA  . GLY D 2 194 ? 134.277 136.025 204.252 1.00 187.54 ? 171 GLY D CA  1 
ATOM   10330 C  C   . GLY D 2 194 ? 134.604 134.581 204.563 1.00 188.23 ? 171 GLY D C   1 
ATOM   10331 O  O   . GLY D 2 194 ? 135.790 134.239 204.651 1.00 187.84 ? 171 GLY D O   1 
ATOM   10332 N  N   . LYS D 2 195 ? 133.602 133.725 204.732 1.00 188.47 ? 172 LYS D N   1 
ATOM   10333 C  CA  . LYS D 2 195 ? 133.836 132.317 205.008 1.00 187.54 ? 172 LYS D CA  1 
ATOM   10334 C  C   . LYS D 2 195 ? 133.915 131.522 203.705 1.00 187.91 ? 172 LYS D C   1 
ATOM   10335 O  O   . LYS D 2 195 ? 133.637 132.027 202.615 1.00 187.85 ? 172 LYS D O   1 
ATOM   10336 C  CB  . LYS D 2 195 ? 132.737 131.759 205.913 1.00 186.86 ? 172 LYS D CB  1 
ATOM   10337 C  CG  . LYS D 2 195 ? 132.737 132.347 207.314 1.00 186.64 ? 172 LYS D CG  1 
ATOM   10338 C  CD  . LYS D 2 195 ? 134.086 132.158 207.990 1.00 186.67 ? 172 LYS D CD  1 
ATOM   10339 C  CE  . LYS D 2 195 ? 134.148 132.881 209.328 1.00 186.65 ? 172 LYS D CE  1 
ATOM   10340 N  NZ  . LYS D 2 195 ? 134.218 134.359 209.161 1.00 186.48 ? 172 LYS D NZ  1 
ATOM   10341 N  N   . TYR D 2 196 ? 134.306 130.257 203.831 1.00 186.09 ? 173 TYR D N   1 
ATOM   10342 C  CA  . TYR D 2 196 ? 134.457 129.384 202.674 1.00 185.77 ? 173 TYR D CA  1 
ATOM   10343 C  C   . TYR D 2 196 ? 133.102 128.791 202.306 1.00 185.22 ? 173 TYR D C   1 
ATOM   10344 O  O   . TYR D 2 196 ? 132.502 128.060 203.102 1.00 184.59 ? 173 TYR D O   1 
ATOM   10345 C  CB  . TYR D 2 196 ? 135.473 128.283 202.970 1.00 185.20 ? 173 TYR D CB  1 
ATOM   10346 C  CG  . TYR D 2 196 ? 135.947 127.532 201.746 1.00 185.49 ? 173 TYR D CG  1 
ATOM   10347 C  CD1 . TYR D 2 196 ? 136.851 128.106 200.861 1.00 185.25 ? 173 TYR D CD1 1 
ATOM   10348 C  CD2 . TYR D 2 196 ? 135.497 126.246 201.479 1.00 185.40 ? 173 TYR D CD2 1 
ATOM   10349 C  CE1 . TYR D 2 196 ? 137.289 127.423 199.743 1.00 185.23 ? 173 TYR D CE1 1 
ATOM   10350 C  CE2 . TYR D 2 196 ? 135.930 125.554 200.363 1.00 185.59 ? 173 TYR D CE2 1 
ATOM   10351 C  CZ  . TYR D 2 196 ? 136.826 126.147 199.499 1.00 185.78 ? 173 TYR D CZ  1 
ATOM   10352 O  OH  . TYR D 2 196 ? 137.258 125.461 198.388 1.00 184.98 ? 173 TYR D OH  1 
ATOM   10353 N  N   . HIS D 2 197 ? 132.621 129.107 201.106 1.00 185.81 ? 174 HIS D N   1 
ATOM   10354 C  CA  . HIS D 2 197 ? 131.333 128.630 200.619 1.00 186.21 ? 174 HIS D CA  1 
ATOM   10355 C  C   . HIS D 2 197 ? 131.536 127.871 199.317 1.00 185.92 ? 174 HIS D C   1 
ATOM   10356 O  O   . HIS D 2 197 ? 132.217 128.360 198.411 1.00 185.17 ? 174 HIS D O   1 
ATOM   10357 C  CB  . HIS D 2 197 ? 130.362 129.792 200.399 1.00 186.30 ? 174 HIS D CB  1 
ATOM   10358 C  CG  . HIS D 2 197 ? 130.234 130.706 201.576 1.00 186.15 ? 174 HIS D CG  1 
ATOM   10359 N  ND1 . HIS D 2 197 ? 129.503 130.379 202.698 1.00 185.93 ? 174 HIS D ND1 1 
ATOM   10360 C  CD2 . HIS D 2 197 ? 130.746 131.938 201.806 1.00 185.41 ? 174 HIS D CD2 1 
ATOM   10361 C  CE1 . HIS D 2 197 ? 129.569 131.371 203.567 1.00 185.92 ? 174 HIS D CE1 1 
ATOM   10362 N  NE2 . HIS D 2 197 ? 130.317 132.330 203.050 1.00 186.05 ? 174 HIS D NE2 1 
ATOM   10363 N  N   . VAL D 2 198 ? 130.939 126.688 199.220 1.00 181.84 ? 175 VAL D N   1 
ATOM   10364 C  CA  . VAL D 2 198 ? 131.021 125.859 198.023 1.00 181.78 ? 175 VAL D CA  1 
ATOM   10365 C  C   . VAL D 2 198 ? 129.691 125.939 197.288 1.00 181.26 ? 175 VAL D C   1 
ATOM   10366 O  O   . VAL D 2 198 ? 128.630 125.707 197.882 1.00 180.20 ? 175 VAL D O   1 
ATOM   10367 C  CB  . VAL D 2 198 ? 131.375 124.404 198.372 1.00 180.27 ? 175 VAL D CB  1 
ATOM   10368 C  CG1 . VAL D 2 198 ? 131.656 123.610 197.107 1.00 179.58 ? 175 VAL D CG1 1 
ATOM   10369 C  CG2 . VAL D 2 198 ? 132.571 124.360 199.310 1.00 179.22 ? 175 VAL D CG2 1 
ATOM   10370 N  N   . VAL D 2 199 ? 129.744 126.269 196.000 1.00 177.88 ? 176 VAL D N   1 
ATOM   10371 C  CA  . VAL D 2 199 ? 128.560 126.430 195.166 1.00 176.90 ? 176 VAL D CA  1 
ATOM   10372 C  C   . VAL D 2 199 ? 128.632 125.429 194.022 1.00 176.18 ? 176 VAL D C   1 
ATOM   10373 O  O   . VAL D 2 199 ? 129.658 125.329 193.336 1.00 176.29 ? 176 VAL D O   1 
ATOM   10374 C  CB  . VAL D 2 199 ? 128.431 127.868 194.629 1.00 176.61 ? 176 VAL D CB  1 
ATOM   10375 C  CG1 . VAL D 2 199 ? 127.842 128.776 195.689 1.00 176.75 ? 176 VAL D CG1 1 
ATOM   10376 C  CG2 . VAL D 2 199 ? 129.785 128.394 194.177 1.00 175.98 ? 176 VAL D CG2 1 
ATOM   10377 N  N   . ARG D 2 200 ? 127.542 124.691 193.824 1.00 168.01 ? 177 ARG D N   1 
ATOM   10378 C  CA  . ARG D 2 200 ? 127.405 123.744 192.730 1.00 168.20 ? 177 ARG D CA  1 
ATOM   10379 C  C   . ARG D 2 200 ? 126.120 124.042 191.970 1.00 168.47 ? 177 ARG D C   1 
ATOM   10380 O  O   . ARG D 2 200 ? 125.178 124.637 192.501 1.00 167.87 ? 177 ARG D O   1 
ATOM   10381 C  CB  . ARG D 2 200 ? 127.405 122.292 193.230 1.00 168.03 ? 177 ARG D CB  1 
ATOM   10382 C  CG  . ARG D 2 200 ? 128.574 121.948 194.143 1.00 168.17 ? 177 ARG D CG  1 
ATOM   10383 C  CD  . ARG D 2 200 ? 128.388 120.587 194.795 1.00 168.06 ? 177 ARG D CD  1 
ATOM   10384 N  NE  . ARG D 2 200 ? 129.155 120.461 196.028 1.00 168.62 ? 177 ARG D NE  1 
ATOM   10385 C  CZ  . ARG D 2 200 ? 130.372 119.939 196.104 1.00 168.48 ? 177 ARG D CZ  1 
ATOM   10386 N  NH1 . ARG D 2 200 ? 130.995 119.481 195.031 1.00 168.10 ? 177 ARG D NH1 1 
ATOM   10387 N  NH2 . ARG D 2 200 ? 130.978 119.875 197.286 1.00 168.64 ? 177 ARG D NH2 1 
ATOM   10388 N  N   . PHE D 2 201 ? 126.094 123.616 190.712 1.00 159.98 ? 178 PHE D N   1 
ATOM   10389 C  CA  . PHE D 2 201 ? 125.016 123.980 189.800 1.00 158.81 ? 178 PHE D CA  1 
ATOM   10390 C  C   . PHE D 2 201 ? 124.904 122.911 188.727 1.00 157.77 ? 178 PHE D C   1 
ATOM   10391 O  O   . PHE D 2 201 ? 125.845 122.705 187.956 1.00 156.84 ? 178 PHE D O   1 
ATOM   10392 C  CB  . PHE D 2 201 ? 125.282 125.354 189.184 1.00 159.39 ? 178 PHE D CB  1 
ATOM   10393 C  CG  . PHE D 2 201 ? 124.634 125.565 187.850 1.00 159.20 ? 178 PHE D CG  1 
ATOM   10394 C  CD1 . PHE D 2 201 ? 123.258 125.648 187.738 1.00 159.09 ? 178 PHE D CD1 1 
ATOM   10395 C  CD2 . PHE D 2 201 ? 125.405 125.705 186.709 1.00 157.86 ? 178 PHE D CD2 1 
ATOM   10396 C  CE1 . PHE D 2 201 ? 122.663 125.852 186.511 1.00 158.25 ? 178 PHE D CE1 1 
ATOM   10397 C  CE2 . PHE D 2 201 ? 124.816 125.910 185.480 1.00 157.12 ? 178 PHE D CE2 1 
ATOM   10398 C  CZ  . PHE D 2 201 ? 123.444 125.984 185.382 1.00 158.12 ? 178 PHE D CZ  1 
ATOM   10399 N  N   . THR D 2 202 ? 123.761 122.233 188.685 1.00 155.67 ? 179 THR D N   1 
ATOM   10400 C  CA  . THR D 2 202 ? 123.498 121.178 187.716 1.00 156.05 ? 179 THR D CA  1 
ATOM   10401 C  C   . THR D 2 202 ? 122.440 121.648 186.728 1.00 155.50 ? 179 THR D C   1 
ATOM   10402 O  O   . THR D 2 202 ? 121.358 122.091 187.129 1.00 154.36 ? 179 THR D O   1 
ATOM   10403 C  CB  . THR D 2 202 ? 123.040 119.892 188.408 1.00 156.68 ? 179 THR D CB  1 
ATOM   10404 O  OG1 . THR D 2 202 ? 121.832 120.142 189.135 1.00 157.40 ? 179 THR D OG1 1 
ATOM   10405 C  CG2 . THR D 2 202 ? 124.110 119.392 189.367 1.00 155.66 ? 179 THR D CG2 1 
ATOM   10406 N  N   . ARG D 2 203 ? 122.753 121.539 185.440 1.00 141.06 ? 180 ARG D N   1 
ATOM   10407 C  CA  . ARG D 2 203 ? 121.893 122.021 184.369 1.00 140.04 ? 180 ARG D CA  1 
ATOM   10408 C  C   . ARG D 2 203 ? 121.423 120.845 183.527 1.00 139.94 ? 180 ARG D C   1 
ATOM   10409 O  O   . ARG D 2 203 ? 122.208 119.941 183.227 1.00 140.11 ? 180 ARG D O   1 
ATOM   10410 C  CB  . ARG D 2 203 ? 122.634 123.032 183.494 1.00 138.85 ? 180 ARG D CB  1 
ATOM   10411 C  CG  . ARG D 2 203 ? 121.757 124.132 182.940 1.00 138.43 ? 180 ARG D CG  1 
ATOM   10412 C  CD  . ARG D 2 203 ? 121.276 123.785 181.548 1.00 137.38 ? 180 ARG D CD  1 
ATOM   10413 N  NE  . ARG D 2 203 ? 122.339 123.888 180.558 1.00 137.22 ? 180 ARG D NE  1 
ATOM   10414 C  CZ  . ARG D 2 203 ? 122.154 123.771 179.252 1.00 138.44 ? 180 ARG D CZ  1 
ATOM   10415 N  NH1 . ARG D 2 203 ? 120.955 123.550 178.742 1.00 140.70 ? 180 ARG D NH1 1 
ATOM   10416 N  NH2 . ARG D 2 203 ? 123.198 123.880 178.437 1.00 137.73 ? 180 ARG D NH2 1 
ATOM   10417 N  N   . SER D 2 204 ? 120.143 120.855 183.155 1.00 140.26 ? 181 SER D N   1 
ATOM   10418 C  CA  . SER D 2 204 ? 119.581 119.853 182.248 1.00 139.68 ? 181 SER D CA  1 
ATOM   10419 C  C   . SER D 2 204 ? 118.601 120.576 181.331 1.00 139.48 ? 181 SER D C   1 
ATOM   10420 O  O   . SER D 2 204 ? 117.419 120.711 181.662 1.00 140.56 ? 181 SER D O   1 
ATOM   10421 C  CB  . SER D 2 204 ? 118.899 118.726 183.013 1.00 137.99 ? 181 SER D CB  1 
ATOM   10422 O  OG  . SER D 2 204 ? 119.815 117.690 183.321 1.00 136.61 ? 181 SER D OG  1 
ATOM   10423 N  N   . GLY D 2 205 ? 119.093 121.032 180.183 1.00 132.07 ? 182 GLY D N   1 
ATOM   10424 C  CA  . GLY D 2 205 ? 118.236 121.761 179.264 1.00 131.43 ? 182 GLY D CA  1 
ATOM   10425 C  C   . GLY D 2 205 ? 117.719 123.035 179.895 1.00 131.59 ? 182 GLY D C   1 
ATOM   10426 O  O   . GLY D 2 205 ? 118.474 123.971 180.174 1.00 131.95 ? 182 GLY D O   1 
ATOM   10427 N  N   . GLY D 2 206 ? 116.407 123.087 180.111 1.00 141.50 ? 183 GLY D N   1 
ATOM   10428 C  CA  . GLY D 2 206 ? 115.823 124.213 180.809 1.00 142.87 ? 183 GLY D CA  1 
ATOM   10429 C  C   . GLY D 2 206 ? 115.842 124.111 182.318 1.00 144.66 ? 183 GLY D C   1 
ATOM   10430 O  O   . GLY D 2 206 ? 115.792 125.141 182.996 1.00 143.89 ? 183 GLY D O   1 
ATOM   10431 N  N   . ASN D 2 207 ? 115.933 122.900 182.859 1.00 149.39 ? 184 ASN D N   1 
ATOM   10432 C  CA  . ASN D 2 207 ? 115.916 122.711 184.301 1.00 147.46 ? 184 ASN D CA  1 
ATOM   10433 C  C   . ASN D 2 207 ? 117.268 123.075 184.900 1.00 148.16 ? 184 ASN D C   1 
ATOM   10434 O  O   . ASN D 2 207 ? 118.319 122.788 184.320 1.00 148.56 ? 184 ASN D O   1 
ATOM   10435 C  CB  . ASN D 2 207 ? 115.561 121.264 184.642 1.00 146.93 ? 184 ASN D CB  1 
ATOM   10436 C  CG  . ASN D 2 207 ? 114.279 120.808 183.975 1.00 148.36 ? 184 ASN D CG  1 
ATOM   10437 O  OD1 . ASN D 2 207 ? 113.377 121.608 183.729 1.00 147.00 ? 184 ASN D OD1 1 
ATOM   10438 N  ND2 . ASN D 2 207 ? 114.193 119.517 183.677 1.00 149.95 ? 184 ASN D ND2 1 
ATOM   10439 N  N   . ALA D 2 208 ? 117.238 123.711 186.070 1.00 158.48 ? 185 ALA D N   1 
ATOM   10440 C  CA  . ALA D 2 208 ? 118.470 124.142 186.722 1.00 158.64 ? 185 ALA D CA  1 
ATOM   10441 C  C   . ALA D 2 208 ? 118.361 123.970 188.229 1.00 160.04 ? 185 ALA D C   1 
ATOM   10442 O  O   . ALA D 2 208 ? 117.371 124.393 188.830 1.00 160.47 ? 185 ALA D O   1 
ATOM   10443 C  CB  . ALA D 2 208 ? 118.791 125.602 186.383 1.00 157.94 ? 185 ALA D CB  1 
ATOM   10444 N  N   . THR D 2 209 ? 119.379 123.364 188.840 1.00 166.33 ? 186 THR D N   1 
ATOM   10445 C  CA  . THR D 2 209 ? 119.431 123.190 190.288 1.00 166.67 ? 186 THR D CA  1 
ATOM   10446 C  C   . THR D 2 209 ? 120.697 123.847 190.816 1.00 165.80 ? 186 THR D C   1 
ATOM   10447 O  O   . THR D 2 209 ? 121.806 123.464 190.429 1.00 164.52 ? 186 THR D O   1 
ATOM   10448 C  CB  . THR D 2 209 ? 119.403 121.710 190.681 1.00 165.55 ? 186 THR D CB  1 
ATOM   10449 O  OG1 . THR D 2 209 ? 120.740 121.196 190.700 1.00 166.18 ? 186 THR D OG1 1 
ATOM   10450 C  CG2 . THR D 2 209 ? 118.568 120.903 189.696 1.00 164.72 ? 186 THR D CG2 1 
ATOM   10451 N  N   . LEU D 2 210 ? 120.532 124.819 191.707 1.00 169.03 ? 187 LEU D N   1 
ATOM   10452 C  CA  . LEU D 2 210 ? 121.645 125.549 192.296 1.00 169.60 ? 187 LEU D CA  1 
ATOM   10453 C  C   . LEU D 2 210 ? 121.708 125.258 193.788 1.00 171.00 ? 187 LEU D C   1 
ATOM   10454 O  O   . LEU D 2 210 ? 120.713 125.428 194.500 1.00 170.62 ? 187 LEU D O   1 
ATOM   10455 C  CB  . LEU D 2 210 ? 121.501 127.053 192.053 1.00 169.02 ? 187 LEU D CB  1 
ATOM   10456 C  CG  . LEU D 2 210 ? 122.656 127.938 192.524 1.00 169.55 ? 187 LEU D CG  1 
ATOM   10457 C  CD1 . LEU D 2 210 ? 123.938 127.592 191.784 1.00 168.73 ? 187 LEU D CD1 1 
ATOM   10458 C  CD2 . LEU D 2 210 ? 122.313 129.410 192.349 1.00 169.01 ? 187 LEU D CD2 1 
ATOM   10459 N  N   . GLN D 2 211 ? 122.876 124.825 194.260 1.00 173.70 ? 188 GLN D N   1 
ATOM   10460 C  CA  . GLN D 2 211 ? 123.077 124.482 195.658 1.00 172.91 ? 188 GLN D CA  1 
ATOM   10461 C  C   . GLN D 2 211 ? 124.305 125.206 196.187 1.00 172.66 ? 188 GLN D C   1 
ATOM   10462 O  O   . GLN D 2 211 ? 125.283 125.414 195.466 1.00 171.83 ? 188 GLN D O   1 
ATOM   10463 C  CB  . GLN D 2 211 ? 123.247 122.966 195.844 1.00 172.66 ? 188 GLN D CB  1 
ATOM   10464 C  CG  . GLN D 2 211 ? 123.330 122.516 197.295 1.00 172.70 ? 188 GLN D CG  1 
ATOM   10465 C  CD  . GLN D 2 211 ? 123.999 121.166 197.446 1.00 172.37 ? 188 GLN D CD  1 
ATOM   10466 O  OE1 . GLN D 2 211 ? 125.122 120.962 196.986 1.00 171.78 ? 188 GLN D OE1 1 
ATOM   10467 N  NE2 . GLN D 2 211 ? 123.309 120.232 198.091 1.00 172.50 ? 188 GLN D NE2 1 
ATOM   10468 N  N   . VAL D 2 212 ? 124.238 125.601 197.455 1.00 181.55 ? 189 VAL D N   1 
ATOM   10469 C  CA  . VAL D 2 212 ? 125.361 126.224 198.144 1.00 181.82 ? 189 VAL D CA  1 
ATOM   10470 C  C   . VAL D 2 212 ? 125.490 125.603 199.529 1.00 182.58 ? 189 VAL D C   1 
ATOM   10471 O  O   . VAL D 2 212 ? 124.512 125.537 200.281 1.00 181.97 ? 189 VAL D O   1 
ATOM   10472 C  CB  . VAL D 2 212 ? 125.206 127.757 198.219 1.00 181.62 ? 189 VAL D CB  1 
ATOM   10473 C  CG1 . VAL D 2 212 ? 123.879 128.142 198.847 1.00 181.76 ? 189 VAL D CG1 1 
ATOM   10474 C  CG2 . VAL D 2 212 ? 126.358 128.365 198.998 1.00 181.35 ? 189 VAL D CG2 1 
ATOM   10475 N  N   . ASP D 2 213 ? 126.696 125.128 199.852 1.00 183.91 ? 190 ASP D N   1 
ATOM   10476 C  CA  . ASP D 2 213 ? 126.995 124.505 201.138 1.00 183.83 ? 190 ASP D CA  1 
ATOM   10477 C  C   . ASP D 2 213 ? 126.030 123.368 201.451 1.00 183.63 ? 190 ASP D C   1 
ATOM   10478 O  O   . ASP D 2 213 ? 126.013 122.345 200.759 1.00 182.49 ? 190 ASP D O   1 
ATOM   10479 C  CB  . ASP D 2 213 ? 126.962 125.547 202.259 1.00 183.31 ? 190 ASP D CB  1 
ATOM   10480 C  CG  . ASP D 2 213 ? 127.591 126.860 201.849 1.00 183.14 ? 190 ASP D CG  1 
ATOM   10481 O  OD1 . ASP D 2 213 ? 128.571 126.832 201.076 1.00 183.66 ? 190 ASP D OD1 1 
ATOM   10482 O  OD2 . ASP D 2 213 ? 127.104 127.921 202.293 1.00 182.61 ? 190 ASP D OD2 1 
ATOM   10483 N  N   . SER D 2 214 ? 125.226 123.543 202.498 1.00 188.41 ? 191 SER D N   1 
ATOM   10484 C  CA  . SER D 2 214 ? 124.225 122.565 202.893 1.00 188.11 ? 191 SER D CA  1 
ATOM   10485 C  C   . SER D 2 214 ? 122.805 123.096 202.784 1.00 188.42 ? 191 SER D C   1 
ATOM   10486 O  O   . SER D 2 214 ? 121.863 122.384 203.151 1.00 188.24 ? 191 SER D O   1 
ATOM   10487 C  CB  . SER D 2 214 ? 124.483 122.091 204.330 1.00 188.07 ? 191 SER D CB  1 
ATOM   10488 O  OG  . SER D 2 214 ? 124.501 123.186 205.231 1.00 187.52 ? 191 SER D OG  1 
ATOM   10489 N  N   . TRP D 2 215 ? 122.624 124.322 202.301 1.00 188.62 ? 192 TRP D N   1 
ATOM   10490 C  CA  . TRP D 2 215 ? 121.294 124.893 202.185 1.00 188.42 ? 192 TRP D CA  1 
ATOM   10491 C  C   . TRP D 2 215 ? 120.498 124.167 201.101 1.00 188.51 ? 192 TRP D C   1 
ATOM   10492 O  O   . TRP D 2 215 ? 121.077 123.614 200.161 1.00 187.73 ? 192 TRP D O   1 
ATOM   10493 C  CB  . TRP D 2 215 ? 121.385 126.385 201.877 1.00 187.73 ? 192 TRP D CB  1 
ATOM   10494 C  CG  . TRP D 2 215 ? 121.800 127.197 203.068 1.00 188.06 ? 192 TRP D CG  1 
ATOM   10495 C  CD1 . TRP D 2 215 ? 121.475 126.959 204.372 1.00 188.12 ? 192 TRP D CD1 1 
ATOM   10496 C  CD2 . TRP D 2 215 ? 122.624 128.370 203.070 1.00 188.80 ? 192 TRP D CD2 1 
ATOM   10497 N  NE1 . TRP D 2 215 ? 122.039 127.912 205.183 1.00 188.43 ? 192 TRP D NE1 1 
ATOM   10498 C  CE2 . TRP D 2 215 ? 122.750 128.790 204.408 1.00 189.02 ? 192 TRP D CE2 1 
ATOM   10499 C  CE3 . TRP D 2 215 ? 123.263 129.107 202.070 1.00 188.50 ? 192 TRP D CE3 1 
ATOM   10500 C  CZ2 . TRP D 2 215 ? 123.490 129.913 204.772 1.00 188.55 ? 192 TRP D CZ2 1 
ATOM   10501 C  CZ3 . TRP D 2 215 ? 123.999 130.221 202.433 1.00 188.52 ? 192 TRP D CZ3 1 
ATOM   10502 C  CH2 . TRP D 2 215 ? 124.105 130.614 203.772 1.00 188.40 ? 192 TRP D CH2 1 
ATOM   10503 N  N   . PRO D 2 216 ? 119.168 124.140 201.219 1.00 183.72 ? 193 PRO D N   1 
ATOM   10504 C  CA  . PRO D 2 216 ? 118.359 123.366 200.268 1.00 183.50 ? 193 PRO D CA  1 
ATOM   10505 C  C   . PRO D 2 216 ? 118.558 123.836 198.835 1.00 183.72 ? 193 PRO D C   1 
ATOM   10506 O  O   . PRO D 2 216 ? 118.748 125.024 198.567 1.00 183.47 ? 193 PRO D O   1 
ATOM   10507 C  CB  . PRO D 2 216 ? 116.921 123.604 200.746 1.00 182.60 ? 193 PRO D CB  1 
ATOM   10508 C  CG  . PRO D 2 216 ? 116.992 124.808 201.636 1.00 182.04 ? 193 PRO D CG  1 
ATOM   10509 C  CD  . PRO D 2 216 ? 118.341 124.754 202.270 1.00 182.25 ? 193 PRO D CD  1 
ATOM   10510 N  N   . VAL D 2 217 ? 118.515 122.877 197.910 1.00 176.98 ? 194 VAL D N   1 
ATOM   10511 C  CA  . VAL D 2 217 ? 118.780 123.163 196.507 1.00 175.92 ? 194 VAL D CA  1 
ATOM   10512 C  C   . VAL D 2 217 ? 117.621 123.951 195.915 1.00 176.37 ? 194 VAL D C   1 
ATOM   10513 O  O   . VAL D 2 217 ? 116.450 123.582 196.075 1.00 175.56 ? 194 VAL D O   1 
ATOM   10514 C  CB  . VAL D 2 217 ? 119.016 121.859 195.730 1.00 175.99 ? 194 VAL D CB  1 
ATOM   10515 C  CG1 . VAL D 2 217 ? 119.377 122.163 194.290 1.00 175.86 ? 194 VAL D CG1 1 
ATOM   10516 C  CG2 . VAL D 2 217 ? 120.101 121.030 196.397 1.00 175.75 ? 194 VAL D CG2 1 
ATOM   10517 N  N   . ILE D 2 218 ? 117.942 125.042 195.230 1.00 177.09 ? 195 ILE D N   1 
ATOM   10518 C  CA  . ILE D 2 218 ? 116.953 125.836 194.511 1.00 177.30 ? 195 ILE D CA  1 
ATOM   10519 C  C   . ILE D 2 218 ? 116.758 125.213 193.136 1.00 176.65 ? 195 ILE D C   1 
ATOM   10520 O  O   . ILE D 2 218 ? 117.719 125.063 192.372 1.00 176.07 ? 195 ILE D O   1 
ATOM   10521 C  CB  . ILE D 2 218 ? 117.390 127.303 194.394 1.00 176.67 ? 195 ILE D CB  1 
ATOM   10522 C  CG1 . ILE D 2 218 ? 117.913 127.813 195.736 1.00 176.28 ? 195 ILE D CG1 1 
ATOM   10523 C  CG2 . ILE D 2 218 ? 116.235 128.162 193.910 1.00 175.33 ? 195 ILE D CG2 1 
ATOM   10524 C  CD1 . ILE D 2 218 ? 118.362 129.251 195.699 1.00 174.99 ? 195 ILE D CD1 1 
ATOM   10525 N  N   . GLU D 2 219 ? 115.518 124.856 192.817 1.00 168.54 ? 196 GLU D N   1 
ATOM   10526 C  CA  . GLU D 2 219 ? 115.186 124.196 191.564 1.00 168.36 ? 196 GLU D CA  1 
ATOM   10527 C  C   . GLU D 2 219 ? 114.382 125.135 190.675 1.00 168.17 ? 196 GLU D C   1 
ATOM   10528 O  O   . GLU D 2 219 ? 113.559 125.916 191.162 1.00 167.98 ? 196 GLU D O   1 
ATOM   10529 C  CB  . GLU D 2 219 ? 114.397 122.908 191.815 1.00 168.07 ? 196 GLU D CB  1 
ATOM   10530 C  CG  . GLU D 2 219 ? 115.175 121.840 192.565 1.00 168.06 ? 196 GLU D CG  1 
ATOM   10531 C  CD  . GLU D 2 219 ? 114.326 120.630 192.903 1.00 168.60 ? 196 GLU D CD  1 
ATOM   10532 O  OE1 . GLU D 2 219 ? 113.102 120.675 192.659 1.00 167.50 ? 196 GLU D OE1 1 
ATOM   10533 O  OE2 . GLU D 2 219 ? 114.883 119.633 193.410 1.00 168.84 ? 196 GLU D OE2 1 
ATOM   10534 N  N   . ARG D 2 220 ? 114.632 125.056 189.369 1.00 159.41 ? 197 ARG D N   1 
ATOM   10535 C  CA  . ARG D 2 220 ? 113.968 125.896 188.382 1.00 158.74 ? 197 ARG D CA  1 
ATOM   10536 C  C   . ARG D 2 220 ? 113.549 125.030 187.206 1.00 158.59 ? 197 ARG D C   1 
ATOM   10537 O  O   . ARG D 2 220 ? 114.393 124.362 186.596 1.00 159.18 ? 197 ARG D O   1 
ATOM   10538 C  CB  . ARG D 2 220 ? 114.887 127.022 187.909 1.00 159.24 ? 197 ARG D CB  1 
ATOM   10539 C  CG  . ARG D 2 220 ? 114.377 127.788 186.701 1.00 159.38 ? 197 ARG D CG  1 
ATOM   10540 C  CD  . ARG D 2 220 ? 113.119 128.568 187.033 1.00 159.02 ? 197 ARG D CD  1 
ATOM   10541 N  NE  . ARG D 2 220 ? 112.805 129.554 186.006 1.00 158.76 ? 197 ARG D NE  1 
ATOM   10542 C  CZ  . ARG D 2 220 ? 113.246 130.804 186.009 1.00 158.58 ? 197 ARG D CZ  1 
ATOM   10543 N  NH1 . ARG D 2 220 ? 114.031 131.258 186.972 1.00 158.16 ? 197 ARG D NH1 1 
ATOM   10544 N  NH2 . ARG D 2 220 ? 112.890 131.620 185.021 1.00 158.57 ? 197 ARG D NH2 1 
ATOM   10545 N  N   . TYR D 2 221 ? 112.253 125.054 186.894 1.00 155.26 ? 198 TYR D N   1 
ATOM   10546 C  CA  . TYR D 2 221 ? 111.670 124.333 185.763 1.00 155.59 ? 198 TYR D CA  1 
ATOM   10547 C  C   . TYR D 2 221 ? 110.847 125.332 184.961 1.00 155.52 ? 198 TYR D C   1 
ATOM   10548 O  O   . TYR D 2 221 ? 109.626 125.431 185.138 1.00 155.89 ? 198 TYR D O   1 
ATOM   10549 C  CB  . TYR D 2 221 ? 110.805 123.161 186.230 1.00 155.23 ? 198 TYR D CB  1 
ATOM   10550 C  CG  . TYR D 2 221 ? 111.570 122.001 186.832 1.00 156.94 ? 198 TYR D CG  1 
ATOM   10551 C  CD1 . TYR D 2 221 ? 112.227 122.130 188.050 1.00 156.07 ? 198 TYR D CD1 1 
ATOM   10552 C  CD2 . TYR D 2 221 ? 111.621 120.772 186.188 1.00 156.70 ? 198 TYR D CD2 1 
ATOM   10553 C  CE1 . TYR D 2 221 ? 112.923 121.072 188.603 1.00 155.72 ? 198 TYR D CE1 1 
ATOM   10554 C  CE2 . TYR D 2 221 ? 112.314 119.708 186.735 1.00 156.74 ? 198 TYR D CE2 1 
ATOM   10555 C  CZ  . TYR D 2 221 ? 112.963 119.863 187.942 1.00 156.20 ? 198 TYR D CZ  1 
ATOM   10556 O  OH  . TYR D 2 221 ? 113.654 118.807 188.488 1.00 154.75 ? 198 TYR D OH  1 
ATOM   10557 N  N   . PRO D 2 222 ? 111.487 126.103 184.081 1.00 154.64 ? 199 PRO D N   1 
ATOM   10558 C  CA  . PRO D 2 222 ? 110.756 127.132 183.331 1.00 154.09 ? 199 PRO D CA  1 
ATOM   10559 C  C   . PRO D 2 222 ? 109.702 126.528 182.415 1.00 154.22 ? 199 PRO D C   1 
ATOM   10560 O  O   . PRO D 2 222 ? 109.834 125.402 181.931 1.00 154.48 ? 199 PRO D O   1 
ATOM   10561 C  CB  . PRO D 2 222 ? 111.857 127.837 182.528 1.00 153.25 ? 199 PRO D CB  1 
ATOM   10562 C  CG  . PRO D 2 222 ? 113.130 127.494 183.229 1.00 153.62 ? 199 PRO D CG  1 
ATOM   10563 C  CD  . PRO D 2 222 ? 112.926 126.121 183.782 1.00 154.46 ? 199 PRO D CD  1 
ATOM   10564 N  N   . ALA D 2 223 ? 108.645 127.298 182.182 1.00 157.13 ? 200 ALA D N   1 
ATOM   10565 C  CA  . ALA D 2 223 ? 107.521 126.856 181.373 1.00 158.24 ? 200 ALA D CA  1 
ATOM   10566 C  C   . ALA D 2 223 ? 107.746 127.178 179.898 1.00 158.21 ? 200 ALA D C   1 
ATOM   10567 O  O   . ALA D 2 223 ? 108.618 127.968 179.530 1.00 157.27 ? 200 ALA D O   1 
ATOM   10568 C  CB  . ALA D 2 223 ? 106.222 127.502 181.856 1.00 157.08 ? 200 ALA D CB  1 
ATOM   10569 N  N   . GLY D 2 224 ? 106.932 126.549 179.051 1.00 151.42 ? 201 GLY D N   1 
ATOM   10570 C  CA  . GLY D 2 224 ? 107.014 126.754 177.621 1.00 149.98 ? 201 GLY D CA  1 
ATOM   10571 C  C   . GLY D 2 224 ? 108.081 125.898 176.966 1.00 150.56 ? 201 GLY D C   1 
ATOM   10572 O  O   . GLY D 2 224 ? 108.798 125.125 177.604 1.00 149.43 ? 201 GLY D O   1 
ATOM   10573 N  N   . ARG D 2 225 ? 108.193 126.054 175.641 1.00 145.50 ? 232 ARG D N   1 
ATOM   10574 C  CA  . ARG D 2 225 ? 109.191 125.319 174.829 1.00 143.72 ? 232 ARG D CA  1 
ATOM   10575 C  C   . ARG D 2 225 ? 110.542 125.929 175.173 1.00 144.31 ? 232 ARG D C   1 
ATOM   10576 O  O   . ARG D 2 225 ? 110.613 127.155 175.149 1.00 143.69 ? 232 ARG D O   1 
ATOM   10577 C  CB  . ARG D 2 225 ? 108.899 125.573 173.350 1.00 142.73 ? 232 ARG D CB  1 
ATOM   10578 C  CG  . ARG D 2 225 ? 109.317 124.443 172.425 1.00 144.08 ? 232 ARG D CG  1 
ATOM   10579 C  CD  . ARG D 2 225 ? 110.429 124.886 171.491 1.00 145.01 ? 232 ARG D CD  1 
ATOM   10580 N  NE  . ARG D 2 225 ? 110.890 123.978 170.438 1.00 146.65 ? 232 ARG D NE  1 
ATOM   10581 C  CZ  . ARG D 2 225 ? 110.821 122.647 170.410 1.00 145.40 ? 232 ARG D CZ  1 
ATOM   10582 N  NH1 . ARG D 2 225 ? 110.264 121.965 171.395 1.00 144.29 ? 232 ARG D NH1 1 
ATOM   10583 N  NH2 . ARG D 2 225 ? 111.302 122.002 169.365 1.00 144.34 ? 232 ARG D NH2 1 
ATOM   10584 N  N   . GLN D 2 226 ? 111.540 125.107 175.496 1.00 140.60 ? 233 GLN D N   1 
ATOM   10585 C  CA  . GLN D 2 226 ? 112.865 125.560 175.888 1.00 139.77 ? 233 GLN D CA  1 
ATOM   10586 C  C   . GLN D 2 226 ? 113.922 124.868 175.043 1.00 139.66 ? 233 GLN D C   1 
ATOM   10587 O  O   . GLN D 2 226 ? 113.841 123.662 174.797 1.00 139.38 ? 233 GLN D O   1 
ATOM   10588 C  CB  . GLN D 2 226 ? 113.130 125.282 177.374 1.00 139.46 ? 233 GLN D CB  1 
ATOM   10589 C  CG  . GLN D 2 226 ? 112.228 126.048 178.328 1.00 141.08 ? 233 GLN D CG  1 
ATOM   10590 C  CD  . GLN D 2 226 ? 112.591 127.515 178.424 1.00 141.12 ? 233 GLN D CD  1 
ATOM   10591 O  OE1 . GLN D 2 226 ? 113.764 127.881 178.366 1.00 140.71 ? 233 GLN D OE1 1 
ATOM   10592 N  NE2 . GLN D 2 226 ? 111.582 128.366 178.571 1.00 140.19 ? 233 GLN D NE2 1 
ATOM   10593 N  N   . LEU D 2 227 ? 114.907 125.641 174.597 1.00 126.92 ? 234 LEU D N   1 
ATOM   10594 C  CA  . LEU D 2 227 ? 116.095 125.062 173.994 1.00 126.72 ? 234 LEU D CA  1 
ATOM   10595 C  C   . LEU D 2 227 ? 116.977 124.468 175.083 1.00 129.06 ? 234 LEU D C   1 
ATOM   10596 O  O   . LEU D 2 227 ? 116.924 124.878 176.245 1.00 131.56 ? 234 LEU D O   1 
ATOM   10597 C  CB  . LEU D 2 227 ? 116.868 126.112 173.197 1.00 123.39 ? 234 LEU D CB  1 
ATOM   10598 C  CG  . LEU D 2 227 ? 116.087 126.869 172.124 1.00 122.73 ? 234 LEU D CG  1 
ATOM   10599 C  CD1 . LEU D 2 227 ? 117.041 127.555 171.166 1.00 124.92 ? 234 LEU D CD1 1 
ATOM   10600 C  CD2 . LEU D 2 227 ? 115.155 125.941 171.369 1.00 123.35 ? 234 LEU D CD2 1 
ATOM   10601 N  N   . THR D 2 228 ? 117.791 123.489 174.702 1.00 118.66 ? 235 THR D N   1 
ATOM   10602 C  CA  . THR D 2 228 ? 118.556 122.724 175.674 1.00 116.94 ? 235 THR D CA  1 
ATOM   10603 C  C   . THR D 2 228 ? 120.057 122.720 175.435 1.00 117.89 ? 235 THR D C   1 
ATOM   10604 O  O   . THR D 2 228 ? 120.814 122.629 176.402 1.00 120.77 ? 235 THR D O   1 
ATOM   10605 C  CB  . THR D 2 228 ? 118.069 121.269 175.705 1.00 116.41 ? 235 THR D CB  1 
ATOM   10606 O  OG1 . THR D 2 228 ? 118.301 120.662 174.429 1.00 116.13 ? 235 THR D OG1 1 
ATOM   10607 C  CG2 . THR D 2 228 ? 116.586 121.210 176.021 1.00 116.27 ? 235 THR D CG2 1 
ATOM   10608 N  N   . ILE D 2 229 ? 120.509 122.825 174.192 1.00 109.11 ? 236 ILE D N   1 
ATOM   10609 C  CA  . ILE D 2 229 ? 121.902 122.560 173.853 1.00 108.74 ? 236 ILE D CA  1 
ATOM   10610 C  C   . ILE D 2 229 ? 122.730 123.829 174.005 1.00 109.03 ? 236 ILE D C   1 
ATOM   10611 O  O   . ILE D 2 229 ? 122.397 124.875 173.437 1.00 109.79 ? 236 ILE D O   1 
ATOM   10612 C  CB  . ILE D 2 229 ? 122.020 121.994 172.431 1.00 104.26 ? 236 ILE D CB  1 
ATOM   10613 C  CG1 . ILE D 2 229 ? 121.330 120.638 172.352 1.00 104.88 ? 236 ILE D CG1 1 
ATOM   10614 C  CG2 . ILE D 2 229 ? 123.473 121.854 172.041 1.00 107.08 ? 236 ILE D CG2 1 
ATOM   10615 C  CD1 . ILE D 2 229 ? 122.020 119.568 173.154 1.00 108.97 ? 236 ILE D CD1 1 
ATOM   10616 N  N   . PHE D 2 230 ? 123.814 123.728 174.774 1.00 117.48 ? 237 PHE D N   1 
ATOM   10617 C  CA  . PHE D 2 230 ? 124.816 124.785 174.898 1.00 115.86 ? 237 PHE D CA  1 
ATOM   10618 C  C   . PHE D 2 230 ? 125.787 124.618 173.737 1.00 115.78 ? 237 PHE D C   1 
ATOM   10619 O  O   . PHE D 2 230 ? 126.701 123.794 173.793 1.00 120.16 ? 237 PHE D O   1 
ATOM   10620 C  CB  . PHE D 2 230 ? 125.523 124.685 176.243 1.00 117.46 ? 237 PHE D CB  1 
ATOM   10621 C  CG  . PHE D 2 230 ? 126.108 125.977 176.727 1.00 116.64 ? 237 PHE D CG  1 
ATOM   10622 C  CD1 . PHE D 2 230 ? 126.915 126.742 175.909 1.00 116.63 ? 237 PHE D CD1 1 
ATOM   10623 C  CD2 . PHE D 2 230 ? 125.853 126.423 178.010 1.00 119.62 ? 237 PHE D CD2 1 
ATOM   10624 C  CE1 . PHE D 2 230 ? 127.454 127.927 176.360 1.00 119.93 ? 237 PHE D CE1 1 
ATOM   10625 C  CE2 . PHE D 2 230 ? 126.388 127.607 178.465 1.00 120.29 ? 237 PHE D CE2 1 
ATOM   10626 C  CZ  . PHE D 2 230 ? 127.190 128.359 177.639 1.00 120.45 ? 237 PHE D CZ  1 
ATOM   10627 N  N   . ASN D 2 231 ? 125.599 125.408 172.685 1.00 106.44 ? 238 ASN D N   1 
ATOM   10628 C  CA  . ASN D 2 231 ? 126.256 125.143 171.411 1.00 108.54 ? 238 ASN D CA  1 
ATOM   10629 C  C   . ASN D 2 231 ? 127.667 125.719 171.387 1.00 106.88 ? 238 ASN D C   1 
ATOM   10630 O  O   . ASN D 2 231 ? 127.861 126.914 171.624 1.00 106.83 ? 238 ASN D O   1 
ATOM   10631 C  CB  . ASN D 2 231 ? 125.429 125.717 170.265 1.00 107.53 ? 238 ASN D CB  1 
ATOM   10632 C  CG  . ASN D 2 231 ? 124.064 125.083 170.166 1.00 106.26 ? 238 ASN D CG  1 
ATOM   10633 O  OD1 . ASN D 2 231 ? 123.109 125.538 170.794 1.00 106.99 ? 238 ASN D OD1 1 
ATOM   10634 N  ND2 . ASN D 2 231 ? 123.963 124.019 169.378 1.00 104.89 ? 238 ASN D ND2 1 
ATOM   10635 N  N   . SER D 2 232 ? 128.643 124.857 171.099 1.00 114.36 ? 239 SER D N   1 
ATOM   10636 C  CA  . SER D 2 232 ? 129.995 125.256 170.708 1.00 113.73 ? 239 SER D CA  1 
ATOM   10637 C  C   . SER D 2 232 ? 130.640 126.186 171.736 1.00 117.32 ? 239 SER D C   1 
ATOM   10638 O  O   . SER D 2 232 ? 130.941 127.349 171.462 1.00 119.33 ? 239 SER D O   1 
ATOM   10639 C  CB  . SER D 2 232 ? 129.982 125.901 169.319 1.00 114.04 ? 239 SER D CB  1 
ATOM   10640 O  OG  . SER D 2 232 ? 131.299 126.069 168.830 1.00 116.64 ? 239 SER D OG  1 
ATOM   10641 N  N   . GLN D 2 233 ? 130.849 125.650 172.936 1.00 124.83 ? 240 GLN D N   1 
ATOM   10642 C  CA  . GLN D 2 233 ? 131.575 126.391 173.958 1.00 125.06 ? 240 GLN D CA  1 
ATOM   10643 C  C   . GLN D 2 233 ? 133.010 126.631 173.507 1.00 126.91 ? 240 GLN D C   1 
ATOM   10644 O  O   . GLN D 2 233 ? 133.687 125.712 173.039 1.00 126.31 ? 240 GLN D O   1 
ATOM   10645 C  CB  . GLN D 2 233 ? 131.546 125.625 175.279 1.00 124.29 ? 240 GLN D CB  1 
ATOM   10646 C  CG  . GLN D 2 233 ? 130.224 125.732 176.010 1.00 123.59 ? 240 GLN D CG  1 
ATOM   10647 C  CD  . GLN D 2 233 ? 129.875 124.477 176.779 1.00 125.65 ? 240 GLN D CD  1 
ATOM   10648 O  OE1 . GLN D 2 233 ? 130.535 123.448 176.644 1.00 127.53 ? 240 GLN D OE1 1 
ATOM   10649 N  NE2 . GLN D 2 233 ? 128.829 124.555 177.591 1.00 124.89 ? 240 GLN D NE2 1 
ATOM   10650 N  N   . ALA D 2 234 ? 133.471 127.875 173.640 1.00 135.51 ? 241 ALA D N   1 
ATOM   10651 C  CA  . ALA D 2 234 ? 134.769 128.284 173.122 1.00 135.08 ? 241 ALA D CA  1 
ATOM   10652 C  C   . ALA D 2 234 ? 135.799 128.500 174.223 1.00 137.40 ? 241 ALA D C   1 
ATOM   10653 O  O   . ALA D 2 234 ? 136.866 127.882 174.200 1.00 137.10 ? 241 ALA D O   1 
ATOM   10654 C  CB  . ALA D 2 234 ? 134.617 129.558 172.282 1.00 133.63 ? 241 ALA D CB  1 
ATOM   10655 N  N   . THR D 2 235 ? 135.514 129.372 175.188 1.00 149.69 ? 242 THR D N   1 
ATOM   10656 C  CA  . THR D 2 235 ? 136.468 129.700 176.236 1.00 150.57 ? 242 THR D CA  1 
ATOM   10657 C  C   . THR D 2 235 ? 135.768 129.708 177.585 1.00 149.57 ? 242 THR D C   1 
ATOM   10658 O  O   . THR D 2 235 ? 134.559 129.934 177.675 1.00 147.45 ? 242 THR D O   1 
ATOM   10659 C  CB  . THR D 2 235 ? 137.132 131.070 176.019 1.00 149.78 ? 242 THR D CB  1 
ATOM   10660 O  OG1 . THR D 2 235 ? 136.125 132.088 175.964 1.00 150.71 ? 242 THR D OG1 1 
ATOM   10661 C  CG2 . THR D 2 235 ? 137.936 131.088 174.731 1.00 149.18 ? 242 THR D CG2 1 
ATOM   10662 N  N   . ILE D 2 236 ? 136.547 129.465 178.634 1.00 158.98 ? 243 ILE D N   1 
ATOM   10663 C  CA  . ILE D 2 236 ? 136.092 129.617 180.009 1.00 159.46 ? 243 ILE D CA  1 
ATOM   10664 C  C   . ILE D 2 236 ? 136.927 130.713 180.658 1.00 159.96 ? 243 ILE D C   1 
ATOM   10665 O  O   . ILE D 2 236 ? 138.165 130.700 180.572 1.00 159.22 ? 243 ILE D O   1 
ATOM   10666 C  CB  . ILE D 2 236 ? 136.171 128.294 180.797 1.00 158.19 ? 243 ILE D CB  1 
ATOM   10667 C  CG1 . ILE D 2 236 ? 135.807 128.516 182.265 1.00 157.85 ? 243 ILE D CG1 1 
ATOM   10668 C  CG2 . ILE D 2 236 ? 137.527 127.666 180.676 1.00 157.57 ? 243 ILE D CG2 1 
ATOM   10669 C  CD1 . ILE D 2 236 ? 134.445 129.111 182.458 1.00 157.03 ? 243 ILE D CD1 1 
ATOM   10670 N  N   . ILE D 2 237 ? 136.238 131.665 181.284 1.00 167.07 ? 244 ILE D N   1 
ATOM   10671 C  CA  . ILE D 2 237 ? 136.815 132.897 181.804 1.00 166.47 ? 244 ILE D CA  1 
ATOM   10672 C  C   . ILE D 2 237 ? 136.605 132.907 183.311 1.00 167.41 ? 244 ILE D C   1 
ATOM   10673 O  O   . ILE D 2 237 ? 135.483 132.688 183.782 1.00 166.81 ? 244 ILE D O   1 
ATOM   10674 C  CB  . ILE D 2 237 ? 136.148 134.132 181.167 1.00 165.90 ? 244 ILE D CB  1 
ATOM   10675 C  CG1 . ILE D 2 237 ? 136.725 134.423 179.784 1.00 166.09 ? 244 ILE D CG1 1 
ATOM   10676 C  CG2 . ILE D 2 237 ? 136.310 135.354 182.062 1.00 165.80 ? 244 ILE D CG2 1 
ATOM   10677 C  CD1 . ILE D 2 237 ? 138.192 134.635 179.780 1.00 165.65 ? 244 ILE D CD1 1 
ATOM   10678 N  N   . ILE D 2 238 ? 137.673 133.157 184.070 1.00 174.37 ? 245 ILE D N   1 
ATOM   10679 C  CA  . ILE D 2 238 ? 137.557 133.329 185.513 1.00 174.23 ? 245 ILE D CA  1 
ATOM   10680 C  C   . ILE D 2 238 ? 138.179 134.663 185.901 1.00 174.29 ? 245 ILE D C   1 
ATOM   10681 O  O   . ILE D 2 238 ? 139.305 134.972 185.494 1.00 174.04 ? 245 ILE D O   1 
ATOM   10682 C  CB  . ILE D 2 238 ? 138.206 132.171 186.295 1.00 173.83 ? 245 ILE D CB  1 
ATOM   10683 C  CG1 . ILE D 2 238 ? 138.028 130.851 185.544 1.00 173.96 ? 245 ILE D CG1 1 
ATOM   10684 C  CG2 . ILE D 2 238 ? 137.606 132.073 187.683 1.00 173.17 ? 245 ILE D CG2 1 
ATOM   10685 C  CD1 . ILE D 2 238 ? 138.981 129.767 185.971 1.00 173.25 ? 245 ILE D CD1 1 
ATOM   10686 N  N   . GLY D 2 239 ? 137.444 135.446 186.687 1.00 178.92 ? 246 GLY D N   1 
ATOM   10687 C  CA  . GLY D 2 239 ? 137.879 136.766 187.100 1.00 179.64 ? 246 GLY D CA  1 
ATOM   10688 C  C   . GLY D 2 239 ? 136.878 137.848 186.752 1.00 179.76 ? 246 GLY D C   1 
ATOM   10689 O  O   . GLY D 2 239 ? 136.629 138.755 187.552 1.00 179.55 ? 246 GLY D O   1 
ATOM   10690 N  N   . GLY D 2 240 ? 136.290 137.756 185.561 1.00 181.90 ? 247 GLY D N   1 
ATOM   10691 C  CA  . GLY D 2 240 ? 135.240 138.678 185.159 1.00 181.82 ? 247 GLY D CA  1 
ATOM   10692 C  C   . GLY D 2 240 ? 135.664 140.126 185.063 1.00 182.32 ? 247 GLY D C   1 
ATOM   10693 O  O   . GLY D 2 240 ? 134.857 141.020 185.339 1.00 181.37 ? 247 GLY D O   1 
ATOM   10694 N  N   . LYS D 2 241 ? 136.913 140.388 184.676 1.00 179.95 ? 248 LYS D N   1 
ATOM   10695 C  CA  . LYS D 2 241 ? 137.362 141.769 184.536 1.00 178.98 ? 248 LYS D CA  1 
ATOM   10696 C  C   . LYS D 2 241 ? 136.806 142.417 183.272 1.00 179.04 ? 248 LYS D C   1 
ATOM   10697 O  O   . LYS D 2 241 ? 136.411 143.588 183.295 1.00 178.51 ? 248 LYS D O   1 
ATOM   10698 C  CB  . LYS D 2 241 ? 138.889 141.830 184.541 1.00 178.68 ? 248 LYS D CB  1 
ATOM   10699 C  CG  . LYS D 2 241 ? 139.453 143.231 184.384 1.00 178.49 ? 248 LYS D CG  1 
ATOM   10700 C  CD  . LYS D 2 241 ? 140.971 143.220 184.383 1.00 178.05 ? 248 LYS D CD  1 
ATOM   10701 C  CE  . LYS D 2 241 ? 141.528 144.583 184.007 1.00 177.74 ? 248 LYS D CE  1 
ATOM   10702 N  NZ  . LYS D 2 241 ? 140.941 145.669 184.838 1.00 177.94 ? 248 LYS D NZ  1 
ATOM   10703 N  N   . GLU D 2 242 ? 136.768 141.674 182.162 1.00 176.75 ? 249 GLU D N   1 
ATOM   10704 C  CA  . GLU D 2 242 ? 136.291 142.245 180.907 1.00 176.16 ? 249 GLU D CA  1 
ATOM   10705 C  C   . GLU D 2 242 ? 134.788 142.493 180.929 1.00 176.09 ? 249 GLU D C   1 
ATOM   10706 O  O   . GLU D 2 242 ? 134.297 143.371 180.211 1.00 175.15 ? 249 GLU D O   1 
ATOM   10707 C  CB  . GLU D 2 242 ? 136.653 141.329 179.738 1.00 175.48 ? 249 GLU D CB  1 
ATOM   10708 C  CG  . GLU D 2 242 ? 138.145 141.204 179.477 1.00 174.90 ? 249 GLU D CG  1 
ATOM   10709 C  CD  . GLU D 2 242 ? 138.475 140.060 178.538 1.00 175.41 ? 249 GLU D CD  1 
ATOM   10710 O  OE1 . GLU D 2 242 ? 137.537 139.491 177.941 1.00 176.13 ? 249 GLU D OE1 1 
ATOM   10711 O  OE2 . GLU D 2 242 ? 139.671 139.727 178.400 1.00 175.05 ? 249 GLU D OE2 1 
ATOM   10712 N  N   . GLN D 2 243 ? 134.045 141.730 181.735 1.00 175.81 ? 250 GLN D N   1 
ATOM   10713 C  CA  . GLN D 2 243 ? 132.595 141.886 181.774 1.00 175.61 ? 250 GLN D CA  1 
ATOM   10714 C  C   . GLN D 2 243 ? 132.198 143.254 182.312 1.00 174.97 ? 250 GLN D C   1 
ATOM   10715 O  O   . GLN D 2 243 ? 131.238 143.865 181.829 1.00 173.95 ? 250 GLN D O   1 
ATOM   10716 C  CB  . GLN D 2 243 ? 131.972 140.774 182.617 1.00 174.99 ? 250 GLN D CB  1 
ATOM   10717 C  CG  . GLN D 2 243 ? 131.579 139.541 181.822 1.00 175.30 ? 250 GLN D CG  1 
ATOM   10718 C  CD  . GLN D 2 243 ? 132.771 138.854 181.186 1.00 175.63 ? 250 GLN D CD  1 
ATOM   10719 O  OE1 . GLN D 2 243 ? 133.851 138.790 181.773 1.00 175.10 ? 250 GLN D OE1 1 
ATOM   10720 N  NE2 . GLN D 2 243 ? 132.581 138.337 179.978 1.00 174.91 ? 250 GLN D NE2 1 
ATOM   10721 N  N   . GLY D 2 244 ? 132.921 143.748 183.313 1.00 179.91 ? 251 GLY D N   1 
ATOM   10722 C  CA  . GLY D 2 244 ? 132.633 145.048 183.885 1.00 180.26 ? 251 GLY D CA  1 
ATOM   10723 C  C   . GLY D 2 244 ? 132.547 145.023 185.396 1.00 180.63 ? 251 GLY D C   1 
ATOM   10724 O  O   . GLY D 2 244 ? 132.440 146.072 186.038 1.00 180.33 ? 251 GLY D O   1 
ATOM   10725 N  N   . GLN D 2 245 ? 132.593 143.826 185.978 1.00 182.01 ? 252 GLN D N   1 
ATOM   10726 C  CA  . GLN D 2 245 ? 132.516 143.636 187.426 1.00 181.84 ? 252 GLN D CA  1 
ATOM   10727 C  C   . GLN D 2 245 ? 133.674 142.748 187.860 1.00 182.77 ? 252 GLN D C   1 
ATOM   10728 O  O   . GLN D 2 245 ? 133.500 141.541 188.076 1.00 182.94 ? 252 GLN D O   1 
ATOM   10729 C  CB  . GLN D 2 245 ? 131.170 143.034 187.833 1.00 180.71 ? 252 GLN D CB  1 
ATOM   10730 C  CG  . GLN D 2 245 ? 129.964 143.769 187.269 1.00 181.08 ? 252 GLN D CG  1 
ATOM   10731 C  CD  . GLN D 2 245 ? 128.649 143.134 187.677 1.00 181.83 ? 252 GLN D CD  1 
ATOM   10732 O  OE1 . GLN D 2 245 ? 128.496 142.663 188.804 1.00 181.84 ? 252 GLN D OE1 1 
ATOM   10733 N  NE2 . GLN D 2 245 ? 127.691 143.118 186.758 1.00 181.96 ? 252 GLN D NE2 1 
ATOM   10734 N  N   . PRO D 2 246 ? 134.875 143.312 187.994 1.00 182.51 ? 253 PRO D N   1 
ATOM   10735 C  CA  . PRO D 2 246 ? 136.034 142.497 188.379 1.00 181.90 ? 253 PRO D CA  1 
ATOM   10736 C  C   . PRO D 2 246 ? 135.862 141.894 189.765 1.00 181.32 ? 253 PRO D C   1 
ATOM   10737 O  O   . PRO D 2 246 ? 135.172 142.443 190.627 1.00 180.89 ? 253 PRO D O   1 
ATOM   10738 C  CB  . PRO D 2 246 ? 137.200 143.494 188.343 1.00 180.76 ? 253 PRO D CB  1 
ATOM   10739 C  CG  . PRO D 2 246 ? 136.717 144.625 187.488 1.00 179.74 ? 253 PRO D CG  1 
ATOM   10740 C  CD  . PRO D 2 246 ? 135.246 144.714 187.740 1.00 180.50 ? 253 PRO D CD  1 
ATOM   10741 N  N   . PHE D 2 247 ? 136.496 140.743 189.967 1.00 183.59 ? 254 PHE D N   1 
ATOM   10742 C  CA  . PHE D 2 247 ? 136.377 139.979 191.200 1.00 184.22 ? 254 PHE D CA  1 
ATOM   10743 C  C   . PHE D 2 247 ? 137.691 140.006 191.970 1.00 185.16 ? 254 PHE D C   1 
ATOM   10744 O  O   . PHE D 2 247 ? 138.772 139.938 191.377 1.00 183.78 ? 254 PHE D O   1 
ATOM   10745 C  CB  . PHE D 2 247 ? 135.974 138.532 190.904 1.00 183.51 ? 254 PHE D CB  1 
ATOM   10746 C  CG  . PHE D 2 247 ? 136.155 137.601 192.067 1.00 183.39 ? 254 PHE D CG  1 
ATOM   10747 C  CD1 . PHE D 2 247 ? 135.239 137.582 193.103 1.00 183.60 ? 254 PHE D CD1 1 
ATOM   10748 C  CD2 . PHE D 2 247 ? 137.240 136.741 192.121 1.00 183.25 ? 254 PHE D CD2 1 
ATOM   10749 C  CE1 . PHE D 2 247 ? 135.401 136.727 194.173 1.00 184.24 ? 254 PHE D CE1 1 
ATOM   10750 C  CE2 . PHE D 2 247 ? 137.408 135.885 193.190 1.00 183.50 ? 254 PHE D CE2 1 
ATOM   10751 C  CZ  . PHE D 2 247 ? 136.486 135.877 194.217 1.00 184.11 ? 254 PHE D CZ  1 
ATOM   10752 N  N   . GLN D 2 248 ? 137.588 140.103 193.296 1.00 185.08 ? 255 GLN D N   1 
ATOM   10753 C  CA  . GLN D 2 248 ? 138.750 140.122 194.182 1.00 183.52 ? 255 GLN D CA  1 
ATOM   10754 C  C   . GLN D 2 248 ? 138.447 139.235 195.382 1.00 183.15 ? 255 GLN D C   1 
ATOM   10755 O  O   . GLN D 2 248 ? 137.653 139.613 196.249 1.00 182.35 ? 255 GLN D O   1 
ATOM   10756 C  CB  . GLN D 2 248 ? 139.085 141.546 194.624 1.00 182.36 ? 255 GLN D CB  1 
ATOM   10757 C  CG  . GLN D 2 248 ? 140.317 141.652 195.506 1.00 182.56 ? 255 GLN D CG  1 
ATOM   10758 C  CD  . GLN D 2 248 ? 140.590 143.074 195.956 1.00 182.31 ? 255 GLN D CD  1 
ATOM   10759 O  OE1 . GLN D 2 248 ? 139.727 143.946 195.854 1.00 181.90 ? 255 GLN D OE1 1 
ATOM   10760 N  NE2 . GLN D 2 248 ? 141.797 143.316 196.456 1.00 182.36 ? 255 GLN D NE2 1 
ATOM   10761 N  N   . GLY D 2 249 ? 139.077 138.064 195.435 1.00 183.66 ? 256 GLY D N   1 
ATOM   10762 C  CA  . GLY D 2 249 ? 138.848 137.124 196.515 1.00 183.57 ? 256 GLY D CA  1 
ATOM   10763 C  C   . GLY D 2 249 ? 139.650 135.848 196.365 1.00 183.67 ? 256 GLY D C   1 
ATOM   10764 O  O   . GLY D 2 249 ? 140.733 135.861 195.771 1.00 183.15 ? 256 GLY D O   1 
ATOM   10765 N  N   . GLN D 2 250 ? 139.139 134.738 196.895 1.00 186.12 ? 257 GLN D N   1 
ATOM   10766 C  CA  . GLN D 2 250 ? 139.819 133.453 196.810 1.00 186.22 ? 257 GLN D CA  1 
ATOM   10767 C  C   . GLN D 2 250 ? 138.898 132.412 196.190 1.00 186.66 ? 257 GLN D C   1 
ATOM   10768 O  O   . GLN D 2 250 ? 137.710 132.348 196.518 1.00 186.64 ? 257 GLN D O   1 
ATOM   10769 C  CB  . GLN D 2 250 ? 140.290 132.983 198.190 1.00 186.59 ? 257 GLN D CB  1 
ATOM   10770 C  CG  . GLN D 2 250 ? 141.217 133.965 198.892 1.00 186.56 ? 257 GLN D CG  1 
ATOM   10771 C  CD  . GLN D 2 250 ? 141.958 133.343 200.060 1.00 186.43 ? 257 GLN D CD  1 
ATOM   10772 O  OE1 . GLN D 2 250 ? 141.590 132.273 200.545 1.00 186.89 ? 257 GLN D OE1 1 
ATOM   10773 N  NE2 . GLN D 2 250 ? 143.012 134.011 200.514 1.00 185.29 ? 257 GLN D NE2 1 
ATOM   10774 N  N   . LEU D 2 251 ? 139.457 131.594 195.298 1.00 186.28 ? 258 LEU D N   1 
ATOM   10775 C  CA  . LEU D 2 251 ? 138.715 130.561 194.587 1.00 185.81 ? 258 LEU D CA  1 
ATOM   10776 C  C   . LEU D 2 251 ? 139.446 129.231 194.708 1.00 185.49 ? 258 LEU D C   1 
ATOM   10777 O  O   . LEU D 2 251 ? 140.654 129.186 194.944 1.00 185.57 ? 258 LEU D O   1 
ATOM   10778 C  CB  . LEU D 2 251 ? 138.533 130.917 193.106 1.00 185.44 ? 258 LEU D CB  1 
ATOM   10779 C  CG  . LEU D 2 251 ? 137.923 132.282 192.791 1.00 185.26 ? 258 LEU D CG  1 
ATOM   10780 C  CD1 . LEU D 2 251 ? 137.849 132.494 191.292 1.00 184.58 ? 258 LEU D CD1 1 
ATOM   10781 C  CD2 . LEU D 2 251 ? 136.548 132.403 193.416 1.00 184.63 ? 258 LEU D CD2 1 
ATOM   10782 N  N   . SER D 2 252 ? 138.701 128.139 194.541 1.00 186.34 ? 259 SER D N   1 
ATOM   10783 C  CA  . SER D 2 252 ? 139.282 126.806 194.639 1.00 186.16 ? 259 SER D CA  1 
ATOM   10784 C  C   . SER D 2 252 ? 138.442 125.810 193.853 1.00 186.25 ? 259 SER D C   1 
ATOM   10785 O  O   . SER D 2 252 ? 137.218 125.754 194.017 1.00 186.16 ? 259 SER D O   1 
ATOM   10786 C  CB  . SER D 2 252 ? 139.394 126.357 196.100 1.00 186.21 ? 259 SER D CB  1 
ATOM   10787 O  OG  . SER D 2 252 ? 140.309 127.166 196.818 1.00 187.19 ? 259 SER D OG  1 
ATOM   10788 N  N   . GLY D 2 253 ? 139.110 125.024 193.010 1.00 179.06 ? 260 GLY D N   1 
ATOM   10789 C  CA  . GLY D 2 253 ? 138.490 123.914 192.312 1.00 178.50 ? 260 GLY D CA  1 
ATOM   10790 C  C   . GLY D 2 253 ? 137.268 124.258 191.488 1.00 178.29 ? 260 GLY D C   1 
ATOM   10791 O  O   . GLY D 2 253 ? 136.152 123.871 191.843 1.00 178.41 ? 260 GLY D O   1 
ATOM   10792 N  N   . LEU D 2 254 ? 137.455 124.987 190.391 1.00 173.05 ? 261 LEU D N   1 
ATOM   10793 C  CA  . LEU D 2 254 ? 136.349 125.291 189.485 1.00 173.25 ? 261 LEU D CA  1 
ATOM   10794 C  C   . LEU D 2 254 ? 136.076 124.057 188.635 1.00 172.92 ? 261 LEU D C   1 
ATOM   10795 O  O   . LEU D 2 254 ? 136.732 123.828 187.616 1.00 171.83 ? 261 LEU D O   1 
ATOM   10796 C  CB  . LEU D 2 254 ? 136.669 126.501 188.616 1.00 172.93 ? 261 LEU D CB  1 
ATOM   10797 C  CG  . LEU D 2 254 ? 135.561 126.871 187.626 1.00 172.41 ? 261 LEU D CG  1 
ATOM   10798 C  CD1 . LEU D 2 254 ? 134.237 127.038 188.348 1.00 171.55 ? 261 LEU D CD1 1 
ATOM   10799 C  CD2 . LEU D 2 254 ? 135.910 128.130 186.858 1.00 172.12 ? 261 LEU D CD2 1 
ATOM   10800 N  N   . TYR D 2 255 ? 135.102 123.256 189.056 1.00 168.23 ? 262 TYR D N   1 
ATOM   10801 C  CA  . TYR D 2 255 ? 134.715 122.055 188.331 1.00 166.34 ? 262 TYR D CA  1 
ATOM   10802 C  C   . TYR D 2 255 ? 133.722 122.423 187.238 1.00 166.72 ? 262 TYR D C   1 
ATOM   10803 O  O   . TYR D 2 255 ? 132.728 123.107 187.501 1.00 166.98 ? 262 TYR D O   1 
ATOM   10804 C  CB  . TYR D 2 255 ? 134.103 121.026 189.281 1.00 165.78 ? 262 TYR D CB  1 
ATOM   10805 C  CG  . TYR D 2 255 ? 133.705 119.731 188.616 1.00 166.80 ? 262 TYR D CG  1 
ATOM   10806 C  CD1 . TYR D 2 255 ? 134.656 118.777 188.284 1.00 166.51 ? 262 TYR D CD1 1 
ATOM   10807 C  CD2 . TYR D 2 255 ? 132.375 119.459 188.324 1.00 167.73 ? 262 TYR D CD2 1 
ATOM   10808 C  CE1 . TYR D 2 255 ? 134.295 117.589 187.679 1.00 167.74 ? 262 TYR D CE1 1 
ATOM   10809 C  CE2 . TYR D 2 255 ? 132.004 118.274 187.716 1.00 168.01 ? 262 TYR D CE2 1 
ATOM   10810 C  CZ  . TYR D 2 255 ? 132.969 117.343 187.395 1.00 167.85 ? 262 TYR D CZ  1 
ATOM   10811 O  OH  . TYR D 2 255 ? 132.606 116.161 186.791 1.00 165.75 ? 262 TYR D OH  1 
ATOM   10812 N  N   . TYR D 2 256 ? 133.996 121.977 186.013 1.00 157.28 ? 263 TYR D N   1 
ATOM   10813 C  CA  . TYR D 2 256 ? 133.121 122.284 184.884 1.00 156.38 ? 263 TYR D CA  1 
ATOM   10814 C  C   . TYR D 2 256 ? 133.162 121.098 183.924 1.00 156.35 ? 263 TYR D C   1 
ATOM   10815 O  O   . TYR D 2 256 ? 134.069 121.004 183.092 1.00 155.85 ? 263 TYR D O   1 
ATOM   10816 C  CB  . TYR D 2 256 ? 133.543 123.574 184.195 1.00 155.05 ? 263 TYR D CB  1 
ATOM   10817 C  CG  . TYR D 2 256 ? 132.662 123.952 183.030 1.00 154.86 ? 263 TYR D CG  1 
ATOM   10818 C  CD1 . TYR D 2 256 ? 131.305 124.180 183.209 1.00 154.46 ? 263 TYR D CD1 1 
ATOM   10819 C  CD2 . TYR D 2 256 ? 133.183 124.074 181.751 1.00 155.03 ? 263 TYR D CD2 1 
ATOM   10820 C  CE1 . TYR D 2 256 ? 130.493 124.523 182.149 1.00 155.74 ? 263 TYR D CE1 1 
ATOM   10821 C  CE2 . TYR D 2 256 ? 132.378 124.416 180.684 1.00 155.08 ? 263 TYR D CE2 1 
ATOM   10822 C  CZ  . TYR D 2 256 ? 131.035 124.640 180.889 1.00 156.27 ? 263 TYR D CZ  1 
ATOM   10823 O  OH  . TYR D 2 256 ? 130.229 124.981 179.831 1.00 156.60 ? 263 TYR D OH  1 
ATOM   10824 N  N   . ASN D 2 257 ? 132.177 120.209 184.047 1.00 153.95 ? 264 ASN D N   1 
ATOM   10825 C  CA  . ASN D 2 257 ? 132.028 119.053 183.165 1.00 153.08 ? 264 ASN D CA  1 
ATOM   10826 C  C   . ASN D 2 257 ? 133.315 118.234 183.100 1.00 153.83 ? 264 ASN D C   1 
ATOM   10827 O  O   . ASN D 2 257 ? 133.847 117.943 182.027 1.00 154.57 ? 264 ASN D O   1 
ATOM   10828 C  CB  . ASN D 2 257 ? 131.585 119.489 181.768 1.00 153.14 ? 264 ASN D CB  1 
ATOM   10829 C  CG  . ASN D 2 257 ? 130.449 120.489 181.803 1.00 153.48 ? 264 ASN D CG  1 
ATOM   10830 O  OD1 . ASN D 2 257 ? 129.498 120.339 182.568 1.00 153.93 ? 264 ASN D OD1 1 
ATOM   10831 N  ND2 . ASN D 2 257 ? 130.542 121.517 180.970 1.00 152.30 ? 264 ASN D ND2 1 
ATOM   10832 N  N   . GLY D 2 258 ? 133.822 117.865 184.272 1.00 160.19 ? 265 GLY D N   1 
ATOM   10833 C  CA  . GLY D 2 258 ? 135.007 117.036 184.342 1.00 160.24 ? 265 GLY D CA  1 
ATOM   10834 C  C   . GLY D 2 258 ? 136.307 117.741 184.038 1.00 160.77 ? 265 GLY D C   1 
ATOM   10835 O  O   . GLY D 2 258 ? 137.321 117.066 183.825 1.00 161.53 ? 265 GLY D O   1 
ATOM   10836 N  N   . LEU D 2 259 ? 136.315 119.069 184.003 1.00 162.95 ? 266 LEU D N   1 
ATOM   10837 C  CA  . LEU D 2 259 ? 137.520 119.849 183.736 1.00 163.51 ? 266 LEU D CA  1 
ATOM   10838 C  C   . LEU D 2 259 ? 137.891 120.606 185.007 1.00 164.46 ? 266 LEU D C   1 
ATOM   10839 O  O   . LEU D 2 259 ? 137.261 121.611 185.349 1.00 165.18 ? 266 LEU D O   1 
ATOM   10840 C  CB  . LEU D 2 259 ? 137.307 120.801 182.564 1.00 162.42 ? 266 LEU D CB  1 
ATOM   10841 C  CG  . LEU D 2 259 ? 137.162 120.148 181.191 1.00 161.42 ? 266 LEU D CG  1 
ATOM   10842 C  CD1 . LEU D 2 259 ? 136.809 121.184 180.142 1.00 161.77 ? 266 LEU D CD1 1 
ATOM   10843 C  CD2 . LEU D 2 259 ? 138.439 119.416 180.815 1.00 161.54 ? 266 LEU D CD2 1 
ATOM   10844 N  N   . LYS D 2 260 ? 138.912 120.118 185.705 1.00 163.45 ? 267 LYS D N   1 
ATOM   10845 C  CA  . LYS D 2 260 ? 139.459 120.814 186.868 1.00 163.33 ? 267 LYS D CA  1 
ATOM   10846 C  C   . LYS D 2 260 ? 140.302 121.967 186.343 1.00 162.98 ? 267 LYS D C   1 
ATOM   10847 O  O   . LYS D 2 260 ? 141.512 121.847 186.146 1.00 162.89 ? 267 LYS D O   1 
ATOM   10848 C  CB  . LYS D 2 260 ? 140.269 119.861 187.737 1.00 161.84 ? 267 LYS D CB  1 
ATOM   10849 C  CG  . LYS D 2 260 ? 139.468 118.680 188.258 1.00 161.29 ? 267 LYS D CG  1 
ATOM   10850 C  CD  . LYS D 2 260 ? 140.267 117.859 189.254 1.00 161.49 ? 267 LYS D CD  1 
ATOM   10851 C  CE  . LYS D 2 260 ? 139.456 116.681 189.767 1.00 161.78 ? 267 LYS D CE  1 
ATOM   10852 N  NZ  . LYS D 2 260 ? 140.235 115.837 190.714 1.00 162.09 ? 267 LYS D NZ  1 
ATOM   10853 N  N   . VAL D 2 261 ? 139.641 123.102 186.106 1.00 168.03 ? 268 VAL D N   1 
ATOM   10854 C  CA  . VAL D 2 261 ? 140.285 124.218 185.417 1.00 168.45 ? 268 VAL D CA  1 
ATOM   10855 C  C   . VAL D 2 261 ? 141.427 124.782 186.254 1.00 169.68 ? 268 VAL D C   1 
ATOM   10856 O  O   . VAL D 2 261 ? 142.524 125.042 185.745 1.00 169.89 ? 268 VAL D O   1 
ATOM   10857 C  CB  . VAL D 2 261 ? 139.248 125.303 185.075 1.00 168.96 ? 268 VAL D CB  1 
ATOM   10858 C  CG1 . VAL D 2 261 ? 139.941 126.583 184.648 1.00 169.07 ? 268 VAL D CG1 1 
ATOM   10859 C  CG2 . VAL D 2 261 ? 138.308 124.811 183.989 1.00 168.86 ? 268 VAL D CG2 1 
ATOM   10860 N  N   . LEU D 2 262 ? 141.188 124.983 187.551 1.00 173.58 ? 269 LEU D N   1 
ATOM   10861 C  CA  . LEU D 2 262 ? 142.221 125.565 188.402 1.00 173.22 ? 269 LEU D CA  1 
ATOM   10862 C  C   . LEU D 2 262 ? 143.409 124.624 188.560 1.00 172.58 ? 269 LEU D C   1 
ATOM   10863 O  O   . LEU D 2 262 ? 144.562 125.069 188.572 1.00 172.29 ? 269 LEU D O   1 
ATOM   10864 C  CB  . LEU D 2 262 ? 141.634 125.934 189.764 1.00 172.62 ? 269 LEU D CB  1 
ATOM   10865 C  CG  . LEU D 2 262 ? 140.741 127.177 189.764 1.00 172.48 ? 269 LEU D CG  1 
ATOM   10866 C  CD1 . LEU D 2 262 ? 140.271 127.508 191.169 1.00 172.44 ? 269 LEU D CD1 1 
ATOM   10867 C  CD2 . LEU D 2 262 ? 141.467 128.362 189.146 1.00 172.71 ? 269 LEU D CD2 1 
ATOM   10868 N  N   . ASN D 2 263 ? 143.150 123.320 188.677 1.00 170.38 ? 270 ASN D N   1 
ATOM   10869 C  CA  . ASN D 2 263 ? 144.239 122.361 188.837 1.00 170.33 ? 270 ASN D CA  1 
ATOM   10870 C  C   . ASN D 2 263 ? 145.128 122.319 187.599 1.00 170.00 ? 270 ASN D C   1 
ATOM   10871 O  O   . ASN D 2 263 ? 146.360 122.333 187.706 1.00 170.03 ? 270 ASN D O   1 
ATOM   10872 C  CB  . ASN D 2 263 ? 143.675 120.975 189.143 1.00 169.45 ? 270 ASN D CB  1 
ATOM   10873 C  CG  . ASN D 2 263 ? 144.745 119.906 189.166 1.00 169.40 ? 270 ASN D CG  1 
ATOM   10874 O  OD1 . ASN D 2 263 ? 144.964 119.207 188.175 1.00 168.75 ? 270 ASN D OD1 1 
ATOM   10875 N  ND2 . ASN D 2 263 ? 145.425 119.775 190.299 1.00 170.04 ? 270 ASN D ND2 1 
ATOM   10876 N  N   . MET D 2 264 ? 144.523 122.272 186.410 1.00 171.64 ? 271 MET D N   1 
ATOM   10877 C  CA  . MET D 2 264 ? 145.322 122.260 185.189 1.00 171.52 ? 271 MET D CA  1 
ATOM   10878 C  C   . MET D 2 264 ? 146.003 123.603 184.954 1.00 172.01 ? 271 MET D C   1 
ATOM   10879 O  O   . MET D 2 264 ? 147.098 123.647 184.382 1.00 171.40 ? 271 MET D O   1 
ATOM   10880 C  CB  . MET D 2 264 ? 144.456 121.872 183.989 1.00 171.75 ? 271 MET D CB  1 
ATOM   10881 C  CG  . MET D 2 264 ? 143.299 122.814 183.703 1.00 172.38 ? 271 MET D CG  1 
ATOM   10882 S  SD  . MET D 2 264 ? 143.655 123.992 182.387 1.00 174.40 ? 271 MET D SD  1 
ATOM   10883 C  CE  . MET D 2 264 ? 143.699 122.900 180.970 1.00 171.05 ? 271 MET D CE  1 
ATOM   10884 N  N   . ALA D 2 265 ? 145.375 124.701 185.382 1.00 171.99 ? 272 ALA D N   1 
ATOM   10885 C  CA  . ALA D 2 265 ? 146.030 126.002 185.309 1.00 171.31 ? 272 ALA D CA  1 
ATOM   10886 C  C   . ALA D 2 265 ? 147.271 126.036 186.190 1.00 172.12 ? 272 ALA D C   1 
ATOM   10887 O  O   . ALA D 2 265 ? 148.305 126.591 185.802 1.00 171.51 ? 272 ALA D O   1 
ATOM   10888 C  CB  . ALA D 2 265 ? 145.053 127.104 185.715 1.00 170.78 ? 272 ALA D CB  1 
ATOM   10889 N  N   . ALA D 2 266 ? 147.180 125.453 187.388 1.00 172.61 ? 273 ALA D N   1 
ATOM   10890 C  CA  . ALA D 2 266 ? 148.356 125.316 188.239 1.00 172.02 ? 273 ALA D CA  1 
ATOM   10891 C  C   . ALA D 2 266 ? 149.391 124.391 187.614 1.00 172.05 ? 273 ALA D C   1 
ATOM   10892 O  O   . ALA D 2 266 ? 150.596 124.592 187.804 1.00 171.52 ? 273 ALA D O   1 
ATOM   10893 C  CB  . ALA D 2 266 ? 147.950 124.804 189.618 1.00 170.91 ? 273 ALA D CB  1 
ATOM   10894 N  N   . GLU D 2 267 ? 148.944 123.378 186.869 1.00 169.80 ? 274 GLU D N   1 
ATOM   10895 C  CA  . GLU D 2 267 ? 149.853 122.481 186.163 1.00 168.26 ? 274 GLU D CA  1 
ATOM   10896 C  C   . GLU D 2 267 ? 150.520 123.135 184.963 1.00 167.86 ? 274 GLU D C   1 
ATOM   10897 O  O   . GLU D 2 267 ? 151.387 122.504 184.348 1.00 166.71 ? 274 GLU D O   1 
ATOM   10898 C  CB  . GLU D 2 267 ? 149.110 121.221 185.714 1.00 168.11 ? 274 GLU D CB  1 
ATOM   10899 C  CG  . GLU D 2 267 ? 148.861 120.221 186.829 1.00 168.69 ? 274 GLU D CG  1 
ATOM   10900 C  CD  . GLU D 2 267 ? 150.144 119.770 187.501 1.00 168.76 ? 274 GLU D CD  1 
ATOM   10901 O  OE1 . GLU D 2 267 ? 151.153 119.574 186.790 1.00 167.85 ? 274 GLU D OE1 1 
ATOM   10902 O  OE2 . GLU D 2 267 ? 150.145 119.614 188.740 1.00 169.21 ? 274 GLU D OE2 1 
ATOM   10903 N  N   . ASN D 2 268 ? 150.129 124.361 184.614 1.00 169.28 ? 275 ASN D N   1 
ATOM   10904 C  CA  . ASN D 2 268 ? 150.741 125.124 183.526 1.00 169.37 ? 275 ASN D CA  1 
ATOM   10905 C  C   . ASN D 2 268 ? 150.582 124.399 182.187 1.00 170.08 ? 275 ASN D C   1 
ATOM   10906 O  O   . ASN D 2 268 ? 151.553 124.032 181.522 1.00 169.35 ? 275 ASN D O   1 
ATOM   10907 C  CB  . ASN D 2 268 ? 152.214 125.420 183.829 1.00 168.61 ? 275 ASN D CB  1 
ATOM   10908 C  CG  . ASN D 2 268 ? 152.708 126.677 183.145 1.00 168.64 ? 275 ASN D CG  1 
ATOM   10909 O  OD1 . ASN D 2 268 ? 152.100 127.156 182.187 1.00 168.72 ? 275 ASN D OD1 1 
ATOM   10910 N  ND2 . ASN D 2 268 ? 153.818 127.218 183.631 1.00 168.43 ? 275 ASN D ND2 1 
ATOM   10911 N  N   . ASP D 2 269 ? 149.324 124.198 181.802 1.00 170.59 ? 276 ASP D N   1 
ATOM   10912 C  CA  . ASP D 2 269 ? 149.021 123.579 180.523 1.00 170.35 ? 276 ASP D CA  1 
ATOM   10913 C  C   . ASP D 2 269 ? 149.303 124.557 179.381 1.00 171.03 ? 276 ASP D C   1 
ATOM   10914 O  O   . ASP D 2 269 ? 149.561 125.747 179.588 1.00 170.19 ? 276 ASP D O   1 
ATOM   10915 C  CB  . ASP D 2 269 ? 147.564 123.116 180.484 1.00 168.40 ? 276 ASP D CB  1 
ATOM   10916 C  CG  . ASP D 2 269 ? 147.321 122.040 179.444 1.00 168.08 ? 276 ASP D CG  1 
ATOM   10917 O  OD1 . ASP D 2 269 ? 148.210 121.823 178.593 1.00 168.65 ? 276 ASP D OD1 1 
ATOM   10918 O  OD2 . ASP D 2 269 ? 146.241 121.415 179.472 1.00 168.62 ? 276 ASP D OD2 1 
ATOM   10919 N  N   . ALA D 2 270 ? 149.267 124.034 178.156 1.00 167.71 ? 277 ALA D N   1 
ATOM   10920 C  CA  . ALA D 2 270 ? 149.489 124.857 176.976 1.00 165.51 ? 277 ALA D CA  1 
ATOM   10921 C  C   . ALA D 2 270 ? 148.234 125.587 176.516 1.00 165.22 ? 277 ALA D C   1 
ATOM   10922 O  O   . ALA D 2 270 ? 148.322 126.421 175.609 1.00 164.95 ? 277 ALA D O   1 
ATOM   10923 C  CB  . ALA D 2 270 ? 150.032 124.000 175.831 1.00 164.86 ? 277 ALA D CB  1 
ATOM   10924 N  N   . ASN D 2 271 ? 147.078 125.297 177.113 1.00 165.87 ? 278 ASN D N   1 
ATOM   10925 C  CA  . ASN D 2 271 ? 145.819 125.921 176.731 1.00 166.57 ? 278 ASN D CA  1 
ATOM   10926 C  C   . ASN D 2 271 ? 145.279 126.859 177.802 1.00 166.10 ? 278 ASN D C   1 
ATOM   10927 O  O   . ASN D 2 271 ? 144.102 127.231 177.749 1.00 165.19 ? 278 ASN D O   1 
ATOM   10928 C  CB  . ASN D 2 271 ? 144.775 124.851 176.402 1.00 166.34 ? 278 ASN D CB  1 
ATOM   10929 C  CG  . ASN D 2 271 ? 145.141 124.032 175.180 1.00 165.28 ? 278 ASN D CG  1 
ATOM   10930 O  OD1 . ASN D 2 271 ? 144.929 124.458 174.045 1.00 163.93 ? 278 ASN D OD1 1 
ATOM   10931 N  ND2 . ASN D 2 271 ? 145.690 122.845 175.408 1.00 165.31 ? 278 ASN D ND2 1 
ATOM   10932 N  N   . ILE D 2 272 ? 146.103 127.251 178.770 1.00 169.11 ? 279 ILE D N   1 
ATOM   10933 C  CA  . ILE D 2 272 ? 145.678 128.103 179.874 1.00 169.40 ? 279 ILE D CA  1 
ATOM   10934 C  C   . ILE D 2 272 ? 146.559 129.345 179.891 1.00 169.72 ? 279 ILE D C   1 
ATOM   10935 O  O   . ILE D 2 272 ? 147.786 129.244 179.773 1.00 169.34 ? 279 ILE D O   1 
ATOM   10936 C  CB  . ILE D 2 272 ? 145.742 127.358 181.221 1.00 169.20 ? 279 ILE D CB  1 
ATOM   10937 C  CG1 . ILE D 2 272 ? 145.536 128.327 182.384 1.00 168.90 ? 279 ILE D CG1 1 
ATOM   10938 C  CG2 . ILE D 2 272 ? 147.056 126.618 181.372 1.00 168.86 ? 279 ILE D CG2 1 
ATOM   10939 C  CD1 . ILE D 2 272 ? 144.150 128.911 182.434 1.00 168.17 ? 279 ILE D CD1 1 
ATOM   10940 N  N   . ALA D 2 273 ? 145.934 130.514 180.022 1.00 173.67 ? 280 ALA D N   1 
ATOM   10941 C  CA  . ALA D 2 273 ? 146.648 131.780 180.076 1.00 173.60 ? 280 ALA D CA  1 
ATOM   10942 C  C   . ALA D 2 273 ? 146.185 132.576 181.288 1.00 173.68 ? 280 ALA D C   1 
ATOM   10943 O  O   . ALA D 2 273 ? 145.040 132.457 181.728 1.00 173.02 ? 280 ALA D O   1 
ATOM   10944 C  CB  . ALA D 2 273 ? 146.440 132.601 178.798 1.00 173.00 ? 280 ALA D CB  1 
ATOM   10945 N  N   . ILE D 2 274 ? 147.093 133.383 181.832 1.00 178.63 ? 281 ILE D N   1 
ATOM   10946 C  CA  . ILE D 2 274 ? 146.830 134.187 183.020 1.00 178.60 ? 281 ILE D CA  1 
ATOM   10947 C  C   . ILE D 2 274 ? 147.216 135.630 182.730 1.00 178.66 ? 281 ILE D C   1 
ATOM   10948 O  O   . ILE D 2 274 ? 148.262 135.890 182.125 1.00 178.12 ? 281 ILE D O   1 
ATOM   10949 C  CB  . ILE D 2 274 ? 147.601 133.664 184.251 1.00 178.38 ? 281 ILE D CB  1 
ATOM   10950 C  CG1 . ILE D 2 274 ? 147.677 132.135 184.236 1.00 178.18 ? 281 ILE D CG1 1 
ATOM   10951 C  CG2 . ILE D 2 274 ? 146.951 134.155 185.532 1.00 177.85 ? 281 ILE D CG2 1 
ATOM   10952 C  CD1 . ILE D 2 274 ? 148.387 131.544 185.432 1.00 177.45 ? 281 ILE D CD1 1 
ATOM   10953 N  N   . VAL D 2 275 ? 146.374 136.570 183.158 1.00 182.66 ? 282 VAL D N   1 
ATOM   10954 C  CA  . VAL D 2 275 ? 146.682 137.989 183.051 1.00 182.95 ? 282 VAL D CA  1 
ATOM   10955 C  C   . VAL D 2 275 ? 146.173 138.688 184.303 1.00 183.20 ? 282 VAL D C   1 
ATOM   10956 O  O   . VAL D 2 275 ? 145.197 138.259 184.926 1.00 183.00 ? 282 VAL D O   1 
ATOM   10957 C  CB  . VAL D 2 275 ? 146.080 138.623 181.775 1.00 181.94 ? 282 VAL D CB  1 
ATOM   10958 C  CG1 . VAL D 2 275 ? 144.621 139.005 181.991 1.00 180.75 ? 282 VAL D CG1 1 
ATOM   10959 C  CG2 . VAL D 2 275 ? 146.898 139.831 181.345 1.00 181.68 ? 282 VAL D CG2 1 
ATOM   10960 N  N   . GLY D 2 276 ? 146.852 139.768 184.678 1.00 186.04 ? 283 GLY D N   1 
ATOM   10961 C  CA  . GLY D 2 276 ? 146.449 140.541 185.835 1.00 185.59 ? 283 GLY D CA  1 
ATOM   10962 C  C   . GLY D 2 276 ? 147.104 140.085 187.121 1.00 185.87 ? 283 GLY D C   1 
ATOM   10963 O  O   . GLY D 2 276 ? 148.265 139.665 187.121 1.00 185.46 ? 283 GLY D O   1 
ATOM   10964 N  N   . ASN D 2 277 ? 146.365 140.159 188.226 1.00 186.73 ? 284 ASN D N   1 
ATOM   10965 C  CA  . ASN D 2 277 ? 146.882 139.854 189.555 1.00 186.20 ? 284 ASN D CA  1 
ATOM   10966 C  C   . ASN D 2 277 ? 146.346 138.525 190.084 1.00 185.65 ? 284 ASN D C   1 
ATOM   10967 O  O   . ASN D 2 277 ? 146.039 138.388 191.269 1.00 185.05 ? 284 ASN D O   1 
ATOM   10968 C  CB  . ASN D 2 277 ? 146.559 140.986 190.526 1.00 185.87 ? 284 ASN D CB  1 
ATOM   10969 C  CG  . ASN D 2 277 ? 147.121 142.320 190.072 1.00 186.05 ? 284 ASN D CG  1 
ATOM   10970 O  OD1 . ASN D 2 277 ? 148.085 142.372 189.307 1.00 186.19 ? 284 ASN D OD1 1 
ATOM   10971 N  ND2 . ASN D 2 277 ? 146.521 143.407 190.542 1.00 185.83 ? 284 ASN D ND2 1 
ATOM   10972 N  N   . VAL D 2 278 ? 146.220 137.534 189.207 1.00 187.53 ? 285 VAL D N   1 
ATOM   10973 C  CA  . VAL D 2 278 ? 145.831 136.190 189.620 1.00 188.09 ? 285 VAL D CA  1 
ATOM   10974 C  C   . VAL D 2 278 ? 147.075 135.466 190.120 1.00 188.15 ? 285 VAL D C   1 
ATOM   10975 O  O   . VAL D 2 278 ? 148.056 135.317 189.383 1.00 187.46 ? 285 VAL D O   1 
ATOM   10976 C  CB  . VAL D 2 278 ? 145.169 135.424 188.466 1.00 187.23 ? 285 VAL D CB  1 
ATOM   10977 C  CG1 . VAL D 2 278 ? 144.410 134.216 188.994 1.00 186.55 ? 285 VAL D CG1 1 
ATOM   10978 C  CG2 . VAL D 2 278 ? 144.249 136.343 187.675 1.00 185.84 ? 285 VAL D CG2 1 
ATOM   10979 N  N   . ARG D 2 279 ? 147.041 135.014 191.373 1.00 187.79 ? 286 ARG D N   1 
ATOM   10980 C  CA  . ARG D 2 279 ? 148.214 134.449 192.021 1.00 186.91 ? 286 ARG D CA  1 
ATOM   10981 C  C   . ARG D 2 279 ? 147.883 133.110 192.664 1.00 186.68 ? 286 ARG D C   1 
ATOM   10982 O  O   . ARG D 2 279 ? 146.751 132.866 193.091 1.00 186.62 ? 286 ARG D O   1 
ATOM   10983 C  CB  . ARG D 2 279 ? 148.781 135.409 193.075 1.00 187.02 ? 286 ARG D CB  1 
ATOM   10984 C  CG  . ARG D 2 279 ? 149.437 136.647 192.487 1.00 186.73 ? 286 ARG D CG  1 
ATOM   10985 C  CD  . ARG D 2 279 ? 149.851 137.628 193.570 1.00 186.82 ? 286 ARG D CD  1 
ATOM   10986 N  NE  . ARG D 2 279 ? 150.583 136.979 194.651 1.00 187.23 ? 286 ARG D NE  1 
ATOM   10987 C  CZ  . ARG D 2 279 ? 150.190 136.962 195.917 1.00 186.96 ? 286 ARG D CZ  1 
ATOM   10988 N  NH1 . ARG D 2 279 ? 149.073 137.557 196.301 1.00 186.90 ? 286 ARG D NH1 1 
ATOM   10989 N  NH2 . ARG D 2 279 ? 150.938 136.335 196.821 1.00 186.05 ? 286 ARG D NH2 1 
ATOM   10990 N  N   . LEU D 2 280 ? 148.896 132.250 192.735 1.00 184.29 ? 287 LEU D N   1 
ATOM   10991 C  CA  . LEU D 2 280 ? 148.776 130.914 193.298 1.00 184.91 ? 287 LEU D CA  1 
ATOM   10992 C  C   . LEU D 2 280 ? 148.998 130.942 194.807 1.00 185.17 ? 287 LEU D C   1 
ATOM   10993 O  O   . LEU D 2 280 ? 149.743 131.775 195.330 1.00 184.63 ? 287 LEU D O   1 
ATOM   10994 C  CB  . LEU D 2 280 ? 149.785 129.973 192.631 1.00 184.49 ? 287 LEU D CB  1 
ATOM   10995 C  CG  . LEU D 2 280 ? 149.979 128.542 193.141 1.00 183.99 ? 287 LEU D CG  1 
ATOM   10996 C  CD1 . LEU D 2 280 ? 148.666 127.776 193.160 1.00 184.07 ? 287 LEU D CD1 1 
ATOM   10997 C  CD2 . LEU D 2 280 ? 151.016 127.811 192.297 1.00 183.54 ? 287 LEU D CD2 1 
ATOM   10998 N  N   . VAL D 2 281 ? 148.336 130.021 195.504 1.00 191.25 ? 288 VAL D N   1 
ATOM   10999 C  CA  . VAL D 2 281 ? 148.467 129.869 196.950 1.00 191.84 ? 288 VAL D CA  1 
ATOM   11000 C  C   . VAL D 2 281 ? 149.453 128.744 197.231 1.00 190.96 ? 288 VAL D C   1 
ATOM   11001 O  O   . VAL D 2 281 ? 149.320 127.640 196.688 1.00 190.59 ? 288 VAL D O   1 
ATOM   11002 C  CB  . VAL D 2 281 ? 147.106 129.579 197.606 1.00 190.33 ? 288 VAL D CB  1 
ATOM   11003 C  CG1 . VAL D 2 281 ? 147.288 129.176 199.062 1.00 189.03 ? 288 VAL D CG1 1 
ATOM   11004 C  CG2 . VAL D 2 281 ? 146.197 130.787 197.494 1.00 189.89 ? 288 VAL D CG2 1 
ATOM   11005 N  N   . GLY D 2 282 ? 150.441 129.021 198.076 1.00 180.92 ? 289 GLY D N   1 
ATOM   11006 C  CA  . GLY D 2 282 ? 151.425 128.020 198.447 1.00 179.81 ? 289 GLY D CA  1 
ATOM   11007 C  C   . GLY D 2 282 ? 152.820 128.581 198.632 1.00 179.78 ? 289 GLY D C   1 
ATOM   11008 O  O   . GLY D 2 282 ? 153.794 127.832 198.706 1.00 179.71 ? 289 GLY D O   1 
HETATM 11009 C  C1  . NAG E 3 .   ? 126.068 183.702 99.892  1.00 122.24 ? 901 NAG A C1  1 
HETATM 11010 C  C2  . NAG E 3 .   ? 126.897 184.601 98.957  1.00 122.28 ? 901 NAG A C2  1 
HETATM 11011 C  C3  . NAG E 3 .   ? 127.825 185.516 99.758  1.00 122.79 ? 901 NAG A C3  1 
HETATM 11012 C  C4  . NAG E 3 .   ? 127.040 186.301 100.796 1.00 122.46 ? 901 NAG A C4  1 
HETATM 11013 C  C5  . NAG E 3 .   ? 126.326 185.323 101.714 1.00 123.32 ? 901 NAG A C5  1 
HETATM 11014 C  C6  . NAG E 3 .   ? 125.450 186.007 102.738 1.00 122.55 ? 901 NAG A C6  1 
HETATM 11015 C  C7  . NAG E 3 .   ? 127.786 184.078 96.720  1.00 122.52 ? 901 NAG A C7  1 
HETATM 11016 C  C8  . NAG E 3 .   ? 127.052 185.294 96.237  1.00 119.23 ? 901 NAG A C8  1 
HETATM 11017 N  N2  . NAG E 3 .   ? 127.669 183.796 98.022  1.00 123.47 ? 901 NAG A N2  1 
HETATM 11018 O  O3  . NAG E 3 .   ? 128.488 186.414 98.875  1.00 120.75 ? 901 NAG A O3  1 
HETATM 11019 O  O4  . NAG E 3 .   ? 127.914 187.123 101.562 1.00 121.90 ? 901 NAG A O4  1 
HETATM 11020 O  O5  . NAG E 3 .   ? 125.459 184.498 100.928 1.00 123.72 ? 901 NAG A O5  1 
HETATM 11021 O  O6  . NAG E 3 .   ? 124.071 185.792 102.465 1.00 120.93 ? 901 NAG A O6  1 
HETATM 11022 O  O7  . NAG E 3 .   ? 128.452 183.378 95.963  1.00 122.64 ? 901 NAG A O7  1 
HETATM 11023 C  C1  . NAG F 3 .   ? 144.625 160.799 124.739 1.00 30.00  ? 902 NAG A C1  1 
HETATM 11024 C  C2  . NAG F 3 .   ? 143.600 160.833 125.869 1.00 30.00  ? 902 NAG A C2  1 
HETATM 11025 C  C3  . NAG F 3 .   ? 144.065 161.794 126.952 1.00 30.00  ? 902 NAG A C3  1 
HETATM 11026 C  C4  . NAG F 3 .   ? 145.440 161.367 127.441 1.00 30.00  ? 902 NAG A C4  1 
HETATM 11027 C  C5  . NAG F 3 .   ? 146.402 161.317 126.262 1.00 30.00  ? 902 NAG A C5  1 
HETATM 11028 C  C6  . NAG F 3 .   ? 147.783 160.850 126.708 1.00 30.00  ? 902 NAG A C6  1 
HETATM 11029 C  C7  . NAG F 3 .   ? 141.399 160.361 125.039 1.00 30.00  ? 902 NAG A C7  1 
HETATM 11030 C  C8  . NAG F 3 .   ? 139.971 160.817 125.054 1.00 30.00  ? 902 NAG A C8  1 
HETATM 11031 N  N2  . NAG F 3 .   ? 142.306 161.262 125.384 1.00 30.00  ? 902 NAG A N2  1 
HETATM 11032 O  O3  . NAG F 3 .   ? 143.140 161.775 128.044 1.00 30.00  ? 902 NAG A O3  1 
HETATM 11033 O  O4  . NAG F 3 .   ? 145.917 162.301 128.415 1.00 30.00  ? 902 NAG A O4  1 
HETATM 11034 O  O5  . NAG F 3 .   ? 145.900 160.425 125.267 1.00 30.00  ? 902 NAG A O5  1 
HETATM 11035 O  O6  . NAG F 3 .   ? 147.716 159.476 127.106 1.00 30.00  ? 902 NAG A O6  1 
HETATM 11036 O  O7  . NAG F 3 .   ? 141.733 159.231 124.726 1.00 30.00  ? 902 NAG A O7  1 
HETATM 11037 C  C1  . NAG G 3 .   ? 127.459 75.064  166.410 1.00 119.58 ? 901 NAG B C1  1 
HETATM 11038 C  C2  . NAG G 3 .   ? 126.465 74.177  167.167 1.00 118.44 ? 901 NAG B C2  1 
HETATM 11039 C  C3  . NAG G 3 .   ? 126.992 72.747  167.273 1.00 120.26 ? 901 NAG B C3  1 
HETATM 11040 C  C4  . NAG G 3 .   ? 127.378 72.213  165.901 1.00 120.11 ? 901 NAG B C4  1 
HETATM 11041 C  C5  . NAG G 3 .   ? 128.365 73.166  165.240 1.00 119.29 ? 901 NAG B C5  1 
HETATM 11042 C  C6  . NAG G 3 .   ? 128.732 72.758  163.833 1.00 118.77 ? 901 NAG B C6  1 
HETATM 11043 C  C7  . NAG G 3 .   ? 125.212 75.589  168.738 1.00 119.90 ? 901 NAG B C7  1 
HETATM 11044 C  C8  . NAG G 3 .   ? 125.077 76.038  170.162 1.00 118.33 ? 901 NAG B C8  1 
HETATM 11045 N  N2  . NAG G 3 .   ? 126.194 74.717  168.490 1.00 118.78 ? 901 NAG B N2  1 
HETATM 11046 O  O3  . NAG G 3 .   ? 125.987 71.919  167.849 1.00 121.04 ? 901 NAG B O3  1 
HETATM 11047 O  O4  . NAG G 3 .   ? 127.975 70.927  166.022 1.00 119.28 ? 901 NAG B O4  1 
HETATM 11048 O  O5  . NAG G 3 .   ? 127.775 74.469  165.148 1.00 121.11 ? 901 NAG B O5  1 
HETATM 11049 O  O6  . NAG G 3 .   ? 128.924 73.894  163.001 1.00 117.47 ? 901 NAG B O6  1 
HETATM 11050 O  O7  . NAG G 3 .   ? 124.466 75.998  167.854 1.00 120.19 ? 901 NAG B O7  1 
HETATM 11051 C  C1  . NAG H 3 .   ? 132.373 95.583  130.208 1.00 122.93 ? 902 NAG B C1  1 
HETATM 11052 C  C2  . NAG H 3 .   ? 133.728 95.308  129.583 1.00 122.37 ? 902 NAG B C2  1 
HETATM 11053 C  C3  . NAG H 3 .   ? 134.019 96.344  128.514 1.00 120.27 ? 902 NAG B C3  1 
HETATM 11054 C  C4  . NAG H 3 .   ? 132.892 96.353  127.490 1.00 122.16 ? 902 NAG B C4  1 
HETATM 11055 C  C5  . NAG H 3 .   ? 131.516 96.443  128.157 1.00 123.16 ? 902 NAG B C5  1 
HETATM 11056 C  C6  . NAG H 3 .   ? 130.396 96.195  127.175 1.00 121.10 ? 902 NAG B C6  1 
HETATM 11057 C  C7  . NAG H 3 .   ? 135.399 94.143  130.940 1.00 120.65 ? 902 NAG B C7  1 
HETATM 11058 C  C8  . NAG H 3 .   ? 136.471 94.281  131.977 1.00 117.70 ? 902 NAG B C8  1 
HETATM 11059 N  N2  . NAG H 3 .   ? 134.782 95.273  130.581 1.00 123.30 ? 902 NAG B N2  1 
HETATM 11060 O  O3  . NAG H 3 .   ? 135.245 96.056  127.854 1.00 119.05 ? 902 NAG B O3  1 
HETATM 11061 O  O4  . NAG H 3 .   ? 133.045 97.450  126.593 1.00 122.40 ? 902 NAG B O4  1 
HETATM 11062 O  O5  . NAG H 3 .   ? 131.368 95.473  129.213 1.00 121.97 ? 902 NAG B O5  1 
HETATM 11063 O  O6  . NAG H 3 .   ? 130.542 97.012  126.020 1.00 122.88 ? 902 NAG B O6  1 
HETATM 11064 O  O7  . NAG H 3 .   ? 135.112 93.058  130.444 1.00 119.59 ? 902 NAG B O7  1 
HETATM 11065 CA CA  . CA  I 4 .   ? 96.941  141.194 108.386 1.00 68.88  ? 501 CA  C CA  1 
HETATM 11066 C  C1  . NAG J 3 .   ? 86.858  153.988 105.265 1.00 126.35 ? 502 NAG C C1  1 
HETATM 11067 C  C2  . NAG J 3 .   ? 88.151  154.796 105.343 1.00 128.61 ? 502 NAG C C2  1 
HETATM 11068 C  C3  . NAG J 3 .   ? 88.096  155.775 106.511 1.00 129.84 ? 502 NAG C C3  1 
HETATM 11069 C  C4  . NAG J 3 .   ? 86.850  156.644 106.416 1.00 130.73 ? 502 NAG C C4  1 
HETATM 11070 C  C5  . NAG J 3 .   ? 85.607  155.769 106.304 1.00 128.46 ? 502 NAG C C5  1 
HETATM 11071 C  C6  . NAG J 3 .   ? 84.345  156.568 106.076 1.00 128.28 ? 502 NAG C C6  1 
HETATM 11072 C  C7  . NAG J 3 .   ? 90.227  153.793 104.502 1.00 127.72 ? 502 NAG C C7  1 
HETATM 11073 C  C8  . NAG J 3 .   ? 91.352  152.848 104.793 1.00 126.03 ? 502 NAG C C8  1 
HETATM 11074 N  N2  . NAG J 3 .   ? 89.306  153.921 105.463 1.00 128.53 ? 502 NAG C N2  1 
HETATM 11075 O  O3  . NAG J 3 .   ? 89.260  156.593 106.495 1.00 129.17 ? 502 NAG C O3  1 
HETATM 11076 O  O4  . NAG J 3 .   ? 86.738  157.472 107.568 1.00 128.61 ? 502 NAG C O4  1 
HETATM 11077 O  O5  . NAG J 3 .   ? 85.737  154.878 105.186 1.00 127.39 ? 502 NAG C O5  1 
HETATM 11078 O  O6  . NAG J 3 .   ? 84.561  157.628 105.155 1.00 128.23 ? 502 NAG C O6  1 
HETATM 11079 O  O7  . NAG J 3 .   ? 90.155  154.413 103.446 1.00 127.90 ? 502 NAG C O7  1 
HETATM 11080 CA CA  . CA  K 4 .   ? 121.381 126.835 171.675 1.00 106.04 ? 501 CA  D CA  1 
HETATM 11081 C  C1  . NAG L 3 .   ? 113.027 118.957 183.037 1.00 150.52 ? 502 NAG D C1  1 
HETATM 11082 C  C2  . NAG L 3 .   ? 113.434 118.074 181.857 1.00 150.58 ? 502 NAG D C2  1 
HETATM 11083 C  C3  . NAG L 3 .   ? 112.202 117.445 181.215 1.00 151.51 ? 502 NAG D C3  1 
HETATM 11084 C  C4  . NAG L 3 .   ? 111.374 116.711 182.260 1.00 152.37 ? 502 NAG D C4  1 
HETATM 11085 C  C5  . NAG L 3 .   ? 111.035 117.654 183.409 1.00 151.52 ? 502 NAG D C5  1 
HETATM 11086 C  C6  . NAG L 3 .   ? 110.301 116.966 184.535 1.00 150.50 ? 502 NAG D C6  1 
HETATM 11087 C  C7  . NAG L 3 .   ? 115.177 118.295 180.148 1.00 149.54 ? 502 NAG D C7  1 
HETATM 11088 C  C8  . NAG L 3 .   ? 115.848 119.213 179.175 1.00 149.38 ? 502 NAG D C8  1 
HETATM 11089 N  N2  . NAG L 3 .   ? 114.190 118.830 180.874 1.00 149.91 ? 502 NAG D N2  1 
HETATM 11090 O  O3  . NAG L 3 .   ? 112.609 116.540 180.194 1.00 151.02 ? 502 NAG D O3  1 
HETATM 11091 O  O4  . NAG L 3 .   ? 110.170 116.222 181.680 1.00 151.89 ? 502 NAG D O4  1 
HETATM 11092 O  O5  . NAG L 3 .   ? 112.243 118.192 183.967 1.00 150.19 ? 502 NAG D O5  1 
HETATM 11093 O  O6  . NAG L 3 .   ? 109.816 115.693 184.131 1.00 149.80 ? 502 NAG D O6  1 
HETATM 11094 O  O7  . NAG L 3 .   ? 115.511 117.122 180.272 1.00 149.75 ? 502 NAG D O7  1 
# 
