data_8G80
# 
_entry.id   8G80 
# 
_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   8G80         pdb_00008g80 10.2210/pdb8g80/pdb 
WWPDB D_1000272048 ?            ?                   
EMDB  EMD-29830    ?            ?                   
# 
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                        8G80 
_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 (K6c6)' 
_pdbx_database_related.db_id          EMD-29830 
_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 ?   ?   ?   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 ?   ?   ?   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 1017 1017 NAG NAG A . 
F 3 NAG 1 1018 1018 NAG NAG A . 
G 3 NAG 1 1017 1017 NAG NAG B . 
H 3 NAG 1 1018 1018 NAG NAG B . 
I 4 CA  1 1007 1007 CA  CA  C . 
J 3 NAG 1 1008 1008 NAG NAG C . 
K 4 CA  1 1007 1007 CA  CA  D . 
L 3 NAG 1 1008 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 61  ? CG  ? A GLU 103 CG  
5   1 Y 1 A GLU 61  ? CD  ? A GLU 103 CD  
6   1 Y 1 A GLU 61  ? OE1 ? A GLU 103 OE1 
7   1 Y 1 A GLU 61  ? OE2 ? A GLU 103 OE2 
8   1 Y 1 A ASP 358 ? CG  ? A ASP 383 CG  
9   1 Y 1 A ASP 358 ? OD1 ? A ASP 383 OD1 
10  1 Y 1 A ASP 358 ? OD2 ? A ASP 383 OD2 
11  1 Y 1 A GLU 392 ? CG  ? A GLU 417 CG  
12  1 Y 1 A GLU 392 ? CD  ? A GLU 417 CD  
13  1 Y 1 A GLU 392 ? OE1 ? A GLU 417 OE1 
14  1 Y 1 A GLU 392 ? OE2 ? A GLU 417 OE2 
15  1 Y 1 A ASP 393 ? CG  ? A ASP 418 CG  
16  1 Y 1 A ASP 393 ? OD1 ? A ASP 418 OD1 
17  1 Y 1 A ASP 393 ? OD2 ? A ASP 418 OD2 
18  1 Y 1 A GLU 396 ? CG  ? A GLU 421 CG  
19  1 Y 1 A GLU 396 ? CD  ? A GLU 421 CD  
20  1 Y 1 A GLU 396 ? OE1 ? A GLU 421 OE1 
21  1 Y 1 A GLU 396 ? OE2 ? A GLU 421 OE2 
22  1 Y 1 A GLU 398 ? CG  ? A GLU 423 CG  
23  1 Y 1 A GLU 398 ? CD  ? A GLU 423 CD  
24  1 Y 1 A GLU 398 ? OE1 ? A GLU 423 OE1 
25  1 Y 1 A GLU 398 ? OE2 ? A GLU 423 OE2 
26  1 Y 1 A TYR 420 ? CG  ? A TYR 445 CG  
27  1 Y 1 A TYR 420 ? CD1 ? A TYR 445 CD1 
28  1 Y 1 A TYR 420 ? CD2 ? A TYR 445 CD2 
29  1 Y 1 A TYR 420 ? CE1 ? A TYR 445 CE1 
30  1 Y 1 A TYR 420 ? CE2 ? A TYR 445 CE2 
31  1 Y 1 A TYR 420 ? CZ  ? A TYR 445 CZ  
32  1 Y 1 A TYR 420 ? OH  ? A TYR 445 OH  
33  1 Y 1 A GLU 422 ? CG  ? A GLU 447 CG  
34  1 Y 1 A GLU 422 ? CD  ? A GLU 447 CD  
35  1 Y 1 A GLU 422 ? OE1 ? A GLU 447 OE1 
36  1 Y 1 A GLU 422 ? OE2 ? A GLU 447 OE2 
37  1 Y 1 A LYS 424 ? CG  ? A LYS 449 CG  
38  1 Y 1 A LYS 424 ? CD  ? A LYS 449 CD  
39  1 Y 1 A LYS 424 ? CE  ? A LYS 449 CE  
40  1 Y 1 A LYS 424 ? NZ  ? A LYS 449 NZ  
41  1 Y 1 A ASP 442 ? CG  ? A ASP 467 CG  
42  1 Y 1 A ASP 442 ? OD1 ? A ASP 467 OD1 
43  1 Y 1 A ASP 442 ? OD2 ? A ASP 467 OD2 
44  1 Y 1 A GLU 490 ? CG  ? A GLU 515 CG  
45  1 Y 1 A GLU 490 ? CD  ? A GLU 515 CD  
46  1 Y 1 A GLU 490 ? OE1 ? A GLU 515 OE1 
47  1 Y 1 A GLU 490 ? OE2 ? A GLU 515 OE2 
48  1 Y 1 A GLU 494 ? CG  ? A GLU 519 CG  
49  1 Y 1 A GLU 494 ? CD  ? A GLU 519 CD  
50  1 Y 1 A GLU 494 ? OE1 ? A GLU 519 OE1 
51  1 Y 1 A GLU 494 ? OE2 ? A GLU 519 OE2 
52  1 Y 1 A LYS 525 ? CG  ? A LYS 550 CG  
53  1 Y 1 A LYS 525 ? CD  ? A LYS 550 CD  
54  1 Y 1 A LYS 525 ? CE  ? A LYS 550 CE  
55  1 Y 1 A LYS 525 ? NZ  ? A LYS 550 NZ  
56  1 Y 1 A GLN 549 ? CG  ? A GLN 574 CG  
57  1 Y 1 A GLN 549 ? CD  ? A GLN 574 CD  
58  1 Y 1 A GLN 549 ? OE1 ? A GLN 574 OE1 
59  1 Y 1 A GLN 549 ? NE2 ? A GLN 574 NE2 
60  1 Y 1 A ARG 564 ? CG  ? A ARG 589 CG  
61  1 Y 1 A ARG 564 ? CD  ? A ARG 589 CD  
62  1 Y 1 A ARG 564 ? NE  ? A ARG 589 NE  
63  1 Y 1 A ARG 564 ? CZ  ? A ARG 589 CZ  
64  1 Y 1 A ARG 564 ? NH1 ? A ARG 589 NH1 
65  1 Y 1 A ARG 564 ? NH2 ? A ARG 589 NH2 
66  1 Y 1 A PHE 565 ? CG  ? A PHE 590 CG  
67  1 Y 1 A PHE 565 ? CD1 ? A PHE 590 CD1 
68  1 Y 1 A PHE 565 ? CD2 ? A PHE 590 CD2 
69  1 Y 1 A PHE 565 ? CE1 ? A PHE 590 CE1 
70  1 Y 1 A PHE 565 ? CE2 ? A PHE 590 CE2 
71  1 Y 1 A PHE 565 ? CZ  ? A PHE 590 CZ  
72  1 Y 1 A ASN 574 ? CG  ? A ASN 599 CG  
73  1 Y 1 A ASN 574 ? OD1 ? A ASN 599 OD1 
74  1 Y 1 A ASN 574 ? ND2 ? A ASN 599 ND2 
75  1 Y 1 A LYS 586 ? CG  ? A LYS 611 CG  
76  1 Y 1 A LYS 586 ? CD  ? A LYS 611 CD  
77  1 Y 1 A LYS 586 ? CE  ? A LYS 611 CE  
78  1 Y 1 A LYS 586 ? NZ  ? A LYS 611 NZ  
79  1 Y 1 B ASN 59  ? CG  ? B ASN 101 CG  
80  1 Y 1 B ASN 59  ? OD1 ? B ASN 101 OD1 
81  1 Y 1 B ASN 59  ? ND2 ? B ASN 101 ND2 
82  1 Y 1 B GLU 392 ? CG  ? B GLU 417 CG  
83  1 Y 1 B GLU 392 ? CD  ? B GLU 417 CD  
84  1 Y 1 B GLU 392 ? OE1 ? B GLU 417 OE1 
85  1 Y 1 B GLU 392 ? OE2 ? B GLU 417 OE2 
86  1 Y 1 B ASP 393 ? CG  ? B ASP 418 CG  
87  1 Y 1 B ASP 393 ? OD1 ? B ASP 418 OD1 
88  1 Y 1 B ASP 393 ? OD2 ? B ASP 418 OD2 
89  1 Y 1 B GLU 396 ? CG  ? B GLU 421 CG  
90  1 Y 1 B GLU 396 ? CD  ? B GLU 421 CD  
91  1 Y 1 B GLU 396 ? OE1 ? B GLU 421 OE1 
92  1 Y 1 B GLU 396 ? OE2 ? B GLU 421 OE2 
93  1 Y 1 B GLU 398 ? CG  ? B GLU 423 CG  
94  1 Y 1 B GLU 398 ? CD  ? B GLU 423 CD  
95  1 Y 1 B GLU 398 ? OE1 ? B GLU 423 OE1 
96  1 Y 1 B GLU 398 ? OE2 ? B GLU 423 OE2 
97  1 Y 1 B TYR 420 ? CG  ? B TYR 445 CG  
98  1 Y 1 B TYR 420 ? CD1 ? B TYR 445 CD1 
99  1 Y 1 B TYR 420 ? CD2 ? B TYR 445 CD2 
100 1 Y 1 B TYR 420 ? CE1 ? B TYR 445 CE1 
101 1 Y 1 B TYR 420 ? CE2 ? B TYR 445 CE2 
102 1 Y 1 B TYR 420 ? CZ  ? B TYR 445 CZ  
103 1 Y 1 B TYR 420 ? OH  ? B TYR 445 OH  
104 1 Y 1 B GLU 422 ? CG  ? B GLU 447 CG  
105 1 Y 1 B GLU 422 ? CD  ? B GLU 447 CD  
106 1 Y 1 B GLU 422 ? OE1 ? B GLU 447 OE1 
107 1 Y 1 B GLU 422 ? OE2 ? B GLU 447 OE2 
108 1 Y 1 B LYS 424 ? CG  ? B LYS 449 CG  
109 1 Y 1 B LYS 424 ? CD  ? B LYS 449 CD  
110 1 Y 1 B LYS 424 ? CE  ? B LYS 449 CE  
111 1 Y 1 B LYS 424 ? NZ  ? B LYS 449 NZ  
112 1 Y 1 B ASP 442 ? CG  ? B ASP 467 CG  
113 1 Y 1 B ASP 442 ? OD1 ? B ASP 467 OD1 
114 1 Y 1 B ASP 442 ? OD2 ? B ASP 467 OD2 
115 1 Y 1 B GLU 490 ? CG  ? B GLU 515 CG  
116 1 Y 1 B GLU 490 ? CD  ? B GLU 515 CD  
117 1 Y 1 B GLU 490 ? OE1 ? B GLU 515 OE1 
118 1 Y 1 B GLU 490 ? OE2 ? B GLU 515 OE2 
119 1 Y 1 B GLU 494 ? CG  ? B GLU 519 CG  
120 1 Y 1 B GLU 494 ? CD  ? B GLU 519 CD  
121 1 Y 1 B GLU 494 ? OE1 ? B GLU 519 OE1 
122 1 Y 1 B GLU 494 ? OE2 ? B GLU 519 OE2 
123 1 Y 1 B LYS 525 ? CG  ? B LYS 550 CG  
124 1 Y 1 B LYS 525 ? CD  ? B LYS 550 CD  
125 1 Y 1 B LYS 525 ? CE  ? B LYS 550 CE  
126 1 Y 1 B LYS 525 ? NZ  ? B LYS 550 NZ  
127 1 Y 1 B GLN 549 ? CG  ? B GLN 574 CG  
128 1 Y 1 B GLN 549 ? CD  ? B GLN 574 CD  
129 1 Y 1 B GLN 549 ? OE1 ? B GLN 574 OE1 
130 1 Y 1 B GLN 549 ? NE2 ? B GLN 574 NE2 
131 1 Y 1 B ASN 574 ? CG  ? B ASN 599 CG  
132 1 Y 1 B ASN 574 ? OD1 ? B ASN 599 OD1 
133 1 Y 1 B ASN 574 ? ND2 ? B ASN 599 ND2 
134 1 Y 1 B LYS 586 ? CG  ? B LYS 611 CG  
135 1 Y 1 B LYS 586 ? CD  ? B LYS 611 CD  
136 1 Y 1 B LYS 586 ? CE  ? B LYS 611 CE  
137 1 Y 1 B LYS 586 ? NZ  ? B LYS 611 NZ  
# 
_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                     8G80 
_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                         8G80 
_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                   8G80 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 8G80 
_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' ? 0.002 ? 11342 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.497 ? 15447 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 4.233 ? 1582  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.043 ? 1705  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.004 ? 2021  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     8G80 
_struct.title                        
'Cryo-EM structure of full length Neuroligin-2 from Mouse bound to two Neurexin-1 Beta conformation two' 
_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        8G80 
_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 8G80 A 56 ? 861 ? Q62888 14 ? 819 ? 14  836 
2 1 8G80 B 56 ? 861 ? Q62888 14 ? 819 ? 14  836 
3 2 8G80 C 1  ? 62  ? E0CZA5 1  ? 62  ? -22 39  
4 3 8G80 C 91 ? 461 ? E0CZA5 68 ? 438 ? 68  468 
5 2 8G80 D 1  ? 62  ? E0CZA5 1  ? 62  ? -22 39  
6 3 8G80 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 8G80 MET A 1   ? UNP Q62888 ?   ?   'initiating methionine' -41 1   
1 8G80 ALA A 2   ? UNP Q62888 ?   ?   'expression tag'        -40 2   
1 8G80 LEU A 3   ? UNP Q62888 ?   ?   'expression tag'        -39 3   
1 8G80 PRO A 4   ? UNP Q62888 ?   ?   'expression tag'        -38 4   
1 8G80 ARG A 5   ? UNP Q62888 ?   ?   'expression tag'        -37 5   
1 8G80 CYS A 6   ? UNP Q62888 ?   ?   'expression tag'        -36 6   
1 8G80 MET A 7   ? UNP Q62888 ?   ?   'expression tag'        -35 7   
1 8G80 TRP A 8   ? UNP Q62888 ?   ?   'expression tag'        -34 8   
1 8G80 PRO A 9   ? UNP Q62888 ?   ?   'expression tag'        -33 9   
1 8G80 ASN A 10  ? UNP Q62888 ?   ?   'expression tag'        -32 10  
1 8G80 TYR A 11  ? UNP Q62888 ?   ?   'expression tag'        -31 11  
1 8G80 VAL A 12  ? UNP Q62888 ?   ?   'expression tag'        -30 12  
1 8G80 TRP A 13  ? UNP Q62888 ?   ?   'expression tag'        -29 13  
1 8G80 ARG A 14  ? UNP Q62888 ?   ?   'expression tag'        -28 14  
1 8G80 ALA A 15  ? UNP Q62888 ?   ?   'expression tag'        -27 15  
1 8G80 MET A 16  ? UNP Q62888 ?   ?   'expression tag'        -26 16  
1 8G80 MET A 17  ? UNP Q62888 ?   ?   'expression tag'        -25 17  
1 8G80 ALA A 18  ? UNP Q62888 ?   ?   'expression tag'        -24 18  
1 8G80 CYS A 19  ? UNP Q62888 ?   ?   'expression tag'        -23 19  
1 8G80 VAL A 20  ? UNP Q62888 ?   ?   'expression tag'        -22 20  
1 8G80 VAL A 21  ? UNP Q62888 ?   ?   'expression tag'        -21 21  
1 8G80 HIS A 22  ? UNP Q62888 ?   ?   'expression tag'        -20 22  
1 8G80 ARG A 23  ? UNP Q62888 ?   ?   'expression tag'        -19 23  
1 8G80 GLY A 24  ? UNP Q62888 ?   ?   'expression tag'        -18 24  
1 8G80 SER A 25  ? UNP Q62888 ?   ?   'expression tag'        -17 25  
1 8G80 GLY A 26  ? UNP Q62888 ?   ?   'expression tag'        -16 26  
1 8G80 ALA A 27  ? UNP Q62888 ?   ?   'expression tag'        -15 27  
1 8G80 PRO A 28  ? UNP Q62888 ?   ?   'expression tag'        -14 28  
1 8G80 LEU A 29  ? UNP Q62888 ?   ?   'expression tag'        -13 29  
1 8G80 THR A 30  ? UNP Q62888 ?   ?   'expression tag'        -12 30  
1 8G80 LEU A 31  ? UNP Q62888 ?   ?   'expression tag'        -11 31  
1 8G80 CYS A 32  ? UNP Q62888 ?   ?   'expression tag'        -10 32  
1 8G80 LEU A 33  ? UNP Q62888 ?   ?   'expression tag'        -9  33  
1 8G80 LEU A 34  ? UNP Q62888 ?   ?   'expression tag'        -8  34  
1 8G80 GLY A 35  ? UNP Q62888 ?   ?   'expression tag'        -7  35  
1 8G80 CYS A 36  ? UNP Q62888 ?   ?   'expression tag'        -6  36  
1 8G80 LEU A 37  ? UNP Q62888 ?   ?   'expression tag'        -5  37  
1 8G80 LEU A 38  ? UNP Q62888 ?   ?   'expression tag'        -4  38  
1 8G80 GLN A 39  ? UNP Q62888 ?   ?   'expression tag'        -3  39  
1 8G80 THR A 40  ? UNP Q62888 ?   ?   'expression tag'        -2  40  
1 8G80 PHE A 41  ? UNP Q62888 ?   ?   'expression tag'        -1  41  
1 8G80 HIS A 42  ? UNP Q62888 ?   ?   'expression tag'        0   42  
1 8G80 VAL A 43  ? UNP Q62888 ?   ?   'expression tag'        1   43  
1 8G80 LEU A 44  ? UNP Q62888 ?   ?   'expression tag'        2   44  
1 8G80 SER A 45  ? UNP Q62888 ?   ?   'expression tag'        3   45  
1 8G80 GLN A 46  ? UNP Q62888 ?   ?   'expression tag'        4   46  
1 8G80 LYS A 47  ? UNP Q62888 ?   ?   'expression tag'        5   47  
1 8G80 TYR A 48  ? UNP Q62888 ?   ?   'expression tag'        6   48  
1 8G80 PRO A 49  ? UNP Q62888 ?   ?   'expression tag'        7   49  
1 8G80 TYR A 50  ? UNP Q62888 ?   ?   'expression tag'        8   50  
1 8G80 ASP A 51  ? UNP Q62888 ?   ?   'expression tag'        9   51  
1 8G80 VAL A 52  ? UNP Q62888 ?   ?   'expression tag'        10  52  
1 8G80 PRO A 53  ? UNP Q62888 ?   ?   'expression tag'        11  53  
1 8G80 ASP A 54  ? UNP Q62888 ?   ?   'expression tag'        12  54  
1 8G80 TYR A 55  ? UNP Q62888 ?   ?   'expression tag'        13  55  
1 8G80 VAL A 235 ? UNP Q62888 ALA 193 conflict                210 56  
1 8G80 SER A 862 ? UNP Q62888 ?   ?   'expression tag'        837 57  
1 8G80 ASN A 863 ? UNP Q62888 ?   ?   'expression tag'        838 58  
1 8G80 SER A 864 ? UNP Q62888 ?   ?   'expression tag'        839 59  
1 8G80 LEU A 865 ? UNP Q62888 ?   ?   'expression tag'        840 60  
1 8G80 GLU A 866 ? UNP Q62888 ?   ?   'expression tag'        841 61  
1 8G80 VAL A 867 ? UNP Q62888 ?   ?   'expression tag'        842 62  
1 8G80 LEU A 868 ? UNP Q62888 ?   ?   'expression tag'        843 63  
1 8G80 PHE A 869 ? UNP Q62888 ?   ?   'expression tag'        844 64  
1 8G80 GLN A 870 ? UNP Q62888 ?   ?   'expression tag'        845 65  
2 8G80 MET B 1   ? UNP Q62888 ?   ?   'initiating methionine' -41 66  
2 8G80 ALA B 2   ? UNP Q62888 ?   ?   'expression tag'        -40 67  
2 8G80 LEU B 3   ? UNP Q62888 ?   ?   'expression tag'        -39 68  
2 8G80 PRO B 4   ? UNP Q62888 ?   ?   'expression tag'        -38 69  
2 8G80 ARG B 5   ? UNP Q62888 ?   ?   'expression tag'        -37 70  
2 8G80 CYS B 6   ? UNP Q62888 ?   ?   'expression tag'        -36 71  
2 8G80 MET B 7   ? UNP Q62888 ?   ?   'expression tag'        -35 72  
2 8G80 TRP B 8   ? UNP Q62888 ?   ?   'expression tag'        -34 73  
2 8G80 PRO B 9   ? UNP Q62888 ?   ?   'expression tag'        -33 74  
2 8G80 ASN B 10  ? UNP Q62888 ?   ?   'expression tag'        -32 75  
2 8G80 TYR B 11  ? UNP Q62888 ?   ?   'expression tag'        -31 76  
2 8G80 VAL B 12  ? UNP Q62888 ?   ?   'expression tag'        -30 77  
2 8G80 TRP B 13  ? UNP Q62888 ?   ?   'expression tag'        -29 78  
2 8G80 ARG B 14  ? UNP Q62888 ?   ?   'expression tag'        -28 79  
2 8G80 ALA B 15  ? UNP Q62888 ?   ?   'expression tag'        -27 80  
2 8G80 MET B 16  ? UNP Q62888 ?   ?   'expression tag'        -26 81  
2 8G80 MET B 17  ? UNP Q62888 ?   ?   'expression tag'        -25 82  
2 8G80 ALA B 18  ? UNP Q62888 ?   ?   'expression tag'        -24 83  
2 8G80 CYS B 19  ? UNP Q62888 ?   ?   'expression tag'        -23 84  
2 8G80 VAL B 20  ? UNP Q62888 ?   ?   'expression tag'        -22 85  
2 8G80 VAL B 21  ? UNP Q62888 ?   ?   'expression tag'        -21 86  
2 8G80 HIS B 22  ? UNP Q62888 ?   ?   'expression tag'        -20 87  
2 8G80 ARG B 23  ? UNP Q62888 ?   ?   'expression tag'        -19 88  
2 8G80 GLY B 24  ? UNP Q62888 ?   ?   'expression tag'        -18 89  
2 8G80 SER B 25  ? UNP Q62888 ?   ?   'expression tag'        -17 90  
2 8G80 GLY B 26  ? UNP Q62888 ?   ?   'expression tag'        -16 91  
2 8G80 ALA B 27  ? UNP Q62888 ?   ?   'expression tag'        -15 92  
2 8G80 PRO B 28  ? UNP Q62888 ?   ?   'expression tag'        -14 93  
2 8G80 LEU B 29  ? UNP Q62888 ?   ?   'expression tag'        -13 94  
2 8G80 THR B 30  ? UNP Q62888 ?   ?   'expression tag'        -12 95  
2 8G80 LEU B 31  ? UNP Q62888 ?   ?   'expression tag'        -11 96  
2 8G80 CYS B 32  ? UNP Q62888 ?   ?   'expression tag'        -10 97  
2 8G80 LEU B 33  ? UNP Q62888 ?   ?   'expression tag'        -9  98  
2 8G80 LEU B 34  ? UNP Q62888 ?   ?   'expression tag'        -8  99  
2 8G80 GLY B 35  ? UNP Q62888 ?   ?   'expression tag'        -7  100 
2 8G80 CYS B 36  ? UNP Q62888 ?   ?   'expression tag'        -6  101 
2 8G80 LEU B 37  ? UNP Q62888 ?   ?   'expression tag'        -5  102 
2 8G80 LEU B 38  ? UNP Q62888 ?   ?   'expression tag'        -4  103 
2 8G80 GLN B 39  ? UNP Q62888 ?   ?   'expression tag'        -3  104 
2 8G80 THR B 40  ? UNP Q62888 ?   ?   'expression tag'        -2  105 
2 8G80 PHE B 41  ? UNP Q62888 ?   ?   'expression tag'        -1  106 
2 8G80 HIS B 42  ? UNP Q62888 ?   ?   'expression tag'        0   107 
2 8G80 VAL B 43  ? UNP Q62888 ?   ?   'expression tag'        1   108 
2 8G80 LEU B 44  ? UNP Q62888 ?   ?   'expression tag'        2   109 
2 8G80 SER B 45  ? UNP Q62888 ?   ?   'expression tag'        3   110 
2 8G80 GLN B 46  ? UNP Q62888 ?   ?   'expression tag'        4   111 
2 8G80 LYS B 47  ? UNP Q62888 ?   ?   'expression tag'        5   112 
2 8G80 TYR B 48  ? UNP Q62888 ?   ?   'expression tag'        6   113 
2 8G80 PRO B 49  ? UNP Q62888 ?   ?   'expression tag'        7   114 
2 8G80 TYR B 50  ? UNP Q62888 ?   ?   'expression tag'        8   115 
2 8G80 ASP B 51  ? UNP Q62888 ?   ?   'expression tag'        9   116 
2 8G80 VAL B 52  ? UNP Q62888 ?   ?   'expression tag'        10  117 
2 8G80 PRO B 53  ? UNP Q62888 ?   ?   'expression tag'        11  118 
2 8G80 ASP B 54  ? UNP Q62888 ?   ?   'expression tag'        12  119 
2 8G80 TYR B 55  ? UNP Q62888 ?   ?   'expression tag'        13  120 
2 8G80 VAL B 235 ? UNP Q62888 ALA 193 conflict                210 121 
2 8G80 SER B 862 ? UNP Q62888 ?   ?   'expression tag'        837 122 
2 8G80 ASN B 863 ? UNP Q62888 ?   ?   'expression tag'        838 123 
2 8G80 SER B 864 ? UNP Q62888 ?   ?   'expression tag'        839 124 
2 8G80 LEU B 865 ? UNP Q62888 ?   ?   'expression tag'        840 125 
2 8G80 GLU B 866 ? UNP Q62888 ?   ?   'expression tag'        841 126 
2 8G80 VAL B 867 ? UNP Q62888 ?   ?   'expression tag'        842 127 
2 8G80 LEU B 868 ? UNP Q62888 ?   ?   'expression tag'        843 128 
2 8G80 PHE B 869 ? UNP Q62888 ?   ?   'expression tag'        844 129 
2 8G80 GLN B 870 ? UNP Q62888 ?   ?   'expression tag'        845 130 
3 8G80 GLY C 38  ? UNP E0CZA5 SER 38  conflict                15  131 
3 8G80 LYS C 63  ? UNP E0CZA5 ?   ?   insertion               40  132 
3 8G80 GLU C 64  ? UNP E0CZA5 ?   ?   insertion               41  133 
3 8G80 PHE C 65  ? UNP E0CZA5 ?   ?   insertion               42  134 
3 8G80 GLU C 66  ? UNP E0CZA5 ?   ?   insertion               43  135 
3 8G80 GLN C 67  ? UNP E0CZA5 ?   ?   insertion               44  136 
3 8G80 LYS C 68  ? UNP E0CZA5 ?   ?   insertion               45  137 
3 8G80 LEU C 69  ? UNP E0CZA5 ?   ?   insertion               46  138 
3 8G80 ILE C 70  ? UNP E0CZA5 ?   ?   insertion               47  139 
3 8G80 SER C 71  ? UNP E0CZA5 ?   ?   insertion               48  140 
3 8G80 GLU C 72  ? UNP E0CZA5 ?   ?   insertion               49  141 
3 8G80 GLU C 73  ? UNP E0CZA5 ?   ?   insertion               50  142 
3 8G80 ASP C 74  ? UNP E0CZA5 ?   ?   insertion               51  143 
3 8G80 LEU C 75  ? UNP E0CZA5 ?   ?   insertion               52  144 
3 8G80 GLY C 76  ? UNP E0CZA5 ?   ?   insertion               53  145 
3 8G80 PHE C 77  ? UNP E0CZA5 ?   ?   insertion               54  146 
3 8G80 GLU C 78  ? UNP E0CZA5 ?   ?   insertion               55  147 
3 8G80 ILE C 79  ? UNP E0CZA5 ?   ?   insertion               56  148 
3 8G80 ASP C 80  ? UNP E0CZA5 ?   ?   insertion               57  149 
3 8G80 LYS C 81  ? UNP E0CZA5 ?   ?   insertion               58  150 
3 8G80 VAL C 82  ? UNP E0CZA5 ?   ?   insertion               59  151 
3 8G80 TRP C 83  ? UNP E0CZA5 ?   ?   insertion               60  152 
3 8G80 HIS C 84  ? UNP E0CZA5 ?   ?   insertion               61  153 
3 8G80 ASP C 85  ? UNP E0CZA5 ?   ?   insertion               62  154 
3 8G80 PHE C 86  ? UNP E0CZA5 ?   ?   insertion               63  155 
3 8G80 PRO C 87  ? UNP E0CZA5 ?   ?   insertion               64  156 
3 8G80 ALA C 88  ? UNP E0CZA5 ?   ?   insertion               65  157 
3 8G80 THR C 89  ? UNP E0CZA5 ?   ?   insertion               66  158 
3 8G80 SER C 90  ? UNP E0CZA5 ?   ?   insertion               67  159 
4 8G80 SER C 462 ? UNP E0CZA5 ?   ?   'expression tag'        469 160 
4 8G80 ASN C 463 ? UNP E0CZA5 ?   ?   'expression tag'        470 161 
4 8G80 SER C 464 ? UNP E0CZA5 ?   ?   'expression tag'        471 162 
4 8G80 LEU C 465 ? UNP E0CZA5 ?   ?   'expression tag'        472 163 
4 8G80 GLU C 466 ? UNP E0CZA5 ?   ?   'expression tag'        473 164 
4 8G80 VAL C 467 ? UNP E0CZA5 ?   ?   'expression tag'        474 165 
4 8G80 LEU C 468 ? UNP E0CZA5 ?   ?   'expression tag'        475 166 
4 8G80 PHE C 469 ? UNP E0CZA5 ?   ?   'expression tag'        476 167 
4 8G80 GLN C 470 ? UNP E0CZA5 ?   ?   'expression tag'        477 168 
5 8G80 GLY D 38  ? UNP E0CZA5 SER 38  conflict                15  169 
5 8G80 LYS D 63  ? UNP E0CZA5 ?   ?   insertion               40  170 
5 8G80 GLU D 64  ? UNP E0CZA5 ?   ?   insertion               41  171 
5 8G80 PHE D 65  ? UNP E0CZA5 ?   ?   insertion               42  172 
5 8G80 GLU D 66  ? UNP E0CZA5 ?   ?   insertion               43  173 
5 8G80 GLN D 67  ? UNP E0CZA5 ?   ?   insertion               44  174 
5 8G80 LYS D 68  ? UNP E0CZA5 ?   ?   insertion               45  175 
5 8G80 LEU D 69  ? UNP E0CZA5 ?   ?   insertion               46  176 
5 8G80 ILE D 70  ? UNP E0CZA5 ?   ?   insertion               47  177 
5 8G80 SER D 71  ? UNP E0CZA5 ?   ?   insertion               48  178 
5 8G80 GLU D 72  ? UNP E0CZA5 ?   ?   insertion               49  179 
5 8G80 GLU D 73  ? UNP E0CZA5 ?   ?   insertion               50  180 
5 8G80 ASP D 74  ? UNP E0CZA5 ?   ?   insertion               51  181 
5 8G80 LEU D 75  ? UNP E0CZA5 ?   ?   insertion               52  182 
5 8G80 GLY D 76  ? UNP E0CZA5 ?   ?   insertion               53  183 
5 8G80 PHE D 77  ? UNP E0CZA5 ?   ?   insertion               54  184 
5 8G80 GLU D 78  ? UNP E0CZA5 ?   ?   insertion               55  185 
5 8G80 ILE D 79  ? UNP E0CZA5 ?   ?   insertion               56  186 
5 8G80 ASP D 80  ? UNP E0CZA5 ?   ?   insertion               57  187 
5 8G80 LYS D 81  ? UNP E0CZA5 ?   ?   insertion               58  188 
5 8G80 VAL D 82  ? UNP E0CZA5 ?   ?   insertion               59  189 
5 8G80 TRP D 83  ? UNP E0CZA5 ?   ?   insertion               60  190 
5 8G80 HIS D 84  ? UNP E0CZA5 ?   ?   insertion               61  191 
5 8G80 ASP D 85  ? UNP E0CZA5 ?   ?   insertion               62  192 
5 8G80 PHE D 86  ? UNP E0CZA5 ?   ?   insertion               63  193 
5 8G80 PRO D 87  ? UNP E0CZA5 ?   ?   insertion               64  194 
5 8G80 ALA D 88  ? UNP E0CZA5 ?   ?   insertion               65  195 
5 8G80 THR D 89  ? UNP E0CZA5 ?   ?   insertion               66  196 
5 8G80 SER D 90  ? UNP E0CZA5 ?   ?   insertion               67  197 
6 8G80 SER D 462 ? UNP E0CZA5 ?   ?   'expression tag'        469 198 
6 8G80 ASN D 463 ? UNP E0CZA5 ?   ?   'expression tag'        470 199 
6 8G80 SER D 464 ? UNP E0CZA5 ?   ?   'expression tag'        471 200 
6 8G80 LEU D 465 ? UNP E0CZA5 ?   ?   'expression tag'        472 201 
6 8G80 GLU D 466 ? UNP E0CZA5 ?   ?   'expression tag'        473 202 
6 8G80 VAL D 467 ? UNP E0CZA5 ?   ?   'expression tag'        474 203 
6 8G80 LEU D 468 ? UNP E0CZA5 ?   ?   'expression tag'        475 204 
6 8G80 PHE D 469 ? UNP E0CZA5 ?   ?   'expression tag'        476 205 
6 8G80 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 SER A 224 ? ASN A 231 ? SER A 199 ASN A 206 1 ? 8  
HELX_P HELX_P4  AA4 GLY A 242 ? LEU A 247 ? GLY A 217 LEU A 222 1 ? 6  
HELX_P HELX_P5  AA5 ASN A 257 ? ILE A 274 ? ASN A 232 ILE A 249 1 ? 18 
HELX_P HELX_P6  AA6 ALA A 275 ? GLY A 278 ? ALA A 250 GLY A 253 5 ? 4  
HELX_P HELX_P7  AA7 GLY A 290 ? LEU A 301 ? GLY A 265 LEU A 276 1 ? 12 
HELX_P HELX_P8  AA8 GLN A 328 ? GLY A 341 ? GLN A 303 GLY A 316 1 ? 14 
HELX_P HELX_P9  AA9 ASP A 346 ? ARG A 355 ? ASP A 321 ARG A 330 1 ? 10 
HELX_P HELX_P10 AB1 SER A 358 ? ASP A 364 ? SER A 333 ASP A 339 1 ? 7  
HELX_P HELX_P11 AB2 ASP A 388 ? MET A 393 ? ASP A 363 MET A 368 1 ? 6  
HELX_P HELX_P12 AB3 SER A 427 ? TYR A 443 ? SER A 402 TYR A 418 1 ? 17 
HELX_P HELX_P13 AB4 TYR A 445 ? LYS A 449 ? TYR A 420 LYS A 424 5 ? 5  
HELX_P HELX_P14 AB5 ASP A 450 ? TYR A 460 ? ASP A 425 TYR A 435 1 ? 11 
HELX_P HELX_P15 AB6 GLY A 469 ? TRP A 485 ? GLY A 444 TRP A 460 1 ? 17 
HELX_P HELX_P16 AB7 TRP A 485 ? TYR A 499 ? TRP A 460 TYR A 474 1 ? 15 
HELX_P HELX_P17 AB8 GLU A 528 ? PHE A 533 ? GLU A 503 PHE A 508 1 ? 6  
HELX_P HELX_P18 AB9 SER A 549 ? GLY A 570 ? SER A 524 GLY A 545 1 ? 22 
HELX_P HELX_P19 AC1 ARG A 619 ? GLU A 628 ? ARG A 594 GLU A 603 1 ? 10 
HELX_P HELX_P20 AC2 GLU A 628 ? LEU A 633 ? GLU A 603 LEU A 608 1 ? 6  
HELX_P HELX_P21 AC3 PRO B 162 ? ASN B 168 ? PRO B 120 ASN B 126 1 ? 7  
HELX_P HELX_P22 AC4 ASN B 168 ? VAL B 176 ? ASN B 126 VAL B 134 1 ? 9  
HELX_P HELX_P23 AC5 GLY B 223 ? ASN B 231 ? GLY B 198 ASN B 206 1 ? 9  
HELX_P HELX_P24 AC6 GLY B 242 ? LEU B 247 ? GLY B 217 LEU B 222 1 ? 6  
HELX_P HELX_P25 AC7 ASN B 257 ? ILE B 274 ? ASN B 232 ILE B 249 1 ? 18 
HELX_P HELX_P26 AC8 GLY B 290 ? LEU B 299 ? GLY B 265 LEU B 274 1 ? 10 
HELX_P HELX_P27 AC9 GLN B 328 ? GLY B 341 ? GLN B 303 GLY B 316 1 ? 14 
HELX_P HELX_P28 AD1 ASP B 346 ? ARG B 355 ? ASP B 321 ARG B 330 1 ? 10 
HELX_P HELX_P29 AD2 ASP B 388 ? GLN B 395 ? ASP B 363 GLN B 370 1 ? 8  
HELX_P HELX_P30 AD3 SER B 427 ? TYR B 443 ? SER B 402 TYR B 418 1 ? 17 
HELX_P HELX_P31 AD4 VAL B 451 ? TYR B 460 ? VAL B 426 TYR B 435 1 ? 10 
HELX_P HELX_P32 AD5 ASP B 462 ? ARG B 466 ? ASP B 437 ARG B 441 5 ? 5  
HELX_P HELX_P33 AD6 ARG B 472 ? TRP B 485 ? ARG B 447 TRP B 460 1 ? 14 
HELX_P HELX_P34 AD7 TRP B 485 ? ASP B 498 ? TRP B 460 ASP B 473 1 ? 14 
HELX_P HELX_P35 AD8 GLU B 528 ? PHE B 533 ? GLU B 503 PHE B 508 1 ? 6  
HELX_P HELX_P36 AD9 SER B 549 ? GLY B 570 ? SER B 524 GLY B 545 1 ? 22 
HELX_P HELX_P37 AE1 ARG B 619 ? LEU B 629 ? ARG B 594 LEU B 604 1 ? 11 
HELX_P HELX_P38 AE2 VAL B 630 ? LEU B 633 ? VAL B 605 LEU B 608 5 ? 4  
HELX_P HELX_P39 AE3 VAL C 261 ? GLU C 267 ? VAL C 268 GLU C 274 1 ? 7  
HELX_P HELX_P40 AE4 PRO D 124 ? ARG D 128 ? PRO D 101 ARG D 105 5 ? 5  
HELX_P HELX_P41 AE5 VAL D 261 ? ALA D 266 ? VAL D 268 ALA D 273 1 ? 6  
# 
_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 ? ? ? ? ? ? ? 2.031 ? ?               
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 1017 1_555 ? ? ? ? ? ? ? 1.440 ? N-Glycosylation 
covale2  covale one ? A ASN 547 ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 522 A NAG 1018 1_555 ? ? ? ? ? ? ? 1.439 ? N-Glycosylation 
covale3  covale one ? B ASN 140 ND2 ? ? ? 1_555 G NAG .   C1 ? ? B ASN 98  B NAG 1017 1_555 ? ? ? ? ? ? ? 1.440 ? N-Glycosylation 
covale4  covale one ? B ASN 547 ND2 ? ? ? 1_555 H NAG .   C1 ? ? B ASN 522 B NAG 1018 1_555 ? ? ? ? ? ? ? 1.441 ? N-Glycosylation 
covale5  covale one ? C ASN 207 ND2 ? ? ? 1_555 J NAG .   C1 ? ? C ASN 184 C NAG 1008 1_555 ? ? ? ? ? ? ? 1.439 ? N-Glycosylation 
covale6  covale one ? D ASN 207 ND2 ? ? ? 1_555 L NAG .   C1 ? ? D ASN 184 D NAG 1008 1_555 ? ? ? ? ? ? ? 1.442 ? N-Glycosylation 
metalc1  metalc ?   ? C ASP 160 OD1 ? ? ? 1_555 I CA  .   CA ? ? C ASP 137 C CA  1007 1_555 ? ? ? ? ? ? ? 2.920 ? ?               
metalc2  metalc ?   ? C ASP 160 OD2 ? ? ? 1_555 I CA  .   CA ? ? C ASP 137 C CA  1007 1_555 ? ? ? ? ? ? ? 2.924 ? ?               
metalc3  metalc ?   ? C VAL 177 O   ? ? ? 1_555 I CA  .   CA ? ? C VAL 154 C CA  1007 1_555 ? ? ? ? ? ? ? 2.526 ? ?               
metalc4  metalc ?   ? C ILE 229 O   ? ? ? 1_555 I CA  .   CA ? ? C ILE 236 C CA  1007 1_555 ? ? ? ? ? ? ? 2.703 ? ?               
metalc5  metalc ?   ? C ASN 231 OD1 ? ? ? 1_555 I CA  .   CA ? ? C ASN 238 C CA  1007 1_555 ? ? ? ? ? ? ? 2.339 ? ?               
metalc6  metalc ?   ? D ASP 160 OD1 ? ? ? 1_555 K CA  .   CA ? ? D ASP 137 D CA  1007 1_555 ? ? ? ? ? ? ? 3.018 ? ?               
metalc7  metalc ?   ? D ASP 160 OD2 ? ? ? 1_555 K CA  .   CA ? ? D ASP 137 D CA  1007 1_555 ? ? ? ? ? ? ? 2.873 ? ?               
metalc8  metalc ?   ? D VAL 177 O   ? ? ? 1_555 K CA  .   CA ? ? D VAL 154 D CA  1007 1_555 ? ? ? ? ? ? ? 2.990 ? ?               
metalc9  metalc ?   ? D ILE 229 O   ? ? ? 1_555 K CA  .   CA ? ? D ILE 236 D CA  1007 1_555 ? ? ? ? ? ? ? 2.638 ? ?               
metalc10 metalc ?   ? D ASN 231 OD1 ? ? ? 1_555 K CA  .   CA ? ? D ASN 238 D CA  1007 1_555 ? ? ? ? ? ? ? 2.368 ? ?               
# 
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 1007 ? 1_555 OD2 ? C ASP 160 ? C ASP 137 ? 1_555 44.0  ? 
2  OD1 ? C ASP 160 ? C ASP 137 ? 1_555 CA ? I CA . ? C CA 1007 ? 1_555 O   ? C VAL 177 ? C VAL 154 ? 1_555 67.7  ? 
3  OD2 ? C ASP 160 ? C ASP 137 ? 1_555 CA ? I CA . ? C CA 1007 ? 1_555 O   ? C VAL 177 ? C VAL 154 ? 1_555 111.3 ? 
4  OD1 ? C ASP 160 ? C ASP 137 ? 1_555 CA ? I CA . ? C CA 1007 ? 1_555 O   ? C ILE 229 ? C ILE 236 ? 1_555 106.6 ? 
5  OD2 ? C ASP 160 ? C ASP 137 ? 1_555 CA ? I CA . ? C CA 1007 ? 1_555 O   ? C ILE 229 ? C ILE 236 ? 1_555 96.9  ? 
6  O   ? C VAL 177 ? C VAL 154 ? 1_555 CA ? I CA . ? C CA 1007 ? 1_555 O   ? C ILE 229 ? C ILE 236 ? 1_555 95.4  ? 
7  OD1 ? C ASP 160 ? C ASP 137 ? 1_555 CA ? I CA . ? C CA 1007 ? 1_555 OD1 ? C ASN 231 ? C ASN 238 ? 1_555 109.9 ? 
8  OD2 ? C ASP 160 ? C ASP 137 ? 1_555 CA ? I CA . ? C CA 1007 ? 1_555 OD1 ? C ASN 231 ? C ASN 238 ? 1_555 65.8  ? 
9  O   ? C VAL 177 ? C VAL 154 ? 1_555 CA ? I CA . ? C CA 1007 ? 1_555 OD1 ? C ASN 231 ? C ASN 238 ? 1_555 172.7 ? 
10 O   ? C ILE 229 ? C ILE 236 ? 1_555 CA ? I CA . ? C CA 1007 ? 1_555 OD1 ? C ASN 231 ? C ASN 238 ? 1_555 78.5  ? 
11 OD1 ? D ASP 160 ? D ASP 137 ? 1_555 CA ? K CA . ? D CA 1007 ? 1_555 OD2 ? D ASP 160 ? D ASP 137 ? 1_555 43.6  ? 
12 OD1 ? D ASP 160 ? D ASP 137 ? 1_555 CA ? K CA . ? D CA 1007 ? 1_555 O   ? D VAL 177 ? D VAL 154 ? 1_555 63.3  ? 
13 OD2 ? D ASP 160 ? D ASP 137 ? 1_555 CA ? K CA . ? D CA 1007 ? 1_555 O   ? D VAL 177 ? D VAL 154 ? 1_555 106.1 ? 
14 OD1 ? D ASP 160 ? D ASP 137 ? 1_555 CA ? K CA . ? D CA 1007 ? 1_555 O   ? D ILE 229 ? D ILE 236 ? 1_555 82.5  ? 
15 OD2 ? D ASP 160 ? D ASP 137 ? 1_555 CA ? K CA . ? D CA 1007 ? 1_555 O   ? D ILE 229 ? D ILE 236 ? 1_555 94.5  ? 
16 O   ? D VAL 177 ? D VAL 154 ? 1_555 CA ? K CA . ? D CA 1007 ? 1_555 O   ? D ILE 229 ? D ILE 236 ? 1_555 84.3  ? 
17 OD1 ? D ASP 160 ? D ASP 137 ? 1_555 CA ? K CA . ? D CA 1007 ? 1_555 OD1 ? D ASN 231 ? D ASN 238 ? 1_555 107.1 ? 
18 OD2 ? D ASP 160 ? D ASP 137 ? 1_555 CA ? K CA . ? D CA 1007 ? 1_555 OD1 ? D ASN 231 ? D ASN 238 ? 1_555 70.0  ? 
19 O   ? D VAL 177 ? D VAL 154 ? 1_555 CA ? K CA . ? D CA 1007 ? 1_555 OD1 ? D ASN 231 ? D ASN 238 ? 1_555 158.5 ? 
20 O   ? D ILE 229 ? D ILE 236 ? 1_555 CA ? K CA . ? D CA 1007 ? 1_555 OD1 ? D ASN 231 ? D ASN 238 ? 1_555 75.2  ? 
# 
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 1017 ? 1_555 ASN A 98  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG F .   ? ASN A 547 ? NAG A 1018 ? 1_555 ASN A 522 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG G .   ? ASN B 140 ? NAG B 1017 ? 1_555 ASN B 98  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG H .   ? ASN B 547 ? NAG B 1018 ? 1_555 ASN B 522 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  NAG J .   ? ASN C 207 ? NAG C 1008 ? 1_555 ASN C 184 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6  NAG L .   ? ASN D 207 ? NAG D 1008 ? 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 ? 8 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 8 ? 
AA6 ? 2 ? 
AA7 ? 8 ? 
AA8 ? 7 ? 
AA9 ? 8 ? 
AB1 ? 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      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? 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      
AA6 1 2 ? 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 
AA7 7 8 ? 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 
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 
AA9 7 8 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB1 5 6 ? anti-parallel 
AB1 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 85  ? ASN A 87  ? VAL A 43  ASN A 45  
AA1 2 ARG A 92  ? ARG A 94  ? ARG A 50  ARG A 52  
AA1 3 VAL A 138 ? ASN A 140 ? VAL A 96  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 ? ASN A 238 ? ILE A 208 ASN A 213 
AA2 4 VAL A 204 ? PHE A 207 ? VAL A 179 PHE A 182 
AA2 5 ILE A 284 ? SER A 289 ? ILE A 259 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 
AA3 1 TYR A 605 ? LEU A 606 ? TYR A 580 LEU A 581 
AA3 2 VAL A 614 ? ARG A 615 ? VAL A 589 ARG A 590 
AA4 1 VAL B 85  ? ASN B 87  ? VAL B 43  ASN B 45  
AA4 2 ARG B 92  ? ARG B 94  ? ARG B 50  ARG B 52  
AA4 3 VAL B 138 ? ASN B 140 ? VAL B 96  ASN B 98  
AA5 1 VAL B 108 ? PRO B 115 ? VAL B 66  PRO B 73  
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 
AA6 1 TYR B 605 ? LEU B 606 ? TYR B 580 LEU B 581 
AA6 2 VAL B 614 ? ARG B 615 ? VAL B 589 ARG B 590 
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 THR C 109 ? LYS C 122 ? THR C 86  LYS C 99  
AA7 7 GLN C 250 ? TYR C 256 ? GLN C 257 TYR C 263 
AA7 8 LEU C 259 ? LYS C 260 ? LEU C 266 LYS C 267 
AA8 1 ILE C 218 ? ARG C 220 ? ILE C 195 ARG C 197 
AA8 2 ASN C 207 ? VAL C 212 ? ASN C 184 VAL C 189 
AA8 3 HIS C 197 ? SER C 204 ? HIS C 174 SER C 181 
AA8 4 ALA C 133 ? SER C 141 ? ALA C 110 SER C 118 
AA8 5 GLN C 250 ? TYR C 256 ? GLN C 257 TYR C 263 
AA8 6 THR C 109 ? LYS C 122 ? THR C 86  LYS C 99  
AA8 7 ALA C 273 ? VAL C 281 ? ALA C 280 VAL C 288 
AA9 1 ASP D 181 ? GLU D 185 ? ASP D 158 GLU D 162 
AA9 2 LYS D 170 ? ASN D 176 ? LYS D 147 ASN D 153 
AA9 3 TYR D 161 ? HIS D 167 ? TYR D 138 HIS D 144 
AA9 4 GLU D 146 ? SER D 154 ? GLU D 123 SER D 131 
AA9 5 GLN D 233 ? ILE D 238 ? GLN D 240 ILE D 245 
AA9 6 TYR D 110 ? LYS D 122 ? TYR D 87  LYS D 99  
AA9 7 GLN D 250 ? TYR D 256 ? GLN D 257 TYR D 263 
AA9 8 LEU D 259 ? LYS D 260 ? LEU D 266 LYS D 267 
AB1 1 ILE D 218 ? ARG D 220 ? ILE D 195 ARG D 197 
AB1 2 ASN D 207 ? VAL D 212 ? ASN D 184 VAL D 189 
AB1 3 HIS D 197 ? SER D 204 ? HIS D 174 SER D 181 
AB1 4 ALA D 133 ? SER D 141 ? ALA D 110 SER D 118 
AB1 5 GLN D 250 ? TYR D 256 ? GLN D 257 TYR D 263 
AB1 6 TYR D 110 ? LYS D 122 ? TYR D 87  LYS D 99  
AB1 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 VAL A 86  ? N VAL A 44  O VAL A 93  ? O VAL A 51  
AA1 2 3 N ARG A 94  ? N ARG A 52  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 TYR A 185 ? N TYR A 143 O ASN A 238 ? O ASN A 213 
AA2 3 4 O VAL A 235 ? O VAL A 210 N MET A 205 ? N MET A 180 
AA2 4 5 N VAL A 204 ? N VAL A 179 O THR A 285 ? O THR A 260 
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 
AA3 1 2 N TYR A 605 ? N TYR A 580 O ARG A 615 ? O ARG A 590 
AA4 1 2 N VAL B 86  ? N VAL B 44  O VAL B 93  ? O VAL B 51  
AA4 2 3 N ARG B 92  ? N ARG B 50  O ARG B 139 ? O ARG B 97  
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 VAL B 235 ? O VAL B 210 N MET B 205 ? N MET B 180 
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 
AA6 1 2 N TYR B 605 ? N TYR B 580 O ARG B 615 ? O ARG B 590 
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 236 ? O ILE C 243 N TYR C 121 ? N TYR C 98  
AA7 6 7 N TYR C 110 ? N TYR C 87  O LEU C 251 ? O LEU C 258 
AA7 7 8 N TYR C 256 ? N TYR C 263 O LEU C 259 ? O LEU C 266 
AA8 1 2 O ARG C 220 ? O ARG C 197 N ALA C 208 ? N ALA C 185 
AA8 2 3 O GLN C 211 ? O GLN C 188 N ARG C 200 ? N ARG C 177 
AA8 3 4 O ARG C 203 ? O ARG C 180 N ASP C 134 ? N ASP C 111 
AA8 4 5 N ALA C 137 ? N ALA C 114 O TYR C 255 ? O TYR C 262 
AA8 5 6 O LEU C 251 ? O LEU C 258 N TYR C 110 ? N TYR C 87  
AA8 6 7 N ILE C 111 ? N ILE C 88  O ARG C 279 ? O ARG C 286 
AA9 1 2 O ILE D 182 ? O ILE D 159 N PHE D 175 ? N PHE D 152 
AA9 2 3 O LYS D 170 ? O LYS D 147 N HIS D 167 ? N HIS D 144 
AA9 3 4 O LEU D 162 ? O LEU D 139 N VAL D 152 ? N VAL D 129 
AA9 4 5 N ARG D 151 ? N ARG D 128 O ILE D 237 ? O ILE D 244 
AA9 5 6 O ILE D 238 ? O ILE D 245 N ILE D 119 ? N ILE D 96  
AA9 6 7 N TYR D 110 ? N TYR D 87  O LEU D 251 ? O LEU D 258 
AA9 7 8 N TYR D 256 ? N TYR D 263 O LEU D 259 ? O LEU D 266 
AB1 1 2 O ILE D 218 ? O ILE D 195 N LEU D 210 ? N LEU D 187 
AB1 2 3 O ASN D 207 ? O ASN D 184 N SER D 204 ? N SER D 181 
AB1 3 4 O PHE D 201 ? O PHE D 178 N LEU D 136 ? N LEU D 113 
AB1 4 5 N ALA D 137 ? N ALA D 114 O TYR D 255 ? O TYR D 262 
AB1 5 6 O LEU D 251 ? O LEU D 258 N TYR D 110 ? N TYR D 87  
AB1 6 7 N THR D 120 ? N THR D 97  O ALA D 273 ? O ALA D 280 
# 
_pdbx_entry_details.entry_id                   8G80 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   ND2 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   ASN 
_pdbx_validate_close_contact.auth_seq_id_1    522 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O5 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   NAG 
_pdbx_validate_close_contact.auth_seq_id_2    1018 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.14 
# 
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 PRO A 90  ? ? -69.97  -178.83 
2  1 HIS A 111 ? ? -90.90  52.60   
3  1 ASN A 126 ? ? -98.47  59.56   
4  1 GLU A 281 ? ? -94.27  -60.51  
5  1 MET A 446 ? ? -84.71  46.23   
6  1 ARG A 447 ? ? -131.69 -34.36  
7  1 ASN B 126 ? ? -95.33  55.08   
8  1 SER B 187 ? ? -126.98 -169.31 
9  1 GLN B 370 ? ? -93.67  50.41   
10 1 ARG B 447 ? ? -130.44 -31.03  
11 1 PRO B 547 ? ? -69.75  7.51    
12 1 THR C 156 ? ? -94.45  -62.81  
13 1 ASN C 165 ? ? -90.26  52.98   
14 1 ASN C 169 ? ? -91.08  52.88   
15 1 ASP C 190 ? ? 51.19   -121.49 
16 1 ASP D 190 ? ? 60.28   -135.26 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8G80 
_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                    8G80 
_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                  3.25 
_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               50603 
_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 two' 
_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                8G80 
_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                        8G80 
_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              8G80 
_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                8G80 
_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              8G80 
_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 SER 174 ? A SER 199 
89   1 Y 1 A ASP 554 ? A ASP 579 
90   1 Y 1 A THR 555 ? A THR 580 
91   1 Y 1 A LYS 556 ? A LYS 581 
92   1 Y 1 A PHE 557 ? A PHE 582 
93   1 Y 1 A ILE 558 ? A ILE 583 
94   1 Y 1 A HIS 559 ? A HIS 584 
95   1 Y 1 A THR 560 ? A THR 585 
96   1 Y 1 A LYS 561 ? A LYS 586 
97   1 Y 1 A PRO 562 ? A PRO 587 
98   1 Y 1 A ASN 563 ? A ASN 588 
99   1 Y 1 A HIS 609 ? A HIS 634 
100  1 Y 1 A ASN 610 ? A ASN 635 
101  1 Y 1 A LEU 611 ? A LEU 636 
102  1 Y 1 A HIS 612 ? A HIS 637 
103  1 Y 1 A THR 613 ? A THR 638 
104  1 Y 1 A GLU 614 ? A GLU 639 
105  1 Y 1 A LEU 615 ? A LEU 640 
106  1 Y 1 A PHE 616 ? A PHE 641 
107  1 Y 1 A THR 617 ? A THR 642 
108  1 Y 1 A THR 618 ? A THR 643 
109  1 Y 1 A THR 619 ? A THR 644 
110  1 Y 1 A THR 620 ? A THR 645 
111  1 Y 1 A ARG 621 ? A ARG 646 
112  1 Y 1 A LEU 622 ? A LEU 647 
113  1 Y 1 A PRO 623 ? A PRO 648 
114  1 Y 1 A PRO 624 ? A PRO 649 
115  1 Y 1 A TYR 625 ? A TYR 650 
116  1 Y 1 A ALA 626 ? A ALA 651 
117  1 Y 1 A THR 627 ? A THR 652 
118  1 Y 1 A ARG 628 ? A ARG 653 
119  1 Y 1 A TRP 629 ? A TRP 654 
120  1 Y 1 A PRO 630 ? A PRO 655 
121  1 Y 1 A PRO 631 ? A PRO 656 
122  1 Y 1 A ARG 632 ? A ARG 657 
123  1 Y 1 A THR 633 ? A THR 658 
124  1 Y 1 A PRO 634 ? A PRO 659 
125  1 Y 1 A GLY 635 ? A GLY 660 
126  1 Y 1 A PRO 636 ? A PRO 661 
127  1 Y 1 A GLY 637 ? A GLY 662 
128  1 Y 1 A THR 638 ? A THR 663 
129  1 Y 1 A SER 639 ? A SER 664 
130  1 Y 1 A GLY 640 ? A GLY 665 
131  1 Y 1 A THR 641 ? A THR 666 
132  1 Y 1 A ARG 642 ? A ARG 667 
133  1 Y 1 A ARG 643 ? A ARG 668 
134  1 Y 1 A PRO 644 ? A PRO 669 
135  1 Y 1 A PRO 645 ? A PRO 670 
136  1 Y 1 A PRO 646 ? A PRO 671 
137  1 Y 1 A PRO 647 ? A PRO 672 
138  1 Y 1 A ALA 648 ? A ALA 673 
139  1 Y 1 A THR 649 ? A THR 674 
140  1 Y 1 A LEU 650 ? A LEU 675 
141  1 Y 1 A PRO 651 ? A PRO 676 
142  1 Y 1 A PRO 652 ? A PRO 677 
143  1 Y 1 A GLU 653 ? A GLU 678 
144  1 Y 1 A SER 654 ? A SER 679 
145  1 Y 1 A ASP 655 ? A ASP 680 
146  1 Y 1 A ILE 656 ? A ILE 681 
147  1 Y 1 A ASP 657 ? A ASP 682 
148  1 Y 1 A LEU 658 ? A LEU 683 
149  1 Y 1 A GLY 659 ? A GLY 684 
150  1 Y 1 A PRO 660 ? A PRO 685 
151  1 Y 1 A ARG 661 ? A ARG 686 
152  1 Y 1 A ALA 662 ? A ALA 687 
153  1 Y 1 A TYR 663 ? A TYR 688 
154  1 Y 1 A ASP 664 ? A ASP 689 
155  1 Y 1 A ARG 665 ? A ARG 690 
156  1 Y 1 A PHE 666 ? A PHE 691 
157  1 Y 1 A PRO 667 ? A PRO 692 
158  1 Y 1 A GLY 668 ? A GLY 693 
159  1 Y 1 A ASP 669 ? A ASP 694 
160  1 Y 1 A SER 670 ? A SER 695 
161  1 Y 1 A ARG 671 ? A ARG 696 
162  1 Y 1 A ASP 672 ? A ASP 697 
163  1 Y 1 A TYR 673 ? A TYR 698 
164  1 Y 1 A SER 674 ? A SER 699 
165  1 Y 1 A THR 675 ? A THR 700 
166  1 Y 1 A GLU 676 ? A GLU 701 
167  1 Y 1 A LEU 677 ? A LEU 702 
168  1 Y 1 A SER 678 ? A SER 703 
169  1 Y 1 A VAL 679 ? A VAL 704 
170  1 Y 1 A THR 680 ? A THR 705 
171  1 Y 1 A VAL 681 ? A VAL 706 
172  1 Y 1 A ALA 682 ? A ALA 707 
173  1 Y 1 A VAL 683 ? A VAL 708 
174  1 Y 1 A GLY 684 ? A GLY 709 
175  1 Y 1 A ALA 685 ? A ALA 710 
176  1 Y 1 A SER 686 ? A SER 711 
177  1 Y 1 A LEU 687 ? A LEU 712 
178  1 Y 1 A LEU 688 ? A LEU 713 
179  1 Y 1 A PHE 689 ? A PHE 714 
180  1 Y 1 A LEU 690 ? A LEU 715 
181  1 Y 1 A ASN 691 ? A ASN 716 
182  1 Y 1 A ILE 692 ? A ILE 717 
183  1 Y 1 A LEU 693 ? A LEU 718 
184  1 Y 1 A ALA 694 ? A ALA 719 
185  1 Y 1 A PHE 695 ? A PHE 720 
186  1 Y 1 A ALA 696 ? A ALA 721 
187  1 Y 1 A ALA 697 ? A ALA 722 
188  1 Y 1 A LEU 698 ? A LEU 723 
189  1 Y 1 A TYR 699 ? A TYR 724 
190  1 Y 1 A TYR 700 ? A TYR 725 
191  1 Y 1 A LYS 701 ? A LYS 726 
192  1 Y 1 A ARG 702 ? A ARG 727 
193  1 Y 1 A ASP 703 ? A ASP 728 
194  1 Y 1 A ARG 704 ? A ARG 729 
195  1 Y 1 A ARG 705 ? A ARG 730 
196  1 Y 1 A GLN 706 ? A GLN 731 
197  1 Y 1 A GLU 707 ? A GLU 732 
198  1 Y 1 A LEU 708 ? A LEU 733 
199  1 Y 1 A ARG 709 ? A ARG 734 
200  1 Y 1 A CYS 710 ? A CYS 735 
201  1 Y 1 A ARG 711 ? A ARG 736 
202  1 Y 1 A ARG 712 ? A ARG 737 
203  1 Y 1 A LEU 713 ? A LEU 738 
204  1 Y 1 A SER 714 ? A SER 739 
205  1 Y 1 A PRO 715 ? A PRO 740 
206  1 Y 1 A PRO 716 ? A PRO 741 
207  1 Y 1 A GLY 717 ? A GLY 742 
208  1 Y 1 A GLY 718 ? A GLY 743 
209  1 Y 1 A SER 719 ? A SER 744 
210  1 Y 1 A GLY 720 ? A GLY 745 
211  1 Y 1 A SER 721 ? A SER 746 
212  1 Y 1 A GLY 722 ? A GLY 747 
213  1 Y 1 A VAL 723 ? A VAL 748 
214  1 Y 1 A PRO 724 ? A PRO 749 
215  1 Y 1 A GLY 725 ? A GLY 750 
216  1 Y 1 A GLY 726 ? A GLY 751 
217  1 Y 1 A GLY 727 ? A GLY 752 
218  1 Y 1 A PRO 728 ? A PRO 753 
219  1 Y 1 A LEU 729 ? A LEU 754 
220  1 Y 1 A LEU 730 ? A LEU 755 
221  1 Y 1 A PRO 731 ? A PRO 756 
222  1 Y 1 A THR 732 ? A THR 757 
223  1 Y 1 A ALA 733 ? A ALA 758 
224  1 Y 1 A GLY 734 ? A GLY 759 
225  1 Y 1 A ARG 735 ? A ARG 760 
226  1 Y 1 A GLU 736 ? A GLU 761 
227  1 Y 1 A LEU 737 ? A LEU 762 
228  1 Y 1 A PRO 738 ? A PRO 763 
229  1 Y 1 A PRO 739 ? A PRO 764 
230  1 Y 1 A GLU 740 ? A GLU 765 
231  1 Y 1 A GLU 741 ? A GLU 766 
232  1 Y 1 A GLU 742 ? A GLU 767 
233  1 Y 1 A LEU 743 ? A LEU 768 
234  1 Y 1 A VAL 744 ? A VAL 769 
235  1 Y 1 A SER 745 ? A SER 770 
236  1 Y 1 A LEU 746 ? A LEU 771 
237  1 Y 1 A GLN 747 ? A GLN 772 
238  1 Y 1 A LEU 748 ? A LEU 773 
239  1 Y 1 A LYS 749 ? A LYS 774 
240  1 Y 1 A ARG 750 ? A ARG 775 
241  1 Y 1 A GLY 751 ? A GLY 776 
242  1 Y 1 A GLY 752 ? A GLY 777 
243  1 Y 1 A GLY 753 ? A GLY 778 
244  1 Y 1 A VAL 754 ? A VAL 779 
245  1 Y 1 A GLY 755 ? A GLY 780 
246  1 Y 1 A ALA 756 ? A ALA 781 
247  1 Y 1 A ASP 757 ? A ASP 782 
248  1 Y 1 A PRO 758 ? A PRO 783 
249  1 Y 1 A ALA 759 ? A ALA 784 
250  1 Y 1 A GLU 760 ? A GLU 785 
251  1 Y 1 A ALA 761 ? A ALA 786 
252  1 Y 1 A LEU 762 ? A LEU 787 
253  1 Y 1 A ARG 763 ? A ARG 788 
254  1 Y 1 A PRO 764 ? A PRO 789 
255  1 Y 1 A ALA 765 ? A ALA 790 
256  1 Y 1 A CYS 766 ? A CYS 791 
257  1 Y 1 A PRO 767 ? A PRO 792 
258  1 Y 1 A PRO 768 ? A PRO 793 
259  1 Y 1 A ASP 769 ? A ASP 794 
260  1 Y 1 A TYR 770 ? A TYR 795 
261  1 Y 1 A THR 771 ? A THR 796 
262  1 Y 1 A LEU 772 ? A LEU 797 
263  1 Y 1 A ALA 773 ? A ALA 798 
264  1 Y 1 A LEU 774 ? A LEU 799 
265  1 Y 1 A ARG 775 ? A ARG 800 
266  1 Y 1 A ARG 776 ? A ARG 801 
267  1 Y 1 A ALA 777 ? A ALA 802 
268  1 Y 1 A PRO 778 ? A PRO 803 
269  1 Y 1 A ASP 779 ? A ASP 804 
270  1 Y 1 A ASP 780 ? A ASP 805 
271  1 Y 1 A VAL 781 ? A VAL 806 
272  1 Y 1 A PRO 782 ? A PRO 807 
273  1 Y 1 A LEU 783 ? A LEU 808 
274  1 Y 1 A LEU 784 ? A LEU 809 
275  1 Y 1 A ALA 785 ? A ALA 810 
276  1 Y 1 A PRO 786 ? A PRO 811 
277  1 Y 1 A GLY 787 ? A GLY 812 
278  1 Y 1 A ALA 788 ? A ALA 813 
279  1 Y 1 A LEU 789 ? A LEU 814 
280  1 Y 1 A THR 790 ? A THR 815 
281  1 Y 1 A LEU 791 ? A LEU 816 
282  1 Y 1 A LEU 792 ? A LEU 817 
283  1 Y 1 A PRO 793 ? A PRO 818 
284  1 Y 1 A SER 794 ? A SER 819 
285  1 Y 1 A GLY 795 ? A GLY 820 
286  1 Y 1 A LEU 796 ? A LEU 821 
287  1 Y 1 A GLY 797 ? A GLY 822 
288  1 Y 1 A PRO 798 ? A PRO 823 
289  1 Y 1 A PRO 799 ? A PRO 824 
290  1 Y 1 A PRO 800 ? A PRO 825 
291  1 Y 1 A PRO 801 ? A PRO 826 
292  1 Y 1 A PRO 802 ? A PRO 827 
293  1 Y 1 A PRO 803 ? A PRO 828 
294  1 Y 1 A PRO 804 ? A PRO 829 
295  1 Y 1 A PRO 805 ? A PRO 830 
296  1 Y 1 A SER 806 ? A SER 831 
297  1 Y 1 A LEU 807 ? A LEU 832 
298  1 Y 1 A HIS 808 ? A HIS 833 
299  1 Y 1 A PRO 809 ? A PRO 834 
300  1 Y 1 A PHE 810 ? A PHE 835 
301  1 Y 1 A GLY 811 ? A GLY 836 
302  1 Y 1 A PRO 812 ? A PRO 837 
303  1 Y 1 A PHE 813 ? A PHE 838 
304  1 Y 1 A PRO 814 ? A PRO 839 
305  1 Y 1 A PRO 815 ? A PRO 840 
306  1 Y 1 A PRO 816 ? A PRO 841 
307  1 Y 1 A PRO 817 ? A PRO 842 
308  1 Y 1 A PRO 818 ? A PRO 843 
309  1 Y 1 A THR 819 ? A THR 844 
310  1 Y 1 A ALA 820 ? A ALA 845 
311  1 Y 1 A THR 821 ? A THR 846 
312  1 Y 1 A SER 822 ? A SER 847 
313  1 Y 1 A HIS 823 ? A HIS 848 
314  1 Y 1 A ASN 824 ? A ASN 849 
315  1 Y 1 A ASN 825 ? A ASN 850 
316  1 Y 1 A THR 826 ? A THR 851 
317  1 Y 1 A LEU 827 ? A LEU 852 
318  1 Y 1 A PRO 828 ? A PRO 853 
319  1 Y 1 A HIS 829 ? A HIS 854 
320  1 Y 1 A PRO 830 ? A PRO 855 
321  1 Y 1 A HIS 831 ? A HIS 856 
322  1 Y 1 A SER 832 ? A SER 857 
323  1 Y 1 A THR 833 ? A THR 858 
324  1 Y 1 A THR 834 ? A THR 859 
325  1 Y 1 A ARG 835 ? A ARG 860 
326  1 Y 1 A VAL 836 ? A VAL 861 
327  1 Y 1 A SER 837 ? A SER 862 
328  1 Y 1 A ASN 838 ? A ASN 863 
329  1 Y 1 A SER 839 ? A SER 864 
330  1 Y 1 A LEU 840 ? A LEU 865 
331  1 Y 1 A GLU 841 ? A GLU 866 
332  1 Y 1 A VAL 842 ? A VAL 867 
333  1 Y 1 A LEU 843 ? A LEU 868 
334  1 Y 1 A PHE 844 ? A PHE 869 
335  1 Y 1 A GLN 845 ? A GLN 870 
336  1 Y 1 B MET -41 ? B MET 1   
337  1 Y 1 B ALA -40 ? B ALA 2   
338  1 Y 1 B LEU -39 ? B LEU 3   
339  1 Y 1 B PRO -38 ? B PRO 4   
340  1 Y 1 B ARG -37 ? B ARG 5   
341  1 Y 1 B CYS -36 ? B CYS 6   
342  1 Y 1 B MET -35 ? B MET 7   
343  1 Y 1 B TRP -34 ? B TRP 8   
344  1 Y 1 B PRO -33 ? B PRO 9   
345  1 Y 1 B ASN -32 ? B ASN 10  
346  1 Y 1 B TYR -31 ? B TYR 11  
347  1 Y 1 B VAL -30 ? B VAL 12  
348  1 Y 1 B TRP -29 ? B TRP 13  
349  1 Y 1 B ARG -28 ? B ARG 14  
350  1 Y 1 B ALA -27 ? B ALA 15  
351  1 Y 1 B MET -26 ? B MET 16  
352  1 Y 1 B MET -25 ? B MET 17  
353  1 Y 1 B ALA -24 ? B ALA 18  
354  1 Y 1 B CYS -23 ? B CYS 19  
355  1 Y 1 B VAL -22 ? B VAL 20  
356  1 Y 1 B VAL -21 ? B VAL 21  
357  1 Y 1 B HIS -20 ? B HIS 22  
358  1 Y 1 B ARG -19 ? B ARG 23  
359  1 Y 1 B GLY -18 ? B GLY 24  
360  1 Y 1 B SER -17 ? B SER 25  
361  1 Y 1 B GLY -16 ? B GLY 26  
362  1 Y 1 B ALA -15 ? B ALA 27  
363  1 Y 1 B PRO -14 ? B PRO 28  
364  1 Y 1 B LEU -13 ? B LEU 29  
365  1 Y 1 B THR -12 ? B THR 30  
366  1 Y 1 B LEU -11 ? B LEU 31  
367  1 Y 1 B CYS -10 ? B CYS 32  
368  1 Y 1 B LEU -9  ? B LEU 33  
369  1 Y 1 B LEU -8  ? B LEU 34  
370  1 Y 1 B GLY -7  ? B GLY 35  
371  1 Y 1 B CYS -6  ? B CYS 36  
372  1 Y 1 B LEU -5  ? B LEU 37  
373  1 Y 1 B LEU -4  ? B LEU 38  
374  1 Y 1 B GLN -3  ? B GLN 39  
375  1 Y 1 B THR -2  ? B THR 40  
376  1 Y 1 B PHE -1  ? B PHE 41  
377  1 Y 1 B HIS 0   ? B HIS 42  
378  1 Y 1 B VAL 1   ? B VAL 43  
379  1 Y 1 B LEU 2   ? B LEU 44  
380  1 Y 1 B SER 3   ? B SER 45  
381  1 Y 1 B GLN 4   ? B GLN 46  
382  1 Y 1 B LYS 5   ? B LYS 47  
383  1 Y 1 B TYR 6   ? B TYR 48  
384  1 Y 1 B PRO 7   ? B PRO 49  
385  1 Y 1 B TYR 8   ? B TYR 50  
386  1 Y 1 B ASP 9   ? B ASP 51  
387  1 Y 1 B VAL 10  ? B VAL 52  
388  1 Y 1 B PRO 11  ? B PRO 53  
389  1 Y 1 B ASP 12  ? B ASP 54  
390  1 Y 1 B TYR 13  ? B TYR 55  
391  1 Y 1 B ALA 14  ? B ALA 56  
392  1 Y 1 B GLN 15  ? B GLN 57  
393  1 Y 1 B ARG 16  ? B ARG 58  
394  1 Y 1 B GLY 17  ? B GLY 59  
395  1 Y 1 B GLY 18  ? B GLY 60  
396  1 Y 1 B GLY 19  ? B GLY 61  
397  1 Y 1 B GLY 20  ? B GLY 62  
398  1 Y 1 B PRO 21  ? B PRO 63  
399  1 Y 1 B GLY 22  ? B GLY 64  
400  1 Y 1 B GLY 23  ? B GLY 65  
401  1 Y 1 B GLY 24  ? B GLY 66  
402  1 Y 1 B ALA 25  ? B ALA 67  
403  1 Y 1 B PRO 26  ? B PRO 68  
404  1 Y 1 B GLY 27  ? B GLY 69  
405  1 Y 1 B GLY 28  ? B GLY 70  
406  1 Y 1 B PRO 29  ? B PRO 71  
407  1 Y 1 B GLY 30  ? B GLY 72  
408  1 Y 1 B LEU 31  ? B LEU 73  
409  1 Y 1 B GLY 32  ? B GLY 74  
410  1 Y 1 B LEU 33  ? B LEU 75  
411  1 Y 1 B GLY 34  ? B GLY 76  
412  1 Y 1 B SER 35  ? B SER 77  
413  1 Y 1 B LEU 36  ? B LEU 78  
414  1 Y 1 B GLY 37  ? B GLY 79  
415  1 Y 1 B GLU 38  ? B GLU 80  
416  1 Y 1 B GLU 39  ? B GLU 81  
417  1 Y 1 B GLU 168 ? B GLU 193 
418  1 Y 1 B ASP 169 ? B ASP 194 
419  1 Y 1 B ASP 170 ? B ASP 195 
420  1 Y 1 B ILE 171 ? B ILE 196 
421  1 Y 1 B ARG 172 ? B ARG 197 
422  1 Y 1 B ASP 173 ? B ASP 198 
423  1 Y 1 B ASP 554 ? B ASP 579 
424  1 Y 1 B THR 555 ? B THR 580 
425  1 Y 1 B LYS 556 ? B LYS 581 
426  1 Y 1 B PHE 557 ? B PHE 582 
427  1 Y 1 B ILE 558 ? B ILE 583 
428  1 Y 1 B HIS 559 ? B HIS 584 
429  1 Y 1 B THR 560 ? B THR 585 
430  1 Y 1 B LYS 561 ? B LYS 586 
431  1 Y 1 B PRO 562 ? B PRO 587 
432  1 Y 1 B ASN 563 ? B ASN 588 
433  1 Y 1 B HIS 609 ? B HIS 634 
434  1 Y 1 B ASN 610 ? B ASN 635 
435  1 Y 1 B LEU 611 ? B LEU 636 
436  1 Y 1 B HIS 612 ? B HIS 637 
437  1 Y 1 B THR 613 ? B THR 638 
438  1 Y 1 B GLU 614 ? B GLU 639 
439  1 Y 1 B LEU 615 ? B LEU 640 
440  1 Y 1 B PHE 616 ? B PHE 641 
441  1 Y 1 B THR 617 ? B THR 642 
442  1 Y 1 B THR 618 ? B THR 643 
443  1 Y 1 B THR 619 ? B THR 644 
444  1 Y 1 B THR 620 ? B THR 645 
445  1 Y 1 B ARG 621 ? B ARG 646 
446  1 Y 1 B LEU 622 ? B LEU 647 
447  1 Y 1 B PRO 623 ? B PRO 648 
448  1 Y 1 B PRO 624 ? B PRO 649 
449  1 Y 1 B TYR 625 ? B TYR 650 
450  1 Y 1 B ALA 626 ? B ALA 651 
451  1 Y 1 B THR 627 ? B THR 652 
452  1 Y 1 B ARG 628 ? B ARG 653 
453  1 Y 1 B TRP 629 ? B TRP 654 
454  1 Y 1 B PRO 630 ? B PRO 655 
455  1 Y 1 B PRO 631 ? B PRO 656 
456  1 Y 1 B ARG 632 ? B ARG 657 
457  1 Y 1 B THR 633 ? B THR 658 
458  1 Y 1 B PRO 634 ? B PRO 659 
459  1 Y 1 B GLY 635 ? B GLY 660 
460  1 Y 1 B PRO 636 ? B PRO 661 
461  1 Y 1 B GLY 637 ? B GLY 662 
462  1 Y 1 B THR 638 ? B THR 663 
463  1 Y 1 B SER 639 ? B SER 664 
464  1 Y 1 B GLY 640 ? B GLY 665 
465  1 Y 1 B THR 641 ? B THR 666 
466  1 Y 1 B ARG 642 ? B ARG 667 
467  1 Y 1 B ARG 643 ? B ARG 668 
468  1 Y 1 B PRO 644 ? B PRO 669 
469  1 Y 1 B PRO 645 ? B PRO 670 
470  1 Y 1 B PRO 646 ? B PRO 671 
471  1 Y 1 B PRO 647 ? B PRO 672 
472  1 Y 1 B ALA 648 ? B ALA 673 
473  1 Y 1 B THR 649 ? B THR 674 
474  1 Y 1 B LEU 650 ? B LEU 675 
475  1 Y 1 B PRO 651 ? B PRO 676 
476  1 Y 1 B PRO 652 ? B PRO 677 
477  1 Y 1 B GLU 653 ? B GLU 678 
478  1 Y 1 B SER 654 ? B SER 679 
479  1 Y 1 B ASP 655 ? B ASP 680 
480  1 Y 1 B ILE 656 ? B ILE 681 
481  1 Y 1 B ASP 657 ? B ASP 682 
482  1 Y 1 B LEU 658 ? B LEU 683 
483  1 Y 1 B GLY 659 ? B GLY 684 
484  1 Y 1 B PRO 660 ? B PRO 685 
485  1 Y 1 B ARG 661 ? B ARG 686 
486  1 Y 1 B ALA 662 ? B ALA 687 
487  1 Y 1 B TYR 663 ? B TYR 688 
488  1 Y 1 B ASP 664 ? B ASP 689 
489  1 Y 1 B ARG 665 ? B ARG 690 
490  1 Y 1 B PHE 666 ? B PHE 691 
491  1 Y 1 B PRO 667 ? B PRO 692 
492  1 Y 1 B GLY 668 ? B GLY 693 
493  1 Y 1 B ASP 669 ? B ASP 694 
494  1 Y 1 B SER 670 ? B SER 695 
495  1 Y 1 B ARG 671 ? B ARG 696 
496  1 Y 1 B ASP 672 ? B ASP 697 
497  1 Y 1 B TYR 673 ? B TYR 698 
498  1 Y 1 B SER 674 ? B SER 699 
499  1 Y 1 B THR 675 ? B THR 700 
500  1 Y 1 B GLU 676 ? B GLU 701 
501  1 Y 1 B LEU 677 ? B LEU 702 
502  1 Y 1 B SER 678 ? B SER 703 
503  1 Y 1 B VAL 679 ? B VAL 704 
504  1 Y 1 B THR 680 ? B THR 705 
505  1 Y 1 B VAL 681 ? B VAL 706 
506  1 Y 1 B ALA 682 ? B ALA 707 
507  1 Y 1 B VAL 683 ? B VAL 708 
508  1 Y 1 B GLY 684 ? B GLY 709 
509  1 Y 1 B ALA 685 ? B ALA 710 
510  1 Y 1 B SER 686 ? B SER 711 
511  1 Y 1 B LEU 687 ? B LEU 712 
512  1 Y 1 B LEU 688 ? B LEU 713 
513  1 Y 1 B PHE 689 ? B PHE 714 
514  1 Y 1 B LEU 690 ? B LEU 715 
515  1 Y 1 B ASN 691 ? B ASN 716 
516  1 Y 1 B ILE 692 ? B ILE 717 
517  1 Y 1 B LEU 693 ? B LEU 718 
518  1 Y 1 B ALA 694 ? B ALA 719 
519  1 Y 1 B PHE 695 ? B PHE 720 
520  1 Y 1 B ALA 696 ? B ALA 721 
521  1 Y 1 B ALA 697 ? B ALA 722 
522  1 Y 1 B LEU 698 ? B LEU 723 
523  1 Y 1 B TYR 699 ? B TYR 724 
524  1 Y 1 B TYR 700 ? B TYR 725 
525  1 Y 1 B LYS 701 ? B LYS 726 
526  1 Y 1 B ARG 702 ? B ARG 727 
527  1 Y 1 B ASP 703 ? B ASP 728 
528  1 Y 1 B ARG 704 ? B ARG 729 
529  1 Y 1 B ARG 705 ? B ARG 730 
530  1 Y 1 B GLN 706 ? B GLN 731 
531  1 Y 1 B GLU 707 ? B GLU 732 
532  1 Y 1 B LEU 708 ? B LEU 733 
533  1 Y 1 B ARG 709 ? B ARG 734 
534  1 Y 1 B CYS 710 ? B CYS 735 
535  1 Y 1 B ARG 711 ? B ARG 736 
536  1 Y 1 B ARG 712 ? B ARG 737 
537  1 Y 1 B LEU 713 ? B LEU 738 
538  1 Y 1 B SER 714 ? B SER 739 
539  1 Y 1 B PRO 715 ? B PRO 740 
540  1 Y 1 B PRO 716 ? B PRO 741 
541  1 Y 1 B GLY 717 ? B GLY 742 
542  1 Y 1 B GLY 718 ? B GLY 743 
543  1 Y 1 B SER 719 ? B SER 744 
544  1 Y 1 B GLY 720 ? B GLY 745 
545  1 Y 1 B SER 721 ? B SER 746 
546  1 Y 1 B GLY 722 ? B GLY 747 
547  1 Y 1 B VAL 723 ? B VAL 748 
548  1 Y 1 B PRO 724 ? B PRO 749 
549  1 Y 1 B GLY 725 ? B GLY 750 
550  1 Y 1 B GLY 726 ? B GLY 751 
551  1 Y 1 B GLY 727 ? B GLY 752 
552  1 Y 1 B PRO 728 ? B PRO 753 
553  1 Y 1 B LEU 729 ? B LEU 754 
554  1 Y 1 B LEU 730 ? B LEU 755 
555  1 Y 1 B PRO 731 ? B PRO 756 
556  1 Y 1 B THR 732 ? B THR 757 
557  1 Y 1 B ALA 733 ? B ALA 758 
558  1 Y 1 B GLY 734 ? B GLY 759 
559  1 Y 1 B ARG 735 ? B ARG 760 
560  1 Y 1 B GLU 736 ? B GLU 761 
561  1 Y 1 B LEU 737 ? B LEU 762 
562  1 Y 1 B PRO 738 ? B PRO 763 
563  1 Y 1 B PRO 739 ? B PRO 764 
564  1 Y 1 B GLU 740 ? B GLU 765 
565  1 Y 1 B GLU 741 ? B GLU 766 
566  1 Y 1 B GLU 742 ? B GLU 767 
567  1 Y 1 B LEU 743 ? B LEU 768 
568  1 Y 1 B VAL 744 ? B VAL 769 
569  1 Y 1 B SER 745 ? B SER 770 
570  1 Y 1 B LEU 746 ? B LEU 771 
571  1 Y 1 B GLN 747 ? B GLN 772 
572  1 Y 1 B LEU 748 ? B LEU 773 
573  1 Y 1 B LYS 749 ? B LYS 774 
574  1 Y 1 B ARG 750 ? B ARG 775 
575  1 Y 1 B GLY 751 ? B GLY 776 
576  1 Y 1 B GLY 752 ? B GLY 777 
577  1 Y 1 B GLY 753 ? B GLY 778 
578  1 Y 1 B VAL 754 ? B VAL 779 
579  1 Y 1 B GLY 755 ? B GLY 780 
580  1 Y 1 B ALA 756 ? B ALA 781 
581  1 Y 1 B ASP 757 ? B ASP 782 
582  1 Y 1 B PRO 758 ? B PRO 783 
583  1 Y 1 B ALA 759 ? B ALA 784 
584  1 Y 1 B GLU 760 ? B GLU 785 
585  1 Y 1 B ALA 761 ? B ALA 786 
586  1 Y 1 B LEU 762 ? B LEU 787 
587  1 Y 1 B ARG 763 ? B ARG 788 
588  1 Y 1 B PRO 764 ? B PRO 789 
589  1 Y 1 B ALA 765 ? B ALA 790 
590  1 Y 1 B CYS 766 ? B CYS 791 
591  1 Y 1 B PRO 767 ? B PRO 792 
592  1 Y 1 B PRO 768 ? B PRO 793 
593  1 Y 1 B ASP 769 ? B ASP 794 
594  1 Y 1 B TYR 770 ? B TYR 795 
595  1 Y 1 B THR 771 ? B THR 796 
596  1 Y 1 B LEU 772 ? B LEU 797 
597  1 Y 1 B ALA 773 ? B ALA 798 
598  1 Y 1 B LEU 774 ? B LEU 799 
599  1 Y 1 B ARG 775 ? B ARG 800 
600  1 Y 1 B ARG 776 ? B ARG 801 
601  1 Y 1 B ALA 777 ? B ALA 802 
602  1 Y 1 B PRO 778 ? B PRO 803 
603  1 Y 1 B ASP 779 ? B ASP 804 
604  1 Y 1 B ASP 780 ? B ASP 805 
605  1 Y 1 B VAL 781 ? B VAL 806 
606  1 Y 1 B PRO 782 ? B PRO 807 
607  1 Y 1 B LEU 783 ? B LEU 808 
608  1 Y 1 B LEU 784 ? B LEU 809 
609  1 Y 1 B ALA 785 ? B ALA 810 
610  1 Y 1 B PRO 786 ? B PRO 811 
611  1 Y 1 B GLY 787 ? B GLY 812 
612  1 Y 1 B ALA 788 ? B ALA 813 
613  1 Y 1 B LEU 789 ? B LEU 814 
614  1 Y 1 B THR 790 ? B THR 815 
615  1 Y 1 B LEU 791 ? B LEU 816 
616  1 Y 1 B LEU 792 ? B LEU 817 
617  1 Y 1 B PRO 793 ? B PRO 818 
618  1 Y 1 B SER 794 ? B SER 819 
619  1 Y 1 B GLY 795 ? B GLY 820 
620  1 Y 1 B LEU 796 ? B LEU 821 
621  1 Y 1 B GLY 797 ? B GLY 822 
622  1 Y 1 B PRO 798 ? B PRO 823 
623  1 Y 1 B PRO 799 ? B PRO 824 
624  1 Y 1 B PRO 800 ? B PRO 825 
625  1 Y 1 B PRO 801 ? B PRO 826 
626  1 Y 1 B PRO 802 ? B PRO 827 
627  1 Y 1 B PRO 803 ? B PRO 828 
628  1 Y 1 B PRO 804 ? B PRO 829 
629  1 Y 1 B PRO 805 ? B PRO 830 
630  1 Y 1 B SER 806 ? B SER 831 
631  1 Y 1 B LEU 807 ? B LEU 832 
632  1 Y 1 B HIS 808 ? B HIS 833 
633  1 Y 1 B PRO 809 ? B PRO 834 
634  1 Y 1 B PHE 810 ? B PHE 835 
635  1 Y 1 B GLY 811 ? B GLY 836 
636  1 Y 1 B PRO 812 ? B PRO 837 
637  1 Y 1 B PHE 813 ? B PHE 838 
638  1 Y 1 B PRO 814 ? B PRO 839 
639  1 Y 1 B PRO 815 ? B PRO 840 
640  1 Y 1 B PRO 816 ? B PRO 841 
641  1 Y 1 B PRO 817 ? B PRO 842 
642  1 Y 1 B PRO 818 ? B PRO 843 
643  1 Y 1 B THR 819 ? B THR 844 
644  1 Y 1 B ALA 820 ? B ALA 845 
645  1 Y 1 B THR 821 ? B THR 846 
646  1 Y 1 B SER 822 ? B SER 847 
647  1 Y 1 B HIS 823 ? B HIS 848 
648  1 Y 1 B ASN 824 ? B ASN 849 
649  1 Y 1 B ASN 825 ? B ASN 850 
650  1 Y 1 B THR 826 ? B THR 851 
651  1 Y 1 B LEU 827 ? B LEU 852 
652  1 Y 1 B PRO 828 ? B PRO 853 
653  1 Y 1 B HIS 829 ? B HIS 854 
654  1 Y 1 B PRO 830 ? B PRO 855 
655  1 Y 1 B HIS 831 ? B HIS 856 
656  1 Y 1 B SER 832 ? B SER 857 
657  1 Y 1 B THR 833 ? B THR 858 
658  1 Y 1 B THR 834 ? B THR 859 
659  1 Y 1 B ARG 835 ? B ARG 860 
660  1 Y 1 B VAL 836 ? B VAL 861 
661  1 Y 1 B SER 837 ? B SER 862 
662  1 Y 1 B ASN 838 ? B ASN 863 
663  1 Y 1 B SER 839 ? B SER 864 
664  1 Y 1 B LEU 840 ? B LEU 865 
665  1 Y 1 B GLU 841 ? B GLU 866 
666  1 Y 1 B VAL 842 ? B VAL 867 
667  1 Y 1 B LEU 843 ? B LEU 868 
668  1 Y 1 B PHE 844 ? B PHE 869 
669  1 Y 1 B GLN 845 ? B GLN 870 
670  1 Y 1 C MET -22 ? C MET 1   
671  1 Y 1 C TYR -21 ? C TYR 2   
672  1 Y 1 C GLN -20 ? C GLN 3   
673  1 Y 1 C ARG -19 ? C ARG 4   
674  1 Y 1 C MET -18 ? C MET 5   
675  1 Y 1 C LEU -17 ? C LEU 6   
676  1 Y 1 C ARG -16 ? C ARG 7   
677  1 Y 1 C CYS -15 ? C CYS 8   
678  1 Y 1 C GLY -14 ? C GLY 9   
679  1 Y 1 C ALA -13 ? C ALA 10  
680  1 Y 1 C ASP -12 ? C ASP 11  
681  1 Y 1 C LEU -11 ? C LEU 12  
682  1 Y 1 C GLY -10 ? C GLY 13  
683  1 Y 1 C SER -9  ? C SER 14  
684  1 Y 1 C PRO -8  ? C PRO 15  
685  1 Y 1 C GLY -7  ? C GLY 16  
686  1 Y 1 C GLY -6  ? C GLY 17  
687  1 Y 1 C GLY -5  ? C GLY 18  
688  1 Y 1 C SER -4  ? C SER 19  
689  1 Y 1 C GLY -3  ? C GLY 20  
690  1 Y 1 C GLY -2  ? C GLY 21  
691  1 Y 1 C GLY -1  ? C GLY 22  
692  1 Y 1 C ALA 0   ? C ALA 23  
693  1 Y 1 C GLY 1   ? C GLY 24  
694  1 Y 1 C GLY 2   ? C GLY 25  
695  1 Y 1 C ARG 3   ? C ARG 26  
696  1 Y 1 C LEU 4   ? C LEU 27  
697  1 Y 1 C ALA 5   ? C ALA 28  
698  1 Y 1 C LEU 6   ? C LEU 29  
699  1 Y 1 C ILE 7   ? C ILE 30  
700  1 Y 1 C TRP 8   ? C TRP 31  
701  1 Y 1 C ILE 9   ? C ILE 32  
702  1 Y 1 C VAL 10  ? C VAL 33  
703  1 Y 1 C PRO 11  ? C PRO 34  
704  1 Y 1 C LEU 12  ? C LEU 35  
705  1 Y 1 C THR 13  ? C THR 36  
706  1 Y 1 C LEU 14  ? C LEU 37  
707  1 Y 1 C GLY 15  ? C GLY 38  
708  1 Y 1 C GLY 16  ? C GLY 39  
709  1 Y 1 C LEU 17  ? C LEU 40  
710  1 Y 1 C LEU 18  ? C LEU 41  
711  1 Y 1 C GLY 19  ? C GLY 42  
712  1 Y 1 C VAL 20  ? C VAL 43  
713  1 Y 1 C ALA 21  ? C ALA 44  
714  1 Y 1 C TRP 22  ? C TRP 45  
715  1 Y 1 C GLY 23  ? C GLY 46  
716  1 Y 1 C ALA 24  ? C ALA 47  
717  1 Y 1 C SER 25  ? C SER 48  
718  1 Y 1 C SER 26  ? C SER 49  
719  1 Y 1 C LEU 27  ? C LEU 50  
720  1 Y 1 C GLY 28  ? C GLY 51  
721  1 Y 1 C ALA 29  ? C ALA 52  
722  1 Y 1 C HIS 30  ? C HIS 53  
723  1 Y 1 C HIS 31  ? C HIS 54  
724  1 Y 1 C ILE 32  ? C ILE 55  
725  1 Y 1 C HIS 33  ? C HIS 56  
726  1 Y 1 C HIS 34  ? C HIS 57  
727  1 Y 1 C PHE 35  ? C PHE 58  
728  1 Y 1 C HIS 36  ? C HIS 59  
729  1 Y 1 C GLY 37  ? C GLY 60  
730  1 Y 1 C SER 38  ? C SER 61  
731  1 Y 1 C SER 39  ? C SER 62  
732  1 Y 1 C LYS 40  ? C LYS 63  
733  1 Y 1 C GLU 41  ? C GLU 64  
734  1 Y 1 C PHE 42  ? C PHE 65  
735  1 Y 1 C GLU 43  ? C GLU 66  
736  1 Y 1 C GLN 44  ? C GLN 67  
737  1 Y 1 C LYS 45  ? C LYS 68  
738  1 Y 1 C LEU 46  ? C LEU 69  
739  1 Y 1 C ILE 47  ? C ILE 70  
740  1 Y 1 C SER 48  ? C SER 71  
741  1 Y 1 C GLU 49  ? C GLU 72  
742  1 Y 1 C GLU 50  ? C GLU 73  
743  1 Y 1 C ASP 51  ? C ASP 74  
744  1 Y 1 C LEU 52  ? C LEU 75  
745  1 Y 1 C GLY 53  ? C GLY 76  
746  1 Y 1 C PHE 54  ? C PHE 77  
747  1 Y 1 C GLU 55  ? C GLU 78  
748  1 Y 1 C ILE 56  ? C ILE 79  
749  1 Y 1 C ASP 57  ? C ASP 80  
750  1 Y 1 C LYS 58  ? C LYS 81  
751  1 Y 1 C VAL 59  ? C VAL 82  
752  1 Y 1 C TRP 60  ? C TRP 83  
753  1 Y 1 C HIS 61  ? C HIS 84  
754  1 Y 1 C ASP 62  ? C ASP 85  
755  1 Y 1 C PHE 63  ? C PHE 86  
756  1 Y 1 C PRO 64  ? C PRO 87  
757  1 Y 1 C ALA 65  ? C ALA 88  
758  1 Y 1 C THR 66  ? C THR 89  
759  1 Y 1 C SER 67  ? C SER 90  
760  1 Y 1 C PRO 68  ? C PRO 91  
761  1 Y 1 C ILE 69  ? C ILE 92  
762  1 Y 1 C ALA 70  ? C ALA 93  
763  1 Y 1 C ILE 71  ? C ILE 94  
764  1 Y 1 C TYR 72  ? C TYR 95  
765  1 Y 1 C ARG 73  ? C ARG 96  
766  1 Y 1 C SER 74  ? C SER 97  
767  1 Y 1 C PRO 75  ? C PRO 98  
768  1 Y 1 C ALA 76  ? C ALA 99  
769  1 Y 1 C SER 77  ? C SER 100 
770  1 Y 1 C LEU 78  ? C LEU 101 
771  1 Y 1 C ARG 79  ? C ARG 102 
772  1 Y 1 C GLY 80  ? C GLY 103 
773  1 Y 1 C GLY 81  ? C GLY 104 
774  1 Y 1 C HIS 82  ? C HIS 105 
775  1 Y 1 C GLU 290 ? C GLU 283 
776  1 Y 1 C VAL 291 ? C VAL 284 
777  1 Y 1 C PRO 292 ? C PRO 285 
778  1 Y 1 C SER 293 ? C SER 286 
779  1 Y 1 C SER 294 ? C SER 287 
780  1 Y 1 C MET 295 ? C MET 288 
781  1 Y 1 C THR 296 ? C THR 289 
782  1 Y 1 C THR 297 ? C THR 290 
783  1 Y 1 C GLU 298 ? C GLU 291 
784  1 Y 1 C SER 299 ? C SER 292 
785  1 Y 1 C THR 300 ? C THR 293 
786  1 Y 1 C ALA 301 ? C ALA 294 
787  1 Y 1 C THR 302 ? C THR 295 
788  1 Y 1 C ALA 303 ? C ALA 296 
789  1 Y 1 C MET 304 ? C MET 297 
790  1 Y 1 C GLN 305 ? C GLN 298 
791  1 Y 1 C SER 306 ? C SER 299 
792  1 Y 1 C GLU 307 ? C GLU 300 
793  1 Y 1 C MET 308 ? C MET 301 
794  1 Y 1 C SER 309 ? C SER 302 
795  1 Y 1 C THR 310 ? C THR 303 
796  1 Y 1 C SER 311 ? C SER 304 
797  1 Y 1 C ILE 312 ? C ILE 305 
798  1 Y 1 C MET 313 ? C MET 306 
799  1 Y 1 C GLU 314 ? C GLU 307 
800  1 Y 1 C THR 315 ? C THR 308 
801  1 Y 1 C THR 316 ? C THR 309 
802  1 Y 1 C THR 317 ? C THR 310 
803  1 Y 1 C THR 318 ? C THR 311 
804  1 Y 1 C LEU 319 ? C LEU 312 
805  1 Y 1 C ALA 320 ? C ALA 313 
806  1 Y 1 C THR 321 ? C THR 314 
807  1 Y 1 C SER 322 ? C SER 315 
808  1 Y 1 C THR 323 ? C THR 316 
809  1 Y 1 C ALA 324 ? C ALA 317 
810  1 Y 1 C ARG 325 ? C ARG 318 
811  1 Y 1 C ARG 326 ? C ARG 319 
812  1 Y 1 C GLY 327 ? C GLY 320 
813  1 Y 1 C LYS 328 ? C LYS 321 
814  1 Y 1 C PRO 329 ? C PRO 322 
815  1 Y 1 C PRO 330 ? C PRO 323 
816  1 Y 1 C THR 331 ? C THR 324 
817  1 Y 1 C LYS 332 ? C LYS 325 
818  1 Y 1 C GLU 333 ? C GLU 326 
819  1 Y 1 C PRO 334 ? C PRO 327 
820  1 Y 1 C ILE 335 ? C ILE 328 
821  1 Y 1 C SER 336 ? C SER 329 
822  1 Y 1 C GLN 337 ? C GLN 330 
823  1 Y 1 C THR 338 ? C THR 331 
824  1 Y 1 C THR 339 ? C THR 332 
825  1 Y 1 C ASP 340 ? C ASP 333 
826  1 Y 1 C ASP 341 ? C ASP 334 
827  1 Y 1 C ILE 342 ? C ILE 335 
828  1 Y 1 C LEU 343 ? C LEU 336 
829  1 Y 1 C VAL 344 ? C VAL 337 
830  1 Y 1 C ALA 345 ? C ALA 338 
831  1 Y 1 C SER 346 ? C SER 339 
832  1 Y 1 C ALA 347 ? C ALA 340 
833  1 Y 1 C GLU 348 ? C GLU 341 
834  1 Y 1 C CYS 349 ? C CYS 342 
835  1 Y 1 C PRO 350 ? C PRO 343 
836  1 Y 1 C SER 351 ? C SER 344 
837  1 Y 1 C ASP 352 ? C ASP 345 
838  1 Y 1 C ASP 353 ? C ASP 346 
839  1 Y 1 C GLU 354 ? C GLU 347 
840  1 Y 1 C ASP 355 ? C ASP 348 
841  1 Y 1 C ILE 356 ? C ILE 349 
842  1 Y 1 C ASP 357 ? C ASP 350 
843  1 Y 1 C PRO 358 ? C PRO 351 
844  1 Y 1 C CYS 359 ? C CYS 352 
845  1 Y 1 C GLU 360 ? C GLU 353 
846  1 Y 1 C PRO 361 ? C PRO 354 
847  1 Y 1 C SER 362 ? C SER 355 
848  1 Y 1 C SER 363 ? C SER 356 
849  1 Y 1 C GLY 364 ? C GLY 357 
850  1 Y 1 C GLY 365 ? C GLY 358 
851  1 Y 1 C LEU 366 ? C LEU 359 
852  1 Y 1 C ALA 367 ? C ALA 360 
853  1 Y 1 C ASN 368 ? C ASN 361 
854  1 Y 1 C PRO 369 ? C PRO 362 
855  1 Y 1 C THR 370 ? C THR 363 
856  1 Y 1 C ARG 371 ? C ARG 364 
857  1 Y 1 C VAL 372 ? C VAL 365 
858  1 Y 1 C GLY 373 ? C GLY 366 
859  1 Y 1 C GLY 374 ? C GLY 367 
860  1 Y 1 C ARG 375 ? C ARG 368 
861  1 Y 1 C GLU 376 ? C GLU 369 
862  1 Y 1 C PRO 377 ? C PRO 370 
863  1 Y 1 C TYR 378 ? C TYR 371 
864  1 Y 1 C PRO 379 ? C PRO 372 
865  1 Y 1 C GLY 380 ? C GLY 373 
866  1 Y 1 C SER 381 ? C SER 374 
867  1 Y 1 C ALA 382 ? C ALA 375 
868  1 Y 1 C GLU 383 ? C GLU 376 
869  1 Y 1 C VAL 384 ? C VAL 377 
870  1 Y 1 C ILE 385 ? C ILE 378 
871  1 Y 1 C ARG 386 ? C ARG 379 
872  1 Y 1 C GLU 387 ? C GLU 380 
873  1 Y 1 C SER 388 ? C SER 381 
874  1 Y 1 C SER 389 ? C SER 382 
875  1 Y 1 C SER 390 ? C SER 383 
876  1 Y 1 C THR 391 ? C THR 384 
877  1 Y 1 C THR 392 ? C THR 385 
878  1 Y 1 C GLY 393 ? C GLY 386 
879  1 Y 1 C MET 394 ? C MET 387 
880  1 Y 1 C VAL 395 ? C VAL 388 
881  1 Y 1 C VAL 396 ? C VAL 389 
882  1 Y 1 C GLY 397 ? C GLY 390 
883  1 Y 1 C ILE 398 ? C ILE 391 
884  1 Y 1 C VAL 399 ? C VAL 392 
885  1 Y 1 C ALA 400 ? C ALA 393 
886  1 Y 1 C ALA 401 ? C ALA 394 
887  1 Y 1 C ALA 402 ? C ALA 395 
888  1 Y 1 C ALA 403 ? C ALA 396 
889  1 Y 1 C LEU 404 ? C LEU 397 
890  1 Y 1 C CYS 405 ? C CYS 398 
891  1 Y 1 C ILE 406 ? C ILE 399 
892  1 Y 1 C LEU 407 ? C LEU 400 
893  1 Y 1 C ILE 408 ? C ILE 401 
894  1 Y 1 C LEU 409 ? C LEU 402 
895  1 Y 1 C LEU 410 ? C LEU 403 
896  1 Y 1 C TYR 411 ? C TYR 404 
897  1 Y 1 C ALA 412 ? C ALA 405 
898  1 Y 1 C MET 413 ? C MET 406 
899  1 Y 1 C TYR 414 ? C TYR 407 
900  1 Y 1 C LYS 415 ? C LYS 408 
901  1 Y 1 C TYR 416 ? C TYR 409 
902  1 Y 1 C ARG 417 ? C ARG 410 
903  1 Y 1 C ASN 418 ? C ASN 411 
904  1 Y 1 C ARG 419 ? C ARG 412 
905  1 Y 1 C ASP 420 ? C ASP 413 
906  1 Y 1 C GLU 421 ? C GLU 414 
907  1 Y 1 C GLY 422 ? C GLY 415 
908  1 Y 1 C SER 423 ? C SER 416 
909  1 Y 1 C TYR 424 ? C TYR 417 
910  1 Y 1 C HIS 425 ? C HIS 418 
911  1 Y 1 C VAL 426 ? C VAL 419 
912  1 Y 1 C ASP 427 ? C ASP 420 
913  1 Y 1 C GLU 428 ? C GLU 421 
914  1 Y 1 C SER 429 ? C SER 422 
915  1 Y 1 C ARG 430 ? C ARG 423 
916  1 Y 1 C ASN 431 ? C ASN 424 
917  1 Y 1 C TYR 432 ? C TYR 425 
918  1 Y 1 C ILE 433 ? C ILE 426 
919  1 Y 1 C SER 434 ? C SER 427 
920  1 Y 1 C ASN 435 ? C ASN 428 
921  1 Y 1 C SER 436 ? C SER 429 
922  1 Y 1 C ALA 437 ? C ALA 430 
923  1 Y 1 C GLN 438 ? C GLN 431 
924  1 Y 1 C SER 439 ? C SER 432 
925  1 Y 1 C ASN 440 ? C ASN 433 
926  1 Y 1 C GLY 441 ? C GLY 434 
927  1 Y 1 C ALA 442 ? C ALA 435 
928  1 Y 1 C VAL 443 ? C VAL 436 
929  1 Y 1 C VAL 444 ? C VAL 437 
930  1 Y 1 C LYS 445 ? C LYS 438 
931  1 Y 1 C GLU 446 ? C GLU 439 
932  1 Y 1 C LYS 447 ? C LYS 440 
933  1 Y 1 C GLN 448 ? C GLN 441 
934  1 Y 1 C PRO 449 ? C PRO 442 
935  1 Y 1 C SER 450 ? C SER 443 
936  1 Y 1 C SER 451 ? C SER 444 
937  1 Y 1 C ALA 452 ? C ALA 445 
938  1 Y 1 C LYS 453 ? C LYS 446 
939  1 Y 1 C SER 454 ? C SER 447 
940  1 Y 1 C ALA 455 ? C ALA 448 
941  1 Y 1 C ASN 456 ? C ASN 449 
942  1 Y 1 C LYS 457 ? C LYS 450 
943  1 Y 1 C ASN 458 ? C ASN 451 
944  1 Y 1 C LYS 459 ? C LYS 452 
945  1 Y 1 C LYS 460 ? C LYS 453 
946  1 Y 1 C ASN 461 ? C ASN 454 
947  1 Y 1 C LYS 462 ? C LYS 455 
948  1 Y 1 C ASP 463 ? C ASP 456 
949  1 Y 1 C LYS 464 ? C LYS 457 
950  1 Y 1 C GLU 465 ? C GLU 458 
951  1 Y 1 C TYR 466 ? C TYR 459 
952  1 Y 1 C TYR 467 ? C TYR 460 
953  1 Y 1 C VAL 468 ? C VAL 461 
954  1 Y 1 C SER 469 ? C SER 462 
955  1 Y 1 C ASN 470 ? C ASN 463 
956  1 Y 1 C SER 471 ? C SER 464 
957  1 Y 1 C LEU 472 ? C LEU 465 
958  1 Y 1 C GLU 473 ? C GLU 466 
959  1 Y 1 C VAL 474 ? C VAL 467 
960  1 Y 1 C LEU 475 ? C LEU 468 
961  1 Y 1 C PHE 476 ? C PHE 469 
962  1 Y 1 C GLN 477 ? C GLN 470 
963  1 Y 1 D MET -22 ? D MET 1   
964  1 Y 1 D TYR -21 ? D TYR 2   
965  1 Y 1 D GLN -20 ? D GLN 3   
966  1 Y 1 D ARG -19 ? D ARG 4   
967  1 Y 1 D MET -18 ? D MET 5   
968  1 Y 1 D LEU -17 ? D LEU 6   
969  1 Y 1 D ARG -16 ? D ARG 7   
970  1 Y 1 D CYS -15 ? D CYS 8   
971  1 Y 1 D GLY -14 ? D GLY 9   
972  1 Y 1 D ALA -13 ? D ALA 10  
973  1 Y 1 D ASP -12 ? D ASP 11  
974  1 Y 1 D LEU -11 ? D LEU 12  
975  1 Y 1 D GLY -10 ? D GLY 13  
976  1 Y 1 D SER -9  ? D SER 14  
977  1 Y 1 D PRO -8  ? D PRO 15  
978  1 Y 1 D GLY -7  ? D GLY 16  
979  1 Y 1 D GLY -6  ? D GLY 17  
980  1 Y 1 D GLY -5  ? D GLY 18  
981  1 Y 1 D SER -4  ? D SER 19  
982  1 Y 1 D GLY -3  ? D GLY 20  
983  1 Y 1 D GLY -2  ? D GLY 21  
984  1 Y 1 D GLY -1  ? D GLY 22  
985  1 Y 1 D ALA 0   ? D ALA 23  
986  1 Y 1 D GLY 1   ? D GLY 24  
987  1 Y 1 D GLY 2   ? D GLY 25  
988  1 Y 1 D ARG 3   ? D ARG 26  
989  1 Y 1 D LEU 4   ? D LEU 27  
990  1 Y 1 D ALA 5   ? D ALA 28  
991  1 Y 1 D LEU 6   ? D LEU 29  
992  1 Y 1 D ILE 7   ? D ILE 30  
993  1 Y 1 D TRP 8   ? D TRP 31  
994  1 Y 1 D ILE 9   ? D ILE 32  
995  1 Y 1 D VAL 10  ? D VAL 33  
996  1 Y 1 D PRO 11  ? D PRO 34  
997  1 Y 1 D LEU 12  ? D LEU 35  
998  1 Y 1 D THR 13  ? D THR 36  
999  1 Y 1 D LEU 14  ? D LEU 37  
1000 1 Y 1 D GLY 15  ? D GLY 38  
1001 1 Y 1 D GLY 16  ? D GLY 39  
1002 1 Y 1 D LEU 17  ? D LEU 40  
1003 1 Y 1 D LEU 18  ? D LEU 41  
1004 1 Y 1 D GLY 19  ? D GLY 42  
1005 1 Y 1 D VAL 20  ? D VAL 43  
1006 1 Y 1 D ALA 21  ? D ALA 44  
1007 1 Y 1 D TRP 22  ? D TRP 45  
1008 1 Y 1 D GLY 23  ? D GLY 46  
1009 1 Y 1 D ALA 24  ? D ALA 47  
1010 1 Y 1 D SER 25  ? D SER 48  
1011 1 Y 1 D SER 26  ? D SER 49  
1012 1 Y 1 D LEU 27  ? D LEU 50  
1013 1 Y 1 D GLY 28  ? D GLY 51  
1014 1 Y 1 D ALA 29  ? D ALA 52  
1015 1 Y 1 D HIS 30  ? D HIS 53  
1016 1 Y 1 D HIS 31  ? D HIS 54  
1017 1 Y 1 D ILE 32  ? D ILE 55  
1018 1 Y 1 D HIS 33  ? D HIS 56  
1019 1 Y 1 D HIS 34  ? D HIS 57  
1020 1 Y 1 D PHE 35  ? D PHE 58  
1021 1 Y 1 D HIS 36  ? D HIS 59  
1022 1 Y 1 D GLY 37  ? D GLY 60  
1023 1 Y 1 D SER 38  ? D SER 61  
1024 1 Y 1 D SER 39  ? D SER 62  
1025 1 Y 1 D LYS 40  ? D LYS 63  
1026 1 Y 1 D GLU 41  ? D GLU 64  
1027 1 Y 1 D PHE 42  ? D PHE 65  
1028 1 Y 1 D GLU 43  ? D GLU 66  
1029 1 Y 1 D GLN 44  ? D GLN 67  
1030 1 Y 1 D LYS 45  ? D LYS 68  
1031 1 Y 1 D LEU 46  ? D LEU 69  
1032 1 Y 1 D ILE 47  ? D ILE 70  
1033 1 Y 1 D SER 48  ? D SER 71  
1034 1 Y 1 D GLU 49  ? D GLU 72  
1035 1 Y 1 D GLU 50  ? D GLU 73  
1036 1 Y 1 D ASP 51  ? D ASP 74  
1037 1 Y 1 D LEU 52  ? D LEU 75  
1038 1 Y 1 D GLY 53  ? D GLY 76  
1039 1 Y 1 D PHE 54  ? D PHE 77  
1040 1 Y 1 D GLU 55  ? D GLU 78  
1041 1 Y 1 D ILE 56  ? D ILE 79  
1042 1 Y 1 D ASP 57  ? D ASP 80  
1043 1 Y 1 D LYS 58  ? D LYS 81  
1044 1 Y 1 D VAL 59  ? D VAL 82  
1045 1 Y 1 D TRP 60  ? D TRP 83  
1046 1 Y 1 D HIS 61  ? D HIS 84  
1047 1 Y 1 D ASP 62  ? D ASP 85  
1048 1 Y 1 D PHE 63  ? D PHE 86  
1049 1 Y 1 D PRO 64  ? D PRO 87  
1050 1 Y 1 D ALA 65  ? D ALA 88  
1051 1 Y 1 D THR 66  ? D THR 89  
1052 1 Y 1 D SER 67  ? D SER 90  
1053 1 Y 1 D PRO 68  ? D PRO 91  
1054 1 Y 1 D ILE 69  ? D ILE 92  
1055 1 Y 1 D ALA 70  ? D ALA 93  
1056 1 Y 1 D ILE 71  ? D ILE 94  
1057 1 Y 1 D TYR 72  ? D TYR 95  
1058 1 Y 1 D ARG 73  ? D ARG 96  
1059 1 Y 1 D SER 74  ? D SER 97  
1060 1 Y 1 D PRO 75  ? D PRO 98  
1061 1 Y 1 D ALA 76  ? D ALA 99  
1062 1 Y 1 D SER 77  ? D SER 100 
1063 1 Y 1 D LEU 78  ? D LEU 101 
1064 1 Y 1 D ARG 79  ? D ARG 102 
1065 1 Y 1 D GLY 80  ? D GLY 103 
1066 1 Y 1 D GLY 81  ? D GLY 104 
1067 1 Y 1 D HIS 82  ? D HIS 105 
1068 1 Y 1 D GLU 290 ? D GLU 283 
1069 1 Y 1 D VAL 291 ? D VAL 284 
1070 1 Y 1 D PRO 292 ? D PRO 285 
1071 1 Y 1 D SER 293 ? D SER 286 
1072 1 Y 1 D SER 294 ? D SER 287 
1073 1 Y 1 D MET 295 ? D MET 288 
1074 1 Y 1 D THR 296 ? D THR 289 
1075 1 Y 1 D THR 297 ? D THR 290 
1076 1 Y 1 D GLU 298 ? D GLU 291 
1077 1 Y 1 D SER 299 ? D SER 292 
1078 1 Y 1 D THR 300 ? D THR 293 
1079 1 Y 1 D ALA 301 ? D ALA 294 
1080 1 Y 1 D THR 302 ? D THR 295 
1081 1 Y 1 D ALA 303 ? D ALA 296 
1082 1 Y 1 D MET 304 ? D MET 297 
1083 1 Y 1 D GLN 305 ? D GLN 298 
1084 1 Y 1 D SER 306 ? D SER 299 
1085 1 Y 1 D GLU 307 ? D GLU 300 
1086 1 Y 1 D MET 308 ? D MET 301 
1087 1 Y 1 D SER 309 ? D SER 302 
1088 1 Y 1 D THR 310 ? D THR 303 
1089 1 Y 1 D SER 311 ? D SER 304 
1090 1 Y 1 D ILE 312 ? D ILE 305 
1091 1 Y 1 D MET 313 ? D MET 306 
1092 1 Y 1 D GLU 314 ? D GLU 307 
1093 1 Y 1 D THR 315 ? D THR 308 
1094 1 Y 1 D THR 316 ? D THR 309 
1095 1 Y 1 D THR 317 ? D THR 310 
1096 1 Y 1 D THR 318 ? D THR 311 
1097 1 Y 1 D LEU 319 ? D LEU 312 
1098 1 Y 1 D ALA 320 ? D ALA 313 
1099 1 Y 1 D THR 321 ? D THR 314 
1100 1 Y 1 D SER 322 ? D SER 315 
1101 1 Y 1 D THR 323 ? D THR 316 
1102 1 Y 1 D ALA 324 ? D ALA 317 
1103 1 Y 1 D ARG 325 ? D ARG 318 
1104 1 Y 1 D ARG 326 ? D ARG 319 
1105 1 Y 1 D GLY 327 ? D GLY 320 
1106 1 Y 1 D LYS 328 ? D LYS 321 
1107 1 Y 1 D PRO 329 ? D PRO 322 
1108 1 Y 1 D PRO 330 ? D PRO 323 
1109 1 Y 1 D THR 331 ? D THR 324 
1110 1 Y 1 D LYS 332 ? D LYS 325 
1111 1 Y 1 D GLU 333 ? D GLU 326 
1112 1 Y 1 D PRO 334 ? D PRO 327 
1113 1 Y 1 D ILE 335 ? D ILE 328 
1114 1 Y 1 D SER 336 ? D SER 329 
1115 1 Y 1 D GLN 337 ? D GLN 330 
1116 1 Y 1 D THR 338 ? D THR 331 
1117 1 Y 1 D THR 339 ? D THR 332 
1118 1 Y 1 D ASP 340 ? D ASP 333 
1119 1 Y 1 D ASP 341 ? D ASP 334 
1120 1 Y 1 D ILE 342 ? D ILE 335 
1121 1 Y 1 D LEU 343 ? D LEU 336 
1122 1 Y 1 D VAL 344 ? D VAL 337 
1123 1 Y 1 D ALA 345 ? D ALA 338 
1124 1 Y 1 D SER 346 ? D SER 339 
1125 1 Y 1 D ALA 347 ? D ALA 340 
1126 1 Y 1 D GLU 348 ? D GLU 341 
1127 1 Y 1 D CYS 349 ? D CYS 342 
1128 1 Y 1 D PRO 350 ? D PRO 343 
1129 1 Y 1 D SER 351 ? D SER 344 
1130 1 Y 1 D ASP 352 ? D ASP 345 
1131 1 Y 1 D ASP 353 ? D ASP 346 
1132 1 Y 1 D GLU 354 ? D GLU 347 
1133 1 Y 1 D ASP 355 ? D ASP 348 
1134 1 Y 1 D ILE 356 ? D ILE 349 
1135 1 Y 1 D ASP 357 ? D ASP 350 
1136 1 Y 1 D PRO 358 ? D PRO 351 
1137 1 Y 1 D CYS 359 ? D CYS 352 
1138 1 Y 1 D GLU 360 ? D GLU 353 
1139 1 Y 1 D PRO 361 ? D PRO 354 
1140 1 Y 1 D SER 362 ? D SER 355 
1141 1 Y 1 D SER 363 ? D SER 356 
1142 1 Y 1 D GLY 364 ? D GLY 357 
1143 1 Y 1 D GLY 365 ? D GLY 358 
1144 1 Y 1 D LEU 366 ? D LEU 359 
1145 1 Y 1 D ALA 367 ? D ALA 360 
1146 1 Y 1 D ASN 368 ? D ASN 361 
1147 1 Y 1 D PRO 369 ? D PRO 362 
1148 1 Y 1 D THR 370 ? D THR 363 
1149 1 Y 1 D ARG 371 ? D ARG 364 
1150 1 Y 1 D VAL 372 ? D VAL 365 
1151 1 Y 1 D GLY 373 ? D GLY 366 
1152 1 Y 1 D GLY 374 ? D GLY 367 
1153 1 Y 1 D ARG 375 ? D ARG 368 
1154 1 Y 1 D GLU 376 ? D GLU 369 
1155 1 Y 1 D PRO 377 ? D PRO 370 
1156 1 Y 1 D TYR 378 ? D TYR 371 
1157 1 Y 1 D PRO 379 ? D PRO 372 
1158 1 Y 1 D GLY 380 ? D GLY 373 
1159 1 Y 1 D SER 381 ? D SER 374 
1160 1 Y 1 D ALA 382 ? D ALA 375 
1161 1 Y 1 D GLU 383 ? D GLU 376 
1162 1 Y 1 D VAL 384 ? D VAL 377 
1163 1 Y 1 D ILE 385 ? D ILE 378 
1164 1 Y 1 D ARG 386 ? D ARG 379 
1165 1 Y 1 D GLU 387 ? D GLU 380 
1166 1 Y 1 D SER 388 ? D SER 381 
1167 1 Y 1 D SER 389 ? D SER 382 
1168 1 Y 1 D SER 390 ? D SER 383 
1169 1 Y 1 D THR 391 ? D THR 384 
1170 1 Y 1 D THR 392 ? D THR 385 
1171 1 Y 1 D GLY 393 ? D GLY 386 
1172 1 Y 1 D MET 394 ? D MET 387 
1173 1 Y 1 D VAL 395 ? D VAL 388 
1174 1 Y 1 D VAL 396 ? D VAL 389 
1175 1 Y 1 D GLY 397 ? D GLY 390 
1176 1 Y 1 D ILE 398 ? D ILE 391 
1177 1 Y 1 D VAL 399 ? D VAL 392 
1178 1 Y 1 D ALA 400 ? D ALA 393 
1179 1 Y 1 D ALA 401 ? D ALA 394 
1180 1 Y 1 D ALA 402 ? D ALA 395 
1181 1 Y 1 D ALA 403 ? D ALA 396 
1182 1 Y 1 D LEU 404 ? D LEU 397 
1183 1 Y 1 D CYS 405 ? D CYS 398 
1184 1 Y 1 D ILE 406 ? D ILE 399 
1185 1 Y 1 D LEU 407 ? D LEU 400 
1186 1 Y 1 D ILE 408 ? D ILE 401 
1187 1 Y 1 D LEU 409 ? D LEU 402 
1188 1 Y 1 D LEU 410 ? D LEU 403 
1189 1 Y 1 D TYR 411 ? D TYR 404 
1190 1 Y 1 D ALA 412 ? D ALA 405 
1191 1 Y 1 D MET 413 ? D MET 406 
1192 1 Y 1 D TYR 414 ? D TYR 407 
1193 1 Y 1 D LYS 415 ? D LYS 408 
1194 1 Y 1 D TYR 416 ? D TYR 409 
1195 1 Y 1 D ARG 417 ? D ARG 410 
1196 1 Y 1 D ASN 418 ? D ASN 411 
1197 1 Y 1 D ARG 419 ? D ARG 412 
1198 1 Y 1 D ASP 420 ? D ASP 413 
1199 1 Y 1 D GLU 421 ? D GLU 414 
1200 1 Y 1 D GLY 422 ? D GLY 415 
1201 1 Y 1 D SER 423 ? D SER 416 
1202 1 Y 1 D TYR 424 ? D TYR 417 
1203 1 Y 1 D HIS 425 ? D HIS 418 
1204 1 Y 1 D VAL 426 ? D VAL 419 
1205 1 Y 1 D ASP 427 ? D ASP 420 
1206 1 Y 1 D GLU 428 ? D GLU 421 
1207 1 Y 1 D SER 429 ? D SER 422 
1208 1 Y 1 D ARG 430 ? D ARG 423 
1209 1 Y 1 D ASN 431 ? D ASN 424 
1210 1 Y 1 D TYR 432 ? D TYR 425 
1211 1 Y 1 D ILE 433 ? D ILE 426 
1212 1 Y 1 D SER 434 ? D SER 427 
1213 1 Y 1 D ASN 435 ? D ASN 428 
1214 1 Y 1 D SER 436 ? D SER 429 
1215 1 Y 1 D ALA 437 ? D ALA 430 
1216 1 Y 1 D GLN 438 ? D GLN 431 
1217 1 Y 1 D SER 439 ? D SER 432 
1218 1 Y 1 D ASN 440 ? D ASN 433 
1219 1 Y 1 D GLY 441 ? D GLY 434 
1220 1 Y 1 D ALA 442 ? D ALA 435 
1221 1 Y 1 D VAL 443 ? D VAL 436 
1222 1 Y 1 D VAL 444 ? D VAL 437 
1223 1 Y 1 D LYS 445 ? D LYS 438 
1224 1 Y 1 D GLU 446 ? D GLU 439 
1225 1 Y 1 D LYS 447 ? D LYS 440 
1226 1 Y 1 D GLN 448 ? D GLN 441 
1227 1 Y 1 D PRO 449 ? D PRO 442 
1228 1 Y 1 D SER 450 ? D SER 443 
1229 1 Y 1 D SER 451 ? D SER 444 
1230 1 Y 1 D ALA 452 ? D ALA 445 
1231 1 Y 1 D LYS 453 ? D LYS 446 
1232 1 Y 1 D SER 454 ? D SER 447 
1233 1 Y 1 D ALA 455 ? D ALA 448 
1234 1 Y 1 D ASN 456 ? D ASN 449 
1235 1 Y 1 D LYS 457 ? D LYS 450 
1236 1 Y 1 D ASN 458 ? D ASN 451 
1237 1 Y 1 D LYS 459 ? D LYS 452 
1238 1 Y 1 D LYS 460 ? D LYS 453 
1239 1 Y 1 D ASN 461 ? D ASN 454 
1240 1 Y 1 D LYS 462 ? D LYS 455 
1241 1 Y 1 D ASP 463 ? D ASP 456 
1242 1 Y 1 D LYS 464 ? D LYS 457 
1243 1 Y 1 D GLU 465 ? D GLU 458 
1244 1 Y 1 D TYR 466 ? D TYR 459 
1245 1 Y 1 D TYR 467 ? D TYR 460 
1246 1 Y 1 D VAL 468 ? D VAL 461 
1247 1 Y 1 D SER 469 ? D SER 462 
1248 1 Y 1 D ASN 470 ? D ASN 463 
1249 1 Y 1 D SER 471 ? D SER 464 
1250 1 Y 1 D LEU 472 ? D LEU 465 
1251 1 Y 1 D GLU 473 ? D GLU 466 
1252 1 Y 1 D VAL 474 ? D VAL 467 
1253 1 Y 1 D LEU 475 ? D LEU 468 
1254 1 Y 1 D PHE 476 ? D PHE 469 
1255 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           8G80 
_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 two' 
# 
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                    8G80 
_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  ? 139.975 172.828 95.330  1.00 82.46  ? 40   ARG A N   1 
ATOM   2     C  CA  . ARG A 1 82  ? 138.868 173.195 94.455  1.00 83.99  ? 40   ARG A CA  1 
ATOM   3     C  C   . ARG A 1 82  ? 137.597 173.449 95.255  1.00 83.04  ? 40   ARG A C   1 
ATOM   4     O  O   . ARG A 1 82  ? 137.411 172.888 96.334  1.00 82.55  ? 40   ARG A O   1 
ATOM   5     C  CB  . ARG A 1 82  ? 138.624 172.102 93.412  1.00 83.80  ? 40   ARG A CB  1 
ATOM   6     C  CG  . ARG A 1 82  ? 138.083 172.616 92.088  1.00 81.30  ? 40   ARG A CG  1 
ATOM   7     C  CD  . ARG A 1 82  ? 137.885 171.484 91.094  1.00 80.31  ? 40   ARG A CD  1 
ATOM   8     N  NE  . ARG A 1 82  ? 139.055 170.617 91.017  1.00 82.92  ? 40   ARG A NE  1 
ATOM   9     C  CZ  . ARG A 1 82  ? 139.043 169.383 90.533  1.00 83.90  ? 40   ARG A CZ  1 
ATOM   10    N  NH1 . ARG A 1 82  ? 137.931 168.831 90.075  1.00 83.72  ? 40   ARG A NH1 1 
ATOM   11    N  NH2 . ARG A 1 82  ? 140.175 168.685 90.507  1.00 82.95  ? 40   ARG A NH2 1 
ATOM   12    N  N   . PHE A 1 83  ? 136.719 174.294 94.711  1.00 77.41  ? 41   PHE A N   1 
ATOM   13    C  CA  . PHE A 1 83  ? 135.438 174.640 95.325  1.00 74.24  ? 41   PHE A CA  1 
ATOM   14    C  C   . PHE A 1 83  ? 134.330 174.286 94.339  1.00 74.07  ? 41   PHE A C   1 
ATOM   15    O  O   . PHE A 1 83  ? 133.719 175.174 93.729  1.00 73.99  ? 41   PHE A O   1 
ATOM   16    C  CB  . PHE A 1 83  ? 135.359 176.122 95.696  1.00 71.45  ? 41   PHE A CB  1 
ATOM   17    C  CG  . PHE A 1 83  ? 136.123 176.502 96.941  1.00 74.35  ? 41   PHE A CG  1 
ATOM   18    C  CD1 . PHE A 1 83  ? 137.144 175.710 97.435  1.00 77.23  ? 41   PHE A CD1 1 
ATOM   19    C  CD2 . PHE A 1 83  ? 135.811 177.670 97.616  1.00 74.65  ? 41   PHE A CD2 1 
ATOM   20    C  CE1 . PHE A 1 83  ? 137.837 176.072 98.575  1.00 77.98  ? 41   PHE A CE1 1 
ATOM   21    C  CE2 . PHE A 1 83  ? 136.498 178.038 98.756  1.00 76.39  ? 41   PHE A CE2 1 
ATOM   22    C  CZ  . PHE A 1 83  ? 137.512 177.237 99.237  1.00 77.18  ? 41   PHE A CZ  1 
ATOM   23    N  N   . PRO A 1 84  ? 134.045 172.997 94.161  1.00 70.39  ? 42   PRO A N   1 
ATOM   24    C  CA  . PRO A 1 84  ? 133.082 172.590 93.132  1.00 69.38  ? 42   PRO A CA  1 
ATOM   25    C  C   . PRO A 1 84  ? 131.675 173.077 93.435  1.00 69.48  ? 42   PRO A C   1 
ATOM   26    O  O   . PRO A 1 84  ? 131.288 173.266 94.590  1.00 73.82  ? 42   PRO A O   1 
ATOM   27    C  CB  . PRO A 1 84  ? 133.155 171.059 93.166  1.00 66.36  ? 42   PRO A CB  1 
ATOM   28    C  CG  . PRO A 1 84  ? 133.628 170.744 94.537  1.00 68.52  ? 42   PRO A CG  1 
ATOM   29    C  CD  . PRO A 1 84  ? 134.583 171.841 94.895  1.00 70.29  ? 42   PRO A CD  1 
ATOM   30    N  N   . VAL A 1 85  ? 130.909 173.282 92.367  1.00 70.50  ? 43   VAL A N   1 
ATOM   31    C  CA  . VAL A 1 85  ? 129.524 173.727 92.450  1.00 72.22  ? 43   VAL A CA  1 
ATOM   32    C  C   . VAL A 1 85  ? 128.639 172.659 91.823  1.00 73.10  ? 43   VAL A C   1 
ATOM   33    O  O   . VAL A 1 85  ? 128.910 172.198 90.708  1.00 73.00  ? 43   VAL A O   1 
ATOM   34    C  CB  . VAL A 1 85  ? 129.319 175.086 91.755  1.00 72.08  ? 43   VAL A CB  1 
ATOM   35    C  CG1 . VAL A 1 85  ? 129.712 176.218 92.686  1.00 71.86  ? 43   VAL A CG1 1 
ATOM   36    C  CG2 . VAL A 1 85  ? 130.129 175.153 90.471  1.00 70.57  ? 43   VAL A CG2 1 
ATOM   37    N  N   . VAL A 1 86  ? 127.591 172.264 92.541  1.00 72.83  ? 44   VAL A N   1 
ATOM   38    C  CA  . VAL A 1 86  ? 126.634 171.270 92.071  1.00 73.14  ? 44   VAL A CA  1 
ATOM   39    C  C   . VAL A 1 86  ? 125.255 171.911 92.043  1.00 72.65  ? 44   VAL A C   1 
ATOM   40    O  O   . VAL A 1 86  ? 124.838 172.542 93.021  1.00 72.39  ? 44   VAL A O   1 
ATOM   41    C  CB  . VAL A 1 86  ? 126.635 170.011 92.957  1.00 69.39  ? 44   VAL A CB  1 
ATOM   42    C  CG1 . VAL A 1 86  ? 125.746 168.941 92.350  1.00 69.08  ? 44   VAL A CG1 1 
ATOM   43    C  CG2 . VAL A 1 86  ? 128.050 169.489 93.131  1.00 70.96  ? 44   VAL A CG2 1 
ATOM   44    N  N   . ASN A 1 87  ? 124.552 171.748 90.927  1.00 79.72  ? 45   ASN A N   1 
ATOM   45    C  CA  . ASN A 1 87  ? 123.238 172.347 90.741  1.00 79.11  ? 45   ASN A CA  1 
ATOM   46    C  C   . ASN A 1 87  ? 122.160 171.431 91.303  1.00 78.07  ? 45   ASN A C   1 
ATOM   47    O  O   . ASN A 1 87  ? 122.096 170.248 90.952  1.00 76.50  ? 45   ASN A O   1 
ATOM   48    C  CB  . ASN A 1 87  ? 122.977 172.620 89.259  1.00 79.10  ? 45   ASN A CB  1 
ATOM   49    C  CG  . ASN A 1 87  ? 121.525 172.946 88.974  1.00 79.76  ? 45   ASN A CG  1 
ATOM   50    O  OD1 . ASN A 1 87  ? 121.073 174.068 89.197  1.00 81.01  ? 45   ASN A OD1 1 
ATOM   51    N  ND2 . ASN A 1 87  ? 120.784 171.962 88.475  1.00 77.51  ? 45   ASN A ND2 1 
ATOM   52    N  N   . THR A 1 88  ? 121.317 171.980 92.172  1.00 81.36  ? 46   THR A N   1 
ATOM   53    C  CA  . THR A 1 88  ? 120.174 171.267 92.713  1.00 76.64  ? 46   THR A CA  1 
ATOM   54    C  C   . THR A 1 88  ? 118.900 171.747 92.022  1.00 80.87  ? 46   THR A C   1 
ATOM   55    O  O   . THR A 1 88  ? 118.917 172.656 91.189  1.00 81.72  ? 46   THR A O   1 
ATOM   56    C  CB  . THR A 1 88  ? 120.082 171.458 94.228  1.00 72.37  ? 46   THR A CB  1 
ATOM   57    O  OG1 . THR A 1 88  ? 119.359 172.660 94.517  1.00 74.65  ? 46   THR A OG1 1 
ATOM   58    C  CG2 . THR A 1 88  ? 121.470 171.552 94.838  1.00 75.14  ? 46   THR A CG2 1 
ATOM   59    N  N   . ALA A 1 89  ? 117.776 171.123 92.376  1.00 78.74  ? 47   ALA A N   1 
ATOM   60    C  CA  . ALA A 1 89  ? 116.497 171.478 91.773  1.00 78.11  ? 47   ALA A CA  1 
ATOM   61    C  C   . ALA A 1 89  ? 116.023 172.871 92.163  1.00 79.91  ? 47   ALA A C   1 
ATOM   62    O  O   . ALA A 1 89  ? 115.079 173.377 91.547  1.00 81.69  ? 47   ALA A O   1 
ATOM   63    C  CB  . ALA A 1 89  ? 115.434 170.446 92.150  1.00 76.05  ? 47   ALA A CB  1 
ATOM   64    N  N   . TYR A 1 90  ? 116.643 173.498 93.165  1.00 81.83  ? 48   TYR A N   1 
ATOM   65    C  CA  . TYR A 1 90  ? 116.278 174.845 93.579  1.00 82.86  ? 48   TYR A CA  1 
ATOM   66    C  C   . TYR A 1 90  ? 117.322 175.896 93.237  1.00 83.98  ? 48   TYR A C   1 
ATOM   67    O  O   . TYR A 1 90  ? 116.987 177.084 93.204  1.00 86.60  ? 48   TYR A O   1 
ATOM   68    C  CB  . TYR A 1 90  ? 116.015 174.887 95.092  1.00 81.87  ? 48   TYR A CB  1 
ATOM   69    C  CG  . TYR A 1 90  ? 114.984 173.890 95.566  1.00 82.34  ? 48   TYR A CG  1 
ATOM   70    C  CD1 . TYR A 1 90  ? 113.635 174.075 95.298  1.00 81.64  ? 48   TYR A CD1 1 
ATOM   71    C  CD2 . TYR A 1 90  ? 115.360 172.766 96.288  1.00 82.52  ? 48   TYR A CD2 1 
ATOM   72    C  CE1 . TYR A 1 90  ? 112.690 173.166 95.731  1.00 80.54  ? 48   TYR A CE1 1 
ATOM   73    C  CE2 . TYR A 1 90  ? 114.422 171.852 96.726  1.00 82.57  ? 48   TYR A CE2 1 
ATOM   74    C  CZ  . TYR A 1 90  ? 113.089 172.057 96.445  1.00 82.39  ? 48   TYR A CZ  1 
ATOM   75    O  OH  . TYR A 1 90  ? 112.152 171.149 96.880  1.00 82.83  ? 48   TYR A OH  1 
ATOM   76    N  N   . GLY A 1 91  ? 118.564 175.498 92.982  1.00 85.61  ? 49   GLY A N   1 
ATOM   77    C  CA  . GLY A 1 91  ? 119.607 176.461 92.684  1.00 88.29  ? 49   GLY A CA  1 
ATOM   78    C  C   . GLY A 1 91  ? 120.955 175.775 92.584  1.00 86.20  ? 49   GLY A C   1 
ATOM   79    O  O   . GLY A 1 91  ? 121.033 174.566 92.358  1.00 86.48  ? 49   GLY A O   1 
ATOM   80    N  N   . ARG A 1 92  ? 122.011 176.567 92.751  1.00 88.09  ? 50   ARG A N   1 
ATOM   81    C  CA  . ARG A 1 92  ? 123.378 176.072 92.697  1.00 86.99  ? 50   ARG A CA  1 
ATOM   82    C  C   . ARG A 1 92  ? 124.091 176.363 94.009  1.00 89.69  ? 50   ARG A C   1 
ATOM   83    O  O   . ARG A 1 92  ? 124.027 177.483 94.531  1.00 92.19  ? 50   ARG A O   1 
ATOM   84    C  CB  . ARG A 1 92  ? 124.152 176.697 91.530  1.00 90.08  ? 50   ARG A CB  1 
ATOM   85    C  CG  . ARG A 1 92  ? 123.810 176.101 90.174  1.00 89.61  ? 50   ARG A CG  1 
ATOM   86    C  CD  . ARG A 1 92  ? 124.499 176.850 89.044  1.00 90.45  ? 50   ARG A CD  1 
ATOM   87    N  NE  . ARG A 1 92  ? 124.286 178.289 89.128  1.00 91.45  ? 50   ARG A NE  1 
ATOM   88    C  CZ  . ARG A 1 92  ? 123.169 178.905 88.764  1.00 90.25  ? 50   ARG A CZ  1 
ATOM   89    N  NH1 . ARG A 1 92  ? 122.139 178.235 88.274  1.00 90.13  ? 50   ARG A NH1 1 
ATOM   90    N  NH2 . ARG A 1 92  ? 123.085 180.225 88.892  1.00 89.94  ? 50   ARG A NH2 1 
ATOM   91    N  N   . VAL A 1 93  ? 124.785 175.351 94.526  1.00 78.77  ? 51   VAL A N   1 
ATOM   92    C  CA  . VAL A 1 93  ? 125.471 175.437 95.807  1.00 78.48  ? 51   VAL A CA  1 
ATOM   93    C  C   . VAL A 1 93  ? 126.949 175.134 95.604  1.00 77.83  ? 51   VAL A C   1 
ATOM   94    O  O   . VAL A 1 93  ? 127.337 174.383 94.704  1.00 78.62  ? 51   VAL A O   1 
ATOM   95    C  CB  . VAL A 1 93  ? 124.857 174.478 96.853  1.00 76.18  ? 51   VAL A CB  1 
ATOM   96    C  CG1 . VAL A 1 93  ? 123.404 174.836 97.112  1.00 76.97  ? 51   VAL A CG1 1 
ATOM   97    C  CG2 . VAL A 1 93  ? 124.977 173.037 96.392  1.00 74.41  ? 51   VAL A CG2 1 
ATOM   98    N  N   . ARG A 1 94  ? 127.774 175.740 96.451  1.00 77.36  ? 52   ARG A N   1 
ATOM   99    C  CA  . ARG A 1 94  ? 129.216 175.539 96.450  1.00 78.71  ? 52   ARG A CA  1 
ATOM   100   C  C   . ARG A 1 94  ? 129.649 174.868 97.745  1.00 76.75  ? 52   ARG A C   1 
ATOM   101   O  O   . ARG A 1 94  ? 129.113 175.160 98.819  1.00 78.06  ? 52   ARG A O   1 
ATOM   102   C  CB  . ARG A 1 94  ? 129.978 176.860 96.291  1.00 77.41  ? 52   ARG A CB  1 
ATOM   103   C  CG  . ARG A 1 94  ? 131.450 176.643 95.951  1.00 77.99  ? 52   ARG A CG  1 
ATOM   104   C  CD  . ARG A 1 94  ? 132.147 177.856 95.349  1.00 76.56  ? 52   ARG A CD  1 
ATOM   105   N  NE  . ARG A 1 94  ? 131.266 178.733 94.591  1.00 76.88  ? 52   ARG A NE  1 
ATOM   106   C  CZ  . ARG A 1 94  ? 130.919 179.952 94.980  1.00 79.47  ? 52   ARG A CZ  1 
ATOM   107   N  NH1 . ARG A 1 94  ? 131.346 180.460 96.124  1.00 82.03  ? 52   ARG A NH1 1 
ATOM   108   N  NH2 . ARG A 1 94  ? 130.135 180.684 94.196  1.00 78.14  ? 52   ARG A NH2 1 
ATOM   109   N  N   . GLY A 1 95  ? 130.625 173.966 97.635  1.00 68.44  ? 53   GLY A N   1 
ATOM   110   C  CA  . GLY A 1 95  ? 131.215 173.323 98.789  1.00 68.24  ? 53   GLY A CA  1 
ATOM   111   C  C   . GLY A 1 95  ? 132.730 173.390 98.734  1.00 72.99  ? 53   GLY A C   1 
ATOM   112   O  O   . GLY A 1 95  ? 133.315 173.947 97.803  1.00 77.27  ? 53   GLY A O   1 
ATOM   113   N  N   . VAL A 1 96  ? 133.348 172.806 99.754  1.00 73.16  ? 54   VAL A N   1 
ATOM   114   C  CA  . VAL A 1 96  ? 134.797 172.754 99.861  1.00 70.71  ? 54   VAL A CA  1 
ATOM   115   C  C   . VAL A 1 96  ? 135.252 171.316 99.634  1.00 69.53  ? 54   VAL A C   1 
ATOM   116   O  O   . VAL A 1 96  ? 134.447 170.394 99.528  1.00 71.64  ? 54   VAL A O   1 
ATOM   117   C  CB  . VAL A 1 96  ? 135.298 173.292 101.215 1.00 72.69  ? 54   VAL A CB  1 
ATOM   118   C  CG1 . VAL A 1 96  ? 135.308 174.809 101.208 1.00 72.07  ? 54   VAL A CG1 1 
ATOM   119   C  CG2 . VAL A 1 96  ? 134.428 172.770 102.344 1.00 70.54  ? 54   VAL A CG2 1 
ATOM   120   N  N   . ARG A 1 97  ? 136.567 171.134 99.561  1.00 78.22  ? 55   ARG A N   1 
ATOM   121   C  CA  . ARG A 1 97  ? 137.189 169.840 99.290  1.00 80.46  ? 55   ARG A CA  1 
ATOM   122   C  C   . ARG A 1 97  ? 138.200 169.508 100.380 1.00 81.34  ? 55   ARG A C   1 
ATOM   123   O  O   . ARG A 1 97  ? 139.362 169.190 100.119 1.00 84.32  ? 55   ARG A O   1 
ATOM   124   C  CB  . ARG A 1 97  ? 137.839 169.822 97.908  1.00 82.20  ? 55   ARG A CB  1 
ATOM   125   C  CG  . ARG A 1 97  ? 138.132 168.424 97.379  1.00 80.21  ? 55   ARG A CG  1 
ATOM   126   C  CD  . ARG A 1 97  ? 138.716 168.462 95.978  1.00 80.11  ? 55   ARG A CD  1 
ATOM   127   N  NE  . ARG A 1 97  ? 137.677 168.465 94.956  1.00 82.79  ? 55   ARG A NE  1 
ATOM   128   C  CZ  . ARG A 1 97  ? 137.689 167.697 93.875  1.00 83.32  ? 55   ARG A CZ  1 
ATOM   129   N  NH1 . ARG A 1 97  ? 138.674 166.845 93.644  1.00 82.51  ? 55   ARG A NH1 1 
ATOM   130   N  NH2 . ARG A 1 97  ? 136.687 167.785 93.005  1.00 82.06  ? 55   ARG A NH2 1 
ATOM   131   N  N   . ARG A 1 98  ? 137.757 169.608 101.633 1.00 78.34  ? 56   ARG A N   1 
ATOM   132   C  CA  . ARG A 1 98  ? 138.645 169.421 102.773 1.00 78.81  ? 56   ARG A CA  1 
ATOM   133   C  C   . ARG A 1 98  ? 139.297 168.044 102.747 1.00 82.34  ? 56   ARG A C   1 
ATOM   134   O  O   . ARG A 1 98  ? 138.675 167.047 102.369 1.00 81.23  ? 56   ARG A O   1 
ATOM   135   C  CB  . ARG A 1 98  ? 137.868 169.605 104.076 1.00 77.86  ? 56   ARG A CB  1 
ATOM   136   C  CG  . ARG A 1 98  ? 138.677 170.223 105.202 1.00 80.01  ? 56   ARG A CG  1 
ATOM   137   C  CD  . ARG A 1 98  ? 138.509 171.732 105.232 1.00 80.96  ? 56   ARG A CD  1 
ATOM   138   N  NE  . ARG A 1 98  ? 137.136 172.115 105.534 1.00 79.60  ? 56   ARG A NE  1 
ATOM   139   C  CZ  . ARG A 1 98  ? 136.743 173.355 105.791 1.00 81.12  ? 56   ARG A CZ  1 
ATOM   140   N  NH1 . ARG A 1 98  ? 137.597 174.365 105.792 1.00 82.20  ? 56   ARG A NH1 1 
ATOM   141   N  NH2 . ARG A 1 98  ? 135.461 173.587 106.056 1.00 81.99  ? 56   ARG A NH2 1 
ATOM   142   N  N   . GLU A 1 99  ? 140.563 167.998 103.150 1.00 91.09  ? 57   GLU A N   1 
ATOM   143   C  CA  . GLU A 1 99  ? 141.350 166.775 103.179 1.00 90.56  ? 57   GLU A CA  1 
ATOM   144   C  C   . GLU A 1 99  ? 141.383 166.209 104.595 1.00 90.01  ? 57   GLU A C   1 
ATOM   145   O  O   . GLU A 1 99  ? 141.292 166.946 105.580 1.00 89.21  ? 57   GLU A O   1 
ATOM   146   C  CB  . GLU A 1 99  ? 142.775 167.039 102.685 1.00 87.94  ? 57   GLU A CB  1 
ATOM   147   C  CG  . GLU A 1 99  ? 143.586 165.793 102.358 1.00 90.64  ? 57   GLU A CG  1 
ATOM   148   C  CD  . GLU A 1 99  ? 142.725 164.631 101.907 1.00 92.05  ? 57   GLU A CD  1 
ATOM   149   O  OE1 . GLU A 1 99  ? 142.280 164.637 100.740 1.00 91.34  ? 57   GLU A OE1 1 
ATOM   150   O  OE2 . GLU A 1 99  ? 142.493 163.711 102.719 1.00 90.98  ? 57   GLU A OE2 1 
ATOM   151   N  N   . LEU A 1 100 ? 141.515 164.891 104.687 1.00 89.70  ? 58   LEU A N   1 
ATOM   152   C  CA  . LEU A 1 100 ? 141.490 164.183 105.958 1.00 90.62  ? 58   LEU A CA  1 
ATOM   153   C  C   . LEU A 1 100 ? 142.904 163.946 106.478 1.00 92.46  ? 58   LEU A C   1 
ATOM   154   O  O   . LEU A 1 100 ? 143.884 163.970 105.729 1.00 92.18  ? 58   LEU A O   1 
ATOM   155   C  CB  . LEU A 1 100 ? 140.751 162.850 105.817 1.00 90.04  ? 58   LEU A CB  1 
ATOM   156   C  CG  . LEU A 1 100 ? 139.423 162.923 105.063 1.00 88.32  ? 58   LEU A CG  1 
ATOM   157   C  CD1 . LEU A 1 100 ? 138.745 161.567 105.035 1.00 87.52  ? 58   LEU A CD1 1 
ATOM   158   C  CD2 . LEU A 1 100 ? 138.515 163.963 105.693 1.00 88.40  ? 58   LEU A CD2 1 
ATOM   159   N  N   . ASN A 1 101 ? 142.994 163.719 107.791 1.00 100.26 ? 59   ASN A N   1 
ATOM   160   C  CA  . ASN A 1 101 ? 144.293 163.520 108.427 1.00 98.99  ? 59   ASN A CA  1 
ATOM   161   C  C   . ASN A 1 101 ? 144.954 162.229 107.959 1.00 100.48 ? 59   ASN A C   1 
ATOM   162   O  O   . ASN A 1 101 ? 146.168 162.198 107.725 1.00 100.15 ? 59   ASN A O   1 
ATOM   163   C  CB  . ASN A 1 101 ? 144.137 163.520 109.947 1.00 96.16  ? 59   ASN A CB  1 
ATOM   164   N  N   . ASN A 1 102 ? 144.180 161.156 107.820 1.00 103.61 ? 60   ASN A N   1 
ATOM   165   C  CA  . ASN A 1 102 ? 144.748 159.872 107.442 1.00 103.43 ? 60   ASN A CA  1 
ATOM   166   C  C   . ASN A 1 102 ? 145.196 159.891 105.982 1.00 104.11 ? 60   ASN A C   1 
ATOM   167   O  O   . ASN A 1 102 ? 144.761 160.720 105.177 1.00 102.47 ? 60   ASN A O   1 
ATOM   168   C  CB  . ASN A 1 102 ? 143.739 158.749 107.673 1.00 101.21 ? 60   ASN A CB  1 
ATOM   169   C  CG  . ASN A 1 102 ? 144.404 157.400 107.860 1.00 102.59 ? 60   ASN A CG  1 
ATOM   170   O  OD1 . ASN A 1 102 ? 144.906 156.806 106.907 1.00 103.25 ? 60   ASN A OD1 1 
ATOM   171   N  ND2 . ASN A 1 102 ? 144.411 156.910 109.094 1.00 102.23 ? 60   ASN A ND2 1 
ATOM   172   N  N   . GLU A 1 103 ? 146.084 158.957 105.645 1.00 107.44 ? 61   GLU A N   1 
ATOM   173   C  CA  . GLU A 1 103 ? 146.704 158.904 104.329 1.00 107.59 ? 61   GLU A CA  1 
ATOM   174   C  C   . GLU A 1 103 ? 146.138 157.802 103.440 1.00 105.97 ? 61   GLU A C   1 
ATOM   175   O  O   . GLU A 1 103 ? 146.676 157.564 102.354 1.00 106.48 ? 61   GLU A O   1 
ATOM   176   C  CB  . GLU A 1 103 ? 148.218 158.730 104.470 1.00 106.66 ? 61   GLU A CB  1 
ATOM   177   N  N   . ILE A 1 104 ? 145.074 157.123 103.868 1.00 94.01  ? 62   ILE A N   1 
ATOM   178   C  CA  . ILE A 1 104 ? 144.470 156.055 103.085 1.00 93.99  ? 62   ILE A CA  1 
ATOM   179   C  C   . ILE A 1 104 ? 143.056 156.401 102.636 1.00 94.48  ? 62   ILE A C   1 
ATOM   180   O  O   . ILE A 1 104 ? 142.358 155.547 102.088 1.00 94.43  ? 62   ILE A O   1 
ATOM   181   C  CB  . ILE A 1 104 ? 144.485 154.719 103.854 1.00 94.51  ? 62   ILE A CB  1 
ATOM   182   C  CG1 . ILE A 1 104 ? 143.448 154.733 104.978 1.00 96.30  ? 62   ILE A CG1 1 
ATOM   183   C  CG2 . ILE A 1 104 ? 145.872 154.439 104.409 1.00 93.72  ? 62   ILE A CG2 1 
ATOM   184   C  CD1 . ILE A 1 104 ? 143.232 153.383 105.626 1.00 94.53  ? 62   ILE A CD1 1 
ATOM   185   N  N   . LEU A 1 105 ? 142.621 157.639 102.848 1.00 83.87  ? 63   LEU A N   1 
ATOM   186   C  CA  . LEU A 1 105 ? 141.277 158.073 102.497 1.00 81.36  ? 63   LEU A CA  1 
ATOM   187   C  C   . LEU A 1 105 ? 141.348 159.226 101.506 1.00 82.74  ? 63   LEU A C   1 
ATOM   188   O  O   . LEU A 1 105 ? 142.166 160.139 101.658 1.00 83.37  ? 63   LEU A O   1 
ATOM   189   C  CB  . LEU A 1 105 ? 140.491 158.498 103.742 1.00 81.49  ? 63   LEU A CB  1 
ATOM   190   C  CG  . LEU A 1 105 ? 140.784 157.710 105.020 1.00 81.86  ? 63   LEU A CG  1 
ATOM   191   C  CD1 . LEU A 1 105 ? 140.333 158.484 106.246 1.00 79.69  ? 63   LEU A CD1 1 
ATOM   192   C  CD2 . LEU A 1 105 ? 140.117 156.346 104.968 1.00 80.12  ? 63   LEU A CD2 1 
ATOM   193   N  N   . GLY A 1 106 ? 140.489 159.178 100.495 1.00 75.26  ? 64   GLY A N   1 
ATOM   194   C  CA  . GLY A 1 106 ? 140.460 160.197 99.473  1.00 73.72  ? 64   GLY A CA  1 
ATOM   195   C  C   . GLY A 1 106 ? 139.805 161.471 99.954  1.00 71.29  ? 64   GLY A C   1 
ATOM   196   O  O   . GLY A 1 106 ? 139.191 161.538 101.029 1.00 72.73  ? 64   GLY A O   1 
ATOM   197   N  N   . PRO A 1 107 ? 139.937 162.521 99.148  1.00 71.75  ? 65   PRO A N   1 
ATOM   198   C  CA  . PRO A 1 107 ? 139.320 163.804 99.501  1.00 72.08  ? 65   PRO A CA  1 
ATOM   199   C  C   . PRO A 1 107 ? 137.804 163.710 99.516  1.00 74.97  ? 65   PRO A C   1 
ATOM   200   O  O   . PRO A 1 107 ? 137.197 162.916 98.794  1.00 76.19  ? 65   PRO A O   1 
ATOM   201   C  CB  . PRO A 1 107 ? 139.805 164.751 98.396  1.00 73.82  ? 65   PRO A CB  1 
ATOM   202   C  CG  . PRO A 1 107 ? 140.984 164.064 97.776  1.00 73.65  ? 65   PRO A CG  1 
ATOM   203   C  CD  . PRO A 1 107 ? 140.706 162.602 97.896  1.00 74.33  ? 65   PRO A CD  1 
ATOM   204   N  N   . VAL A 1 108 ? 137.192 164.541 100.357 1.00 65.07  ? 66   VAL A N   1 
ATOM   205   C  CA  . VAL A 1 108 ? 135.746 164.573 100.534 1.00 60.09  ? 66   VAL A CA  1 
ATOM   206   C  C   . VAL A 1 108 ? 135.261 165.991 100.268 1.00 61.86  ? 66   VAL A C   1 
ATOM   207   O  O   . VAL A 1 108 ? 135.819 166.954 100.805 1.00 64.48  ? 66   VAL A O   1 
ATOM   208   C  CB  . VAL A 1 108 ? 135.339 164.108 101.944 1.00 55.20  ? 66   VAL A CB  1 
ATOM   209   C  CG1 . VAL A 1 108 ? 134.024 164.743 102.363 1.00 57.16  ? 66   VAL A CG1 1 
ATOM   210   C  CG2 . VAL A 1 108 ? 135.240 162.596 101.991 1.00 55.11  ? 66   VAL A CG2 1 
ATOM   211   N  N   . VAL A 1 109 ? 134.232 166.116 99.435  1.00 58.39  ? 67   VAL A N   1 
ATOM   212   C  CA  . VAL A 1 109 ? 133.612 167.401 99.143  1.00 57.71  ? 67   VAL A CA  1 
ATOM   213   C  C   . VAL A 1 109 ? 132.461 167.606 100.119 1.00 58.67  ? 67   VAL A C   1 
ATOM   214   O  O   . VAL A 1 109 ? 131.519 166.807 100.158 1.00 60.54  ? 67   VAL A O   1 
ATOM   215   C  CB  . VAL A 1 109 ? 133.122 167.465 97.690  1.00 56.18  ? 67   VAL A CB  1 
ATOM   216   C  CG1 . VAL A 1 109 ? 132.544 168.833 97.389  1.00 58.61  ? 67   VAL A CG1 1 
ATOM   217   C  CG2 . VAL A 1 109 ? 134.257 167.141 96.736  1.00 58.56  ? 67   VAL A CG2 1 
ATOM   218   N  N   . GLN A 1 110 ? 132.533 168.674 100.905 1.00 54.69  ? 68   GLN A N   1 
ATOM   219   C  CA  . GLN A 1 110 ? 131.560 168.946 101.954 1.00 52.00  ? 68   GLN A CA  1 
ATOM   220   C  C   . GLN A 1 110 ? 130.676 170.113 101.539 1.00 56.66  ? 68   GLN A C   1 
ATOM   221   O  O   . GLN A 1 110 ? 131.179 171.205 101.253 1.00 63.47  ? 68   GLN A O   1 
ATOM   222   C  CB  . GLN A 1 110 ? 132.259 169.255 103.277 1.00 54.41  ? 68   GLN A CB  1 
ATOM   223   C  CG  . GLN A 1 110 ? 133.341 168.263 103.659 1.00 58.70  ? 68   GLN A CG  1 
ATOM   224   C  CD  . GLN A 1 110 ? 134.007 168.612 104.974 1.00 62.68  ? 68   GLN A CD  1 
ATOM   225   O  OE1 . GLN A 1 110 ? 133.695 169.632 105.588 1.00 61.30  ? 68   GLN A OE1 1 
ATOM   226   N  NE2 . GLN A 1 110 ? 134.930 167.766 105.413 1.00 59.49  ? 68   GLN A NE2 1 
ATOM   227   N  N   . PHE A 1 111 ? 129.368 169.881 101.508 1.00 50.30  ? 69   PHE A N   1 
ATOM   228   C  CA  . PHE A 1 111 ? 128.374 170.938 101.331 1.00 50.36  ? 69   PHE A CA  1 
ATOM   229   C  C   . PHE A 1 111 ? 127.671 171.099 102.672 1.00 50.92  ? 69   PHE A C   1 
ATOM   230   O  O   . PHE A 1 111 ? 126.820 170.283 103.034 1.00 57.62  ? 69   PHE A O   1 
ATOM   231   C  CB  . PHE A 1 111 ? 127.386 170.598 100.220 1.00 47.13  ? 69   PHE A CB  1 
ATOM   232   C  CG  . PHE A 1 111 ? 128.033 170.271 98.908  1.00 50.99  ? 69   PHE A CG  1 
ATOM   233   C  CD1 . PHE A 1 111 ? 128.405 171.278 98.035  1.00 54.79  ? 69   PHE A CD1 1 
ATOM   234   C  CD2 . PHE A 1 111 ? 128.265 168.957 98.544  1.00 49.69  ? 69   PHE A CD2 1 
ATOM   235   C  CE1 . PHE A 1 111 ? 128.998 170.982 96.826  1.00 54.59  ? 69   PHE A CE1 1 
ATOM   236   C  CE2 . PHE A 1 111 ? 128.857 168.653 97.336  1.00 52.29  ? 69   PHE A CE2 1 
ATOM   237   C  CZ  . PHE A 1 111 ? 129.224 169.667 96.476  1.00 58.03  ? 69   PHE A CZ  1 
ATOM   238   N  N   . LEU A 1 112 ? 128.032 172.141 103.413 1.00 51.88  ? 70   LEU A N   1 
ATOM   239   C  CA  . LEU A 1 112 ? 127.543 172.349 104.769 1.00 50.51  ? 70   LEU A CA  1 
ATOM   240   C  C   . LEU A 1 112 ? 126.573 173.521 104.786 1.00 54.28  ? 70   LEU A C   1 
ATOM   241   O  O   . LEU A 1 112 ? 126.959 174.654 104.483 1.00 64.63  ? 70   LEU A O   1 
ATOM   242   C  CB  . LEU A 1 112 ? 128.703 172.603 105.732 1.00 49.67  ? 70   LEU A CB  1 
ATOM   243   C  CG  . LEU A 1 112 ? 129.969 171.774 105.514 1.00 50.21  ? 70   LEU A CG  1 
ATOM   244   C  CD1 . LEU A 1 112 ? 131.059 172.198 106.482 1.00 54.92  ? 70   LEU A CD1 1 
ATOM   245   C  CD2 . LEU A 1 112 ? 129.666 170.295 105.663 1.00 50.34  ? 70   LEU A CD2 1 
ATOM   246   N  N   . GLY A 1 113 ? 125.326 173.251 105.158 1.00 34.16  ? 71   GLY A N   1 
ATOM   247   C  CA  . GLY A 1 113 ? 124.350 174.305 105.333 1.00 37.05  ? 71   GLY A CA  1 
ATOM   248   C  C   . GLY A 1 113 ? 123.373 174.502 104.198 1.00 41.09  ? 71   GLY A C   1 
ATOM   249   O  O   . GLY A 1 113 ? 122.814 175.597 104.070 1.00 46.23  ? 71   GLY A O   1 
ATOM   250   N  N   . VAL A 1 114 ? 123.147 173.489 103.368 1.00 35.14  ? 72   VAL A N   1 
ATOM   251   C  CA  . VAL A 1 114 ? 122.146 173.587 102.308 1.00 35.89  ? 72   VAL A CA  1 
ATOM   252   C  C   . VAL A 1 114 ? 120.763 173.371 102.914 1.00 34.59  ? 72   VAL A C   1 
ATOM   253   O  O   . VAL A 1 114 ? 120.513 172.332 103.542 1.00 38.33  ? 72   VAL A O   1 
ATOM   254   C  CB  . VAL A 1 114 ? 122.439 172.598 101.168 1.00 34.18  ? 72   VAL A CB  1 
ATOM   255   C  CG1 . VAL A 1 114 ? 122.676 171.205 101.708 1.00 31.55  ? 72   VAL A CG1 1 
ATOM   256   C  CG2 . VAL A 1 114 ? 121.294 172.591 100.171 1.00 35.87  ? 72   VAL A CG2 1 
ATOM   257   N  N   . PRO A 1 115 ? 119.847 174.325 102.774 1.00 36.15  ? 73   PRO A N   1 
ATOM   258   C  CA  . PRO A 1 115 ? 118.527 174.178 103.393 1.00 35.21  ? 73   PRO A CA  1 
ATOM   259   C  C   . PRO A 1 115 ? 117.685 173.127 102.690 1.00 40.80  ? 73   PRO A C   1 
ATOM   260   O  O   . PRO A 1 115 ? 117.882 172.809 101.515 1.00 46.39  ? 73   PRO A O   1 
ATOM   261   C  CB  . PRO A 1 115 ? 117.912 175.572 103.241 1.00 38.04  ? 73   PRO A CB  1 
ATOM   262   C  CG  . PRO A 1 115 ? 118.556 176.117 102.016 1.00 40.92  ? 73   PRO A CG  1 
ATOM   263   C  CD  . PRO A 1 115 ? 119.964 175.580 102.013 1.00 43.63  ? 73   PRO A CD  1 
ATOM   264   N  N   . TYR A 1 116 ? 116.725 172.583 103.439 1.00 40.18  ? 74   TYR A N   1 
ATOM   265   C  CA  . TYR A 1 116 ? 115.784 171.618 102.893 1.00 39.17  ? 74   TYR A CA  1 
ATOM   266   C  C   . TYR A 1 116 ? 114.328 171.992 103.123 1.00 42.26  ? 74   TYR A C   1 
ATOM   267   O  O   . TYR A 1 116 ? 113.443 171.278 102.641 1.00 51.05  ? 74   TYR A O   1 
ATOM   268   C  CB  . TYR A 1 116 ? 116.047 170.218 103.471 1.00 36.46  ? 74   TYR A CB  1 
ATOM   269   C  CG  . TYR A 1 116 ? 115.859 170.106 104.967 1.00 38.47  ? 74   TYR A CG  1 
ATOM   270   C  CD1 . TYR A 1 116 ? 114.626 169.773 105.510 1.00 39.40  ? 74   TYR A CD1 1 
ATOM   271   C  CD2 . TYR A 1 116 ? 116.918 170.318 105.836 1.00 37.50  ? 74   TYR A CD2 1 
ATOM   272   C  CE1 . TYR A 1 116 ? 114.453 169.666 106.874 1.00 41.79  ? 74   TYR A CE1 1 
ATOM   273   C  CE2 . TYR A 1 116 ? 116.753 170.211 107.201 1.00 35.00  ? 74   TYR A CE2 1 
ATOM   274   C  CZ  . TYR A 1 116 ? 115.519 169.886 107.714 1.00 41.26  ? 74   TYR A CZ  1 
ATOM   275   O  OH  . TYR A 1 116 ? 115.351 169.780 109.074 1.00 49.80  ? 74   TYR A OH  1 
ATOM   276   N  N   . ALA A 1 117 ? 114.050 173.084 103.832 1.00 41.05  ? 75   ALA A N   1 
ATOM   277   C  CA  . ALA A 1 117 ? 112.678 173.514 104.059 1.00 48.32  ? 75   ALA A CA  1 
ATOM   278   C  C   . ALA A 1 117 ? 112.677 174.994 104.407 1.00 48.89  ? 75   ALA A C   1 
ATOM   279   O  O   . ALA A 1 117 ? 113.700 175.558 104.803 1.00 49.30  ? 75   ALA A O   1 
ATOM   280   C  CB  . ALA A 1 117 ? 112.006 172.696 105.166 1.00 46.22  ? 75   ALA A CB  1 
ATOM   281   N  N   . THR A 1 118 ? 111.512 175.616 104.248 1.00 57.46  ? 76   THR A N   1 
ATOM   282   C  CA  . THR A 1 118 ? 111.376 177.028 104.573 1.00 57.03  ? 76   THR A CA  1 
ATOM   283   C  C   . THR A 1 118 ? 111.542 177.241 106.075 1.00 55.62  ? 76   THR A C   1 
ATOM   284   O  O   . THR A 1 118 ? 111.097 176.411 106.874 1.00 59.18  ? 76   THR A O   1 
ATOM   285   C  CB  . THR A 1 118 ? 110.017 177.562 104.122 1.00 60.76  ? 76   THR A CB  1 
ATOM   286   O  OG1 . THR A 1 118 ? 108.978 176.699 104.600 1.00 65.54  ? 76   THR A OG1 1 
ATOM   287   C  CG2 . THR A 1 118 ? 109.952 177.650 102.607 1.00 56.44  ? 76   THR A CG2 1 
ATOM   288   N  N   . PRO A 1 119 ? 112.177 178.333 106.488 1.00 52.64  ? 77   PRO A N   1 
ATOM   289   C  CA  . PRO A 1 119 ? 112.389 178.579 107.917 1.00 57.80  ? 77   PRO A CA  1 
ATOM   290   C  C   . PRO A 1 119 ? 111.072 178.795 108.637 1.00 61.25  ? 77   PRO A C   1 
ATOM   291   O  O   . PRO A 1 119 ? 110.310 179.713 108.298 1.00 64.47  ? 77   PRO A O   1 
ATOM   292   C  CB  . PRO A 1 119 ? 113.247 179.855 107.932 1.00 62.74  ? 77   PRO A CB  1 
ATOM   293   C  CG  . PRO A 1 119 ? 113.843 179.937 106.565 1.00 58.35  ? 77   PRO A CG  1 
ATOM   294   C  CD  . PRO A 1 119 ? 112.814 179.361 105.651 1.00 56.38  ? 77   PRO A CD  1 
ATOM   295   N  N   . PRO A 1 120 ? 110.766 177.972 109.641 1.00 60.17  ? 78   PRO A N   1 
ATOM   296   C  CA  . PRO A 1 120 ? 109.525 178.143 110.423 1.00 61.70  ? 78   PRO A CA  1 
ATOM   297   C  C   . PRO A 1 120 ? 109.685 179.190 111.519 1.00 64.29  ? 78   PRO A C   1 
ATOM   298   O  O   . PRO A 1 120 ? 109.789 178.896 112.715 1.00 65.62  ? 78   PRO A O   1 
ATOM   299   C  CB  . PRO A 1 120 ? 109.293 176.734 110.974 1.00 56.93  ? 78   PRO A CB  1 
ATOM   300   C  CG  . PRO A 1 120 ? 110.674 176.191 111.162 1.00 54.24  ? 78   PRO A CG  1 
ATOM   301   C  CD  . PRO A 1 120 ? 111.544 176.803 110.088 1.00 54.56  ? 78   PRO A CD  1 
ATOM   302   N  N   . LEU A 1 121 ? 109.705 180.458 111.109 1.00 67.33  ? 79   LEU A N   1 
ATOM   303   C  CA  . LEU A 1 121 ? 110.003 181.554 112.026 1.00 66.76  ? 79   LEU A CA  1 
ATOM   304   C  C   . LEU A 1 121 ? 108.741 182.163 112.633 1.00 68.87  ? 79   LEU A C   1 
ATOM   305   O  O   . LEU A 1 121 ? 108.572 182.166 113.856 1.00 68.36  ? 79   LEU A O   1 
ATOM   306   C  CB  . LEU A 1 121 ? 110.819 182.630 111.301 1.00 66.52  ? 79   LEU A CB  1 
ATOM   307   C  CG  . LEU A 1 121 ? 112.332 182.418 111.250 1.00 66.99  ? 79   LEU A CG  1 
ATOM   308   C  CD1 . LEU A 1 121 ? 112.893 182.887 109.919 1.00 63.80  ? 79   LEU A CD1 1 
ATOM   309   C  CD2 . LEU A 1 121 ? 113.009 183.139 112.403 1.00 71.07  ? 79   LEU A CD2 1 
ATOM   310   N  N   . GLY A 1 122 ? 107.849 182.681 111.792 1.00 80.74  ? 80   GLY A N   1 
ATOM   311   C  CA  . GLY A 1 122 ? 106.697 183.412 112.284 1.00 81.66  ? 80   GLY A CA  1 
ATOM   312   C  C   . GLY A 1 122 ? 105.442 182.577 112.418 1.00 81.24  ? 80   GLY A C   1 
ATOM   313   O  O   . GLY A 1 122 ? 105.365 181.694 113.276 1.00 80.08  ? 80   GLY A O   1 
ATOM   314   N  N   . ALA A 1 123 ? 104.445 182.853 111.575 1.00 87.40  ? 81   ALA A N   1 
ATOM   315   C  CA  . ALA A 1 123 ? 103.200 182.095 111.605 1.00 88.58  ? 81   ALA A CA  1 
ATOM   316   C  C   . ALA A 1 123 ? 103.380 180.654 111.153 1.00 87.57  ? 81   ALA A C   1 
ATOM   317   O  O   . ALA A 1 123 ? 102.483 179.835 111.379 1.00 85.13  ? 81   ALA A O   1 
ATOM   318   C  CB  . ALA A 1 123 ? 102.145 182.781 110.736 1.00 89.54  ? 81   ALA A CB  1 
ATOM   319   N  N   . ARG A 1 124 ? 104.510 180.326 110.527 1.00 77.98  ? 82   ARG A N   1 
ATOM   320   C  CA  . ARG A 1 124 ? 104.806 178.954 110.141 1.00 77.36  ? 82   ARG A CA  1 
ATOM   321   C  C   . ARG A 1 124 ? 105.298 178.111 111.310 1.00 75.65  ? 82   ARG A C   1 
ATOM   322   O  O   . ARG A 1 124 ? 105.474 176.899 111.147 1.00 72.95  ? 82   ARG A O   1 
ATOM   323   C  CB  . ARG A 1 124 ? 105.842 178.942 109.015 1.00 74.36  ? 82   ARG A CB  1 
ATOM   324   C  CG  . ARG A 1 124 ? 105.869 180.227 108.203 1.00 72.42  ? 82   ARG A CG  1 
ATOM   325   C  CD  . ARG A 1 124 ? 107.027 180.251 107.222 1.00 71.35  ? 82   ARG A CD  1 
ATOM   326   N  NE  . ARG A 1 124 ? 106.902 179.215 106.205 1.00 75.27  ? 82   ARG A NE  1 
ATOM   327   C  CZ  . ARG A 1 124 ? 106.542 179.440 104.949 1.00 75.56  ? 82   ARG A CZ  1 
ATOM   328   N  NH1 . ARG A 1 124 ? 106.253 180.658 104.521 1.00 74.38  ? 82   ARG A NH1 1 
ATOM   329   N  NH2 . ARG A 1 124 ? 106.471 178.419 104.101 1.00 73.82  ? 82   ARG A NH2 1 
ATOM   330   N  N   . ARG A 1 125 ? 105.533 178.723 112.469 1.00 73.40  ? 83   ARG A N   1 
ATOM   331   C  CA  . ARG A 1 125 ? 105.883 177.968 113.663 1.00 70.29  ? 83   ARG A CA  1 
ATOM   332   C  C   . ARG A 1 125 ? 104.730 177.056 114.060 1.00 73.30  ? 83   ARG A C   1 
ATOM   333   O  O   . ARG A 1 125 ? 103.558 177.416 113.921 1.00 79.49  ? 83   ARG A O   1 
ATOM   334   C  CB  . ARG A 1 125 ? 106.228 178.928 114.805 1.00 68.01  ? 83   ARG A CB  1 
ATOM   335   C  CG  . ARG A 1 125 ? 106.286 178.292 116.184 1.00 70.50  ? 83   ARG A CG  1 
ATOM   336   C  CD  . ARG A 1 125 ? 106.454 179.340 117.270 1.00 69.43  ? 83   ARG A CD  1 
ATOM   337   N  NE  . ARG A 1 125 ? 107.706 180.075 117.133 1.00 71.16  ? 83   ARG A NE  1 
ATOM   338   C  CZ  . ARG A 1 125 ? 108.118 181.013 117.975 1.00 70.56  ? 83   ARG A CZ  1 
ATOM   339   N  NH1 . ARG A 1 125 ? 107.400 181.358 119.030 1.00 72.51  ? 83   ARG A NH1 1 
ATOM   340   N  NH2 . ARG A 1 125 ? 109.280 181.620 117.751 1.00 70.18  ? 83   ARG A NH2 1 
ATOM   341   N  N   . PHE A 1 126 ? 105.072 175.861 114.547 1.00 59.44  ? 84   PHE A N   1 
ATOM   342   C  CA  . PHE A 1 126 ? 104.093 174.836 114.916 1.00 54.51  ? 84   PHE A CA  1 
ATOM   343   C  C   . PHE A 1 126 ? 103.239 174.417 113.723 1.00 56.72  ? 84   PHE A C   1 
ATOM   344   O  O   . PHE A 1 126 ? 102.054 174.110 113.869 1.00 58.97  ? 84   PHE A O   1 
ATOM   345   C  CB  . PHE A 1 126 ? 103.203 175.297 116.076 1.00 54.66  ? 84   PHE A CB  1 
ATOM   346   C  CG  . PHE A 1 126 ? 103.951 175.542 117.354 1.00 57.71  ? 84   PHE A CG  1 
ATOM   347   C  CD1 . PHE A 1 126 ? 105.106 174.838 117.643 1.00 56.54  ? 84   PHE A CD1 1 
ATOM   348   C  CD2 . PHE A 1 126 ? 103.498 176.478 118.268 1.00 60.71  ? 84   PHE A CD2 1 
ATOM   349   C  CE1 . PHE A 1 126 ? 105.794 175.064 118.818 1.00 60.02  ? 84   PHE A CE1 1 
ATOM   350   C  CE2 . PHE A 1 126 ? 104.183 176.707 119.444 1.00 57.41  ? 84   PHE A CE2 1 
ATOM   351   C  CZ  . PHE A 1 126 ? 105.332 175.999 119.719 1.00 58.38  ? 84   PHE A CZ  1 
ATOM   352   N  N   . GLN A 1 127 ? 103.837 174.404 112.536 1.00 62.24  ? 85   GLN A N   1 
ATOM   353   C  CA  . GLN A 1 127 ? 103.201 173.943 111.315 1.00 65.38  ? 85   GLN A CA  1 
ATOM   354   C  C   . GLN A 1 127 ? 104.143 173.005 110.577 1.00 65.38  ? 85   GLN A C   1 
ATOM   355   O  O   . GLN A 1 127 ? 105.365 173.115 110.715 1.00 67.50  ? 85   GLN A O   1 
ATOM   356   C  CB  . GLN A 1 127 ? 102.823 175.118 110.401 1.00 67.48  ? 85   GLN A CB  1 
ATOM   357   C  CG  . GLN A 1 127 ? 101.861 176.114 111.026 1.00 68.58  ? 85   GLN A CG  1 
ATOM   358   C  CD  . GLN A 1 127 ? 100.441 175.589 111.093 1.00 68.65  ? 85   GLN A CD  1 
ATOM   359   O  OE1 . GLN A 1 127 ? 99.663  175.979 111.964 1.00 69.21  ? 85   GLN A OE1 1 
ATOM   360   N  NE2 . GLN A 1 127 ? 100.094 174.701 110.169 1.00 66.65  ? 85   GLN A NE2 1 
ATOM   361   N  N   . PRO A 1 128 ? 103.606 172.066 109.800 1.00 64.54  ? 86   PRO A N   1 
ATOM   362   C  CA  . PRO A 1 128 ? 104.471 171.162 109.051 1.00 63.02  ? 86   PRO A CA  1 
ATOM   363   C  C   . PRO A 1 128 ? 105.331 171.934 108.070 1.00 64.30  ? 86   PRO A C   1 
ATOM   364   O  O   . PRO A 1 128 ? 104.901 172.962 107.515 1.00 70.78  ? 86   PRO A O   1 
ATOM   365   C  CB  . PRO A 1 128 ? 103.480 170.237 108.329 1.00 65.51  ? 86   PRO A CB  1 
ATOM   366   C  CG  . PRO A 1 128 ? 102.172 170.949 108.370 1.00 65.50  ? 86   PRO A CG  1 
ATOM   367   C  CD  . PRO A 1 128 ? 102.182 171.729 109.639 1.00 66.39  ? 86   PRO A CD  1 
ATOM   368   N  N   . PRO A 1 129 ? 106.557 171.478 107.831 1.00 52.94  ? 87   PRO A N   1 
ATOM   369   C  CA  . PRO A 1 129 ? 107.459 172.215 106.941 1.00 59.84  ? 87   PRO A CA  1 
ATOM   370   C  C   . PRO A 1 129 ? 107.014 172.140 105.489 1.00 60.92  ? 87   PRO A C   1 
ATOM   371   O  O   . PRO A 1 129 ? 106.296 171.231 105.068 1.00 61.08  ? 87   PRO A O   1 
ATOM   372   C  CB  . PRO A 1 129 ? 108.803 171.509 107.143 1.00 56.56  ? 87   PRO A CB  1 
ATOM   373   C  CG  . PRO A 1 129 ? 108.420 170.119 107.505 1.00 55.21  ? 87   PRO A CG  1 
ATOM   374   C  CD  . PRO A 1 129 ? 107.182 170.251 108.350 1.00 50.73  ? 87   PRO A CD  1 
ATOM   375   N  N   . GLU A 1 130 ? 107.460 173.129 104.719 1.00 62.56  ? 88   GLU A N   1 
ATOM   376   C  CA  . GLU A 1 130 ? 107.176 173.219 103.297 1.00 63.30  ? 88   GLU A CA  1 
ATOM   377   C  C   . GLU A 1 130 ? 108.481 173.273 102.514 1.00 64.29  ? 88   GLU A C   1 
ATOM   378   O  O   . GLU A 1 130 ? 109.551 173.543 103.066 1.00 67.23  ? 88   GLU A O   1 
ATOM   379   C  CB  . GLU A 1 130 ? 106.317 174.449 102.977 1.00 65.79  ? 88   GLU A CB  1 
ATOM   380   C  CG  . GLU A 1 130 ? 105.408 174.882 104.116 1.00 67.49  ? 88   GLU A CG  1 
ATOM   381   C  CD  . GLU A 1 130 ? 104.487 176.021 103.727 1.00 71.53  ? 88   GLU A CD  1 
ATOM   382   O  OE1 . GLU A 1 130 ? 104.630 176.544 102.602 1.00 69.73  ? 88   GLU A OE1 1 
ATOM   383   O  OE2 . GLU A 1 130 ? 103.622 176.393 104.547 1.00 73.98  ? 88   GLU A OE2 1 
ATOM   384   N  N   . ALA A 1 131 ? 108.378 173.012 101.213 1.00 66.56  ? 89   ALA A N   1 
ATOM   385   C  CA  . ALA A 1 131 ? 109.552 172.992 100.356 1.00 65.23  ? 89   ALA A CA  1 
ATOM   386   C  C   . ALA A 1 131 ? 110.199 174.377 100.313 1.00 69.33  ? 89   ALA A C   1 
ATOM   387   O  O   . ALA A 1 131 ? 109.510 175.394 100.425 1.00 73.31  ? 89   ALA A O   1 
ATOM   388   C  CB  . ALA A 1 131 ? 109.172 172.543 98.947  1.00 66.63  ? 89   ALA A CB  1 
ATOM   389   N  N   . PRO A 1 132 ? 111.526 174.447 100.145 1.00 65.58  ? 90   PRO A N   1 
ATOM   390   C  CA  . PRO A 1 132 ? 112.208 175.748 100.204 1.00 64.14  ? 90   PRO A CA  1 
ATOM   391   C  C   . PRO A 1 132 ? 111.894 176.640 99.016  1.00 70.52  ? 90   PRO A C   1 
ATOM   392   O  O   . PRO A 1 132 ? 111.121 176.267 98.127  1.00 71.97  ? 90   PRO A O   1 
ATOM   393   C  CB  . PRO A 1 132 ? 113.698 175.372 100.233 1.00 62.21  ? 90   PRO A CB  1 
ATOM   394   C  CG  . PRO A 1 132 ? 113.748 173.887 100.400 1.00 63.46  ? 90   PRO A CG  1 
ATOM   395   C  CD  . PRO A 1 132 ? 112.466 173.350 99.873  1.00 64.20  ? 90   PRO A CD  1 
ATOM   396   N  N   . ALA A 1 133 ? 112.497 177.824 98.993  1.00 75.62  ? 91   ALA A N   1 
ATOM   397   C  CA  . ALA A 1 133 ? 112.302 178.794 97.926  1.00 73.77  ? 91   ALA A CA  1 
ATOM   398   C  C   . ALA A 1 133 ? 113.541 178.827 97.044  1.00 76.07  ? 91   ALA A C   1 
ATOM   399   O  O   . ALA A 1 133 ? 114.667 178.857 97.551  1.00 76.45  ? 91   ALA A O   1 
ATOM   400   C  CB  . ALA A 1 133 ? 112.017 180.185 98.494  1.00 73.76  ? 91   ALA A CB  1 
ATOM   401   N  N   . SER A 1 134 ? 113.330 178.813 95.731  1.00 91.38  ? 92   SER A N   1 
ATOM   402   C  CA  . SER A 1 134 ? 114.443 178.869 94.796  1.00 91.00  ? 92   SER A CA  1 
ATOM   403   C  C   . SER A 1 134 ? 115.170 180.202 94.916  1.00 91.12  ? 92   SER A C   1 
ATOM   404   O  O   . SER A 1 134 ? 114.573 181.238 95.220  1.00 90.98  ? 92   SER A O   1 
ATOM   405   C  CB  . SER A 1 134 ? 113.948 178.667 93.364  1.00 90.86  ? 92   SER A CB  1 
ATOM   406   O  OG  . SER A 1 134 ? 113.145 177.504 93.261  1.00 89.12  ? 92   SER A OG  1 
ATOM   407   N  N   . TRP A 1 135 ? 116.478 180.170 94.675  1.00 100.64 ? 93   TRP A N   1 
ATOM   408   C  CA  . TRP A 1 135 ? 117.293 181.365 94.783  1.00 101.76 ? 93   TRP A CA  1 
ATOM   409   C  C   . TRP A 1 135 ? 118.024 181.618 93.472  1.00 103.44 ? 93   TRP A C   1 
ATOM   410   O  O   . TRP A 1 135 ? 118.472 180.671 92.814  1.00 101.56 ? 93   TRP A O   1 
ATOM   411   C  CB  . TRP A 1 135 ? 118.311 181.237 95.927  1.00 102.47 ? 93   TRP A CB  1 
ATOM   412   C  CG  . TRP A 1 135 ? 119.157 180.003 95.848  1.00 102.15 ? 93   TRP A CG  1 
ATOM   413   C  CD1 . TRP A 1 135 ? 120.288 179.830 95.105  1.00 100.98 ? 93   TRP A CD1 1 
ATOM   414   C  CD2 . TRP A 1 135 ? 118.939 178.768 96.540  1.00 102.53 ? 93   TRP A CD2 1 
ATOM   415   N  NE1 . TRP A 1 135 ? 120.787 178.564 95.290  1.00 102.16 ? 93   TRP A NE1 1 
ATOM   416   C  CE2 . TRP A 1 135 ? 119.977 177.892 96.167  1.00 103.53 ? 93   TRP A CE2 1 
ATOM   417   C  CE3 . TRP A 1 135 ? 117.967 178.318 97.439  1.00 101.10 ? 93   TRP A CE3 1 
ATOM   418   C  CZ2 . TRP A 1 135 ? 120.071 176.593 96.661  1.00 103.58 ? 93   TRP A CZ2 1 
ATOM   419   C  CZ3 . TRP A 1 135 ? 118.062 177.029 97.927  1.00 101.02 ? 93   TRP A CZ3 1 
ATOM   420   C  CH2 . TRP A 1 135 ? 119.106 176.182 97.538  1.00 102.40 ? 93   TRP A CH2 1 
ATOM   421   N  N   . PRO A 1 136 ? 118.152 182.876 93.065  1.00 118.74 ? 94   PRO A N   1 
ATOM   422   C  CA  . PRO A 1 136 ? 118.922 183.189 91.861  1.00 118.12 ? 94   PRO A CA  1 
ATOM   423   C  C   . PRO A 1 136 ? 120.419 183.126 92.123  1.00 117.84 ? 94   PRO A C   1 
ATOM   424   O  O   . PRO A 1 136 ? 120.892 183.265 93.252  1.00 117.99 ? 94   PRO A O   1 
ATOM   425   C  CB  . PRO A 1 136 ? 118.479 184.615 91.524  1.00 118.00 ? 94   PRO A CB  1 
ATOM   426   C  CG  . PRO A 1 136 ? 118.143 185.210 92.850  1.00 118.84 ? 94   PRO A CG  1 
ATOM   427   C  CD  . PRO A 1 136 ? 117.602 184.086 93.703  1.00 117.80 ? 94   PRO A CD  1 
ATOM   428   N  N   . GLY A 1 137 ? 121.164 182.917 91.042  1.00 105.44 ? 95   GLY A N   1 
ATOM   429   C  CA  . GLY A 1 137 ? 122.612 182.879 91.152  1.00 104.66 ? 95   GLY A CA  1 
ATOM   430   C  C   . GLY A 1 137 ? 123.095 181.633 91.868  1.00 104.73 ? 95   GLY A C   1 
ATOM   431   O  O   . GLY A 1 137 ? 122.555 180.534 91.699  1.00 104.10 ? 95   GLY A O   1 
ATOM   432   N  N   . VAL A 1 138 ? 124.134 181.807 92.686  1.00 89.74  ? 96   VAL A N   1 
ATOM   433   C  CA  . VAL A 1 138 ? 124.806 180.706 93.359  1.00 86.51  ? 96   VAL A CA  1 
ATOM   434   C  C   . VAL A 1 138 ? 124.935 181.032 94.843  1.00 90.27  ? 96   VAL A C   1 
ATOM   435   O  O   . VAL A 1 138 ? 124.868 182.191 95.259  1.00 91.40  ? 96   VAL A O   1 
ATOM   436   C  CB  . VAL A 1 138 ? 126.191 180.419 92.737  1.00 84.66  ? 96   VAL A CB  1 
ATOM   437   C  CG1 . VAL A 1 138 ? 127.209 181.421 93.237  1.00 87.73  ? 96   VAL A CG1 1 
ATOM   438   C  CG2 . VAL A 1 138 ? 126.638 178.992 93.027  1.00 83.84  ? 96   VAL A CG2 1 
ATOM   439   N  N   . ARG A 1 139 ? 125.103 179.982 95.643  1.00 86.13  ? 97   ARG A N   1 
ATOM   440   C  CA  . ARG A 1 139 ? 125.190 180.082 97.094  1.00 81.92  ? 97   ARG A CA  1 
ATOM   441   C  C   . ARG A 1 139 ? 126.292 179.161 97.598  1.00 79.64  ? 97   ARG A C   1 
ATOM   442   O  O   . ARG A 1 139 ? 126.223 177.951 97.378  1.00 78.89  ? 97   ARG A O   1 
ATOM   443   C  CB  . ARG A 1 139 ? 123.845 179.690 97.715  1.00 79.58  ? 97   ARG A CB  1 
ATOM   444   C  CG  . ARG A 1 139 ? 123.759 179.703 99.229  1.00 82.19  ? 97   ARG A CG  1 
ATOM   445   C  CD  . ARG A 1 139 ? 122.663 178.732 99.670  1.00 83.05  ? 97   ARG A CD  1 
ATOM   446   N  NE  . ARG A 1 139 ? 121.798 179.269 100.713 1.00 81.48  ? 97   ARG A NE  1 
ATOM   447   C  CZ  . ARG A 1 139 ? 122.023 179.144 102.014 1.00 80.43  ? 97   ARG A CZ  1 
ATOM   448   N  NH1 . ARG A 1 139 ? 123.083 178.499 102.472 1.00 80.11  ? 97   ARG A NH1 1 
ATOM   449   N  NH2 . ARG A 1 139 ? 121.161 179.675 102.876 1.00 78.00  ? 97   ARG A NH2 1 
ATOM   450   N  N   . ASN A 1 140 ? 127.307 179.709 98.273  1.00 83.13  ? 98   ASN A N   1 
ATOM   451   C  CA  . ASN A 1 140 ? 128.225 178.820 98.974  1.00 85.81  ? 98   ASN A CA  1 
ATOM   452   C  C   . ASN A 1 140 ? 127.528 178.168 100.159 1.00 88.62  ? 98   ASN A C   1 
ATOM   453   O  O   . ASN A 1 140 ? 126.629 178.750 100.776 1.00 86.97  ? 98   ASN A O   1 
ATOM   454   C  CB  . ASN A 1 140 ? 129.548 179.493 99.414  1.00 84.02  ? 98   ASN A CB  1 
ATOM   455   C  CG  . ASN A 1 140 ? 129.442 180.310 100.723 1.00 85.62  ? 98   ASN A CG  1 
ATOM   456   O  OD1 . ASN A 1 140 ? 128.793 179.917 101.685 1.00 87.82  ? 98   ASN A OD1 1 
ATOM   457   N  ND2 . ASN A 1 140 ? 130.203 181.403 100.793 1.00 87.77  ? 98   ASN A ND2 1 
ATOM   458   N  N   . ALA A 1 141 ? 127.926 176.930 100.445 1.00 73.55  ? 99   ALA A N   1 
ATOM   459   C  CA  . ALA A 1 141 ? 127.542 176.214 101.656 1.00 66.00  ? 99   ALA A CA  1 
ATOM   460   C  C   . ALA A 1 141 ? 128.846 175.754 102.300 1.00 67.58  ? 99   ALA A C   1 
ATOM   461   O  O   . ALA A 1 141 ? 129.280 174.617 102.100 1.00 67.61  ? 99   ALA A O   1 
ATOM   462   C  CB  . ALA A 1 141 ? 126.608 175.052 101.343 1.00 67.41  ? 99   ALA A CB  1 
ATOM   463   N  N   . THR A 1 142 ? 129.469 176.641 103.075 1.00 74.22  ? 100  THR A N   1 
ATOM   464   C  CA  . THR A 1 142 ? 130.782 176.378 103.650 1.00 76.89  ? 100  THR A CA  1 
ATOM   465   C  C   . THR A 1 142 ? 130.844 176.518 105.163 1.00 77.40  ? 100  THR A C   1 
ATOM   466   O  O   . THR A 1 142 ? 131.694 175.867 105.783 1.00 76.10  ? 100  THR A O   1 
ATOM   467   C  CB  . THR A 1 142 ? 131.834 177.314 103.036 1.00 77.29  ? 100  THR A CB  1 
ATOM   468   O  OG1 . THR A 1 142 ? 131.290 178.634 102.919 1.00 76.81  ? 100  THR A OG1 1 
ATOM   469   C  CG2 . THR A 1 142 ? 132.244 176.822 101.659 1.00 76.42  ? 100  THR A CG2 1 
ATOM   470   N  N   . THR A 1 143 ? 129.991 177.331 105.776 1.00 73.66  ? 101  THR A N   1 
ATOM   471   C  CA  . THR A 1 143 ? 129.953 177.474 107.223 1.00 72.26  ? 101  THR A CA  1 
ATOM   472   C  C   . THR A 1 143 ? 128.868 176.571 107.792 1.00 70.83  ? 101  THR A C   1 
ATOM   473   O  O   . THR A 1 143 ? 127.822 176.373 107.168 1.00 73.47  ? 101  THR A O   1 
ATOM   474   C  CB  . THR A 1 143 ? 129.692 178.926 107.630 1.00 71.96  ? 101  THR A CB  1 
ATOM   475   O  OG1 . THR A 1 143 ? 128.397 179.330 107.168 1.00 72.43  ? 101  THR A OG1 1 
ATOM   476   C  CG2 . THR A 1 143 ? 130.747 179.844 107.033 1.00 69.85  ? 101  THR A CG2 1 
ATOM   477   N  N   . LEU A 1 144 ? 129.128 176.020 108.971 1.00 61.43  ? 102  LEU A N   1 
ATOM   478   C  CA  . LEU A 1 144 ? 128.172 175.116 109.592 1.00 58.67  ? 102  LEU A CA  1 
ATOM   479   C  C   . LEU A 1 144 ? 126.879 175.862 109.906 1.00 60.25  ? 102  LEU A C   1 
ATOM   480   O  O   . LEU A 1 144 ? 126.926 176.969 110.460 1.00 61.22  ? 102  LEU A O   1 
ATOM   481   C  CB  . LEU A 1 144 ? 128.757 174.508 110.865 1.00 58.75  ? 102  LEU A CB  1 
ATOM   482   C  CG  . LEU A 1 144 ? 129.953 173.578 110.659 1.00 58.79  ? 102  LEU A CG  1 
ATOM   483   C  CD1 . LEU A 1 144 ? 130.627 173.267 111.985 1.00 61.04  ? 102  LEU A CD1 1 
ATOM   484   C  CD2 . LEU A 1 144 ? 129.521 172.300 109.960 1.00 56.65  ? 102  LEU A CD2 1 
ATOM   485   N  N   . PRO A 1 145 ? 125.721 175.306 109.567 1.00 53.39  ? 103  PRO A N   1 
ATOM   486   C  CA  . PRO A 1 145 ? 124.458 176.017 109.777 1.00 54.20  ? 103  PRO A CA  1 
ATOM   487   C  C   . PRO A 1 145 ? 124.144 176.159 111.254 1.00 54.65  ? 103  PRO A C   1 
ATOM   488   O  O   . PRO A 1 145 ? 124.632 175.374 112.082 1.00 56.37  ? 103  PRO A O   1 
ATOM   489   C  CB  . PRO A 1 145 ? 123.429 175.122 109.073 1.00 50.67  ? 103  PRO A CB  1 
ATOM   490   C  CG  . PRO A 1 145 ? 124.050 173.772 109.060 1.00 52.79  ? 103  PRO A CG  1 
ATOM   491   C  CD  . PRO A 1 145 ? 125.522 174.000 108.917 1.00 50.69  ? 103  PRO A CD  1 
ATOM   492   N  N   . PRO A 1 146 ? 123.343 177.157 111.626 1.00 56.00  ? 104  PRO A N   1 
ATOM   493   C  CA  . PRO A 1 146 ? 122.962 177.310 113.033 1.00 55.03  ? 104  PRO A CA  1 
ATOM   494   C  C   . PRO A 1 146 ? 122.124 176.136 113.517 1.00 57.84  ? 104  PRO A C   1 
ATOM   495   O  O   . PRO A 1 146 ? 121.392 175.506 112.751 1.00 58.75  ? 104  PRO A O   1 
ATOM   496   C  CB  . PRO A 1 146 ? 122.153 178.613 113.040 1.00 54.92  ? 104  PRO A CB  1 
ATOM   497   C  CG  . PRO A 1 146 ? 121.689 178.783 111.635 1.00 55.56  ? 104  PRO A CG  1 
ATOM   498   C  CD  . PRO A 1 146 ? 122.784 178.226 110.783 1.00 57.61  ? 104  PRO A CD  1 
ATOM   499   N  N   . ALA A 1 147 ? 122.242 175.847 114.808 1.00 58.46  ? 105  ALA A N   1 
ATOM   500   C  CA  . ALA A 1 147 ? 121.481 174.779 115.434 1.00 54.56  ? 105  ALA A CA  1 
ATOM   501   C  C   . ALA A 1 147 ? 120.132 175.297 115.922 1.00 57.09  ? 105  ALA A C   1 
ATOM   502   O  O   . ALA A 1 147 ? 119.916 176.502 116.068 1.00 63.92  ? 105  ALA A O   1 
ATOM   503   C  CB  . ALA A 1 147 ? 122.261 174.170 116.598 1.00 54.99  ? 105  ALA A CB  1 
ATOM   504   N  N   . CYS A 1 148 ? 119.217 174.364 116.163 1.00 56.34  ? 106  CYS A N   1 
ATOM   505   C  CA  . CYS A 1 148 ? 117.896 174.731 116.645 1.00 57.87  ? 106  CYS A CA  1 
ATOM   506   C  C   . CYS A 1 148 ? 117.976 175.213 118.093 1.00 60.14  ? 106  CYS A C   1 
ATOM   507   O  O   . CYS A 1 148 ? 118.888 174.831 118.832 1.00 64.93  ? 106  CYS A O   1 
ATOM   508   C  CB  . CYS A 1 148 ? 116.944 173.545 116.535 1.00 58.39  ? 106  CYS A CB  1 
ATOM   509   S  SG  . CYS A 1 148 ? 116.573 173.060 114.836 1.00 61.29  ? 106  CYS A SG  1 
ATOM   510   N  N   . PRO A 1 149 ? 117.044 176.067 118.518 1.00 62.47  ? 107  PRO A N   1 
ATOM   511   C  CA  . PRO A 1 149 ? 117.096 176.586 119.889 1.00 64.07  ? 107  PRO A CA  1 
ATOM   512   C  C   . PRO A 1 149 ? 117.007 175.466 120.915 1.00 65.84  ? 107  PRO A C   1 
ATOM   513   O  O   . PRO A 1 149 ? 116.254 174.504 120.751 1.00 65.27  ? 107  PRO A O   1 
ATOM   514   C  CB  . PRO A 1 149 ? 115.881 177.517 119.964 1.00 66.30  ? 107  PRO A CB  1 
ATOM   515   C  CG  . PRO A 1 149 ? 115.594 177.879 118.548 1.00 65.27  ? 107  PRO A CG  1 
ATOM   516   C  CD  . PRO A 1 149 ? 115.941 176.664 117.748 1.00 65.31  ? 107  PRO A CD  1 
ATOM   517   N  N   . GLN A 1 150 ? 117.789 175.606 121.982 1.00 69.07  ? 108  GLN A N   1 
ATOM   518   C  CA  . GLN A 1 150 ? 117.824 174.616 123.048 1.00 61.16  ? 108  GLN A CA  1 
ATOM   519   C  C   . GLN A 1 150 ? 118.444 175.252 124.281 1.00 65.74  ? 108  GLN A C   1 
ATOM   520   O  O   . GLN A 1 150 ? 119.096 176.297 124.203 1.00 71.39  ? 108  GLN A O   1 
ATOM   521   C  CB  . GLN A 1 150 ? 118.609 173.369 122.631 1.00 59.43  ? 108  GLN A CB  1 
ATOM   522   C  CG  . GLN A 1 150 ? 119.883 173.673 121.869 1.00 61.87  ? 108  GLN A CG  1 
ATOM   523   C  CD  . GLN A 1 150 ? 120.443 172.458 121.166 1.00 63.02  ? 108  GLN A CD  1 
ATOM   524   O  OE1 . GLN A 1 150 ? 121.144 171.646 121.769 1.00 63.81  ? 108  GLN A OE1 1 
ATOM   525   N  NE2 . GLN A 1 150 ? 120.137 172.324 119.882 1.00 60.34  ? 108  GLN A NE2 1 
ATOM   526   N  N   . ASN A 1 151 ? 118.232 174.606 125.423 1.00 78.03  ? 109  ASN A N   1 
ATOM   527   C  CA  . ASN A 1 151 ? 118.792 175.035 126.701 1.00 77.88  ? 109  ASN A CA  1 
ATOM   528   C  C   . ASN A 1 151 ? 119.682 173.904 127.204 1.00 79.58  ? 109  ASN A C   1 
ATOM   529   O  O   . ASN A 1 151 ? 119.232 173.024 127.940 1.00 78.70  ? 109  ASN A O   1 
ATOM   530   C  CB  . ASN A 1 151 ? 117.692 175.377 127.701 1.00 78.83  ? 109  ASN A CB  1 
ATOM   531   C  CG  . ASN A 1 151 ? 118.123 176.427 128.704 1.00 80.85  ? 109  ASN A CG  1 
ATOM   532   O  OD1 . ASN A 1 151 ? 119.094 177.151 128.484 1.00 80.57  ? 109  ASN A OD1 1 
ATOM   533   N  ND2 . ASN A 1 151 ? 117.402 176.516 129.815 1.00 81.45  ? 109  ASN A ND2 1 
ATOM   534   N  N   . LEU A 1 152 ? 120.954 173.930 126.799 1.00 80.64  ? 110  LEU A N   1 
ATOM   535   C  CA  . LEU A 1 152 ? 121.865 172.859 127.182 1.00 78.81  ? 110  LEU A CA  1 
ATOM   536   C  C   . LEU A 1 152 ? 122.276 172.965 128.644 1.00 81.36  ? 110  LEU A C   1 
ATOM   537   O  O   . LEU A 1 152 ? 122.552 171.944 129.283 1.00 81.20  ? 110  LEU A O   1 
ATOM   538   C  CB  . LEU A 1 152 ? 123.097 172.868 126.282 1.00 76.85  ? 110  LEU A CB  1 
ATOM   539   C  CG  . LEU A 1 152 ? 123.705 171.487 126.043 1.00 78.70  ? 110  LEU A CG  1 
ATOM   540   C  CD1 . LEU A 1 152 ? 122.709 170.604 125.315 1.00 76.65  ? 110  LEU A CD1 1 
ATOM   541   C  CD2 . LEU A 1 152 ? 124.995 171.598 125.258 1.00 81.20  ? 110  LEU A CD2 1 
ATOM   542   N  N   . HIS A 1 153 ? 122.324 174.176 129.189 1.00 90.16  ? 111  HIS A N   1 
ATOM   543   C  CA  . HIS A 1 153 ? 122.614 174.371 130.608 1.00 88.79  ? 111  HIS A CA  1 
ATOM   544   C  C   . HIS A 1 153 ? 121.332 174.389 131.434 1.00 87.56  ? 111  HIS A C   1 
ATOM   545   O  O   . HIS A 1 153 ? 121.074 175.307 132.211 1.00 87.96  ? 111  HIS A O   1 
ATOM   546   C  CB  . HIS A 1 153 ? 123.415 175.653 130.806 1.00 87.65  ? 111  HIS A CB  1 
ATOM   547   C  CG  . HIS A 1 153 ? 124.739 175.651 130.109 1.00 91.18  ? 111  HIS A CG  1 
ATOM   548   N  ND1 . HIS A 1 153 ? 125.773 174.817 130.477 1.00 92.61  ? 111  HIS A ND1 1 
ATOM   549   C  CD2 . HIS A 1 153 ? 125.199 176.382 129.065 1.00 89.59  ? 111  HIS A CD2 1 
ATOM   550   C  CE1 . HIS A 1 153 ? 126.812 175.034 129.690 1.00 90.41  ? 111  HIS A CE1 1 
ATOM   551   N  NE2 . HIS A 1 153 ? 126.490 175.978 128.825 1.00 90.96  ? 111  HIS A NE2 1 
ATOM   552   N  N   . GLY A 1 154 ? 120.515 173.354 131.261 1.00 79.35  ? 112  GLY A N   1 
ATOM   553   C  CA  . GLY A 1 154 ? 119.261 173.245 131.977 1.00 77.76  ? 112  GLY A CA  1 
ATOM   554   C  C   . GLY A 1 154 ? 119.053 171.873 132.580 1.00 79.72  ? 112  GLY A C   1 
ATOM   555   O  O   . GLY A 1 154 ? 120.016 171.135 132.806 1.00 80.84  ? 112  GLY A O   1 
ATOM   556   N  N   . ALA A 1 155 ? 117.800 171.518 132.845 1.00 79.66  ? 113  ALA A N   1 
ATOM   557   C  CA  . ALA A 1 155 ? 117.471 170.225 133.443 1.00 79.55  ? 113  ALA A CA  1 
ATOM   558   C  C   . ALA A 1 155 ? 117.077 169.217 132.364 1.00 78.75  ? 113  ALA A C   1 
ATOM   559   O  O   . ALA A 1 155 ? 115.950 168.725 132.306 1.00 75.53  ? 113  ALA A O   1 
ATOM   560   C  CB  . ALA A 1 155 ? 116.366 170.389 134.482 1.00 78.00  ? 113  ALA A CB  1 
ATOM   561   N  N   . LEU A 1 156 ? 118.038 168.917 131.495 1.00 68.94  ? 114  LEU A N   1 
ATOM   562   C  CA  . LEU A 1 156 ? 117.832 167.891 130.489 1.00 67.06  ? 114  LEU A CA  1 
ATOM   563   C  C   . LEU A 1 156 ? 117.776 166.515 131.152 1.00 69.23  ? 114  LEU A C   1 
ATOM   564   O  O   . LEU A 1 156 ? 118.384 166.300 132.204 1.00 68.84  ? 114  LEU A O   1 
ATOM   565   C  CB  . LEU A 1 156 ? 118.952 167.921 129.454 1.00 63.65  ? 114  LEU A CB  1 
ATOM   566   C  CG  . LEU A 1 156 ? 119.229 169.257 128.764 1.00 67.36  ? 114  LEU A CG  1 
ATOM   567   C  CD1 . LEU A 1 156 ? 120.546 169.201 128.008 1.00 64.90  ? 114  LEU A CD1 1 
ATOM   568   C  CD2 . LEU A 1 156 ? 118.089 169.623 127.829 1.00 68.74  ? 114  LEU A CD2 1 
ATOM   569   N  N   . PRO A 1 157 ? 117.049 165.564 130.558 1.00 57.69  ? 115  PRO A N   1 
ATOM   570   C  CA  . PRO A 1 157 ? 117.034 164.206 131.117 1.00 49.78  ? 115  PRO A CA  1 
ATOM   571   C  C   . PRO A 1 157 ? 118.390 163.542 130.964 1.00 49.60  ? 115  PRO A C   1 
ATOM   572   O  O   . PRO A 1 157 ? 118.788 163.172 129.856 1.00 53.14  ? 115  PRO A O   1 
ATOM   573   C  CB  . PRO A 1 157 ? 115.954 163.491 130.293 1.00 43.16  ? 115  PRO A CB  1 
ATOM   574   C  CG  . PRO A 1 157 ? 115.161 164.586 129.647 1.00 46.52  ? 115  PRO A CG  1 
ATOM   575   C  CD  . PRO A 1 157 ? 116.129 165.699 129.418 1.00 51.18  ? 115  PRO A CD  1 
ATOM   576   N  N   . ALA A 1 158 ? 119.105 163.379 132.074 1.00 40.94  ? 116  ALA A N   1 
ATOM   577   C  CA  . ALA A 1 158 ? 120.483 162.909 132.035 1.00 38.44  ? 116  ALA A CA  1 
ATOM   578   C  C   . ALA A 1 158 ? 120.601 161.394 131.987 1.00 38.08  ? 116  ALA A C   1 
ATOM   579   O  O   . ALA A 1 158 ? 121.725 160.884 131.957 1.00 38.42  ? 116  ALA A O   1 
ATOM   580   C  CB  . ALA A 1 158 ? 121.255 163.444 133.243 1.00 37.85  ? 116  ALA A CB  1 
ATOM   581   N  N   . ILE A 1 159 ? 119.490 160.666 131.986 1.00 36.54  ? 117  ILE A N   1 
ATOM   582   C  CA  . ILE A 1 159 ? 119.552 159.208 131.943 1.00 44.11  ? 117  ILE A CA  1 
ATOM   583   C  C   . ILE A 1 159 ? 119.562 158.693 130.509 1.00 47.03  ? 117  ILE A C   1 
ATOM   584   O  O   . ILE A 1 159 ? 120.319 157.777 130.178 1.00 50.33  ? 117  ILE A O   1 
ATOM   585   C  CB  . ILE A 1 159 ? 118.387 158.610 132.754 1.00 35.83  ? 117  ILE A CB  1 
ATOM   586   C  CG1 . ILE A 1 159 ? 118.569 158.922 134.240 1.00 37.53  ? 117  ILE A CG1 1 
ATOM   587   C  CG2 . ILE A 1 159 ? 118.297 157.115 132.528 1.00 35.82  ? 117  ILE A CG2 1 
ATOM   588   C  CD1 . ILE A 1 159 ? 117.883 157.948 135.169 1.00 40.97  ? 117  ILE A CD1 1 
ATOM   589   N  N   . MET A 1 160 ? 118.739 159.274 129.638 1.00 40.52  ? 118  MET A N   1 
ATOM   590   C  CA  . MET A 1 160 ? 118.673 158.845 128.248 1.00 35.73  ? 118  MET A CA  1 
ATOM   591   C  C   . MET A 1 160 ? 119.790 159.420 127.388 1.00 41.44  ? 118  MET A C   1 
ATOM   592   O  O   . MET A 1 160 ? 119.998 158.935 126.271 1.00 48.38  ? 118  MET A O   1 
ATOM   593   C  CB  . MET A 1 160 ? 117.318 159.229 127.648 1.00 41.42  ? 118  MET A CB  1 
ATOM   594   C  CG  . MET A 1 160 ? 116.925 160.675 127.883 1.00 43.57  ? 118  MET A CG  1 
ATOM   595   S  SD  . MET A 1 160 ? 115.142 160.921 127.832 1.00 44.13  ? 118  MET A SD  1 
ATOM   596   C  CE  . MET A 1 160 ? 114.751 160.175 126.253 1.00 43.81  ? 118  MET A CE  1 
ATOM   597   N  N   . LEU A 1 161 ? 120.507 160.431 127.872 1.00 35.75  ? 119  LEU A N   1 
ATOM   598   C  CA  . LEU A 1 161 ? 121.552 161.055 127.078 1.00 33.93  ? 119  LEU A CA  1 
ATOM   599   C  C   . LEU A 1 161 ? 122.769 160.138 126.965 1.00 39.32  ? 119  LEU A C   1 
ATOM   600   O  O   . LEU A 1 161 ? 123.045 159.344 127.869 1.00 43.32  ? 119  LEU A O   1 
ATOM   601   C  CB  . LEU A 1 161 ? 121.966 162.387 127.693 1.00 34.40  ? 119  LEU A CB  1 
ATOM   602   C  CG  . LEU A 1 161 ? 120.986 163.546 127.520 1.00 35.61  ? 119  LEU A CG  1 
ATOM   603   C  CD1 . LEU A 1 161 ? 121.675 164.876 127.768 1.00 41.81  ? 119  LEU A CD1 1 
ATOM   604   C  CD2 . LEU A 1 161 ? 120.368 163.510 126.140 1.00 34.22  ? 119  LEU A CD2 1 
ATOM   605   N  N   . PRO A 1 162 ? 123.511 160.226 125.863 1.00 36.00  ? 120  PRO A N   1 
ATOM   606   C  CA  . PRO A 1 162 ? 124.745 159.444 125.741 1.00 35.64  ? 120  PRO A CA  1 
ATOM   607   C  C   . PRO A 1 162 ? 125.777 159.884 126.765 1.00 38.06  ? 120  PRO A C   1 
ATOM   608   O  O   . PRO A 1 162 ? 125.790 161.031 127.215 1.00 50.10  ? 120  PRO A O   1 
ATOM   609   C  CB  . PRO A 1 162 ? 125.214 159.740 124.311 1.00 39.84  ? 120  PRO A CB  1 
ATOM   610   C  CG  . PRO A 1 162 ? 123.993 160.236 123.603 1.00 38.27  ? 120  PRO A CG  1 
ATOM   611   C  CD  . PRO A 1 162 ? 123.230 160.992 124.640 1.00 38.90  ? 120  PRO A CD  1 
ATOM   612   N  N   . VAL A 1 163 ? 126.650 158.945 127.136 1.00 29.73  ? 121  VAL A N   1 
ATOM   613   C  CA  . VAL A 1 163 ? 127.579 159.199 128.232 1.00 36.65  ? 121  VAL A CA  1 
ATOM   614   C  C   . VAL A 1 163 ? 128.598 160.270 127.850 1.00 44.41  ? 121  VAL A C   1 
ATOM   615   O  O   . VAL A 1 163 ? 128.975 161.106 128.681 1.00 48.92  ? 121  VAL A O   1 
ATOM   616   C  CB  . VAL A 1 163 ? 128.245 157.883 128.686 1.00 42.05  ? 121  VAL A CB  1 
ATOM   617   C  CG1 . VAL A 1 163 ? 129.457 157.531 127.831 1.00 44.35  ? 121  VAL A CG1 1 
ATOM   618   C  CG2 . VAL A 1 163 ? 128.631 157.968 130.156 1.00 37.48  ? 121  VAL A CG2 1 
ATOM   619   N  N   . TRP A 1 164 ? 129.043 160.286 126.589 1.00 45.39  ? 122  TRP A N   1 
ATOM   620   C  CA  . TRP A 1 164 ? 130.027 161.282 126.180 1.00 42.34  ? 122  TRP A CA  1 
ATOM   621   C  C   . TRP A 1 164 ? 129.417 162.669 126.056 1.00 40.53  ? 122  TRP A C   1 
ATOM   622   O  O   . TRP A 1 164 ? 130.146 163.663 126.146 1.00 49.30  ? 122  TRP A O   1 
ATOM   623   C  CB  . TRP A 1 164 ? 130.689 160.876 124.861 1.00 43.77  ? 122  TRP A CB  1 
ATOM   624   C  CG  . TRP A 1 164 ? 129.733 160.498 123.771 1.00 44.21  ? 122  TRP A CG  1 
ATOM   625   C  CD1 . TRP A 1 164 ? 129.416 159.237 123.367 1.00 44.35  ? 122  TRP A CD1 1 
ATOM   626   C  CD2 . TRP A 1 164 ? 128.996 161.387 122.922 1.00 40.07  ? 122  TRP A CD2 1 
ATOM   627   N  NE1 . TRP A 1 164 ? 128.513 159.282 122.334 1.00 45.46  ? 122  TRP A NE1 1 
ATOM   628   C  CE2 . TRP A 1 164 ? 128.241 160.591 122.041 1.00 41.59  ? 122  TRP A CE2 1 
ATOM   629   C  CE3 . TRP A 1 164 ? 128.897 162.778 122.825 1.00 43.90  ? 122  TRP A CE3 1 
ATOM   630   C  CZ2 . TRP A 1 164 ? 127.398 161.139 121.080 1.00 42.11  ? 122  TRP A CZ2 1 
ATOM   631   C  CZ3 . TRP A 1 164 ? 128.058 163.318 121.874 1.00 41.15  ? 122  TRP A CZ3 1 
ATOM   632   C  CH2 . TRP A 1 164 ? 127.321 162.502 121.013 1.00 40.50  ? 122  TRP A CH2 1 
ATOM   633   N  N   . PHE A 1 165 ? 128.103 162.760 125.848 1.00 41.78  ? 123  PHE A N   1 
ATOM   634   C  CA  . PHE A 1 165 ? 127.448 164.061 125.806 1.00 44.15  ? 123  PHE A CA  1 
ATOM   635   C  C   . PHE A 1 165 ? 127.437 164.706 127.185 1.00 46.34  ? 123  PHE A C   1 
ATOM   636   O  O   . PHE A 1 165 ? 127.762 165.889 127.332 1.00 57.42  ? 123  PHE A O   1 
ATOM   637   C  CB  . PHE A 1 165 ? 126.025 163.910 125.266 1.00 46.44  ? 123  PHE A CB  1 
ATOM   638   C  CG  . PHE A 1 165 ? 125.376 165.210 124.884 1.00 47.74  ? 123  PHE A CG  1 
ATOM   639   C  CD1 . PHE A 1 165 ? 124.818 166.034 125.847 1.00 45.64  ? 123  PHE A CD1 1 
ATOM   640   C  CD2 . PHE A 1 165 ? 125.317 165.604 123.560 1.00 50.56  ? 123  PHE A CD2 1 
ATOM   641   C  CE1 . PHE A 1 165 ? 124.221 167.227 125.496 1.00 49.79  ? 123  PHE A CE1 1 
ATOM   642   C  CE2 . PHE A 1 165 ? 124.720 166.795 123.204 1.00 50.79  ? 123  PHE A CE2 1 
ATOM   643   C  CZ  . PHE A 1 165 ? 124.172 167.607 124.172 1.00 51.81  ? 123  PHE A CZ  1 
ATOM   644   N  N   . THR A 1 166 ? 127.063 163.939 128.209 1.00 39.81  ? 124  THR A N   1 
ATOM   645   C  CA  . THR A 1 166 ? 126.993 164.487 129.557 1.00 43.39  ? 124  THR A CA  1 
ATOM   646   C  C   . THR A 1 166 ? 128.368 164.637 130.194 1.00 44.18  ? 124  THR A C   1 
ATOM   647   O  O   . THR A 1 166 ? 128.567 165.546 131.007 1.00 48.58  ? 124  THR A O   1 
ATOM   648   C  CB  . THR A 1 166 ? 126.098 163.612 130.435 1.00 39.51  ? 124  THR A CB  1 
ATOM   649   O  OG1 . THR A 1 166 ? 126.409 162.232 130.214 1.00 39.73  ? 124  THR A OG1 1 
ATOM   650   C  CG2 . THR A 1 166 ? 124.637 163.859 130.103 1.00 38.73  ? 124  THR A CG2 1 
ATOM   651   N  N   . ASP A 1 167 ? 129.321 163.764 129.855 1.00 45.98  ? 125  ASP A N   1 
ATOM   652   C  CA  . ASP A 1 167 ? 130.662 163.895 130.417 1.00 48.39  ? 125  ASP A CA  1 
ATOM   653   C  C   . ASP A 1 167 ? 131.331 165.182 129.949 1.00 53.09  ? 125  ASP A C   1 
ATOM   654   O  O   . ASP A 1 167 ? 131.804 165.983 130.764 1.00 57.74  ? 125  ASP A O   1 
ATOM   655   C  CB  . ASP A 1 167 ? 131.510 162.681 130.039 1.00 47.11  ? 125  ASP A CB  1 
ATOM   656   C  CG  . ASP A 1 167 ? 131.156 161.449 130.845 1.00 50.50  ? 125  ASP A CG  1 
ATOM   657   O  OD1 . ASP A 1 167 ? 130.284 161.548 131.732 1.00 53.87  ? 125  ASP A OD1 1 
ATOM   658   O  OD2 . ASP A 1 167 ? 131.750 160.381 130.589 1.00 50.64  ? 125  ASP A OD2 1 
ATOM   659   N  N   . ASN A 1 168 ? 131.380 165.396 128.639 1.00 58.71  ? 126  ASN A N   1 
ATOM   660   C  CA  . ASN A 1 168 ? 131.971 166.604 128.062 1.00 57.09  ? 126  ASN A CA  1 
ATOM   661   C  C   . ASN A 1 168 ? 130.888 167.624 127.713 1.00 60.44  ? 126  ASN A C   1 
ATOM   662   O  O   . ASN A 1 168 ? 130.723 168.030 126.564 1.00 61.77  ? 126  ASN A O   1 
ATOM   663   C  CB  . ASN A 1 168 ? 132.811 166.245 126.841 1.00 56.02  ? 126  ASN A CB  1 
ATOM   664   C  CG  . ASN A 1 168 ? 133.480 164.894 126.975 1.00 61.55  ? 126  ASN A CG  1 
ATOM   665   O  OD1 . ASN A 1 168 ? 133.991 164.545 128.039 1.00 61.63  ? 126  ASN A OD1 1 
ATOM   666   N  ND2 . ASN A 1 168 ? 133.477 164.122 125.896 1.00 63.12  ? 126  ASN A ND2 1 
ATOM   667   N  N   . LEU A 1 169 ? 130.135 168.037 128.735 1.00 60.59  ? 127  LEU A N   1 
ATOM   668   C  CA  . LEU A 1 169 ? 129.041 168.975 128.504 1.00 60.39  ? 127  LEU A CA  1 
ATOM   669   C  C   . LEU A 1 169 ? 129.550 170.358 128.120 1.00 63.28  ? 127  LEU A C   1 
ATOM   670   O  O   . LEU A 1 169 ? 128.879 171.074 127.368 1.00 65.61  ? 127  LEU A O   1 
ATOM   671   C  CB  . LEU A 1 169 ? 128.151 169.063 129.742 1.00 59.33  ? 127  LEU A CB  1 
ATOM   672   C  CG  . LEU A 1 169 ? 126.750 169.632 129.510 1.00 60.74  ? 127  LEU A CG  1 
ATOM   673   C  CD1 . LEU A 1 169 ? 126.100 168.979 128.303 1.00 59.96  ? 127  LEU A CD1 1 
ATOM   674   C  CD2 . LEU A 1 169 ? 125.886 169.454 130.747 1.00 62.30  ? 127  LEU A CD2 1 
ATOM   675   N  N   . GLU A 1 170 ? 130.722 170.755 128.621 1.00 66.57  ? 128  GLU A N   1 
ATOM   676   C  CA  . GLU A 1 170 ? 131.259 172.066 128.273 1.00 65.96  ? 128  GLU A CA  1 
ATOM   677   C  C   . GLU A 1 170 ? 131.750 172.097 126.830 1.00 65.04  ? 128  GLU A C   1 
ATOM   678   O  O   . GLU A 1 170 ? 131.593 173.109 126.138 1.00 64.20  ? 128  GLU A O   1 
ATOM   679   C  CB  . GLU A 1 170 ? 132.381 172.451 129.238 1.00 67.82  ? 128  GLU A CB  1 
ATOM   680   C  CG  . GLU A 1 170 ? 133.520 171.448 129.316 1.00 68.89  ? 128  GLU A CG  1 
ATOM   681   C  CD  . GLU A 1 170 ? 133.436 170.564 130.543 1.00 70.93  ? 128  GLU A CD  1 
ATOM   682   O  OE1 . GLU A 1 170 ? 132.460 170.701 131.310 1.00 70.79  ? 128  GLU A OE1 1 
ATOM   683   O  OE2 . GLU A 1 170 ? 134.346 169.731 130.740 1.00 71.65  ? 128  GLU A OE2 1 
ATOM   684   N  N   . ALA A 1 171 ? 132.345 171.000 126.358 1.00 70.86  ? 129  ALA A N   1 
ATOM   685   C  CA  . ALA A 1 171 ? 132.809 170.941 124.978 1.00 69.73  ? 129  ALA A CA  1 
ATOM   686   C  C   . ALA A 1 171 ? 131.658 170.773 123.997 1.00 72.16  ? 129  ALA A C   1 
ATOM   687   O  O   . ALA A 1 171 ? 131.727 171.287 122.875 1.00 72.35  ? 129  ALA A O   1 
ATOM   688   C  CB  . ALA A 1 171 ? 133.814 169.801 124.807 1.00 69.85  ? 129  ALA A CB  1 
ATOM   689   N  N   . ALA A 1 172 ? 130.601 170.063 124.394 1.00 74.48  ? 130  ALA A N   1 
ATOM   690   C  CA  . ALA A 1 172 ? 129.448 169.892 123.520 1.00 70.47  ? 130  ALA A CA  1 
ATOM   691   C  C   . ALA A 1 172 ? 128.588 171.145 123.448 1.00 71.24  ? 130  ALA A C   1 
ATOM   692   O  O   . ALA A 1 172 ? 127.758 171.260 122.540 1.00 72.99  ? 130  ALA A O   1 
ATOM   693   C  CB  . ALA A 1 172 ? 128.604 168.707 123.987 1.00 64.65  ? 130  ALA A CB  1 
ATOM   694   N  N   . ALA A 1 173 ? 128.761 172.082 124.381 1.00 76.20  ? 131  ALA A N   1 
ATOM   695   C  CA  . ALA A 1 173 ? 128.023 173.338 124.333 1.00 76.27  ? 131  ALA A CA  1 
ATOM   696   C  C   . ALA A 1 173 ? 128.603 174.316 123.323 1.00 75.73  ? 131  ALA A C   1 
ATOM   697   O  O   . ALA A 1 173 ? 127.919 175.272 122.944 1.00 77.20  ? 131  ALA A O   1 
ATOM   698   C  CB  . ALA A 1 173 ? 127.991 173.986 125.718 1.00 75.14  ? 131  ALA A CB  1 
ATOM   699   N  N   . THR A 1 174 ? 129.845 174.101 122.887 1.00 77.92  ? 132  THR A N   1 
ATOM   700   C  CA  . THR A 1 174 ? 130.443 174.967 121.877 1.00 78.13  ? 132  THR A CA  1 
ATOM   701   C  C   . THR A 1 174 ? 129.704 174.858 120.548 1.00 79.85  ? 132  THR A C   1 
ATOM   702   O  O   . THR A 1 174 ? 129.476 175.868 119.873 1.00 81.10  ? 132  THR A O   1 
ATOM   703   C  CB  . THR A 1 174 ? 131.922 174.619 121.705 1.00 78.21  ? 132  THR A CB  1 
ATOM   704   O  OG1 . THR A 1 174 ? 132.667 175.136 122.814 1.00 78.46  ? 132  THR A OG1 1 
ATOM   705   C  CG2 . THR A 1 174 ? 132.474 175.202 120.412 1.00 77.34  ? 132  THR A CG2 1 
ATOM   706   N  N   . TYR A 1 175 ? 129.316 173.640 120.162 1.00 72.99  ? 133  TYR A N   1 
ATOM   707   C  CA  . TYR A 1 175 ? 128.651 173.447 118.877 1.00 72.35  ? 133  TYR A CA  1 
ATOM   708   C  C   . TYR A 1 175 ? 127.310 174.169 118.831 1.00 74.01  ? 133  TYR A C   1 
ATOM   709   O  O   . TYR A 1 175 ? 126.968 174.795 117.821 1.00 73.33  ? 133  TYR A O   1 
ATOM   710   C  CB  . TYR A 1 175 ? 128.474 171.955 118.602 1.00 67.43  ? 133  TYR A CB  1 
ATOM   711   C  CG  . TYR A 1 175 ? 129.781 171.213 118.455 1.00 68.28  ? 133  TYR A CG  1 
ATOM   712   C  CD1 . TYR A 1 175 ? 130.411 171.114 117.223 1.00 70.07  ? 133  TYR A CD1 1 
ATOM   713   C  CD2 . TYR A 1 175 ? 130.388 170.616 119.550 1.00 69.28  ? 133  TYR A CD2 1 
ATOM   714   C  CE1 . TYR A 1 175 ? 131.608 170.439 117.085 1.00 68.79  ? 133  TYR A CE1 1 
ATOM   715   C  CE2 . TYR A 1 175 ? 131.584 169.939 119.422 1.00 70.98  ? 133  TYR A CE2 1 
ATOM   716   C  CZ  . TYR A 1 175 ? 132.190 169.854 118.188 1.00 69.68  ? 133  TYR A CZ  1 
ATOM   717   O  OH  . TYR A 1 175 ? 133.381 169.180 118.058 1.00 67.45  ? 133  TYR A OH  1 
ATOM   718   N  N   . VAL A 1 176 ? 126.535 174.090 119.909 1.00 78.55  ? 134  VAL A N   1 
ATOM   719   C  CA  . VAL A 1 176 ? 125.257 174.818 119.993 1.00 76.51  ? 134  VAL A CA  1 
ATOM   720   C  C   . VAL A 1 176 ? 125.573 176.161 120.641 1.00 78.23  ? 134  VAL A C   1 
ATOM   721   O  O   . VAL A 1 176 ? 125.394 176.382 121.841 1.00 81.47  ? 134  VAL A O   1 
ATOM   722   C  CB  . VAL A 1 176 ? 124.186 174.022 120.745 1.00 73.02  ? 134  VAL A CB  1 
ATOM   723   C  CG1 . VAL A 1 176 ? 123.607 172.954 119.845 1.00 76.38  ? 134  VAL A CG1 1 
ATOM   724   C  CG2 . VAL A 1 176 ? 124.778 173.371 121.985 1.00 73.19  ? 134  VAL A CG2 1 
ATOM   725   N  N   . GLN A 1 177 ? 126.045 177.094 119.817 1.00 81.77  ? 135  GLN A N   1 
ATOM   726   C  CA  . GLN A 1 177 ? 126.392 178.425 120.298 1.00 81.90  ? 135  GLN A CA  1 
ATOM   727   C  C   . GLN A 1 177 ? 125.719 179.488 119.441 1.00 86.74  ? 135  GLN A C   1 
ATOM   728   O  O   . GLN A 1 177 ? 125.424 180.588 119.918 1.00 86.85  ? 135  GLN A O   1 
ATOM   729   C  CB  . GLN A 1 177 ? 127.908 178.619 120.298 1.00 82.60  ? 135  GLN A CB  1 
ATOM   730   C  CG  . GLN A 1 177 ? 128.447 179.293 121.547 1.00 85.70  ? 135  GLN A CG  1 
ATOM   731   C  CD  . GLN A 1 177 ? 129.962 179.294 121.600 1.00 86.01  ? 135  GLN A CD  1 
ATOM   732   O  OE1 . GLN A 1 177 ? 130.631 179.295 120.567 1.00 86.62  ? 135  GLN A OE1 1 
ATOM   733   N  NE2 . GLN A 1 177 ? 130.511 179.291 122.808 1.00 84.58  ? 135  GLN A NE2 1 
ATOM   734   N  N   . ASN A 1 178 ? 125.474 179.162 118.174 1.00 83.52  ? 136  ASN A N   1 
ATOM   735   C  CA  . ASN A 1 178 ? 124.810 180.056 117.228 1.00 80.98  ? 136  ASN A CA  1 
ATOM   736   C  C   . ASN A 1 178 ? 123.362 179.642 117.003 1.00 78.68  ? 136  ASN A C   1 
ATOM   737   O  O   . ASN A 1 178 ? 122.853 179.697 115.882 1.00 79.51  ? 136  ASN A O   1 
ATOM   738   C  CB  . ASN A 1 178 ? 125.580 180.090 115.910 1.00 79.32  ? 136  ASN A CB  1 
ATOM   739   C  CG  . ASN A 1 178 ? 125.154 181.235 115.010 1.00 84.06  ? 136  ASN A CG  1 
ATOM   740   O  OD1 . ASN A 1 178 ? 124.514 182.187 115.457 1.00 84.79  ? 136  ASN A OD1 1 
ATOM   741   N  ND2 . ASN A 1 178 ? 125.508 181.147 113.732 1.00 83.61  ? 136  ASN A ND2 1 
ATOM   742   N  N   . GLN A 1 179 ? 122.684 179.208 118.064 1.00 72.93  ? 137  GLN A N   1 
ATOM   743   C  CA  . GLN A 1 179 ? 121.335 178.671 117.934 1.00 71.74  ? 137  GLN A CA  1 
ATOM   744   C  C   . GLN A 1 179 ? 120.376 179.715 117.378 1.00 71.91  ? 137  GLN A C   1 
ATOM   745   O  O   . GLN A 1 179 ? 120.362 180.868 117.820 1.00 73.11  ? 137  GLN A O   1 
ATOM   746   C  CB  . GLN A 1 179 ? 120.839 178.171 119.290 1.00 69.45  ? 137  GLN A CB  1 
ATOM   747   C  CG  . GLN A 1 179 ? 121.862 177.358 120.058 1.00 73.18  ? 137  GLN A CG  1 
ATOM   748   C  CD  . GLN A 1 179 ? 121.619 177.380 121.551 1.00 72.62  ? 137  GLN A CD  1 
ATOM   749   O  OE1 . GLN A 1 179 ? 120.589 177.868 122.015 1.00 71.86  ? 137  GLN A OE1 1 
ATOM   750   N  NE2 . GLN A 1 179 ? 122.568 176.852 122.313 1.00 71.95  ? 137  GLN A NE2 1 
ATOM   751   N  N   . SER A 1 180 ? 119.573 179.302 116.400 1.00 64.63  ? 138  SER A N   1 
ATOM   752   C  CA  . SER A 1 180 ? 118.563 180.162 115.807 1.00 64.77  ? 138  SER A CA  1 
ATOM   753   C  C   . SER A 1 180 ? 117.356 179.312 115.442 1.00 61.66  ? 138  SER A C   1 
ATOM   754   O  O   . SER A 1 180 ? 117.469 178.102 115.232 1.00 61.08  ? 138  SER A O   1 
ATOM   755   C  CB  . SER A 1 180 ? 119.099 180.897 114.573 1.00 67.90  ? 138  SER A CB  1 
ATOM   756   O  OG  . SER A 1 180 ? 118.305 182.030 114.269 1.00 71.13  ? 138  SER A OG  1 
ATOM   757   N  N   . GLU A 1 181 ? 116.192 179.961 115.374 1.00 65.75  ? 139  GLU A N   1 
ATOM   758   C  CA  . GLU A 1 181 ? 114.969 179.242 115.029 1.00 64.66  ? 139  GLU A CA  1 
ATOM   759   C  C   . GLU A 1 181 ? 115.043 178.677 113.617 1.00 66.75  ? 139  GLU A C   1 
ATOM   760   O  O   . GLU A 1 181 ? 114.599 177.550 113.367 1.00 68.16  ? 139  GLU A O   1 
ATOM   761   C  CB  . GLU A 1 181 ? 113.756 180.157 115.182 1.00 66.88  ? 139  GLU A CB  1 
ATOM   762   C  CG  . GLU A 1 181 ? 112.429 179.442 115.001 1.00 66.96  ? 139  GLU A CG  1 
ATOM   763   C  CD  . GLU A 1 181 ? 111.290 180.131 115.723 1.00 69.08  ? 139  GLU A CD  1 
ATOM   764   O  OE1 . GLU A 1 181 ? 111.537 181.173 116.365 1.00 71.37  ? 139  GLU A OE1 1 
ATOM   765   O  OE2 . GLU A 1 181 ? 110.149 179.630 115.651 1.00 68.97  ? 139  GLU A OE2 1 
ATOM   766   N  N   . ASP A 1 182 ? 115.596 179.443 112.680 1.00 64.15  ? 140  ASP A N   1 
ATOM   767   C  CA  . ASP A 1 182 ? 115.816 178.960 111.318 1.00 61.90  ? 140  ASP A CA  1 
ATOM   768   C  C   . ASP A 1 182 ? 117.023 178.033 111.354 1.00 60.46  ? 140  ASP A C   1 
ATOM   769   O  O   . ASP A 1 182 ? 118.169 178.451 111.181 1.00 59.26  ? 140  ASP A O   1 
ATOM   770   C  CB  . ASP A 1 182 ? 116.018 180.124 110.354 1.00 64.01  ? 140  ASP A CB  1 
ATOM   771   C  CG  . ASP A 1 182 ? 116.599 179.687 109.022 1.00 65.14  ? 140  ASP A CG  1 
ATOM   772   O  OD1 . ASP A 1 182 ? 116.190 178.623 108.510 1.00 58.53  ? 140  ASP A OD1 1 
ATOM   773   O  OD2 . ASP A 1 182 ? 117.468 180.408 108.489 1.00 66.55  ? 140  ASP A OD2 1 
ATOM   774   N  N   . CYS A 1 183 ? 116.761 176.752 111.603 1.00 56.13  ? 141  CYS A N   1 
ATOM   775   C  CA  . CYS A 1 183 ? 117.809 175.750 111.705 1.00 54.68  ? 141  CYS A CA  1 
ATOM   776   C  C   . CYS A 1 183 ? 117.635 174.593 110.735 1.00 54.50  ? 141  CYS A C   1 
ATOM   777   O  O   . CYS A 1 183 ? 118.433 173.650 110.774 1.00 57.67  ? 141  CYS A O   1 
ATOM   778   C  CB  . CYS A 1 183 ? 117.882 175.204 113.135 1.00 53.67  ? 141  CYS A CB  1 
ATOM   779   S  SG  . CYS A 1 183 ? 116.274 174.814 113.860 1.00 57.50  ? 141  CYS A SG  1 
ATOM   780   N  N   . LEU A 1 184 ? 116.626 174.633 109.868 1.00 46.57  ? 142  LEU A N   1 
ATOM   781   C  CA  . LEU A 1 184 ? 116.386 173.527 108.951 1.00 43.44  ? 142  LEU A CA  1 
ATOM   782   C  C   . LEU A 1 184 ? 117.440 173.508 107.852 1.00 48.20  ? 142  LEU A C   1 
ATOM   783   O  O   . LEU A 1 184 ? 117.285 174.163 106.817 1.00 52.30  ? 142  LEU A O   1 
ATOM   784   C  CB  . LEU A 1 184 ? 114.981 173.624 108.355 1.00 44.19  ? 142  LEU A CB  1 
ATOM   785   C  CG  . LEU A 1 184 ? 113.840 173.649 109.374 1.00 46.30  ? 142  LEU A CG  1 
ATOM   786   C  CD1 . LEU A 1 184 ? 112.498 173.470 108.688 1.00 46.72  ? 142  LEU A CD1 1 
ATOM   787   C  CD2 . LEU A 1 184 ? 114.043 172.581 110.433 1.00 43.14  ? 142  LEU A CD2 1 
ATOM   788   N  N   . TYR A 1 185 ? 118.516 172.757 108.076 1.00 39.78  ? 143  TYR A N   1 
ATOM   789   C  CA  . TYR A 1 185 ? 119.595 172.627 107.109 1.00 37.59  ? 143  TYR A CA  1 
ATOM   790   C  C   . TYR A 1 185 ? 120.143 171.210 107.186 1.00 38.97  ? 143  TYR A C   1 
ATOM   791   O  O   . TYR A 1 185 ? 119.813 170.441 108.092 1.00 47.52  ? 143  TYR A O   1 
ATOM   792   C  CB  . TYR A 1 185 ? 120.711 173.645 107.363 1.00 41.76  ? 143  TYR A CB  1 
ATOM   793   C  CG  . TYR A 1 185 ? 120.283 175.090 107.253 1.00 41.72  ? 143  TYR A CG  1 
ATOM   794   C  CD1 . TYR A 1 185 ? 120.315 175.754 106.036 1.00 40.31  ? 143  TYR A CD1 1 
ATOM   795   C  CD2 . TYR A 1 185 ? 119.858 175.794 108.371 1.00 43.44  ? 143  TYR A CD2 1 
ATOM   796   C  CE1 . TYR A 1 185 ? 119.927 177.075 105.932 1.00 40.64  ? 143  TYR A CE1 1 
ATOM   797   C  CE2 . TYR A 1 185 ? 119.468 177.116 108.277 1.00 45.24  ? 143  TYR A CE2 1 
ATOM   798   C  CZ  . TYR A 1 185 ? 119.505 177.751 107.056 1.00 45.33  ? 143  TYR A CZ  1 
ATOM   799   O  OH  . TYR A 1 185 ? 119.119 179.067 106.959 1.00 52.01  ? 143  TYR A OH  1 
ATOM   800   N  N   . LEU A 1 186 ? 120.984 170.866 106.214 1.00 36.51  ? 144  LEU A N   1 
ATOM   801   C  CA  . LEU A 1 186 ? 121.663 169.580 106.222 1.00 36.99  ? 144  LEU A CA  1 
ATOM   802   C  C   . LEU A 1 186 ? 123.036 169.741 105.589 1.00 37.15  ? 144  LEU A C   1 
ATOM   803   O  O   . LEU A 1 186 ? 123.290 170.685 104.837 1.00 44.51  ? 144  LEU A O   1 
ATOM   804   C  CB  . LEU A 1 186 ? 120.849 168.498 105.499 1.00 36.78  ? 144  LEU A CB  1 
ATOM   805   C  CG  . LEU A 1 186 ? 120.412 168.736 104.054 1.00 32.67  ? 144  LEU A CG  1 
ATOM   806   C  CD1 . LEU A 1 186 ? 121.377 168.081 103.087 1.00 39.19  ? 144  LEU A CD1 1 
ATOM   807   C  CD2 . LEU A 1 186 ? 119.013 168.201 103.839 1.00 32.58  ? 144  LEU A CD2 1 
ATOM   808   N  N   . ASN A 1 187 ? 123.923 168.805 105.911 1.00 28.88  ? 145  ASN A N   1 
ATOM   809   C  CA  . ASN A 1 187 ? 125.293 168.802 105.423 1.00 32.42  ? 145  ASN A CA  1 
ATOM   810   C  C   . ASN A 1 187 ? 125.571 167.469 104.749 1.00 34.52  ? 145  ASN A C   1 
ATOM   811   O  O   . ASN A 1 187 ? 125.278 166.410 105.316 1.00 48.71  ? 145  ASN A O   1 
ATOM   812   C  CB  . ASN A 1 187 ? 126.286 169.037 106.564 1.00 42.33  ? 145  ASN A CB  1 
ATOM   813   C  CG  . ASN A 1 187 ? 125.713 169.906 107.664 1.00 46.28  ? 145  ASN A CG  1 
ATOM   814   O  OD1 . ASN A 1 187 ? 125.314 171.044 107.427 1.00 50.69  ? 145  ASN A OD1 1 
ATOM   815   N  ND2 . ASN A 1 187 ? 125.672 169.373 108.878 1.00 43.42  ? 145  ASN A ND2 1 
ATOM   816   N  N   . LEU A 1 188 ? 126.137 167.528 103.548 1.00 34.86  ? 146  LEU A N   1 
ATOM   817   C  CA  . LEU A 1 188 ? 126.468 166.352 102.759 1.00 39.71  ? 146  LEU A CA  1 
ATOM   818   C  C   . LEU A 1 188 ? 127.979 166.220 102.634 1.00 45.09  ? 146  LEU A C   1 
ATOM   819   O  O   . LEU A 1 188 ? 128.688 167.221 102.484 1.00 52.76  ? 146  LEU A O   1 
ATOM   820   C  CB  . LEU A 1 188 ? 125.846 166.429 101.364 1.00 37.31  ? 146  LEU A CB  1 
ATOM   821   C  CG  . LEU A 1 188 ? 124.363 166.778 101.279 1.00 36.63  ? 146  LEU A CG  1 
ATOM   822   C  CD1 . LEU A 1 188 ? 124.184 168.131 100.626 1.00 39.00  ? 146  LEU A CD1 1 
ATOM   823   C  CD2 . LEU A 1 188 ? 123.612 165.714 100.507 1.00 39.75  ? 146  LEU A CD2 1 
ATOM   824   N  N   . TYR A 1 189 ? 128.467 164.984 102.692 1.00 46.50  ? 147  TYR A N   1 
ATOM   825   C  CA  . TYR A 1 189 ? 129.893 164.689 102.568 1.00 46.70  ? 147  TYR A CA  1 
ATOM   826   C  C   . TYR A 1 189 ? 130.070 163.692 101.426 1.00 51.03  ? 147  TYR A C   1 
ATOM   827   O  O   . TYR A 1 189 ? 130.059 162.478 101.639 1.00 48.50  ? 147  TYR A O   1 
ATOM   828   C  CB  . TYR A 1 189 ? 130.453 164.152 103.881 1.00 46.01  ? 147  TYR A CB  1 
ATOM   829   C  CG  . TYR A 1 189 ? 130.177 165.043 105.071 1.00 47.49  ? 147  TYR A CG  1 
ATOM   830   C  CD1 . TYR A 1 189 ? 129.017 164.897 105.818 1.00 49.50  ? 147  TYR A CD1 1 
ATOM   831   C  CD2 . TYR A 1 189 ? 131.076 166.031 105.447 1.00 48.50  ? 147  TYR A CD2 1 
ATOM   832   C  CE1 . TYR A 1 189 ? 128.760 165.709 106.905 1.00 49.07  ? 147  TYR A CE1 1 
ATOM   833   C  CE2 . TYR A 1 189 ? 130.826 166.848 106.533 1.00 49.93  ? 147  TYR A CE2 1 
ATOM   834   C  CZ  . TYR A 1 189 ? 129.667 166.682 107.257 1.00 46.66  ? 147  TYR A CZ  1 
ATOM   835   O  OH  . TYR A 1 189 ? 129.413 167.492 108.339 1.00 46.59  ? 147  TYR A OH  1 
ATOM   836   N  N   . VAL A 1 190 ? 130.234 164.208 100.212 1.00 49.37  ? 148  VAL A N   1 
ATOM   837   C  CA  . VAL A 1 190 ? 130.362 163.376 99.018  1.00 46.69  ? 148  VAL A CA  1 
ATOM   838   C  C   . VAL A 1 190 ? 131.806 162.914 98.862  1.00 49.98  ? 148  VAL A C   1 
ATOM   839   O  O   . VAL A 1 190 ? 132.719 163.749 98.806  1.00 53.61  ? 148  VAL A O   1 
ATOM   840   C  CB  . VAL A 1 190 ? 129.892 164.133 97.767  1.00 46.43  ? 148  VAL A CB  1 
ATOM   841   C  CG1 . VAL A 1 190 ? 129.597 163.161 96.641  1.00 50.58  ? 148  VAL A CG1 1 
ATOM   842   C  CG2 . VAL A 1 190 ? 128.667 164.972 98.086  1.00 48.74  ? 148  VAL A CG2 1 
ATOM   843   N  N   . PRO A 1 191 ? 132.067 161.614 98.788  1.00 50.72  ? 149  PRO A N   1 
ATOM   844   C  CA  . PRO A 1 191 ? 133.431 161.148 98.533  1.00 51.35  ? 149  PRO A CA  1 
ATOM   845   C  C   . PRO A 1 191 ? 133.817 161.326 97.072  1.00 58.66  ? 149  PRO A C   1 
ATOM   846   O  O   . PRO A 1 191 ? 132.976 161.513 96.191  1.00 60.92  ? 149  PRO A O   1 
ATOM   847   C  CB  . PRO A 1 191 ? 133.370 159.665 98.910  1.00 47.20  ? 149  PRO A CB  1 
ATOM   848   C  CG  . PRO A 1 191 ? 131.964 159.285 98.633  1.00 44.36  ? 149  PRO A CG  1 
ATOM   849   C  CD  . PRO A 1 191 ? 131.122 160.496 98.946  1.00 48.23  ? 149  PRO A CD  1 
ATOM   850   N  N   . THR A 1 192 ? 135.122 161.267 96.828  1.00 63.23  ? 150  THR A N   1 
ATOM   851   C  CA  . THR A 1 192 ? 135.650 161.388 95.474  1.00 60.35  ? 150  THR A CA  1 
ATOM   852   C  C   . THR A 1 192 ? 136.537 160.198 95.125  1.00 59.72  ? 150  THR A C   1 
ATOM   853   O  O   . THR A 1 192 ? 136.058 159.176 94.634  1.00 56.92  ? 150  THR A O   1 
ATOM   854   C  CB  . THR A 1 192 ? 136.453 162.688 95.290  1.00 57.18  ? 150  THR A CB  1 
ATOM   855   O  OG1 . THR A 1 192 ? 137.518 162.734 96.247  1.00 58.78  ? 150  THR A OG1 1 
ATOM   856   C  CG2 . THR A 1 192 ? 135.557 163.900 95.476  1.00 52.53  ? 150  THR A CG2 1 
ATOM   857   N  N   . GLY A 1 200 ? 127.696 150.903 90.675  1.00 68.16  ? 175  GLY A N   1 
ATOM   858   C  CA  . GLY A 1 200 ? 126.721 151.964 90.510  1.00 69.42  ? 175  GLY A CA  1 
ATOM   859   C  C   . GLY A 1 200 ? 127.057 153.208 91.306  1.00 72.28  ? 175  GLY A C   1 
ATOM   860   O  O   . GLY A 1 200 ? 128.073 153.254 91.999  1.00 71.52  ? 175  GLY A O   1 
ATOM   861   N  N   . LYS A 1 201 ? 126.201 154.222 91.205  1.00 65.56  ? 176  LYS A N   1 
ATOM   862   C  CA  . LYS A 1 201 ? 126.420 155.462 91.933  1.00 62.84  ? 176  LYS A CA  1 
ATOM   863   C  C   . LYS A 1 201 ? 126.309 155.232 93.437  1.00 60.19  ? 176  LYS A C   1 
ATOM   864   O  O   . LYS A 1 201 ? 125.547 154.383 93.907  1.00 60.81  ? 176  LYS A O   1 
ATOM   865   C  CB  . LYS A 1 201 ? 125.431 156.534 91.476  1.00 57.74  ? 176  LYS A CB  1 
ATOM   866   C  CG  . LYS A 1 201 ? 124.208 155.999 90.755  1.00 58.74  ? 176  LYS A CG  1 
ATOM   867   C  CD  . LYS A 1 201 ? 123.407 157.132 90.133  1.00 59.03  ? 176  LYS A CD  1 
ATOM   868   C  CE  . LYS A 1 201 ? 122.031 156.666 89.689  1.00 61.02  ? 176  LYS A CE  1 
ATOM   869   N  NZ  . LYS A 1 201 ? 121.046 157.782 89.686  1.00 63.10  ? 176  LYS A NZ  1 
ATOM   870   N  N   . LYS A 1 202 ? 127.086 156.008 94.190  1.00 50.18  ? 177  LYS A N   1 
ATOM   871   C  CA  . LYS A 1 202 ? 127.267 155.760 95.611  1.00 50.89  ? 177  LYS A CA  1 
ATOM   872   C  C   . LYS A 1 202 ? 125.956 155.950 96.376  1.00 52.57  ? 177  LYS A C   1 
ATOM   873   O  O   . LYS A 1 202 ? 125.124 156.784 96.007  1.00 51.31  ? 177  LYS A O   1 
ATOM   874   C  CB  . LYS A 1 202 ? 128.343 156.688 96.168  1.00 49.13  ? 177  LYS A CB  1 
ATOM   875   C  CG  . LYS A 1 202 ? 128.247 158.113 95.661  1.00 49.21  ? 177  LYS A CG  1 
ATOM   876   C  CD  . LYS A 1 202 ? 129.511 158.890 95.975  1.00 52.06  ? 177  LYS A CD  1 
ATOM   877   C  CE  . LYS A 1 202 ? 130.723 158.261 95.312  1.00 52.86  ? 177  LYS A CE  1 
ATOM   878   N  NZ  . LYS A 1 202 ? 130.512 158.064 93.853  1.00 52.08  ? 177  LYS A NZ  1 
ATOM   879   N  N   . PRO A 1 203 ? 125.749 155.187 97.443  1.00 45.20  ? 178  PRO A N   1 
ATOM   880   C  CA  . PRO A 1 203 ? 124.509 155.282 98.218  1.00 45.24  ? 178  PRO A CA  1 
ATOM   881   C  C   . PRO A 1 203 ? 124.504 156.526 99.100  1.00 48.34  ? 178  PRO A C   1 
ATOM   882   O  O   . PRO A 1 203 ? 125.415 157.349 99.073  1.00 55.29  ? 178  PRO A O   1 
ATOM   883   C  CB  . PRO A 1 203 ? 124.520 154.002 99.065  1.00 40.56  ? 178  PRO A CB  1 
ATOM   884   C  CG  . PRO A 1 203 ? 125.626 153.151 98.507  1.00 42.14  ? 178  PRO A CG  1 
ATOM   885   C  CD  . PRO A 1 203 ? 126.610 154.098 97.925  1.00 41.83  ? 178  PRO A CD  1 
ATOM   886   N  N   . VAL A 1 204 ? 123.443 156.647 99.895  1.00 39.88  ? 179  VAL A N   1 
ATOM   887   C  CA  . VAL A 1 204 ? 123.254 157.762 100.812 1.00 35.17  ? 179  VAL A CA  1 
ATOM   888   C  C   . VAL A 1 204 ? 122.954 157.199 102.193 1.00 37.98  ? 179  VAL A C   1 
ATOM   889   O  O   . VAL A 1 204 ? 122.232 156.205 102.321 1.00 47.85  ? 179  VAL A O   1 
ATOM   890   C  CB  . VAL A 1 204 ? 122.116 158.696 100.346 1.00 37.44  ? 179  VAL A CB  1 
ATOM   891   C  CG1 . VAL A 1 204 ? 121.993 159.897 101.268 1.00 39.74  ? 179  VAL A CG1 1 
ATOM   892   C  CG2 . VAL A 1 204 ? 122.346 159.143 98.917  1.00 40.04  ? 179  VAL A CG2 1 
ATOM   893   N  N   . MET A 1 205 ? 123.521 157.824 103.223 1.00 35.33  ? 180  MET A N   1 
ATOM   894   C  CA  . MET A 1 205 ? 123.277 157.450 104.613 1.00 39.16  ? 180  MET A CA  1 
ATOM   895   C  C   . MET A 1 205 ? 122.921 158.707 105.393 1.00 40.24  ? 180  MET A C   1 
ATOM   896   O  O   . MET A 1 205 ? 123.783 159.557 105.631 1.00 50.60  ? 180  MET A O   1 
ATOM   897   C  CB  . MET A 1 205 ? 124.495 156.761 105.227 1.00 38.25  ? 180  MET A CB  1 
ATOM   898   C  CG  . MET A 1 205 ? 124.915 155.486 104.525 1.00 42.41  ? 180  MET A CG  1 
ATOM   899   S  SD  . MET A 1 205 ? 126.220 154.628 105.421 1.00 47.52  ? 180  MET A SD  1 
ATOM   900   C  CE  . MET A 1 205 ? 125.425 154.377 107.003 1.00 35.49  ? 180  MET A CE  1 
ATOM   901   N  N   . LEU A 1 206 ? 121.655 158.827 105.781 1.00 42.46  ? 181  LEU A N   1 
ATOM   902   C  CA  . LEU A 1 206 ? 121.193 159.940 106.596 1.00 45.04  ? 181  LEU A CA  1 
ATOM   903   C  C   . LEU A 1 206 ? 121.332 159.587 108.069 1.00 46.53  ? 181  LEU A C   1 
ATOM   904   O  O   . LEU A 1 206 ? 121.062 158.452 108.474 1.00 55.99  ? 181  LEU A O   1 
ATOM   905   C  CB  . LEU A 1 206 ? 119.737 160.281 106.271 1.00 46.34  ? 181  LEU A CB  1 
ATOM   906   C  CG  . LEU A 1 206 ? 119.111 161.445 107.042 1.00 46.30  ? 181  LEU A CG  1 
ATOM   907   C  CD1 . LEU A 1 206 ? 119.734 162.764 106.626 1.00 53.48  ? 181  LEU A CD1 1 
ATOM   908   C  CD2 . LEU A 1 206 ? 117.608 161.478 106.841 1.00 47.07  ? 181  LEU A CD2 1 
ATOM   909   N  N   . PHE A 1 207 ? 121.775 160.557 108.865 1.00 43.80  ? 182  PHE A N   1 
ATOM   910   C  CA  . PHE A 1 207 ? 121.993 160.360 110.293 1.00 41.39  ? 182  PHE A CA  1 
ATOM   911   C  C   . PHE A 1 207 ? 120.982 161.185 111.078 1.00 43.37  ? 182  PHE A C   1 
ATOM   912   O  O   . PHE A 1 207 ? 120.889 162.402 110.888 1.00 53.34  ? 182  PHE A O   1 
ATOM   913   C  CB  . PHE A 1 207 ? 123.417 160.745 110.687 1.00 39.10  ? 182  PHE A CB  1 
ATOM   914   C  CG  . PHE A 1 207 ? 123.731 160.499 112.134 1.00 41.28  ? 182  PHE A CG  1 
ATOM   915   C  CD1 . PHE A 1 207 ? 123.660 159.224 112.664 1.00 43.28  ? 182  PHE A CD1 1 
ATOM   916   C  CD2 . PHE A 1 207 ? 124.096 161.541 112.964 1.00 48.22  ? 182  PHE A CD2 1 
ATOM   917   C  CE1 . PHE A 1 207 ? 123.948 158.992 113.992 1.00 39.53  ? 182  PHE A CE1 1 
ATOM   918   C  CE2 . PHE A 1 207 ? 124.383 161.315 114.294 1.00 47.75  ? 182  PHE A CE2 1 
ATOM   919   C  CZ  . PHE A 1 207 ? 124.309 160.039 114.808 1.00 40.31  ? 182  PHE A CZ  1 
ATOM   920   N  N   . LEU A 1 208 ? 120.238 160.525 111.964 1.00 23.04  ? 183  LEU A N   1 
ATOM   921   C  CA  . LEU A 1 208 ? 119.256 161.183 112.825 1.00 26.53  ? 183  LEU A CA  1 
ATOM   922   C  C   . LEU A 1 208 ? 119.847 161.284 114.227 1.00 36.96  ? 183  LEU A C   1 
ATOM   923   O  O   . LEU A 1 208 ? 119.819 160.322 114.998 1.00 41.49  ? 183  LEU A O   1 
ATOM   924   C  CB  . LEU A 1 208 ? 117.935 160.422 112.832 1.00 31.53  ? 183  LEU A CB  1 
ATOM   925   C  CG  . LEU A 1 208 ? 117.199 160.246 111.505 1.00 22.78  ? 183  LEU A CG  1 
ATOM   926   C  CD1 . LEU A 1 208 ? 115.742 159.938 111.774 1.00 29.37  ? 183  LEU A CD1 1 
ATOM   927   C  CD2 . LEU A 1 208 ? 117.328 161.486 110.645 1.00 28.20  ? 183  LEU A CD2 1 
ATOM   928   N  N   . HIS A 1 209 ? 120.373 162.458 114.559 1.00 36.95  ? 184  HIS A N   1 
ATOM   929   C  CA  . HIS A 1 209 ? 121.045 162.677 115.832 1.00 35.50  ? 184  HIS A CA  1 
ATOM   930   C  C   . HIS A 1 209 ? 120.017 162.801 116.955 1.00 37.80  ? 184  HIS A C   1 
ATOM   931   O  O   . HIS A 1 209 ? 118.811 162.641 116.754 1.00 46.79  ? 184  HIS A O   1 
ATOM   932   C  CB  . HIS A 1 209 ? 121.931 163.915 115.749 1.00 34.73  ? 184  HIS A CB  1 
ATOM   933   C  CG  . HIS A 1 209 ? 121.164 165.190 115.586 1.00 38.03  ? 184  HIS A CG  1 
ATOM   934   N  ND1 . HIS A 1 209 ? 120.688 165.914 116.657 1.00 36.22  ? 184  HIS A ND1 1 
ATOM   935   C  CD2 . HIS A 1 209 ? 120.781 165.864 114.476 1.00 41.80  ? 184  HIS A CD2 1 
ATOM   936   C  CE1 . HIS A 1 209 ? 120.049 166.982 116.215 1.00 38.91  ? 184  HIS A CE1 1 
ATOM   937   N  NE2 . HIS A 1 209 ? 120.091 166.976 114.895 1.00 42.73  ? 184  HIS A NE2 1 
ATOM   938   N  N   . GLY A 1 210 ? 120.496 163.090 118.162 1.00 38.19  ? 185  GLY A N   1 
ATOM   939   C  CA  . GLY A 1 210 ? 119.623 163.359 119.286 1.00 31.32  ? 185  GLY A CA  1 
ATOM   940   C  C   . GLY A 1 210 ? 119.649 162.301 120.369 1.00 34.14  ? 185  GLY A C   1 
ATOM   941   O  O   . GLY A 1 210 ? 119.010 161.254 120.237 1.00 30.90  ? 185  GLY A O   1 
ATOM   942   N  N   . GLY A 1 211 ? 120.388 162.563 121.448 1.00 34.47  ? 186  GLY A N   1 
ATOM   943   C  CA  . GLY A 1 211 ? 120.332 161.675 122.597 1.00 33.78  ? 186  GLY A CA  1 
ATOM   944   C  C   . GLY A 1 211 ? 118.964 161.676 123.250 1.00 32.29  ? 186  GLY A C   1 
ATOM   945   O  O   . GLY A 1 211 ? 118.437 160.622 123.614 1.00 41.26  ? 186  GLY A O   1 
ATOM   946   N  N   . SER A 1 212 ? 118.382 162.855 123.418 1.00 30.72  ? 187  SER A N   1 
ATOM   947   C  CA  . SER A 1 212 ? 116.986 163.030 123.787 1.00 29.73  ? 187  SER A CA  1 
ATOM   948   C  C   . SER A 1 212 ? 116.313 163.868 122.701 1.00 46.39  ? 187  SER A C   1 
ATOM   949   O  O   . SER A 1 212 ? 116.900 164.149 121.652 1.00 53.17  ? 187  SER A O   1 
ATOM   950   C  CB  . SER A 1 212 ? 116.860 163.672 125.170 1.00 25.82  ? 187  SER A CB  1 
ATOM   951   O  OG  . SER A 1 212 ? 116.898 165.084 125.082 1.00 34.57  ? 187  SER A OG  1 
ATOM   952   N  N   . TYR A 1 213 ? 115.074 164.269 122.954 1.00 38.99  ? 188  TYR A N   1 
ATOM   953   C  CA  . TYR A 1 213 ? 114.321 165.068 122.000 1.00 34.29  ? 188  TYR A CA  1 
ATOM   954   C  C   . TYR A 1 213 ? 114.451 166.565 122.251 1.00 43.10  ? 188  TYR A C   1 
ATOM   955   O  O   . TYR A 1 213 ? 113.687 167.344 121.674 1.00 43.61  ? 188  TYR A O   1 
ATOM   956   C  CB  . TYR A 1 213 ? 112.848 164.666 122.026 1.00 32.52  ? 188  TYR A CB  1 
ATOM   957   C  CG  . TYR A 1 213 ? 112.581 163.290 121.465 1.00 32.79  ? 188  TYR A CG  1 
ATOM   958   C  CD1 . TYR A 1 213 ? 112.706 163.037 120.108 1.00 34.49  ? 188  TYR A CD1 1 
ATOM   959   C  CD2 . TYR A 1 213 ? 112.203 162.245 122.294 1.00 33.70  ? 188  TYR A CD2 1 
ATOM   960   C  CE1 . TYR A 1 213 ? 112.460 161.782 119.593 1.00 30.34  ? 188  TYR A CE1 1 
ATOM   961   C  CE2 . TYR A 1 213 ? 111.958 160.988 121.789 1.00 34.39  ? 188  TYR A CE2 1 
ATOM   962   C  CZ  . TYR A 1 213 ? 112.087 160.762 120.438 1.00 35.44  ? 188  TYR A CZ  1 
ATOM   963   O  OH  . TYR A 1 213 ? 111.841 159.510 119.932 1.00 41.06  ? 188  TYR A OH  1 
ATOM   964   N  N   . MET A 1 214 ? 115.397 166.985 123.098 1.00 50.76  ? 189  MET A N   1 
ATOM   965   C  CA  . MET A 1 214 ? 115.498 168.394 123.459 1.00 46.74  ? 189  MET A CA  1 
ATOM   966   C  C   . MET A 1 214 ? 116.931 168.919 123.434 1.00 47.28  ? 189  MET A C   1 
ATOM   967   O  O   . MET A 1 214 ? 117.202 169.968 124.029 1.00 50.51  ? 189  MET A O   1 
ATOM   968   C  CB  . MET A 1 214 ? 114.898 168.631 124.849 1.00 45.55  ? 189  MET A CB  1 
ATOM   969   C  CG  . MET A 1 214 ? 113.385 168.508 124.905 1.00 49.15  ? 189  MET A CG  1 
ATOM   970   S  SD  . MET A 1 214 ? 112.661 169.328 126.338 1.00 68.27  ? 189  MET A SD  1 
ATOM   971   C  CE  . MET A 1 214 ? 114.045 169.320 127.474 1.00 51.25  ? 189  MET A CE  1 
ATOM   972   N  N   . GLU A 1 215 ? 117.855 168.234 122.765 1.00 42.68  ? 190  GLU A N   1 
ATOM   973   C  CA  . GLU A 1 215 ? 119.248 168.660 122.771 1.00 44.86  ? 190  GLU A CA  1 
ATOM   974   C  C   . GLU A 1 215 ? 119.965 168.068 121.566 1.00 50.51  ? 190  GLU A C   1 
ATOM   975   O  O   . GLU A 1 215 ? 119.470 167.149 120.910 1.00 47.53  ? 190  GLU A O   1 
ATOM   976   C  CB  . GLU A 1 215 ? 119.947 168.250 124.072 1.00 41.36  ? 190  GLU A CB  1 
ATOM   977   C  CG  . GLU A 1 215 ? 119.663 166.819 124.508 1.00 46.55  ? 190  GLU A CG  1 
ATOM   978   C  CD  . GLU A 1 215 ? 120.314 165.789 123.604 1.00 51.20  ? 190  GLU A CD  1 
ATOM   979   O  OE1 . GLU A 1 215 ? 121.518 165.933 123.308 1.00 53.70  ? 190  GLU A OE1 1 
ATOM   980   O  OE2 . GLU A 1 215 ? 119.620 164.842 123.181 1.00 51.06  ? 190  GLU A OE2 1 
ATOM   981   N  N   . GLY A 1 216 ? 121.154 168.596 121.300 1.00 49.85  ? 191  GLY A N   1 
ATOM   982   C  CA  . GLY A 1 216 ? 122.026 168.076 120.269 1.00 41.38  ? 191  GLY A CA  1 
ATOM   983   C  C   . GLY A 1 216 ? 121.918 168.851 118.967 1.00 43.70  ? 191  GLY A C   1 
ATOM   984   O  O   . GLY A 1 216 ? 121.067 169.725 118.783 1.00 50.27  ? 191  GLY A O   1 
ATOM   985   N  N   . THR A 1 217 ? 122.818 168.510 118.049 1.00 41.31  ? 192  THR A N   1 
ATOM   986   C  CA  . THR A 1 217 ? 122.845 169.120 116.728 1.00 37.25  ? 192  THR A CA  1 
ATOM   987   C  C   . THR A 1 217 ? 123.591 168.193 115.783 1.00 40.08  ? 192  THR A C   1 
ATOM   988   O  O   . THR A 1 217 ? 124.308 167.286 116.212 1.00 45.92  ? 192  THR A O   1 
ATOM   989   C  CB  . THR A 1 217 ? 123.510 170.498 116.748 1.00 41.39  ? 192  THR A CB  1 
ATOM   990   O  OG1 . THR A 1 217 ? 123.811 170.900 115.407 1.00 44.51  ? 192  THR A OG1 1 
ATOM   991   C  CG2 . THR A 1 217 ? 124.800 170.447 117.545 1.00 46.86  ? 192  THR A CG2 1 
ATOM   992   N  N   . GLY A 1 218 ? 123.411 168.433 114.487 1.00 35.46  ? 193  GLY A N   1 
ATOM   993   C  CA  . GLY A 1 218 ? 124.097 167.639 113.490 1.00 37.10  ? 193  GLY A CA  1 
ATOM   994   C  C   . GLY A 1 218 ? 125.528 168.042 113.219 1.00 41.66  ? 193  GLY A C   1 
ATOM   995   O  O   . GLY A 1 218 ? 126.258 167.287 112.572 1.00 45.20  ? 193  GLY A O   1 
ATOM   996   N  N   . ASN A 1 219 ? 125.948 169.212 113.698 1.00 44.15  ? 194  ASN A N   1 
ATOM   997   C  CA  . ASN A 1 219 ? 127.307 169.681 113.468 1.00 43.26  ? 194  ASN A CA  1 
ATOM   998   C  C   . ASN A 1 219 ? 128.336 168.970 114.335 1.00 43.84  ? 194  ASN A C   1 
ATOM   999   O  O   . ASN A 1 219 ? 129.535 169.090 114.066 1.00 50.44  ? 194  ASN A O   1 
ATOM   1000  C  CB  . ASN A 1 219 ? 127.390 171.190 113.710 1.00 42.50  ? 194  ASN A CB  1 
ATOM   1001  C  CG  . ASN A 1 219 ? 126.230 171.945 113.092 1.00 46.11  ? 194  ASN A CG  1 
ATOM   1002  O  OD1 . ASN A 1 219 ? 125.672 172.855 113.704 1.00 47.28  ? 194  ASN A OD1 1 
ATOM   1003  N  ND2 . ASN A 1 219 ? 125.864 171.574 111.871 1.00 48.31  ? 194  ASN A ND2 1 
ATOM   1004  N  N   . MET A 1 220 ? 127.900 168.243 115.366 1.00 52.05  ? 195  MET A N   1 
ATOM   1005  C  CA  . MET A 1 220 ? 128.842 167.553 116.239 1.00 52.51  ? 195  MET A CA  1 
ATOM   1006  C  C   . MET A 1 220 ? 129.566 166.432 115.505 1.00 52.79  ? 195  MET A C   1 
ATOM   1007  O  O   . MET A 1 220 ? 130.766 166.220 115.713 1.00 58.24  ? 195  MET A O   1 
ATOM   1008  C  CB  . MET A 1 220 ? 128.113 167.002 117.464 1.00 49.49  ? 195  MET A CB  1 
ATOM   1009  C  CG  . MET A 1 220 ? 127.836 168.034 118.539 1.00 53.21  ? 195  MET A CG  1 
ATOM   1010  S  SD  . MET A 1 220 ? 126.992 167.333 119.967 1.00 59.74  ? 195  MET A SD  1 
ATOM   1011  C  CE  . MET A 1 220 ? 126.172 168.785 120.615 1.00 53.64  ? 195  MET A CE  1 
ATOM   1012  N  N   . PHE A 1 221 ? 128.858 165.706 114.645 1.00 48.02  ? 196  PHE A N   1 
ATOM   1013  C  CA  . PHE A 1 221 ? 129.388 164.514 113.993 1.00 46.61  ? 196  PHE A CA  1 
ATOM   1014  C  C   . PHE A 1 221 ? 129.869 164.880 112.595 1.00 49.85  ? 196  PHE A C   1 
ATOM   1015  O  O   . PHE A 1 221 ? 129.061 165.189 111.714 1.00 55.21  ? 196  PHE A O   1 
ATOM   1016  C  CB  . PHE A 1 221 ? 128.328 163.419 113.934 1.00 47.25  ? 196  PHE A CB  1 
ATOM   1017  C  CG  . PHE A 1 221 ? 127.713 163.106 115.263 1.00 50.35  ? 196  PHE A CG  1 
ATOM   1018  C  CD1 . PHE A 1 221 ? 128.384 162.323 116.185 1.00 51.20  ? 196  PHE A CD1 1 
ATOM   1019  C  CD2 . PHE A 1 221 ? 126.466 163.603 115.595 1.00 47.45  ? 196  PHE A CD2 1 
ATOM   1020  C  CE1 . PHE A 1 221 ? 127.820 162.036 117.407 1.00 48.95  ? 196  PHE A CE1 1 
ATOM   1021  C  CE2 . PHE A 1 221 ? 125.897 163.319 116.815 1.00 50.63  ? 196  PHE A CE2 1 
ATOM   1022  C  CZ  . PHE A 1 221 ? 126.573 162.534 117.723 1.00 52.65  ? 196  PHE A CZ  1 
ATOM   1023  N  N   . ASP A 1 222 ? 131.183 164.837 112.392 1.00 51.73  ? 197  ASP A N   1 
ATOM   1024  C  CA  . ASP A 1 222 ? 131.781 165.094 111.083 1.00 50.35  ? 197  ASP A CA  1 
ATOM   1025  C  C   . ASP A 1 222 ? 131.825 163.774 110.327 1.00 55.38  ? 197  ASP A C   1 
ATOM   1026  O  O   . ASP A 1 222 ? 132.753 162.978 110.472 1.00 57.53  ? 197  ASP A O   1 
ATOM   1027  C  CB  . ASP A 1 222 ? 133.166 165.709 111.233 1.00 53.01  ? 197  ASP A CB  1 
ATOM   1028  C  CG  . ASP A 1 222 ? 133.584 166.503 110.014 1.00 59.34  ? 197  ASP A CG  1 
ATOM   1029  O  OD1 . ASP A 1 222 ? 133.047 167.612 109.815 1.00 63.47  ? 197  ASP A OD1 1 
ATOM   1030  O  OD2 . ASP A 1 222 ? 134.450 166.018 109.256 1.00 58.92  ? 197  ASP A OD2 1 
ATOM   1031  N  N   . GLY A 1 223 ? 130.804 163.537 109.507 1.00 48.57  ? 198  GLY A N   1 
ATOM   1032  C  CA  . GLY A 1 223 ? 130.717 162.304 108.753 1.00 46.88  ? 198  GLY A CA  1 
ATOM   1033  C  C   . GLY A 1 223 ? 131.551 162.311 107.490 1.00 50.76  ? 198  GLY A C   1 
ATOM   1034  O  O   . GLY A 1 223 ? 131.069 161.942 106.416 1.00 52.46  ? 198  GLY A O   1 
ATOM   1035  N  N   . SER A 1 224 ? 132.810 162.728 107.607 1.00 53.35  ? 199  SER A N   1 
ATOM   1036  C  CA  . SER A 1 224 ? 133.723 162.767 106.474 1.00 47.72  ? 199  SER A CA  1 
ATOM   1037  C  C   . SER A 1 224 ? 134.617 161.541 106.386 1.00 46.67  ? 199  SER A C   1 
ATOM   1038  O  O   . SER A 1 224 ? 134.973 161.124 105.280 1.00 47.40  ? 199  SER A O   1 
ATOM   1039  C  CB  . SER A 1 224 ? 134.598 164.022 106.543 1.00 46.47  ? 199  SER A CB  1 
ATOM   1040  O  OG  . SER A 1 224 ? 135.303 164.216 105.332 1.00 55.10  ? 199  SER A OG  1 
ATOM   1041  N  N   . VAL A 1 225 ? 134.991 160.960 107.527 1.00 45.56  ? 200  VAL A N   1 
ATOM   1042  C  CA  . VAL A 1 225 ? 135.821 159.761 107.517 1.00 42.01  ? 200  VAL A CA  1 
ATOM   1043  C  C   . VAL A 1 225 ? 135.024 158.566 107.014 1.00 42.63  ? 200  VAL A C   1 
ATOM   1044  O  O   . VAL A 1 225 ? 135.531 157.742 106.244 1.00 50.50  ? 200  VAL A O   1 
ATOM   1045  C  CB  . VAL A 1 225 ? 136.393 159.505 108.920 1.00 41.92  ? 200  VAL A CB  1 
ATOM   1046  C  CG1 . VAL A 1 225 ? 137.633 158.636 108.834 1.00 40.90  ? 200  VAL A CG1 1 
ATOM   1047  C  CG2 . VAL A 1 225 ? 136.682 160.823 109.614 1.00 43.36  ? 200  VAL A CG2 1 
ATOM   1048  N  N   . LEU A 1 226 ? 133.768 158.446 107.449 1.00 40.25  ? 201  LEU A N   1 
ATOM   1049  C  CA  . LEU A 1 226 ? 132.914 157.363 106.976 1.00 36.24  ? 201  LEU A CA  1 
ATOM   1050  C  C   . LEU A 1 226 ? 132.630 157.486 105.486 1.00 45.21  ? 201  LEU A C   1 
ATOM   1051  O  O   . LEU A 1 226 ? 132.531 156.471 104.788 1.00 45.57  ? 201  LEU A O   1 
ATOM   1052  C  CB  . LEU A 1 226 ? 131.608 157.349 107.772 1.00 32.88  ? 201  LEU A CB  1 
ATOM   1053  C  CG  . LEU A 1 226 ? 130.469 156.461 107.271 1.00 37.91  ? 201  LEU A CG  1 
ATOM   1054  C  CD1 . LEU A 1 226 ? 130.849 154.998 107.374 1.00 36.87  ? 201  LEU A CD1 1 
ATOM   1055  C  CD2 . LEU A 1 226 ? 129.198 156.739 108.052 1.00 40.98  ? 201  LEU A CD2 1 
ATOM   1056  N  N   . ALA A 1 227 ? 132.497 158.715 104.983 1.00 43.71  ? 202  ALA A N   1 
ATOM   1057  C  CA  . ALA A 1 227 ? 132.196 158.914 103.570 1.00 39.82  ? 202  ALA A CA  1 
ATOM   1058  C  C   . ALA A 1 227 ? 133.360 158.481 102.686 1.00 45.14  ? 202  ALA A C   1 
ATOM   1059  O  O   . ALA A 1 227 ? 133.166 157.770 101.694 1.00 50.85  ? 202  ALA A O   1 
ATOM   1060  C  CB  . ALA A 1 227 ? 131.844 160.378 103.315 1.00 40.99  ? 202  ALA A CB  1 
ATOM   1061  N  N   . ALA A 1 228 ? 134.579 158.905 103.028 1.00 44.33  ? 203  ALA A N   1 
ATOM   1062  C  CA  . ALA A 1 228 ? 135.733 158.581 102.196 1.00 44.89  ? 203  ALA A CA  1 
ATOM   1063  C  C   . ALA A 1 228 ? 136.065 157.096 102.257 1.00 47.95  ? 203  ALA A C   1 
ATOM   1064  O  O   . ALA A 1 228 ? 136.380 156.483 101.231 1.00 49.99  ? 203  ALA A O   1 
ATOM   1065  C  CB  . ALA A 1 228 ? 136.940 159.414 102.623 1.00 45.02  ? 203  ALA A CB  1 
ATOM   1066  N  N   . TYR A 1 229 ? 136.006 156.505 103.450 1.00 41.15  ? 204  TYR A N   1 
ATOM   1067  C  CA  . TYR A 1 229 ? 136.349 155.095 103.604 1.00 41.43  ? 204  TYR A CA  1 
ATOM   1068  C  C   . TYR A 1 229 ? 135.344 154.201 102.890 1.00 45.99  ? 204  TYR A C   1 
ATOM   1069  O  O   . TYR A 1 229 ? 135.725 153.307 102.126 1.00 56.11  ? 204  TYR A O   1 
ATOM   1070  C  CB  . TYR A 1 229 ? 136.434 154.749 105.091 1.00 36.32  ? 204  TYR A CB  1 
ATOM   1071  C  CG  . TYR A 1 229 ? 136.794 153.313 105.408 1.00 41.22  ? 204  TYR A CG  1 
ATOM   1072  C  CD1 . TYR A 1 229 ? 135.834 152.309 105.375 1.00 41.26  ? 204  TYR A CD1 1 
ATOM   1073  C  CD2 . TYR A 1 229 ? 138.089 152.965 105.760 1.00 43.60  ? 204  TYR A CD2 1 
ATOM   1074  C  CE1 . TYR A 1 229 ? 136.158 151.002 105.669 1.00 42.09  ? 204  TYR A CE1 1 
ATOM   1075  C  CE2 . TYR A 1 229 ? 138.421 151.659 106.057 1.00 43.89  ? 204  TYR A CE2 1 
ATOM   1076  C  CZ  . TYR A 1 229 ? 137.452 150.682 106.010 1.00 41.08  ? 204  TYR A CZ  1 
ATOM   1077  O  OH  . TYR A 1 229 ? 137.777 149.379 106.304 1.00 36.82  ? 204  TYR A OH  1 
ATOM   1078  N  N   . GLY A 1 230 ? 134.057 154.423 103.127 1.00 36.73  ? 205  GLY A N   1 
ATOM   1079  C  CA  . GLY A 1 230 ? 133.028 153.576 102.567 1.00 43.22  ? 205  GLY A CA  1 
ATOM   1080  C  C   . GLY A 1 230 ? 132.539 153.939 101.187 1.00 43.20  ? 205  GLY A C   1 
ATOM   1081  O  O   . GLY A 1 230 ? 131.723 153.201 100.627 1.00 42.87  ? 205  GLY A O   1 
ATOM   1082  N  N   . ASN A 1 231 ? 133.013 155.049 100.617 1.00 46.51  ? 206  ASN A N   1 
ATOM   1083  C  CA  . ASN A 1 231 ? 132.562 155.520 99.307  1.00 51.01  ? 206  ASN A CA  1 
ATOM   1084  C  C   . ASN A 1 231 ? 131.049 155.721 99.278  1.00 49.97  ? 206  ASN A C   1 
ATOM   1085  O  O   . ASN A 1 231 ? 130.377 155.382 98.303  1.00 50.34  ? 206  ASN A O   1 
ATOM   1086  C  CB  . ASN A 1 231 ? 133.005 154.569 98.191  1.00 50.59  ? 206  ASN A CB  1 
ATOM   1087  C  CG  . ASN A 1 231 ? 134.361 154.933 97.619  1.00 55.42  ? 206  ASN A CG  1 
ATOM   1088  O  OD1 . ASN A 1 231 ? 135.066 155.787 98.155  1.00 56.34  ? 206  ASN A OD1 1 
ATOM   1089  N  ND2 . ASN A 1 231 ? 134.733 154.281 96.524  1.00 54.83  ? 206  ASN A ND2 1 
ATOM   1090  N  N   . VAL A 1 232 ? 130.506 156.273 100.363 1.00 44.84  ? 207  VAL A N   1 
ATOM   1091  C  CA  . VAL A 1 232 ? 129.085 156.572 100.468 1.00 44.71  ? 207  VAL A CA  1 
ATOM   1092  C  C   . VAL A 1 232 ? 128.926 158.043 100.829 1.00 40.61  ? 207  VAL A C   1 
ATOM   1093  O  O   . VAL A 1 232 ? 129.837 158.681 101.361 1.00 46.78  ? 207  VAL A O   1 
ATOM   1094  C  CB  . VAL A 1 232 ? 128.366 155.678 101.500 1.00 38.98  ? 207  VAL A CB  1 
ATOM   1095  C  CG1 . VAL A 1 232 ? 128.669 154.213 101.243 1.00 38.30  ? 207  VAL A CG1 1 
ATOM   1096  C  CG2 . VAL A 1 232 ? 128.769 156.065 102.910 1.00 38.45  ? 207  VAL A CG2 1 
ATOM   1097  N  N   . ILE A 1 233 ? 127.751 158.582 100.523 1.00 32.92  ? 208  ILE A N   1 
ATOM   1098  C  CA  . ILE A 1 233 ? 127.441 159.981 100.792 1.00 40.60  ? 208  ILE A CA  1 
ATOM   1099  C  C   . ILE A 1 233 ? 126.738 160.052 102.141 1.00 45.09  ? 208  ILE A C   1 
ATOM   1100  O  O   . ILE A 1 233 ? 125.620 159.557 102.292 1.00 54.48  ? 208  ILE A O   1 
ATOM   1101  C  CB  . ILE A 1 233 ? 126.571 160.587 99.686  1.00 43.21  ? 208  ILE A CB  1 
ATOM   1102  C  CG1 . ILE A 1 233 ? 127.266 160.465 98.332  1.00 43.15  ? 208  ILE A CG1 1 
ATOM   1103  C  CG2 . ILE A 1 233 ? 126.261 162.041 99.989  1.00 40.05  ? 208  ILE A CG2 1 
ATOM   1104  C  CD1 . ILE A 1 233 ? 126.579 161.232 97.233  1.00 42.09  ? 208  ILE A CD1 1 
ATOM   1105  N  N   . VAL A 1 234 ? 127.378 160.688 103.118 1.00 41.60  ? 209  VAL A N   1 
ATOM   1106  C  CA  . VAL A 1 234 ? 126.830 160.812 104.463 1.00 37.18  ? 209  VAL A CA  1 
ATOM   1107  C  C   . VAL A 1 234 ? 126.155 162.169 104.592 1.00 37.94  ? 209  VAL A C   1 
ATOM   1108  O  O   . VAL A 1 234 ? 126.739 163.201 104.236 1.00 44.51  ? 209  VAL A O   1 
ATOM   1109  C  CB  . VAL A 1 234 ? 127.923 160.634 105.530 1.00 36.90  ? 209  VAL A CB  1 
ATOM   1110  C  CG1 . VAL A 1 234 ? 127.302 160.566 106.912 1.00 37.58  ? 209  VAL A CG1 1 
ATOM   1111  C  CG2 . VAL A 1 234 ? 128.730 159.383 105.249 1.00 36.66  ? 209  VAL A CG2 1 
ATOM   1112  N  N   . VAL A 1 235 ? 124.924 162.167 105.099 1.00 31.63  ? 210  VAL A N   1 
ATOM   1113  C  CA  . VAL A 1 235 ? 124.128 163.374 105.275 1.00 34.39  ? 210  VAL A CA  1 
ATOM   1114  C  C   . VAL A 1 235 ? 123.774 163.500 106.749 1.00 35.27  ? 210  VAL A C   1 
ATOM   1115  O  O   . VAL A 1 235 ? 123.367 162.517 107.381 1.00 48.76  ? 210  VAL A O   1 
ATOM   1116  C  CB  . VAL A 1 235 ? 122.856 163.348 104.409 1.00 35.20  ? 210  VAL A CB  1 
ATOM   1117  C  CG1 . VAL A 1 235 ? 122.145 164.688 104.471 1.00 33.83  ? 210  VAL A CG1 1 
ATOM   1118  C  CG2 . VAL A 1 235 ? 123.199 162.989 102.975 1.00 34.84  ? 210  VAL A CG2 1 
ATOM   1119  N  N   . THR A 1 236 ? 123.950 164.700 107.296 1.00 31.50  ? 211  THR A N   1 
ATOM   1120  C  CA  . THR A 1 236 ? 123.621 164.982 108.687 1.00 34.26  ? 211  THR A CA  1 
ATOM   1121  C  C   . THR A 1 236 ? 122.809 166.266 108.747 1.00 42.07  ? 211  THR A C   1 
ATOM   1122  O  O   . THR A 1 236 ? 123.244 167.298 108.232 1.00 43.78  ? 211  THR A O   1 
ATOM   1123  C  CB  . THR A 1 236 ? 124.885 165.109 109.540 1.00 35.23  ? 211  THR A CB  1 
ATOM   1124  O  OG1 . THR A 1 236 ? 125.764 164.015 109.254 1.00 35.22  ? 211  THR A OG1 1 
ATOM   1125  C  CG2 . THR A 1 236 ? 124.527 165.076 111.009 1.00 43.81  ? 211  THR A CG2 1 
ATOM   1126  N  N   . LEU A 1 237 ? 121.645 166.210 109.383 1.00 42.80  ? 212  LEU A N   1 
ATOM   1127  C  CA  . LEU A 1 237 ? 120.674 167.292 109.315 1.00 36.42  ? 212  LEU A CA  1 
ATOM   1128  C  C   . LEU A 1 237 ? 120.478 167.936 110.681 1.00 36.11  ? 212  LEU A C   1 
ATOM   1129  O  O   . LEU A 1 237 ? 120.926 167.428 111.711 1.00 42.89  ? 212  LEU A O   1 
ATOM   1130  C  CB  . LEU A 1 237 ? 119.326 166.785 108.785 1.00 33.91  ? 212  LEU A CB  1 
ATOM   1131  C  CG  . LEU A 1 237 ? 118.369 166.198 109.827 1.00 28.20  ? 212  LEU A CG  1 
ATOM   1132  C  CD1 . LEU A 1 237 ? 116.973 166.066 109.256 1.00 38.09  ? 212  LEU A CD1 1 
ATOM   1133  C  CD2 . LEU A 1 237 ? 118.861 164.856 110.332 1.00 22.49  ? 212  LEU A CD2 1 
ATOM   1134  N  N   . ASN A 1 238 ? 119.798 169.081 110.670 1.00 32.22  ? 213  ASN A N   1 
ATOM   1135  C  CA  . ASN A 1 238 ? 119.319 169.739 111.879 1.00 32.00  ? 213  ASN A CA  1 
ATOM   1136  C  C   . ASN A 1 238 ? 117.805 169.854 111.782 1.00 36.37  ? 213  ASN A C   1 
ATOM   1137  O  O   . ASN A 1 238 ? 117.285 170.430 110.821 1.00 41.50  ? 213  ASN A O   1 
ATOM   1138  C  CB  . ASN A 1 238 ? 119.952 171.121 112.050 1.00 34.56  ? 213  ASN A CB  1 
ATOM   1139  C  CG  . ASN A 1 238 ? 121.436 171.052 112.336 1.00 43.56  ? 213  ASN A CG  1 
ATOM   1140  O  OD1 . ASN A 1 238 ? 121.870 171.254 113.469 1.00 50.76  ? 213  ASN A OD1 1 
ATOM   1141  N  ND2 . ASN A 1 238 ? 122.225 170.771 111.307 1.00 43.99  ? 213  ASN A ND2 1 
ATOM   1142  N  N   . TYR A 1 239 ? 117.104 169.308 112.769 1.00 37.03  ? 214  TYR A N   1 
ATOM   1143  C  CA  . TYR A 1 239 ? 115.651 169.338 112.805 1.00 33.66  ? 214  TYR A CA  1 
ATOM   1144  C  C   . TYR A 1 239 ? 115.190 169.965 114.112 1.00 37.93  ? 214  TYR A C   1 
ATOM   1145  O  O   . TYR A 1 239 ? 115.928 170.003 115.098 1.00 43.44  ? 214  TYR A O   1 
ATOM   1146  C  CB  . TYR A 1 239 ? 115.056 167.931 112.646 1.00 37.32  ? 214  TYR A CB  1 
ATOM   1147  C  CG  . TYR A 1 239 ? 115.426 166.962 113.748 1.00 37.60  ? 214  TYR A CG  1 
ATOM   1148  C  CD1 . TYR A 1 239 ? 114.644 166.844 114.890 1.00 39.14  ? 214  TYR A CD1 1 
ATOM   1149  C  CD2 . TYR A 1 239 ? 116.554 166.162 113.644 1.00 37.45  ? 214  TYR A CD2 1 
ATOM   1150  C  CE1 . TYR A 1 239 ? 114.979 165.961 115.896 1.00 41.69  ? 214  TYR A CE1 1 
ATOM   1151  C  CE2 . TYR A 1 239 ? 116.896 165.276 114.645 1.00 33.59  ? 214  TYR A CE2 1 
ATOM   1152  C  CZ  . TYR A 1 239 ? 116.105 165.179 115.768 1.00 33.93  ? 214  TYR A CZ  1 
ATOM   1153  O  OH  . TYR A 1 239 ? 116.442 164.297 116.769 1.00 36.34  ? 214  TYR A OH  1 
ATOM   1154  N  N   . ARG A 1 240 ? 113.957 170.465 114.108 1.00 39.96  ? 215  ARG A N   1 
ATOM   1155  C  CA  . ARG A 1 240 ? 113.421 171.146 115.278 1.00 39.63  ? 215  ARG A CA  1 
ATOM   1156  C  C   . ARG A 1 240 ? 113.320 170.187 116.458 1.00 42.20  ? 215  ARG A C   1 
ATOM   1157  O  O   . ARG A 1 240 ? 112.840 169.060 116.316 1.00 47.47  ? 215  ARG A O   1 
ATOM   1158  C  CB  . ARG A 1 240 ? 112.049 171.733 114.954 1.00 41.28  ? 215  ARG A CB  1 
ATOM   1159  C  CG  . ARG A 1 240 ? 112.093 172.940 114.036 1.00 41.56  ? 215  ARG A CG  1 
ATOM   1160  C  CD  . ARG A 1 240 ? 110.702 173.490 113.788 1.00 40.23  ? 215  ARG A CD  1 
ATOM   1161  N  NE  . ARG A 1 240 ? 110.008 172.754 112.740 1.00 41.99  ? 215  ARG A NE  1 
ATOM   1162  C  CZ  . ARG A 1 240 ? 108.748 172.966 112.386 1.00 45.06  ? 215  ARG A CZ  1 
ATOM   1163  N  NH1 . ARG A 1 240 ? 108.011 173.891 112.978 1.00 44.63  ? 215  ARG A NH1 1 
ATOM   1164  N  NH2 . ARG A 1 240 ? 108.215 172.232 111.414 1.00 45.89  ? 215  ARG A NH2 1 
ATOM   1165  N  N   . LEU A 1 241 ? 113.772 170.638 117.626 1.00 43.46  ? 216  LEU A N   1 
ATOM   1166  C  CA  . LEU A 1 241 ? 113.732 169.830 118.835 1.00 41.56  ? 216  LEU A CA  1 
ATOM   1167  C  C   . LEU A 1 241 ? 113.006 170.586 119.937 1.00 46.64  ? 216  LEU A C   1 
ATOM   1168  O  O   . LEU A 1 241 ? 112.858 171.809 119.890 1.00 46.52  ? 216  LEU A O   1 
ATOM   1169  C  CB  . LEU A 1 241 ? 115.133 169.448 119.338 1.00 38.82  ? 216  LEU A CB  1 
ATOM   1170  C  CG  . LEU A 1 241 ? 116.230 169.024 118.365 1.00 41.81  ? 216  LEU A CG  1 
ATOM   1171  C  CD1 . LEU A 1 241 ? 117.062 170.225 117.957 1.00 42.96  ? 216  LEU A CD1 1 
ATOM   1172  C  CD2 . LEU A 1 241 ? 117.100 167.944 118.973 1.00 44.89  ? 216  LEU A CD2 1 
ATOM   1173  N  N   . GLY A 1 242 ? 112.561 169.832 120.940 1.00 41.66  ? 217  GLY A N   1 
ATOM   1174  C  CA  . GLY A 1 242 ? 111.977 170.434 122.119 1.00 40.00  ? 217  GLY A CA  1 
ATOM   1175  C  C   . GLY A 1 242 ? 110.632 171.084 121.845 1.00 44.47  ? 217  GLY A C   1 
ATOM   1176  O  O   . GLY A 1 242 ? 109.847 170.639 121.001 1.00 47.84  ? 217  GLY A O   1 
ATOM   1177  N  N   . VAL A 1 243 ? 110.378 172.172 122.574 1.00 49.77  ? 218  VAL A N   1 
ATOM   1178  C  CA  . VAL A 1 243 ? 109.084 172.846 122.512 1.00 50.23  ? 218  VAL A CA  1 
ATOM   1179  C  C   . VAL A 1 243 ? 108.763 173.277 121.089 1.00 49.65  ? 218  VAL A C   1 
ATOM   1180  O  O   . VAL A 1 243 ? 107.633 173.112 120.614 1.00 50.58  ? 218  VAL A O   1 
ATOM   1181  C  CB  . VAL A 1 243 ? 109.066 174.046 123.473 1.00 46.73  ? 218  VAL A CB  1 
ATOM   1182  C  CG1 . VAL A 1 243 ? 107.675 174.621 123.546 1.00 48.20  ? 218  VAL A CG1 1 
ATOM   1183  C  CG2 . VAL A 1 243 ? 109.553 173.628 124.851 1.00 50.59  ? 218  VAL A CG2 1 
ATOM   1184  N  N   . LEU A 1 244 ? 109.747 173.833 120.385 1.00 46.00  ? 219  LEU A N   1 
ATOM   1185  C  CA  . LEU A 1 244 ? 109.514 174.324 119.035 1.00 45.03  ? 219  LEU A CA  1 
ATOM   1186  C  C   . LEU A 1 244 ? 109.309 173.204 118.025 1.00 46.45  ? 219  LEU A C   1 
ATOM   1187  O  O   . LEU A 1 244 ? 108.933 173.491 116.884 1.00 53.43  ? 219  LEU A O   1 
ATOM   1188  C  CB  . LEU A 1 244 ? 110.679 175.211 118.596 1.00 46.77  ? 219  LEU A CB  1 
ATOM   1189  C  CG  . LEU A 1 244 ? 110.801 176.544 119.335 1.00 47.53  ? 219  LEU A CG  1 
ATOM   1190  C  CD1 . LEU A 1 244 ? 111.945 177.366 118.771 1.00 53.70  ? 219  LEU A CD1 1 
ATOM   1191  C  CD2 . LEU A 1 244 ? 109.495 177.318 119.265 1.00 47.61  ? 219  LEU A CD2 1 
ATOM   1192  N  N   . GLY A 1 245 ? 109.538 171.950 118.406 1.00 38.91  ? 220  GLY A N   1 
ATOM   1193  C  CA  . GLY A 1 245 ? 109.470 170.871 117.442 1.00 41.97  ? 220  GLY A CA  1 
ATOM   1194  C  C   . GLY A 1 245 ? 108.538 169.730 117.791 1.00 43.33  ? 220  GLY A C   1 
ATOM   1195  O  O   . GLY A 1 245 ? 108.197 168.927 116.919 1.00 46.46  ? 220  GLY A O   1 
ATOM   1196  N  N   . PHE A 1 246 ? 108.119 169.632 119.054 1.00 43.53  ? 221  PHE A N   1 
ATOM   1197  C  CA  . PHE A 1 246 ? 107.309 168.492 119.467 1.00 41.88  ? 221  PHE A CA  1 
ATOM   1198  C  C   . PHE A 1 246 ? 106.131 168.869 120.358 1.00 45.54  ? 221  PHE A C   1 
ATOM   1199  O  O   . PHE A 1 246 ? 105.475 167.969 120.897 1.00 40.96  ? 221  PHE A O   1 
ATOM   1200  C  CB  . PHE A 1 246 ? 108.183 167.454 120.177 1.00 40.02  ? 221  PHE A CB  1 
ATOM   1201  C  CG  . PHE A 1 246 ? 109.110 166.713 119.257 1.00 36.77  ? 221  PHE A CG  1 
ATOM   1202  C  CD1 . PHE A 1 246 ? 108.610 165.864 118.287 1.00 38.48  ? 221  PHE A CD1 1 
ATOM   1203  C  CD2 . PHE A 1 246 ? 110.481 166.867 119.361 1.00 41.65  ? 221  PHE A CD2 1 
ATOM   1204  C  CE1 . PHE A 1 246 ? 109.459 165.182 117.440 1.00 38.04  ? 221  PHE A CE1 1 
ATOM   1205  C  CE2 . PHE A 1 246 ? 111.333 166.187 118.517 1.00 42.24  ? 221  PHE A CE2 1 
ATOM   1206  C  CZ  . PHE A 1 246 ? 110.821 165.344 117.555 1.00 37.26  ? 221  PHE A CZ  1 
ATOM   1207  N  N   . LEU A 1 247 ? 105.841 170.155 120.536 1.00 51.55  ? 222  LEU A N   1 
ATOM   1208  C  CA  . LEU A 1 247 ? 104.699 170.558 121.345 1.00 50.70  ? 222  LEU A CA  1 
ATOM   1209  C  C   . LEU A 1 247 ? 103.398 170.126 120.679 1.00 55.48  ? 222  LEU A C   1 
ATOM   1210  O  O   . LEU A 1 247 ? 103.233 170.252 119.463 1.00 60.58  ? 222  LEU A O   1 
ATOM   1211  C  CB  . LEU A 1 247 ? 104.711 172.072 121.557 1.00 50.16  ? 222  LEU A CB  1 
ATOM   1212  C  CG  . LEU A 1 247 ? 103.507 172.720 122.243 1.00 50.46  ? 222  LEU A CG  1 
ATOM   1213  C  CD1 . LEU A 1 247 ? 103.979 173.738 123.267 1.00 51.53  ? 222  LEU A CD1 1 
ATOM   1214  C  CD2 . LEU A 1 247 ? 102.590 173.378 121.225 1.00 52.08  ? 222  LEU A CD2 1 
ATOM   1215  N  N   . SER A 1 248 ? 102.470 169.614 121.485 1.00 60.62  ? 223  SER A N   1 
ATOM   1216  C  CA  . SER A 1 248 ? 101.192 169.148 120.969 1.00 63.45  ? 223  SER A CA  1 
ATOM   1217  C  C   . SER A 1 248 ? 100.136 169.256 122.056 1.00 64.22  ? 223  SER A C   1 
ATOM   1218  O  O   . SER A 1 248 ? 100.445 169.321 123.248 1.00 65.12  ? 223  SER A O   1 
ATOM   1219  C  CB  . SER A 1 248 ? 101.282 167.705 120.460 1.00 64.25  ? 223  SER A CB  1 
ATOM   1220  O  OG  . SER A 1 248 ? 99.992  167.159 120.251 1.00 66.60  ? 223  SER A OG  1 
ATOM   1221  N  N   . THR A 1 249 ? 98.874  169.271 121.625 1.00 79.25  ? 224  THR A N   1 
ATOM   1222  C  CA  . THR A 1 249 ? 97.739  169.338 122.533 1.00 79.44  ? 224  THR A CA  1 
ATOM   1223  C  C   . THR A 1 249 ? 96.753  168.192 122.363 1.00 78.54  ? 224  THR A C   1 
ATOM   1224  O  O   . THR A 1 249 ? 95.872  168.031 123.214 1.00 80.25  ? 224  THR A O   1 
ATOM   1225  C  CB  . THR A 1 249 ? 96.984  170.665 122.358 1.00 78.95  ? 224  THR A CB  1 
ATOM   1226  O  OG1 . THR A 1 249 ? 96.655  170.852 120.977 1.00 80.32  ? 224  THR A OG1 1 
ATOM   1227  C  CG2 . THR A 1 249 ? 97.834  171.831 122.833 1.00 75.40  ? 224  THR A CG2 1 
ATOM   1228  N  N   . GLY A 1 250 ? 96.869  167.400 121.301 1.00 86.03  ? 225  GLY A N   1 
ATOM   1229  C  CA  . GLY A 1 250 ? 95.960  166.294 121.079 1.00 88.32  ? 225  GLY A CA  1 
ATOM   1230  C  C   . GLY A 1 250 ? 94.946  166.568 119.988 1.00 91.05  ? 225  GLY A C   1 
ATOM   1231  O  O   . GLY A 1 250 ? 94.616  165.677 119.200 1.00 90.05  ? 225  GLY A O   1 
ATOM   1232  N  N   . ASP A 1 251 ? 94.446  167.799 119.932 1.00 102.76 ? 226  ASP A N   1 
ATOM   1233  C  CA  . ASP A 1 251 ? 93.454  168.188 118.942 1.00 103.12 ? 226  ASP A CA  1 
ATOM   1234  C  C   . ASP A 1 251 ? 94.154  168.699 117.684 1.00 102.01 ? 226  ASP A C   1 
ATOM   1235  O  O   . ASP A 1 251 ? 95.367  168.550 117.514 1.00 101.21 ? 226  ASP A O   1 
ATOM   1236  C  CB  . ASP A 1 251 ? 92.500  169.226 119.530 1.00 103.27 ? 226  ASP A CB  1 
ATOM   1237  C  CG  . ASP A 1 251 ? 93.227  170.354 120.232 1.00 104.46 ? 226  ASP A CG  1 
ATOM   1238  O  OD1 . ASP A 1 251 ? 94.476  170.337 120.255 1.00 104.21 ? 226  ASP A OD1 1 
ATOM   1239  O  OD2 . ASP A 1 251 ? 92.549  171.259 120.761 1.00 105.73 ? 226  ASP A OD2 1 
ATOM   1240  N  N   . GLN A 1 252 ? 93.388  169.312 116.781 1.00 107.48 ? 227  GLN A N   1 
ATOM   1241  C  CA  . GLN A 1 252 ? 93.935  169.802 115.523 1.00 107.21 ? 227  GLN A CA  1 
ATOM   1242  C  C   . GLN A 1 252 ? 94.607  171.162 115.650 1.00 107.82 ? 227  GLN A C   1 
ATOM   1243  O  O   . GLN A 1 252 ? 95.191  171.636 114.669 1.00 107.29 ? 227  GLN A O   1 
ATOM   1244  C  CB  . GLN A 1 252 ? 92.831  169.874 114.465 1.00 107.25 ? 227  GLN A CB  1 
ATOM   1245  C  CG  . GLN A 1 252 ? 92.090  168.565 114.255 1.00 109.42 ? 227  GLN A CG  1 
ATOM   1246  C  CD  . GLN A 1 252 ? 92.450  167.895 112.945 1.00 109.18 ? 227  GLN A CD  1 
ATOM   1247  O  OE1 . GLN A 1 252 ? 93.249  168.417 112.166 1.00 108.51 ? 227  GLN A OE1 1 
ATOM   1248  N  NE2 . GLN A 1 252 ? 91.862  166.731 112.693 1.00 108.07 ? 227  GLN A NE2 1 
ATOM   1249  N  N   . ALA A 1 253 ? 94.532  171.804 116.819 1.00 103.08 ? 228  ALA A N   1 
ATOM   1250  C  CA  . ALA A 1 253 ? 95.205  173.087 116.999 1.00 103.12 ? 228  ALA A CA  1 
ATOM   1251  C  C   . ALA A 1 253 ? 96.715  172.941 116.866 1.00 101.81 ? 228  ALA A C   1 
ATOM   1252  O  O   . ALA A 1 253 ? 97.371  173.758 116.210 1.00 100.43 ? 228  ALA A O   1 
ATOM   1253  C  CB  . ALA A 1 253 ? 94.839  173.686 118.356 1.00 102.14 ? 228  ALA A CB  1 
ATOM   1254  N  N   . ALA A 1 254 ? 97.283  171.903 117.481 1.00 84.27  ? 229  ALA A N   1 
ATOM   1255  C  CA  . ALA A 1 254 ? 98.714  171.611 117.364 1.00 81.51  ? 229  ALA A CA  1 
ATOM   1256  C  C   . ALA A 1 254 ? 98.866  170.092 117.454 1.00 76.78  ? 229  ALA A C   1 
ATOM   1257  O  O   . ALA A 1 254 ? 98.933  169.527 118.548 1.00 78.36  ? 229  ALA A O   1 
ATOM   1258  C  CB  . ALA A 1 254 ? 99.524  172.325 118.435 1.00 78.37  ? 229  ALA A CB  1 
ATOM   1259  N  N   . LYS A 1 255 ? 98.910  169.443 116.289 1.00 64.62  ? 230  LYS A N   1 
ATOM   1260  C  CA  . LYS A 1 255 ? 99.002  167.987 116.256 1.00 65.49  ? 230  LYS A CA  1 
ATOM   1261  C  C   . LYS A 1 255 ? 100.320 167.498 116.844 1.00 65.12  ? 230  LYS A C   1 
ATOM   1262  O  O   . LYS A 1 255 ? 100.349 166.507 117.582 1.00 65.04  ? 230  LYS A O   1 
ATOM   1263  C  CB  . LYS A 1 255 ? 98.833  167.484 114.823 1.00 68.53  ? 230  LYS A CB  1 
ATOM   1264  C  CG  . LYS A 1 255 ? 97.389  167.234 114.420 1.00 67.93  ? 230  LYS A CG  1 
ATOM   1265  C  CD  . LYS A 1 255 ? 97.300  166.652 113.019 1.00 67.48  ? 230  LYS A CD  1 
ATOM   1266  C  CE  . LYS A 1 255 ? 95.983  165.927 112.804 1.00 68.46  ? 230  LYS A CE  1 
ATOM   1267  N  NZ  . LYS A 1 255 ? 95.903  164.673 113.601 1.00 65.84  ? 230  LYS A NZ  1 
ATOM   1268  N  N   . GLY A 1 256 ? 101.416 168.175 116.530 1.00 53.31  ? 231  GLY A N   1 
ATOM   1269  C  CA  . GLY A 1 256 ? 102.719 167.792 117.032 1.00 55.42  ? 231  GLY A CA  1 
ATOM   1270  C  C   . GLY A 1 256 ? 103.539 167.043 116.002 1.00 57.30  ? 231  GLY A C   1 
ATOM   1271  O  O   . GLY A 1 256 ? 103.224 166.999 114.809 1.00 58.22  ? 231  GLY A O   1 
ATOM   1272  N  N   . ASN A 1 257 ? 104.624 166.443 116.495 1.00 44.80  ? 232  ASN A N   1 
ATOM   1273  C  CA  . ASN A 1 257 ? 105.549 165.665 115.669 1.00 35.51  ? 232  ASN A CA  1 
ATOM   1274  C  C   . ASN A 1 257 ? 106.117 166.502 114.525 1.00 43.98  ? 232  ASN A C   1 
ATOM   1275  O  O   . ASN A 1 257 ? 106.254 166.030 113.395 1.00 49.74  ? 232  ASN A O   1 
ATOM   1276  C  CB  . ASN A 1 257 ? 104.880 164.399 115.130 1.00 34.67  ? 232  ASN A CB  1 
ATOM   1277  C  CG  . ASN A 1 257 ? 104.338 163.517 116.229 1.00 43.38  ? 232  ASN A CG  1 
ATOM   1278  O  OD1 . ASN A 1 257 ? 103.961 163.998 117.296 1.00 51.16  ? 232  ASN A OD1 1 
ATOM   1279  N  ND2 . ASN A 1 257 ? 104.291 162.216 115.975 1.00 41.71  ? 232  ASN A ND2 1 
ATOM   1280  N  N   . TYR A 1 258 ? 106.451 167.760 114.818 1.00 46.21  ? 233  TYR A N   1 
ATOM   1281  C  CA  . TYR A 1 258 ? 107.056 168.606 113.796 1.00 44.14  ? 233  TYR A CA  1 
ATOM   1282  C  C   . TYR A 1 258 ? 108.490 168.188 113.498 1.00 42.20  ? 233  TYR A C   1 
ATOM   1283  O  O   . TYR A 1 258 ? 108.962 168.372 112.372 1.00 49.37  ? 233  TYR A O   1 
ATOM   1284  C  CB  . TYR A 1 258 ? 107.001 170.073 114.221 1.00 46.46  ? 233  TYR A CB  1 
ATOM   1285  C  CG  . TYR A 1 258 ? 105.617 170.541 114.606 1.00 49.52  ? 233  TYR A CG  1 
ATOM   1286  C  CD1 . TYR A 1 258 ? 104.575 170.513 113.691 1.00 50.60  ? 233  TYR A CD1 1 
ATOM   1287  C  CD2 . TYR A 1 258 ? 105.353 171.012 115.884 1.00 47.66  ? 233  TYR A CD2 1 
ATOM   1288  C  CE1 . TYR A 1 258 ? 103.310 170.938 114.036 1.00 48.55  ? 233  TYR A CE1 1 
ATOM   1289  C  CE2 . TYR A 1 258 ? 104.090 171.440 116.239 1.00 46.89  ? 233  TYR A CE2 1 
ATOM   1290  C  CZ  . TYR A 1 258 ? 103.073 171.401 115.311 1.00 50.76  ? 233  TYR A CZ  1 
ATOM   1291  O  OH  . TYR A 1 258 ? 101.813 171.826 115.658 1.00 56.25  ? 233  TYR A OH  1 
ATOM   1292  N  N   . GLY A 1 259 ? 109.195 167.626 114.480 1.00 33.12  ? 234  GLY A N   1 
ATOM   1293  C  CA  . GLY A 1 259 ? 110.535 167.126 114.218 1.00 35.50  ? 234  GLY A CA  1 
ATOM   1294  C  C   . GLY A 1 259 ? 110.543 165.961 113.247 1.00 39.59  ? 234  GLY A C   1 
ATOM   1295  O  O   . GLY A 1 259 ? 111.388 165.892 112.349 1.00 47.07  ? 234  GLY A O   1 
ATOM   1296  N  N   . LEU A 1 260 ? 109.602 165.028 113.411 1.00 29.83  ? 235  LEU A N   1 
ATOM   1297  C  CA  . LEU A 1 260 ? 109.498 163.915 112.475 1.00 27.31  ? 235  LEU A CA  1 
ATOM   1298  C  C   . LEU A 1 260 ? 109.135 164.407 111.081 1.00 29.89  ? 235  LEU A C   1 
ATOM   1299  O  O   . LEU A 1 260 ? 109.635 163.885 110.079 1.00 38.09  ? 235  LEU A O   1 
ATOM   1300  C  CB  . LEU A 1 260 ? 108.469 162.901 112.974 1.00 27.28  ? 235  LEU A CB  1 
ATOM   1301  C  CG  . LEU A 1 260 ? 108.771 162.190 114.296 1.00 29.16  ? 235  LEU A CG  1 
ATOM   1302  C  CD1 . LEU A 1 260 ? 107.924 160.939 114.434 1.00 31.39  ? 235  LEU A CD1 1 
ATOM   1303  C  CD2 . LEU A 1 260 ? 110.243 161.850 114.404 1.00 32.71  ? 235  LEU A CD2 1 
ATOM   1304  N  N   . LEU A 1 261 ? 108.265 165.415 110.997 1.00 25.17  ? 236  LEU A N   1 
ATOM   1305  C  CA  . LEU A 1 261 ? 107.924 165.987 109.699 1.00 29.78  ? 236  LEU A CA  1 
ATOM   1306  C  C   . LEU A 1 261 ? 109.127 166.671 109.059 1.00 33.60  ? 236  LEU A C   1 
ATOM   1307  O  O   . LEU A 1 261 ? 109.308 166.600 107.840 1.00 40.08  ? 236  LEU A O   1 
ATOM   1308  C  CB  . LEU A 1 261 ? 106.757 166.962 109.845 1.00 31.00  ? 236  LEU A CB  1 
ATOM   1309  C  CG  . LEU A 1 261 ? 105.415 166.319 110.198 1.00 31.20  ? 236  LEU A CG  1 
ATOM   1310  C  CD1 . LEU A 1 261 ? 104.384 167.376 110.550 1.00 34.92  ? 236  LEU A CD1 1 
ATOM   1311  C  CD2 . LEU A 1 261 ? 104.926 165.450 109.052 1.00 30.29  ? 236  LEU A CD2 1 
ATOM   1312  N  N   . ASP A 1 262 ? 109.962 167.337 109.862 1.00 36.43  ? 237  ASP A N   1 
ATOM   1313  C  CA  . ASP A 1 262 ? 111.186 167.926 109.324 1.00 36.16  ? 237  ASP A CA  1 
ATOM   1314  C  C   . ASP A 1 262 ? 112.144 166.852 108.821 1.00 39.94  ? 237  ASP A C   1 
ATOM   1315  O  O   . ASP A 1 262 ? 112.784 167.021 107.777 1.00 47.91  ? 237  ASP A O   1 
ATOM   1316  C  CB  . ASP A 1 262 ? 111.864 168.793 110.384 1.00 38.23  ? 237  ASP A CB  1 
ATOM   1317  C  CG  . ASP A 1 262 ? 111.011 169.971 110.806 1.00 50.12  ? 237  ASP A CG  1 
ATOM   1318  O  OD1 . ASP A 1 262 ? 109.868 170.082 110.319 1.00 45.81  ? 237  ASP A OD1 1 
ATOM   1319  O  OD2 . ASP A 1 262 ? 111.481 170.787 111.626 1.00 50.37  ? 237  ASP A OD2 1 
ATOM   1320  N  N   . GLN A 1 263 ? 112.258 165.743 109.555 1.00 33.81  ? 238  GLN A N   1 
ATOM   1321  C  CA  . GLN A 1 263 ? 113.097 164.639 109.095 1.00 26.48  ? 238  GLN A CA  1 
ATOM   1322  C  C   . GLN A 1 263 ? 112.574 164.058 107.786 1.00 31.62  ? 238  GLN A C   1 
ATOM   1323  O  O   . GLN A 1 263 ? 113.353 163.742 106.879 1.00 35.46  ? 238  GLN A O   1 
ATOM   1324  C  CB  . GLN A 1 263 ? 113.175 163.555 110.168 1.00 21.56  ? 238  GLN A CB  1 
ATOM   1325  C  CG  . GLN A 1 263 ? 114.114 163.886 111.310 1.00 32.27  ? 238  GLN A CG  1 
ATOM   1326  C  CD  . GLN A 1 263 ? 113.863 163.027 112.529 1.00 32.08  ? 238  GLN A CD  1 
ATOM   1327  O  OE1 . GLN A 1 263 ? 112.922 162.236 112.559 1.00 37.00  ? 238  GLN A OE1 1 
ATOM   1328  N  NE2 . GLN A 1 263 ? 114.701 163.181 113.545 1.00 31.18  ? 238  GLN A NE2 1 
ATOM   1329  N  N   . ILE A 1 264 ? 111.254 163.914 107.670 1.00 29.68  ? 239  ILE A N   1 
ATOM   1330  C  CA  . ILE A 1 264 ? 110.666 163.398 106.438 1.00 25.15  ? 239  ILE A CA  1 
ATOM   1331  C  C   . ILE A 1 264 ? 110.873 164.383 105.292 1.00 31.67  ? 239  ILE A C   1 
ATOM   1332  O  O   . ILE A 1 264 ? 111.092 163.982 104.145 1.00 34.56  ? 239  ILE A O   1 
ATOM   1333  C  CB  . ILE A 1 264 ? 109.178 163.072 106.659 1.00 25.84  ? 239  ILE A CB  1 
ATOM   1334  C  CG1 . ILE A 1 264 ? 109.038 161.894 107.623 1.00 27.72  ? 239  ILE A CG1 1 
ATOM   1335  C  CG2 . ILE A 1 264 ? 108.493 162.753 105.343 1.00 32.68  ? 239  ILE A CG2 1 
ATOM   1336  C  CD1 . ILE A 1 264 ? 107.611 161.557 107.973 1.00 28.60  ? 239  ILE A CD1 1 
ATOM   1337  N  N   . GLN A 1 265 ? 110.813 165.685 105.581 1.00 33.44  ? 240  GLN A N   1 
ATOM   1338  C  CA  . GLN A 1 265 ? 111.087 166.685 104.553 1.00 31.09  ? 240  GLN A CA  1 
ATOM   1339  C  C   . GLN A 1 265 ? 112.532 166.605 104.079 1.00 34.62  ? 240  GLN A C   1 
ATOM   1340  O  O   . GLN A 1 265 ? 112.810 166.739 102.882 1.00 43.01  ? 240  GLN A O   1 
ATOM   1341  C  CB  . GLN A 1 265 ? 110.775 168.083 105.082 1.00 30.82  ? 240  GLN A CB  1 
ATOM   1342  C  CG  . GLN A 1 265 ? 109.775 168.855 104.240 1.00 40.54  ? 240  GLN A CG  1 
ATOM   1343  C  CD  . GLN A 1 265 ? 110.286 169.146 102.844 1.00 44.51  ? 240  GLN A CD  1 
ATOM   1344  O  OE1 . GLN A 1 265 ? 111.489 169.275 102.626 1.00 41.01  ? 240  GLN A OE1 1 
ATOM   1345  N  NE2 . GLN A 1 265 ? 109.371 169.251 101.889 1.00 46.59  ? 240  GLN A NE2 1 
ATOM   1346  N  N   . ALA A 1 266 ? 113.468 166.401 105.008 1.00 29.27  ? 241  ALA A N   1 
ATOM   1347  C  CA  . ALA A 1 266 ? 114.863 166.216 104.618 1.00 25.72  ? 241  ALA A CA  1 
ATOM   1348  C  C   . ALA A 1 266 ? 115.030 164.964 103.768 1.00 29.73  ? 241  ALA A C   1 
ATOM   1349  O  O   . ALA A 1 266 ? 115.782 164.965 102.786 1.00 43.36  ? 241  ALA A O   1 
ATOM   1350  C  CB  . ALA A 1 266 ? 115.752 166.145 105.857 1.00 24.72  ? 241  ALA A CB  1 
ATOM   1351  N  N   . LEU A 1 267 ? 114.336 163.884 104.133 1.00 30.86  ? 242  LEU A N   1 
ATOM   1352  C  CA  . LEU A 1 267 ? 114.376 162.670 103.323 1.00 29.90  ? 242  LEU A CA  1 
ATOM   1353  C  C   . LEU A 1 267 ? 113.830 162.923 101.924 1.00 33.40  ? 242  LEU A C   1 
ATOM   1354  O  O   . LEU A 1 267 ? 114.374 162.416 100.938 1.00 35.74  ? 242  LEU A O   1 
ATOM   1355  C  CB  . LEU A 1 267 ? 113.590 161.552 104.008 1.00 28.92  ? 242  LEU A CB  1 
ATOM   1356  C  CG  . LEU A 1 267 ? 114.370 160.633 104.947 1.00 24.17  ? 242  LEU A CG  1 
ATOM   1357  C  CD1 . LEU A 1 267 ? 113.448 159.592 105.551 1.00 25.28  ? 242  LEU A CD1 1 
ATOM   1358  C  CD2 . LEU A 1 267 ? 115.515 159.969 104.207 1.00 28.52  ? 242  LEU A CD2 1 
ATOM   1359  N  N   . ARG A 1 268 ? 112.750 163.697 101.820 1.00 33.66  ? 243  ARG A N   1 
ATOM   1360  C  CA  . ARG A 1 268 ? 112.175 164.018 100.517 1.00 35.57  ? 243  ARG A CA  1 
ATOM   1361  C  C   . ARG A 1 268 ? 113.135 164.852 99.676  1.00 36.70  ? 243  ARG A C   1 
ATOM   1362  O  O   . ARG A 1 268 ? 113.284 164.617 98.468  1.00 42.79  ? 243  ARG A O   1 
ATOM   1363  C  CB  . ARG A 1 268 ? 110.849 164.752 100.706 1.00 31.95  ? 243  ARG A CB  1 
ATOM   1364  C  CG  . ARG A 1 268 ? 109.922 164.698 99.510  1.00 37.40  ? 243  ARG A CG  1 
ATOM   1365  C  CD  . ARG A 1 268 ? 108.669 165.516 99.765  1.00 39.76  ? 243  ARG A CD  1 
ATOM   1366  N  NE  . ARG A 1 268 ? 108.097 165.239 101.077 1.00 37.11  ? 243  ARG A NE  1 
ATOM   1367  C  CZ  . ARG A 1 268 ? 107.252 164.251 101.332 1.00 42.33  ? 243  ARG A CZ  1 
ATOM   1368  N  NH1 . ARG A 1 268 ? 106.856 163.417 100.384 1.00 41.93  ? 243  ARG A NH1 1 
ATOM   1369  N  NH2 . ARG A 1 268 ? 106.791 164.095 102.570 1.00 41.06  ? 243  ARG A NH2 1 
ATOM   1370  N  N   . TRP A 1 269 ? 113.784 165.840 100.298 1.00 33.09  ? 244  TRP A N   1 
ATOM   1371  C  CA  . TRP A 1 269 ? 114.766 166.646 99.581  1.00 31.79  ? 244  TRP A CA  1 
ATOM   1372  C  C   . TRP A 1 269 ? 115.922 165.786 99.095  1.00 32.14  ? 244  TRP A C   1 
ATOM   1373  O  O   . TRP A 1 269 ? 116.407 165.962 97.973  1.00 41.33  ? 244  TRP A O   1 
ATOM   1374  C  CB  . TRP A 1 269 ? 115.277 167.778 100.473 1.00 33.74  ? 244  TRP A CB  1 
ATOM   1375  C  CG  . TRP A 1 269 ? 116.182 168.744 99.764  1.00 38.88  ? 244  TRP A CG  1 
ATOM   1376  C  CD1 . TRP A 1 269 ? 115.827 169.938 99.209  1.00 42.67  ? 244  TRP A CD1 1 
ATOM   1377  C  CD2 . TRP A 1 269 ? 117.591 168.601 99.539  1.00 37.62  ? 244  TRP A CD2 1 
ATOM   1378  N  NE1 . TRP A 1 269 ? 116.925 170.546 98.650  1.00 40.84  ? 244  TRP A NE1 1 
ATOM   1379  C  CE2 . TRP A 1 269 ? 118.020 169.745 98.840  1.00 38.04  ? 244  TRP A CE2 1 
ATOM   1380  C  CE3 . TRP A 1 269 ? 118.530 167.618 99.861  1.00 36.86  ? 244  TRP A CE3 1 
ATOM   1381  C  CZ2 . TRP A 1 269 ? 119.344 169.932 98.456  1.00 39.10  ? 244  TRP A CZ2 1 
ATOM   1382  C  CZ3 . TRP A 1 269 ? 119.844 167.805 99.478  1.00 38.70  ? 244  TRP A CZ3 1 
ATOM   1383  C  CH2 . TRP A 1 269 ? 120.239 168.952 98.784  1.00 38.95  ? 244  TRP A CH2 1 
ATOM   1384  N  N   . LEU A 1 270 ? 116.380 164.849 99.929  1.00 31.75  ? 245  LEU A N   1 
ATOM   1385  C  CA  . LEU A 1 270 ? 117.416 163.919 99.492  1.00 34.91  ? 245  LEU A CA  1 
ATOM   1386  C  C   . LEU A 1 270 ? 116.930 163.058 98.333  1.00 41.45  ? 245  LEU A C   1 
ATOM   1387  O  O   . LEU A 1 270 ? 117.665 162.832 97.366  1.00 38.90  ? 245  LEU A O   1 
ATOM   1388  C  CB  . LEU A 1 270 ? 117.859 163.040 100.661 1.00 30.15  ? 245  LEU A CB  1 
ATOM   1389  C  CG  . LEU A 1 270 ? 118.862 163.641 101.644 1.00 28.98  ? 245  LEU A CG  1 
ATOM   1390  C  CD1 . LEU A 1 270 ? 119.538 162.545 102.444 1.00 36.79  ? 245  LEU A CD1 1 
ATOM   1391  C  CD2 . LEU A 1 270 ? 119.892 164.475 100.907 1.00 35.26  ? 245  LEU A CD2 1 
ATOM   1392  N  N   . SER A 1 271 ? 115.691 162.573 98.410  1.00 40.66  ? 246  SER A N   1 
ATOM   1393  C  CA  . SER A 1 271 ? 115.169 161.694 97.370  1.00 38.91  ? 246  SER A CA  1 
ATOM   1394  C  C   . SER A 1 271 ? 115.087 162.408 96.028  1.00 39.61  ? 246  SER A C   1 
ATOM   1395  O  O   . SER A 1 271 ? 115.410 161.824 94.987  1.00 35.95  ? 246  SER A O   1 
ATOM   1396  C  CB  . SER A 1 271 ? 113.796 161.160 97.776  1.00 30.73  ? 246  SER A CB  1 
ATOM   1397  O  OG  . SER A 1 271 ? 113.151 160.531 96.684  1.00 37.84  ? 246  SER A OG  1 
ATOM   1398  N  N   . GLU A 1 272 ? 114.659 163.668 96.027  1.00 40.07  ? 247  GLU A N   1 
ATOM   1399  C  CA  . GLU A 1 272 ? 114.467 164.397 94.779  1.00 41.38  ? 247  GLU A CA  1 
ATOM   1400  C  C   . GLU A 1 272 ? 115.617 165.345 94.447  1.00 46.33  ? 247  GLU A C   1 
ATOM   1401  O  O   . GLU A 1 272 ? 115.495 166.133 93.504  1.00 50.78  ? 247  GLU A O   1 
ATOM   1402  C  CB  . GLU A 1 272 ? 113.144 165.167 94.812  1.00 40.83  ? 247  GLU A CB  1 
ATOM   1403  C  CG  . GLU A 1 272 ? 113.116 166.348 95.762  1.00 46.28  ? 247  GLU A CG  1 
ATOM   1404  C  CD  . GLU A 1 272 ? 111.710 166.707 96.200  1.00 50.20  ? 247  GLU A CD  1 
ATOM   1405  O  OE1 . GLU A 1 272 ? 110.846 165.807 96.221  1.00 49.08  ? 247  GLU A OE1 1 
ATOM   1406  O  OE2 . GLU A 1 272 ? 111.468 167.891 96.519  1.00 47.51  ? 247  GLU A OE2 1 
ATOM   1407  N  N   . ASN A 1 273 ? 116.728 165.292 95.187  1.00 42.09  ? 248  ASN A N   1 
ATOM   1408  C  CA  . ASN A 1 273 ? 117.847 166.183 94.909  1.00 39.28  ? 248  ASN A CA  1 
ATOM   1409  C  C   . ASN A 1 273 ? 119.227 165.549 95.044  1.00 47.63  ? 248  ASN A C   1 
ATOM   1410  O  O   . ASN A 1 273 ? 120.220 166.268 94.902  1.00 49.55  ? 248  ASN A O   1 
ATOM   1411  C  CB  . ASN A 1 273 ? 117.784 167.416 95.827  1.00 41.97  ? 248  ASN A CB  1 
ATOM   1412  C  CG  . ASN A 1 273 ? 116.811 168.465 95.331  1.00 48.47  ? 248  ASN A CG  1 
ATOM   1413  O  OD1 . ASN A 1 273 ? 115.597 168.284 95.393  1.00 45.44  ? 248  ASN A OD1 1 
ATOM   1414  N  ND2 . ASN A 1 273 ? 117.343 169.576 94.841  1.00 54.75  ? 248  ASN A ND2 1 
ATOM   1415  N  N   . ILE A 1 274 ? 119.334 164.244 95.313  1.00 47.56  ? 249  ILE A N   1 
ATOM   1416  C  CA  . ILE A 1 274 ? 120.649 163.632 95.511  1.00 44.60  ? 249  ILE A CA  1 
ATOM   1417  C  C   . ILE A 1 274 ? 121.247 163.083 94.224  1.00 50.00  ? 249  ILE A C   1 
ATOM   1418  O  O   . ILE A 1 274 ? 122.452 162.786 94.192  1.00 51.44  ? 249  ILE A O   1 
ATOM   1419  C  CB  . ILE A 1 274 ? 120.594 162.504 96.561  1.00 38.53  ? 249  ILE A CB  1 
ATOM   1420  C  CG1 . ILE A 1 274 ? 121.967 162.294 97.199  1.00 41.10  ? 249  ILE A CG1 1 
ATOM   1421  C  CG2 . ILE A 1 274 ? 120.096 161.212 95.938  1.00 43.34  ? 249  ILE A CG2 1 
ATOM   1422  C  CD1 . ILE A 1 274 ? 122.499 163.511 97.901  1.00 44.92  ? 249  ILE A CD1 1 
ATOM   1423  N  N   . ALA A 1 275 ? 120.454 162.943 93.160  1.00 52.59  ? 250  ALA A N   1 
ATOM   1424  C  CA  . ALA A 1 275 ? 121.000 162.450 91.901  1.00 47.33  ? 250  ALA A CA  1 
ATOM   1425  C  C   . ALA A 1 275 ? 122.036 163.407 91.328  1.00 48.67  ? 250  ALA A C   1 
ATOM   1426  O  O   . ALA A 1 275 ? 122.950 162.978 90.615  1.00 50.95  ? 250  ALA A O   1 
ATOM   1427  C  CB  . ALA A 1 275 ? 119.874 162.218 90.895  1.00 47.08  ? 250  ALA A CB  1 
ATOM   1428  N  N   . HIS A 1 276 ? 121.914 164.701 91.628  1.00 49.37  ? 251  HIS A N   1 
ATOM   1429  C  CA  . HIS A 1 276 ? 122.862 165.678 91.105  1.00 52.38  ? 251  HIS A CA  1 
ATOM   1430  C  C   . HIS A 1 276 ? 124.213 165.583 91.801  1.00 54.45  ? 251  HIS A C   1 
ATOM   1431  O  O   . HIS A 1 276 ? 125.240 165.925 91.205  1.00 56.53  ? 251  HIS A O   1 
ATOM   1432  C  CB  . HIS A 1 276 ? 122.292 167.088 91.247  1.00 51.64  ? 251  HIS A CB  1 
ATOM   1433  C  CG  . HIS A 1 276 ? 120.896 167.233 90.726  1.00 55.78  ? 251  HIS A CG  1 
ATOM   1434  N  ND1 . HIS A 1 276 ? 120.047 168.234 91.145  1.00 59.46  ? 251  HIS A ND1 1 
ATOM   1435  C  CD2 . HIS A 1 276 ? 120.201 166.506 89.820  1.00 54.02  ? 251  HIS A CD2 1 
ATOM   1436  C  CE1 . HIS A 1 276 ? 118.888 168.116 90.521  1.00 56.79  ? 251  HIS A CE1 1 
ATOM   1437  N  NE2 . HIS A 1 276 ? 118.955 167.075 89.712  1.00 55.72  ? 251  HIS A NE2 1 
ATOM   1438  N  N   . PHE A 1 277 ? 124.237 165.122 93.049  1.00 51.41  ? 252  PHE A N   1 
ATOM   1439  C  CA  . PHE A 1 277 ? 125.471 164.997 93.812  1.00 52.06  ? 252  PHE A CA  1 
ATOM   1440  C  C   . PHE A 1 277 ? 126.165 163.660 93.597  1.00 51.31  ? 252  PHE A C   1 
ATOM   1441  O  O   . PHE A 1 277 ? 127.194 163.404 94.231  1.00 51.84  ? 252  PHE A O   1 
ATOM   1442  C  CB  . PHE A 1 277 ? 125.194 165.191 95.307  1.00 46.03  ? 252  PHE A CB  1 
ATOM   1443  C  CG  . PHE A 1 277 ? 124.725 166.573 95.665  1.00 47.95  ? 252  PHE A CG  1 
ATOM   1444  C  CD1 . PHE A 1 277 ? 123.397 166.930 95.519  1.00 51.21  ? 252  PHE A CD1 1 
ATOM   1445  C  CD2 . PHE A 1 277 ? 125.615 167.512 96.154  1.00 52.14  ? 252  PHE A CD2 1 
ATOM   1446  C  CE1 . PHE A 1 277 ? 122.966 168.199 95.849  1.00 51.64  ? 252  PHE A CE1 1 
ATOM   1447  C  CE2 . PHE A 1 277 ? 125.190 168.782 96.485  1.00 54.54  ? 252  PHE A CE2 1 
ATOM   1448  C  CZ  . PHE A 1 277 ? 123.863 169.126 96.333  1.00 53.37  ? 252  PHE A CZ  1 
ATOM   1449  N  N   . GLY A 1 278 ? 125.635 162.808 92.723  1.00 49.09  ? 253  GLY A N   1 
ATOM   1450  C  CA  . GLY A 1 278 ? 126.180 161.488 92.510  1.00 50.31  ? 253  GLY A CA  1 
ATOM   1451  C  C   . GLY A 1 278 ? 125.565 160.400 93.361  1.00 50.38  ? 253  GLY A C   1 
ATOM   1452  O  O   . GLY A 1 278 ? 125.901 159.225 93.172  1.00 51.70  ? 253  GLY A O   1 
ATOM   1453  N  N   . GLY A 1 279 ? 124.682 160.749 94.289  1.00 52.07  ? 254  GLY A N   1 
ATOM   1454  C  CA  . GLY A 1 279 ? 124.053 159.754 95.129  1.00 54.11  ? 254  GLY A CA  1 
ATOM   1455  C  C   . GLY A 1 279 ? 122.987 158.965 94.395  1.00 56.93  ? 254  GLY A C   1 
ATOM   1456  O  O   . GLY A 1 279 ? 122.531 159.318 93.307  1.00 55.99  ? 254  GLY A O   1 
ATOM   1457  N  N   . ASP A 1 280 ? 122.584 157.864 95.019  1.00 53.88  ? 255  ASP A N   1 
ATOM   1458  C  CA  . ASP A 1 280 ? 121.569 156.982 94.457  1.00 50.44  ? 255  ASP A CA  1 
ATOM   1459  C  C   . ASP A 1 280 ? 120.265 157.153 95.220  1.00 51.95  ? 255  ASP A C   1 
ATOM   1460  O  O   . ASP A 1 280 ? 120.204 156.812 96.412  1.00 54.81  ? 255  ASP A O   1 
ATOM   1461  C  CB  . ASP A 1 280 ? 122.032 155.526 94.510  1.00 50.50  ? 255  ASP A CB  1 
ATOM   1462  C  CG  . ASP A 1 280 ? 121.479 154.696 93.370  1.00 57.50  ? 255  ASP A CG  1 
ATOM   1463  O  OD1 . ASP A 1 280 ? 120.283 154.848 93.048  1.00 57.69  ? 255  ASP A OD1 1 
ATOM   1464  O  OD2 . ASP A 1 280 ? 122.241 153.892 92.796  1.00 58.89  ? 255  ASP A OD2 1 
ATOM   1465  N  N   . PRO A 1 281 ? 119.204 157.665 94.596  1.00 53.87  ? 256  PRO A N   1 
ATOM   1466  C  CA  . PRO A 1 281 ? 117.938 157.845 95.319  1.00 52.06  ? 256  PRO A CA  1 
ATOM   1467  C  C   . PRO A 1 281 ? 117.189 156.539 95.533  1.00 54.28  ? 256  PRO A C   1 
ATOM   1468  O  O   . PRO A 1 281 ? 116.031 156.545 95.962  1.00 53.13  ? 256  PRO A O   1 
ATOM   1469  C  CB  . PRO A 1 281 ? 117.153 158.796 94.410  1.00 52.83  ? 256  PRO A CB  1 
ATOM   1470  C  CG  . PRO A 1 281 ? 117.683 158.523 93.048  1.00 54.33  ? 256  PRO A CG  1 
ATOM   1471  C  CD  . PRO A 1 281 ? 119.142 158.200 93.225  1.00 55.45  ? 256  PRO A CD  1 
ATOM   1472  N  N   . GLU A 1 282 ? 117.837 155.413 95.237  1.00 55.87  ? 257  GLU A N   1 
ATOM   1473  C  CA  . GLU A 1 282 ? 117.233 154.098 95.410  1.00 52.52  ? 257  GLU A CA  1 
ATOM   1474  C  C   . GLU A 1 282 ? 118.017 153.216 96.374  1.00 51.23  ? 257  GLU A C   1 
ATOM   1475  O  O   . GLU A 1 282 ? 117.733 152.016 96.468  1.00 48.52  ? 257  GLU A O   1 
ATOM   1476  C  CB  . GLU A 1 282 ? 117.090 153.398 94.055  1.00 53.78  ? 257  GLU A CB  1 
ATOM   1477  C  CG  . GLU A 1 282 ? 115.846 152.534 93.925  1.00 55.74  ? 257  GLU A CG  1 
ATOM   1478  C  CD  . GLU A 1 282 ? 114.602 153.340 93.608  1.00 56.75  ? 257  GLU A CD  1 
ATOM   1479  O  OE1 . GLU A 1 282 ? 114.717 154.570 93.426  1.00 59.37  ? 257  GLU A OE1 1 
ATOM   1480  O  OE2 . GLU A 1 282 ? 113.507 152.743 93.542  1.00 53.73  ? 257  GLU A OE2 1 
ATOM   1481  N  N   . ARG A 1 283 ? 118.996 153.771 97.087  1.00 49.79  ? 258  ARG A N   1 
ATOM   1482  C  CA  . ARG A 1 283 ? 119.782 153.021 98.063  1.00 50.22  ? 258  ARG A CA  1 
ATOM   1483  C  C   . ARG A 1 283 ? 120.003 153.852 99.319  1.00 49.29  ? 258  ARG A C   1 
ATOM   1484  O  O   . ARG A 1 283 ? 121.109 153.903 99.865  1.00 50.60  ? 258  ARG A O   1 
ATOM   1485  C  CB  . ARG A 1 283 ? 121.117 152.572 97.471  1.00 52.21  ? 258  ARG A CB  1 
ATOM   1486  C  CG  . ARG A 1 283 ? 120.987 151.604 96.305  1.00 53.45  ? 258  ARG A CG  1 
ATOM   1487  C  CD  . ARG A 1 283 ? 122.233 150.755 96.142  1.00 51.06  ? 258  ARG A CD  1 
ATOM   1488  N  NE  . ARG A 1 283 ? 123.381 151.547 95.720  1.00 49.42  ? 258  ARG A NE  1 
ATOM   1489  C  CZ  . ARG A 1 283 ? 124.517 151.035 95.267  1.00 50.99  ? 258  ARG A CZ  1 
ATOM   1490  N  NH1 . ARG A 1 283 ? 124.692 149.729 95.163  1.00 52.41  ? 258  ARG A NH1 1 
ATOM   1491  N  NH2 . ARG A 1 283 ? 125.500 151.855 94.910  1.00 51.93  ? 258  ARG A NH2 1 
ATOM   1492  N  N   . ILE A 1 284 ? 118.952 154.511 99.797  1.00 46.08  ? 259  ILE A N   1 
ATOM   1493  C  CA  . ILE A 1 284 ? 119.053 155.431 100.925 1.00 40.54  ? 259  ILE A CA  1 
ATOM   1494  C  C   . ILE A 1 284 ? 118.884 154.652 102.223 1.00 40.02  ? 259  ILE A C   1 
ATOM   1495  O  O   . ILE A 1 284 ? 117.875 153.967 102.420 1.00 48.70  ? 259  ILE A O   1 
ATOM   1496  C  CB  . ILE A 1 284 ? 118.011 156.554 100.819 1.00 39.44  ? 259  ILE A CB  1 
ATOM   1497  C  CG1 . ILE A 1 284 ? 118.388 157.528 99.703  1.00 41.66  ? 259  ILE A CG1 1 
ATOM   1498  C  CG2 . ILE A 1 284 ? 117.881 157.288 102.143 1.00 33.58  ? 259  ILE A CG2 1 
ATOM   1499  C  CD1 . ILE A 1 284 ? 117.400 158.656 99.523  1.00 42.83  ? 259  ILE A CD1 1 
ATOM   1500  N  N   . THR A 1 285 ? 119.870 154.760 103.107 1.00 33.90  ? 260  THR A N   1 
ATOM   1501  C  CA  . THR A 1 285 ? 119.828 154.193 104.443 1.00 27.14  ? 260  THR A CA  1 
ATOM   1502  C  C   . THR A 1 285 ? 119.647 155.318 105.452 1.00 36.08  ? 260  THR A C   1 
ATOM   1503  O  O   . THR A 1 285 ? 120.133 156.433 105.250 1.00 53.69  ? 260  THR A O   1 
ATOM   1504  C  CB  . THR A 1 285 ? 121.114 153.416 104.748 1.00 35.24  ? 260  THR A CB  1 
ATOM   1505  O  OG1 . THR A 1 285 ? 121.352 152.460 103.708 1.00 49.61  ? 260  THR A OG1 1 
ATOM   1506  C  CG2 . THR A 1 285 ? 121.011 152.687 106.074 1.00 39.80  ? 260  THR A CG2 1 
ATOM   1507  N  N   . ILE A 1 286 ? 118.929 155.029 106.533 1.00 25.30  ? 261  ILE A N   1 
ATOM   1508  C  CA  . ILE A 1 286 ? 118.697 155.989 107.604 1.00 23.77  ? 261  ILE A CA  1 
ATOM   1509  C  C   . ILE A 1 286 ? 119.133 155.345 108.911 1.00 25.92  ? 261  ILE A C   1 
ATOM   1510  O  O   . ILE A 1 286 ? 118.806 154.183 109.172 1.00 44.52  ? 261  ILE A O   1 
ATOM   1511  C  CB  . ILE A 1 286 ? 117.222 156.435 107.658 1.00 18.49  ? 261  ILE A CB  1 
ATOM   1512  C  CG1 . ILE A 1 286 ? 116.990 157.436 108.784 1.00 31.21  ? 261  ILE A CG1 1 
ATOM   1513  C  CG2 . ILE A 1 286 ? 116.291 155.248 107.815 1.00 28.34  ? 261  ILE A CG2 1 
ATOM   1514  C  CD1 . ILE A 1 286 ? 115.552 157.865 108.893 1.00 26.83  ? 261  ILE A CD1 1 
ATOM   1515  N  N   . PHE A 1 287 ? 119.899 156.079 109.716 1.00 28.55  ? 262  PHE A N   1 
ATOM   1516  C  CA  . PHE A 1 287 ? 120.419 155.498 110.945 1.00 31.80  ? 262  PHE A CA  1 
ATOM   1517  C  C   . PHE A 1 287 ? 120.615 156.578 111.997 1.00 37.60  ? 262  PHE A C   1 
ATOM   1518  O  O   . PHE A 1 287 ? 120.714 157.768 111.689 1.00 47.65  ? 262  PHE A O   1 
ATOM   1519  C  CB  . PHE A 1 287 ? 121.727 154.735 110.692 1.00 31.88  ? 262  PHE A CB  1 
ATOM   1520  C  CG  . PHE A 1 287 ? 122.944 155.607 110.585 1.00 36.23  ? 262  PHE A CG  1 
ATOM   1521  C  CD1 . PHE A 1 287 ? 123.123 156.442 109.500 1.00 42.28  ? 262  PHE A CD1 1 
ATOM   1522  C  CD2 . PHE A 1 287 ? 123.927 155.564 111.557 1.00 38.82  ? 262  PHE A CD2 1 
ATOM   1523  C  CE1 . PHE A 1 287 ? 124.248 157.235 109.396 1.00 40.27  ? 262  PHE A CE1 1 
ATOM   1524  C  CE2 . PHE A 1 287 ? 125.054 156.352 111.458 1.00 35.71  ? 262  PHE A CE2 1 
ATOM   1525  C  CZ  . PHE A 1 287 ? 125.215 157.189 110.375 1.00 36.10  ? 262  PHE A CZ  1 
ATOM   1526  N  N   . GLY A 1 288 ? 120.656 156.141 113.248 1.00 17.77  ? 263  GLY A N   1 
ATOM   1527  C  CA  . GLY A 1 288 ? 120.847 157.050 114.360 1.00 19.39  ? 263  GLY A CA  1 
ATOM   1528  C  C   . GLY A 1 288 ? 120.962 156.268 115.649 1.00 19.71  ? 263  GLY A C   1 
ATOM   1529  O  O   . GLY A 1 288 ? 120.560 155.104 115.734 1.00 28.36  ? 263  GLY A O   1 
ATOM   1530  N  N   . SER A 1 289 ? 121.523 156.933 116.655 1.00 16.84  ? 264  SER A N   1 
ATOM   1531  C  CA  . SER A 1 289 ? 121.739 156.339 117.966 1.00 15.39  ? 264  SER A CA  1 
ATOM   1532  C  C   . SER A 1 289 ? 121.089 157.201 119.038 1.00 22.83  ? 264  SER A C   1 
ATOM   1533  O  O   . SER A 1 289 ? 121.170 158.432 118.991 1.00 34.82  ? 264  SER A O   1 
ATOM   1534  C  CB  . SER A 1 289 ? 123.231 156.179 118.266 1.00 23.63  ? 264  SER A CB  1 
ATOM   1535  O  OG  . SER A 1 289 ? 123.461 156.090 119.661 1.00 23.56  ? 264  SER A OG  1 
ATOM   1536  N  N   . GLY A 1 290 ? 120.453 156.548 120.006 1.00 18.43  ? 265  GLY A N   1 
ATOM   1537  C  CA  . GLY A 1 290 ? 119.763 157.257 121.065 1.00 24.54  ? 265  GLY A CA  1 
ATOM   1538  C  C   . GLY A 1 290 ? 118.318 157.541 120.717 1.00 20.87  ? 265  GLY A C   1 
ATOM   1539  O  O   . GLY A 1 290 ? 117.673 156.738 120.037 1.00 28.00  ? 265  GLY A O   1 
ATOM   1540  N  N   . ALA A 1 291 ? 117.797 158.684 121.172 1.00 17.14  ? 266  ALA A N   1 
ATOM   1541  C  CA  . ALA A 1 291 ? 116.425 159.049 120.837 1.00 19.56  ? 266  ALA A CA  1 
ATOM   1542  C  C   . ALA A 1 291 ? 116.240 159.194 119.335 1.00 26.28  ? 266  ALA A C   1 
ATOM   1543  O  O   . ALA A 1 291 ? 115.158 158.903 118.813 1.00 30.73  ? 266  ALA A O   1 
ATOM   1544  C  CB  . ALA A 1 291 ? 116.030 160.343 121.543 1.00 25.07  ? 266  ALA A CB  1 
ATOM   1545  N  N   . GLY A 1 292 ? 117.283 159.629 118.625 1.00 21.04  ? 267  GLY A N   1 
ATOM   1546  C  CA  . GLY A 1 292 ? 117.212 159.659 117.174 1.00 13.22  ? 267  GLY A CA  1 
ATOM   1547  C  C   . GLY A 1 292 ? 116.911 158.294 116.590 1.00 24.56  ? 267  GLY A C   1 
ATOM   1548  O  O   . GLY A 1 292 ? 116.147 158.174 115.629 1.00 25.84  ? 267  GLY A O   1 
ATOM   1549  N  N   . ALA A 1 293 ? 117.494 157.244 117.177 1.00 17.21  ? 268  ALA A N   1 
ATOM   1550  C  CA  . ALA A 1 293 ? 117.162 155.886 116.762 1.00 14.35  ? 268  ALA A CA  1 
ATOM   1551  C  C   . ALA A 1 293 ? 115.670 155.627 116.896 1.00 17.80  ? 268  ALA A C   1 
ATOM   1552  O  O   . ALA A 1 293 ? 115.056 155.022 116.009 1.00 36.68  ? 268  ALA A O   1 
ATOM   1553  C  CB  . ALA A 1 293 ? 117.955 154.874 117.585 1.00 19.02  ? 268  ALA A CB  1 
ATOM   1554  N  N   . SER A 1 294 ? 115.064 156.102 117.987 1.00 11.43  ? 269  SER A N   1 
ATOM   1555  C  CA  . SER A 1 294 ? 113.618 155.987 118.134 1.00 9.67   ? 269  SER A CA  1 
ATOM   1556  C  C   . SER A 1 294 ? 112.904 156.645 116.964 1.00 18.33  ? 269  SER A C   1 
ATOM   1557  O  O   . SER A 1 294 ? 111.941 156.088 116.422 1.00 27.16  ? 269  SER A O   1 
ATOM   1558  C  CB  . SER A 1 294 ? 113.171 156.607 119.455 1.00 12.25  ? 269  SER A CB  1 
ATOM   1559  O  OG  . SER A 1 294 ? 113.585 155.819 120.557 1.00 22.03  ? 269  SER A OG  1 
ATOM   1560  N  N   . CYS A 1 295 ? 113.387 157.817 116.537 1.00 17.99  ? 270  CYS A N   1 
ATOM   1561  C  CA  . CYS A 1 295 ? 112.818 158.473 115.366 1.00 12.10  ? 270  CYS A CA  1 
ATOM   1562  C  C   . CYS A 1 295 ? 112.821 157.537 114.168 1.00 17.08  ? 270  CYS A C   1 
ATOM   1563  O  O   . CYS A 1 295 ? 111.826 157.445 113.440 1.00 25.19  ? 270  CYS A O   1 
ATOM   1564  C  CB  . CYS A 1 295 ? 113.592 159.751 115.047 1.00 4.70   ? 270  CYS A CB  1 
ATOM   1565  S  SG  . CYS A 1 295 ? 113.380 161.079 116.250 1.00 26.01  ? 270  CYS A SG  1 
ATOM   1566  N  N   . VAL A 1 296 ? 113.922 156.806 113.971 1.00 14.88  ? 271  VAL A N   1 
ATOM   1567  C  CA  . VAL A 1 296 ? 113.980 155.833 112.883 1.00 16.06  ? 271  VAL A CA  1 
ATOM   1568  C  C   . VAL A 1 296 ? 112.835 154.840 113.008 1.00 26.10  ? 271  VAL A C   1 
ATOM   1569  O  O   . VAL A 1 296 ? 112.081 154.609 112.056 1.00 35.09  ? 271  VAL A O   1 
ATOM   1570  C  CB  . VAL A 1 296 ? 115.344 155.120 112.871 1.00 6.90   ? 271  VAL A CB  1 
ATOM   1571  C  CG1 . VAL A 1 296 ? 115.399 154.113 111.741 1.00 6.07   ? 271  VAL A CG1 1 
ATOM   1572  C  CG2 . VAL A 1 296 ? 116.467 156.130 112.746 1.00 18.55  ? 271  VAL A CG2 1 
ATOM   1573  N  N   . ASN A 1 297 ? 112.652 154.280 114.205 1.00 18.26  ? 272  ASN A N   1 
ATOM   1574  C  CA  . ASN A 1 297 ? 111.595 153.298 114.393 1.00 15.73  ? 272  ASN A CA  1 
ATOM   1575  C  C   . ASN A 1 297 ? 110.208 153.921 114.364 1.00 21.91  ? 272  ASN A C   1 
ATOM   1576  O  O   . ASN A 1 297 ? 109.219 153.183 114.322 1.00 31.32  ? 272  ASN A O   1 
ATOM   1577  C  CB  . ASN A 1 297 ? 111.806 152.542 115.704 1.00 16.50  ? 272  ASN A CB  1 
ATOM   1578  C  CG  . ASN A 1 297 ? 112.491 151.209 115.499 1.00 28.89  ? 272  ASN A CG  1 
ATOM   1579  O  OD1 . ASN A 1 297 ? 111.844 150.164 115.477 1.00 38.69  ? 272  ASN A OD1 1 
ATOM   1580  N  ND2 . ASN A 1 297 ? 113.808 151.238 115.345 1.00 18.87  ? 272  ASN A ND2 1 
ATOM   1581  N  N   . LEU A 1 298 ? 110.108 155.249 114.386 1.00 11.36  ? 273  LEU A N   1 
ATOM   1582  C  CA  . LEU A 1 298 ? 108.836 155.918 114.172 1.00 10.13  ? 273  LEU A CA  1 
ATOM   1583  C  C   . LEU A 1 298 ? 108.669 156.412 112.743 1.00 25.75  ? 273  LEU A C   1 
ATOM   1584  O  O   . LEU A 1 298 ? 107.570 156.838 112.376 1.00 31.96  ? 273  LEU A O   1 
ATOM   1585  C  CB  . LEU A 1 298 ? 108.676 157.090 115.147 1.00 17.68  ? 273  LEU A CB  1 
ATOM   1586  C  CG  . LEU A 1 298 ? 108.458 156.690 116.607 1.00 16.57  ? 273  LEU A CG  1 
ATOM   1587  C  CD1 . LEU A 1 298 ? 108.854 157.816 117.541 1.00 14.35  ? 273  LEU A CD1 1 
ATOM   1588  C  CD2 . LEU A 1 298 ? 107.013 156.288 116.835 1.00 29.52  ? 273  LEU A CD2 1 
ATOM   1589  N  N   . LEU A 1 299 ? 109.727 156.366 111.933 1.00 29.24  ? 274  LEU A N   1 
ATOM   1590  C  CA  . LEU A 1 299 ? 109.605 156.659 110.513 1.00 18.70  ? 274  LEU A CA  1 
ATOM   1591  C  C   . LEU A 1 299 ? 109.253 155.426 109.698 1.00 20.75  ? 274  LEU A C   1 
ATOM   1592  O  O   . LEU A 1 299 ? 108.712 155.559 108.595 1.00 31.63  ? 274  LEU A O   1 
ATOM   1593  C  CB  . LEU A 1 299 ? 110.904 157.273 109.983 1.00 17.11  ? 274  LEU A CB  1 
ATOM   1594  C  CG  . LEU A 1 299 ? 111.200 158.706 110.428 1.00 11.35  ? 274  LEU A CG  1 
ATOM   1595  C  CD1 . LEU A 1 299 ? 112.265 159.334 109.551 1.00 15.88  ? 274  LEU A CD1 1 
ATOM   1596  C  CD2 . LEU A 1 299 ? 109.936 159.546 110.416 1.00 23.42  ? 274  LEU A CD2 1 
ATOM   1597  N  N   . ILE A 1 300 ? 109.555 154.235 110.215 1.00 23.67  ? 275  ILE A N   1 
ATOM   1598  C  CA  . ILE A 1 300 ? 109.166 153.001 109.542 1.00 24.78  ? 275  ILE A CA  1 
ATOM   1599  C  C   . ILE A 1 300 ? 107.660 152.792 109.631 1.00 25.91  ? 275  ILE A C   1 
ATOM   1600  O  O   . ILE A 1 300 ? 107.012 152.417 108.647 1.00 34.17  ? 275  ILE A O   1 
ATOM   1601  C  CB  . ILE A 1 300 ? 109.944 151.816 110.138 1.00 19.04  ? 275  ILE A CB  1 
ATOM   1602  C  CG1 . ILE A 1 300 ? 111.419 151.919 109.755 1.00 28.15  ? 275  ILE A CG1 1 
ATOM   1603  C  CG2 . ILE A 1 300 ? 109.352 150.497 109.682 1.00 22.59  ? 275  ILE A CG2 1 
ATOM   1604  C  CD1 . ILE A 1 300 ? 112.229 150.731 110.165 1.00 20.55  ? 275  ILE A CD1 1 
ATOM   1605  N  N   . LEU A 1 301 ? 107.078 153.042 110.801 1.00 25.55  ? 276  LEU A N   1 
ATOM   1606  C  CA  . LEU A 1 301 ? 105.653 152.843 111.023 1.00 25.19  ? 276  LEU A CA  1 
ATOM   1607  C  C   . LEU A 1 301 ? 104.811 154.031 110.577 1.00 28.97  ? 276  LEU A C   1 
ATOM   1608  O  O   . LEU A 1 301 ? 103.610 154.062 110.865 1.00 39.59  ? 276  LEU A O   1 
ATOM   1609  C  CB  . LEU A 1 301 ? 105.388 152.554 112.503 1.00 29.03  ? 276  LEU A CB  1 
ATOM   1610  C  CG  . LEU A 1 301 ? 106.375 151.620 113.204 1.00 26.16  ? 276  LEU A CG  1 
ATOM   1611  C  CD1 . LEU A 1 301 ? 106.120 151.593 114.700 1.00 26.02  ? 276  LEU A CD1 1 
ATOM   1612  C  CD2 . LEU A 1 301 ? 106.294 150.223 112.621 1.00 23.73  ? 276  LEU A CD2 1 
ATOM   1613  N  N   . SER A 1 302 ? 105.402 155.000 109.886 1.00 27.10  ? 277  SER A N   1 
ATOM   1614  C  CA  . SER A 1 302 ? 104.699 156.201 109.457 1.00 29.99  ? 277  SER A CA  1 
ATOM   1615  C  C   . SER A 1 302 ? 104.266 156.057 108.005 1.00 35.10  ? 277  SER A C   1 
ATOM   1616  O  O   . SER A 1 302 ? 105.051 155.624 107.156 1.00 39.38  ? 277  SER A O   1 
ATOM   1617  C  CB  . SER A 1 302 ? 105.583 157.437 109.622 1.00 36.25  ? 277  SER A CB  1 
ATOM   1618  O  OG  . SER A 1 302 ? 105.366 158.055 110.877 1.00 37.92  ? 277  SER A OG  1 
ATOM   1619  N  N   . HIS A 1 303 ? 103.012 156.419 107.728 1.00 49.78  ? 278  HIS A N   1 
ATOM   1620  C  CA  . HIS A 1 303 ? 102.497 156.375 106.366 1.00 50.84  ? 278  HIS A CA  1 
ATOM   1621  C  C   . HIS A 1 303 ? 103.159 157.408 105.462 1.00 54.91  ? 278  HIS A C   1 
ATOM   1622  O  O   . HIS A 1 303 ? 103.184 157.221 104.241 1.00 54.80  ? 278  HIS A O   1 
ATOM   1623  C  CB  . HIS A 1 303 ? 100.979 156.575 106.386 1.00 48.89  ? 278  HIS A CB  1 
ATOM   1624  C  CG  . HIS A 1 303 ? 100.450 157.362 105.227 1.00 56.63  ? 278  HIS A CG  1 
ATOM   1625  N  ND1 . HIS A 1 303 ? 100.553 156.928 103.923 1.00 55.52  ? 278  HIS A ND1 1 
ATOM   1626  C  CD2 . HIS A 1 303 ? 99.816  158.557 105.177 1.00 60.18  ? 278  HIS A CD2 1 
ATOM   1627  C  CE1 . HIS A 1 303 ? 100.004 157.821 103.120 1.00 56.69  ? 278  HIS A CE1 1 
ATOM   1628  N  NE2 . HIS A 1 303 ? 99.549  158.819 103.856 1.00 61.46  ? 278  HIS A NE2 1 
ATOM   1629  N  N   . HIS A 1 304 ? 103.704 158.485 106.033 1.00 51.02  ? 279  HIS A N   1 
ATOM   1630  C  CA  . HIS A 1 304 ? 104.294 159.540 105.215 1.00 48.11  ? 279  HIS A CA  1 
ATOM   1631  C  C   . HIS A 1 304 ? 105.549 159.059 104.497 1.00 51.40  ? 279  HIS A C   1 
ATOM   1632  O  O   . HIS A 1 304 ? 105.745 159.357 103.313 1.00 55.29  ? 279  HIS A O   1 
ATOM   1633  C  CB  . HIS A 1 304 ? 104.608 160.758 106.082 1.00 45.22  ? 279  HIS A CB  1 
ATOM   1634  C  CG  . HIS A 1 304 ? 103.394 161.499 106.544 1.00 47.03  ? 279  HIS A CG  1 
ATOM   1635  N  ND1 . HIS A 1 304 ? 102.114 161.030 106.343 1.00 47.16  ? 279  HIS A ND1 1 
ATOM   1636  C  CD2 . HIS A 1 304 ? 103.264 162.678 107.197 1.00 52.30  ? 279  HIS A CD2 1 
ATOM   1637  C  CE1 . HIS A 1 304 ? 101.248 161.887 106.854 1.00 51.20  ? 279  HIS A CE1 1 
ATOM   1638  N  NE2 . HIS A 1 304 ? 101.920 162.896 107.378 1.00 54.22  ? 279  HIS A NE2 1 
ATOM   1639  N  N   . SER A 1 305 ? 106.410 158.319 105.192 1.00 47.14  ? 280  SER A N   1 
ATOM   1640  C  CA  . SER A 1 305 ? 107.675 157.852 104.624 1.00 43.95  ? 280  SER A CA  1 
ATOM   1641  C  C   . SER A 1 305 ? 107.464 156.458 104.051 1.00 41.34  ? 280  SER A C   1 
ATOM   1642  O  O   . SER A 1 305 ? 107.711 155.447 104.709 1.00 40.95  ? 280  SER A O   1 
ATOM   1643  C  CB  . SER A 1 305 ? 108.774 157.865 105.679 1.00 43.78  ? 280  SER A CB  1 
ATOM   1644  O  OG  . SER A 1 305 ? 108.965 156.574 106.227 1.00 40.66  ? 280  SER A OG  1 
ATOM   1645  N  N   . GLU A 1 306 ? 107.000 156.403 102.803 1.00 44.39  ? 281  GLU A N   1 
ATOM   1646  C  CA  . GLU A 1 306 ? 106.750 155.128 102.138 1.00 49.73  ? 281  GLU A CA  1 
ATOM   1647  C  C   . GLU A 1 306 ? 107.948 154.685 101.302 1.00 53.67  ? 281  GLU A C   1 
ATOM   1648  O  O   . GLU A 1 306 ? 108.528 153.623 101.548 1.00 56.54  ? 281  GLU A O   1 
ATOM   1649  C  CB  . GLU A 1 306 ? 105.495 155.230 101.266 1.00 51.09  ? 281  GLU A CB  1 
ATOM   1650  C  CG  . GLU A 1 306 ? 104.196 155.134 102.043 1.00 54.13  ? 281  GLU A CG  1 
ATOM   1651  C  CD  . GLU A 1 306 ? 103.136 154.337 101.312 1.00 58.33  ? 281  GLU A CD  1 
ATOM   1652  O  OE1 . GLU A 1 306 ? 102.992 154.518 100.085 1.00 58.71  ? 281  GLU A OE1 1 
ATOM   1653  O  OE2 . GLU A 1 306 ? 102.446 153.528 101.966 1.00 58.21  ? 281  GLU A OE2 1 
ATOM   1654  N  N   . GLY A 1 307 ? 108.329 155.491 100.313 1.00 44.51  ? 282  GLY A N   1 
ATOM   1655  C  CA  . GLY A 1 307 ? 109.444 155.174 99.444  1.00 41.40  ? 282  GLY A CA  1 
ATOM   1656  C  C   . GLY A 1 307 ? 110.659 156.059 99.590  1.00 43.18  ? 282  GLY A C   1 
ATOM   1657  O  O   . GLY A 1 307 ? 111.559 155.988 98.742  1.00 51.47  ? 282  GLY A O   1 
ATOM   1658  N  N   . LEU A 1 308 ? 110.725 156.900 100.624 1.00 33.77  ? 283  LEU A N   1 
ATOM   1659  C  CA  . LEU A 1 308 ? 111.861 157.803 100.768 1.00 34.32  ? 283  LEU A CA  1 
ATOM   1660  C  C   . LEU A 1 308 ? 113.148 157.037 101.047 1.00 40.17  ? 283  LEU A C   1 
ATOM   1661  O  O   . LEU A 1 308 ? 114.201 157.357 100.483 1.00 48.89  ? 283  LEU A O   1 
ATOM   1662  C  CB  . LEU A 1 308 ? 111.591 158.822 101.876 1.00 37.93  ? 283  LEU A CB  1 
ATOM   1663  C  CG  . LEU A 1 308 ? 110.617 159.965 101.568 1.00 37.60  ? 283  LEU A CG  1 
ATOM   1664  C  CD1 . LEU A 1 308 ? 110.979 160.631 100.251 1.00 41.40  ? 283  LEU A CD1 1 
ATOM   1665  C  CD2 . LEU A 1 308 ? 109.162 159.516 101.572 1.00 41.44  ? 283  LEU A CD2 1 
ATOM   1666  N  N   . PHE A 1 309 ? 113.085 156.025 101.909 1.00 36.01  ? 284  PHE A N   1 
ATOM   1667  C  CA  . PHE A 1 309 ? 114.242 155.217 102.258 1.00 36.53  ? 284  PHE A CA  1 
ATOM   1668  C  C   . PHE A 1 309 ? 113.871 153.743 102.190 1.00 38.16  ? 284  PHE A C   1 
ATOM   1669  O  O   . PHE A 1 309 ? 112.695 153.380 102.120 1.00 45.60  ? 284  PHE A O   1 
ATOM   1670  C  CB  . PHE A 1 309 ? 114.778 155.568 103.653 1.00 35.62  ? 284  PHE A CB  1 
ATOM   1671  C  CG  . PHE A 1 309 ? 113.850 155.198 104.773 1.00 32.08  ? 284  PHE A CG  1 
ATOM   1672  C  CD1 . PHE A 1 309 ? 112.832 156.052 105.155 1.00 37.12  ? 284  PHE A CD1 1 
ATOM   1673  C  CD2 . PHE A 1 309 ? 114.001 154.003 105.451 1.00 32.89  ? 284  PHE A CD2 1 
ATOM   1674  C  CE1 . PHE A 1 309 ? 111.982 155.719 106.185 1.00 39.97  ? 284  PHE A CE1 1 
ATOM   1675  C  CE2 . PHE A 1 309 ? 113.153 153.665 106.482 1.00 33.67  ? 284  PHE A CE2 1 
ATOM   1676  C  CZ  . PHE A 1 309 ? 112.143 154.523 106.849 1.00 36.67  ? 284  PHE A CZ  1 
ATOM   1677  N  N   . GLN A 1 310 ? 114.898 152.890 102.203 1.00 37.98  ? 285  GLN A N   1 
ATOM   1678  C  CA  . GLN A 1 310 ? 114.706 151.455 102.055 1.00 37.87  ? 285  GLN A CA  1 
ATOM   1679  C  C   . GLN A 1 310 ? 115.475 150.615 103.066 1.00 37.36  ? 285  GLN A C   1 
ATOM   1680  O  O   . GLN A 1 310 ? 115.321 149.390 103.065 1.00 46.28  ? 285  GLN A O   1 
ATOM   1681  C  CB  . GLN A 1 310 ? 115.098 151.012 100.637 1.00 40.67  ? 285  GLN A CB  1 
ATOM   1682  C  CG  . GLN A 1 310 ? 114.431 151.822 99.544  1.00 42.85  ? 285  GLN A CG  1 
ATOM   1683  C  CD  . GLN A 1 310 ? 115.359 152.126 98.395  1.00 47.59  ? 285  GLN A CD  1 
ATOM   1684  O  OE1 . GLN A 1 310 ? 115.468 153.272 97.962  1.00 49.43  ? 285  GLN A OE1 1 
ATOM   1685  N  NE2 . GLN A 1 310 ? 116.039 151.102 97.892  1.00 47.49  ? 285  GLN A NE2 1 
ATOM   1686  N  N   . LYS A 1 311 ? 116.293 151.226 103.920 1.00 26.31  ? 286  LYS A N   1 
ATOM   1687  C  CA  . LYS A 1 311 ? 117.028 150.505 104.948 1.00 31.09  ? 286  LYS A CA  1 
ATOM   1688  C  C   . LYS A 1 311 ? 116.967 151.300 106.243 1.00 37.21  ? 286  LYS A C   1 
ATOM   1689  O  O   . LYS A 1 311 ? 116.625 152.484 106.252 1.00 46.67  ? 286  LYS A O   1 
ATOM   1690  C  CB  . LYS A 1 311 ? 118.484 150.257 104.539 1.00 30.25  ? 286  LYS A CB  1 
ATOM   1691  C  CG  . LYS A 1 311 ? 118.647 149.434 103.277 1.00 34.75  ? 286  LYS A CG  1 
ATOM   1692  C  CD  . LYS A 1 311 ? 120.074 149.486 102.774 1.00 37.81  ? 286  LYS A CD  1 
ATOM   1693  C  CE  . LYS A 1 311 ? 120.175 148.937 101.366 1.00 31.51  ? 286  LYS A CE  1 
ATOM   1694  N  NZ  . LYS A 1 311 ? 119.491 147.625 101.247 1.00 33.43  ? 286  LYS A NZ  1 
ATOM   1695  N  N   . ALA A 1 312 ? 117.304 150.639 107.348 1.00 25.46  ? 287  ALA A N   1 
ATOM   1696  C  CA  . ALA A 1 312 ? 117.282 151.287 108.652 1.00 13.90  ? 287  ALA A CA  1 
ATOM   1697  C  C   . ALA A 1 312 ? 118.311 150.632 109.558 1.00 23.38  ? 287  ALA A C   1 
ATOM   1698  O  O   . ALA A 1 312 ? 118.406 149.403 109.600 1.00 45.26  ? 287  ALA A O   1 
ATOM   1699  C  CB  . ALA A 1 312 ? 115.890 151.208 109.283 1.00 23.13  ? 287  ALA A CB  1 
ATOM   1700  N  N   . ILE A 1 313 ? 119.076 151.452 110.275 1.00 24.81  ? 288  ILE A N   1 
ATOM   1701  C  CA  . ILE A 1 313 ? 120.064 150.976 111.244 1.00 27.40  ? 288  ILE A CA  1 
ATOM   1702  C  C   . ILE A 1 313 ? 119.741 151.673 112.562 1.00 36.90  ? 288  ILE A C   1 
ATOM   1703  O  O   . ILE A 1 313 ? 120.152 152.813 112.798 1.00 45.22  ? 288  ILE A O   1 
ATOM   1704  C  CB  . ILE A 1 313 ? 121.506 151.256 110.811 1.00 22.79  ? 288  ILE A CB  1 
ATOM   1705  C  CG1 . ILE A 1 313 ? 121.747 150.774 109.382 1.00 30.49  ? 288  ILE A CG1 1 
ATOM   1706  C  CG2 . ILE A 1 313 ? 122.485 150.600 111.765 1.00 31.11  ? 288  ILE A CG2 1 
ATOM   1707  C  CD1 . ILE A 1 313 ? 123.102 151.154 108.837 1.00 33.72  ? 288  ILE A CD1 1 
ATOM   1708  N  N   . ALA A 1 314 ? 119.003 150.991 113.433 1.00 17.58  ? 289  ALA A N   1 
ATOM   1709  C  CA  . ALA A 1 314 ? 118.613 151.534 114.729 1.00 11.85  ? 289  ALA A CA  1 
ATOM   1710  C  C   . ALA A 1 314 ? 119.512 150.927 115.797 1.00 17.55  ? 289  ALA A C   1 
ATOM   1711  O  O   . ALA A 1 314 ? 119.404 149.736 116.103 1.00 47.30  ? 289  ALA A O   1 
ATOM   1712  C  CB  . ALA A 1 314 ? 117.143 151.245 115.019 1.00 19.24  ? 289  ALA A CB  1 
ATOM   1713  N  N   . GLN A 1 315 ? 120.395 151.742 116.365 1.00 3.21   ? 290  GLN A N   1 
ATOM   1714  C  CA  . GLN A 1 315 ? 121.348 151.292 117.369 1.00 21.50  ? 290  GLN A CA  1 
ATOM   1715  C  C   . GLN A 1 315 ? 121.029 151.937 118.711 1.00 24.03  ? 290  GLN A C   1 
ATOM   1716  O  O   . GLN A 1 315 ? 120.941 153.166 118.808 1.00 30.79  ? 290  GLN A O   1 
ATOM   1717  C  CB  . GLN A 1 315 ? 122.783 151.619 116.948 1.00 17.64  ? 290  GLN A CB  1 
ATOM   1718  C  CG  . GLN A 1 315 ? 122.981 153.020 116.397 1.00 26.65  ? 290  GLN A CG  1 
ATOM   1719  C  CD  . GLN A 1 315 ? 124.168 153.115 115.461 1.00 22.83  ? 290  GLN A CD  1 
ATOM   1720  O  OE1 . GLN A 1 315 ? 124.582 152.123 114.864 1.00 21.51  ? 290  GLN A OE1 1 
ATOM   1721  N  NE2 . GLN A 1 315 ? 124.724 154.312 115.330 1.00 19.17  ? 290  GLN A NE2 1 
ATOM   1722  N  N   . SER A 1 316 ? 120.861 151.104 119.738 1.00 12.55  ? 291  SER A N   1 
ATOM   1723  C  CA  . SER A 1 316 ? 120.593 151.559 121.102 1.00 12.58  ? 291  SER A CA  1 
ATOM   1724  C  C   . SER A 1 316 ? 119.378 152.484 121.151 1.00 30.63  ? 291  SER A C   1 
ATOM   1725  O  O   . SER A 1 316 ? 119.411 153.568 121.736 1.00 35.55  ? 291  SER A O   1 
ATOM   1726  C  CB  . SER A 1 316 ? 121.822 152.243 121.700 1.00 17.65  ? 291  SER A CB  1 
ATOM   1727  O  OG  . SER A 1 316 ? 122.940 151.375 121.697 1.00 36.65  ? 291  SER A OG  1 
ATOM   1728  N  N   . GLY A 1 317 ? 118.294 152.044 120.526 1.00 28.66  ? 292  GLY A N   1 
ATOM   1729  C  CA  . GLY A 1 317 ? 117.080 152.835 120.505 1.00 26.15  ? 292  GLY A CA  1 
ATOM   1730  C  C   . GLY A 1 317 ? 115.901 152.003 120.065 1.00 27.54  ? 292  GLY A C   1 
ATOM   1731  O  O   . GLY A 1 317 ? 116.050 150.995 119.366 1.00 23.86  ? 292  GLY A O   1 
ATOM   1732  N  N   . THR A 1 318 ? 114.718 152.441 120.488 1.00 25.92  ? 293  THR A N   1 
ATOM   1733  C  CA  . THR A 1 318 ? 113.486 151.724 120.195 1.00 14.75  ? 293  THR A CA  1 
ATOM   1734  C  C   . THR A 1 318 ? 112.331 152.712 120.258 1.00 21.99  ? 293  THR A C   1 
ATOM   1735  O  O   . THR A 1 318 ? 112.415 153.749 120.921 1.00 28.10  ? 293  THR A O   1 
ATOM   1736  C  CB  . THR A 1 318 ? 113.266 150.569 121.180 1.00 21.18  ? 293  THR A CB  1 
ATOM   1737  O  OG1 . THR A 1 318 ? 114.485 149.837 121.346 1.00 31.98  ? 293  THR A OG1 1 
ATOM   1738  C  CG2 . THR A 1 318 ? 112.209 149.621 120.663 1.00 21.76  ? 293  THR A CG2 1 
ATOM   1739  N  N   . ALA A 1 319 ? 111.249 152.379 119.558 1.00 16.73  ? 294  ALA A N   1 
ATOM   1740  C  CA  . ALA A 1 319 ? 110.022 153.161 119.601 1.00 13.99  ? 294  ALA A CA  1 
ATOM   1741  C  C   . ALA A 1 319 ? 109.008 152.614 120.593 1.00 23.92  ? 294  ALA A C   1 
ATOM   1742  O  O   . ALA A 1 319 ? 107.901 153.151 120.684 1.00 33.38  ? 294  ALA A O   1 
ATOM   1743  C  CB  . ALA A 1 319 ? 109.385 153.233 118.211 1.00 19.93  ? 294  ALA A CB  1 
ATOM   1744  N  N   . ILE A 1 320 ? 109.355 151.563 121.335 1.00 20.05  ? 295  ILE A N   1 
ATOM   1745  C  CA  . ILE A 1 320 ? 108.454 150.954 122.303 1.00 18.30  ? 295  ILE A CA  1 
ATOM   1746  C  C   . ILE A 1 320 ? 108.945 151.101 123.734 1.00 27.13  ? 295  ILE A C   1 
ATOM   1747  O  O   . ILE A 1 320 ? 108.232 150.708 124.662 1.00 36.09  ? 295  ILE A O   1 
ATOM   1748  C  CB  . ILE A 1 320 ? 108.197 149.469 121.975 1.00 17.00  ? 295  ILE A CB  1 
ATOM   1749  C  CG1 . ILE A 1 320 ? 109.272 148.580 122.594 1.00 20.59  ? 295  ILE A CG1 1 
ATOM   1750  C  CG2 . ILE A 1 320 ? 108.150 149.255 120.475 1.00 19.07  ? 295  ILE A CG2 1 
ATOM   1751  C  CD1 . ILE A 1 320 ? 109.120 147.120 122.242 1.00 24.08  ? 295  ILE A CD1 1 
ATOM   1752  N  N   . SER A 1 321 ? 110.132 151.665 123.944 1.00 23.49  ? 296  SER A N   1 
ATOM   1753  C  CA  . SER A 1 321 ? 110.622 151.898 125.292 1.00 21.11  ? 296  SER A CA  1 
ATOM   1754  C  C   . SER A 1 321 ? 109.818 153.011 125.962 1.00 26.01  ? 296  SER A C   1 
ATOM   1755  O  O   . SER A 1 321 ? 109.050 153.736 125.323 1.00 27.54  ? 296  SER A O   1 
ATOM   1756  C  CB  . SER A 1 321 ? 112.110 152.244 125.270 1.00 24.15  ? 296  SER A CB  1 
ATOM   1757  O  OG  . SER A 1 321 ? 112.332 153.504 124.665 1.00 30.91  ? 296  SER A OG  1 
ATOM   1758  N  N   . SER A 1 322 ? 110.003 153.140 127.278 1.00 32.39  ? 297  SER A N   1 
ATOM   1759  C  CA  . SER A 1 322 ? 109.162 154.040 128.061 1.00 28.91  ? 297  SER A CA  1 
ATOM   1760  C  C   . SER A 1 322 ? 109.363 155.502 127.679 1.00 34.46  ? 297  SER A C   1 
ATOM   1761  O  O   . SER A 1 322 ? 108.435 156.306 127.819 1.00 40.97  ? 297  SER A O   1 
ATOM   1762  C  CB  . SER A 1 322 ? 109.434 153.845 129.552 1.00 30.36  ? 297  SER A CB  1 
ATOM   1763  O  OG  . SER A 1 322 ? 110.429 154.743 130.008 1.00 35.17  ? 297  SER A OG  1 
ATOM   1764  N  N   . TRP A 1 323 ? 110.550 155.868 127.196 1.00 31.83  ? 298  TRP A N   1 
ATOM   1765  C  CA  . TRP A 1 323 ? 110.866 157.253 126.868 1.00 31.70  ? 298  TRP A CA  1 
ATOM   1766  C  C   . TRP A 1 323 ? 110.968 157.485 125.364 1.00 31.05  ? 298  TRP A C   1 
ATOM   1767  O  O   . TRP A 1 323 ? 111.726 158.348 124.914 1.00 32.98  ? 298  TRP A O   1 
ATOM   1768  C  CB  . TRP A 1 323 ? 112.159 157.685 127.559 1.00 32.33  ? 298  TRP A CB  1 
ATOM   1769  C  CG  . TRP A 1 323 ? 113.305 156.736 127.371 1.00 32.67  ? 298  TRP A CG  1 
ATOM   1770  C  CD1 . TRP A 1 323 ? 113.648 156.075 126.228 1.00 37.70  ? 298  TRP A CD1 1 
ATOM   1771  C  CD2 . TRP A 1 323 ? 114.263 156.345 128.360 1.00 27.04  ? 298  TRP A CD2 1 
ATOM   1772  N  NE1 . TRP A 1 323 ? 114.757 155.297 126.445 1.00 30.04  ? 298  TRP A NE1 1 
ATOM   1773  C  CE2 . TRP A 1 323 ? 115.153 155.446 127.747 1.00 22.80  ? 298  TRP A CE2 1 
ATOM   1774  C  CE3 . TRP A 1 323 ? 114.452 156.670 129.706 1.00 34.78  ? 298  TRP A CE3 1 
ATOM   1775  C  CZ2 . TRP A 1 323 ? 116.215 154.868 128.431 1.00 30.62  ? 298  TRP A CZ2 1 
ATOM   1776  C  CZ3 . TRP A 1 323 ? 115.506 156.095 130.382 1.00 36.01  ? 298  TRP A CZ3 1 
ATOM   1777  C  CH2 . TRP A 1 323 ? 116.374 155.205 129.745 1.00 32.32  ? 298  TRP A CH2 1 
ATOM   1778  N  N   . SER A 1 324 ? 110.213 156.725 124.573 1.00 26.24  ? 299  SER A N   1 
ATOM   1779  C  CA  . SER A 1 324 ? 110.249 156.874 123.125 1.00 18.10  ? 299  SER A CA  1 
ATOM   1780  C  C   . SER A 1 324 ? 109.175 157.833 122.623 1.00 28.06  ? 299  SER A C   1 
ATOM   1781  O  O   . SER A 1 324 ? 109.456 158.704 121.795 1.00 36.48  ? 299  SER A O   1 
ATOM   1782  C  CB  . SER A 1 324 ? 110.091 155.510 122.452 1.00 26.60  ? 299  SER A CB  1 
ATOM   1783  O  OG  . SER A 1 324 ? 108.727 155.233 122.195 1.00 36.01  ? 299  SER A OG  1 
ATOM   1784  N  N   . VAL A 1 325 ? 107.945 157.685 123.112 1.00 28.25  ? 300  VAL A N   1 
ATOM   1785  C  CA  . VAL A 1 325 ? 106.839 158.539 122.695 1.00 20.66  ? 300  VAL A CA  1 
ATOM   1786  C  C   . VAL A 1 325 ? 106.280 159.274 123.906 1.00 23.66  ? 300  VAL A C   1 
ATOM   1787  O  O   . VAL A 1 325 ? 106.740 159.074 125.035 1.00 33.45  ? 300  VAL A O   1 
ATOM   1788  C  CB  . VAL A 1 325 ? 105.741 157.723 121.990 1.00 18.14  ? 300  VAL A CB  1 
ATOM   1789  C  CG1 . VAL A 1 325 ? 106.172 157.368 120.580 1.00 26.09  ? 300  VAL A CG1 1 
ATOM   1790  C  CG2 . VAL A 1 325 ? 105.433 156.468 122.780 1.00 25.91  ? 300  VAL A CG2 1 
ATOM   1791  N  N   . ASN A 1 326 ? 105.287 160.130 123.678 1.00 35.83  ? 301  ASN A N   1 
ATOM   1792  C  CA  . ASN A 1 326 ? 104.664 160.923 124.734 1.00 32.68  ? 301  ASN A CA  1 
ATOM   1793  C  C   . ASN A 1 326 ? 103.164 160.669 124.700 1.00 45.55  ? 301  ASN A C   1 
ATOM   1794  O  O   . ASN A 1 326 ? 102.494 161.019 123.723 1.00 50.05  ? 301  ASN A O   1 
ATOM   1795  C  CB  . ASN A 1 326 ? 104.970 162.410 124.557 1.00 32.15  ? 301  ASN A CB  1 
ATOM   1796  C  CG  . ASN A 1 326 ? 104.526 163.240 125.739 1.00 36.53  ? 301  ASN A CG  1 
ATOM   1797  O  OD1 . ASN A 1 326 ? 104.192 162.708 126.796 1.00 41.86  ? 301  ASN A OD1 1 
ATOM   1798  N  ND2 . ASN A 1 326 ? 104.520 164.556 125.568 1.00 41.05  ? 301  ASN A ND2 1 
ATOM   1799  N  N   . TYR A 1 327 ? 102.637 160.064 125.764 1.00 47.14  ? 302  TYR A N   1 
ATOM   1800  C  CA  . TYR A 1 327 ? 101.223 159.724 125.842 1.00 41.45  ? 302  TYR A CA  1 
ATOM   1801  C  C   . TYR A 1 327 ? 100.389 160.756 126.588 1.00 46.65  ? 302  TYR A C   1 
ATOM   1802  O  O   . TYR A 1 327 ? 99.160  160.635 126.607 1.00 51.80  ? 302  TYR A O   1 
ATOM   1803  C  CB  . TYR A 1 327 ? 101.044 158.356 126.507 1.00 39.02  ? 302  TYR A CB  1 
ATOM   1804  C  CG  . TYR A 1 327 ? 101.593 157.206 125.698 1.00 42.85  ? 302  TYR A CG  1 
ATOM   1805  C  CD1 . TYR A 1 327 ? 101.036 156.869 124.473 1.00 44.09  ? 302  TYR A CD1 1 
ATOM   1806  C  CD2 . TYR A 1 327 ? 102.664 156.457 126.159 1.00 46.84  ? 302  TYR A CD2 1 
ATOM   1807  C  CE1 . TYR A 1 327 ? 101.532 155.819 123.729 1.00 46.02  ? 302  TYR A CE1 1 
ATOM   1808  C  CE2 . TYR A 1 327 ? 103.167 155.405 125.422 1.00 48.96  ? 302  TYR A CE2 1 
ATOM   1809  C  CZ  . TYR A 1 327 ? 102.597 155.090 124.209 1.00 51.96  ? 302  TYR A CZ  1 
ATOM   1810  O  OH  . TYR A 1 327 ? 103.096 154.042 123.471 1.00 55.43  ? 302  TYR A OH  1 
ATOM   1811  N  N   . GLN A 1 328 ? 101.013 161.757 127.203 1.00 46.73  ? 303  GLN A N   1 
ATOM   1812  C  CA  . GLN A 1 328 ? 100.304 162.828 127.904 1.00 44.14  ? 303  GLN A CA  1 
ATOM   1813  C  C   . GLN A 1 328 ? 100.835 164.172 127.426 1.00 48.83  ? 303  GLN A C   1 
ATOM   1814  O  O   . GLN A 1 328 ? 101.535 164.876 128.163 1.00 52.32  ? 303  GLN A O   1 
ATOM   1815  C  CB  . GLN A 1 328 ? 100.450 162.692 129.420 1.00 48.25  ? 303  GLN A CB  1 
ATOM   1816  C  CG  . GLN A 1 328 ? 100.295 161.280 129.949 1.00 52.83  ? 303  GLN A CG  1 
ATOM   1817  C  CD  . GLN A 1 328 ? 100.267 161.231 131.462 1.00 56.43  ? 303  GLN A CD  1 
ATOM   1818  O  OE1 . GLN A 1 328 ? 101.302 161.069 132.109 1.00 53.21  ? 303  GLN A OE1 1 
ATOM   1819  N  NE2 . GLN A 1 328 ? 99.079  161.373 132.037 1.00 55.91  ? 303  GLN A NE2 1 
ATOM   1820  N  N   . PRO A 1 329 ? 100.518 164.562 126.194 1.00 50.90  ? 304  PRO A N   1 
ATOM   1821  C  CA  . PRO A 1 329 ? 101.043 165.829 125.672 1.00 51.59  ? 304  PRO A CA  1 
ATOM   1822  C  C   . PRO A 1 329 ? 100.311 167.038 126.231 1.00 56.27  ? 304  PRO A C   1 
ATOM   1823  O  O   . PRO A 1 329 ? 100.919 168.088 126.467 1.00 58.03  ? 304  PRO A O   1 
ATOM   1824  C  CB  . PRO A 1 329 ? 100.830 165.693 124.161 1.00 51.42  ? 304  PRO A CB  1 
ATOM   1825  C  CG  . PRO A 1 329 ? 99.637  164.807 124.038 1.00 55.69  ? 304  PRO A CG  1 
ATOM   1826  C  CD  . PRO A 1 329 ? 99.647  163.877 125.223 1.00 52.92  ? 304  PRO A CD  1 
ATOM   1827  N  N   . LEU A 1 330 ? 99.001  166.893 126.444 1.00 59.99  ? 305  LEU A N   1 
ATOM   1828  C  CA  . LEU A 1 330 ? 98.188  168.023 126.879 1.00 59.91  ? 305  LEU A CA  1 
ATOM   1829  C  C   . LEU A 1 330 ? 98.605  168.511 128.259 1.00 60.54  ? 305  LEU A C   1 
ATOM   1830  O  O   . LEU A 1 330 ? 98.678  169.721 128.500 1.00 62.38  ? 305  LEU A O   1 
ATOM   1831  C  CB  . LEU A 1 330 ? 96.708  167.639 126.867 1.00 59.02  ? 305  LEU A CB  1 
ATOM   1832  C  CG  . LEU A 1 330 ? 95.701  168.791 126.875 1.00 60.78  ? 305  LEU A CG  1 
ATOM   1833  C  CD1 . LEU A 1 330 ? 96.202  169.955 126.038 1.00 61.66  ? 305  LEU A CD1 1 
ATOM   1834  C  CD2 . LEU A 1 330 ? 94.346  168.319 126.376 1.00 60.80  ? 305  LEU A CD2 1 
ATOM   1835  N  N   . LYS A 1 331 ? 98.893  167.585 129.176 1.00 57.29  ? 306  LYS A N   1 
ATOM   1836  C  CA  . LYS A 1 331 ? 99.278  167.972 130.530 1.00 58.30  ? 306  LYS A CA  1 
ATOM   1837  C  C   . LYS A 1 331 ? 100.536 168.832 130.523 1.00 59.58  ? 306  LYS A C   1 
ATOM   1838  O  O   . LYS A 1 331 ? 100.562 169.926 131.101 1.00 63.96  ? 306  LYS A O   1 
ATOM   1839  C  CB  . LYS A 1 331 ? 99.482  166.721 131.385 1.00 55.79  ? 306  LYS A CB  1 
ATOM   1840  C  CG  . LYS A 1 331 ? 100.334 166.939 132.623 1.00 59.69  ? 306  LYS A CG  1 
ATOM   1841  C  CD  . LYS A 1 331 ? 99.909  166.014 133.750 1.00 60.32  ? 306  LYS A CD  1 
ATOM   1842  C  CE  . LYS A 1 331 ? 100.714 164.726 133.739 1.00 56.62  ? 306  LYS A CE  1 
ATOM   1843  N  NZ  . LYS A 1 331 ? 101.974 164.853 134.520 1.00 56.79  ? 306  LYS A NZ  1 
ATOM   1844  N  N   . TYR A 1 332 ? 101.588 168.362 129.850 1.00 62.18  ? 307  TYR A N   1 
ATOM   1845  C  CA  . TYR A 1 332 ? 102.849 169.094 129.861 1.00 62.97  ? 307  TYR A CA  1 
ATOM   1846  C  C   . TYR A 1 332 ? 102.773 170.371 129.036 1.00 62.46  ? 307  TYR A C   1 
ATOM   1847  O  O   . TYR A 1 332 ? 103.385 171.379 129.408 1.00 62.84  ? 307  TYR A O   1 
ATOM   1848  C  CB  . TYR A 1 332 ? 103.983 168.196 129.370 1.00 61.02  ? 307  TYR A CB  1 
ATOM   1849  C  CG  . TYR A 1 332 ? 104.270 167.043 130.302 1.00 58.74  ? 307  TYR A CG  1 
ATOM   1850  C  CD1 . TYR A 1 332 ? 104.994 167.235 131.469 1.00 57.84  ? 307  TYR A CD1 1 
ATOM   1851  C  CD2 . TYR A 1 332 ? 103.810 165.766 130.020 1.00 60.66  ? 307  TYR A CD2 1 
ATOM   1852  C  CE1 . TYR A 1 332 ? 105.255 166.186 132.327 1.00 61.85  ? 307  TYR A CE1 1 
ATOM   1853  C  CE2 . TYR A 1 332 ? 104.067 164.710 130.871 1.00 61.09  ? 307  TYR A CE2 1 
ATOM   1854  C  CZ  . TYR A 1 332 ? 104.790 164.926 132.023 1.00 63.90  ? 307  TYR A CZ  1 
ATOM   1855  O  OH  . TYR A 1 332 ? 105.048 163.876 132.873 1.00 65.82  ? 307  TYR A OH  1 
ATOM   1856  N  N   . THR A 1 333 ? 102.026 170.365 127.927 1.00 63.47  ? 308  THR A N   1 
ATOM   1857  C  CA  . THR A 1 333 ? 101.889 171.602 127.167 1.00 64.96  ? 308  THR A CA  1 
ATOM   1858  C  C   . THR A 1 333 ? 101.097 172.648 127.945 1.00 67.95  ? 308  THR A C   1 
ATOM   1859  O  O   . THR A 1 333 ? 101.406 173.840 127.859 1.00 66.63  ? 308  THR A O   1 
ATOM   1860  C  CB  . THR A 1 333 ? 101.260 171.336 125.794 1.00 63.28  ? 308  THR A CB  1 
ATOM   1861  O  OG1 . THR A 1 333 ? 101.503 172.456 124.935 1.00 66.61  ? 308  THR A OG1 1 
ATOM   1862  C  CG2 . THR A 1 333 ? 99.764  171.116 125.892 1.00 63.18  ? 308  THR A CG2 1 
ATOM   1863  N  N   . ARG A 1 334 ? 100.106 172.229 128.739 1.00 79.44  ? 309  ARG A N   1 
ATOM   1864  C  CA  . ARG A 1 334 ? 99.382  173.183 129.571 1.00 76.72  ? 309  ARG A CA  1 
ATOM   1865  C  C   . ARG A 1 334 ? 100.253 173.686 130.714 1.00 77.27  ? 309  ARG A C   1 
ATOM   1866  O  O   . ARG A 1 334 ? 100.182 174.865 131.080 1.00 83.26  ? 309  ARG A O   1 
ATOM   1867  C  CB  . ARG A 1 334 ? 98.099  172.549 130.106 1.00 76.88  ? 309  ARG A CB  1 
ATOM   1868  C  CG  . ARG A 1 334 ? 96.940  172.602 129.127 1.00 78.45  ? 309  ARG A CG  1 
ATOM   1869  C  CD  . ARG A 1 334 ? 95.633  172.215 129.794 1.00 80.49  ? 309  ARG A CD  1 
ATOM   1870  N  NE  . ARG A 1 334 ? 94.481  172.604 128.990 1.00 80.66  ? 309  ARG A NE  1 
ATOM   1871  C  CZ  . ARG A 1 334 ? 93.950  173.819 128.980 1.00 83.09  ? 309  ARG A CZ  1 
ATOM   1872  N  NH1 . ARG A 1 334 ? 94.443  174.795 129.726 1.00 82.66  ? 309  ARG A NH1 1 
ATOM   1873  N  NH2 . ARG A 1 334 ? 92.898  174.062 128.203 1.00 83.94  ? 309  ARG A NH2 1 
ATOM   1874  N  N   . LEU A 1 335 ? 101.082 172.811 131.288 1.00 71.68  ? 310  LEU A N   1 
ATOM   1875  C  CA  . LEU A 1 335 ? 102.039 173.256 132.296 1.00 70.91  ? 310  LEU A CA  1 
ATOM   1876  C  C   . LEU A 1 335 ? 102.974 174.314 131.722 1.00 72.38  ? 310  LEU A C   1 
ATOM   1877  O  O   . LEU A 1 335 ? 103.210 175.359 132.343 1.00 77.08  ? 310  LEU A O   1 
ATOM   1878  C  CB  . LEU A 1 335 ? 102.838 172.064 132.823 1.00 71.97  ? 310  LEU A CB  1 
ATOM   1879  C  CG  . LEU A 1 335 ? 102.507 171.550 134.224 1.00 74.16  ? 310  LEU A CG  1 
ATOM   1880  C  CD1 . LEU A 1 335 ? 101.214 170.750 134.217 1.00 73.56  ? 310  LEU A CD1 1 
ATOM   1881  C  CD2 . LEU A 1 335 ? 103.654 170.712 134.765 1.00 72.00  ? 310  LEU A CD2 1 
ATOM   1882  N  N   . LEU A 1 336 ? 103.503 174.063 130.523 1.00 74.25  ? 311  LEU A N   1 
ATOM   1883  C  CA  . LEU A 1 336 ? 104.385 175.030 129.880 1.00 76.80  ? 311  LEU A CA  1 
ATOM   1884  C  C   . LEU A 1 336 ? 103.659 176.334 129.575 1.00 78.54  ? 311  LEU A C   1 
ATOM   1885  O  O   . LEU A 1 336 ? 104.215 177.419 129.770 1.00 80.05  ? 311  LEU A O   1 
ATOM   1886  C  CB  . LEU A 1 336 ? 104.962 174.442 128.597 1.00 77.25  ? 311  LEU A CB  1 
ATOM   1887  C  CG  . LEU A 1 336 ? 105.756 175.449 127.767 1.00 71.39  ? 311  LEU A CG  1 
ATOM   1888  C  CD1 . LEU A 1 336 ? 107.203 175.533 128.229 1.00 71.29  ? 311  LEU A CD1 1 
ATOM   1889  C  CD2 . LEU A 1 336 ? 105.657 175.101 126.304 1.00 72.13  ? 311  LEU A CD2 1 
ATOM   1890  N  N   . ALA A 1 337 ? 102.425 176.248 129.074 1.00 87.72  ? 312  ALA A N   1 
ATOM   1891  C  CA  . ALA A 1 337 ? 101.672 177.456 128.756 1.00 87.06  ? 312  ALA A CA  1 
ATOM   1892  C  C   . ALA A 1 337 ? 101.411 178.286 130.005 1.00 87.82  ? 312  ALA A C   1 
ATOM   1893  O  O   . ALA A 1 337 ? 101.544 179.515 129.982 1.00 90.54  ? 312  ALA A O   1 
ATOM   1894  C  CB  . ALA A 1 337 ? 100.359 177.090 128.066 1.00 87.45  ? 312  ALA A CB  1 
ATOM   1895  N  N   . ALA A 1 338 ? 101.043 177.632 131.108 1.00 90.35  ? 313  ALA A N   1 
ATOM   1896  C  CA  . ALA A 1 338 ? 100.828 178.354 132.356 1.00 91.13  ? 313  ALA A CA  1 
ATOM   1897  C  C   . ALA A 1 338 ? 102.120 178.982 132.859 1.00 91.50  ? 313  ALA A C   1 
ATOM   1898  O  O   . ALA A 1 338 ? 102.114 180.110 133.367 1.00 92.26  ? 313  ALA A O   1 
ATOM   1899  C  CB  . ALA A 1 338 ? 100.239 177.417 133.410 1.00 87.35  ? 313  ALA A CB  1 
ATOM   1900  N  N   . LYS A 1 339 ? 103.241 178.268 132.729 1.00 94.29  ? 314  LYS A N   1 
ATOM   1901  C  CA  . LYS A 1 339 ? 104.510 178.800 133.217 1.00 95.23  ? 314  LYS A CA  1 
ATOM   1902  C  C   . LYS A 1 339 ? 104.985 179.982 132.378 1.00 93.55  ? 314  LYS A C   1 
ATOM   1903  O  O   . LYS A 1 339 ? 105.519 180.958 132.919 1.00 94.12  ? 314  LYS A O   1 
ATOM   1904  C  CB  . LYS A 1 339 ? 105.564 177.694 133.235 1.00 92.71  ? 314  LYS A CB  1 
ATOM   1905  C  CG  . LYS A 1 339 ? 106.866 178.088 133.908 1.00 92.23  ? 314  LYS A CG  1 
ATOM   1906  C  CD  . LYS A 1 339 ? 107.774 176.884 134.091 1.00 92.33  ? 314  LYS A CD  1 
ATOM   1907  C  CE  . LYS A 1 339 ? 107.115 175.823 134.958 1.00 93.11  ? 314  LYS A CE  1 
ATOM   1908  N  NZ  . LYS A 1 339 ? 108.037 174.689 135.242 1.00 94.69  ? 314  LYS A NZ  1 
ATOM   1909  N  N   . VAL A 1 340 ? 104.803 179.914 131.057 1.00 99.46  ? 315  VAL A N   1 
ATOM   1910  C  CA  . VAL A 1 340 ? 105.362 180.935 130.175 1.00 102.14 ? 315  VAL A CA  1 
ATOM   1911  C  C   . VAL A 1 340 ? 104.620 182.259 130.316 1.00 103.19 ? 315  VAL A C   1 
ATOM   1912  O  O   . VAL A 1 340 ? 105.223 183.330 130.168 1.00 102.39 ? 315  VAL A O   1 
ATOM   1913  C  CB  . VAL A 1 340 ? 105.383 180.433 128.716 1.00 101.64 ? 315  VAL A CB  1 
ATOM   1914  C  CG1 . VAL A 1 340 ? 104.012 180.551 128.066 1.00 101.07 ? 315  VAL A CG1 1 
ATOM   1915  C  CG2 . VAL A 1 340 ? 106.425 181.192 127.912 1.00 99.01  ? 315  VAL A CG2 1 
ATOM   1916  N  N   . GLY A 1 341 ? 103.320 182.225 130.602 1.00 117.40 ? 316  GLY A N   1 
ATOM   1917  C  CA  . GLY A 1 341 ? 102.593 183.461 130.815 1.00 117.86 ? 316  GLY A CA  1 
ATOM   1918  C  C   . GLY A 1 341 ? 101.188 183.525 130.249 1.00 118.32 ? 316  GLY A C   1 
ATOM   1919  O  O   . GLY A 1 341 ? 100.489 184.519 130.462 1.00 119.92 ? 316  GLY A O   1 
ATOM   1920  N  N   . CYS A 1 342 ? 100.751 182.492 129.531 1.00 120.77 ? 317  CYS A N   1 
ATOM   1921  C  CA  . CYS A 1 342 ? 99.383  182.471 129.021 1.00 122.64 ? 317  CYS A CA  1 
ATOM   1922  C  C   . CYS A 1 342 ? 98.900  181.033 128.921 1.00 121.93 ? 317  CYS A C   1 
ATOM   1923  O  O   . CYS A 1 342 ? 99.494  180.223 128.204 1.00 121.36 ? 317  CYS A O   1 
ATOM   1924  C  CB  . CYS A 1 342 ? 99.280  183.175 127.662 1.00 123.39 ? 317  CYS A CB  1 
ATOM   1925  S  SG  . CYS A 1 342 ? 100.200 182.446 126.284 1.00 126.16 ? 317  CYS A SG  1 
ATOM   1926  N  N   . ASP A 1 343 ? 97.824  180.722 129.644 1.00 114.49 ? 318  ASP A N   1 
ATOM   1927  C  CA  . ASP A 1 343 ? 97.188  179.405 129.608 1.00 114.55 ? 318  ASP A CA  1 
ATOM   1928  C  C   . ASP A 1 343 ? 95.697  179.631 129.378 1.00 115.38 ? 318  ASP A C   1 
ATOM   1929  O  O   . ASP A 1 343 ? 94.916  179.701 130.330 1.00 115.51 ? 318  ASP A O   1 
ATOM   1930  C  CB  . ASP A 1 343 ? 97.453  178.626 130.894 1.00 113.41 ? 318  ASP A CB  1 
ATOM   1931  C  CG  . ASP A 1 343 ? 97.081  177.160 130.775 1.00 112.64 ? 318  ASP A CG  1 
ATOM   1932  O  OD1 . ASP A 1 343 ? 96.592  176.752 129.701 1.00 112.29 ? 318  ASP A OD1 1 
ATOM   1933  O  OD2 . ASP A 1 343 ? 97.278  176.415 131.758 1.00 112.44 ? 318  ASP A OD2 1 
ATOM   1934  N  N   . ARG A 1 344 ? 95.308  179.746 128.113 1.00 125.37 ? 319  ARG A N   1 
ATOM   1935  C  CA  . ARG A 1 344 ? 93.907  179.923 127.764 1.00 124.78 ? 319  ARG A CA  1 
ATOM   1936  C  C   . ARG A 1 344 ? 93.156  178.605 127.894 1.00 125.68 ? 319  ARG A C   1 
ATOM   1937  O  O   . ARG A 1 344 ? 93.696  177.534 127.604 1.00 125.44 ? 319  ARG A O   1 
ATOM   1938  C  CB  . ARG A 1 344 ? 93.773  180.462 126.341 1.00 124.39 ? 319  ARG A CB  1 
ATOM   1939  C  CG  . ARG A 1 344 ? 94.625  181.687 126.050 1.00 124.75 ? 319  ARG A CG  1 
ATOM   1940  C  CD  . ARG A 1 344 ? 94.137  182.891 126.837 1.00 124.56 ? 319  ARG A CD  1 
ATOM   1941  N  NE  . ARG A 1 344 ? 95.104  183.982 126.830 1.00 125.47 ? 319  ARG A NE  1 
ATOM   1942  C  CZ  . ARG A 1 344 ? 95.929  184.258 127.829 1.00 125.47 ? 319  ARG A CZ  1 
ATOM   1943  N  NH1 . ARG A 1 344 ? 95.942  183.534 128.936 1.00 125.44 ? 319  ARG A NH1 1 
ATOM   1944  N  NH2 . ARG A 1 344 ? 96.763  185.289 127.717 1.00 124.80 ? 319  ARG A NH2 1 
ATOM   1945  N  N   . GLU A 1 345 ? 91.900  178.692 128.339 1.00 131.70 ? 320  GLU A N   1 
ATOM   1946  C  CA  . GLU A 1 345 ? 91.064  177.502 128.441 1.00 131.16 ? 320  GLU A CA  1 
ATOM   1947  C  C   . GLU A 1 345 ? 90.792  176.875 127.081 1.00 130.90 ? 320  GLU A C   1 
ATOM   1948  O  O   . GLU A 1 345 ? 90.453  175.689 127.013 1.00 130.79 ? 320  GLU A O   1 
ATOM   1949  C  CB  . GLU A 1 345 ? 89.745  177.845 129.135 1.00 131.54 ? 320  GLU A CB  1 
ATOM   1950  C  CG  . GLU A 1 345 ? 89.913  178.618 130.433 1.00 131.10 ? 320  GLU A CG  1 
ATOM   1951  C  CD  . GLU A 1 345 ? 90.891  177.956 131.385 1.00 131.72 ? 320  GLU A CD  1 
ATOM   1952  O  OE1 . GLU A 1 345 ? 90.765  176.735 131.618 1.00 131.53 ? 320  GLU A OE1 1 
ATOM   1953  O  OE2 . GLU A 1 345 ? 91.787  178.657 131.901 1.00 131.41 ? 320  GLU A OE2 1 
ATOM   1954  N  N   . ASP A 1 346 ? 90.929  177.642 126.004 1.00 130.26 ? 321  ASP A N   1 
ATOM   1955  C  CA  . ASP A 1 346 ? 90.801  177.129 124.648 1.00 131.00 ? 321  ASP A CA  1 
ATOM   1956  C  C   . ASP A 1 346 ? 92.187  176.802 124.110 1.00 132.08 ? 321  ASP A C   1 
ATOM   1957  O  O   . ASP A 1 346 ? 93.107  177.621 124.213 1.00 131.73 ? 321  ASP A O   1 
ATOM   1958  C  CB  . ASP A 1 346 ? 90.103  178.146 123.743 1.00 130.13 ? 321  ASP A CB  1 
ATOM   1959  C  CG  . ASP A 1 346 ? 89.706  177.558 122.404 1.00 131.40 ? 321  ASP A CG  1 
ATOM   1960  O  OD1 . ASP A 1 346 ? 89.637  176.316 122.296 1.00 132.14 ? 321  ASP A OD1 1 
ATOM   1961  O  OD2 . ASP A 1 346 ? 89.464  178.339 121.460 1.00 130.94 ? 321  ASP A OD2 1 
ATOM   1962  N  N   . SER A 1 347 ? 92.335  175.601 123.546 1.00 123.16 ? 322  SER A N   1 
ATOM   1963  C  CA  . SER A 1 347 ? 93.641  175.165 123.063 1.00 120.99 ? 322  SER A CA  1 
ATOM   1964  C  C   . SER A 1 347 ? 94.132  176.040 121.915 1.00 123.25 ? 322  SER A C   1 
ATOM   1965  O  O   . SER A 1 347 ? 95.320  176.375 121.845 1.00 123.18 ? 322  SER A O   1 
ATOM   1966  C  CB  . SER A 1 347 ? 93.578  173.700 122.633 1.00 119.76 ? 322  SER A CB  1 
ATOM   1967  O  OG  . SER A 1 347 ? 93.118  172.879 123.693 1.00 120.49 ? 322  SER A OG  1 
ATOM   1968  N  N   . THR A 1 348 ? 93.232  176.412 121.001 1.00 123.25 ? 323  THR A N   1 
ATOM   1969  C  CA  . THR A 1 348 ? 93.629  177.243 119.868 1.00 121.50 ? 323  THR A CA  1 
ATOM   1970  C  C   . THR A 1 348 ? 94.134  178.604 120.331 1.00 120.46 ? 323  THR A C   1 
ATOM   1971  O  O   . THR A 1 348 ? 95.126  179.119 119.802 1.00 119.45 ? 323  THR A O   1 
ATOM   1972  C  CB  . THR A 1 348 ? 92.457  177.408 118.900 1.00 120.16 ? 323  THR A CB  1 
ATOM   1973  O  OG1 . THR A 1 348 ? 91.981  176.118 118.499 1.00 120.65 ? 323  THR A OG1 1 
ATOM   1974  C  CG2 . THR A 1 348 ? 92.889  178.186 117.668 1.00 120.16 ? 323  THR A CG2 1 
ATOM   1975  N  N   . GLU A 1 349 ? 93.463  179.200 121.319 1.00 123.23 ? 324  GLU A N   1 
ATOM   1976  C  CA  . GLU A 1 349 ? 93.914  180.482 121.850 1.00 124.09 ? 324  GLU A CA  1 
ATOM   1977  C  C   . GLU A 1 349 ? 95.290  180.360 122.491 1.00 125.16 ? 324  GLU A C   1 
ATOM   1978  O  O   . GLU A 1 349 ? 96.143  181.240 122.321 1.00 126.26 ? 324  GLU A O   1 
ATOM   1979  C  CB  . GLU A 1 349 ? 92.897  181.016 122.858 1.00 124.80 ? 324  GLU A CB  1 
ATOM   1980  C  CG  . GLU A 1 349 ? 91.545  181.358 122.255 1.00 125.56 ? 324  GLU A CG  1 
ATOM   1981  C  CD  . GLU A 1 349 ? 90.613  182.016 123.253 1.00 125.75 ? 324  GLU A CD  1 
ATOM   1982  O  OE1 . GLU A 1 349 ? 90.991  182.124 124.439 1.00 125.68 ? 324  GLU A OE1 1 
ATOM   1983  O  OE2 . GLU A 1 349 ? 89.503  182.423 122.853 1.00 125.05 ? 324  GLU A OE2 1 
ATOM   1984  N  N   . ALA A 1 350 ? 95.525  179.276 123.234 1.00 118.99 ? 325  ALA A N   1 
ATOM   1985  C  CA  . ALA A 1 350 ? 96.833  179.066 123.847 1.00 118.40 ? 325  ALA A CA  1 
ATOM   1986  C  C   . ALA A 1 350 ? 97.918  178.903 122.790 1.00 118.06 ? 325  ALA A C   1 
ATOM   1987  O  O   . ALA A 1 350 ? 99.015  179.458 122.925 1.00 117.73 ? 325  ALA A O   1 
ATOM   1988  C  CB  . ALA A 1 350 ? 96.793  177.848 124.768 1.00 117.42 ? 325  ALA A CB  1 
ATOM   1989  N  N   . VAL A 1 351 ? 97.631  178.143 121.730 1.00 108.56 ? 326  VAL A N   1 
ATOM   1990  C  CA  . VAL A 1 351 ? 98.606  177.961 120.658 1.00 107.70 ? 326  VAL A CA  1 
ATOM   1991  C  C   . VAL A 1 351 ? 98.902  179.289 119.975 1.00 108.91 ? 326  VAL A C   1 
ATOM   1992  O  O   . VAL A 1 351 ? 100.061 179.606 119.670 1.00 108.83 ? 326  VAL A O   1 
ATOM   1993  C  CB  . VAL A 1 351 ? 98.105  176.905 119.655 1.00 107.60 ? 326  VAL A CB  1 
ATOM   1994  C  CG1 . VAL A 1 351 ? 98.990  176.879 118.420 1.00 107.15 ? 326  VAL A CG1 1 
ATOM   1995  C  CG2 . VAL A 1 351 ? 98.062  175.534 120.309 1.00 108.18 ? 326  VAL A CG2 1 
ATOM   1996  N  N   . GLU A 1 352 ? 97.863  180.087 119.720 1.00 112.19 ? 327  GLU A N   1 
ATOM   1997  C  CA  . GLU A 1 352 ? 98.066  181.373 119.063 1.00 111.08 ? 327  GLU A CA  1 
ATOM   1998  C  C   . GLU A 1 352 ? 98.863  182.326 119.945 1.00 111.19 ? 327  GLU A C   1 
ATOM   1999  O  O   . GLU A 1 352 ? 99.683  183.102 119.442 1.00 111.79 ? 327  GLU A O   1 
ATOM   2000  C  CB  . GLU A 1 352 ? 96.721  181.987 118.680 1.00 110.70 ? 327  GLU A CB  1 
ATOM   2001  C  CG  . GLU A 1 352 ? 96.720  182.655 117.315 1.00 110.82 ? 327  GLU A CG  1 
ATOM   2002  C  CD  . GLU A 1 352 ? 97.079  181.694 116.197 1.00 111.06 ? 327  GLU A CD  1 
ATOM   2003  O  OE1 . GLU A 1 352 ? 96.628  180.531 116.243 1.00 110.54 ? 327  GLU A OE1 1 
ATOM   2004  O  OE2 . GLU A 1 352 ? 97.815  182.103 115.274 1.00 111.78 ? 327  GLU A OE2 1 
ATOM   2005  N  N   . CYS A 1 353 ? 98.633  182.292 121.261 1.00 109.79 ? 328  CYS A N   1 
ATOM   2006  C  CA  . CYS A 1 353 ? 99.449  183.099 122.163 1.00 109.55 ? 328  CYS A CA  1 
ATOM   2007  C  C   . CYS A 1 353 ? 100.898 182.631 122.159 1.00 110.12 ? 328  CYS A C   1 
ATOM   2008  O  O   . CYS A 1 353 ? 101.821 183.452 122.156 1.00 110.15 ? 328  CYS A O   1 
ATOM   2009  C  CB  . CYS A 1 353 ? 98.888  183.058 123.583 1.00 111.26 ? 328  CYS A CB  1 
ATOM   2010  S  SG  . CYS A 1 353 ? 100.000 183.818 124.800 1.00 121.37 ? 328  CYS A SG  1 
ATOM   2011  N  N   . LEU A 1 354 ? 101.113 181.313 122.161 1.00 99.76  ? 329  LEU A N   1 
ATOM   2012  C  CA  . LEU A 1 354 ? 102.472 180.779 122.157 1.00 99.34  ? 329  LEU A CA  1 
ATOM   2013  C  C   . LEU A 1 354 ? 103.214 181.173 120.887 1.00 98.33  ? 329  LEU A C   1 
ATOM   2014  O  O   . LEU A 1 354 ? 104.420 181.442 120.922 1.00 96.97  ? 329  LEU A O   1 
ATOM   2015  C  CB  . LEU A 1 354 ? 102.438 179.259 122.309 1.00 97.49  ? 329  LEU A CB  1 
ATOM   2016  C  CG  . LEU A 1 354 ? 102.314 178.716 123.733 1.00 98.30  ? 329  LEU A CG  1 
ATOM   2017  C  CD1 . LEU A 1 354 ? 102.083 177.215 123.715 1.00 97.30  ? 329  LEU A CD1 1 
ATOM   2018  C  CD2 . LEU A 1 354 ? 103.551 179.060 124.546 1.00 97.89  ? 329  LEU A CD2 1 
ATOM   2019  N  N   . ARG A 1 355 ? 102.509 181.210 119.754 1.00 89.92  ? 330  ARG A N   1 
ATOM   2020  C  CA  . ARG A 1 355 ? 103.143 181.593 118.497 1.00 88.06  ? 330  ARG A CA  1 
ATOM   2021  C  C   . ARG A 1 355 ? 103.616 183.042 118.493 1.00 88.02  ? 330  ARG A C   1 
ATOM   2022  O  O   . ARG A 1 355 ? 104.410 183.417 117.624 1.00 87.41  ? 330  ARG A O   1 
ATOM   2023  C  CB  . ARG A 1 355 ? 102.186 181.364 117.327 1.00 87.64  ? 330  ARG A CB  1 
ATOM   2024  C  CG  . ARG A 1 355 ? 101.903 179.904 117.031 1.00 85.96  ? 330  ARG A CG  1 
ATOM   2025  C  CD  . ARG A 1 355 ? 101.520 179.708 115.577 1.00 84.81  ? 330  ARG A CD  1 
ATOM   2026  N  NE  . ARG A 1 355 ? 100.579 178.609 115.405 1.00 86.06  ? 330  ARG A NE  1 
ATOM   2027  C  CZ  . ARG A 1 355 ? 100.244 178.089 114.233 1.00 87.46  ? 330  ARG A CZ  1 
ATOM   2028  N  NH1 . ARG A 1 355 ? 100.756 178.546 113.102 1.00 86.17  ? 330  ARG A NH1 1 
ATOM   2029  N  NH2 . ARG A 1 355 ? 99.373  177.084 114.194 1.00 87.60  ? 330  ARG A NH2 1 
ATOM   2030  N  N   . ARG A 1 356 ? 103.151 183.861 119.434 1.00 103.46 ? 331  ARG A N   1 
ATOM   2031  C  CA  . ARG A 1 356 ? 103.524 185.267 119.498 1.00 103.52 ? 331  ARG A CA  1 
ATOM   2032  C  C   . ARG A 1 356 ? 104.702 185.535 120.426 1.00 104.44 ? 331  ARG A C   1 
ATOM   2033  O  O   . ARG A 1 356 ? 105.072 186.699 120.609 1.00 104.55 ? 331  ARG A O   1 
ATOM   2034  C  CB  . ARG A 1 356 ? 102.326 186.111 119.946 1.00 104.03 ? 331  ARG A CB  1 
ATOM   2035  C  CG  . ARG A 1 356 ? 101.108 185.998 119.048 1.00 104.02 ? 331  ARG A CG  1 
ATOM   2036  C  CD  . ARG A 1 356 ? 100.292 187.278 119.076 1.00 104.86 ? 331  ARG A CD  1 
ATOM   2037  N  NE  . ARG A 1 356 ? 99.809  187.586 120.417 1.00 104.89 ? 331  ARG A NE  1 
ATOM   2038  C  CZ  . ARG A 1 356 ? 98.577  187.346 120.844 1.00 104.87 ? 331  ARG A CZ  1 
ATOM   2039  N  NH1 . ARG A 1 356 ? 97.668  186.794 120.057 1.00 104.51 ? 331  ARG A NH1 1 
ATOM   2040  N  NH2 . ARG A 1 356 ? 98.248  187.669 122.091 1.00 105.28 ? 331  ARG A NH2 1 
ATOM   2041  N  N   . LYS A 1 357 ? 105.296 184.501 121.013 1.00 101.13 ? 332  LYS A N   1 
ATOM   2042  C  CA  . LYS A 1 357 ? 106.370 184.661 121.981 1.00 98.95  ? 332  LYS A CA  1 
ATOM   2043  C  C   . LYS A 1 357 ? 107.708 184.272 121.366 1.00 99.57  ? 332  LYS A C   1 
ATOM   2044  O  O   . LYS A 1 357 ? 107.773 183.479 120.423 1.00 102.85 ? 332  LYS A O   1 
ATOM   2045  C  CB  . LYS A 1 357 ? 106.108 183.820 123.232 1.00 97.09  ? 332  LYS A CB  1 
ATOM   2046  C  CG  . LYS A 1 357 ? 104.647 183.758 123.637 1.00 98.95  ? 332  LYS A CG  1 
ATOM   2047  C  CD  . LYS A 1 357 ? 104.489 183.400 125.105 1.00 100.08 ? 332  LYS A CD  1 
ATOM   2048  C  CE  . LYS A 1 357 ? 104.557 184.637 125.983 1.00 100.25 ? 332  LYS A CE  1 
ATOM   2049  N  NZ  . LYS A 1 357 ? 103.396 185.540 125.759 1.00 99.15  ? 332  LYS A NZ  1 
ATOM   2050  N  N   . SER A 1 358 ? 108.778 184.845 121.913 1.00 90.70  ? 333  SER A N   1 
ATOM   2051  C  CA  . SER A 1 358 ? 110.118 184.571 121.417 1.00 91.23  ? 333  SER A CA  1 
ATOM   2052  C  C   . SER A 1 358 ? 110.518 183.130 121.708 1.00 93.65  ? 333  SER A C   1 
ATOM   2053  O  O   . SER A 1 358 ? 110.036 182.506 122.657 1.00 95.13  ? 333  SER A O   1 
ATOM   2054  C  CB  . SER A 1 358 ? 111.128 185.530 122.044 1.00 90.27  ? 333  SER A CB  1 
ATOM   2055  O  OG  . SER A 1 358 ? 111.279 185.276 123.429 1.00 88.64  ? 333  SER A OG  1 
ATOM   2056  N  N   . SER A 1 359 ? 111.411 182.601 120.869 1.00 86.16  ? 334  SER A N   1 
ATOM   2057  C  CA  . SER A 1 359 ? 111.843 181.216 121.021 1.00 82.96  ? 334  SER A CA  1 
ATOM   2058  C  C   . SER A 1 359 ? 112.593 181.005 122.331 1.00 85.09  ? 334  SER A C   1 
ATOM   2059  O  O   . SER A 1 359 ? 112.384 179.998 123.018 1.00 86.59  ? 334  SER A O   1 
ATOM   2060  C  CB  . SER A 1 359 ? 112.714 180.806 119.835 1.00 79.40  ? 334  SER A CB  1 
ATOM   2061  O  OG  . SER A 1 359 ? 113.918 181.551 119.806 1.00 83.09  ? 334  SER A OG  1 
ATOM   2062  N  N   . ARG A 1 360 ? 113.470 181.941 122.694 1.00 85.16  ? 335  ARG A N   1 
ATOM   2063  C  CA  . ARG A 1 360 ? 114.281 181.767 123.893 1.00 84.40  ? 335  ARG A CA  1 
ATOM   2064  C  C   . ARG A 1 360 ? 113.470 181.885 125.175 1.00 84.38  ? 335  ARG A C   1 
ATOM   2065  O  O   . ARG A 1 360 ? 113.926 181.418 126.224 1.00 85.70  ? 335  ARG A O   1 
ATOM   2066  C  CB  . ARG A 1 360 ? 115.426 182.781 123.910 1.00 84.52  ? 335  ARG A CB  1 
ATOM   2067  C  CG  . ARG A 1 360 ? 116.526 182.501 122.895 1.00 85.22  ? 335  ARG A CG  1 
ATOM   2068  C  CD  . ARG A 1 360 ? 116.704 181.008 122.664 1.00 84.28  ? 335  ARG A CD  1 
ATOM   2069  N  NE  . ARG A 1 360 ? 117.403 180.362 123.769 1.00 85.69  ? 335  ARG A NE  1 
ATOM   2070  C  CZ  . ARG A 1 360 ? 118.587 179.775 123.665 1.00 84.49  ? 335  ARG A CZ  1 
ATOM   2071  N  NH1 . ARG A 1 360 ? 119.237 179.730 122.514 1.00 82.61  ? 335  ARG A NH1 1 
ATOM   2072  N  NH2 . ARG A 1 360 ? 119.132 179.218 124.742 1.00 82.95  ? 335  ARG A NH2 1 
ATOM   2073  N  N   . GLU A 1 361 ? 112.287 182.499 125.125 1.00 88.78  ? 336  GLU A N   1 
ATOM   2074  C  CA  . GLU A 1 361 ? 111.494 182.642 126.340 1.00 89.51  ? 336  GLU A CA  1 
ATOM   2075  C  C   . GLU A 1 361 ? 110.847 181.322 126.740 1.00 89.24  ? 336  GLU A C   1 
ATOM   2076  O  O   . GLU A 1 361 ? 110.805 180.981 127.927 1.00 90.13  ? 336  GLU A O   1 
ATOM   2077  C  CB  . GLU A 1 361 ? 110.431 183.724 126.159 1.00 90.65  ? 336  GLU A CB  1 
ATOM   2078  C  CG  . GLU A 1 361 ? 109.583 183.955 127.401 1.00 91.32  ? 336  GLU A CG  1 
ATOM   2079  C  CD  . GLU A 1 361 ? 108.144 184.283 127.072 1.00 92.30  ? 336  GLU A CD  1 
ATOM   2080  O  OE1 . GLU A 1 361 ? 107.711 183.974 125.944 1.00 92.32  ? 336  GLU A OE1 1 
ATOM   2081  O  OE2 . GLU A 1 361 ? 107.447 184.848 127.940 1.00 92.17  ? 336  GLU A OE2 1 
ATOM   2082  N  N   . LEU A 1 362 ? 110.337 180.564 125.767 1.00 82.92  ? 337  LEU A N   1 
ATOM   2083  C  CA  . LEU A 1 362 ? 109.658 179.310 126.066 1.00 84.95  ? 337  LEU A CA  1 
ATOM   2084  C  C   . LEU A 1 362 ? 110.550 178.086 125.911 1.00 82.41  ? 337  LEU A C   1 
ATOM   2085  O  O   . LEU A 1 362 ? 110.216 177.028 126.454 1.00 82.59  ? 337  LEU A O   1 
ATOM   2086  C  CB  . LEU A 1 362 ? 108.410 179.151 125.186 1.00 84.34  ? 337  LEU A CB  1 
ATOM   2087  C  CG  . LEU A 1 362 ? 108.513 178.470 123.820 1.00 80.63  ? 337  LEU A CG  1 
ATOM   2088  C  CD1 . LEU A 1 362 ? 107.125 178.208 123.265 1.00 81.28  ? 337  LEU A CD1 1 
ATOM   2089  C  CD2 . LEU A 1 362 ? 109.304 179.319 122.852 1.00 79.35  ? 337  LEU A CD2 1 
ATOM   2090  N  N   . VAL A 1 363 ? 111.667 178.196 125.189 1.00 80.67  ? 338  VAL A N   1 
ATOM   2091  C  CA  . VAL A 1 363 ? 112.640 177.109 125.178 1.00 80.83  ? 338  VAL A CA  1 
ATOM   2092  C  C   . VAL A 1 363 ? 113.356 177.020 126.520 1.00 82.35  ? 338  VAL A C   1 
ATOM   2093  O  O   . VAL A 1 363 ? 113.578 175.925 127.051 1.00 81.48  ? 338  VAL A O   1 
ATOM   2094  C  CB  . VAL A 1 363 ? 113.629 177.288 124.012 1.00 80.66  ? 338  VAL A CB  1 
ATOM   2095  C  CG1 . VAL A 1 363 ? 114.872 176.452 124.235 1.00 80.93  ? 338  VAL A CG1 1 
ATOM   2096  C  CG2 . VAL A 1 363 ? 112.968 176.897 122.702 1.00 79.67  ? 338  VAL A CG2 1 
ATOM   2097  N  N   . ASP A 1 364 ? 113.715 178.169 127.098 1.00 87.44  ? 339  ASP A N   1 
ATOM   2098  C  CA  . ASP A 1 364 ? 114.429 178.188 128.368 1.00 88.20  ? 339  ASP A CA  1 
ATOM   2099  C  C   . ASP A 1 364 ? 113.563 177.762 129.546 1.00 88.56  ? 339  ASP A C   1 
ATOM   2100  O  O   . ASP A 1 364 ? 114.103 177.532 130.633 1.00 88.18  ? 339  ASP A O   1 
ATOM   2101  C  CB  . ASP A 1 364 ? 114.998 179.583 128.631 1.00 88.13  ? 339  ASP A CB  1 
ATOM   2102  C  CG  . ASP A 1 364 ? 116.292 179.834 127.884 1.00 89.24  ? 339  ASP A CG  1 
ATOM   2103  O  OD1 . ASP A 1 364 ? 116.766 178.913 127.187 1.00 87.62  ? 339  ASP A OD1 1 
ATOM   2104  O  OD2 . ASP A 1 364 ? 116.837 180.953 127.992 1.00 88.76  ? 339  ASP A OD2 1 
ATOM   2105  N  N   . GLN A 1 365 ? 112.249 177.657 129.366 1.00 94.80  ? 340  GLN A N   1 
ATOM   2106  C  CA  . GLN A 1 365 ? 111.386 177.193 130.443 1.00 93.04  ? 340  GLN A CA  1 
ATOM   2107  C  C   . GLN A 1 365 ? 111.685 175.736 130.766 1.00 93.73  ? 340  GLN A C   1 
ATOM   2108  O  O   . GLN A 1 365 ? 111.889 174.912 129.870 1.00 94.44  ? 340  GLN A O   1 
ATOM   2109  C  CB  . GLN A 1 365 ? 109.916 177.358 130.061 1.00 93.96  ? 340  GLN A CB  1 
ATOM   2110  C  CG  . GLN A 1 365 ? 109.480 178.801 129.887 1.00 96.15  ? 340  GLN A CG  1 
ATOM   2111  C  CD  . GLN A 1 365 ? 109.743 179.641 131.120 1.00 96.24  ? 340  GLN A CD  1 
ATOM   2112  O  OE1 . GLN A 1 365 ? 109.403 179.249 132.236 1.00 96.36  ? 340  GLN A OE1 1 
ATOM   2113  N  NE2 . GLN A 1 365 ? 110.355 180.803 130.925 1.00 94.73  ? 340  GLN A NE2 1 
ATOM   2114  N  N   . ASP A 1 366 ? 111.708 175.419 132.057 1.00 90.40  ? 341  ASP A N   1 
ATOM   2115  C  CA  . ASP A 1 366 ? 112.066 174.085 132.533 1.00 90.90  ? 341  ASP A CA  1 
ATOM   2116  C  C   . ASP A 1 366 ? 110.793 173.362 132.961 1.00 90.40  ? 341  ASP A C   1 
ATOM   2117  O  O   . ASP A 1 366 ? 110.257 173.611 134.043 1.00 91.34  ? 341  ASP A O   1 
ATOM   2118  C  CB  . ASP A 1 366 ? 113.070 174.172 133.678 1.00 90.58  ? 341  ASP A CB  1 
ATOM   2119  C  CG  . ASP A 1 366 ? 113.314 172.831 134.339 1.00 90.89  ? 341  ASP A CG  1 
ATOM   2120  O  OD1 . ASP A 1 366 ? 113.603 171.856 133.615 1.00 88.79  ? 341  ASP A OD1 1 
ATOM   2121  O  OD2 . ASP A 1 366 ? 113.219 172.752 135.582 1.00 92.48  ? 341  ASP A OD2 1 
ATOM   2122  N  N   . VAL A 1 367 ? 110.312 172.467 132.105 1.00 73.69  ? 342  VAL A N   1 
ATOM   2123  C  CA  . VAL A 1 367 ? 109.180 171.602 132.411 1.00 70.57  ? 342  VAL A CA  1 
ATOM   2124  C  C   . VAL A 1 367 ? 109.739 170.204 132.634 1.00 71.58  ? 342  VAL A C   1 
ATOM   2125  O  O   . VAL A 1 367 ? 110.249 169.573 131.700 1.00 75.54  ? 342  VAL A O   1 
ATOM   2126  C  CB  . VAL A 1 367 ? 108.129 171.615 131.293 1.00 71.47  ? 342  VAL A CB  1 
ATOM   2127  C  CG1 . VAL A 1 367 ? 107.153 170.462 131.468 1.00 72.93  ? 342  VAL A CG1 1 
ATOM   2128  C  CG2 . VAL A 1 367 ? 107.392 172.943 131.277 1.00 72.50  ? 342  VAL A CG2 1 
ATOM   2129  N  N   . GLN A 1 368 ? 109.650 169.720 133.869 1.00 64.87  ? 343  GLN A N   1 
ATOM   2130  C  CA  . GLN A 1 368 ? 110.257 168.448 134.232 1.00 66.43  ? 343  GLN A CA  1 
ATOM   2131  C  C   . GLN A 1 368 ? 109.231 167.331 134.117 1.00 67.27  ? 343  GLN A C   1 
ATOM   2132  O  O   . GLN A 1 368 ? 108.172 167.411 134.754 1.00 67.01  ? 343  GLN A O   1 
ATOM   2133  C  CB  . GLN A 1 368 ? 110.812 168.503 135.646 1.00 66.58  ? 343  GLN A CB  1 
ATOM   2134  C  CG  . GLN A 1 368 ? 111.981 167.562 135.891 1.00 67.53  ? 343  GLN A CG  1 
ATOM   2135  C  CD  . GLN A 1 368 ? 113.162 167.840 134.979 1.00 67.83  ? 343  GLN A CD  1 
ATOM   2136  O  OE1 . GLN A 1 368 ? 113.367 168.969 134.534 1.00 67.62  ? 343  GLN A OE1 1 
ATOM   2137  N  NE2 . GLN A 1 368 ? 113.946 166.806 134.696 1.00 68.81  ? 343  GLN A NE2 1 
ATOM   2138  N  N   . PRO A 1 369 ? 109.489 166.290 133.330 1.00 55.62  ? 344  PRO A N   1 
ATOM   2139  C  CA  . PRO A 1 369 ? 108.532 165.184 133.229 1.00 54.44  ? 344  PRO A CA  1 
ATOM   2140  C  C   . PRO A 1 369 ? 108.744 164.141 134.313 1.00 56.51  ? 344  PRO A C   1 
ATOM   2141  O  O   . PRO A 1 369 ? 109.666 164.261 135.126 1.00 57.25  ? 344  PRO A O   1 
ATOM   2142  C  CB  . PRO A 1 369 ? 108.824 164.614 131.840 1.00 52.38  ? 344  PRO A CB  1 
ATOM   2143  C  CG  . PRO A 1 369 ? 110.304 164.810 131.696 1.00 49.73  ? 344  PRO A CG  1 
ATOM   2144  C  CD  . PRO A 1 369 ? 110.651 166.086 132.447 1.00 54.00  ? 344  PRO A CD  1 
ATOM   2145  N  N   . ALA A 1 370 ? 107.897 163.117 134.335 1.00 47.12  ? 345  ALA A N   1 
ATOM   2146  C  CA  . ALA A 1 370 ? 108.099 162.010 135.253 1.00 42.10  ? 345  ALA A CA  1 
ATOM   2147  C  C   . ALA A 1 370 ? 109.377 161.259 134.894 1.00 48.17  ? 345  ALA A C   1 
ATOM   2148  O  O   . ALA A 1 370 ? 109.845 161.287 133.752 1.00 55.55  ? 345  ALA A O   1 
ATOM   2149  C  CB  . ALA A 1 370 ? 106.901 161.061 135.227 1.00 40.46  ? 345  ALA A CB  1 
ATOM   2150  N  N   . ARG A 1 371 ? 109.952 160.592 135.892 1.00 47.66  ? 346  ARG A N   1 
ATOM   2151  C  CA  . ARG A 1 371 ? 111.203 159.879 135.679 1.00 44.98  ? 346  ARG A CA  1 
ATOM   2152  C  C   . ARG A 1 371 ? 111.015 158.765 134.658 1.00 46.65  ? 346  ARG A C   1 
ATOM   2153  O  O   . ARG A 1 371 ? 109.961 158.125 134.599 1.00 49.11  ? 346  ARG A O   1 
ATOM   2154  C  CB  . ARG A 1 371 ? 111.721 159.310 136.999 1.00 43.02  ? 346  ARG A CB  1 
ATOM   2155  C  CG  . ARG A 1 371 ? 112.549 160.294 137.806 1.00 43.58  ? 346  ARG A CG  1 
ATOM   2156  C  CD  . ARG A 1 371 ? 113.205 159.625 138.999 1.00 49.39  ? 346  ARG A CD  1 
ATOM   2157  N  NE  . ARG A 1 371 ? 114.252 158.696 138.593 1.00 50.79  ? 346  ARG A NE  1 
ATOM   2158  C  CZ  . ARG A 1 371 ? 115.548 158.979 138.598 1.00 54.75  ? 346  ARG A CZ  1 
ATOM   2159  N  NH1 . ARG A 1 371 ? 115.994 160.164 138.980 1.00 53.92  ? 346  ARG A NH1 1 
ATOM   2160  N  NH2 . ARG A 1 371 ? 116.416 158.050 138.210 1.00 49.97  ? 346  ARG A NH2 1 
ATOM   2161  N  N   . TYR A 1 372 ? 112.049 158.547 133.842 1.00 42.12  ? 347  TYR A N   1 
ATOM   2162  C  CA  . TYR A 1 372 ? 112.017 157.575 132.748 1.00 40.29  ? 347  TYR A CA  1 
ATOM   2163  C  C   . TYR A 1 372 ? 110.900 157.882 131.754 1.00 46.38  ? 347  TYR A C   1 
ATOM   2164  O  O   . TYR A 1 372 ? 110.313 156.974 131.161 1.00 54.89  ? 347  TYR A O   1 
ATOM   2165  C  CB  . TYR A 1 372 ? 111.894 156.143 133.275 1.00 40.01  ? 347  TYR A CB  1 
ATOM   2166  C  CG  . TYR A 1 372 ? 112.803 155.850 134.446 1.00 42.95  ? 347  TYR A CG  1 
ATOM   2167  C  CD1 . TYR A 1 372 ? 114.145 156.200 134.412 1.00 42.89  ? 347  TYR A CD1 1 
ATOM   2168  C  CD2 . TYR A 1 372 ? 112.318 155.230 135.588 1.00 42.70  ? 347  TYR A CD2 1 
ATOM   2169  C  CE1 . TYR A 1 372 ? 114.977 155.937 135.478 1.00 43.28  ? 347  TYR A CE1 1 
ATOM   2170  C  CE2 . TYR A 1 372 ? 113.144 154.964 136.660 1.00 40.50  ? 347  TYR A CE2 1 
ATOM   2171  C  CZ  . TYR A 1 372 ? 114.472 155.320 136.600 1.00 41.43  ? 347  TYR A CZ  1 
ATOM   2172  O  OH  . TYR A 1 372 ? 115.300 155.058 137.666 1.00 42.38  ? 347  TYR A OH  1 
ATOM   2173  N  N   . HIS A 1 373 ? 110.599 159.167 131.573 1.00 36.78  ? 348  HIS A N   1 
ATOM   2174  C  CA  . HIS A 1 373 ? 109.620 159.627 130.599 1.00 34.89  ? 348  HIS A CA  1 
ATOM   2175  C  C   . HIS A 1 373 ? 110.127 160.927 129.989 1.00 45.21  ? 348  HIS A C   1 
ATOM   2176  O  O   . HIS A 1 373 ? 111.193 161.433 130.351 1.00 50.24  ? 348  HIS A O   1 
ATOM   2177  C  CB  . HIS A 1 373 ? 108.239 159.822 131.236 1.00 32.50  ? 348  HIS A CB  1 
ATOM   2178  C  CG  . HIS A 1 373 ? 107.530 158.544 131.553 1.00 36.04  ? 348  HIS A CG  1 
ATOM   2179  N  ND1 . HIS A 1 373 ? 107.844 157.769 132.649 1.00 45.70  ? 348  HIS A ND1 1 
ATOM   2180  C  CD2 . HIS A 1 373 ? 106.515 157.907 130.922 1.00 37.39  ? 348  HIS A CD2 1 
ATOM   2181  C  CE1 . HIS A 1 373 ? 107.057 156.709 132.677 1.00 40.69  ? 348  HIS A CE1 1 
ATOM   2182  N  NE2 . HIS A 1 373 ? 106.241 156.769 131.640 1.00 39.08  ? 348  HIS A NE2 1 
ATOM   2183  N  N   . ILE A 1 374 ? 109.353 161.474 129.052 1.00 37.70  ? 349  ILE A N   1 
ATOM   2184  C  CA  . ILE A 1 374 ? 109.688 162.736 128.410 1.00 32.24  ? 349  ILE A CA  1 
ATOM   2185  C  C   . ILE A 1 374 ? 108.475 163.653 128.458 1.00 40.27  ? 349  ILE A C   1 
ATOM   2186  O  O   . ILE A 1 374 ? 107.330 163.207 128.560 1.00 45.69  ? 349  ILE A O   1 
ATOM   2187  C  CB  . ILE A 1 374 ? 110.159 162.549 126.953 1.00 29.03  ? 349  ILE A CB  1 
ATOM   2188  C  CG1 . ILE A 1 374 ? 109.183 161.658 126.186 1.00 34.33  ? 349  ILE A CG1 1 
ATOM   2189  C  CG2 . ILE A 1 374 ? 111.558 161.963 126.915 1.00 37.17  ? 349  ILE A CG2 1 
ATOM   2190  C  CD1 . ILE A 1 374 ? 109.516 161.521 124.721 1.00 38.80  ? 349  ILE A CD1 1 
ATOM   2191  N  N   . ALA A 1 375 ? 108.744 164.955 128.384 1.00 47.50  ? 350  ALA A N   1 
ATOM   2192  C  CA  . ALA A 1 375 ? 107.685 165.958 128.358 1.00 45.50  ? 350  ALA A CA  1 
ATOM   2193  C  C   . ALA A 1 375 ? 107.249 166.262 126.928 1.00 43.29  ? 350  ALA A C   1 
ATOM   2194  O  O   . ALA A 1 375 ? 106.068 166.136 126.591 1.00 43.83  ? 350  ALA A O   1 
ATOM   2195  C  CB  . ALA A 1 375 ? 108.152 167.234 129.067 1.00 45.15  ? 350  ALA A CB  1 
ATOM   2196  N  N   . PHE A 1 376 ? 108.192 166.660 126.080 1.00 44.25  ? 351  PHE A N   1 
ATOM   2197  C  CA  . PHE A 1 376 ? 107.925 166.961 124.680 1.00 42.57  ? 351  PHE A CA  1 
ATOM   2198  C  C   . PHE A 1 376 ? 108.630 165.930 123.810 1.00 43.53  ? 351  PHE A C   1 
ATOM   2199  O  O   . PHE A 1 376 ? 109.851 165.765 123.901 1.00 52.28  ? 351  PHE A O   1 
ATOM   2200  C  CB  . PHE A 1 376 ? 108.386 168.375 124.329 1.00 45.27  ? 351  PHE A CB  1 
ATOM   2201  C  CG  . PHE A 1 376 ? 107.798 169.439 125.210 1.00 47.04  ? 351  PHE A CG  1 
ATOM   2202  C  CD1 . PHE A 1 376 ? 106.454 169.755 125.130 1.00 46.72  ? 351  PHE A CD1 1 
ATOM   2203  C  CD2 . PHE A 1 376 ? 108.588 170.121 126.118 1.00 49.26  ? 351  PHE A CD2 1 
ATOM   2204  C  CE1 . PHE A 1 376 ? 105.909 170.731 125.937 1.00 47.49  ? 351  PHE A CE1 1 
ATOM   2205  C  CE2 . PHE A 1 376 ? 108.048 171.098 126.928 1.00 48.16  ? 351  PHE A CE2 1 
ATOM   2206  C  CZ  . PHE A 1 376 ? 106.707 171.403 126.837 1.00 48.22  ? 351  PHE A CZ  1 
ATOM   2207  N  N   . GLY A 1 377 ? 107.859 165.244 122.972 1.00 30.28  ? 352  GLY A N   1 
ATOM   2208  C  CA  . GLY A 1 377 ? 108.383 164.221 122.100 1.00 30.59  ? 352  GLY A CA  1 
ATOM   2209  C  C   . GLY A 1 377 ? 107.347 163.793 121.084 1.00 33.32  ? 352  GLY A C   1 
ATOM   2210  O  O   . GLY A 1 377 ? 106.318 164.451 120.907 1.00 43.99  ? 352  GLY A O   1 
ATOM   2211  N  N   . PRO A 1 378 ? 107.606 162.693 120.380 1.00 23.96  ? 353  PRO A N   1 
ATOM   2212  C  CA  . PRO A 1 378 ? 106.614 162.185 119.426 1.00 28.09  ? 353  PRO A CA  1 
ATOM   2213  C  C   . PRO A 1 378 ? 105.306 161.847 120.122 1.00 34.73  ? 353  PRO A C   1 
ATOM   2214  O  O   . PRO A 1 378 ? 105.290 161.301 121.226 1.00 46.64  ? 353  PRO A O   1 
ATOM   2215  C  CB  . PRO A 1 378 ? 107.286 160.935 118.849 1.00 31.28  ? 353  PRO A CB  1 
ATOM   2216  C  CG  . PRO A 1 378 ? 108.739 161.152 119.070 1.00 28.61  ? 353  PRO A CG  1 
ATOM   2217  C  CD  . PRO A 1 378 ? 108.845 161.903 120.359 1.00 27.78  ? 353  PRO A CD  1 
ATOM   2218  N  N   . VAL A 1 379 ? 104.201 162.178 119.462 1.00 34.42  ? 354  VAL A N   1 
ATOM   2219  C  CA  . VAL A 1 379 ? 102.861 161.956 119.989 1.00 34.25  ? 354  VAL A CA  1 
ATOM   2220  C  C   . VAL A 1 379 ? 102.074 161.135 118.981 1.00 43.08  ? 354  VAL A C   1 
ATOM   2221  O  O   . VAL A 1 379 ? 102.188 161.351 117.770 1.00 52.11  ? 354  VAL A O   1 
ATOM   2222  C  CB  . VAL A 1 379 ? 102.130 163.281 120.288 1.00 44.47  ? 354  VAL A CB  1 
ATOM   2223  C  CG1 . VAL A 1 379 ? 100.990 163.043 121.256 1.00 49.78  ? 354  VAL A CG1 1 
ATOM   2224  C  CG2 . VAL A 1 379 ? 103.092 164.318 120.840 1.00 41.30  ? 354  VAL A CG2 1 
ATOM   2225  N  N   . VAL A 1 380 ? 101.277 160.194 119.480 1.00 44.69  ? 355  VAL A N   1 
ATOM   2226  C  CA  . VAL A 1 380 ? 100.386 159.424 118.618 1.00 49.21  ? 355  VAL A CA  1 
ATOM   2227  C  C   . VAL A 1 380 ? 99.160  160.282 118.309 1.00 52.58  ? 355  VAL A C   1 
ATOM   2228  O  O   . VAL A 1 380 ? 98.397  160.657 119.202 1.00 55.69  ? 355  VAL A O   1 
ATOM   2229  C  CB  . VAL A 1 380 ? 100.012 158.072 119.246 1.00 48.00  ? 355  VAL A CB  1 
ATOM   2230  C  CG1 . VAL A 1 380 ? 101.270 157.275 119.526 1.00 47.08  ? 355  VAL A CG1 1 
ATOM   2231  C  CG2 . VAL A 1 380 ? 99.252  158.241 120.554 1.00 50.50  ? 355  VAL A CG2 1 
ATOM   2232  N  N   . ASP A 1 381 ? 99.005  160.649 117.040 1.00 55.96  ? 356  ASP A N   1 
ATOM   2233  C  CA  . ASP A 1 381 ? 97.909  161.504 116.603 1.00 58.61  ? 356  ASP A CA  1 
ATOM   2234  C  C   . ASP A 1 381 ? 97.031  160.839 115.556 1.00 63.91  ? 356  ASP A C   1 
ATOM   2235  O  O   . ASP A 1 381 ? 95.800  160.883 115.666 1.00 65.27  ? 356  ASP A O   1 
ATOM   2236  C  CB  . ASP A 1 381 ? 98.462  162.832 116.061 1.00 56.48  ? 356  ASP A CB  1 
ATOM   2237  C  CG  . ASP A 1 381 ? 99.652  162.637 115.145 1.00 62.68  ? 356  ASP A CG  1 
ATOM   2238  O  OD1 . ASP A 1 381 ? 99.584  161.765 114.254 1.00 64.14  ? 356  ASP A OD1 1 
ATOM   2239  O  OD2 . ASP A 1 381 ? 100.656 163.358 115.313 1.00 63.65  ? 356  ASP A OD2 1 
ATOM   2240  N  N   . GLY A 1 382 ? 97.631  160.228 114.539 1.00 61.80  ? 357  GLY A N   1 
ATOM   2241  C  CA  . GLY A 1 382 ? 96.873  159.612 113.470 1.00 61.56  ? 357  GLY A CA  1 
ATOM   2242  C  C   . GLY A 1 382 ? 97.433  159.938 112.102 1.00 61.71  ? 357  GLY A C   1 
ATOM   2243  O  O   . GLY A 1 382 ? 97.146  159.243 111.124 1.00 61.89  ? 357  GLY A O   1 
ATOM   2244  N  N   . ASP A 1 383 ? 98.235  161.000 112.021 1.00 56.65  ? 358  ASP A N   1 
ATOM   2245  C  CA  . ASP A 1 383 ? 98.861  161.408 110.768 1.00 58.20  ? 358  ASP A CA  1 
ATOM   2246  C  C   . ASP A 1 383 ? 100.270 160.842 110.626 1.00 58.82  ? 358  ASP A C   1 
ATOM   2247  O  O   . ASP A 1 383 ? 100.553 160.102 109.679 1.00 58.16  ? 358  ASP A O   1 
ATOM   2248  C  CB  . ASP A 1 383 ? 98.886  162.940 110.668 1.00 55.34  ? 358  ASP A CB  1 
ATOM   2249  N  N   . VAL A 1 384 ? 101.163 161.175 111.558 1.00 50.88  ? 359  VAL A N   1 
ATOM   2250  C  CA  . VAL A 1 384 ? 102.533 160.677 111.485 1.00 49.31  ? 359  VAL A CA  1 
ATOM   2251  C  C   . VAL A 1 384 ? 102.639 159.303 112.129 1.00 53.07  ? 359  VAL A C   1 
ATOM   2252  O  O   . VAL A 1 384 ? 103.127 158.348 111.515 1.00 58.98  ? 359  VAL A O   1 
ATOM   2253  C  CB  . VAL A 1 384 ? 103.502 161.680 112.134 1.00 52.64  ? 359  VAL A CB  1 
ATOM   2254  C  CG1 . VAL A 1 384 ? 104.922 161.144 112.087 1.00 48.85  ? 359  VAL A CG1 1 
ATOM   2255  C  CG2 . VAL A 1 384 ? 103.415 163.025 111.438 1.00 48.94  ? 359  VAL A CG2 1 
ATOM   2256  N  N   . VAL A 1 385 ? 102.186 159.181 113.372 1.00 52.45  ? 360  VAL A N   1 
ATOM   2257  C  CA  . VAL A 1 385 ? 102.145 157.893 114.059 1.00 55.44  ? 360  VAL A CA  1 
ATOM   2258  C  C   . VAL A 1 385 ? 100.680 157.529 114.264 1.00 56.66  ? 360  VAL A C   1 
ATOM   2259  O  O   . VAL A 1 385 ? 100.024 158.086 115.156 1.00 61.55  ? 360  VAL A O   1 
ATOM   2260  C  CB  . VAL A 1 385 ? 102.908 157.941 115.392 1.00 52.47  ? 360  VAL A CB  1 
ATOM   2261  C  CG1 . VAL A 1 385 ? 103.103 156.538 115.939 1.00 51.98  ? 360  VAL A CG1 1 
ATOM   2262  C  CG2 . VAL A 1 385 ? 104.245 158.642 115.215 1.00 46.35  ? 360  VAL A CG2 1 
ATOM   2263  N  N   . PRO A 1 386 ? 100.123 156.621 113.458 1.00 51.67  ? 361  PRO A N   1 
ATOM   2264  C  CA  . PRO A 1 386 ? 98.676  156.352 113.558 1.00 55.11  ? 361  PRO A CA  1 
ATOM   2265  C  C   . PRO A 1 386 ? 98.249  155.785 114.901 1.00 56.16  ? 361  PRO A C   1 
ATOM   2266  O  O   . PRO A 1 386 ? 97.259  156.250 115.480 1.00 55.67  ? 361  PRO A O   1 
ATOM   2267  C  CB  . PRO A 1 386 ? 98.431  155.361 112.409 1.00 56.49  ? 361  PRO A CB  1 
ATOM   2268  C  CG  . PRO A 1 386 ? 99.582  155.554 111.475 1.00 51.66  ? 361  PRO A CG  1 
ATOM   2269  C  CD  . PRO A 1 386 ? 100.749 155.895 112.342 1.00 48.38  ? 361  PRO A CD  1 
ATOM   2270  N  N   . ASP A 1 387 ? 98.968  154.791 115.416 1.00 59.00  ? 362  ASP A N   1 
ATOM   2271  C  CA  . ASP A 1 387 ? 98.583  154.143 116.663 1.00 58.47  ? 362  ASP A CA  1 
ATOM   2272  C  C   . ASP A 1 387 ? 99.782  153.989 117.589 1.00 60.22  ? 362  ASP A C   1 
ATOM   2273  O  O   . ASP A 1 387 ? 100.851 154.551 117.327 1.00 59.60  ? 362  ASP A O   1 
ATOM   2274  C  CB  . ASP A 1 387 ? 97.951  152.780 116.381 1.00 55.74  ? 362  ASP A CB  1 
ATOM   2275  C  CG  . ASP A 1 387 ? 96.738  152.512 117.246 1.00 60.85  ? 362  ASP A CG  1 
ATOM   2276  O  OD1 . ASP A 1 387 ? 96.542  153.243 118.239 1.00 62.44  ? 362  ASP A OD1 1 
ATOM   2277  O  OD2 . ASP A 1 387 ? 95.981  151.569 116.933 1.00 64.89  ? 362  ASP A OD2 1 
ATOM   2278  N  N   . ASP A 1 388 ? 99.613  153.245 118.674 1.00 53.02  ? 363  ASP A N   1 
ATOM   2279  C  CA  . ASP A 1 388 ? 100.729 152.971 119.566 1.00 48.10  ? 363  ASP A CA  1 
ATOM   2280  C  C   . ASP A 1 388 ? 101.780 152.149 118.827 1.00 49.39  ? 363  ASP A C   1 
ATOM   2281  O  O   . ASP A 1 388 ? 101.431 151.168 118.158 1.00 57.54  ? 363  ASP A O   1 
ATOM   2282  C  CB  . ASP A 1 388 ? 100.254 152.222 120.809 1.00 50.55  ? 363  ASP A CB  1 
ATOM   2283  C  CG  . ASP A 1 388 ? 99.482  153.107 121.763 1.00 58.05  ? 363  ASP A CG  1 
ATOM   2284  O  OD1 . ASP A 1 388 ? 99.193  154.266 121.399 1.00 61.66  ? 363  ASP A OD1 1 
ATOM   2285  O  OD2 . ASP A 1 388 ? 99.163  152.644 122.878 1.00 60.99  ? 363  ASP A OD2 1 
ATOM   2286  N  N   . PRO A 1 389 ? 103.061 152.515 118.910 1.00 38.80  ? 364  PRO A N   1 
ATOM   2287  C  CA  . PRO A 1 389 ? 104.087 151.739 118.196 1.00 37.74  ? 364  PRO A CA  1 
ATOM   2288  C  C   . PRO A 1 389 ? 104.154 150.284 118.622 1.00 38.01  ? 364  PRO A C   1 
ATOM   2289  O  O   . PRO A 1 389 ? 104.532 149.429 117.812 1.00 49.60  ? 364  PRO A O   1 
ATOM   2290  C  CB  . PRO A 1 389 ? 105.383 152.488 118.533 1.00 37.64  ? 364  PRO A CB  1 
ATOM   2291  C  CG  . PRO A 1 389 ? 104.940 153.874 118.863 1.00 40.87  ? 364  PRO A CG  1 
ATOM   2292  C  CD  . PRO A 1 389 ? 103.621 153.713 119.553 1.00 45.71  ? 364  PRO A CD  1 
ATOM   2293  N  N   . GLU A 1 390 ? 103.801 149.973 119.870 1.00 36.63  ? 365  GLU A N   1 
ATOM   2294  C  CA  . GLU A 1 390 ? 103.799 148.581 120.306 1.00 35.91  ? 365  GLU A CA  1 
ATOM   2295  C  C   . GLU A 1 390 ? 102.659 147.803 119.661 1.00 43.63  ? 365  GLU A C   1 
ATOM   2296  O  O   . GLU A 1 390 ? 102.822 146.631 119.306 1.00 46.47  ? 365  GLU A O   1 
ATOM   2297  C  CB  . GLU A 1 390 ? 103.705 148.509 121.829 1.00 39.64  ? 365  GLU A CB  1 
ATOM   2298  C  CG  . GLU A 1 390 ? 104.140 147.178 122.414 1.00 45.80  ? 365  GLU A CG  1 
ATOM   2299  C  CD  . GLU A 1 390 ? 104.590 147.299 123.856 1.00 49.56  ? 365  GLU A CD  1 
ATOM   2300  O  OE1 . GLU A 1 390 ? 104.573 148.426 124.393 1.00 45.94  ? 365  GLU A OE1 1 
ATOM   2301  O  OE2 . GLU A 1 390 ? 104.964 146.267 124.452 1.00 48.00  ? 365  GLU A OE2 1 
ATOM   2302  N  N   . ILE A 1 391 ? 101.497 148.438 119.506 1.00 50.34  ? 366  ILE A N   1 
ATOM   2303  C  CA  . ILE A 1 391 ? 100.366 147.783 118.857 1.00 47.99  ? 366  ILE A CA  1 
ATOM   2304  C  C   . ILE A 1 391 ? 100.503 147.839 117.339 1.00 48.62  ? 366  ILE A C   1 
ATOM   2305  O  O   . ILE A 1 391 ? 100.119 146.892 116.641 1.00 47.24  ? 366  ILE A O   1 
ATOM   2306  C  CB  . ILE A 1 391 ? 99.049  148.420 119.336 1.00 43.84  ? 366  ILE A CB  1 
ATOM   2307  C  CG1 . ILE A 1 391 ? 98.530  147.701 120.581 1.00 46.92  ? 366  ILE A CG1 1 
ATOM   2308  C  CG2 . ILE A 1 391 ? 97.994  148.410 118.241 1.00 41.95  ? 366  ILE A CG2 1 
ATOM   2309  C  CD1 . ILE A 1 391 ? 97.257  148.296 121.137 1.00 49.41  ? 366  ILE A CD1 1 
ATOM   2310  N  N   . LEU A 1 392 ? 101.068 148.927 116.809 1.00 49.04  ? 367  LEU A N   1 
ATOM   2311  C  CA  . LEU A 1 392 ? 101.156 149.095 115.362 1.00 42.56  ? 367  LEU A CA  1 
ATOM   2312  C  C   . LEU A 1 392 ? 102.016 148.014 114.722 1.00 44.33  ? 367  LEU A C   1 
ATOM   2313  O  O   . LEU A 1 392 ? 101.670 147.484 113.661 1.00 55.77  ? 367  LEU A O   1 
ATOM   2314  C  CB  . LEU A 1 392 ? 101.712 150.479 115.032 1.00 39.59  ? 367  LEU A CB  1 
ATOM   2315  C  CG  . LEU A 1 392 ? 101.152 151.183 113.798 1.00 46.14  ? 367  LEU A CG  1 
ATOM   2316  C  CD1 . LEU A 1 392 ? 99.700  150.803 113.574 1.00 48.47  ? 367  LEU A CD1 1 
ATOM   2317  C  CD2 . LEU A 1 392 ? 101.296 152.685 113.943 1.00 47.07  ? 367  LEU A CD2 1 
ATOM   2318  N  N   . MET A 1 393 ? 103.142 147.673 115.349 1.00 33.04  ? 368  MET A N   1 
ATOM   2319  C  CA  . MET A 1 393 ? 104.057 146.705 114.760 1.00 33.30  ? 368  MET A CA  1 
ATOM   2320  C  C   . MET A 1 393 ? 103.672 145.260 115.051 1.00 35.09  ? 368  MET A C   1 
ATOM   2321  O  O   . MET A 1 393 ? 104.205 144.356 114.400 1.00 45.42  ? 368  MET A O   1 
ATOM   2322  C  CB  . MET A 1 393 ? 105.485 146.971 115.241 1.00 32.36  ? 368  MET A CB  1 
ATOM   2323  C  CG  . MET A 1 393 ? 105.925 146.130 116.421 1.00 35.53  ? 368  MET A CG  1 
ATOM   2324  S  SD  . MET A 1 393 ? 107.631 146.467 116.892 1.00 48.36  ? 368  MET A SD  1 
ATOM   2325  C  CE  . MET A 1 393 ? 107.713 148.236 116.629 1.00 28.64  ? 368  MET A CE  1 
ATOM   2326  N  N   . GLN A 1 394 ? 102.764 145.017 115.997 1.00 41.98  ? 369  GLN A N   1 
ATOM   2327  C  CA  . GLN A 1 394 ? 102.282 143.656 116.209 1.00 47.38  ? 369  GLN A CA  1 
ATOM   2328  C  C   . GLN A 1 394 ? 101.403 143.191 115.057 1.00 46.65  ? 369  GLN A C   1 
ATOM   2329  O  O   . GLN A 1 394 ? 101.387 141.999 114.731 1.00 46.54  ? 369  GLN A O   1 
ATOM   2330  C  CB  . GLN A 1 394 ? 101.518 143.560 117.529 1.00 47.66  ? 369  GLN A CB  1 
ATOM   2331  C  CG  . GLN A 1 394 ? 102.407 143.490 118.756 1.00 47.88  ? 369  GLN A CG  1 
ATOM   2332  C  CD  . GLN A 1 394 ? 101.616 143.478 120.048 1.00 50.48  ? 369  GLN A CD  1 
ATOM   2333  O  OE1 . GLN A 1 394 ? 100.394 143.630 120.042 1.00 55.47  ? 369  GLN A OE1 1 
ATOM   2334  N  NE2 . GLN A 1 394 ? 102.310 143.297 121.165 1.00 51.13  ? 369  GLN A NE2 1 
ATOM   2335  N  N   . GLN A 1 395 ? 100.673 144.111 114.432 1.00 50.98  ? 370  GLN A N   1 
ATOM   2336  C  CA  . GLN A 1 395 ? 99.779  143.798 113.327 1.00 49.76  ? 370  GLN A CA  1 
ATOM   2337  C  C   . GLN A 1 395 ? 100.452 143.931 111.967 1.00 48.25  ? 370  GLN A C   1 
ATOM   2338  O  O   . GLN A 1 395 ? 99.772  143.829 110.941 1.00 52.31  ? 370  GLN A O   1 
ATOM   2339  C  CB  . GLN A 1 395 ? 98.540  144.693 113.391 1.00 47.83  ? 370  GLN A CB  1 
ATOM   2340  C  CG  . GLN A 1 395 ? 97.943  144.812 114.784 1.00 47.64  ? 370  GLN A CG  1 
ATOM   2341  C  CD  . GLN A 1 395 ? 96.970  145.967 114.906 1.00 54.22  ? 370  GLN A CD  1 
ATOM   2342  O  OE1 . GLN A 1 395 ? 97.087  146.970 114.204 1.00 54.11  ? 370  GLN A OE1 1 
ATOM   2343  N  NE2 . GLN A 1 395 ? 96.001  145.831 115.803 1.00 56.02  ? 370  GLN A NE2 1 
ATOM   2344  N  N   . GLY A 1 396 ? 101.763 144.157 111.935 1.00 43.58  ? 371  GLY A N   1 
ATOM   2345  C  CA  . GLY A 1 396 ? 102.496 144.230 110.686 1.00 45.84  ? 371  GLY A CA  1 
ATOM   2346  C  C   . GLY A 1 396 ? 102.217 145.461 109.849 1.00 46.44  ? 371  GLY A C   1 
ATOM   2347  O  O   . GLY A 1 396 ? 102.027 145.359 108.634 1.00 52.67  ? 371  GLY A O   1 
ATOM   2348  N  N   . GLU A 1 397 ? 102.191 146.628 110.482 1.00 40.16  ? 372  GLU A N   1 
ATOM   2349  C  CA  . GLU A 1 397 ? 101.973 147.892 109.778 1.00 41.86  ? 372  GLU A CA  1 
ATOM   2350  C  C   . GLU A 1 397 ? 103.303 148.565 109.436 1.00 41.76  ? 372  GLU A C   1 
ATOM   2351  O  O   . GLU A 1 397 ? 103.605 149.672 109.878 1.00 43.15  ? 372  GLU A O   1 
ATOM   2352  C  CB  . GLU A 1 397 ? 101.088 148.812 110.613 1.00 41.90  ? 372  GLU A CB  1 
ATOM   2353  C  CG  . GLU A 1 397 ? 99.716  148.246 110.911 1.00 45.06  ? 372  GLU A CG  1 
ATOM   2354  C  CD  . GLU A 1 397 ? 98.631  148.896 110.080 1.00 51.59  ? 372  GLU A CD  1 
ATOM   2355  O  OE1 . GLU A 1 397 ? 98.465  148.506 108.906 1.00 56.06  ? 372  GLU A OE1 1 
ATOM   2356  O  OE2 . GLU A 1 397 ? 97.942  149.797 110.602 1.00 52.54  ? 372  GLU A OE2 1 
ATOM   2357  N  N   . PHE A 1 398 ? 104.104 147.875 108.627 1.00 41.36  ? 373  PHE A N   1 
ATOM   2358  C  CA  . PHE A 1 398 ? 105.357 148.434 108.139 1.00 40.83  ? 373  PHE A CA  1 
ATOM   2359  C  C   . PHE A 1 398 ? 105.641 147.875 106.753 1.00 44.07  ? 373  PHE A C   1 
ATOM   2360  O  O   . PHE A 1 398 ? 105.095 146.844 106.353 1.00 49.40  ? 373  PHE A O   1 
ATOM   2361  C  CB  . PHE A 1 398 ? 106.525 148.158 109.097 1.00 45.67  ? 373  PHE A CB  1 
ATOM   2362  C  CG  . PHE A 1 398 ? 106.462 146.821 109.775 1.00 40.83  ? 373  PHE A CG  1 
ATOM   2363  C  CD1 . PHE A 1 398 ? 105.793 146.671 110.977 1.00 37.56  ? 373  PHE A CD1 1 
ATOM   2364  C  CD2 . PHE A 1 398 ? 107.088 145.720 109.222 1.00 41.08  ? 373  PHE A CD2 1 
ATOM   2365  C  CE1 . PHE A 1 398 ? 105.739 145.447 111.606 1.00 35.41  ? 373  PHE A CE1 1 
ATOM   2366  C  CE2 . PHE A 1 398 ? 107.037 144.494 109.848 1.00 42.73  ? 373  PHE A CE2 1 
ATOM   2367  C  CZ  . PHE A 1 398 ? 106.361 144.357 111.041 1.00 36.91  ? 373  PHE A CZ  1 
ATOM   2368  N  N   . LEU A 1 399 ? 106.509 148.572 106.021 1.00 36.30  ? 374  LEU A N   1 
ATOM   2369  C  CA  . LEU A 1 399 ? 106.684 148.354 104.585 1.00 41.14  ? 374  LEU A CA  1 
ATOM   2370  C  C   . LEU A 1 399 ? 107.961 147.594 104.246 1.00 40.97  ? 374  LEU A C   1 
ATOM   2371  O  O   . LEU A 1 399 ? 108.595 147.876 103.226 1.00 46.69  ? 374  LEU A O   1 
ATOM   2372  C  CB  . LEU A 1 399 ? 106.650 149.689 103.848 1.00 44.45  ? 374  LEU A CB  1 
ATOM   2373  C  CG  . LEU A 1 399 ? 105.270 150.321 103.659 1.00 41.49  ? 374  LEU A CG  1 
ATOM   2374  C  CD1 . LEU A 1 399 ? 105.379 151.646 102.924 1.00 41.25  ? 374  LEU A CD1 1 
ATOM   2375  C  CD2 . LEU A 1 399 ? 104.346 149.373 102.920 1.00 43.31  ? 374  LEU A CD2 1 
ATOM   2376  N  N   . ASN A 1 400 ? 108.358 146.625 105.074 1.00 34.91  ? 375  ASN A N   1 
ATOM   2377  C  CA  . ASN A 1 400 ? 109.407 145.660 104.735 1.00 41.59  ? 375  ASN A CA  1 
ATOM   2378  C  C   . ASN A 1 400 ? 110.739 146.357 104.432 1.00 47.31  ? 375  ASN A C   1 
ATOM   2379  O  O   . ASN A 1 400 ? 111.244 146.346 103.308 1.00 49.94  ? 375  ASN A O   1 
ATOM   2380  C  CB  . ASN A 1 400 ? 108.963 144.782 103.558 1.00 42.25  ? 375  ASN A CB  1 
ATOM   2381  C  CG  . ASN A 1 400 ? 109.813 143.538 103.401 1.00 47.56  ? 375  ASN A CG  1 
ATOM   2382  O  OD1 . ASN A 1 400 ? 110.953 143.603 102.942 1.00 49.87  ? 375  ASN A OD1 1 
ATOM   2383  N  ND2 . ASN A 1 400 ? 109.258 142.393 103.777 1.00 46.75  ? 375  ASN A ND2 1 
ATOM   2384  N  N   . TYR A 1 401 ? 111.291 146.975 105.472 1.00 42.80  ? 376  TYR A N   1 
ATOM   2385  C  CA  . TYR A 1 401 ? 112.607 147.595 105.404 1.00 30.73  ? 376  TYR A CA  1 
ATOM   2386  C  C   . TYR A 1 401 ? 113.656 146.679 106.020 1.00 36.56  ? 376  TYR A C   1 
ATOM   2387  O  O   . TYR A 1 401 ? 113.413 146.048 107.053 1.00 40.26  ? 376  TYR A O   1 
ATOM   2388  C  CB  . TYR A 1 401 ? 112.627 148.942 106.129 1.00 25.93  ? 376  TYR A CB  1 
ATOM   2389  C  CG  . TYR A 1 401 ? 111.585 149.929 105.665 1.00 31.04  ? 376  TYR A CG  1 
ATOM   2390  C  CD1 . TYR A 1 401 ? 111.788 150.700 104.531 1.00 40.77  ? 376  TYR A CD1 1 
ATOM   2391  C  CD2 . TYR A 1 401 ? 110.404 150.099 106.367 1.00 36.48  ? 376  TYR A CD2 1 
ATOM   2392  C  CE1 . TYR A 1 401 ? 110.840 151.608 104.107 1.00 36.56  ? 376  TYR A CE1 1 
ATOM   2393  C  CE2 . TYR A 1 401 ? 109.451 151.005 105.951 1.00 35.84  ? 376  TYR A CE2 1 
ATOM   2394  C  CZ  . TYR A 1 401 ? 109.674 151.756 104.821 1.00 34.15  ? 376  TYR A CZ  1 
ATOM   2395  O  OH  . TYR A 1 401 ? 108.725 152.659 104.404 1.00 39.83  ? 376  TYR A OH  1 
ATOM   2396  N  N   . ASP A 1 402 ? 114.820 146.604 105.377 1.00 39.78  ? 377  ASP A N   1 
ATOM   2397  C  CA  . ASP A 1 402 ? 115.955 145.916 105.977 1.00 36.98  ? 377  ASP A CA  1 
ATOM   2398  C  C   . ASP A 1 402 ? 116.383 146.641 107.245 1.00 38.67  ? 377  ASP A C   1 
ATOM   2399  O  O   . ASP A 1 402 ? 116.398 147.873 107.297 1.00 52.62  ? 377  ASP A O   1 
ATOM   2400  C  CB  . ASP A 1 402 ? 117.119 145.844 104.990 1.00 36.97  ? 377  ASP A CB  1 
ATOM   2401  C  CG  . ASP A 1 402 ? 116.717 145.252 103.654 1.00 46.31  ? 377  ASP A CG  1 
ATOM   2402  O  OD1 . ASP A 1 402 ? 115.502 145.118 103.402 1.00 49.40  ? 377  ASP A OD1 1 
ATOM   2403  O  OD2 . ASP A 1 402 ? 117.618 144.921 102.855 1.00 46.11  ? 377  ASP A OD2 1 
ATOM   2404  N  N   . MET A 1 403 ? 116.738 145.875 108.273 1.00 33.41  ? 378  MET A N   1 
ATOM   2405  C  CA  . MET A 1 403 ? 116.991 146.441 109.589 1.00 33.60  ? 378  MET A CA  1 
ATOM   2406  C  C   . MET A 1 403 ? 118.294 145.918 110.169 1.00 28.67  ? 378  MET A C   1 
ATOM   2407  O  O   . MET A 1 403 ? 118.654 144.753 109.972 1.00 43.74  ? 378  MET A O   1 
ATOM   2408  C  CB  . MET A 1 403 ? 115.839 146.131 110.547 1.00 38.27  ? 378  MET A CB  1 
ATOM   2409  C  CG  . MET A 1 403 ? 114.602 146.962 110.283 1.00 46.58  ? 378  MET A CG  1 
ATOM   2410  S  SD  . MET A 1 403 ? 114.559 148.456 111.284 1.00 49.46  ? 378  MET A SD  1 
ATOM   2411  C  CE  . MET A 1 403 ? 114.313 147.767 112.912 1.00 39.39  ? 378  MET A CE  1 
ATOM   2412  N  N   . LEU A 1 404 ? 118.986 146.785 110.907 1.00 39.96  ? 379  LEU A N   1 
ATOM   2413  C  CA  . LEU A 1 404 ? 120.212 146.439 111.625 1.00 46.64  ? 379  LEU A CA  1 
ATOM   2414  C  C   . LEU A 1 404 ? 120.064 146.990 113.040 1.00 50.54  ? 379  LEU A C   1 
ATOM   2415  O  O   . LEU A 1 404 ? 120.390 148.150 113.304 1.00 54.35  ? 379  LEU A O   1 
ATOM   2416  C  CB  . LEU A 1 404 ? 121.445 146.992 110.922 1.00 48.48  ? 379  LEU A CB  1 
ATOM   2417  C  CG  . LEU A 1 404 ? 122.766 146.280 111.219 1.00 44.44  ? 379  LEU A CG  1 
ATOM   2418  C  CD1 . LEU A 1 404 ? 123.576 146.112 109.947 1.00 49.19  ? 379  LEU A CD1 1 
ATOM   2419  C  CD2 . LEU A 1 404 ? 123.560 147.036 112.263 1.00 54.05  ? 379  LEU A CD2 1 
ATOM   2420  N  N   . ILE A 1 405 ? 119.571 146.154 113.943 1.00 42.94  ? 380  ILE A N   1 
ATOM   2421  C  CA  . ILE A 1 405 ? 119.330 146.534 115.328 1.00 33.20  ? 380  ILE A CA  1 
ATOM   2422  C  C   . ILE A 1 405 ? 120.543 146.136 116.153 1.00 45.05  ? 380  ILE A C   1 
ATOM   2423  O  O   . ILE A 1 405 ? 121.237 145.159 115.849 1.00 65.72  ? 380  ILE A O   1 
ATOM   2424  C  CB  . ILE A 1 405 ? 118.042 145.875 115.865 1.00 44.62  ? 380  ILE A CB  1 
ATOM   2425  C  CG1 . ILE A 1 405 ? 116.837 146.317 115.045 1.00 45.36  ? 380  ILE A CG1 1 
ATOM   2426  C  CG2 . ILE A 1 405 ? 117.797 146.243 117.315 1.00 55.32  ? 380  ILE A CG2 1 
ATOM   2427  C  CD1 . ILE A 1 405 ? 115.565 145.613 115.434 1.00 56.21  ? 380  ILE A CD1 1 
ATOM   2428  N  N   . GLY A 1 406 ? 120.816 146.900 117.203 1.00 27.99  ? 381  GLY A N   1 
ATOM   2429  C  CA  . GLY A 1 406 ? 121.929 146.565 118.066 1.00 36.27  ? 381  GLY A CA  1 
ATOM   2430  C  C   . GLY A 1 406 ? 121.790 147.179 119.436 1.00 39.95  ? 381  GLY A C   1 
ATOM   2431  O  O   . GLY A 1 406 ? 121.058 148.152 119.639 1.00 46.44  ? 381  GLY A O   1 
ATOM   2432  N  N   . VAL A 1 407 ? 122.509 146.583 120.384 1.00 35.02  ? 382  VAL A N   1 
ATOM   2433  C  CA  . VAL A 1 407 ? 122.570 147.072 121.753 1.00 17.70  ? 382  VAL A CA  1 
ATOM   2434  C  C   . VAL A 1 407 ? 124.025 147.073 122.201 1.00 29.72  ? 382  VAL A C   1 
ATOM   2435  O  O   . VAL A 1 407 ? 124.921 146.636 121.481 1.00 46.88  ? 382  VAL A O   1 
ATOM   2436  C  CB  . VAL A 1 407 ? 121.710 146.237 122.723 1.00 19.18  ? 382  VAL A CB  1 
ATOM   2437  C  CG1 . VAL A 1 407 ? 120.292 146.109 122.208 1.00 33.16  ? 382  VAL A CG1 1 
ATOM   2438  C  CG2 . VAL A 1 407 ? 122.324 144.871 122.924 1.00 30.15  ? 382  VAL A CG2 1 
ATOM   2439  N  N   . ASN A 1 408 ? 124.253 147.599 123.398 1.00 26.20  ? 383  ASN A N   1 
ATOM   2440  C  CA  . ASN A 1 408 ? 125.550 147.545 124.054 1.00 27.86  ? 383  ASN A CA  1 
ATOM   2441  C  C   . ASN A 1 408 ? 125.460 146.636 125.273 1.00 31.76  ? 383  ASN A C   1 
ATOM   2442  O  O   . ASN A 1 408 ? 124.371 146.263 125.717 1.00 40.96  ? 383  ASN A O   1 
ATOM   2443  C  CB  . ASN A 1 408 ? 126.023 148.946 124.458 1.00 32.06  ? 383  ASN A CB  1 
ATOM   2444  C  CG  . ASN A 1 408 ? 126.065 149.905 123.287 1.00 28.67  ? 383  ASN A CG  1 
ATOM   2445  O  OD1 . ASN A 1 408 ? 125.381 149.709 122.286 1.00 23.00  ? 383  ASN A OD1 1 
ATOM   2446  N  ND2 . ASN A 1 408 ? 126.876 150.948 123.407 1.00 31.97  ? 383  ASN A ND2 1 
ATOM   2447  N  N   . GLN A 1 409 ? 126.623 146.266 125.809 1.00 35.52  ? 384  GLN A N   1 
ATOM   2448  C  CA  . GLN A 1 409 ? 126.643 145.374 126.964 1.00 36.99  ? 384  GLN A CA  1 
ATOM   2449  C  C   . GLN A 1 409 ? 125.964 146.022 128.164 1.00 45.71  ? 384  GLN A C   1 
ATOM   2450  O  O   . GLN A 1 409 ? 124.934 145.541 128.648 1.00 48.00  ? 384  GLN A O   1 
ATOM   2451  C  CB  . GLN A 1 409 ? 128.077 144.975 127.307 1.00 36.40  ? 384  GLN A CB  1 
ATOM   2452  C  CG  . GLN A 1 409 ? 128.159 144.007 128.476 1.00 39.98  ? 384  GLN A CG  1 
ATOM   2453  C  CD  . GLN A 1 409 ? 129.446 144.138 129.260 1.00 47.38  ? 384  GLN A CD  1 
ATOM   2454  O  OE1 . GLN A 1 409 ? 129.455 144.655 130.377 1.00 51.61  ? 384  GLN A OE1 1 
ATOM   2455  N  NE2 . GLN A 1 409 ? 130.542 143.662 128.683 1.00 46.97  ? 384  GLN A NE2 1 
ATOM   2456  N  N   . GLY A 1 410 ? 126.531 147.117 128.660 1.00 34.32  ? 385  GLY A N   1 
ATOM   2457  C  CA  . GLY A 1 410 ? 125.899 147.848 129.737 1.00 33.92  ? 385  GLY A CA  1 
ATOM   2458  C  C   . GLY A 1 410 ? 125.645 149.297 129.389 1.00 32.04  ? 385  GLY A C   1 
ATOM   2459  O  O   . GLY A 1 410 ? 126.580 150.097 129.317 1.00 39.39  ? 385  GLY A O   1 
ATOM   2460  N  N   . GLU A 1 411 ? 124.376 149.656 129.206 1.00 37.25  ? 386  GLU A N   1 
ATOM   2461  C  CA  . GLU A 1 411 ? 124.014 151.004 128.795 1.00 38.39  ? 386  GLU A CA  1 
ATOM   2462  C  C   . GLU A 1 411 ? 123.459 151.848 129.930 1.00 38.09  ? 386  GLU A C   1 
ATOM   2463  O  O   . GLU A 1 411 ? 123.489 153.079 129.837 1.00 46.57  ? 386  GLU A O   1 
ATOM   2464  C  CB  . GLU A 1 411 ? 122.991 150.951 127.656 1.00 34.71  ? 386  GLU A CB  1 
ATOM   2465  C  CG  . GLU A 1 411 ? 123.155 149.744 126.754 1.00 37.09  ? 386  GLU A CG  1 
ATOM   2466  C  CD  . GLU A 1 411 ? 122.408 149.887 125.447 1.00 48.84  ? 386  GLU A CD  1 
ATOM   2467  O  OE1 . GLU A 1 411 ? 121.880 150.985 125.181 1.00 49.92  ? 386  GLU A OE1 1 
ATOM   2468  O  OE2 . GLU A 1 411 ? 122.351 148.901 124.684 1.00 54.94  ? 386  GLU A OE2 1 
ATOM   2469  N  N   . GLY A 1 412 ? 122.962 151.224 130.992 1.00 19.38  ? 387  GLY A N   1 
ATOM   2470  C  CA  . GLY A 1 412 ? 122.465 151.964 132.132 1.00 15.50  ? 387  GLY A CA  1 
ATOM   2471  C  C   . GLY A 1 412 ? 123.570 152.379 133.078 1.00 25.75  ? 387  GLY A C   1 
ATOM   2472  O  O   . GLY A 1 412 ? 123.407 152.309 134.299 1.00 36.90  ? 387  GLY A O   1 
ATOM   2473  N  N   . LEU A 1 413 ? 124.707 152.807 132.524 1.00 31.05  ? 388  LEU A N   1 
ATOM   2474  C  CA  . LEU A 1 413 ? 125.820 153.244 133.361 1.00 31.63  ? 388  LEU A CA  1 
ATOM   2475  C  C   . LEU A 1 413 ? 125.443 154.451 134.207 1.00 32.79  ? 388  LEU A C   1 
ATOM   2476  O  O   . LEU A 1 413 ? 126.006 154.653 135.289 1.00 38.80  ? 388  LEU A O   1 
ATOM   2477  C  CB  . LEU A 1 413 ? 127.037 153.559 132.491 1.00 30.51  ? 388  LEU A CB  1 
ATOM   2478  C  CG  . LEU A 1 413 ? 128.286 154.068 133.209 1.00 30.77  ? 388  LEU A CG  1 
ATOM   2479  C  CD1 . LEU A 1 413 ? 128.785 153.036 134.202 1.00 29.37  ? 388  LEU A CD1 1 
ATOM   2480  C  CD2 . LEU A 1 413 ? 129.373 154.420 132.211 1.00 40.66  ? 388  LEU A CD2 1 
ATOM   2481  N  N   . LYS A 1 414 ? 124.490 155.254 133.744 1.00 30.27  ? 389  LYS A N   1 
ATOM   2482  C  CA  . LYS A 1 414 ? 124.037 156.411 134.498 1.00 28.63  ? 389  LYS A CA  1 
ATOM   2483  C  C   . LYS A 1 414 ? 122.917 156.084 135.476 1.00 34.33  ? 389  LYS A C   1 
ATOM   2484  O  O   . LYS A 1 414 ? 122.548 156.948 136.278 1.00 42.03  ? 389  LYS A O   1 
ATOM   2485  C  CB  . LYS A 1 414 ? 123.585 157.513 133.538 1.00 28.07  ? 389  LYS A CB  1 
ATOM   2486  C  CG  . LYS A 1 414 ? 124.393 157.556 132.254 1.00 35.93  ? 389  LYS A CG  1 
ATOM   2487  C  CD  . LYS A 1 414 ? 124.176 158.857 131.517 1.00 38.04  ? 389  LYS A CD  1 
ATOM   2488  C  CE  . LYS A 1 414 ? 124.785 160.016 132.280 1.00 41.58  ? 389  LYS A CE  1 
ATOM   2489  N  NZ  . LYS A 1 414 ? 124.059 161.281 132.002 1.00 42.85  ? 389  LYS A NZ  1 
ATOM   2490  N  N   . PHE A 1 415 ? 122.365 154.869 135.427 1.00 30.44  ? 390  PHE A N   1 
ATOM   2491  C  CA  . PHE A 1 415 ? 121.436 154.446 136.469 1.00 31.38  ? 390  PHE A CA  1 
ATOM   2492  C  C   . PHE A 1 415 ? 122.139 154.346 137.815 1.00 37.62  ? 390  PHE A C   1 
ATOM   2493  O  O   . PHE A 1 415 ? 121.617 154.815 138.833 1.00 44.88  ? 390  PHE A O   1 
ATOM   2494  C  CB  . PHE A 1 415 ? 120.800 153.107 136.102 1.00 32.07  ? 390  PHE A CB  1 
ATOM   2495  C  CG  . PHE A 1 415 ? 119.763 152.637 137.084 1.00 32.92  ? 390  PHE A CG  1 
ATOM   2496  C  CD1 . PHE A 1 415 ? 118.841 153.520 137.615 1.00 36.28  ? 390  PHE A CD1 1 
ATOM   2497  C  CD2 . PHE A 1 415 ? 119.715 151.312 137.479 1.00 31.62  ? 390  PHE A CD2 1 
ATOM   2498  C  CE1 . PHE A 1 415 ? 117.889 153.088 138.516 1.00 39.88  ? 390  PHE A CE1 1 
ATOM   2499  C  CE2 . PHE A 1 415 ? 118.765 150.876 138.378 1.00 27.88  ? 390  PHE A CE2 1 
ATOM   2500  C  CZ  . PHE A 1 415 ? 117.852 151.764 138.897 1.00 33.38  ? 390  PHE A CZ  1 
ATOM   2501  N  N   . VAL A 1 416 ? 123.321 153.741 137.837 1.00 32.45  ? 391  VAL A N   1 
ATOM   2502  C  CA  . VAL A 1 416 ? 124.143 153.669 139.041 1.00 36.60  ? 391  VAL A CA  1 
ATOM   2503  C  C   . VAL A 1 416 ? 125.141 154.818 138.943 1.00 39.67  ? 391  VAL A C   1 
ATOM   2504  O  O   . VAL A 1 416 ? 126.266 154.665 138.465 1.00 38.93  ? 391  VAL A O   1 
ATOM   2505  C  CB  . VAL A 1 416 ? 124.821 152.308 139.187 1.00 27.58  ? 391  VAL A CB  1 
ATOM   2506  C  CG1 . VAL A 1 416 ? 123.863 151.317 139.815 1.00 34.27  ? 391  VAL A CG1 1 
ATOM   2507  C  CG2 . VAL A 1 416 ? 125.277 151.792 137.832 1.00 25.08  ? 391  VAL A CG2 1 
ATOM   2508  N  N   . GLU A 1 417 ? 124.721 155.991 139.412 1.00 43.20  ? 392  GLU A N   1 
ATOM   2509  C  CA  . GLU A 1 417 ? 125.563 157.179 139.411 1.00 44.03  ? 392  GLU A CA  1 
ATOM   2510  C  C   . GLU A 1 417 ? 125.916 157.666 140.804 1.00 50.71  ? 392  GLU A C   1 
ATOM   2511  O  O   . GLU A 1 417 ? 127.017 158.182 141.003 1.00 53.45  ? 392  GLU A O   1 
ATOM   2512  C  CB  . GLU A 1 417 ? 124.879 158.318 138.646 1.00 47.78  ? 392  GLU A CB  1 
ATOM   2513  N  N   . ASP A 1 418 ? 125.010 157.515 141.769 1.00 69.07  ? 393  ASP A N   1 
ATOM   2514  C  CA  . ASP A 1 418 ? 125.313 157.837 143.156 1.00 68.89  ? 393  ASP A CA  1 
ATOM   2515  C  C   . ASP A 1 418 ? 126.139 156.758 143.841 1.00 73.34  ? 393  ASP A C   1 
ATOM   2516  O  O   . ASP A 1 418 ? 126.610 156.979 144.962 1.00 75.44  ? 393  ASP A O   1 
ATOM   2517  C  CB  . ASP A 1 418 ? 124.017 158.067 143.938 1.00 65.89  ? 393  ASP A CB  1 
ATOM   2518  N  N   . SER A 1 419 ? 126.325 155.605 143.201 1.00 74.08  ? 394  SER A N   1 
ATOM   2519  C  CA  . SER A 1 419 ? 127.095 154.505 143.764 1.00 74.82  ? 394  SER A CA  1 
ATOM   2520  C  C   . SER A 1 419 ? 128.480 154.381 143.143 1.00 76.59  ? 394  SER A C   1 
ATOM   2521  O  O   . SER A 1 419 ? 129.187 153.406 143.419 1.00 76.05  ? 394  SER A O   1 
ATOM   2522  C  CB  . SER A 1 419 ? 126.331 153.191 143.602 1.00 72.34  ? 394  SER A CB  1 
ATOM   2523  O  OG  . SER A 1 419 ? 126.746 152.504 142.436 1.00 72.92  ? 394  SER A OG  1 
ATOM   2524  N  N   . ALA A 1 420 ? 128.884 155.338 142.311 1.00 82.58  ? 395  ALA A N   1 
ATOM   2525  C  CA  . ALA A 1 420 ? 130.218 155.334 141.730 1.00 82.39  ? 395  ALA A CA  1 
ATOM   2526  C  C   . ALA A 1 420 ? 131.246 156.034 142.606 1.00 85.27  ? 395  ALA A C   1 
ATOM   2527  O  O   . ALA A 1 420 ? 132.437 156.013 142.276 1.00 82.94  ? 395  ALA A O   1 
ATOM   2528  C  CB  . ALA A 1 420 ? 130.197 155.990 140.345 1.00 82.53  ? 395  ALA A CB  1 
ATOM   2529  N  N   . GLU A 1 421 ? 130.818 156.648 143.708 1.00 97.96  ? 396  GLU A N   1 
ATOM   2530  C  CA  . GLU A 1 421 ? 131.713 157.312 144.644 1.00 97.33  ? 396  GLU A CA  1 
ATOM   2531  C  C   . GLU A 1 421 ? 132.054 156.439 145.844 1.00 95.88  ? 396  GLU A C   1 
ATOM   2532  O  O   . GLU A 1 421 ? 132.642 156.933 146.811 1.00 96.51  ? 396  GLU A O   1 
ATOM   2533  C  CB  . GLU A 1 421 ? 131.099 158.632 145.116 1.00 94.22  ? 396  GLU A CB  1 
ATOM   2534  N  N   . SER A 1 422 ? 131.697 155.159 145.805 1.00 93.10  ? 397  SER A N   1 
ATOM   2535  C  CA  . SER A 1 422 ? 131.962 154.228 146.891 1.00 92.57  ? 397  SER A CA  1 
ATOM   2536  C  C   . SER A 1 422 ? 133.030 153.231 146.465 1.00 93.33  ? 397  SER A C   1 
ATOM   2537  O  O   . SER A 1 422 ? 133.028 152.755 145.325 1.00 92.99  ? 397  SER A O   1 
ATOM   2538  C  CB  . SER A 1 422 ? 130.687 153.486 147.302 1.00 93.24  ? 397  SER A CB  1 
ATOM   2539  O  OG  . SER A 1 422 ? 129.762 154.362 147.923 1.00 94.03  ? 397  SER A OG  1 
ATOM   2540  N  N   . GLU A 1 423 ? 133.948 152.927 147.386 1.00 96.17  ? 398  GLU A N   1 
ATOM   2541  C  CA  . GLU A 1 423 ? 135.011 151.974 147.084 1.00 95.41  ? 398  GLU A CA  1 
ATOM   2542  C  C   . GLU A 1 423 ? 134.444 150.592 146.790 1.00 95.84  ? 398  GLU A C   1 
ATOM   2543  O  O   . GLU A 1 423 ? 134.901 149.906 145.868 1.00 95.89  ? 398  GLU A O   1 
ATOM   2544  C  CB  . GLU A 1 423 ? 136.006 151.912 148.243 1.00 93.21  ? 398  GLU A CB  1 
ATOM   2545  N  N   . ASP A 1 424 ? 133.450 150.165 147.562 1.00 88.28  ? 399  ASP A N   1 
ATOM   2546  C  CA  . ASP A 1 424 ? 132.770 148.903 147.326 1.00 88.12  ? 399  ASP A CA  1 
ATOM   2547  C  C   . ASP A 1 424 ? 131.623 149.128 146.341 1.00 89.01  ? 399  ASP A C   1 
ATOM   2548  O  O   . ASP A 1 424 ? 131.533 150.167 145.683 1.00 89.28  ? 399  ASP A O   1 
ATOM   2549  C  CB  . ASP A 1 424 ? 132.282 148.310 148.646 1.00 86.30  ? 399  ASP A CB  1 
ATOM   2550  C  CG  . ASP A 1 424 ? 131.553 149.324 149.505 1.00 86.72  ? 399  ASP A CG  1 
ATOM   2551  O  OD1 . ASP A 1 424 ? 131.574 150.524 149.159 1.00 85.48  ? 399  ASP A OD1 1 
ATOM   2552  O  OD2 . ASP A 1 424 ? 130.957 148.921 150.526 1.00 87.59  ? 399  ASP A OD2 1 
ATOM   2553  N  N   . GLY A 1 425 ? 130.732 148.148 146.229 1.00 71.97  ? 400  GLY A N   1 
ATOM   2554  C  CA  . GLY A 1 425 ? 129.564 148.293 145.384 1.00 68.70  ? 400  GLY A CA  1 
ATOM   2555  C  C   . GLY A 1 425 ? 128.440 149.015 146.094 1.00 66.24  ? 400  GLY A C   1 
ATOM   2556  O  O   . GLY A 1 425 ? 128.657 150.074 146.691 1.00 68.36  ? 400  GLY A O   1 
ATOM   2557  N  N   . VAL A 1 426 ? 127.234 148.460 146.039 1.00 50.65  ? 401  VAL A N   1 
ATOM   2558  C  CA  . VAL A 1 426 ? 126.080 149.012 146.736 1.00 52.65  ? 401  VAL A CA  1 
ATOM   2559  C  C   . VAL A 1 426 ? 125.731 148.088 147.894 1.00 54.55  ? 401  VAL A C   1 
ATOM   2560  O  O   . VAL A 1 426 ? 125.884 146.864 147.797 1.00 59.19  ? 401  VAL A O   1 
ATOM   2561  C  CB  . VAL A 1 426 ? 124.877 149.213 145.790 1.00 51.95  ? 401  VAL A CB  1 
ATOM   2562  C  CG1 . VAL A 1 426 ? 125.332 149.835 144.483 1.00 50.51  ? 401  VAL A CG1 1 
ATOM   2563  C  CG2 . VAL A 1 426 ? 124.151 147.906 145.530 1.00 54.10  ? 401  VAL A CG2 1 
ATOM   2564  N  N   . SER A 1 427 ? 125.308 148.680 149.006 1.00 49.02  ? 402  SER A N   1 
ATOM   2565  C  CA  . SER A 1 427 ? 124.934 147.896 150.171 1.00 52.72  ? 402  SER A CA  1 
ATOM   2566  C  C   . SER A 1 427 ? 123.564 147.256 149.967 1.00 54.95  ? 402  SER A C   1 
ATOM   2567  O  O   . SER A 1 427 ? 122.804 147.620 149.065 1.00 58.47  ? 402  SER A O   1 
ATOM   2568  C  CB  . SER A 1 427 ? 124.928 148.770 151.424 1.00 55.95  ? 402  SER A CB  1 
ATOM   2569  O  OG  . SER A 1 427 ? 124.428 150.064 151.139 1.00 54.20  ? 402  SER A OG  1 
ATOM   2570  N  N   . ALA A 1 428 ? 123.256 146.279 150.824 1.00 55.49  ? 403  ALA A N   1 
ATOM   2571  C  CA  . ALA A 1 428 ? 121.960 145.613 150.749 1.00 54.89  ? 403  ALA A CA  1 
ATOM   2572  C  C   . ALA A 1 428 ? 120.815 146.587 150.989 1.00 54.31  ? 403  ALA A C   1 
ATOM   2573  O  O   . ALA A 1 428 ? 119.708 146.379 150.481 1.00 55.34  ? 403  ALA A O   1 
ATOM   2574  C  CB  . ALA A 1 428 ? 121.899 144.463 151.753 1.00 58.15  ? 403  ALA A CB  1 
ATOM   2575  N  N   . SER A 1 429 ? 121.055 147.646 151.762 1.00 54.94  ? 404  SER A N   1 
ATOM   2576  C  CA  . SER A 1 429 ? 120.050 148.682 151.952 1.00 54.81  ? 404  SER A CA  1 
ATOM   2577  C  C   . SER A 1 429 ? 119.946 149.618 150.756 1.00 57.26  ? 404  SER A C   1 
ATOM   2578  O  O   . SER A 1 429 ? 118.940 150.322 150.623 1.00 58.20  ? 404  SER A O   1 
ATOM   2579  C  CB  . SER A 1 429 ? 120.356 149.491 153.214 1.00 57.78  ? 404  SER A CB  1 
ATOM   2580  O  OG  . SER A 1 429 ? 120.336 148.666 154.366 1.00 60.77  ? 404  SER A OG  1 
ATOM   2581  N  N   . ALA A 1 430 ? 120.961 149.649 149.895 1.00 56.49  ? 405  ALA A N   1 
ATOM   2582  C  CA  . ALA A 1 430 ? 120.928 150.466 148.691 1.00 56.29  ? 405  ALA A CA  1 
ATOM   2583  C  C   . ALA A 1 430 ? 120.458 149.701 147.462 1.00 54.78  ? 405  ALA A C   1 
ATOM   2584  O  O   . ALA A 1 430 ? 120.258 150.317 146.410 1.00 57.09  ? 405  ALA A O   1 
ATOM   2585  C  CB  . ALA A 1 430 ? 122.311 151.065 148.418 1.00 50.83  ? 405  ALA A CB  1 
ATOM   2586  N  N   . PHE A 1 431 ? 120.281 148.385 147.564 1.00 43.90  ? 406  PHE A N   1 
ATOM   2587  C  CA  . PHE A 1 431 ? 119.792 147.587 146.449 1.00 39.24  ? 406  PHE A CA  1 
ATOM   2588  C  C   . PHE A 1 431 ? 118.288 147.372 146.486 1.00 47.10  ? 406  PHE A C   1 
ATOM   2589  O  O   . PHE A 1 431 ? 117.672 147.209 145.429 1.00 60.34  ? 406  PHE A O   1 
ATOM   2590  C  CB  . PHE A 1 431 ? 120.492 146.224 146.421 1.00 46.17  ? 406  PHE A CB  1 
ATOM   2591  C  CG  . PHE A 1 431 ? 120.096 145.362 145.257 1.00 46.20  ? 406  PHE A CG  1 
ATOM   2592  C  CD1 . PHE A 1 431 ? 120.595 145.614 143.991 1.00 47.05  ? 406  PHE A CD1 1 
ATOM   2593  C  CD2 . PHE A 1 431 ? 119.226 144.301 145.427 1.00 45.48  ? 406  PHE A CD2 1 
ATOM   2594  C  CE1 . PHE A 1 431 ? 120.233 144.823 142.920 1.00 44.13  ? 406  PHE A CE1 1 
ATOM   2595  C  CE2 . PHE A 1 431 ? 118.861 143.509 144.358 1.00 46.32  ? 406  PHE A CE2 1 
ATOM   2596  C  CZ  . PHE A 1 431 ? 119.365 143.771 143.104 1.00 41.77  ? 406  PHE A CZ  1 
ATOM   2597  N  N   . ASP A 1 432 ? 117.682 147.367 147.671 1.00 49.10  ? 407  ASP A N   1 
ATOM   2598  C  CA  . ASP A 1 432 ? 116.235 147.267 147.791 1.00 49.57  ? 407  ASP A CA  1 
ATOM   2599  C  C   . ASP A 1 432 ? 115.545 148.622 147.750 1.00 51.23  ? 407  ASP A C   1 
ATOM   2600  O  O   . ASP A 1 432 ? 114.311 148.673 147.738 1.00 56.52  ? 407  ASP A O   1 
ATOM   2601  C  CB  . ASP A 1 432 ? 115.859 146.536 149.084 1.00 55.23  ? 407  ASP A CB  1 
ATOM   2602  C  CG  . ASP A 1 432 ? 116.688 146.982 150.267 1.00 62.77  ? 407  ASP A CG  1 
ATOM   2603  O  OD1 . ASP A 1 432 ? 117.304 148.065 150.188 1.00 64.78  ? 407  ASP A OD1 1 
ATOM   2604  O  OD2 . ASP A 1 432 ? 116.729 146.248 151.277 1.00 61.50  ? 407  ASP A OD2 1 
ATOM   2605  N  N   . PHE A 1 433 ? 116.308 149.714 147.734 1.00 47.39  ? 408  PHE A N   1 
ATOM   2606  C  CA  . PHE A 1 433 ? 115.756 151.052 147.569 1.00 49.77  ? 408  PHE A CA  1 
ATOM   2607  C  C   . PHE A 1 433 ? 115.702 151.466 146.105 1.00 52.09  ? 408  PHE A C   1 
ATOM   2608  O  O   . PHE A 1 433 ? 114.687 152.007 145.649 1.00 48.81  ? 408  PHE A O   1 
ATOM   2609  C  CB  . PHE A 1 433 ? 116.582 152.063 148.368 1.00 47.92  ? 408  PHE A CB  1 
ATOM   2610  C  CG  . PHE A 1 433 ? 115.978 153.436 148.419 1.00 50.98  ? 408  PHE A CG  1 
ATOM   2611  C  CD1 . PHE A 1 433 ? 114.637 153.609 148.712 1.00 51.21  ? 408  PHE A CD1 1 
ATOM   2612  C  CD2 . PHE A 1 433 ? 116.756 154.556 148.177 1.00 51.62  ? 408  PHE A CD2 1 
ATOM   2613  C  CE1 . PHE A 1 433 ? 114.082 154.874 148.762 1.00 51.41  ? 408  PHE A CE1 1 
ATOM   2614  C  CE2 . PHE A 1 433 ? 116.208 155.822 148.225 1.00 50.32  ? 408  PHE A CE2 1 
ATOM   2615  C  CZ  . PHE A 1 433 ? 114.869 155.981 148.518 1.00 51.24  ? 408  PHE A CZ  1 
ATOM   2616  N  N   . THR A 1 434 ? 116.783 151.219 145.359 1.00 50.55  ? 409  THR A N   1 
ATOM   2617  C  CA  . THR A 1 434 ? 116.781 151.523 143.933 1.00 46.35  ? 409  THR A CA  1 
ATOM   2618  C  C   . THR A 1 434 ? 115.738 150.694 143.198 1.00 43.89  ? 409  THR A C   1 
ATOM   2619  O  O   . THR A 1 434 ? 115.029 151.209 142.328 1.00 52.51  ? 409  THR A O   1 
ATOM   2620  C  CB  . THR A 1 434 ? 118.167 151.286 143.336 1.00 40.82  ? 409  THR A CB  1 
ATOM   2621  O  OG1 . THR A 1 434 ? 118.564 149.930 143.568 1.00 44.54  ? 409  THR A OG1 1 
ATOM   2622  C  CG2 . THR A 1 434 ? 119.186 152.223 143.960 1.00 40.47  ? 409  THR A CG2 1 
ATOM   2623  N  N   . VAL A 1 435 ? 115.619 149.410 143.542 1.00 33.74  ? 410  VAL A N   1 
ATOM   2624  C  CA  . VAL A 1 435 ? 114.623 148.559 142.898 1.00 38.11  ? 410  VAL A CA  1 
ATOM   2625  C  C   . VAL A 1 435 ? 113.213 149.018 143.251 1.00 44.54  ? 410  VAL A C   1 
ATOM   2626  O  O   . VAL A 1 435 ? 112.316 149.020 142.399 1.00 52.20  ? 410  VAL A O   1 
ATOM   2627  C  CB  . VAL A 1 435 ? 114.858 147.086 143.278 1.00 32.66  ? 410  VAL A CB  1 
ATOM   2628  C  CG1 . VAL A 1 435 ? 113.698 146.228 142.822 1.00 36.91  ? 410  VAL A CG1 1 
ATOM   2629  C  CG2 . VAL A 1 435 ? 116.150 146.587 142.659 1.00 34.29  ? 410  VAL A CG2 1 
ATOM   2630  N  N   . SER A 1 436 ? 112.991 149.410 144.508 1.00 45.78  ? 411  SER A N   1 
ATOM   2631  C  CA  . SER A 1 436 ? 111.673 149.899 144.903 1.00 46.71  ? 411  SER A CA  1 
ATOM   2632  C  C   . SER A 1 436 ? 111.305 151.170 144.148 1.00 52.88  ? 411  SER A C   1 
ATOM   2633  O  O   . SER A 1 436 ? 110.178 151.302 143.653 1.00 57.46  ? 411  SER A O   1 
ATOM   2634  C  CB  . SER A 1 436 ? 111.633 150.143 146.411 1.00 51.38  ? 411  SER A CB  1 
ATOM   2635  O  OG  . SER A 1 436 ? 111.710 148.924 147.127 1.00 58.11  ? 411  SER A OG  1 
ATOM   2636  N  N   . ASN A 1 437 ? 112.243 152.114 144.044 1.00 46.08  ? 412  ASN A N   1 
ATOM   2637  C  CA  . ASN A 1 437 ? 111.981 153.332 143.282 1.00 44.23  ? 412  ASN A CA  1 
ATOM   2638  C  C   . ASN A 1 437 ? 111.752 153.019 141.810 1.00 46.13  ? 412  ASN A C   1 
ATOM   2639  O  O   . ASN A 1 437 ? 110.903 153.637 141.159 1.00 47.42  ? 412  ASN A O   1 
ATOM   2640  C  CB  . ASN A 1 437 ? 113.140 154.314 143.446 1.00 48.23  ? 412  ASN A CB  1 
ATOM   2641  C  CG  . ASN A 1 437 ? 113.120 155.019 144.785 1.00 55.05  ? 412  ASN A CG  1 
ATOM   2642  O  OD1 . ASN A 1 437 ? 112.118 155.624 145.166 1.00 58.55  ? 412  ASN A OD1 1 
ATOM   2643  N  ND2 . ASN A 1 437 ? 114.230 154.945 145.507 1.00 51.03  ? 412  ASN A ND2 1 
ATOM   2644  N  N   . PHE A 1 438 ? 112.510 152.064 141.269 1.00 44.82  ? 413  PHE A N   1 
ATOM   2645  C  CA  . PHE A 1 438 ? 112.346 151.643 139.883 1.00 40.99  ? 413  PHE A CA  1 
ATOM   2646  C  C   . PHE A 1 438 ? 110.937 151.118 139.634 1.00 45.34  ? 413  PHE A C   1 
ATOM   2647  O  O   . PHE A 1 438 ? 110.270 151.519 138.672 1.00 54.27  ? 413  PHE A O   1 
ATOM   2648  C  CB  . PHE A 1 438 ? 113.407 150.583 139.574 1.00 42.25  ? 413  PHE A CB  1 
ATOM   2649  C  CG  . PHE A 1 438 ? 113.285 149.945 138.223 1.00 43.30  ? 413  PHE A CG  1 
ATOM   2650  C  CD1 . PHE A 1 438 ? 112.475 148.840 138.032 1.00 43.33  ? 413  PHE A CD1 1 
ATOM   2651  C  CD2 . PHE A 1 438 ? 114.021 150.421 137.155 1.00 47.66  ? 413  PHE A CD2 1 
ATOM   2652  C  CE1 . PHE A 1 438 ? 112.379 148.247 136.797 1.00 43.72  ? 413  PHE A CE1 1 
ATOM   2653  C  CE2 . PHE A 1 438 ? 113.930 149.828 135.920 1.00 44.74  ? 413  PHE A CE2 1 
ATOM   2654  C  CZ  . PHE A 1 438 ? 113.108 148.740 135.742 1.00 40.26  ? 413  PHE A CZ  1 
ATOM   2655  N  N   . VAL A 1 439 ? 110.462 150.229 140.509 1.00 41.87  ? 414  VAL A N   1 
ATOM   2656  C  CA  . VAL A 1 439 ? 109.121 149.670 140.358 1.00 42.14  ? 414  VAL A CA  1 
ATOM   2657  C  C   . VAL A 1 439 ? 108.067 150.758 140.513 1.00 49.98  ? 414  VAL A C   1 
ATOM   2658  O  O   . VAL A 1 439 ? 107.083 150.800 139.763 1.00 52.17  ? 414  VAL A O   1 
ATOM   2659  C  CB  . VAL A 1 439 ? 108.899 148.524 141.361 1.00 37.77  ? 414  VAL A CB  1 
ATOM   2660  C  CG1 . VAL A 1 439 ? 107.475 148.008 141.270 1.00 41.55  ? 414  VAL A CG1 1 
ATOM   2661  C  CG2 . VAL A 1 439 ? 109.877 147.404 141.101 1.00 44.53  ? 414  VAL A CG2 1 
ATOM   2662  N  N   . ASP A 1 440 ? 108.249 151.651 141.488 1.00 50.50  ? 415  ASP A N   1 
ATOM   2663  C  CA  . ASP A 1 440 ? 107.271 152.712 141.706 1.00 46.49  ? 415  ASP A CA  1 
ATOM   2664  C  C   . ASP A 1 440 ? 107.181 153.641 140.502 1.00 51.49  ? 415  ASP A C   1 
ATOM   2665  O  O   . ASP A 1 440 ? 106.083 154.041 140.098 1.00 53.75  ? 415  ASP A O   1 
ATOM   2666  C  CB  . ASP A 1 440 ? 107.629 153.501 142.965 1.00 47.17  ? 415  ASP A CB  1 
ATOM   2667  C  CG  . ASP A 1 440 ? 107.059 152.879 144.223 1.00 57.01  ? 415  ASP A CG  1 
ATOM   2668  O  OD1 . ASP A 1 440 ? 106.558 151.737 144.150 1.00 58.66  ? 415  ASP A OD1 1 
ATOM   2669  O  OD2 . ASP A 1 440 ? 107.114 153.531 145.287 1.00 59.12  ? 415  ASP A OD2 1 
ATOM   2670  N  N   . ASN A 1 441 ? 108.326 153.995 139.914 1.00 45.35  ? 416  ASN A N   1 
ATOM   2671  C  CA  . ASN A 1 441 ? 108.331 154.949 138.810 1.00 39.89  ? 416  ASN A CA  1 
ATOM   2672  C  C   . ASN A 1 441 ? 107.841 154.316 137.515 1.00 44.25  ? 416  ASN A C   1 
ATOM   2673  O  O   . ASN A 1 441 ? 107.129 154.960 136.736 1.00 50.46  ? 416  ASN A O   1 
ATOM   2674  C  CB  . ASN A 1 441 ? 109.734 155.521 138.621 1.00 36.63  ? 416  ASN A CB  1 
ATOM   2675  C  CG  . ASN A 1 441 ? 110.175 156.378 139.786 1.00 46.46  ? 416  ASN A CG  1 
ATOM   2676  O  OD1 . ASN A 1 441 ? 109.352 156.969 140.483 1.00 48.67  ? 416  ASN A OD1 1 
ATOM   2677  N  ND2 . ASN A 1 441 ? 111.482 156.450 140.005 1.00 49.94  ? 416  ASN A ND2 1 
ATOM   2678  N  N   . LEU A 1 442 ? 108.208 153.060 137.262 1.00 43.01  ? 417  LEU A N   1 
ATOM   2679  C  CA  . LEU A 1 442 ? 107.958 152.485 135.946 1.00 38.75  ? 417  LEU A CA  1 
ATOM   2680  C  C   . LEU A 1 442 ? 106.678 151.660 135.887 1.00 42.51  ? 417  LEU A C   1 
ATOM   2681  O  O   . LEU A 1 442 ? 105.919 151.775 134.918 1.00 48.78  ? 417  LEU A O   1 
ATOM   2682  C  CB  . LEU A 1 442 ? 109.154 151.636 135.518 1.00 37.06  ? 417  LEU A CB  1 
ATOM   2683  C  CG  . LEU A 1 442 ? 110.100 152.398 134.592 1.00 41.74  ? 417  LEU A CG  1 
ATOM   2684  C  CD1 . LEU A 1 442 ? 111.372 151.621 134.357 1.00 48.41  ? 417  LEU A CD1 1 
ATOM   2685  C  CD2 . LEU A 1 442 ? 109.406 152.701 133.279 1.00 46.28  ? 417  LEU A CD2 1 
ATOM   2686  N  N   . TYR A 1 443 ? 106.415 150.826 136.892 1.00 48.33  ? 418  TYR A N   1 
ATOM   2687  C  CA  . TYR A 1 443 ? 105.198 150.021 136.919 1.00 50.11  ? 418  TYR A CA  1 
ATOM   2688  C  C   . TYR A 1 443 ? 104.132 150.633 137.822 1.00 53.50  ? 418  TYR A C   1 
ATOM   2689  O  O   . TYR A 1 443 ? 103.035 150.955 137.358 1.00 53.51  ? 418  TYR A O   1 
ATOM   2690  C  CB  . TYR A 1 443 ? 105.531 148.589 137.357 1.00 49.43  ? 418  TYR A CB  1 
ATOM   2691  C  CG  . TYR A 1 443 ? 106.256 147.797 136.293 1.00 47.77  ? 418  TYR A CG  1 
ATOM   2692  C  CD1 . TYR A 1 443 ? 105.567 147.253 135.220 1.00 49.31  ? 418  TYR A CD1 1 
ATOM   2693  C  CD2 . TYR A 1 443 ? 107.628 147.603 136.356 1.00 46.50  ? 418  TYR A CD2 1 
ATOM   2694  C  CE1 . TYR A 1 443 ? 106.220 146.534 134.243 1.00 47.84  ? 418  TYR A CE1 1 
ATOM   2695  C  CE2 . TYR A 1 443 ? 108.291 146.883 135.382 1.00 46.69  ? 418  TYR A CE2 1 
ATOM   2696  C  CZ  . TYR A 1 443 ? 107.581 146.351 134.328 1.00 46.25  ? 418  TYR A CZ  1 
ATOM   2697  O  OH  . TYR A 1 443 ? 108.232 145.634 133.353 1.00 47.91  ? 418  TYR A OH  1 
ATOM   2698  N  N   . GLY A 1 444 ? 104.442 150.808 139.103 1.00 67.83  ? 419  GLY A N   1 
ATOM   2699  C  CA  . GLY A 1 444 ? 103.553 151.520 140.011 1.00 69.44  ? 419  GLY A CA  1 
ATOM   2700  C  C   . GLY A 1 444 ? 102.157 150.948 140.124 1.00 73.37  ? 419  GLY A C   1 
ATOM   2701  O  O   . GLY A 1 444 ? 101.183 151.709 140.192 1.00 72.74  ? 419  GLY A O   1 
ATOM   2702  N  N   . TYR A 1 445 ? 102.032 149.622 140.148 1.00 93.46  ? 420  TYR A N   1 
ATOM   2703  C  CA  . TYR A 1 445 ? 100.728 148.989 140.272 1.00 91.37  ? 420  TYR A CA  1 
ATOM   2704  C  C   . TYR A 1 445 ? 100.514 148.571 141.717 1.00 94.41  ? 420  TYR A C   1 
ATOM   2705  O  O   . TYR A 1 445 ? 101.211 147.663 142.196 1.00 96.90  ? 420  TYR A O   1 
ATOM   2706  C  CB  . TYR A 1 445 ? 100.624 147.779 139.345 1.00 91.05  ? 420  TYR A CB  1 
ATOM   2707  N  N   . PRO A 1 446 ? 99.580  149.187 142.446 1.00 101.59 ? 421  PRO A N   1 
ATOM   2708  C  CA  . PRO A 1 446 ? 99.401  148.830 143.863 1.00 101.23 ? 421  PRO A CA  1 
ATOM   2709  C  C   . PRO A 1 446 ? 99.040  147.373 144.087 1.00 101.07 ? 421  PRO A C   1 
ATOM   2710  O  O   . PRO A 1 446 ? 99.390  146.813 145.134 1.00 101.28 ? 421  PRO A O   1 
ATOM   2711  C  CB  . PRO A 1 446 ? 98.271  149.765 144.318 1.00 101.28 ? 421  PRO A CB  1 
ATOM   2712  C  CG  . PRO A 1 446 ? 98.294  150.898 143.343 1.00 100.37 ? 421  PRO A CG  1 
ATOM   2713  C  CD  . PRO A 1 446 ? 98.699  150.292 142.035 1.00 101.29 ? 421  PRO A CD  1 
ATOM   2714  N  N   . GLU A 1 447 ? 98.341  146.744 143.139 1.00 100.22 ? 422  GLU A N   1 
ATOM   2715  C  CA  . GLU A 1 447 ? 97.917  145.359 143.324 1.00 100.90 ? 422  GLU A CA  1 
ATOM   2716  C  C   . GLU A 1 447 ? 99.110  144.416 143.428 1.00 103.33 ? 422  GLU A C   1 
ATOM   2717  O  O   . GLU A 1 447 ? 99.120  143.508 144.267 1.00 105.46 ? 422  GLU A O   1 
ATOM   2718  C  CB  . GLU A 1 447 ? 96.999  144.936 142.177 1.00 100.95 ? 422  GLU A CB  1 
ATOM   2719  N  N   . GLY A 1 448 ? 100.124 144.612 142.589 1.00 93.90  ? 423  GLY A N   1 
ATOM   2720  C  CA  . GLY A 1 448 ? 101.253 143.704 142.563 1.00 91.57  ? 423  GLY A CA  1 
ATOM   2721  C  C   . GLY A 1 448 ? 102.609 144.372 142.652 1.00 88.93  ? 423  GLY A C   1 
ATOM   2722  O  O   . GLY A 1 448 ? 103.566 143.921 142.018 1.00 90.75  ? 423  GLY A O   1 
ATOM   2723  N  N   . LYS A 1 449 ? 102.710 145.447 143.434 1.00 84.73  ? 424  LYS A N   1 
ATOM   2724  C  CA  . LYS A 1 449 ? 103.987 146.129 143.602 1.00 83.04  ? 424  LYS A CA  1 
ATOM   2725  C  C   . LYS A 1 449 ? 104.893 145.452 144.620 1.00 83.67  ? 424  LYS A C   1 
ATOM   2726  O  O   . LYS A 1 449 ? 106.082 145.783 144.679 1.00 85.01  ? 424  LYS A O   1 
ATOM   2727  C  CB  . LYS A 1 449 ? 103.761 147.585 144.018 1.00 82.38  ? 424  LYS A CB  1 
ATOM   2728  N  N   . ASP A 1 450 ? 104.370 144.519 145.416 1.00 73.69  ? 425  ASP A N   1 
ATOM   2729  C  CA  . ASP A 1 450 ? 105.180 143.807 146.394 1.00 71.98  ? 425  ASP A CA  1 
ATOM   2730  C  C   . ASP A 1 450 ? 105.581 142.413 145.939 1.00 72.45  ? 425  ASP A C   1 
ATOM   2731  O  O   . ASP A 1 450 ? 106.539 141.854 146.482 1.00 73.93  ? 425  ASP A O   1 
ATOM   2732  C  CB  . ASP A 1 450 ? 104.438 143.706 147.732 1.00 73.50  ? 425  ASP A CB  1 
ATOM   2733  C  CG  . ASP A 1 450 ? 102.948 143.492 147.558 1.00 78.52  ? 425  ASP A CG  1 
ATOM   2734  O  OD1 . ASP A 1 450 ? 102.556 142.753 146.631 1.00 78.81  ? 425  ASP A OD1 1 
ATOM   2735  O  OD2 . ASP A 1 450 ? 102.169 144.063 148.350 1.00 74.29  ? 425  ASP A OD2 1 
ATOM   2736  N  N   . VAL A 1 451 ? 104.873 141.840 144.970 1.00 52.95  ? 426  VAL A N   1 
ATOM   2737  C  CA  . VAL A 1 451 ? 105.283 140.571 144.378 1.00 47.06  ? 426  VAL A CA  1 
ATOM   2738  C  C   . VAL A 1 451 ? 106.305 140.789 143.271 1.00 51.97  ? 426  VAL A C   1 
ATOM   2739  O  O   . VAL A 1 451 ? 107.309 140.077 143.195 1.00 56.09  ? 426  VAL A O   1 
ATOM   2740  C  CB  . VAL A 1 451 ? 104.048 139.807 143.863 1.00 40.52  ? 426  VAL A CB  1 
ATOM   2741  C  CG1 . VAL A 1 451 ? 104.464 138.678 142.937 1.00 41.13  ? 426  VAL A CG1 1 
ATOM   2742  C  CG2 . VAL A 1 451 ? 103.236 139.272 145.029 1.00 46.89  ? 426  VAL A CG2 1 
ATOM   2743  N  N   . LEU A 1 452 ? 106.064 141.776 142.406 1.00 49.05  ? 427  LEU A N   1 
ATOM   2744  C  CA  . LEU A 1 452 ? 107.006 142.077 141.334 1.00 42.85  ? 427  LEU A CA  1 
ATOM   2745  C  C   . LEU A 1 452 ? 108.348 142.537 141.889 1.00 46.62  ? 427  LEU A C   1 
ATOM   2746  O  O   . LEU A 1 452 ? 109.406 142.152 141.376 1.00 53.11  ? 427  LEU A O   1 
ATOM   2747  C  CB  . LEU A 1 452 ? 106.416 143.139 140.407 1.00 42.63  ? 427  LEU A CB  1 
ATOM   2748  C  CG  . LEU A 1 452 ? 107.086 143.311 139.045 1.00 41.41  ? 427  LEU A CG  1 
ATOM   2749  C  CD1 . LEU A 1 452 ? 107.199 141.976 138.337 1.00 44.50  ? 427  LEU A CD1 1 
ATOM   2750  C  CD2 . LEU A 1 452 ? 106.306 144.302 138.202 1.00 47.58  ? 427  LEU A CD2 1 
ATOM   2751  N  N   . ARG A 1 453 ? 108.327 143.361 142.937 1.00 42.15  ? 428  ARG A N   1 
ATOM   2752  C  CA  . ARG A 1 453 ? 109.576 143.847 143.511 1.00 40.39  ? 428  ARG A CA  1 
ATOM   2753  C  C   . ARG A 1 453 ? 110.432 142.694 144.017 1.00 47.79  ? 428  ARG A C   1 
ATOM   2754  O  O   . ARG A 1 453 ? 111.640 142.650 143.760 1.00 53.04  ? 428  ARG A O   1 
ATOM   2755  C  CB  . ARG A 1 453 ? 109.284 144.839 144.636 1.00 44.19  ? 428  ARG A CB  1 
ATOM   2756  C  CG  . ARG A 1 453 ? 110.368 144.909 145.694 1.00 45.98  ? 428  ARG A CG  1 
ATOM   2757  C  CD  . ARG A 1 453 ? 110.186 146.105 146.615 1.00 51.27  ? 428  ARG A CD  1 
ATOM   2758  N  NE  . ARG A 1 453 ? 108.931 146.049 147.354 1.00 52.67  ? 428  ARG A NE  1 
ATOM   2759  C  CZ  . ARG A 1 453 ? 107.933 146.910 147.203 1.00 54.37  ? 428  ARG A CZ  1 
ATOM   2760  N  NH1 . ARG A 1 453 ? 108.009 147.911 146.341 1.00 49.52  ? 428  ARG A NH1 1 
ATOM   2761  N  NH2 . ARG A 1 453 ? 106.834 146.765 147.937 1.00 53.22  ? 428  ARG A NH2 1 
ATOM   2762  N  N   . GLU A 1 454 ? 109.817 141.731 144.707 1.00 48.49  ? 429  GLU A N   1 
ATOM   2763  C  CA  . GLU A 1 454 ? 110.575 140.598 145.228 1.00 43.59  ? 429  GLU A CA  1 
ATOM   2764  C  C   . GLU A 1 454 ? 111.139 139.736 144.105 1.00 41.22  ? 429  GLU A C   1 
ATOM   2765  O  O   . GLU A 1 454 ? 112.288 139.285 144.183 1.00 46.15  ? 429  GLU A O   1 
ATOM   2766  C  CB  . GLU A 1 454 ? 109.699 139.760 146.159 1.00 39.36  ? 429  GLU A CB  1 
ATOM   2767  C  CG  . GLU A 1 454 ? 109.277 140.473 147.435 1.00 45.95  ? 429  GLU A CG  1 
ATOM   2768  C  CD  . GLU A 1 454 ? 110.453 140.978 148.254 1.00 53.49  ? 429  GLU A CD  1 
ATOM   2769  O  OE1 . GLU A 1 454 ? 111.533 140.352 148.207 1.00 57.01  ? 429  GLU A OE1 1 
ATOM   2770  O  OE2 . GLU A 1 454 ? 110.296 142.004 148.949 1.00 50.48  ? 429  GLU A OE2 1 
ATOM   2771  N  N   . THR A 1 455 ? 110.359 139.499 143.047 1.00 30.12  ? 430  THR A N   1 
ATOM   2772  C  CA  . THR A 1 455 ? 110.841 138.607 141.997 1.00 30.68  ? 430  THR A CA  1 
ATOM   2773  C  C   . THR A 1 455 ? 111.928 139.261 141.150 1.00 35.96  ? 430  THR A C   1 
ATOM   2774  O  O   . THR A 1 455 ? 112.862 138.575 140.718 1.00 42.62  ? 430  THR A O   1 
ATOM   2775  C  CB  . THR A 1 455 ? 109.682 138.115 141.124 1.00 31.56  ? 430  THR A CB  1 
ATOM   2776  O  OG1 . THR A 1 455 ? 110.160 137.112 140.220 1.00 32.90  ? 430  THR A OG1 1 
ATOM   2777  C  CG2 . THR A 1 455 ? 109.065 139.241 140.325 1.00 38.04  ? 430  THR A CG2 1 
ATOM   2778  N  N   . ILE A 1 456 ? 111.857 140.579 140.922 1.00 36.00  ? 431  ILE A N   1 
ATOM   2779  C  CA  . ILE A 1 456 ? 112.954 141.230 140.205 1.00 33.28  ? 431  ILE A CA  1 
ATOM   2780  C  C   . ILE A 1 456 ? 114.126 141.555 141.114 1.00 38.77  ? 431  ILE A C   1 
ATOM   2781  O  O   . ILE A 1 456 ? 115.209 141.882 140.614 1.00 40.73  ? 431  ILE A O   1 
ATOM   2782  C  CB  . ILE A 1 456 ? 112.521 142.516 139.475 1.00 27.44  ? 431  ILE A CB  1 
ATOM   2783  C  CG1 . ILE A 1 456 ? 112.542 143.717 140.415 1.00 32.26  ? 431  ILE A CG1 1 
ATOM   2784  C  CG2 . ILE A 1 456 ? 111.157 142.345 138.828 1.00 39.31  ? 431  ILE A CG2 1 
ATOM   2785  C  CD1 . ILE A 1 456 ? 112.148 145.000 139.736 1.00 37.80  ? 431  ILE A CD1 1 
ATOM   2786  N  N   . LYS A 1 457 ? 113.946 141.479 142.434 1.00 45.40  ? 432  LYS A N   1 
ATOM   2787  C  CA  . LYS A 1 457 ? 115.095 141.484 143.331 1.00 38.73  ? 432  LYS A CA  1 
ATOM   2788  C  C   . LYS A 1 457 ? 115.797 140.134 143.316 1.00 39.51  ? 432  LYS A C   1 
ATOM   2789  O  O   . LYS A 1 457 ? 117.029 140.065 143.381 1.00 42.82  ? 432  LYS A O   1 
ATOM   2790  C  CB  . LYS A 1 457 ? 114.654 141.830 144.751 1.00 35.99  ? 432  LYS A CB  1 
ATOM   2791  C  CG  . LYS A 1 457 ? 114.670 143.305 145.077 1.00 39.21  ? 432  LYS A CG  1 
ATOM   2792  C  CD  . LYS A 1 457 ? 114.561 143.517 146.574 1.00 42.59  ? 432  LYS A CD  1 
ATOM   2793  C  CE  . LYS A 1 457 ? 113.712 144.730 146.892 1.00 52.72  ? 432  LYS A CE  1 
ATOM   2794  N  NZ  . LYS A 1 457 ? 113.118 144.652 148.253 1.00 47.66  ? 432  LYS A NZ  1 
ATOM   2795  N  N   . PHE A 1 458 ? 115.023 139.051 143.238 1.00 35.77  ? 433  PHE A N   1 
ATOM   2796  C  CA  . PHE A 1 458 ? 115.611 137.717 143.232 1.00 37.06  ? 433  PHE A CA  1 
ATOM   2797  C  C   . PHE A 1 458 ? 116.284 137.411 141.901 1.00 44.00  ? 433  PHE A C   1 
ATOM   2798  O  O   . PHE A 1 458 ? 117.320 136.738 141.865 1.00 56.45  ? 433  PHE A O   1 
ATOM   2799  C  CB  . PHE A 1 458 ? 114.543 136.669 143.534 1.00 33.90  ? 433  PHE A CB  1 
ATOM   2800  C  CG  . PHE A 1 458 ? 114.854 135.315 142.968 1.00 29.97  ? 433  PHE A CG  1 
ATOM   2801  C  CD1 . PHE A 1 458 ? 115.787 134.496 143.573 1.00 33.98  ? 433  PHE A CD1 1 
ATOM   2802  C  CD2 . PHE A 1 458 ? 114.230 134.872 141.817 1.00 41.34  ? 433  PHE A CD2 1 
ATOM   2803  C  CE1 . PHE A 1 458 ? 116.080 133.256 143.052 1.00 34.89  ? 433  PHE A CE1 1 
ATOM   2804  C  CE2 . PHE A 1 458 ? 114.519 133.633 141.292 1.00 40.49  ? 433  PHE A CE2 1 
ATOM   2805  C  CZ  . PHE A 1 458 ? 115.446 132.825 141.910 1.00 35.03  ? 433  PHE A CZ  1 
ATOM   2806  N  N   . MET A 1 459 ? 115.702 137.873 140.793 1.00 36.37  ? 434  MET A N   1 
ATOM   2807  C  CA  . MET A 1 459 ? 116.265 137.539 139.489 1.00 35.97  ? 434  MET A CA  1 
ATOM   2808  C  C   . MET A 1 459 ? 117.594 138.246 139.255 1.00 44.15  ? 434  MET A C   1 
ATOM   2809  O  O   . MET A 1 459 ? 118.547 137.637 138.758 1.00 48.15  ? 434  MET A O   1 
ATOM   2810  C  CB  . MET A 1 459 ? 115.267 137.881 138.385 1.00 40.18  ? 434  MET A CB  1 
ATOM   2811  C  CG  . MET A 1 459 ? 115.606 137.274 137.036 1.00 43.35  ? 434  MET A CG  1 
ATOM   2812  S  SD  . MET A 1 459 ? 115.204 135.521 136.935 1.00 61.14  ? 434  MET A SD  1 
ATOM   2813  C  CE  . MET A 1 459 ? 113.676 135.466 137.867 1.00 42.45  ? 434  MET A CE  1 
ATOM   2814  N  N   . TYR A 1 460 ? 117.681 139.525 139.605 1.00 43.98  ? 435  TYR A N   1 
ATOM   2815  C  CA  . TYR A 1 460 ? 118.889 140.316 139.368 1.00 42.70  ? 435  TYR A CA  1 
ATOM   2816  C  C   . TYR A 1 460 ? 119.775 140.361 140.612 1.00 45.37  ? 435  TYR A C   1 
ATOM   2817  O  O   . TYR A 1 460 ? 120.040 141.416 141.186 1.00 44.03  ? 435  TYR A O   1 
ATOM   2818  C  CB  . TYR A 1 460 ? 118.517 141.719 138.899 1.00 39.47  ? 435  TYR A CB  1 
ATOM   2819  C  CG  . TYR A 1 460 ? 117.902 141.736 137.523 1.00 39.46  ? 435  TYR A CG  1 
ATOM   2820  C  CD1 . TYR A 1 460 ? 118.685 141.554 136.395 1.00 42.98  ? 435  TYR A CD1 1 
ATOM   2821  C  CD2 . TYR A 1 460 ? 116.540 141.919 137.351 1.00 45.73  ? 435  TYR A CD2 1 
ATOM   2822  C  CE1 . TYR A 1 460 ? 118.133 141.561 135.137 1.00 40.49  ? 435  TYR A CE1 1 
ATOM   2823  C  CE2 . TYR A 1 460 ? 115.977 141.928 136.094 1.00 45.92  ? 435  TYR A CE2 1 
ATOM   2824  C  CZ  . TYR A 1 460 ? 116.780 141.748 134.992 1.00 42.93  ? 435  TYR A CZ  1 
ATOM   2825  O  OH  . TYR A 1 460 ? 116.229 141.755 133.736 1.00 52.01  ? 435  TYR A OH  1 
ATOM   2826  N  N   . THR A 1 461 ? 120.238 139.184 141.025 1.00 36.56  ? 436  THR A N   1 
ATOM   2827  C  CA  . THR A 1 461 ? 121.258 139.085 142.059 1.00 38.77  ? 436  THR A CA  1 
ATOM   2828  C  C   . THR A 1 461 ? 122.030 137.791 141.855 1.00 41.66  ? 436  THR A C   1 
ATOM   2829  O  O   . THR A 1 461 ? 121.440 136.744 141.574 1.00 47.19  ? 436  THR A O   1 
ATOM   2830  C  CB  . THR A 1 461 ? 120.661 139.138 143.472 1.00 36.84  ? 436  THR A CB  1 
ATOM   2831  O  OG1 . THR A 1 461 ? 121.689 138.875 144.435 1.00 44.57  ? 436  THR A OG1 1 
ATOM   2832  C  CG2 . THR A 1 461 ? 119.558 138.116 143.636 1.00 36.85  ? 436  THR A CG2 1 
ATOM   2833  N  N   . ASP A 1 462 ? 123.352 137.874 141.976 1.00 41.79  ? 437  ASP A N   1 
ATOM   2834  C  CA  . ASP A 1 462 ? 124.212 136.708 141.811 1.00 44.04  ? 437  ASP A CA  1 
ATOM   2835  C  C   . ASP A 1 462 ? 124.224 135.927 143.118 1.00 51.98  ? 437  ASP A C   1 
ATOM   2836  O  O   . ASP A 1 462 ? 124.742 136.406 144.131 1.00 56.93  ? 437  ASP A O   1 
ATOM   2837  C  CB  . ASP A 1 462 ? 125.620 137.131 141.408 1.00 43.51  ? 437  ASP A CB  1 
ATOM   2838  C  CG  . ASP A 1 462 ? 126.416 135.997 140.794 1.00 51.47  ? 437  ASP A CG  1 
ATOM   2839  O  OD1 . ASP A 1 462 ? 125.945 134.842 140.842 1.00 51.00  ? 437  ASP A OD1 1 
ATOM   2840  O  OD2 . ASP A 1 462 ? 127.516 136.259 140.263 1.00 55.80  ? 437  ASP A OD2 1 
ATOM   2841  N  N   . TRP A 1 463 ? 123.655 134.722 143.100 1.00 46.62  ? 438  TRP A N   1 
ATOM   2842  C  CA  . TRP A 1 463 ? 123.539 133.931 144.316 1.00 41.10  ? 438  TRP A CA  1 
ATOM   2843  C  C   . TRP A 1 463 ? 124.822 133.194 144.675 1.00 47.06  ? 438  TRP A C   1 
ATOM   2844  O  O   . TRP A 1 463 ? 124.909 132.643 145.777 1.00 54.57  ? 438  TRP A O   1 
ATOM   2845  C  CB  . TRP A 1 463 ? 122.384 132.938 144.186 1.00 43.72  ? 438  TRP A CB  1 
ATOM   2846  C  CG  . TRP A 1 463 ? 121.044 133.603 144.188 1.00 41.36  ? 438  TRP A CG  1 
ATOM   2847  C  CD1 . TRP A 1 463 ? 120.187 133.721 143.136 1.00 43.01  ? 438  TRP A CD1 1 
ATOM   2848  C  CD2 . TRP A 1 463 ? 120.413 134.255 145.295 1.00 43.08  ? 438  TRP A CD2 1 
ATOM   2849  N  NE1 . TRP A 1 463 ? 119.058 134.401 143.520 1.00 46.14  ? 438  TRP A NE1 1 
ATOM   2850  C  CE2 . TRP A 1 463 ? 119.172 134.739 144.843 1.00 41.51  ? 438  TRP A CE2 1 
ATOM   2851  C  CE3 . TRP A 1 463 ? 120.775 134.472 146.627 1.00 48.62  ? 438  TRP A CE3 1 
ATOM   2852  C  CZ2 . TRP A 1 463 ? 118.293 135.428 145.673 1.00 40.76  ? 438  TRP A CZ2 1 
ATOM   2853  C  CZ3 . TRP A 1 463 ? 119.900 135.156 147.449 1.00 46.44  ? 438  TRP A CZ3 1 
ATOM   2854  C  CH2 . TRP A 1 463 ? 118.674 135.626 146.969 1.00 40.64  ? 438  TRP A CH2 1 
ATOM   2855  N  N   . ALA A 1 464 ? 125.810 133.166 143.783 1.00 49.18  ? 439  ALA A N   1 
ATOM   2856  C  CA  . ALA A 1 464 ? 127.130 132.661 144.128 1.00 52.68  ? 439  ALA A CA  1 
ATOM   2857  C  C   . ALA A 1 464 ? 128.008 133.717 144.784 1.00 53.23  ? 439  ALA A C   1 
ATOM   2858  O  O   . ALA A 1 464 ? 129.051 133.372 145.350 1.00 54.34  ? 439  ALA A O   1 
ATOM   2859  C  CB  . ALA A 1 464 ? 127.832 132.113 142.882 1.00 51.24  ? 439  ALA A CB  1 
ATOM   2860  N  N   . ASP A 1 465 ? 127.610 134.985 144.721 1.00 51.13  ? 440  ASP A N   1 
ATOM   2861  C  CA  . ASP A 1 465 ? 128.296 136.109 145.352 1.00 48.89  ? 440  ASP A CA  1 
ATOM   2862  C  C   . ASP A 1 465 ? 127.282 137.001 146.055 1.00 53.50  ? 440  ASP A C   1 
ATOM   2863  O  O   . ASP A 1 465 ? 127.259 138.221 145.881 1.00 58.57  ? 440  ASP A O   1 
ATOM   2864  C  CB  . ASP A 1 465 ? 129.105 136.903 144.331 1.00 53.02  ? 440  ASP A CB  1 
ATOM   2865  C  CG  . ASP A 1 465 ? 130.221 136.088 143.710 1.00 57.48  ? 440  ASP A CG  1 
ATOM   2866  O  OD1 . ASP A 1 465 ? 130.898 135.344 144.449 1.00 58.77  ? 440  ASP A OD1 1 
ATOM   2867  O  OD2 . ASP A 1 465 ? 130.421 136.190 142.481 1.00 58.28  ? 440  ASP A OD2 1 
ATOM   2868  N  N   . ARG A 1 466 ? 126.416 136.375 146.857 1.00 51.12  ? 441  ARG A N   1 
ATOM   2869  C  CA  . ARG A 1 466 ? 125.255 137.062 147.420 1.00 49.35  ? 441  ARG A CA  1 
ATOM   2870  C  C   . ARG A 1 466 ? 125.642 138.307 148.210 1.00 51.82  ? 441  ARG A C   1 
ATOM   2871  O  O   . ARG A 1 466 ? 124.879 139.279 148.243 1.00 53.54  ? 441  ARG A O   1 
ATOM   2872  C  CB  . ARG A 1 466 ? 124.469 136.093 148.303 1.00 50.34  ? 441  ARG A CB  1 
ATOM   2873  C  CG  . ARG A 1 466 ? 123.243 136.688 148.970 1.00 52.35  ? 441  ARG A CG  1 
ATOM   2874  C  CD  . ARG A 1 466 ? 122.558 135.658 149.851 1.00 52.42  ? 441  ARG A CD  1 
ATOM   2875  N  NE  . ARG A 1 466 ? 122.716 134.307 149.324 1.00 53.21  ? 441  ARG A NE  1 
ATOM   2876  C  CZ  . ARG A 1 466 ? 121.972 133.270 149.683 1.00 54.38  ? 441  ARG A CZ  1 
ATOM   2877  N  NH1 . ARG A 1 466 ? 121.002 133.391 150.575 1.00 54.43  ? 441  ARG A NH1 1 
ATOM   2878  N  NH2 . ARG A 1 466 ? 122.206 132.082 149.133 1.00 50.68  ? 441  ARG A NH2 1 
ATOM   2879  N  N   . ASP A 1 467 ? 126.816 138.308 148.838 1.00 57.34  ? 442  ASP A N   1 
ATOM   2880  C  CA  . ASP A 1 467 ? 127.234 139.449 149.643 1.00 55.62  ? 442  ASP A CA  1 
ATOM   2881  C  C   . ASP A 1 467 ? 128.510 140.070 149.090 1.00 61.22  ? 442  ASP A C   1 
ATOM   2882  O  O   . ASP A 1 467 ? 129.440 140.369 149.845 1.00 66.13  ? 442  ASP A O   1 
ATOM   2883  C  CB  . ASP A 1 467 ? 127.437 139.029 151.100 1.00 54.11  ? 442  ASP A CB  1 
ATOM   2884  N  N   . ASN A 1 468 ? 128.562 140.266 147.770 1.00 59.84  ? 443  ASN A N   1 
ATOM   2885  C  CA  . ASN A 1 468 ? 129.760 140.817 147.146 1.00 56.31  ? 443  ASN A CA  1 
ATOM   2886  C  C   . ASN A 1 468 ? 129.772 142.340 147.185 1.00 59.03  ? 443  ASN A C   1 
ATOM   2887  O  O   . ASN A 1 468 ? 130.799 142.945 147.509 1.00 65.79  ? 443  ASN A O   1 
ATOM   2888  C  CB  . ASN A 1 468 ? 129.872 140.323 145.704 1.00 58.47  ? 443  ASN A CB  1 
ATOM   2889  C  CG  . ASN A 1 468 ? 131.294 140.367 145.180 1.00 62.63  ? 443  ASN A CG  1 
ATOM   2890  O  OD1 . ASN A 1 468 ? 132.033 141.317 145.435 1.00 64.77  ? 443  ASN A OD1 1 
ATOM   2891  N  ND2 . ASN A 1 468 ? 131.684 139.335 144.443 1.00 64.96  ? 443  ASN A ND2 1 
ATOM   2892  N  N   . GLY A 1 469 ? 128.648 142.974 146.865 1.00 55.38  ? 444  GLY A N   1 
ATOM   2893  C  CA  . GLY A 1 469 ? 128.601 144.421 146.781 1.00 58.35  ? 444  GLY A CA  1 
ATOM   2894  C  C   . GLY A 1 469 ? 128.839 144.933 145.376 1.00 61.60  ? 444  GLY A C   1 
ATOM   2895  O  O   . GLY A 1 469 ? 127.962 145.573 144.788 1.00 66.13  ? 444  GLY A O   1 
ATOM   2896  N  N   . GLU A 1 470 ? 130.026 144.662 144.827 1.00 62.57  ? 445  GLU A N   1 
ATOM   2897  C  CA  . GLU A 1 470 ? 130.313 145.051 143.449 1.00 61.36  ? 445  GLU A CA  1 
ATOM   2898  C  C   . GLU A 1 470 ? 129.380 144.341 142.475 1.00 63.05  ? 445  GLU A C   1 
ATOM   2899  O  O   . GLU A 1 470 ? 128.869 144.955 141.525 1.00 67.13  ? 445  GLU A O   1 
ATOM   2900  C  CB  . GLU A 1 470 ? 131.773 144.749 143.116 1.00 57.33  ? 445  GLU A CB  1 
ATOM   2901  C  CG  . GLU A 1 470 ? 132.350 145.602 142.002 1.00 63.17  ? 445  GLU A CG  1 
ATOM   2902  C  CD  . GLU A 1 470 ? 132.150 144.988 140.631 1.00 67.25  ? 445  GLU A CD  1 
ATOM   2903  O  OE1 . GLU A 1 470 ? 131.818 143.786 140.559 1.00 69.04  ? 445  GLU A OE1 1 
ATOM   2904  O  OE2 . GLU A 1 470 ? 132.328 145.706 139.626 1.00 65.97  ? 445  GLU A OE2 1 
ATOM   2905  N  N   . MET A 1 471 ? 129.135 143.050 142.699 1.00 53.76  ? 446  MET A N   1 
ATOM   2906  C  CA  . MET A 1 471 ? 128.159 142.339 141.887 1.00 54.56  ? 446  MET A CA  1 
ATOM   2907  C  C   . MET A 1 471 ? 126.776 142.575 142.483 1.00 59.73  ? 446  MET A C   1 
ATOM   2908  O  O   . MET A 1 471 ? 125.988 141.642 142.671 1.00 61.04  ? 446  MET A O   1 
ATOM   2909  C  CB  . MET A 1 471 ? 128.500 140.848 141.818 1.00 57.70  ? 446  MET A CB  1 
ATOM   2910  C  CG  . MET A 1 471 ? 127.715 140.058 140.780 1.00 62.68  ? 446  MET A CG  1 
ATOM   2911  S  SD  . MET A 1 471 ? 128.466 140.135 139.145 1.00 74.00  ? 446  MET A SD  1 
ATOM   2912  C  CE  . MET A 1 471 ? 130.095 139.484 139.498 1.00 61.05  ? 446  MET A CE  1 
ATOM   2913  N  N   . ARG A 1 472 ? 126.493 143.835 142.805 1.00 47.74  ? 447  ARG A N   1 
ATOM   2914  C  CA  . ARG A 1 472 ? 125.138 144.325 142.998 1.00 43.37  ? 447  ARG A CA  1 
ATOM   2915  C  C   . ARG A 1 472 ? 125.019 145.612 142.197 1.00 51.26  ? 447  ARG A C   1 
ATOM   2916  O  O   . ARG A 1 472 ? 123.976 145.892 141.601 1.00 62.89  ? 447  ARG A O   1 
ATOM   2917  C  CB  . ARG A 1 472 ? 124.827 144.545 144.477 1.00 47.26  ? 447  ARG A CB  1 
ATOM   2918  C  CG  . ARG A 1 472 ? 124.275 143.313 145.172 1.00 53.30  ? 447  ARG A CG  1 
ATOM   2919  C  CD  . ARG A 1 472 ? 123.802 143.629 146.579 1.00 56.43  ? 447  ARG A CD  1 
ATOM   2920  N  NE  . ARG A 1 472 ? 124.889 144.092 147.432 1.00 54.87  ? 447  ARG A NE  1 
ATOM   2921  C  CZ  . ARG A 1 472 ? 124.944 143.899 148.742 1.00 56.55  ? 447  ARG A CZ  1 
ATOM   2922  N  NH1 . ARG A 1 472 ? 123.990 143.244 149.383 1.00 55.90  ? 447  ARG A NH1 1 
ATOM   2923  N  NH2 . ARG A 1 472 ? 125.981 144.374 149.425 1.00 55.08  ? 447  ARG A NH2 1 
ATOM   2924  N  N   . ARG A 1 473 ? 126.117 146.367 142.132 1.00 51.74  ? 448  ARG A N   1 
ATOM   2925  C  CA  . ARG A 1 473 ? 126.213 147.456 141.167 1.00 48.02  ? 448  ARG A CA  1 
ATOM   2926  C  C   . ARG A 1 473 ? 126.144 146.920 139.746 1.00 47.89  ? 448  ARG A C   1 
ATOM   2927  O  O   . ARG A 1 473 ? 125.424 147.465 138.896 1.00 54.35  ? 448  ARG A O   1 
ATOM   2928  C  CB  . ARG A 1 473 ? 127.516 148.226 141.382 1.00 45.07  ? 448  ARG A CB  1 
ATOM   2929  C  CG  . ARG A 1 473 ? 127.566 149.583 140.713 1.00 53.68  ? 448  ARG A CG  1 
ATOM   2930  C  CD  . ARG A 1 473 ? 128.809 150.347 141.136 1.00 58.44  ? 448  ARG A CD  1 
ATOM   2931  N  NE  . ARG A 1 473 ? 130.013 149.534 141.020 1.00 57.96  ? 448  ARG A NE  1 
ATOM   2932  C  CZ  . ARG A 1 473 ? 131.125 149.738 141.713 1.00 59.92  ? 448  ARG A CZ  1 
ATOM   2933  N  NH1 . ARG A 1 473 ? 131.219 150.719 142.596 1.00 58.07  ? 448  ARG A NH1 1 
ATOM   2934  N  NH2 . ARG A 1 473 ? 132.169 148.938 141.516 1.00 58.99  ? 448  ARG A NH2 1 
ATOM   2935  N  N   . LYS A 1 474 ? 126.875 145.834 139.477 1.00 45.28  ? 449  LYS A N   1 
ATOM   2936  C  CA  . LYS A 1 474 ? 126.824 145.228 138.151 1.00 42.53  ? 449  LYS A CA  1 
ATOM   2937  C  C   . LYS A 1 474 ? 125.413 144.760 137.816 1.00 43.12  ? 449  LYS A C   1 
ATOM   2938  O  O   . LYS A 1 474 ? 124.938 144.955 136.691 1.00 50.03  ? 449  LYS A O   1 
ATOM   2939  C  CB  . LYS A 1 474 ? 127.808 144.063 138.065 1.00 46.41  ? 449  LYS A CB  1 
ATOM   2940  C  CG  . LYS A 1 474 ? 129.265 144.481 137.955 1.00 50.55  ? 449  LYS A CG  1 
ATOM   2941  C  CD  . LYS A 1 474 ? 129.480 145.455 136.811 1.00 50.99  ? 449  LYS A CD  1 
ATOM   2942  C  CE  . LYS A 1 474 ? 130.958 145.621 136.506 1.00 52.41  ? 449  LYS A CE  1 
ATOM   2943  N  NZ  . LYS A 1 474 ? 131.609 144.313 136.222 1.00 55.28  ? 449  LYS A NZ  1 
ATOM   2944  N  N   . THR A 1 475 ? 124.717 144.162 138.786 1.00 38.81  ? 450  THR A N   1 
ATOM   2945  C  CA  . THR A 1 475 ? 123.377 143.654 138.512 1.00 32.12  ? 450  THR A CA  1 
ATOM   2946  C  C   . THR A 1 475 ? 122.356 144.778 138.380 1.00 34.66  ? 450  THR A C   1 
ATOM   2947  O  O   . THR A 1 475 ? 121.404 144.645 137.612 1.00 47.21  ? 450  THR A O   1 
ATOM   2948  C  CB  . THR A 1 475 ? 122.940 142.673 139.597 1.00 38.18  ? 450  THR A CB  1 
ATOM   2949  O  OG1 . THR A 1 475 ? 123.065 143.290 140.881 1.00 44.37  ? 450  THR A OG1 1 
ATOM   2950  C  CG2 . THR A 1 475 ? 123.800 141.422 139.554 1.00 37.37  ? 450  THR A CG2 1 
ATOM   2951  N  N   . LEU A 1 476 ? 122.526 145.884 139.109 1.00 30.80  ? 451  LEU A N   1 
ATOM   2952  C  CA  . LEU A 1 476 ? 121.647 147.034 138.909 1.00 30.84  ? 451  LEU A CA  1 
ATOM   2953  C  C   . LEU A 1 476 ? 121.825 147.622 137.514 1.00 33.79  ? 451  LEU A C   1 
ATOM   2954  O  O   . LEU A 1 476 ? 120.841 147.955 136.833 1.00 37.87  ? 451  LEU A O   1 
ATOM   2955  C  CB  . LEU A 1 476 ? 121.926 148.096 139.971 1.00 31.91  ? 451  LEU A CB  1 
ATOM   2956  C  CG  . LEU A 1 476 ? 121.173 147.976 141.292 1.00 31.03  ? 451  LEU A CG  1 
ATOM   2957  C  CD1 . LEU A 1 476 ? 121.567 149.105 142.225 1.00 32.15  ? 451  LEU A CD1 1 
ATOM   2958  C  CD2 . LEU A 1 476 ? 119.678 147.976 141.047 1.00 42.74  ? 451  LEU A CD2 1 
ATOM   2959  N  N   . LEU A 1 477 ? 123.078 147.756 137.072 1.00 32.60  ? 452  LEU A N   1 
ATOM   2960  C  CA  . LEU A 1 477 ? 123.335 148.223 135.715 1.00 28.49  ? 452  LEU A CA  1 
ATOM   2961  C  C   . LEU A 1 477 ? 122.724 147.277 134.689 1.00 28.58  ? 452  LEU A C   1 
ATOM   2962  O  O   . LEU A 1 477 ? 122.098 147.719 133.715 1.00 39.67  ? 452  LEU A O   1 
ATOM   2963  C  CB  . LEU A 1 477 ? 124.841 148.364 135.501 1.00 25.66  ? 452  LEU A CB  1 
ATOM   2964  C  CG  . LEU A 1 477 ? 125.368 148.877 134.165 1.00 29.38  ? 452  LEU A CG  1 
ATOM   2965  C  CD1 . LEU A 1 477 ? 126.538 149.809 134.400 1.00 32.59  ? 452  LEU A CD1 1 
ATOM   2966  C  CD2 . LEU A 1 477 ? 125.793 147.711 133.297 1.00 37.53  ? 452  LEU A CD2 1 
ATOM   2967  N  N   . ALA A 1 478 ? 122.879 145.968 134.906 1.00 25.99  ? 453  ALA A N   1 
ATOM   2968  C  CA  . ALA A 1 478 ? 122.290 144.986 134.003 1.00 28.91  ? 453  ALA A CA  1 
ATOM   2969  C  C   . ALA A 1 478 ? 120.770 145.073 134.003 1.00 31.37  ? 453  ALA A C   1 
ATOM   2970  O  O   . ALA A 1 478 ? 120.137 144.910 132.959 1.00 43.48  ? 453  ALA A O   1 
ATOM   2971  C  CB  . ALA A 1 478 ? 122.746 143.580 134.386 1.00 30.69  ? 453  ALA A CB  1 
ATOM   2972  N  N   . LEU A 1 479 ? 120.168 145.323 135.166 1.00 33.64  ? 454  LEU A N   1 
ATOM   2973  C  CA  . LEU A 1 479 ? 118.715 145.438 135.254 1.00 33.41  ? 454  LEU A CA  1 
ATOM   2974  C  C   . LEU A 1 479 ? 118.209 146.612 134.429 1.00 28.93  ? 454  LEU A C   1 
ATOM   2975  O  O   . LEU A 1 479 ? 117.261 146.475 133.642 1.00 35.31  ? 454  LEU A O   1 
ATOM   2976  C  CB  . LEU A 1 479 ? 118.302 145.586 136.720 1.00 30.71  ? 454  LEU A CB  1 
ATOM   2977  C  CG  . LEU A 1 479 ? 117.020 146.338 137.084 1.00 25.11  ? 454  LEU A CG  1 
ATOM   2978  C  CD1 . LEU A 1 479 ? 115.789 145.643 136.535 1.00 33.80  ? 454  LEU A CD1 1 
ATOM   2979  C  CD2 . LEU A 1 479 ? 116.914 146.503 138.591 1.00 30.45  ? 454  LEU A CD2 1 
ATOM   2980  N  N   . PHE A 1 480 ? 118.835 147.780 134.592 1.00 34.92  ? 455  PHE A N   1 
ATOM   2981  C  CA  . PHE A 1 480 ? 118.393 148.939 133.821 1.00 33.15  ? 455  PHE A CA  1 
ATOM   2982  C  C   . PHE A 1 480 ? 118.604 148.722 132.328 1.00 37.69  ? 455  PHE A C   1 
ATOM   2983  O  O   . PHE A 1 480 ? 117.720 149.028 131.516 1.00 45.88  ? 455  PHE A O   1 
ATOM   2984  C  CB  . PHE A 1 480 ? 119.113 150.203 134.277 1.00 31.13  ? 455  PHE A CB  1 
ATOM   2985  C  CG  . PHE A 1 480 ? 118.403 151.466 133.893 1.00 31.29  ? 455  PHE A CG  1 
ATOM   2986  C  CD1 . PHE A 1 480 ? 117.076 151.656 134.233 1.00 35.13  ? 455  PHE A CD1 1 
ATOM   2987  C  CD2 . PHE A 1 480 ? 119.053 152.453 133.175 1.00 38.58  ? 455  PHE A CD2 1 
ATOM   2988  C  CE1 . PHE A 1 480 ? 116.415 152.814 133.878 1.00 43.30  ? 455  PHE A CE1 1 
ATOM   2989  C  CE2 . PHE A 1 480 ? 118.397 153.612 132.818 1.00 39.16  ? 455  PHE A CE2 1 
ATOM   2990  C  CZ  . PHE A 1 480 ? 117.077 153.793 133.169 1.00 37.08  ? 455  PHE A CZ  1 
ATOM   2991  N  N   . THR A 1 481 ? 119.766 148.180 131.947 1.00 34.33  ? 456  THR A N   1 
ATOM   2992  C  CA  . THR A 1 481 ? 120.033 147.927 130.535 1.00 26.42  ? 456  THR A CA  1 
ATOM   2993  C  C   . THR A 1 481 ? 119.036 146.931 129.953 1.00 34.50  ? 456  THR A C   1 
ATOM   2994  O  O   . THR A 1 481 ? 118.537 147.120 128.838 1.00 42.48  ? 456  THR A O   1 
ATOM   2995  C  CB  . THR A 1 481 ? 121.464 147.423 130.358 1.00 31.71  ? 456  THR A CB  1 
ATOM   2996  O  OG1 . THR A 1 481 ? 122.379 148.506 130.565 1.00 40.95  ? 456  THR A OG1 1 
ATOM   2997  C  CG2 . THR A 1 481 ? 121.670 146.860 128.965 1.00 34.34  ? 456  THR A CG2 1 
ATOM   2998  N  N   . ASP A 1 482 ? 118.726 145.870 130.700 1.00 34.63  ? 457  ASP A N   1 
ATOM   2999  C  CA  . ASP A 1 482 ? 117.795 144.859 130.218 1.00 28.14  ? 457  ASP A CA  1 
ATOM   3000  C  C   . ASP A 1 482 ? 116.397 145.430 130.042 1.00 32.43  ? 457  ASP A C   1 
ATOM   3001  O  O   . ASP A 1 482 ? 115.730 145.144 129.043 1.00 46.97  ? 457  ASP A O   1 
ATOM   3002  C  CB  . ASP A 1 482 ? 117.766 143.674 131.182 1.00 36.96  ? 457  ASP A CB  1 
ATOM   3003  C  CG  . ASP A 1 482 ? 118.839 142.651 130.879 1.00 45.73  ? 457  ASP A CG  1 
ATOM   3004  O  OD1 . ASP A 1 482 ? 118.898 142.173 129.728 1.00 49.54  ? 457  ASP A OD1 1 
ATOM   3005  O  OD2 . ASP A 1 482 ? 119.625 142.323 131.791 1.00 42.16  ? 457  ASP A OD2 1 
ATOM   3006  N  N   . HIS A 1 483 ? 115.927 146.236 130.997 1.00 39.11  ? 458  HIS A N   1 
ATOM   3007  C  CA  . HIS A 1 483 ? 114.560 146.731 130.876 1.00 43.00  ? 458  HIS A CA  1 
ATOM   3008  C  C   . HIS A 1 483 ? 114.439 147.786 129.786 1.00 52.59  ? 458  HIS A C   1 
ATOM   3009  O  O   . HIS A 1 483 ? 113.495 147.752 128.989 1.00 59.57  ? 458  HIS A O   1 
ATOM   3010  C  CB  . HIS A 1 483 ? 114.054 147.297 132.198 1.00 50.08  ? 458  HIS A CB  1 
ATOM   3011  C  CG  . HIS A 1 483 ? 112.597 147.636 132.171 1.00 47.06  ? 458  HIS A CG  1 
ATOM   3012  N  ND1 . HIS A 1 483 ? 112.053 148.673 132.896 1.00 46.94  ? 458  HIS A ND1 1 
ATOM   3013  C  CD2 . HIS A 1 483 ? 111.568 147.072 131.496 1.00 49.52  ? 458  HIS A CD2 1 
ATOM   3014  C  CE1 . HIS A 1 483 ? 110.753 148.730 132.673 1.00 49.16  ? 458  HIS A CE1 1 
ATOM   3015  N  NE2 . HIS A 1 483 ? 110.433 147.769 131.826 1.00 47.86  ? 458  HIS A NE2 1 
ATOM   3016  N  N   . GLN A 1 484 ? 115.376 148.733 129.730 1.00 56.24  ? 459  GLN A N   1 
ATOM   3017  C  CA  . GLN A 1 484 ? 115.177 149.880 128.852 1.00 44.29  ? 459  GLN A CA  1 
ATOM   3018  C  C   . GLN A 1 484 ? 115.636 149.639 127.419 1.00 47.75  ? 459  GLN A C   1 
ATOM   3019  O  O   . GLN A 1 484 ? 114.952 150.058 126.480 1.00 52.61  ? 459  GLN A O   1 
ATOM   3020  C  CB  . GLN A 1 484 ? 115.889 151.107 129.423 1.00 44.56  ? 459  GLN A CB  1 
ATOM   3021  C  CG  . GLN A 1 484 ? 115.271 151.640 130.703 1.00 49.09  ? 459  GLN A CG  1 
ATOM   3022  C  CD  . GLN A 1 484 ? 113.840 152.106 130.512 1.00 51.83  ? 459  GLN A CD  1 
ATOM   3023  O  OE1 . GLN A 1 484 ? 113.417 152.418 129.401 1.00 56.97  ? 459  GLN A OE1 1 
ATOM   3024  N  NE2 . GLN A 1 484 ? 113.087 152.156 131.601 1.00 53.29  ? 459  GLN A NE2 1 
ATOM   3025  N  N   . TRP A 1 485 ? 116.771 148.977 127.218 1.00 34.12  ? 460  TRP A N   1 
ATOM   3026  C  CA  . TRP A 1 485 ? 117.382 148.906 125.896 1.00 22.51  ? 460  TRP A CA  1 
ATOM   3027  C  C   . TRP A 1 485 ? 117.393 147.516 125.282 1.00 22.21  ? 460  TRP A C   1 
ATOM   3028  O  O   . TRP A 1 485 ? 117.179 147.387 124.077 1.00 31.52  ? 460  TRP A O   1 
ATOM   3029  C  CB  . TRP A 1 485 ? 118.818 149.433 125.954 1.00 22.38  ? 460  TRP A CB  1 
ATOM   3030  C  CG  . TRP A 1 485 ? 118.897 150.922 126.022 1.00 28.27  ? 460  TRP A CG  1 
ATOM   3031  C  CD1 . TRP A 1 485 ? 118.702 151.799 124.998 1.00 36.69  ? 460  TRP A CD1 1 
ATOM   3032  C  CD2 . TRP A 1 485 ? 119.193 151.713 127.177 1.00 23.35  ? 460  TRP A CD2 1 
ATOM   3033  N  NE1 . TRP A 1 485 ? 118.859 153.087 125.443 1.00 28.97  ? 460  TRP A NE1 1 
ATOM   3034  C  CE2 . TRP A 1 485 ? 119.160 153.061 126.779 1.00 28.99  ? 460  TRP A CE2 1 
ATOM   3035  C  CE3 . TRP A 1 485 ? 119.482 151.412 128.510 1.00 30.32  ? 460  TRP A CE3 1 
ATOM   3036  C  CZ2 . TRP A 1 485 ? 119.407 154.105 127.663 1.00 33.41  ? 460  TRP A CZ2 1 
ATOM   3037  C  CZ3 . TRP A 1 485 ? 119.725 152.449 129.385 1.00 29.92  ? 460  TRP A CZ3 1 
ATOM   3038  C  CH2 . TRP A 1 485 ? 119.685 153.779 128.960 1.00 27.46  ? 460  TRP A CH2 1 
ATOM   3039  N  N   . VAL A 1 486 ? 117.637 146.468 126.066 1.00 16.91  ? 461  VAL A N   1 
ATOM   3040  C  CA  . VAL A 1 486 ? 117.820 145.143 125.481 1.00 19.71  ? 461  VAL A CA  1 
ATOM   3041  C  C   . VAL A 1 486 ? 116.478 144.493 125.169 1.00 27.86  ? 461  VAL A C   1 
ATOM   3042  O  O   . VAL A 1 486 ? 116.263 143.991 124.060 1.00 38.96  ? 461  VAL A O   1 
ATOM   3043  C  CB  . VAL A 1 486 ? 118.673 144.261 126.411 1.00 23.77  ? 461  VAL A CB  1 
ATOM   3044  C  CG1 . VAL A 1 486 ? 118.592 142.809 125.982 1.00 15.02  ? 461  VAL A CG1 1 
ATOM   3045  C  CG2 . VAL A 1 486 ? 120.113 144.733 126.404 1.00 29.64  ? 461  VAL A CG2 1 
ATOM   3046  N  N   . ALA A 1 487 ? 115.562 144.481 126.137 1.00 33.43  ? 462  ALA A N   1 
ATOM   3047  C  CA  . ALA A 1 487 ? 114.266 143.844 125.911 1.00 23.10  ? 462  ALA A CA  1 
ATOM   3048  C  C   . ALA A 1 487 ? 113.461 144.509 124.801 1.00 30.81  ? 462  ALA A C   1 
ATOM   3049  O  O   . ALA A 1 487 ? 112.920 143.784 123.948 1.00 40.50  ? 462  ALA A O   1 
ATOM   3050  C  CB  . ALA A 1 487 ? 113.478 143.788 127.223 1.00 24.34  ? 462  ALA A CB  1 
ATOM   3051  N  N   . PRO A 1 488 ? 113.309 145.841 124.751 1.00 23.98  ? 463  PRO A N   1 
ATOM   3052  C  CA  . PRO A 1 488 ? 112.606 146.432 123.599 1.00 19.38  ? 463  PRO A CA  1 
ATOM   3053  C  C   . PRO A 1 488 ? 113.283 146.154 122.269 1.00 27.26  ? 463  PRO A C   1 
ATOM   3054  O  O   . PRO A 1 488 ? 112.596 145.938 121.263 1.00 34.21  ? 463  PRO A O   1 
ATOM   3055  C  CB  . PRO A 1 488 ? 112.598 147.930 123.932 1.00 17.88  ? 463  PRO A CB  1 
ATOM   3056  C  CG  . PRO A 1 488 ? 112.692 147.979 125.406 1.00 20.90  ? 463  PRO A CG  1 
ATOM   3057  C  CD  . PRO A 1 488 ? 113.627 146.868 125.759 1.00 27.92  ? 463  PRO A CD  1 
ATOM   3058  N  N   . ALA A 1 489 ? 114.618 146.149 122.233 1.00 20.55  ? 464  ALA A N   1 
ATOM   3059  C  CA  . ALA A 1 489 ? 115.317 145.868 120.984 1.00 8.57   ? 464  ALA A CA  1 
ATOM   3060  C  C   . ALA A 1 489 ? 115.061 144.442 120.519 1.00 19.44  ? 464  ALA A C   1 
ATOM   3061  O  O   . ALA A 1 489 ? 114.812 144.208 119.331 1.00 33.26  ? 464  ALA A O   1 
ATOM   3062  C  CB  . ALA A 1 489 ? 116.813 146.118 121.146 1.00 9.32   ? 464  ALA A CB  1 
ATOM   3063  N  N   . VAL A 1 490 ? 115.104 143.477 121.439 1.00 15.31  ? 465  VAL A N   1 
ATOM   3064  C  CA  . VAL A 1 490 ? 114.829 142.094 121.066 1.00 9.47   ? 465  VAL A CA  1 
ATOM   3065  C  C   . VAL A 1 490 ? 113.376 141.935 120.639 1.00 22.31  ? 465  VAL A C   1 
ATOM   3066  O  O   . VAL A 1 490 ? 113.074 141.210 119.684 1.00 39.33  ? 465  VAL A O   1 
ATOM   3067  C  CB  . VAL A 1 490 ? 115.193 141.142 122.219 1.00 0.18   ? 465  VAL A CB  1 
ATOM   3068  C  CG1 . VAL A 1 490 ? 114.763 139.727 121.892 1.00 9.30   ? 465  VAL A CG1 1 
ATOM   3069  C  CG2 . VAL A 1 490 ? 116.684 141.185 122.482 1.00 13.75  ? 465  VAL A CG2 1 
ATOM   3070  N  N   . ALA A 1 491 ? 112.454 142.616 121.324 1.00 18.53  ? 466  ALA A N   1 
ATOM   3071  C  CA  . ALA A 1 491 ? 111.045 142.526 120.956 1.00 14.86  ? 466  ALA A CA  1 
ATOM   3072  C  C   . ALA A 1 491 ? 110.807 143.071 119.553 1.00 21.34  ? 466  ALA A C   1 
ATOM   3073  O  O   . ALA A 1 491 ? 110.102 142.455 118.746 1.00 31.40  ? 466  ALA A O   1 
ATOM   3074  C  CB  . ALA A 1 491 ? 110.187 143.269 121.977 1.00 18.96  ? 466  ALA A CB  1 
ATOM   3075  N  N   . THR A 1 492 ? 111.401 144.225 119.237 1.00 17.69  ? 467  THR A N   1 
ATOM   3076  C  CA  . THR A 1 492 ? 111.222 144.794 117.905 1.00 19.20  ? 467  THR A CA  1 
ATOM   3077  C  C   . THR A 1 492 ? 111.925 143.969 116.837 1.00 20.24  ? 467  THR A C   1 
ATOM   3078  O  O   . THR A 1 492 ? 111.413 143.848 115.721 1.00 31.36  ? 467  THR A O   1 
ATOM   3079  C  CB  . THR A 1 492 ? 111.715 146.238 117.865 1.00 17.41  ? 467  THR A CB  1 
ATOM   3080  O  OG1 . THR A 1 492 ? 113.018 146.319 118.454 1.00 30.54  ? 467  THR A OG1 1 
ATOM   3081  C  CG2 . THR A 1 492 ? 110.760 147.137 118.620 1.00 23.23  ? 467  THR A CG2 1 
ATOM   3082  N  N   . ALA A 1 493 ? 113.087 143.393 117.151 1.00 7.19   ? 468  ALA A N   1 
ATOM   3083  C  CA  . ALA A 1 493 ? 113.744 142.515 116.191 1.00 9.45   ? 468  ALA A CA  1 
ATOM   3084  C  C   . ALA A 1 493 ? 112.892 141.287 115.901 1.00 20.98  ? 468  ALA A C   1 
ATOM   3085  O  O   . ALA A 1 493 ? 112.760 140.875 114.743 1.00 33.48  ? 468  ALA A O   1 
ATOM   3086  C  CB  . ALA A 1 493 ? 115.123 142.109 116.707 1.00 9.92   ? 468  ALA A CB  1 
ATOM   3087  N  N   . LYS A 1 494 ? 112.293 140.696 116.938 1.00 22.70  ? 469  LYS A N   1 
ATOM   3088  C  CA  . LYS A 1 494 ? 111.403 139.560 116.726 1.00 23.24  ? 469  LYS A CA  1 
ATOM   3089  C  C   . LYS A 1 494 ? 110.184 139.958 115.905 1.00 30.99  ? 469  LYS A C   1 
ATOM   3090  O  O   . LYS A 1 494 ? 109.770 139.226 115.000 1.00 39.13  ? 469  LYS A O   1 
ATOM   3091  C  CB  . LYS A 1 494 ? 110.970 138.971 118.067 1.00 18.62  ? 469  LYS A CB  1 
ATOM   3092  C  CG  . LYS A 1 494 ? 112.078 138.272 118.830 1.00 29.39  ? 469  LYS A CG  1 
ATOM   3093  C  CD  . LYS A 1 494 ? 111.516 137.354 119.903 1.00 34.32  ? 469  LYS A CD  1 
ATOM   3094  C  CE  . LYS A 1 494 ? 110.363 138.005 120.649 1.00 36.07  ? 469  LYS A CE  1 
ATOM   3095  N  NZ  . LYS A 1 494 ? 109.959 137.215 121.843 1.00 34.35  ? 469  LYS A NZ  1 
ATOM   3096  N  N   . LEU A 1 495 ? 109.597 141.120 116.204 1.00 23.98  ? 470  LEU A N   1 
ATOM   3097  C  CA  . LEU A 1 495 ? 108.410 141.555 115.475 1.00 18.69  ? 470  LEU A CA  1 
ATOM   3098  C  C   . LEU A 1 495 ? 108.728 141.840 114.012 1.00 25.94  ? 470  LEU A C   1 
ATOM   3099  O  O   . LEU A 1 495 ? 107.903 141.577 113.130 1.00 30.81  ? 470  LEU A O   1 
ATOM   3100  C  CB  . LEU A 1 495 ? 107.807 142.788 116.144 1.00 20.17  ? 470  LEU A CB  1 
ATOM   3101  C  CG  . LEU A 1 495 ? 106.584 142.535 117.024 1.00 24.24  ? 470  LEU A CG  1 
ATOM   3102  C  CD1 . LEU A 1 495 ? 105.497 141.842 116.226 1.00 28.42  ? 470  LEU A CD1 1 
ATOM   3103  C  CD2 . LEU A 1 495 ? 106.958 141.716 118.247 1.00 27.30  ? 470  LEU A CD2 1 
ATOM   3104  N  N   . HIS A 1 496 ? 109.915 142.383 113.734 1.00 29.69  ? 471  HIS A N   1 
ATOM   3105  C  CA  . HIS A 1 496 ? 110.291 142.664 112.353 1.00 22.46  ? 471  HIS A CA  1 
ATOM   3106  C  C   . HIS A 1 496 ? 110.641 141.386 111.602 1.00 28.76  ? 471  HIS A C   1 
ATOM   3107  O  O   . HIS A 1 496 ? 110.306 141.246 110.420 1.00 38.36  ? 471  HIS A O   1 
ATOM   3108  C  CB  . HIS A 1 496 ? 111.461 143.646 112.315 1.00 24.32  ? 471  HIS A CB  1 
ATOM   3109  C  CG  . HIS A 1 496 ? 111.045 145.083 112.339 1.00 29.66  ? 471  HIS A CG  1 
ATOM   3110  N  ND1 . HIS A 1 496 ? 110.341 145.636 113.386 1.00 35.70  ? 471  HIS A ND1 1 
ATOM   3111  C  CD2 . HIS A 1 496 ? 111.234 146.080 111.444 1.00 36.07  ? 471  HIS A CD2 1 
ATOM   3112  C  CE1 . HIS A 1 496 ? 110.113 146.913 113.135 1.00 36.05  ? 471  HIS A CE1 1 
ATOM   3113  N  NE2 . HIS A 1 496 ? 110.645 147.208 111.963 1.00 40.54  ? 471  HIS A NE2 1 
ATOM   3114  N  N   . ALA A 1 497 ? 111.313 140.441 112.264 1.00 24.77  ? 472  ALA A N   1 
ATOM   3115  C  CA  . ALA A 1 497 ? 111.685 139.194 111.610 1.00 21.69  ? 472  ALA A CA  1 
ATOM   3116  C  C   . ALA A 1 497 ? 110.515 138.231 111.464 1.00 31.19  ? 472  ALA A C   1 
ATOM   3117  O  O   . ALA A 1 497 ? 110.588 137.313 110.640 1.00 41.07  ? 472  ALA A O   1 
ATOM   3118  C  CB  . ALA A 1 497 ? 112.814 138.512 112.382 1.00 19.80  ? 472  ALA A CB  1 
ATOM   3119  N  N   . ASP A 1 498 ? 109.445 138.414 112.241 1.00 32.27  ? 473  ASP A N   1 
ATOM   3120  C  CA  . ASP A 1 498 ? 108.272 137.562 112.089 1.00 31.55  ? 473  ASP A CA  1 
ATOM   3121  C  C   . ASP A 1 498 ? 107.555 137.823 110.773 1.00 37.89  ? 473  ASP A C   1 
ATOM   3122  O  O   . ASP A 1 498 ? 106.992 136.894 110.182 1.00 43.66  ? 473  ASP A O   1 
ATOM   3123  C  CB  . ASP A 1 498 ? 107.316 137.772 113.262 1.00 29.43  ? 473  ASP A CB  1 
ATOM   3124  C  CG  . ASP A 1 498 ? 107.533 136.771 114.375 1.00 37.56  ? 473  ASP A CG  1 
ATOM   3125  O  OD1 . ASP A 1 498 ? 108.389 135.878 114.213 1.00 41.76  ? 473  ASP A OD1 1 
ATOM   3126  O  OD2 . ASP A 1 498 ? 106.847 136.878 115.413 1.00 40.87  ? 473  ASP A OD2 1 
ATOM   3127  N  N   . TYR A 1 499 ? 107.560 139.070 110.300 1.00 35.72  ? 474  TYR A N   1 
ATOM   3128  C  CA  . TYR A 1 499 ? 106.895 139.439 109.057 1.00 35.24  ? 474  TYR A CA  1 
ATOM   3129  C  C   . TYR A 1 499 ? 107.828 139.379 107.854 1.00 36.55  ? 474  TYR A C   1 
ATOM   3130  O  O   . TYR A 1 499 ? 107.631 140.120 106.882 1.00 40.40  ? 474  TYR A O   1 
ATOM   3131  C  CB  . TYR A 1 499 ? 106.271 140.828 109.189 1.00 31.71  ? 474  TYR A CB  1 
ATOM   3132  C  CG  . TYR A 1 499 ? 105.039 140.844 110.062 1.00 32.56  ? 474  TYR A CG  1 
ATOM   3133  C  CD1 . TYR A 1 499 ? 103.785 140.581 109.531 1.00 38.52  ? 474  TYR A CD1 1 
ATOM   3134  C  CD2 . TYR A 1 499 ? 105.131 141.107 111.420 1.00 37.02  ? 474  TYR A CD2 1 
ATOM   3135  C  CE1 . TYR A 1 499 ? 102.657 140.590 110.327 1.00 40.55  ? 474  TYR A CE1 1 
ATOM   3136  C  CE2 . TYR A 1 499 ? 104.010 141.118 112.223 1.00 40.40  ? 474  TYR A CE2 1 
ATOM   3137  C  CZ  . TYR A 1 499 ? 102.776 140.859 111.672 1.00 40.53  ? 474  TYR A CZ  1 
ATOM   3138  O  OH  . TYR A 1 499 ? 101.656 140.869 112.469 1.00 43.61  ? 474  TYR A OH  1 
ATOM   3139  N  N   . GLN A 1 500 ? 108.844 138.516 107.905 1.00 34.42  ? 475  GLN A N   1 
ATOM   3140  C  CA  . GLN A 1 500 ? 109.710 138.209 106.767 1.00 37.33  ? 475  GLN A CA  1 
ATOM   3141  C  C   . GLN A 1 500 ? 110.399 139.463 106.225 1.00 44.16  ? 475  GLN A C   1 
ATOM   3142  O  O   . GLN A 1 500 ? 110.202 139.873 105.080 1.00 49.37  ? 475  GLN A O   1 
ATOM   3143  C  CB  . GLN A 1 500 ? 108.924 137.487 105.666 1.00 38.86  ? 475  GLN A CB  1 
ATOM   3144  C  CG  . GLN A 1 500 ? 107.927 136.456 106.181 1.00 42.39  ? 475  GLN A CG  1 
ATOM   3145  C  CD  . GLN A 1 500 ? 108.598 135.222 106.752 1.00 47.10  ? 475  GLN A CD  1 
ATOM   3146  O  OE1 . GLN A 1 500 ? 109.795 135.008 106.565 1.00 50.94  ? 475  GLN A OE1 1 
ATOM   3147  N  NE2 . GLN A 1 500 ? 107.826 134.403 107.456 1.00 41.70  ? 475  GLN A NE2 1 
ATOM   3148  N  N   . SER A 1 501 ? 111.219 140.071 107.079 1.00 38.64  ? 476  SER A N   1 
ATOM   3149  C  CA  . SER A 1 501 ? 112.088 141.161 106.673 1.00 38.57  ? 476  SER A CA  1 
ATOM   3150  C  C   . SER A 1 501 ? 113.487 140.918 107.221 1.00 34.57  ? 476  SER A C   1 
ATOM   3151  O  O   . SER A 1 501 ? 113.635 140.405 108.336 1.00 39.61  ? 476  SER A O   1 
ATOM   3152  C  CB  . SER A 1 501 ? 111.557 142.514 107.167 1.00 34.38  ? 476  SER A CB  1 
ATOM   3153  O  OG  . SER A 1 501 ? 111.559 142.580 108.580 1.00 46.16  ? 476  SER A OG  1 
ATOM   3154  N  N   . PRO A 1 502 ? 114.529 141.265 106.465 1.00 27.85  ? 477  PRO A N   1 
ATOM   3155  C  CA  . PRO A 1 502 ? 115.902 140.989 106.918 1.00 32.47  ? 477  PRO A CA  1 
ATOM   3156  C  C   . PRO A 1 502 ? 116.252 141.834 108.134 1.00 37.75  ? 477  PRO A C   1 
ATOM   3157  O  O   . PRO A 1 502 ? 116.193 143.064 108.087 1.00 52.25  ? 477  PRO A O   1 
ATOM   3158  C  CB  . PRO A 1 502 ? 116.761 141.362 105.703 1.00 36.47  ? 477  PRO A CB  1 
ATOM   3159  C  CG  . PRO A 1 502 ? 115.810 141.428 104.547 1.00 34.86  ? 477  PRO A CG  1 
ATOM   3160  C  CD  . PRO A 1 502 ? 114.501 141.856 105.119 1.00 32.37  ? 477  PRO A CD  1 
ATOM   3161  N  N   . VAL A 1 503 ? 116.621 141.167 109.224 1.00 45.12  ? 478  VAL A N   1 
ATOM   3162  C  CA  . VAL A 1 503 ? 117.019 141.828 110.461 1.00 40.86  ? 478  VAL A CA  1 
ATOM   3163  C  C   . VAL A 1 503 ? 118.373 141.281 110.881 1.00 40.57  ? 478  VAL A C   1 
ATOM   3164  O  O   . VAL A 1 503 ? 118.565 140.062 110.931 1.00 55.86  ? 478  VAL A O   1 
ATOM   3165  C  CB  . VAL A 1 503 ? 115.982 141.621 111.580 1.00 38.13  ? 478  VAL A CB  1 
ATOM   3166  C  CG1 . VAL A 1 503 ? 116.524 142.120 112.905 1.00 38.37  ? 478  VAL A CG1 1 
ATOM   3167  C  CG2 . VAL A 1 503 ? 114.687 142.327 111.234 1.00 46.77  ? 478  VAL A CG2 1 
ATOM   3168  N  N   . TYR A 1 504 ? 119.311 142.178 111.175 1.00 39.76  ? 479  TYR A N   1 
ATOM   3169  C  CA  . TYR A 1 504 ? 120.633 141.805 111.658 1.00 41.02  ? 479  TYR A CA  1 
ATOM   3170  C  C   . TYR A 1 504 ? 120.846 142.411 113.038 1.00 47.78  ? 479  TYR A C   1 
ATOM   3171  O  O   . TYR A 1 504 ? 120.722 143.626 113.210 1.00 60.77  ? 479  TYR A O   1 
ATOM   3172  C  CB  . TYR A 1 504 ? 121.723 142.274 110.691 1.00 43.70  ? 479  TYR A CB  1 
ATOM   3173  C  CG  . TYR A 1 504 ? 121.748 141.513 109.386 1.00 37.64  ? 479  TYR A CG  1 
ATOM   3174  C  CD1 . TYR A 1 504 ? 120.861 141.819 108.365 1.00 41.75  ? 479  TYR A CD1 1 
ATOM   3175  C  CD2 . TYR A 1 504 ? 122.656 140.487 109.176 1.00 44.96  ? 479  TYR A CD2 1 
ATOM   3176  C  CE1 . TYR A 1 504 ? 120.879 141.126 107.173 1.00 43.57  ? 479  TYR A CE1 1 
ATOM   3177  C  CE2 . TYR A 1 504 ? 122.680 139.787 107.988 1.00 42.65  ? 479  TYR A CE2 1 
ATOM   3178  C  CZ  . TYR A 1 504 ? 121.790 140.111 106.990 1.00 44.61  ? 479  TYR A CZ  1 
ATOM   3179  O  OH  . TYR A 1 504 ? 121.811 139.417 105.805 1.00 48.59  ? 479  TYR A OH  1 
ATOM   3180  N  N   . PHE A 1 505 ? 121.183 141.570 114.011 1.00 44.98  ? 480  PHE A N   1 
ATOM   3181  C  CA  . PHE A 1 505 ? 121.319 141.983 115.400 1.00 44.06  ? 480  PHE A CA  1 
ATOM   3182  C  C   . PHE A 1 505 ? 122.790 142.030 115.788 1.00 48.74  ? 480  PHE A C   1 
ATOM   3183  O  O   . PHE A 1 505 ? 123.561 141.133 115.436 1.00 59.29  ? 480  PHE A O   1 
ATOM   3184  C  CB  . PHE A 1 505 ? 120.563 141.022 116.322 1.00 50.11  ? 480  PHE A CB  1 
ATOM   3185  C  CG  . PHE A 1 505 ? 120.203 141.608 117.656 1.00 47.57  ? 480  PHE A CG  1 
ATOM   3186  C  CD1 . PHE A 1 505 ? 119.011 142.284 117.830 1.00 49.10  ? 480  PHE A CD1 1 
ATOM   3187  C  CD2 . PHE A 1 505 ? 121.051 141.468 118.740 1.00 50.88  ? 480  PHE A CD2 1 
ATOM   3188  C  CE1 . PHE A 1 505 ? 118.676 142.818 119.056 1.00 52.24  ? 480  PHE A CE1 1 
ATOM   3189  C  CE2 . PHE A 1 505 ? 120.721 142.001 119.968 1.00 48.14  ? 480  PHE A CE2 1 
ATOM   3190  C  CZ  . PHE A 1 505 ? 119.533 142.676 120.126 1.00 48.39  ? 480  PHE A CZ  1 
ATOM   3191  N  N   . TYR A 1 506 ? 123.181 143.081 116.508 1.00 40.74  ? 481  TYR A N   1 
ATOM   3192  C  CA  . TYR A 1 506 ? 124.558 143.206 116.967 1.00 33.99  ? 481  TYR A CA  1 
ATOM   3193  C  C   . TYR A 1 506 ? 124.591 143.644 118.424 1.00 36.50  ? 481  TYR A C   1 
ATOM   3194  O  O   . TYR A 1 506 ? 123.667 144.295 118.923 1.00 50.76  ? 481  TYR A O   1 
ATOM   3195  C  CB  . TYR A 1 506 ? 125.376 144.176 116.088 1.00 41.10  ? 481  TYR A CB  1 
ATOM   3196  C  CG  . TYR A 1 506 ? 125.323 145.644 116.467 1.00 45.66  ? 481  TYR A CG  1 
ATOM   3197  C  CD1 . TYR A 1 506 ? 126.148 146.159 117.460 1.00 49.36  ? 481  TYR A CD1 1 
ATOM   3198  C  CD2 . TYR A 1 506 ? 124.484 146.524 115.799 1.00 41.20  ? 481  TYR A CD2 1 
ATOM   3199  C  CE1 . TYR A 1 506 ? 126.110 147.494 117.800 1.00 45.23  ? 481  TYR A CE1 1 
ATOM   3200  C  CE2 . TYR A 1 506 ? 124.444 147.864 116.132 1.00 35.06  ? 481  TYR A CE2 1 
ATOM   3201  C  CZ  . TYR A 1 506 ? 125.259 148.341 117.134 1.00 40.49  ? 481  TYR A CZ  1 
ATOM   3202  O  OH  . TYR A 1 506 ? 125.227 149.671 117.473 1.00 50.82  ? 481  TYR A OH  1 
ATOM   3203  N  N   . THR A 1 507 ? 125.683 143.289 119.098 1.00 41.46  ? 482  THR A N   1 
ATOM   3204  C  CA  . THR A 1 507 ? 125.884 143.597 120.513 1.00 39.82  ? 482  THR A CA  1 
ATOM   3205  C  C   . THR A 1 507 ? 127.299 144.134 120.697 1.00 45.14  ? 482  THR A C   1 
ATOM   3206  O  O   . THR A 1 507 ? 128.250 143.362 120.842 1.00 54.74  ? 482  THR A O   1 
ATOM   3207  C  CB  . THR A 1 507 ? 125.647 142.369 121.379 1.00 39.95  ? 482  THR A CB  1 
ATOM   3208  O  OG1 . THR A 1 507 ? 124.546 141.621 120.852 1.00 56.35  ? 482  THR A OG1 1 
ATOM   3209  C  CG2 . THR A 1 507 ? 125.330 142.786 122.795 1.00 46.30  ? 482  THR A CG2 1 
ATOM   3210  N  N   . PHE A 1 508 ? 127.429 145.456 120.695 1.00 40.07  ? 483  PHE A N   1 
ATOM   3211  C  CA  . PHE A 1 508 ? 128.726 146.091 120.878 1.00 37.71  ? 483  PHE A CA  1 
ATOM   3212  C  C   . PHE A 1 508 ? 129.229 145.848 122.296 1.00 42.09  ? 483  PHE A C   1 
ATOM   3213  O  O   . PHE A 1 508 ? 128.486 146.018 123.266 1.00 48.78  ? 483  PHE A O   1 
ATOM   3214  C  CB  . PHE A 1 508 ? 128.617 147.587 120.599 1.00 36.36  ? 483  PHE A CB  1 
ATOM   3215  C  CG  . PHE A 1 508 ? 129.843 148.181 119.978 1.00 36.05  ? 483  PHE A CG  1 
ATOM   3216  C  CD1 . PHE A 1 508 ? 130.110 147.995 118.635 1.00 40.10  ? 483  PHE A CD1 1 
ATOM   3217  C  CD2 . PHE A 1 508 ? 130.722 148.935 120.732 1.00 39.29  ? 483  PHE A CD2 1 
ATOM   3218  C  CE1 . PHE A 1 508 ? 131.235 148.540 118.058 1.00 43.91  ? 483  PHE A CE1 1 
ATOM   3219  C  CE2 . PHE A 1 508 ? 131.848 149.484 120.159 1.00 43.37  ? 483  PHE A CE2 1 
ATOM   3220  C  CZ  . PHE A 1 508 ? 132.105 149.286 118.821 1.00 46.75  ? 483  PHE A CZ  1 
ATOM   3221  N  N   . TYR A 1 509 ? 130.491 145.451 122.415 1.00 37.53  ? 484  TYR A N   1 
ATOM   3222  C  CA  . TYR A 1 509 ? 131.088 145.134 123.707 1.00 36.77  ? 484  TYR A CA  1 
ATOM   3223  C  C   . TYR A 1 509 ? 132.343 145.935 124.008 1.00 42.43  ? 484  TYR A C   1 
ATOM   3224  O  O   . TYR A 1 509 ? 132.546 146.341 125.154 1.00 46.69  ? 484  TYR A O   1 
ATOM   3225  C  CB  . TYR A 1 509 ? 131.413 143.637 123.781 1.00 35.82  ? 484  TYR A CB  1 
ATOM   3226  C  CG  . TYR A 1 509 ? 130.353 142.818 124.478 1.00 38.18  ? 484  TYR A CG  1 
ATOM   3227  C  CD1 . TYR A 1 509 ? 129.159 142.511 123.846 1.00 41.24  ? 484  TYR A CD1 1 
ATOM   3228  C  CD2 . TYR A 1 509 ? 130.549 142.349 125.768 1.00 38.02  ? 484  TYR A CD2 1 
ATOM   3229  C  CE1 . TYR A 1 509 ? 128.189 141.762 124.479 1.00 42.72  ? 484  TYR A CE1 1 
ATOM   3230  C  CE2 . TYR A 1 509 ? 129.584 141.599 126.408 1.00 40.86  ? 484  TYR A CE2 1 
ATOM   3231  C  CZ  . TYR A 1 509 ? 128.406 141.309 125.760 1.00 45.10  ? 484  TYR A CZ  1 
ATOM   3232  O  OH  . TYR A 1 509 ? 127.440 140.562 126.393 1.00 51.11  ? 484  TYR A OH  1 
ATOM   3233  N  N   . HIS A 1 510 ? 133.193 146.169 123.015 1.00 56.72  ? 485  HIS A N   1 
ATOM   3234  C  CA  . HIS A 1 510 ? 134.399 146.954 123.232 1.00 55.83  ? 485  HIS A CA  1 
ATOM   3235  C  C   . HIS A 1 510 ? 134.054 148.421 123.461 1.00 54.17  ? 485  HIS A C   1 
ATOM   3236  O  O   . HIS A 1 510 ? 133.050 148.934 122.961 1.00 58.29  ? 485  HIS A O   1 
ATOM   3237  C  CB  . HIS A 1 510 ? 135.342 146.818 122.038 1.00 56.39  ? 485  HIS A CB  1 
ATOM   3238  C  CG  . HIS A 1 510 ? 136.650 147.524 122.216 1.00 55.84  ? 485  HIS A CG  1 
ATOM   3239  N  ND1 . HIS A 1 510 ? 137.691 146.992 122.945 1.00 57.42  ? 485  HIS A ND1 1 
ATOM   3240  C  CD2 . HIS A 1 510 ? 137.084 148.722 121.759 1.00 54.28  ? 485  HIS A CD2 1 
ATOM   3241  C  CE1 . HIS A 1 510 ? 138.711 147.831 122.930 1.00 57.99  ? 485  HIS A CE1 1 
ATOM   3242  N  NE2 . HIS A 1 510 ? 138.369 148.889 122.217 1.00 56.13  ? 485  HIS A NE2 1 
ATOM   3243  N  N   . HIS A 1 511 ? 134.899 149.096 124.234 1.00 62.46  ? 486  HIS A N   1 
ATOM   3244  C  CA  . HIS A 1 511 ? 134.717 150.513 124.505 1.00 65.01  ? 486  HIS A CA  1 
ATOM   3245  C  C   . HIS A 1 511 ? 136.079 151.177 124.618 1.00 75.05  ? 486  HIS A C   1 
ATOM   3246  O  O   . HIS A 1 511 ? 137.025 150.586 125.144 1.00 77.46  ? 486  HIS A O   1 
ATOM   3247  C  CB  . HIS A 1 511 ? 133.910 150.744 125.787 1.00 66.33  ? 486  HIS A CB  1 
ATOM   3248  C  CG  . HIS A 1 511 ? 134.660 150.420 127.041 1.00 72.08  ? 486  HIS A CG  1 
ATOM   3249  N  ND1 . HIS A 1 511 ? 134.762 151.301 128.095 1.00 68.86  ? 486  HIS A ND1 1 
ATOM   3250  C  CD2 . HIS A 1 511 ? 135.341 149.310 127.412 1.00 72.20  ? 486  HIS A CD2 1 
ATOM   3251  C  CE1 . HIS A 1 511 ? 135.476 150.750 129.060 1.00 70.84  ? 486  HIS A CE1 1 
ATOM   3252  N  NE2 . HIS A 1 511 ? 135.839 149.541 128.671 1.00 72.42  ? 486  HIS A NE2 1 
ATOM   3253  N  N   . CYS A 1 512 ? 136.170 152.403 124.113 1.00 98.61  ? 487  CYS A N   1 
ATOM   3254  C  CA  . CYS A 1 512 ? 137.402 153.168 124.227 1.00 98.23  ? 487  CYS A CA  1 
ATOM   3255  C  C   . CYS A 1 512 ? 137.645 153.571 125.676 1.00 98.55  ? 487  CYS A C   1 
ATOM   3256  O  O   . CYS A 1 512 ? 136.716 153.934 126.403 1.00 99.08  ? 487  CYS A O   1 
ATOM   3257  C  CB  . CYS A 1 512 ? 137.340 154.403 123.330 1.00 97.77  ? 487  CYS A CB  1 
ATOM   3258  S  SG  . CYS A 1 512 ? 136.155 155.658 123.860 1.00 102.29 ? 487  CYS A SG  1 
ATOM   3259  N  N   . GLN A 1 513 ? 138.904 153.495 126.098 1.00 109.15 ? 488  GLN A N   1 
ATOM   3260  C  CA  . GLN A 1 513 ? 139.278 153.826 127.470 1.00 111.30 ? 488  GLN A CA  1 
ATOM   3261  C  C   . GLN A 1 513 ? 139.248 155.339 127.636 1.00 111.55 ? 488  GLN A C   1 
ATOM   3262  O  O   . GLN A 1 513 ? 140.172 156.042 127.221 1.00 112.56 ? 488  GLN A O   1 
ATOM   3263  C  CB  . GLN A 1 513 ? 140.654 153.257 127.797 1.00 112.55 ? 488  GLN A CB  1 
ATOM   3264  C  CG  . GLN A 1 513 ? 140.899 151.865 127.233 1.00 113.10 ? 488  GLN A CG  1 
ATOM   3265  C  CD  . GLN A 1 513 ? 139.909 150.836 127.747 1.00 113.56 ? 488  GLN A CD  1 
ATOM   3266  O  OE1 . GLN A 1 513 ? 139.393 150.952 128.859 1.00 114.61 ? 488  GLN A OE1 1 
ATOM   3267  N  NE2 . GLN A 1 513 ? 139.639 149.820 126.935 1.00 111.53 ? 488  GLN A NE2 1 
ATOM   3268  N  N   . ALA A 1 514 ? 138.183 155.846 128.250 1.00 107.51 ? 489  ALA A N   1 
ATOM   3269  C  CA  . ALA A 1 514 ? 137.999 157.281 128.415 1.00 107.88 ? 489  ALA A CA  1 
ATOM   3270  C  C   . ALA A 1 514 ? 138.881 157.786 129.556 1.00 109.33 ? 489  ALA A C   1 
ATOM   3271  O  O   . ALA A 1 514 ? 139.711 157.059 130.107 1.00 110.13 ? 489  ALA A O   1 
ATOM   3272  C  CB  . ALA A 1 514 ? 136.525 157.600 128.646 1.00 106.44 ? 489  ALA A CB  1 
ATOM   3273  N  N   . GLU A 1 515 ? 138.705 159.055 129.924 1.00 102.93 ? 490  GLU A N   1 
ATOM   3274  C  CA  . GLU A 1 515 ? 139.523 159.673 130.963 1.00 102.83 ? 490  GLU A CA  1 
ATOM   3275  C  C   . GLU A 1 515 ? 138.911 159.491 132.350 1.00 104.10 ? 490  GLU A C   1 
ATOM   3276  O  O   . GLU A 1 515 ? 139.550 158.936 133.250 1.00 103.78 ? 490  GLU A O   1 
ATOM   3277  C  CB  . GLU A 1 515 ? 139.721 161.161 130.654 1.00 101.41 ? 490  GLU A CB  1 
ATOM   3278  N  N   . GLY A 1 516 ? 137.678 159.954 132.536 1.00 96.07  ? 491  GLY A N   1 
ATOM   3279  C  CA  . GLY A 1 516 ? 137.049 159.913 133.841 1.00 94.81  ? 491  GLY A CA  1 
ATOM   3280  C  C   . GLY A 1 516 ? 136.091 158.759 134.049 1.00 94.07  ? 491  GLY A C   1 
ATOM   3281  O  O   . GLY A 1 516 ? 135.598 158.554 135.162 1.00 93.33  ? 491  GLY A O   1 
ATOM   3282  N  N   . ARG A 1 517 ? 135.813 158.002 132.992 1.00 78.64  ? 492  ARG A N   1 
ATOM   3283  C  CA  . ARG A 1 517 ? 134.887 156.887 133.110 1.00 77.50  ? 492  ARG A CA  1 
ATOM   3284  C  C   . ARG A 1 517 ? 135.485 155.797 133.998 1.00 79.28  ? 492  ARG A C   1 
ATOM   3285  O  O   . ARG A 1 517 ? 136.684 155.513 133.911 1.00 80.64  ? 492  ARG A O   1 
ATOM   3286  C  CB  . ARG A 1 517 ? 134.549 156.320 131.732 1.00 77.64  ? 492  ARG A CB  1 
ATOM   3287  C  CG  . ARG A 1 517 ? 133.644 157.223 130.904 1.00 78.00  ? 492  ARG A CG  1 
ATOM   3288  C  CD  . ARG A 1 517 ? 133.060 156.499 129.699 1.00 75.41  ? 492  ARG A CD  1 
ATOM   3289  N  NE  . ARG A 1 517 ? 132.277 155.330 130.081 1.00 72.99  ? 492  ARG A NE  1 
ATOM   3290  C  CZ  . ARG A 1 517 ? 132.694 154.077 129.963 1.00 74.06  ? 492  ARG A CZ  1 
ATOM   3291  N  NH1 . ARG A 1 517 ? 133.892 153.790 129.480 1.00 78.77  ? 492  ARG A NH1 1 
ATOM   3292  N  NH2 . ARG A 1 517 ? 131.891 153.087 130.340 1.00 72.24  ? 492  ARG A NH2 1 
ATOM   3293  N  N   . PRO A 1 518 ? 134.682 155.180 134.865 1.00 80.78  ? 493  PRO A N   1 
ATOM   3294  C  CA  . PRO A 1 518 ? 135.226 154.188 135.800 1.00 80.64  ? 493  PRO A CA  1 
ATOM   3295  C  C   . PRO A 1 518 ? 135.776 152.967 135.079 1.00 81.70  ? 493  PRO A C   1 
ATOM   3296  O  O   . PRO A 1 518 ? 135.305 152.582 134.007 1.00 80.87  ? 493  PRO A O   1 
ATOM   3297  C  CB  . PRO A 1 518 ? 134.020 153.824 136.674 1.00 78.76  ? 493  PRO A CB  1 
ATOM   3298  C  CG  . PRO A 1 518 ? 133.052 154.951 136.492 1.00 80.54  ? 493  PRO A CG  1 
ATOM   3299  C  CD  . PRO A 1 518 ? 133.248 155.420 135.088 1.00 78.96  ? 493  PRO A CD  1 
ATOM   3300  N  N   . GLU A 1 519 ? 136.794 152.356 135.691 1.00 87.80  ? 494  GLU A N   1 
ATOM   3301  C  CA  . GLU A 1 519 ? 137.440 151.196 135.084 1.00 87.07  ? 494  GLU A CA  1 
ATOM   3302  C  C   . GLU A 1 519 ? 136.518 149.983 135.072 1.00 86.88  ? 494  GLU A C   1 
ATOM   3303  O  O   . GLU A 1 519 ? 136.548 149.185 134.129 1.00 88.87  ? 494  GLU A O   1 
ATOM   3304  C  CB  . GLU A 1 519 ? 138.738 150.875 135.824 1.00 87.40  ? 494  GLU A CB  1 
ATOM   3305  N  N   . TRP A 1 520 ? 135.694 149.824 136.111 1.00 73.88  ? 495  TRP A N   1 
ATOM   3306  C  CA  . TRP A 1 520 ? 134.801 148.673 136.180 1.00 75.47  ? 495  TRP A CA  1 
ATOM   3307  C  C   . TRP A 1 520 ? 133.702 148.725 135.128 1.00 73.81  ? 495  TRP A C   1 
ATOM   3308  O  O   . TRP A 1 520 ? 133.078 147.696 134.851 1.00 71.15  ? 495  TRP A O   1 
ATOM   3309  C  CB  . TRP A 1 520 ? 134.169 148.573 137.571 1.00 71.81  ? 495  TRP A CB  1 
ATOM   3310  C  CG  . TRP A 1 520 ? 133.310 149.749 137.929 1.00 71.25  ? 495  TRP A CG  1 
ATOM   3311  C  CD1 . TRP A 1 520 ? 133.686 150.855 138.633 1.00 70.98  ? 495  TRP A CD1 1 
ATOM   3312  C  CD2 . TRP A 1 520 ? 131.927 149.936 137.600 1.00 71.77  ? 495  TRP A CD2 1 
ATOM   3313  N  NE1 . TRP A 1 520 ? 132.625 151.718 138.763 1.00 71.43  ? 495  TRP A NE1 1 
ATOM   3314  C  CE2 . TRP A 1 520 ? 131.534 151.177 138.137 1.00 71.33  ? 495  TRP A CE2 1 
ATOM   3315  C  CE3 . TRP A 1 520 ? 130.983 149.174 136.904 1.00 68.42  ? 495  TRP A CE3 1 
ATOM   3316  C  CZ2 . TRP A 1 520 ? 130.240 151.674 137.999 1.00 68.08  ? 495  TRP A CZ2 1 
ATOM   3317  C  CZ3 . TRP A 1 520 ? 129.701 149.669 136.768 1.00 69.27  ? 495  TRP A CZ3 1 
ATOM   3318  C  CH2 . TRP A 1 520 ? 129.341 150.906 137.313 1.00 68.76  ? 495  TRP A CH2 1 
ATOM   3319  N  N   . ALA A 1 521 ? 133.453 149.893 134.540 1.00 73.96  ? 496  ALA A N   1 
ATOM   3320  C  CA  . ALA A 1 521 ? 132.353 150.058 133.605 1.00 72.61  ? 496  ALA A CA  1 
ATOM   3321  C  C   . ALA A 1 521 ? 132.653 149.341 132.290 1.00 71.09  ? 496  ALA A C   1 
ATOM   3322  O  O   . ALA A 1 521 ? 133.706 148.725 132.103 1.00 74.01  ? 496  ALA A O   1 
ATOM   3323  C  CB  . ALA A 1 521 ? 132.080 151.540 133.368 1.00 73.34  ? 496  ALA A CB  1 
ATOM   3324  N  N   . ASP A 1 522 ? 131.704 149.431 131.364 1.00 52.76  ? 497  ASP A N   1 
ATOM   3325  C  CA  . ASP A 1 522 ? 131.818 148.807 130.053 1.00 51.84  ? 497  ASP A CA  1 
ATOM   3326  C  C   . ASP A 1 522 ? 131.265 149.785 129.023 1.00 54.19  ? 497  ASP A C   1 
ATOM   3327  O  O   . ASP A 1 522 ? 131.089 150.974 129.304 1.00 64.60  ? 497  ASP A O   1 
ATOM   3328  C  CB  . ASP A 1 522 ? 131.099 147.453 130.034 1.00 49.54  ? 497  ASP A CB  1 
ATOM   3329  C  CG  . ASP A 1 522 ? 131.625 146.533 128.955 1.00 56.85  ? 497  ASP A CG  1 
ATOM   3330  O  OD1 . ASP A 1 522 ? 131.431 146.847 127.762 1.00 59.32  ? 497  ASP A OD1 1 
ATOM   3331  O  OD2 . ASP A 1 522 ? 132.232 145.497 129.296 1.00 59.95  ? 497  ASP A OD2 1 
ATOM   3332  N  N   . ALA A 1 523 ? 131.000 149.290 127.814 1.00 41.39  ? 498  ALA A N   1 
ATOM   3333  C  CA  . ALA A 1 523 ? 130.499 150.144 126.745 1.00 44.40  ? 498  ALA A CA  1 
ATOM   3334  C  C   . ALA A 1 523 ? 129.151 150.741 127.122 1.00 41.88  ? 498  ALA A C   1 
ATOM   3335  O  O   . ALA A 1 523 ? 128.139 150.036 127.143 1.00 44.98  ? 498  ALA A O   1 
ATOM   3336  C  CB  . ALA A 1 523 ? 130.384 149.359 125.439 1.00 42.77  ? 498  ALA A CB  1 
ATOM   3337  N  N   . ALA A 1 524 ? 129.127 152.042 127.396 1.00 34.87  ? 499  ALA A N   1 
ATOM   3338  C  CA  . ALA A 1 524 ? 127.929 152.709 127.886 1.00 32.89  ? 499  ALA A CA  1 
ATOM   3339  C  C   . ALA A 1 524 ? 127.008 153.049 126.717 1.00 42.05  ? 499  ALA A C   1 
ATOM   3340  O  O   . ALA A 1 524 ? 127.198 152.594 125.586 1.00 50.24  ? 499  ALA A O   1 
ATOM   3341  C  CB  . ALA A 1 524 ? 128.308 153.948 128.691 1.00 31.49  ? 499  ALA A CB  1 
ATOM   3342  N  N   . HIS A 1 525 ? 125.987 153.858 126.986 1.00 37.71  ? 500  HIS A N   1 
ATOM   3343  C  CA  . HIS A 1 525 ? 125.049 154.253 125.947 1.00 34.33  ? 500  HIS A CA  1 
ATOM   3344  C  C   . HIS A 1 525 ? 125.723 155.197 124.960 1.00 38.73  ? 500  HIS A C   1 
ATOM   3345  O  O   . HIS A 1 525 ? 126.362 156.176 125.357 1.00 35.27  ? 500  HIS A O   1 
ATOM   3346  C  CB  . HIS A 1 525 ? 123.822 154.920 126.566 1.00 29.50  ? 500  HIS A CB  1 
ATOM   3347  C  CG  . HIS A 1 525 ? 122.772 155.300 125.570 1.00 30.96  ? 500  HIS A CG  1 
ATOM   3348  N  ND1 . HIS A 1 525 ? 121.800 156.239 125.838 1.00 35.73  ? 500  HIS A ND1 1 
ATOM   3349  C  CD2 . HIS A 1 525 ? 122.539 154.866 124.310 1.00 33.01  ? 500  HIS A CD2 1 
ATOM   3350  C  CE1 . HIS A 1 525 ? 121.015 156.369 124.784 1.00 37.12  ? 500  HIS A CE1 1 
ATOM   3351  N  NE2 . HIS A 1 525 ? 121.442 155.548 123.842 1.00 36.64  ? 500  HIS A NE2 1 
ATOM   3352  N  N   . GLY A 1 526 ? 125.572 154.904 123.672 1.00 37.39  ? 501  GLY A N   1 
ATOM   3353  C  CA  . GLY A 1 526 ? 126.159 155.737 122.642 1.00 30.22  ? 501  GLY A CA  1 
ATOM   3354  C  C   . GLY A 1 526 ? 127.668 155.715 122.601 1.00 34.60  ? 501  GLY A C   1 
ATOM   3355  O  O   . GLY A 1 526 ? 128.284 156.716 122.225 1.00 39.00  ? 501  GLY A O   1 
ATOM   3356  N  N   . ASP A 1 527 ? 128.287 154.597 122.976 1.00 34.49  ? 502  ASP A N   1 
ATOM   3357  C  CA  . ASP A 1 527 ? 129.733 154.452 122.920 1.00 32.91  ? 502  ASP A CA  1 
ATOM   3358  C  C   . ASP A 1 527 ? 130.202 153.762 121.647 1.00 40.53  ? 502  ASP A C   1 
ATOM   3359  O  O   . ASP A 1 527 ? 131.391 153.455 121.524 1.00 51.29  ? 502  ASP A O   1 
ATOM   3360  C  CB  . ASP A 1 527 ? 130.242 153.691 124.145 1.00 36.14  ? 502  ASP A CB  1 
ATOM   3361  C  CG  . ASP A 1 527 ? 130.909 154.601 125.159 1.00 43.35  ? 502  ASP A CG  1 
ATOM   3362  O  OD1 . ASP A 1 527 ? 130.993 155.819 124.899 1.00 44.43  ? 502  ASP A OD1 1 
ATOM   3363  O  OD2 . ASP A 1 527 ? 131.349 154.101 126.215 1.00 43.72  ? 502  ASP A OD2 1 
ATOM   3364  N  N   . GLU A 1 528 ? 129.297 153.505 120.703 1.00 33.85  ? 503  GLU A N   1 
ATOM   3365  C  CA  . GLU A 1 528 ? 129.674 152.998 119.392 1.00 34.60  ? 503  GLU A CA  1 
ATOM   3366  C  C   . GLU A 1 528 ? 129.732 154.091 118.338 1.00 38.32  ? 503  GLU A C   1 
ATOM   3367  O  O   . GLU A 1 528 ? 130.267 153.853 117.251 1.00 51.72  ? 503  GLU A O   1 
ATOM   3368  C  CB  . GLU A 1 528 ? 128.695 151.914 118.931 1.00 27.09  ? 503  GLU A CB  1 
ATOM   3369  C  CG  . GLU A 1 528 ? 127.337 152.453 118.530 1.00 31.64  ? 503  GLU A CG  1 
ATOM   3370  C  CD  . GLU A 1 528 ? 126.289 152.234 119.596 1.00 45.83  ? 503  GLU A CD  1 
ATOM   3371  O  OE1 . GLU A 1 528 ? 126.538 151.427 120.514 1.00 45.37  ? 503  GLU A OE1 1 
ATOM   3372  O  OE2 . GLU A 1 528 ? 125.218 152.871 119.518 1.00 49.63  ? 503  GLU A OE2 1 
ATOM   3373  N  N   . LEU A 1 529 ? 129.192 155.273 118.632 1.00 31.46  ? 504  LEU A N   1 
ATOM   3374  C  CA  . LEU A 1 529 ? 129.242 156.374 117.674 1.00 27.40  ? 504  LEU A CA  1 
ATOM   3375  C  C   . LEU A 1 529 ? 130.659 156.763 117.267 1.00 37.20  ? 504  LEU A C   1 
ATOM   3376  O  O   . LEU A 1 529 ? 130.867 157.037 116.073 1.00 45.35  ? 504  LEU A O   1 
ATOM   3377  C  CB  . LEU A 1 529 ? 128.481 157.581 118.236 1.00 26.51  ? 504  LEU A CB  1 
ATOM   3378  C  CG  . LEU A 1 529 ? 126.968 157.554 118.022 1.00 31.93  ? 504  LEU A CG  1 
ATOM   3379  C  CD1 . LEU A 1 529 ? 126.311 158.770 118.651 1.00 37.63  ? 504  LEU A CD1 1 
ATOM   3380  C  CD2 . LEU A 1 529 ? 126.643 157.471 116.542 1.00 32.39  ? 504  LEU A CD2 1 
ATOM   3381  N  N   . PRO A 1 530 ? 131.651 156.838 118.166 1.00 40.69  ? 505  PRO A N   1 
ATOM   3382  C  CA  . PRO A 1 530 ? 133.019 157.109 117.691 1.00 36.56  ? 505  PRO A CA  1 
ATOM   3383  C  C   . PRO A 1 530 ? 133.514 156.096 116.676 1.00 37.45  ? 505  PRO A C   1 
ATOM   3384  O  O   . PRO A 1 530 ? 134.211 156.466 115.724 1.00 46.18  ? 505  PRO A O   1 
ATOM   3385  C  CB  . PRO A 1 530 ? 133.850 157.067 118.979 1.00 39.25  ? 505  PRO A CB  1 
ATOM   3386  C  CG  . PRO A 1 530 ? 132.900 157.405 120.049 1.00 37.93  ? 505  PRO A CG  1 
ATOM   3387  C  CD  . PRO A 1 530 ? 131.582 156.835 119.639 1.00 40.72  ? 505  PRO A CD  1 
ATOM   3388  N  N   . TYR A 1 531 ? 133.163 154.821 116.848 1.00 35.35  ? 506  TYR A N   1 
ATOM   3389  C  CA  . TYR A 1 531 ? 133.640 153.793 115.930 1.00 38.06  ? 506  TYR A CA  1 
ATOM   3390  C  C   . TYR A 1 531 ? 132.910 153.859 114.594 1.00 41.05  ? 506  TYR A C   1 
ATOM   3391  O  O   . TYR A 1 531 ? 133.516 153.648 113.538 1.00 50.38  ? 506  TYR A O   1 
ATOM   3392  C  CB  . TYR A 1 531 ? 133.483 152.412 116.565 1.00 30.89  ? 506  TYR A CB  1 
ATOM   3393  C  CG  . TYR A 1 531 ? 134.256 152.248 117.853 1.00 31.55  ? 506  TYR A CG  1 
ATOM   3394  C  CD1 . TYR A 1 531 ? 133.736 152.692 119.060 1.00 37.09  ? 506  TYR A CD1 1 
ATOM   3395  C  CD2 . TYR A 1 531 ? 135.510 151.658 117.861 1.00 34.68  ? 506  TYR A CD2 1 
ATOM   3396  C  CE1 . TYR A 1 531 ? 134.439 152.550 120.236 1.00 39.89  ? 506  TYR A CE1 1 
ATOM   3397  C  CE2 . TYR A 1 531 ? 136.220 151.510 119.033 1.00 40.25  ? 506  TYR A CE2 1 
ATOM   3398  C  CZ  . TYR A 1 531 ? 135.680 151.958 120.217 1.00 44.93  ? 506  TYR A CZ  1 
ATOM   3399  O  OH  . TYR A 1 531 ? 136.384 151.814 121.389 1.00 52.72  ? 506  TYR A OH  1 
ATOM   3400  N  N   . VAL A 1 532 ? 131.608 154.148 114.621 1.00 31.96  ? 507  VAL A N   1 
ATOM   3401  C  CA  . VAL A 1 532 ? 130.832 154.214 113.387 1.00 25.30  ? 507  VAL A CA  1 
ATOM   3402  C  C   . VAL A 1 532 ? 131.268 155.400 112.536 1.00 36.93  ? 507  VAL A C   1 
ATOM   3403  O  O   . VAL A 1 532 ? 131.287 155.322 111.302 1.00 47.21  ? 507  VAL A O   1 
ATOM   3404  C  CB  . VAL A 1 532 ? 129.329 154.267 113.711 1.00 33.38  ? 507  VAL A CB  1 
ATOM   3405  C  CG1 . VAL A 1 532 ? 128.515 154.404 112.439 1.00 34.06  ? 507  VAL A CG1 1 
ATOM   3406  C  CG2 . VAL A 1 532 ? 128.914 153.024 114.473 1.00 39.81  ? 507  VAL A CG2 1 
ATOM   3407  N  N   . PHE A 1 533 ? 131.622 156.514 113.170 1.00 39.30  ? 508  PHE A N   1 
ATOM   3408  C  CA  . PHE A 1 533 ? 131.972 157.734 112.456 1.00 33.23  ? 508  PHE A CA  1 
ATOM   3409  C  C   . PHE A 1 533 ? 133.468 157.867 112.197 1.00 33.67  ? 508  PHE A C   1 
ATOM   3410  O  O   . PHE A 1 533 ? 133.905 158.903 111.688 1.00 42.53  ? 508  PHE A O   1 
ATOM   3411  C  CB  . PHE A 1 533 ? 131.464 158.954 113.224 1.00 33.99  ? 508  PHE A CB  1 
ATOM   3412  C  CG  . PHE A 1 533 ? 130.088 159.389 112.817 1.00 34.51  ? 508  PHE A CG  1 
ATOM   3413  C  CD1 . PHE A 1 533 ? 129.898 160.155 111.682 1.00 45.15  ? 508  PHE A CD1 1 
ATOM   3414  C  CD2 . PHE A 1 533 ? 128.985 159.022 113.562 1.00 33.93  ? 508  PHE A CD2 1 
ATOM   3415  C  CE1 . PHE A 1 533 ? 128.634 160.552 111.303 1.00 39.38  ? 508  PHE A CE1 1 
ATOM   3416  C  CE2 . PHE A 1 533 ? 127.720 159.416 113.188 1.00 42.29  ? 508  PHE A CE2 1 
ATOM   3417  C  CZ  . PHE A 1 533 ? 127.544 160.182 112.057 1.00 41.80  ? 508  PHE A CZ  1 
ATOM   3418  N  N   . GLY A 1 534 ? 134.257 156.851 112.534 1.00 30.66  ? 509  GLY A N   1 
ATOM   3419  C  CA  . GLY A 1 534 ? 135.684 156.895 112.279 1.00 33.58  ? 509  GLY A CA  1 
ATOM   3420  C  C   . GLY A 1 534 ? 136.445 157.925 113.079 1.00 38.91  ? 509  GLY A C   1 
ATOM   3421  O  O   . GLY A 1 534 ? 137.406 158.508 112.570 1.00 48.93  ? 509  GLY A O   1 
ATOM   3422  N  N   . VAL A 1 535 ? 136.034 158.175 114.324 1.00 38.40  ? 510  VAL A N   1 
ATOM   3423  C  CA  . VAL A 1 535 ? 136.814 159.055 115.198 1.00 36.02  ? 510  VAL A CA  1 
ATOM   3424  C  C   . VAL A 1 535 ? 138.202 158.496 115.480 1.00 46.13  ? 510  VAL A C   1 
ATOM   3425  O  O   . VAL A 1 535 ? 139.175 159.261 115.412 1.00 47.65  ? 510  VAL A O   1 
ATOM   3426  C  CB  . VAL A 1 535 ? 136.019 159.376 116.470 1.00 39.55  ? 510  VAL A CB  1 
ATOM   3427  C  CG1 . VAL A 1 535 ? 136.874 160.165 117.446 1.00 46.27  ? 510  VAL A CG1 1 
ATOM   3428  C  CG2 . VAL A 1 535 ? 134.761 160.153 116.122 1.00 43.04  ? 510  VAL A CG2 1 
ATOM   3429  N  N   . PRO A 1 536 ? 138.385 157.208 115.804 1.00 50.95  ? 511  PRO A N   1 
ATOM   3430  C  CA  . PRO A 1 536 ? 139.743 156.723 116.106 1.00 52.21  ? 511  PRO A CA  1 
ATOM   3431  C  C   . PRO A 1 536 ? 140.727 156.862 114.957 1.00 51.50  ? 511  PRO A C   1 
ATOM   3432  O  O   . PRO A 1 536 ? 141.937 156.926 115.208 1.00 54.35  ? 511  PRO A O   1 
ATOM   3433  C  CB  . PRO A 1 536 ? 139.517 155.247 116.463 1.00 53.23  ? 511  PRO A CB  1 
ATOM   3434  C  CG  . PRO A 1 536 ? 138.119 155.189 116.925 1.00 49.78  ? 511  PRO A CG  1 
ATOM   3435  C  CD  . PRO A 1 536 ? 137.383 156.156 116.058 1.00 48.92  ? 511  PRO A CD  1 
ATOM   3436  N  N   . MET A 1 537 ? 140.261 156.910 113.712 1.00 47.65  ? 512  MET A N   1 
ATOM   3437  C  CA  . MET A 1 537 ? 141.169 156.979 112.574 1.00 42.55  ? 512  MET A CA  1 
ATOM   3438  C  C   . MET A 1 537 ? 141.643 158.394 112.272 1.00 46.10  ? 512  MET A C   1 
ATOM   3439  O  O   . MET A 1 537 ? 142.416 158.579 111.327 1.00 52.63  ? 512  MET A O   1 
ATOM   3440  C  CB  . MET A 1 537 ? 140.505 156.374 111.334 1.00 42.70  ? 512  MET A CB  1 
ATOM   3441  C  CG  . MET A 1 537 ? 140.285 154.871 111.438 1.00 48.24  ? 512  MET A CG  1 
ATOM   3442  S  SD  . MET A 1 537 ? 139.454 154.136 110.017 1.00 61.76  ? 512  MET A SD  1 
ATOM   3443  C  CE  . MET A 1 537 ? 139.471 155.499 108.859 1.00 51.66  ? 512  MET A CE  1 
ATOM   3444  N  N   . VAL A 1 538 ? 141.204 159.391 113.040 1.00 45.14  ? 513  VAL A N   1 
ATOM   3445  C  CA  . VAL A 1 538 ? 141.669 160.763 112.863 1.00 50.25  ? 513  VAL A CA  1 
ATOM   3446  C  C   . VAL A 1 538 ? 142.280 161.258 114.166 1.00 52.87  ? 513  VAL A C   1 
ATOM   3447  O  O   . VAL A 1 538 ? 143.147 162.139 114.164 1.00 58.10  ? 513  VAL A O   1 
ATOM   3448  C  CB  . VAL A 1 538 ? 140.525 161.684 112.401 1.00 50.37  ? 513  VAL A CB  1 
ATOM   3449  C  CG1 . VAL A 1 538 ? 141.069 163.037 111.970 1.00 49.75  ? 513  VAL A CG1 1 
ATOM   3450  C  CG2 . VAL A 1 538 ? 139.765 161.041 111.265 1.00 48.66  ? 513  VAL A CG2 1 
ATOM   3451  N  N   . GLY A 1 539 ? 141.845 160.693 115.283 1.00 53.42  ? 514  GLY A N   1 
ATOM   3452  C  CA  . GLY A 1 539 ? 142.364 161.043 116.587 1.00 54.99  ? 514  GLY A CA  1 
ATOM   3453  C  C   . GLY A 1 539 ? 141.266 161.472 117.540 1.00 55.80  ? 514  GLY A C   1 
ATOM   3454  O  O   . GLY A 1 539 ? 140.077 161.445 117.223 1.00 56.05  ? 514  GLY A O   1 
ATOM   3455  N  N   . ALA A 1 540 ? 141.697 161.874 118.732 1.00 68.72  ? 515  ALA A N   1 
ATOM   3456  C  CA  . ALA A 1 540 ? 140.777 162.300 119.778 1.00 68.05  ? 515  ALA A CA  1 
ATOM   3457  C  C   . ALA A 1 540 ? 140.339 163.737 119.528 1.00 68.50  ? 515  ALA A C   1 
ATOM   3458  O  O   . ALA A 1 540 ? 141.177 164.641 119.439 1.00 73.03  ? 515  ALA A O   1 
ATOM   3459  C  CB  . ALA A 1 540 ? 141.435 162.168 121.150 1.00 68.50  ? 515  ALA A CB  1 
ATOM   3460  N  N   . THR A 1 541 ? 139.033 163.948 119.417 1.00 72.47  ? 516  THR A N   1 
ATOM   3461  C  CA  . THR A 1 541 ? 138.465 165.269 119.211 1.00 75.52  ? 516  THR A CA  1 
ATOM   3462  C  C   . THR A 1 541 ? 137.964 165.824 120.543 1.00 75.59  ? 516  THR A C   1 
ATOM   3463  O  O   . THR A 1 541 ? 138.169 165.232 121.607 1.00 76.65  ? 516  THR A O   1 
ATOM   3464  C  CB  . THR A 1 541 ? 137.348 165.209 118.167 1.00 76.73  ? 516  THR A CB  1 
ATOM   3465  O  OG1 . THR A 1 541 ? 136.148 164.717 118.776 1.00 76.03  ? 516  THR A OG1 1 
ATOM   3466  C  CG2 . THR A 1 541 ? 137.739 164.291 117.021 1.00 74.98  ? 516  THR A CG2 1 
ATOM   3467  N  N   . ASP A 1 542 ? 137.305 166.984 120.490 1.00 79.58  ? 517  ASP A N   1 
ATOM   3468  C  CA  . ASP A 1 542 ? 136.765 167.584 121.706 1.00 79.86  ? 517  ASP A CA  1 
ATOM   3469  C  C   . ASP A 1 542 ? 135.694 166.700 122.331 1.00 79.33  ? 517  ASP A C   1 
ATOM   3470  O  O   . ASP A 1 542 ? 135.654 166.530 123.555 1.00 81.06  ? 517  ASP A O   1 
ATOM   3471  C  CB  . ASP A 1 542 ? 136.200 168.971 121.402 1.00 82.82  ? 517  ASP A CB  1 
ATOM   3472  C  CG  . ASP A 1 542 ? 137.080 169.767 120.460 1.00 84.65  ? 517  ASP A CG  1 
ATOM   3473  O  OD1 . ASP A 1 542 ? 138.153 170.232 120.897 1.00 85.89  ? 517  ASP A OD1 1 
ATOM   3474  O  OD2 . ASP A 1 542 ? 136.697 169.928 119.281 1.00 83.47  ? 517  ASP A OD2 1 
ATOM   3475  N  N   . LEU A 1 543 ? 134.814 166.132 121.504 1.00 74.68  ? 518  LEU A N   1 
ATOM   3476  C  CA  . LEU A 1 543 ? 133.730 165.306 122.025 1.00 76.54  ? 518  LEU A CA  1 
ATOM   3477  C  C   . LEU A 1 543 ? 134.254 164.002 122.613 1.00 77.27  ? 518  LEU A C   1 
ATOM   3478  O  O   . LEU A 1 543 ? 133.732 163.517 123.623 1.00 76.26  ? 518  LEU A O   1 
ATOM   3479  C  CB  . LEU A 1 543 ? 132.712 165.029 120.920 1.00 76.07  ? 518  LEU A CB  1 
ATOM   3480  C  CG  . LEU A 1 543 ? 131.558 166.025 120.788 1.00 75.94  ? 518  LEU A CG  1 
ATOM   3481  C  CD1 . LEU A 1 543 ? 130.352 165.365 120.144 1.00 74.83  ? 518  LEU A CD1 1 
ATOM   3482  C  CD2 . LEU A 1 543 ? 131.188 166.612 122.141 1.00 75.06  ? 518  LEU A CD2 1 
ATOM   3483  N  N   . PHE A 1 544 ? 135.282 163.418 121.997 1.00 75.96  ? 519  PHE A N   1 
ATOM   3484  C  CA  . PHE A 1 544 ? 135.853 162.146 122.436 1.00 71.06  ? 519  PHE A CA  1 
ATOM   3485  C  C   . PHE A 1 544 ? 137.351 162.324 122.637 1.00 75.52  ? 519  PHE A C   1 
ATOM   3486  O  O   . PHE A 1 544 ? 138.147 162.062 121.725 1.00 77.05  ? 519  PHE A O   1 
ATOM   3487  C  CB  . PHE A 1 544 ? 135.562 161.033 121.431 1.00 67.07  ? 519  PHE A CB  1 
ATOM   3488  C  CG  . PHE A 1 544 ? 134.213 161.140 120.781 1.00 70.64  ? 519  PHE A CG  1 
ATOM   3489  C  CD1 . PHE A 1 544 ? 133.097 160.586 121.380 1.00 71.14  ? 519  PHE A CD1 1 
ATOM   3490  C  CD2 . PHE A 1 544 ? 134.064 161.784 119.565 1.00 74.12  ? 519  PHE A CD2 1 
ATOM   3491  C  CE1 . PHE A 1 544 ? 131.855 160.679 120.781 1.00 70.62  ? 519  PHE A CE1 1 
ATOM   3492  C  CE2 . PHE A 1 544 ? 132.825 161.880 118.963 1.00 72.32  ? 519  PHE A CE2 1 
ATOM   3493  C  CZ  . PHE A 1 544 ? 131.720 161.326 119.571 1.00 69.85  ? 519  PHE A CZ  1 
ATOM   3494  N  N   . PRO A 1 545 ? 137.775 162.768 123.822 1.00 90.96  ? 520  PRO A N   1 
ATOM   3495  C  CA  . PRO A 1 545 ? 139.209 162.976 124.065 1.00 92.37  ? 520  PRO A CA  1 
ATOM   3496  C  C   . PRO A 1 545 ? 139.932 161.700 124.468 1.00 90.48  ? 520  PRO A C   1 
ATOM   3497  O  O   . PRO A 1 545 ? 141.054 161.749 124.980 1.00 90.99  ? 520  PRO A O   1 
ATOM   3498  C  CB  . PRO A 1 545 ? 139.216 164.003 125.201 1.00 87.94  ? 520  PRO A CB  1 
ATOM   3499  C  CG  . PRO A 1 545 ? 137.969 163.696 125.967 1.00 87.93  ? 520  PRO A CG  1 
ATOM   3500  C  CD  . PRO A 1 545 ? 136.953 163.177 124.974 1.00 88.09  ? 520  PRO A CD  1 
ATOM   3501  N  N   . CYS A 1 546 ? 139.298 160.554 124.241 1.00 101.04 ? 521  CYS A N   1 
ATOM   3502  C  CA  . CYS A 1 546 ? 139.834 159.286 124.711 1.00 101.56 ? 521  CYS A CA  1 
ATOM   3503  C  C   . CYS A 1 546 ? 141.065 158.868 123.912 1.00 103.03 ? 521  CYS A C   1 
ATOM   3504  O  O   . CYS A 1 546 ? 141.213 159.195 122.732 1.00 103.48 ? 521  CYS A O   1 
ATOM   3505  C  CB  . CYS A 1 546 ? 138.762 158.202 124.624 1.00 103.20 ? 521  CYS A CB  1 
ATOM   3506  S  SG  . CYS A 1 546 ? 137.086 158.823 124.886 1.00 112.43 ? 521  CYS A SG  1 
ATOM   3507  N  N   . ASN A 1 547 ? 141.954 158.134 124.578 1.00 115.18 ? 522  ASN A N   1 
ATOM   3508  C  CA  . ASN A 1 547 ? 143.135 157.575 123.935 1.00 113.75 ? 522  ASN A CA  1 
ATOM   3509  C  C   . ASN A 1 547 ? 142.736 156.371 123.091 1.00 112.68 ? 522  ASN A C   1 
ATOM   3510  O  O   . ASN A 1 547 ? 142.015 155.487 123.563 1.00 114.47 ? 522  ASN A O   1 
ATOM   3511  C  CB  . ASN A 1 547 ? 144.163 157.159 124.987 1.00 113.53 ? 522  ASN A CB  1 
ATOM   3512  C  CG  . ASN A 1 547 ? 145.357 158.090 125.044 1.00 116.47 ? 522  ASN A CG  1 
ATOM   3513  O  OD1 . ASN A 1 547 ? 145.285 159.245 124.625 1.00 117.88 ? 522  ASN A OD1 1 
ATOM   3514  N  ND2 . ASN A 1 547 ? 146.466 157.586 125.574 1.00 119.34 ? 522  ASN A ND2 1 
ATOM   3515  N  N   . PHE A 1 548 ? 143.208 156.331 121.849 1.00 80.85  ? 523  PHE A N   1 
ATOM   3516  C  CA  . PHE A 1 548 ? 142.862 155.266 120.917 1.00 82.19  ? 523  PHE A CA  1 
ATOM   3517  C  C   . PHE A 1 548 ? 144.109 154.478 120.538 1.00 81.18  ? 523  PHE A C   1 
ATOM   3518  O  O   . PHE A 1 548 ? 145.109 155.059 120.104 1.00 82.02  ? 523  PHE A O   1 
ATOM   3519  C  CB  . PHE A 1 548 ? 142.190 155.832 119.665 1.00 81.14  ? 523  PHE A CB  1 
ATOM   3520  C  CG  . PHE A 1 548 ? 140.800 156.347 119.906 1.00 81.83  ? 523  PHE A CG  1 
ATOM   3521  C  CD1 . PHE A 1 548 ? 139.748 155.470 120.106 1.00 81.96  ? 523  PHE A CD1 1 
ATOM   3522  C  CD2 . PHE A 1 548 ? 140.545 157.707 119.930 1.00 80.03  ? 523  PHE A CD2 1 
ATOM   3523  C  CE1 . PHE A 1 548 ? 138.469 155.940 120.330 1.00 78.76  ? 523  PHE A CE1 1 
ATOM   3524  C  CE2 . PHE A 1 548 ? 139.268 158.182 120.152 1.00 79.94  ? 523  PHE A CE2 1 
ATOM   3525  C  CZ  . PHE A 1 548 ? 138.229 157.297 120.352 1.00 79.32  ? 523  PHE A CZ  1 
ATOM   3526  N  N   . SER A 1 549 ? 144.043 153.160 120.703 1.00 71.79  ? 524  SER A N   1 
ATOM   3527  C  CA  . SER A 1 549 ? 145.131 152.270 120.332 1.00 71.03  ? 524  SER A CA  1 
ATOM   3528  C  C   . SER A 1 549 ? 144.904 151.747 118.914 1.00 72.53  ? 524  SER A C   1 
ATOM   3529  O  O   . SER A 1 549 ? 144.042 152.233 118.178 1.00 76.25  ? 524  SER A O   1 
ATOM   3530  C  CB  . SER A 1 549 ? 145.251 151.133 121.345 1.00 71.59  ? 524  SER A CB  1 
ATOM   3531  O  OG  . SER A 1 549 ? 144.369 150.072 121.024 1.00 68.61  ? 524  SER A OG  1 
ATOM   3532  N  N   . LYS A 1 550 ? 145.690 150.745 118.511 1.00 65.97  ? 525  LYS A N   1 
ATOM   3533  C  CA  . LYS A 1 550 ? 145.500 150.142 117.197 1.00 64.29  ? 525  LYS A CA  1 
ATOM   3534  C  C   . LYS A 1 550 ? 144.259 149.260 117.157 1.00 67.25  ? 525  LYS A C   1 
ATOM   3535  O  O   . LYS A 1 550 ? 143.611 149.149 116.109 1.00 70.73  ? 525  LYS A O   1 
ATOM   3536  C  CB  . LYS A 1 550 ? 146.737 149.335 116.805 1.00 65.47  ? 525  LYS A CB  1 
ATOM   3537  N  N   . ASN A 1 551 ? 143.918 148.623 118.281 1.00 63.69  ? 526  ASN A N   1 
ATOM   3538  C  CA  . ASN A 1 551 ? 142.721 147.791 118.330 1.00 65.07  ? 526  ASN A CA  1 
ATOM   3539  C  C   . ASN A 1 551 ? 141.467 148.620 118.089 1.00 65.33  ? 526  ASN A C   1 
ATOM   3540  O  O   . ASN A 1 551 ? 140.535 148.170 117.411 1.00 65.11  ? 526  ASN A O   1 
ATOM   3541  C  CB  . ASN A 1 551 ? 142.635 147.070 119.674 1.00 63.52  ? 526  ASN A CB  1 
ATOM   3542  C  CG  . ASN A 1 551 ? 143.717 146.025 119.845 1.00 66.54  ? 526  ASN A CG  1 
ATOM   3543  O  OD1 . ASN A 1 551 ? 144.317 145.571 118.871 1.00 66.64  ? 526  ASN A OD1 1 
ATOM   3544  N  ND2 . ASN A 1 551 ? 143.973 145.637 121.089 1.00 68.78  ? 526  ASN A ND2 1 
ATOM   3545  N  N   . ASP A 1 552 ? 141.422 149.833 118.645 1.00 60.04  ? 527  ASP A N   1 
ATOM   3546  C  CA  . ASP A 1 552 ? 140.281 150.711 118.417 1.00 55.75  ? 527  ASP A CA  1 
ATOM   3547  C  C   . ASP A 1 552 ? 140.156 151.080 116.945 1.00 57.01  ? 527  ASP A C   1 
ATOM   3548  O  O   . ASP A 1 552 ? 139.049 151.113 116.399 1.00 60.19  ? 527  ASP A O   1 
ATOM   3549  C  CB  . ASP A 1 552 ? 140.405 151.965 119.279 1.00 55.50  ? 527  ASP A CB  1 
ATOM   3550  C  CG  . ASP A 1 552 ? 140.639 151.642 120.740 1.00 63.29  ? 527  ASP A CG  1 
ATOM   3551  O  OD1 . ASP A 1 552 ? 140.267 150.531 121.170 1.00 63.31  ? 527  ASP A OD1 1 
ATOM   3552  O  OD2 . ASP A 1 552 ? 141.194 152.498 121.459 1.00 65.94  ? 527  ASP A OD2 1 
ATOM   3553  N  N   . VAL A 1 553 ? 141.282 151.356 116.283 1.00 54.17  ? 528  VAL A N   1 
ATOM   3554  C  CA  . VAL A 1 553 ? 141.246 151.683 114.861 1.00 54.13  ? 528  VAL A CA  1 
ATOM   3555  C  C   . VAL A 1 553 ? 140.772 150.485 114.047 1.00 47.91  ? 528  VAL A C   1 
ATOM   3556  O  O   . VAL A 1 553 ? 139.971 150.628 113.114 1.00 53.84  ? 528  VAL A O   1 
ATOM   3557  C  CB  . VAL A 1 553 ? 142.626 152.179 114.393 1.00 49.16  ? 528  VAL A CB  1 
ATOM   3558  C  CG1 . VAL A 1 553 ? 142.663 152.304 112.879 1.00 47.51  ? 528  VAL A CG1 1 
ATOM   3559  C  CG2 . VAL A 1 553 ? 142.959 153.509 115.047 1.00 46.06  ? 528  VAL A CG2 1 
ATOM   3560  N  N   . MET A 1 554 ? 141.254 149.287 114.384 1.00 39.60  ? 529  MET A N   1 
ATOM   3561  C  CA  . MET A 1 554 ? 140.816 148.091 113.671 1.00 47.12  ? 529  MET A CA  1 
ATOM   3562  C  C   . MET A 1 554 ? 139.320 147.856 113.851 1.00 53.90  ? 529  MET A C   1 
ATOM   3563  O  O   . MET A 1 554 ? 138.613 147.535 112.887 1.00 57.61  ? 529  MET A O   1 
ATOM   3564  C  CB  . MET A 1 554 ? 141.610 146.876 114.148 1.00 50.19  ? 529  MET A CB  1 
ATOM   3565  C  CG  . MET A 1 554 ? 141.260 145.585 113.430 1.00 52.07  ? 529  MET A CG  1 
ATOM   3566  S  SD  . MET A 1 554 ? 140.188 144.518 114.412 1.00 68.75  ? 529  MET A SD  1 
ATOM   3567  C  CE  . MET A 1 554 ? 141.253 144.159 115.806 1.00 52.94  ? 529  MET A CE  1 
ATOM   3568  N  N   . LEU A 1 555 ? 138.818 148.021 115.076 1.00 47.16  ? 530  LEU A N   1 
ATOM   3569  C  CA  . LEU A 1 555 ? 137.391 147.835 115.319 1.00 40.25  ? 530  LEU A CA  1 
ATOM   3570  C  C   . LEU A 1 555 ? 136.563 148.894 114.604 1.00 38.06  ? 530  LEU A C   1 
ATOM   3571  O  O   . LEU A 1 555 ? 135.475 148.599 114.096 1.00 42.59  ? 530  LEU A O   1 
ATOM   3572  C  CB  . LEU A 1 555 ? 137.103 147.857 116.817 1.00 36.70  ? 530  LEU A CB  1 
ATOM   3573  C  CG  . LEU A 1 555 ? 135.694 147.397 117.184 1.00 39.04  ? 530  LEU A CG  1 
ATOM   3574  C  CD1 . LEU A 1 555 ? 135.540 145.905 116.949 1.00 34.35  ? 530  LEU A CD1 1 
ATOM   3575  C  CD2 . LEU A 1 555 ? 135.381 147.755 118.620 1.00 45.33  ? 530  LEU A CD2 1 
ATOM   3576  N  N   . SER A 1 556 ? 137.048 150.137 114.574 1.00 34.13  ? 531  SER A N   1 
ATOM   3577  C  CA  . SER A 1 556 ? 136.344 151.185 113.846 1.00 33.77  ? 531  SER A CA  1 
ATOM   3578  C  C   . SER A 1 556 ? 136.274 150.860 112.363 1.00 30.74  ? 531  SER A C   1 
ATOM   3579  O  O   . SER A 1 556 ? 135.225 151.030 111.733 1.00 37.53  ? 531  SER A O   1 
ATOM   3580  C  CB  . SER A 1 556 ? 137.026 152.533 114.070 1.00 37.80  ? 531  SER A CB  1 
ATOM   3581  O  OG  . SER A 1 556 ? 136.637 153.466 113.079 1.00 36.69  ? 531  SER A OG  1 
ATOM   3582  N  N   . ALA A 1 557 ? 137.378 150.377 111.791 1.00 37.85  ? 532  ALA A N   1 
ATOM   3583  C  CA  . ALA A 1 557 ? 137.361 149.971 110.391 1.00 39.22  ? 532  ALA A CA  1 
ATOM   3584  C  C   . ALA A 1 557 ? 136.376 148.833 110.162 1.00 39.88  ? 532  ALA A C   1 
ATOM   3585  O  O   . ALA A 1 557 ? 135.641 148.830 109.169 1.00 45.52  ? 532  ALA A O   1 
ATOM   3586  C  CB  . ALA A 1 557 ? 138.764 149.565 109.942 1.00 35.82  ? 532  ALA A CB  1 
ATOM   3587  N  N   . VAL A 1 558 ? 136.333 147.867 111.082 1.00 32.87  ? 533  VAL A N   1 
ATOM   3588  C  CA  . VAL A 1 558 ? 135.437 146.724 110.923 1.00 32.43  ? 533  VAL A CA  1 
ATOM   3589  C  C   . VAL A 1 558 ? 133.979 147.173 110.949 1.00 40.41  ? 533  VAL A C   1 
ATOM   3590  O  O   . VAL A 1 558 ? 133.180 146.802 110.078 1.00 45.38  ? 533  VAL A O   1 
ATOM   3591  C  CB  . VAL A 1 558 ? 135.722 145.670 112.008 1.00 34.88  ? 533  VAL A CB  1 
ATOM   3592  C  CG1 . VAL A 1 558 ? 134.540 144.729 112.161 1.00 36.99  ? 533  VAL A CG1 1 
ATOM   3593  C  CG2 . VAL A 1 558 ? 136.989 144.899 111.678 1.00 39.30  ? 533  VAL A CG2 1 
ATOM   3594  N  N   . VAL A 1 559 ? 133.608 147.983 111.944 1.00 40.30  ? 534  VAL A N   1 
ATOM   3595  C  CA  . VAL A 1 559 ? 132.214 148.403 112.063 1.00 33.27  ? 534  VAL A CA  1 
ATOM   3596  C  C   . VAL A 1 559 ? 131.831 149.332 110.916 1.00 33.42  ? 534  VAL A C   1 
ATOM   3597  O  O   . VAL A 1 559 ? 130.699 149.290 110.420 1.00 35.68  ? 534  VAL A O   1 
ATOM   3598  C  CB  . VAL A 1 559 ? 131.943 149.042 113.439 1.00 27.29  ? 534  VAL A CB  1 
ATOM   3599  C  CG1 . VAL A 1 559 ? 132.289 148.068 114.551 1.00 30.56  ? 534  VAL A CG1 1 
ATOM   3600  C  CG2 . VAL A 1 559 ? 132.710 150.337 113.609 1.00 28.95  ? 534  VAL A CG2 1 
ATOM   3601  N  N   . MET A 1 560 ? 132.761 150.178 110.466 1.00 36.79  ? 535  MET A N   1 
ATOM   3602  C  CA  . MET A 1 560 ? 132.470 151.051 109.337 1.00 35.70  ? 535  MET A CA  1 
ATOM   3603  C  C   . MET A 1 560 ? 132.272 150.248 108.060 1.00 38.16  ? 535  MET A C   1 
ATOM   3604  O  O   . MET A 1 560 ? 131.381 150.555 107.259 1.00 43.81  ? 535  MET A O   1 
ATOM   3605  C  CB  . MET A 1 560 ? 133.590 152.075 109.180 1.00 24.63  ? 535  MET A CB  1 
ATOM   3606  C  CG  . MET A 1 560 ? 133.251 153.413 109.794 1.00 27.75  ? 535  MET A CG  1 
ATOM   3607  S  SD  . MET A 1 560 ? 134.677 154.485 110.006 1.00 48.37  ? 535  MET A SD  1 
ATOM   3608  C  CE  . MET A 1 560 ? 135.443 154.343 108.404 1.00 41.27  ? 535  MET A CE  1 
ATOM   3609  N  N   . THR A 1 561 ? 133.083 149.206 107.858 1.00 32.82  ? 536  THR A N   1 
ATOM   3610  C  CA  . THR A 1 561 ? 132.888 148.335 106.706 1.00 33.00  ? 536  THR A CA  1 
ATOM   3611  C  C   . THR A 1 561 ? 131.540 147.630 106.777 1.00 33.83  ? 536  THR A C   1 
ATOM   3612  O  O   . THR A 1 561 ? 130.840 147.516 105.765 1.00 37.69  ? 536  THR A O   1 
ATOM   3613  C  CB  . THR A 1 561 ? 134.022 147.315 106.617 1.00 36.51  ? 536  THR A CB  1 
ATOM   3614  O  OG1 . THR A 1 561 ? 135.260 147.997 106.381 1.00 44.87  ? 536  THR A OG1 1 
ATOM   3615  C  CG2 . THR A 1 561 ? 133.772 146.343 105.478 1.00 34.01  ? 536  THR A CG2 1 
ATOM   3616  N  N   . TYR A 1 562 ? 131.155 147.159 107.966 1.00 34.02  ? 537  TYR A N   1 
ATOM   3617  C  CA  . TYR A 1 562 ? 129.854 146.510 108.116 1.00 37.22  ? 537  TYR A CA  1 
ATOM   3618  C  C   . TYR A 1 562 ? 128.717 147.469 107.775 1.00 36.39  ? 537  TYR A C   1 
ATOM   3619  O  O   . TYR A 1 562 ? 127.798 147.124 107.019 1.00 43.22  ? 537  TYR A O   1 
ATOM   3620  C  CB  . TYR A 1 562 ? 129.697 145.981 109.541 1.00 38.29  ? 537  TYR A CB  1 
ATOM   3621  C  CG  . TYR A 1 562 ? 130.245 144.590 109.753 1.00 37.52  ? 537  TYR A CG  1 
ATOM   3622  C  CD1 . TYR A 1 562 ? 130.170 143.633 108.753 1.00 40.15  ? 537  TYR A CD1 1 
ATOM   3623  C  CD2 . TYR A 1 562 ? 130.835 144.233 110.957 1.00 37.78  ? 537  TYR A CD2 1 
ATOM   3624  C  CE1 . TYR A 1 562 ? 130.669 142.361 108.945 1.00 40.01  ? 537  TYR A CE1 1 
ATOM   3625  C  CE2 . TYR A 1 562 ? 131.336 142.965 111.158 1.00 37.58  ? 537  TYR A CE2 1 
ATOM   3626  C  CZ  . TYR A 1 562 ? 131.250 142.033 110.149 1.00 39.20  ? 537  TYR A CZ  1 
ATOM   3627  O  OH  . TYR A 1 562 ? 131.749 140.767 110.345 1.00 43.97  ? 537  TYR A OH  1 
ATOM   3628  N  N   . TRP A 1 563 ? 128.772 148.687 108.320 1.00 30.03  ? 538  TRP A N   1 
ATOM   3629  C  CA  . TRP A 1 563 ? 127.720 149.666 108.064 1.00 31.09  ? 538  TRP A CA  1 
ATOM   3630  C  C   . TRP A 1 563 ? 127.649 150.030 106.586 1.00 35.46  ? 538  TRP A C   1 
ATOM   3631  O  O   . TRP A 1 563 ? 126.556 150.131 106.015 1.00 39.54  ? 538  TRP A O   1 
ATOM   3632  C  CB  . TRP A 1 563 ? 127.953 150.922 108.905 1.00 32.98  ? 538  TRP A CB  1 
ATOM   3633  C  CG  . TRP A 1 563 ? 127.319 150.930 110.276 1.00 26.83  ? 538  TRP A CG  1 
ATOM   3634  C  CD1 . TRP A 1 563 ? 126.650 151.971 110.847 1.00 27.99  ? 538  TRP A CD1 1 
ATOM   3635  C  CD2 . TRP A 1 563 ? 127.324 149.877 111.255 1.00 33.10  ? 538  TRP A CD2 1 
ATOM   3636  N  NE1 . TRP A 1 563 ? 126.223 151.632 112.105 1.00 35.79  ? 538  TRP A NE1 1 
ATOM   3637  C  CE2 . TRP A 1 563 ? 126.625 150.352 112.381 1.00 30.28  ? 538  TRP A CE2 1 
ATOM   3638  C  CE3 . TRP A 1 563 ? 127.843 148.579 111.286 1.00 36.03  ? 538  TRP A CE3 1 
ATOM   3639  C  CZ2 . TRP A 1 563 ? 126.433 149.579 113.521 1.00 30.21  ? 538  TRP A CZ2 1 
ATOM   3640  C  CZ3 . TRP A 1 563 ? 127.651 147.814 112.419 1.00 29.51  ? 538  TRP A CZ3 1 
ATOM   3641  C  CH2 . TRP A 1 563 ? 126.952 148.315 113.520 1.00 30.46  ? 538  TRP A CH2 1 
ATOM   3642  N  N   . THR A 1 564 ? 128.803 150.228 105.946 1.00 31.38  ? 539  THR A N   1 
ATOM   3643  C  CA  . THR A 1 564 ? 128.802 150.620 104.542 1.00 25.05  ? 539  THR A CA  1 
ATOM   3644  C  C   . THR A 1 564 ? 128.336 149.479 103.646 1.00 37.61  ? 539  THR A C   1 
ATOM   3645  O  O   . THR A 1 564 ? 127.654 149.715 102.644 1.00 45.01  ? 539  THR A O   1 
ATOM   3646  C  CB  . THR A 1 564 ? 130.190 151.100 104.130 1.00 26.96  ? 539  THR A CB  1 
ATOM   3647  O  OG1 . THR A 1 564 ? 131.177 150.191 104.628 1.00 37.18  ? 539  THR A OG1 1 
ATOM   3648  C  CG2 . THR A 1 564 ? 130.450 152.477 104.707 1.00 30.00  ? 539  THR A CG2 1 
ATOM   3649  N  N   . ASN A 1 565 ? 128.687 148.236 103.985 1.00 34.75  ? 540  ASN A N   1 
ATOM   3650  C  CA  . ASN A 1 565 ? 128.165 147.098 103.238 1.00 29.33  ? 540  ASN A CA  1 
ATOM   3651  C  C   . ASN A 1 565 ? 126.652 147.008 103.367 1.00 31.61  ? 540  ASN A C   1 
ATOM   3652  O  O   . ASN A 1 565 ? 125.950 146.740 102.383 1.00 35.56  ? 540  ASN A O   1 
ATOM   3653  C  CB  . ASN A 1 565 ? 128.819 145.806 103.721 1.00 29.10  ? 540  ASN A CB  1 
ATOM   3654  C  CG  . ASN A 1 565 ? 130.290 145.740 103.384 1.00 41.26  ? 540  ASN A CG  1 
ATOM   3655  O  OD1 . ASN A 1 565 ? 130.864 146.701 102.875 1.00 46.68  ? 540  ASN A OD1 1 
ATOM   3656  N  ND2 . ASN A 1 565 ? 130.913 144.602 103.668 1.00 40.82  ? 540  ASN A ND2 1 
ATOM   3657  N  N   . PHE A 1 566 ? 126.130 147.228 104.577 1.00 30.87  ? 541  PHE A N   1 
ATOM   3658  C  CA  . PHE A 1 566 ? 124.683 147.235 104.757 1.00 32.21  ? 541  PHE A CA  1 
ATOM   3659  C  C   . PHE A 1 566 ? 124.032 148.331 103.925 1.00 35.63  ? 541  PHE A C   1 
ATOM   3660  O  O   . PHE A 1 566 ? 122.983 148.114 103.309 1.00 42.27  ? 541  PHE A O   1 
ATOM   3661  C  CB  . PHE A 1 566 ? 124.330 147.409 106.233 1.00 35.25  ? 541  PHE A CB  1 
ATOM   3662  C  CG  . PHE A 1 566 ? 122.861 147.311 106.513 1.00 29.22  ? 541  PHE A CG  1 
ATOM   3663  C  CD1 . PHE A 1 566 ? 122.232 146.082 106.554 1.00 25.68  ? 541  PHE A CD1 1 
ATOM   3664  C  CD2 . PHE A 1 566 ? 122.108 148.451 106.721 1.00 31.35  ? 541  PHE A CD2 1 
ATOM   3665  C  CE1 . PHE A 1 566 ? 120.881 145.991 106.807 1.00 30.62  ? 541  PHE A CE1 1 
ATOM   3666  C  CE2 . PHE A 1 566 ? 120.757 148.366 106.973 1.00 37.51  ? 541  PHE A CE2 1 
ATOM   3667  C  CZ  . PHE A 1 566 ? 120.143 147.134 107.016 1.00 40.00  ? 541  PHE A CZ  1 
ATOM   3668  N  N   . ALA A 1 567 ? 124.639 149.518 103.898 1.00 28.86  ? 542  ALA A N   1 
ATOM   3669  C  CA  . ALA A 1 567 ? 124.088 150.606 103.096 1.00 24.17  ? 542  ALA A CA  1 
ATOM   3670  C  C   . ALA A 1 567 ? 124.134 150.276 101.609 1.00 31.44  ? 542  ALA A C   1 
ATOM   3671  O  O   . ALA A 1 567 ? 123.220 150.635 100.858 1.00 30.43  ? 542  ALA A O   1 
ATOM   3672  C  CB  . ALA A 1 567 ? 124.841 151.903 103.380 1.00 23.83  ? 542  ALA A CB  1 
ATOM   3673  N  N   . LYS A 1 568 ? 125.194 149.598 101.165 1.00 40.01  ? 543  LYS A N   1 
ATOM   3674  C  CA  . LYS A 1 568 ? 125.351 149.308 99.743  1.00 31.30  ? 543  LYS A CA  1 
ATOM   3675  C  C   . LYS A 1 568 ? 124.366 148.244 99.273  1.00 29.82  ? 543  LYS A C   1 
ATOM   3676  O  O   . LYS A 1 568 ? 123.717 148.406 98.234  1.00 31.15  ? 543  LYS A O   1 
ATOM   3677  C  CB  . LYS A 1 568 ? 126.785 148.869 99.450  1.00 25.26  ? 543  LYS A CB  1 
ATOM   3678  C  CG  . LYS A 1 568 ? 127.797 149.998 99.429  1.00 27.40  ? 543  LYS A CG  1 
ATOM   3679  C  CD  . LYS A 1 568 ? 129.211 149.455 99.535  1.00 26.71  ? 543  LYS A CD  1 
ATOM   3680  C  CE  . LYS A 1 568 ? 130.232 150.574 99.566  1.00 28.43  ? 543  LYS A CE  1 
ATOM   3681  N  NZ  . LYS A 1 568 ? 131.557 150.098 100.045 1.00 32.06  ? 543  LYS A NZ  1 
ATOM   3682  N  N   . THR A 1 569 ? 124.238 147.145 100.022 1.00 32.37  ? 544  THR A N   1 
ATOM   3683  C  CA  . THR A 1 569 ? 123.478 146.004 99.529  1.00 36.67  ? 544  THR A CA  1 
ATOM   3684  C  C   . THR A 1 569 ? 122.474 145.425 100.516 1.00 33.27  ? 544  THR A C   1 
ATOM   3685  O  O   . THR A 1 569 ? 121.767 144.477 100.160 1.00 38.43  ? 544  THR A O   1 
ATOM   3686  C  CB  . THR A 1 569 ? 124.429 144.879 99.094  1.00 34.97  ? 544  THR A CB  1 
ATOM   3687  O  OG1 . THR A 1 569 ? 123.699 143.903 98.341  1.00 35.82  ? 544  THR A OG1 1 
ATOM   3688  C  CG2 . THR A 1 569 ? 125.032 144.208 100.309 1.00 28.65  ? 544  THR A CG2 1 
ATOM   3689  N  N   . GLY A 1 570 ? 122.382 145.954 101.732 1.00 27.13  ? 545  GLY A N   1 
ATOM   3690  C  CA  . GLY A 1 570 ? 121.497 145.354 102.708 1.00 30.03  ? 545  GLY A CA  1 
ATOM   3691  C  C   . GLY A 1 570 ? 122.009 144.074 103.323 1.00 35.86  ? 545  GLY A C   1 
ATOM   3692  O  O   . GLY A 1 570 ? 121.251 143.388 104.014 1.00 39.67  ? 545  GLY A O   1 
ATOM   3693  N  N   . ASP A 1 571 ? 123.272 143.731 103.092 1.00 36.85  ? 546  ASP A N   1 
ATOM   3694  C  CA  . ASP A 1 571 ? 123.907 142.546 103.651 1.00 33.62  ? 546  ASP A CA  1 
ATOM   3695  C  C   . ASP A 1 571 ? 125.265 142.961 104.201 1.00 41.89  ? 546  ASP A C   1 
ATOM   3696  O  O   . ASP A 1 571 ? 126.127 143.422 103.443 1.00 58.23  ? 546  ASP A O   1 
ATOM   3697  C  CB  . ASP A 1 571 ? 124.044 141.455 102.586 1.00 36.15  ? 546  ASP A CB  1 
ATOM   3698  C  CG  . ASP A 1 571 ? 124.469 140.117 103.162 1.00 45.10  ? 546  ASP A CG  1 
ATOM   3699  O  OD1 . ASP A 1 571 ? 124.749 140.040 104.375 1.00 52.19  ? 546  ASP A OD1 1 
ATOM   3700  O  OD2 . ASP A 1 571 ? 124.523 139.134 102.395 1.00 48.23  ? 546  ASP A OD2 1 
ATOM   3701  N  N   . PRO A 1 572 ? 125.491 142.823 105.509 1.00 37.29  ? 547  PRO A N   1 
ATOM   3702  C  CA  . PRO A 1 572 ? 126.704 143.400 106.113 1.00 39.83  ? 547  PRO A CA  1 
ATOM   3703  C  C   . PRO A 1 572 ? 128.012 142.818 105.598 1.00 48.64  ? 547  PRO A C   1 
ATOM   3704  O  O   . PRO A 1 572 ? 129.062 143.438 105.803 1.00 51.47  ? 547  PRO A O   1 
ATOM   3705  C  CB  . PRO A 1 572 ? 126.519 143.110 107.607 1.00 32.93  ? 547  PRO A CB  1 
ATOM   3706  C  CG  . PRO A 1 572 ? 125.049 142.995 107.784 1.00 38.19  ? 547  PRO A CG  1 
ATOM   3707  C  CD  . PRO A 1 572 ? 124.541 142.353 106.530 1.00 39.43  ? 547  PRO A CD  1 
ATOM   3708  N  N   . ASN A 1 573 ? 127.999 141.654 104.951 1.00 48.03  ? 548  ASN A N   1 
ATOM   3709  C  CA  . ASN A 1 573 ? 129.236 141.010 104.533 1.00 48.68  ? 548  ASN A CA  1 
ATOM   3710  C  C   . ASN A 1 573 ? 129.334 140.752 103.035 1.00 49.90  ? 548  ASN A C   1 
ATOM   3711  O  O   . ASN A 1 573 ? 130.317 140.146 102.594 1.00 52.71  ? 548  ASN A O   1 
ATOM   3712  C  CB  . ASN A 1 573 ? 129.416 139.684 105.284 1.00 47.02  ? 548  ASN A CB  1 
ATOM   3713  C  CG  . ASN A 1 573 ? 128.113 138.933 105.456 1.00 44.26  ? 548  ASN A CG  1 
ATOM   3714  O  OD1 . ASN A 1 573 ? 127.112 139.500 105.890 1.00 38.68  ? 548  ASN A OD1 1 
ATOM   3715  N  ND2 . ASN A 1 573 ? 128.118 137.651 105.115 1.00 46.93  ? 548  ASN A ND2 1 
ATOM   3716  N  N   . GLN A 1 574 ? 128.352 141.189 102.235 1.00 50.16  ? 549  GLN A N   1 
ATOM   3717  C  CA  . GLN A 1 574 ? 128.344 140.799 100.824 1.00 50.58  ? 549  GLN A CA  1 
ATOM   3718  C  C   . GLN A 1 574 ? 129.390 141.542 99.999  1.00 56.41  ? 549  GLN A C   1 
ATOM   3719  O  O   . GLN A 1 574 ? 130.295 140.890 99.449  1.00 62.61  ? 549  GLN A O   1 
ATOM   3720  C  CB  . GLN A 1 574 ? 126.935 140.957 100.247 1.00 50.16  ? 549  GLN A CB  1 
ATOM   3721  N  N   . PRO A 1 575 ? 129.340 142.887 99.858  1.00 56.39  ? 550  PRO A N   1 
ATOM   3722  C  CA  . PRO A 1 575 ? 130.196 143.542 98.856  1.00 53.32  ? 550  PRO A CA  1 
ATOM   3723  C  C   . PRO A 1 575 ? 131.682 143.477 99.164  1.00 55.81  ? 550  PRO A C   1 
ATOM   3724  O  O   . PRO A 1 575 ? 132.473 143.007 98.340  1.00 57.69  ? 550  PRO A O   1 
ATOM   3725  C  CB  . PRO A 1 575 ? 129.704 144.998 98.866  1.00 48.34  ? 550  PRO A CB  1 
ATOM   3726  C  CG  . PRO A 1 575 ? 128.439 144.995 99.664  1.00 53.59  ? 550  PRO A CG  1 
ATOM   3727  C  CD  . PRO A 1 575 ? 128.592 143.882 100.639 1.00 51.31  ? 550  PRO A CD  1 
ATOM   3728  N  N   . VAL A 1 576 ? 132.073 143.941 100.346 1.00 63.90  ? 551  VAL A N   1 
ATOM   3729  C  CA  . VAL A 1 576 ? 133.475 144.095 100.712 1.00 65.72  ? 551  VAL A CA  1 
ATOM   3730  C  C   . VAL A 1 576 ? 133.793 143.074 101.803 1.00 65.90  ? 551  VAL A C   1 
ATOM   3731  O  O   . VAL A 1 576 ? 133.336 143.227 102.945 1.00 67.87  ? 551  VAL A O   1 
ATOM   3732  C  CB  . VAL A 1 576 ? 133.784 145.522 101.181 1.00 61.64  ? 551  VAL A CB  1 
ATOM   3733  C  CG1 . VAL A 1 576 ? 135.179 145.594 101.783 1.00 57.84  ? 551  VAL A CG1 1 
ATOM   3734  C  CG2 . VAL A 1 576 ? 133.645 146.500 100.025 1.00 60.28  ? 551  VAL A CG2 1 
ATOM   3735  N  N   . PRO A 1 577 ? 134.550 142.022 101.504 1.00 78.54  ? 552  PRO A N   1 
ATOM   3736  C  CA  . PRO A 1 577 ? 135.013 141.127 102.568 1.00 81.08  ? 552  PRO A CA  1 
ATOM   3737  C  C   . PRO A 1 577 ? 135.983 141.840 103.494 1.00 79.98  ? 552  PRO A C   1 
ATOM   3738  O  O   . PRO A 1 577 ? 136.673 142.785 103.103 1.00 78.41  ? 552  PRO A O   1 
ATOM   3739  C  CB  . PRO A 1 577 ? 135.701 139.989 101.805 1.00 82.55  ? 552  PRO A CB  1 
ATOM   3740  C  CG  . PRO A 1 577 ? 136.055 140.577 100.478 1.00 79.30  ? 552  PRO A CG  1 
ATOM   3741  C  CD  . PRO A 1 577 ? 134.978 141.571 100.169 1.00 77.44  ? 552  PRO A CD  1 
ATOM   3742  N  N   . GLN A 1 578 ? 136.023 141.379 104.740 1.00 75.98  ? 553  GLN A N   1 
ATOM   3743  C  CA  . GLN A 1 578 ? 136.863 141.992 105.763 1.00 75.78  ? 553  GLN A CA  1 
ATOM   3744  C  C   . GLN A 1 578 ? 138.343 141.909 105.401 1.00 75.07  ? 553  GLN A C   1 
ATOM   3745  O  O   . GLN A 1 578 ? 139.037 140.973 105.794 1.00 79.92  ? 553  GLN A O   1 
ATOM   3746  C  CB  . GLN A 1 578 ? 136.620 141.329 107.119 1.00 76.98  ? 553  GLN A CB  1 
ATOM   3747  C  CG  . GLN A 1 578 ? 135.224 141.548 107.671 1.00 75.63  ? 553  GLN A CG  1 
ATOM   3748  C  CD  . GLN A 1 578 ? 134.944 143.002 107.983 1.00 74.40  ? 553  GLN A CD  1 
ATOM   3749  O  OE1 . GLN A 1 578 ? 135.371 143.519 109.013 1.00 76.77  ? 553  GLN A OE1 1 
ATOM   3750  N  NE2 . GLN A 1 578 ? 134.223 143.669 107.092 1.00 72.92  ? 553  GLN A NE2 1 
ATOM   3751  N  N   . ARG A 1 589 ? 140.223 137.990 114.845 1.00 96.14  ? 564  ARG A N   1 
ATOM   3752  C  CA  . ARG A 1 589 ? 139.477 136.958 114.136 1.00 96.64  ? 564  ARG A CA  1 
ATOM   3753  C  C   . ARG A 1 589 ? 138.174 137.516 113.576 1.00 97.02  ? 564  ARG A C   1 
ATOM   3754  O  O   . ARG A 1 589 ? 137.099 137.269 114.119 1.00 97.06  ? 564  ARG A O   1 
ATOM   3755  C  CB  . ARG A 1 589 ? 139.188 135.774 115.061 1.00 94.83  ? 564  ARG A CB  1 
ATOM   3756  N  N   . PHE A 1 590 ? 138.278 138.270 112.480 1.00 108.20 ? 565  PHE A N   1 
ATOM   3757  C  CA  . PHE A 1 590 ? 137.118 138.903 111.869 1.00 109.93 ? 565  PHE A CA  1 
ATOM   3758  C  C   . PHE A 1 590 ? 136.922 138.562 110.399 1.00 109.60 ? 565  PHE A C   1 
ATOM   3759  O  O   . PHE A 1 590 ? 135.917 138.990 109.820 1.00 107.43 ? 565  PHE A O   1 
ATOM   3760  C  CB  . PHE A 1 590 ? 137.203 140.431 112.011 1.00 107.19 ? 565  PHE A CB  1 
ATOM   3761  N  N   . GLU A 1 591 ? 137.839 137.822 109.775 1.00 117.61 ? 566  GLU A N   1 
ATOM   3762  C  CA  . GLU A 1 591 ? 137.714 137.510 108.357 1.00 116.52 ? 566  GLU A CA  1 
ATOM   3763  C  C   . GLU A 1 591 ? 136.815 136.310 108.085 1.00 115.45 ? 566  GLU A C   1 
ATOM   3764  O  O   . GLU A 1 591 ? 136.275 136.199 106.979 1.00 115.59 ? 566  GLU A O   1 
ATOM   3765  C  CB  . GLU A 1 591 ? 139.094 137.254 107.744 1.00 116.43 ? 566  GLU A CB  1 
ATOM   3766  C  CG  . GLU A 1 591 ? 140.048 138.440 107.801 1.00 116.35 ? 566  GLU A CG  1 
ATOM   3767  C  CD  . GLU A 1 591 ? 140.759 138.563 109.135 1.00 117.92 ? 566  GLU A CD  1 
ATOM   3768  O  OE1 . GLU A 1 591 ? 140.984 137.523 109.790 1.00 118.14 ? 566  GLU A OE1 1 
ATOM   3769  O  OE2 . GLU A 1 591 ? 141.097 139.699 109.528 1.00 117.61 ? 566  GLU A OE2 1 
ATOM   3770  N  N   . GLU A 1 592 ? 136.639 135.416 109.058 1.00 107.28 ? 567  GLU A N   1 
ATOM   3771  C  CA  . GLU A 1 592 ? 135.914 134.170 108.845 1.00 107.49 ? 567  GLU A CA  1 
ATOM   3772  C  C   . GLU A 1 592 ? 134.588 134.113 109.595 1.00 107.07 ? 567  GLU A C   1 
ATOM   3773  O  O   . GLU A 1 592 ? 134.004 133.031 109.716 1.00 107.63 ? 567  GLU A O   1 
ATOM   3774  C  CB  . GLU A 1 592 ? 136.790 132.978 109.239 1.00 108.79 ? 567  GLU A CB  1 
ATOM   3775  C  CG  . GLU A 1 592 ? 137.015 132.828 110.737 1.00 108.02 ? 567  GLU A CG  1 
ATOM   3776  C  CD  . GLU A 1 592 ? 138.129 133.716 111.255 1.00 109.27 ? 567  GLU A CD  1 
ATOM   3777  O  OE1 . GLU A 1 592 ? 138.785 134.391 110.434 1.00 109.84 ? 567  GLU A OE1 1 
ATOM   3778  O  OE2 . GLU A 1 592 ? 138.350 133.738 112.484 1.00 109.53 ? 567  GLU A OE2 1 
ATOM   3779  N  N   . VAL A 1 593 ? 134.093 135.242 110.091 1.00 78.93  ? 568  VAL A N   1 
ATOM   3780  C  CA  . VAL A 1 593 ? 132.815 135.296 110.791 1.00 74.12  ? 568  VAL A CA  1 
ATOM   3781  C  C   . VAL A 1 593 ? 131.749 135.743 109.801 1.00 70.15  ? 568  VAL A C   1 
ATOM   3782  O  O   . VAL A 1 593 ? 131.881 136.794 109.163 1.00 70.51  ? 568  VAL A O   1 
ATOM   3783  C  CB  . VAL A 1 593 ? 132.877 136.234 112.007 1.00 71.74  ? 568  VAL A CB  1 
ATOM   3784  C  CG1 . VAL A 1 593 ? 133.471 135.509 113.201 1.00 71.89  ? 568  VAL A CG1 1 
ATOM   3785  C  CG2 . VAL A 1 593 ? 133.690 137.474 111.682 1.00 72.49  ? 568  VAL A CG2 1 
ATOM   3786  N  N   . VAL A 1 594 ? 130.697 134.943 109.666 1.00 45.96  ? 569  VAL A N   1 
ATOM   3787  C  CA  . VAL A 1 594 ? 129.597 135.233 108.755 1.00 47.47  ? 569  VAL A CA  1 
ATOM   3788  C  C   . VAL A 1 594 ? 128.428 135.734 109.591 1.00 52.51  ? 569  VAL A C   1 
ATOM   3789  O  O   . VAL A 1 594 ? 127.806 134.964 110.331 1.00 56.21  ? 569  VAL A O   1 
ATOM   3790  C  CB  . VAL A 1 594 ? 129.209 134.000 107.927 1.00 50.45  ? 569  VAL A CB  1 
ATOM   3791  C  CG1 . VAL A 1 594 ? 127.881 134.226 107.223 1.00 47.14  ? 569  VAL A CG1 1 
ATOM   3792  C  CG2 . VAL A 1 594 ? 130.299 133.675 106.922 1.00 52.64  ? 569  VAL A CG2 1 
ATOM   3793  N  N   . TRP A 1 595 ? 128.128 137.025 109.479 1.00 47.11  ? 570  TRP A N   1 
ATOM   3794  C  CA  . TRP A 1 595 ? 127.012 137.615 110.209 1.00 39.66  ? 570  TRP A CA  1 
ATOM   3795  C  C   . TRP A 1 595 ? 125.706 137.095 109.625 1.00 42.75  ? 570  TRP A C   1 
ATOM   3796  O  O   . TRP A 1 595 ? 125.302 137.498 108.529 1.00 44.35  ? 570  TRP A O   1 
ATOM   3797  C  CB  . TRP A 1 595 ? 127.085 139.137 110.136 1.00 38.84  ? 570  TRP A CB  1 
ATOM   3798  C  CG  . TRP A 1 595 ? 126.203 139.843 111.119 1.00 39.17  ? 570  TRP A CG  1 
ATOM   3799  C  CD1 . TRP A 1 595 ? 125.213 139.294 111.878 1.00 39.19  ? 570  TRP A CD1 1 
ATOM   3800  C  CD2 . TRP A 1 595 ? 126.235 141.235 111.449 1.00 39.20  ? 570  TRP A CD2 1 
ATOM   3801  N  NE1 . TRP A 1 595 ? 124.625 140.258 112.658 1.00 44.37  ? 570  TRP A NE1 1 
ATOM   3802  C  CE2 . TRP A 1 595 ? 125.236 141.459 112.413 1.00 42.19  ? 570  TRP A CE2 1 
ATOM   3803  C  CE3 . TRP A 1 595 ? 127.012 142.314 111.022 1.00 41.00  ? 570  TRP A CE3 1 
ATOM   3804  C  CZ2 . TRP A 1 595 ? 124.993 142.715 112.955 1.00 43.33  ? 570  TRP A CZ2 1 
ATOM   3805  C  CZ3 . TRP A 1 595 ? 126.769 143.560 111.562 1.00 40.01  ? 570  TRP A CZ3 1 
ATOM   3806  C  CH2 . TRP A 1 595 ? 125.769 143.751 112.518 1.00 39.01  ? 570  TRP A CH2 1 
ATOM   3807  N  N   . SER A 1 596 ? 125.045 136.202 110.352 1.00 34.08  ? 571  SER A N   1 
ATOM   3808  C  CA  . SER A 1 596 ? 123.825 135.571 109.877 1.00 36.15  ? 571  SER A CA  1 
ATOM   3809  C  C   . SER A 1 596 ? 122.600 136.379 110.297 1.00 35.85  ? 571  SER A C   1 
ATOM   3810  O  O   . SER A 1 596 ? 122.666 137.262 111.154 1.00 41.20  ? 571  SER A O   1 
ATOM   3811  C  CB  . SER A 1 596 ? 123.730 134.140 110.401 1.00 36.58  ? 571  SER A CB  1 
ATOM   3812  O  OG  . SER A 1 596 ? 124.042 134.085 111.781 1.00 31.90  ? 571  SER A OG  1 
ATOM   3813  N  N   . LYS A 1 597 ? 121.468 136.061 109.675 1.00 30.17  ? 572  LYS A N   1 
ATOM   3814  C  CA  . LYS A 1 597 ? 120.232 136.781 109.931 1.00 27.59  ? 572  LYS A CA  1 
ATOM   3815  C  C   . LYS A 1 597 ? 119.753 136.543 111.361 1.00 31.52  ? 572  LYS A C   1 
ATOM   3816  O  O   . LYS A 1 597 ? 120.261 135.685 112.088 1.00 42.06  ? 572  LYS A O   1 
ATOM   3817  C  CB  . LYS A 1 597 ? 119.149 136.355 108.942 1.00 28.55  ? 572  LYS A CB  1 
ATOM   3818  C  CG  . LYS A 1 597 ? 119.260 137.001 107.576 1.00 36.30  ? 572  LYS A CG  1 
ATOM   3819  C  CD  . LYS A 1 597 ? 117.890 137.208 106.956 1.00 35.63  ? 572  LYS A CD  1 
ATOM   3820  C  CE  . LYS A 1 597 ? 118.006 137.664 105.514 1.00 37.62  ? 572  LYS A CE  1 
ATOM   3821  N  NZ  . LYS A 1 597 ? 118.708 136.655 104.674 1.00 38.81  ? 572  LYS A NZ  1 
ATOM   3822  N  N   . PHE A 1 598 ? 118.753 137.321 111.759 1.00 31.55  ? 573  PHE A N   1 
ATOM   3823  C  CA  . PHE A 1 598 ? 118.122 137.211 113.071 1.00 31.26  ? 573  PHE A CA  1 
ATOM   3824  C  C   . PHE A 1 598 ? 116.763 136.550 112.858 1.00 31.07  ? 573  PHE A C   1 
ATOM   3825  O  O   . PHE A 1 598 ? 115.757 137.223 112.634 1.00 33.81  ? 573  PHE A O   1 
ATOM   3826  C  CB  . PHE A 1 598 ? 117.991 138.583 113.735 1.00 35.92  ? 573  PHE A CB  1 
ATOM   3827  C  CG  . PHE A 1 598 ? 117.366 138.549 115.104 1.00 29.76  ? 573  PHE A CG  1 
ATOM   3828  C  CD1 . PHE A 1 598 ? 115.994 138.626 115.262 1.00 25.04  ? 573  PHE A CD1 1 
ATOM   3829  C  CD2 . PHE A 1 598 ? 118.156 138.464 116.234 1.00 35.89  ? 573  PHE A CD2 1 
ATOM   3830  C  CE1 . PHE A 1 598 ? 115.423 138.601 116.516 1.00 26.68  ? 573  PHE A CE1 1 
ATOM   3831  C  CE2 . PHE A 1 598 ? 117.590 138.443 117.491 1.00 31.11  ? 573  PHE A CE2 1 
ATOM   3832  C  CZ  . PHE A 1 598 ? 116.222 138.510 117.631 1.00 31.18  ? 573  PHE A CZ  1 
ATOM   3833  N  N   . ASN A 1 599 ? 116.745 135.223 112.903 1.00 36.40  ? 574  ASN A N   1 
ATOM   3834  C  CA  . ASN A 1 599 ? 115.491 134.492 112.851 1.00 32.25  ? 574  ASN A CA  1 
ATOM   3835  C  C   . ASN A 1 599 ? 114.832 134.499 114.224 1.00 35.21  ? 574  ASN A C   1 
ATOM   3836  O  O   . ASN A 1 599 ? 115.503 134.513 115.258 1.00 40.73  ? 574  ASN A O   1 
ATOM   3837  C  CB  . ASN A 1 599 ? 115.721 133.055 112.383 1.00 25.79  ? 574  ASN A CB  1 
ATOM   3838  N  N   . SER A 1 600 ? 113.499 134.503 114.227 1.00 32.42  ? 575  SER A N   1 
ATOM   3839  C  CA  . SER A 1 600 ? 112.781 134.526 115.496 1.00 25.23  ? 575  SER A CA  1 
ATOM   3840  C  C   . SER A 1 600 ? 112.970 133.231 116.276 1.00 36.87  ? 575  SER A C   1 
ATOM   3841  O  O   . SER A 1 600 ? 113.019 133.257 117.511 1.00 35.95  ? 575  SER A O   1 
ATOM   3842  C  CB  . SER A 1 600 ? 111.296 134.787 115.258 1.00 25.54  ? 575  SER A CB  1 
ATOM   3843  O  OG  . SER A 1 600 ? 110.577 134.766 116.478 1.00 27.36  ? 575  SER A OG  1 
ATOM   3844  N  N   . LYS A 1 601 ? 113.073 132.096 115.583 1.00 37.76  ? 576  LYS A N   1 
ATOM   3845  C  CA  . LYS A 1 601 ? 113.203 130.817 116.275 1.00 28.47  ? 576  LYS A CA  1 
ATOM   3846  C  C   . LYS A 1 601 ? 114.565 130.688 116.951 1.00 41.18  ? 576  LYS A C   1 
ATOM   3847  O  O   . LYS A 1 601 ? 114.648 130.332 118.133 1.00 47.46  ? 576  LYS A O   1 
ATOM   3848  C  CB  . LYS A 1 601 ? 112.960 129.669 115.297 1.00 29.58  ? 576  LYS A CB  1 
ATOM   3849  C  CG  . LYS A 1 601 ? 113.036 128.289 115.924 1.00 37.30  ? 576  LYS A CG  1 
ATOM   3850  C  CD  . LYS A 1 601 ? 112.860 127.201 114.877 1.00 39.60  ? 576  LYS A CD  1 
ATOM   3851  C  CE  . LYS A 1 601 ? 113.058 125.820 115.476 1.00 37.86  ? 576  LYS A CE  1 
ATOM   3852  N  NZ  . LYS A 1 601 ? 114.390 125.687 116.124 1.00 39.67  ? 576  LYS A NZ  1 
ATOM   3853  N  N   . GLU A 1 602 ? 115.646 130.975 116.225 1.00 44.63  ? 577  GLU A N   1 
ATOM   3854  C  CA  . GLU A 1 602 ? 116.984 131.061 116.806 1.00 37.73  ? 577  GLU A CA  1 
ATOM   3855  C  C   . GLU A 1 602 ? 117.486 132.488 116.622 1.00 38.11  ? 577  GLU A C   1 
ATOM   3856  O  O   . GLU A 1 602 ? 117.746 132.924 115.495 1.00 48.33  ? 577  GLU A O   1 
ATOM   3857  C  CB  . GLU A 1 602 ? 117.947 130.038 116.192 1.00 28.23  ? 577  GLU A CB  1 
ATOM   3858  C  CG  . GLU A 1 602 ? 118.090 130.058 114.672 1.00 44.45  ? 577  GLU A CG  1 
ATOM   3859  C  CD  . GLU A 1 602 ? 116.997 129.294 113.954 1.00 50.06  ? 577  GLU A CD  1 
ATOM   3860  O  OE1 . GLU A 1 602 ? 115.885 129.179 114.504 1.00 50.14  ? 577  GLU A OE1 1 
ATOM   3861  O  OE2 . GLU A 1 602 ? 117.253 128.804 112.834 1.00 46.61  ? 577  GLU A OE2 1 
ATOM   3862  N  N   . LYS A 1 603 ? 117.620 133.216 117.730 1.00 26.00  ? 578  LYS A N   1 
ATOM   3863  C  CA  . LYS A 1 603 ? 117.897 134.651 117.694 1.00 30.63  ? 578  LYS A CA  1 
ATOM   3864  C  C   . LYS A 1 603 ? 119.402 134.891 117.567 1.00 34.30  ? 578  LYS A C   1 
ATOM   3865  O  O   . LYS A 1 603 ? 120.064 135.432 118.454 1.00 45.82  ? 578  LYS A O   1 
ATOM   3866  C  CB  . LYS A 1 603 ? 117.325 135.324 118.933 1.00 36.17  ? 578  LYS A CB  1 
ATOM   3867  C  CG  . LYS A 1 603 ? 115.939 134.834 119.312 1.00 35.42  ? 578  LYS A CG  1 
ATOM   3868  C  CD  . LYS A 1 603 ? 115.256 135.797 120.265 1.00 33.74  ? 578  LYS A CD  1 
ATOM   3869  C  CE  . LYS A 1 603 ? 114.156 135.105 121.047 1.00 27.67  ? 578  LYS A CE  1 
ATOM   3870  N  NZ  . LYS A 1 603 ? 113.221 134.375 120.152 1.00 28.89  ? 578  LYS A NZ  1 
ATOM   3871  N  N   . GLN A 1 604 ? 119.939 134.486 116.420 1.00 37.98  ? 579  GLN A N   1 
ATOM   3872  C  CA  . GLN A 1 604 ? 121.362 134.646 116.161 1.00 34.04  ? 579  GLN A CA  1 
ATOM   3873  C  C   . GLN A 1 604 ? 121.732 136.119 116.037 1.00 34.30  ? 579  GLN A C   1 
ATOM   3874  O  O   . GLN A 1 604 ? 120.933 136.952 115.603 1.00 39.26  ? 579  GLN A O   1 
ATOM   3875  C  CB  . GLN A 1 604 ? 121.760 133.905 114.887 1.00 31.58  ? 579  GLN A CB  1 
ATOM   3876  C  CG  . GLN A 1 604 ? 121.813 132.400 115.039 1.00 42.96  ? 579  GLN A CG  1 
ATOM   3877  C  CD  . GLN A 1 604 ? 122.344 131.714 113.801 1.00 45.75  ? 579  GLN A CD  1 
ATOM   3878  O  OE1 . GLN A 1 604 ? 121.895 131.985 112.689 1.00 42.61  ? 579  GLN A OE1 1 
ATOM   3879  N  NE2 . GLN A 1 604 ? 123.308 130.822 113.988 1.00 45.00  ? 579  GLN A NE2 1 
ATOM   3880  N  N   . TYR A 1 605 ? 122.964 136.434 116.421 1.00 29.92  ? 580  TYR A N   1 
ATOM   3881  C  CA  . TYR A 1 605 ? 123.478 137.795 116.344 1.00 32.17  ? 580  TYR A CA  1 
ATOM   3882  C  C   . TYR A 1 605 ? 124.995 137.723 116.244 1.00 36.57  ? 580  TYR A C   1 
ATOM   3883  O  O   . TYR A 1 605 ? 125.585 136.640 116.240 1.00 50.64  ? 580  TYR A O   1 
ATOM   3884  C  CB  . TYR A 1 605 ? 123.026 138.624 117.550 1.00 33.54  ? 580  TYR A CB  1 
ATOM   3885  C  CG  . TYR A 1 605 ? 123.654 138.214 118.861 1.00 24.31  ? 580  TYR A CG  1 
ATOM   3886  C  CD1 . TYR A 1 605 ? 123.095 137.213 119.637 1.00 31.28  ? 580  TYR A CD1 1 
ATOM   3887  C  CD2 . TYR A 1 605 ? 124.797 138.841 119.331 1.00 39.24  ? 580  TYR A CD2 1 
ATOM   3888  C  CE1 . TYR A 1 605 ? 123.664 136.839 120.837 1.00 38.79  ? 580  TYR A CE1 1 
ATOM   3889  C  CE2 . TYR A 1 605 ? 125.372 138.475 120.529 1.00 35.74  ? 580  TYR A CE2 1 
ATOM   3890  C  CZ  . TYR A 1 605 ? 124.802 137.475 121.278 1.00 33.64  ? 580  TYR A CZ  1 
ATOM   3891  O  OH  . TYR A 1 605 ? 125.374 137.108 122.472 1.00 42.12  ? 580  TYR A OH  1 
ATOM   3892  N  N   . LEU A 1 606 ? 125.628 138.890 116.161 1.00 31.70  ? 581  LEU A N   1 
ATOM   3893  C  CA  . LEU A 1 606 ? 127.079 138.994 116.099 1.00 35.52  ? 581  LEU A CA  1 
ATOM   3894  C  C   . LEU A 1 606 ? 127.579 139.736 117.327 1.00 32.30  ? 581  LEU A C   1 
ATOM   3895  O  O   . LEU A 1 606 ? 127.098 140.831 117.635 1.00 48.15  ? 581  LEU A O   1 
ATOM   3896  C  CB  . LEU A 1 606 ? 127.532 139.711 114.826 1.00 45.08  ? 581  LEU A CB  1 
ATOM   3897  C  CG  . LEU A 1 606 ? 129.044 139.868 114.654 1.00 41.67  ? 581  LEU A CG  1 
ATOM   3898  C  CD1 . LEU A 1 606 ? 129.686 138.533 114.326 1.00 42.70  ? 581  LEU A CD1 1 
ATOM   3899  C  CD2 . LEU A 1 606 ? 129.356 140.885 113.574 1.00 42.67  ? 581  LEU A CD2 1 
ATOM   3900  N  N   . HIS A 1 607 ? 128.548 139.141 118.022 1.00 28.47  ? 582  HIS A N   1 
ATOM   3901  C  CA  . HIS A 1 607 ? 129.102 139.716 119.246 1.00 32.21  ? 582  HIS A CA  1 
ATOM   3902  C  C   . HIS A 1 607 ? 130.274 140.616 118.867 1.00 39.38  ? 582  HIS A C   1 
ATOM   3903  O  O   . HIS A 1 607 ? 131.446 140.267 119.013 1.00 48.16  ? 582  HIS A O   1 
ATOM   3904  C  CB  . HIS A 1 607 ? 129.516 138.609 120.208 1.00 37.92  ? 582  HIS A CB  1 
ATOM   3905  C  CG  . HIS A 1 607 ? 130.116 139.106 121.486 1.00 43.24  ? 582  HIS A CG  1 
ATOM   3906  N  ND1 . HIS A 1 607 ? 131.414 139.562 121.570 1.00 42.85  ? 582  HIS A ND1 1 
ATOM   3907  C  CD2 . HIS A 1 607 ? 129.601 139.207 122.733 1.00 44.78  ? 582  HIS A CD2 1 
ATOM   3908  C  CE1 . HIS A 1 607 ? 131.670 139.928 122.813 1.00 42.60  ? 582  HIS A CE1 1 
ATOM   3909  N  NE2 . HIS A 1 607 ? 130.586 139.722 123.539 1.00 46.90  ? 582  HIS A NE2 1 
ATOM   3910  N  N   . ILE A 1 608 ? 129.936 141.805 118.362 1.00 30.78  ? 583  ILE A N   1 
ATOM   3911  C  CA  . ILE A 1 608 ? 130.953 142.737 117.889 1.00 27.28  ? 583  ILE A CA  1 
ATOM   3912  C  C   . ILE A 1 608 ? 131.871 143.121 119.039 1.00 29.15  ? 583  ILE A C   1 
ATOM   3913  O  O   . ILE A 1 608 ? 131.414 143.474 120.133 1.00 38.68  ? 583  ILE A O   1 
ATOM   3914  C  CB  . ILE A 1 608 ? 130.295 143.973 117.261 1.00 29.77  ? 583  ILE A CB  1 
ATOM   3915  C  CG1 . ILE A 1 608 ? 129.612 143.600 115.946 1.00 33.55  ? 583  ILE A CG1 1 
ATOM   3916  C  CG2 . ILE A 1 608 ? 131.324 145.062 117.020 1.00 24.69  ? 583  ILE A CG2 1 
ATOM   3917  C  CD1 . ILE A 1 608 ? 129.142 144.788 115.146 1.00 29.85  ? 583  ILE A CD1 1 
ATOM   3918  N  N   . GLY A 1 609 ? 133.174 143.054 118.794 1.00 38.44  ? 584  GLY A N   1 
ATOM   3919  C  CA  . GLY A 1 609 ? 134.145 143.362 119.826 1.00 40.56  ? 584  GLY A CA  1 
ATOM   3920  C  C   . GLY A 1 609 ? 135.529 142.922 119.395 1.00 45.81  ? 584  GLY A C   1 
ATOM   3921  O  O   . GLY A 1 609 ? 135.797 142.751 118.205 1.00 47.18  ? 584  GLY A O   1 
ATOM   3922  N  N   . LEU A 1 610 ? 136.405 142.745 120.386 1.00 48.82  ? 585  LEU A N   1 
ATOM   3923  C  CA  . LEU A 1 610 ? 137.761 142.296 120.094 1.00 49.28  ? 585  LEU A CA  1 
ATOM   3924  C  C   . LEU A 1 610 ? 137.808 140.833 119.678 1.00 50.07  ? 585  LEU A C   1 
ATOM   3925  O  O   . LEU A 1 610 ? 138.741 140.432 118.974 1.00 51.05  ? 585  LEU A O   1 
ATOM   3926  C  CB  . LEU A 1 610 ? 138.663 142.526 121.307 1.00 49.82  ? 585  LEU A CB  1 
ATOM   3927  C  CG  . LEU A 1 610 ? 139.165 143.959 121.491 1.00 52.84  ? 585  LEU A CG  1 
ATOM   3928  C  CD1 . LEU A 1 610 ? 140.282 144.010 122.521 1.00 52.60  ? 585  LEU A CD1 1 
ATOM   3929  C  CD2 . LEU A 1 610 ? 139.627 144.541 120.163 1.00 49.79  ? 585  LEU A CD2 1 
ATOM   3930  N  N   . LYS A 1 611 ? 136.831 140.030 120.092 1.00 47.11  ? 586  LYS A N   1 
ATOM   3931  C  CA  . LYS A 1 611 ? 136.748 138.616 119.730 1.00 47.02  ? 586  LYS A CA  1 
ATOM   3932  C  C   . LYS A 1 611 ? 135.350 138.322 119.203 1.00 46.06  ? 586  LYS A C   1 
ATOM   3933  O  O   . LYS A 1 611 ? 134.533 137.692 119.885 1.00 44.10  ? 586  LYS A O   1 
ATOM   3934  C  CB  . LYS A 1 611 ? 137.087 137.723 120.924 1.00 41.99  ? 586  LYS A CB  1 
ATOM   3935  N  N   . PRO A 1 612 ? 135.039 138.772 117.990 1.00 43.42  ? 587  PRO A N   1 
ATOM   3936  C  CA  . PRO A 1 612 ? 133.688 138.576 117.457 1.00 45.99  ? 587  PRO A CA  1 
ATOM   3937  C  C   . PRO A 1 612 ? 133.380 137.110 117.199 1.00 45.72  ? 587  PRO A C   1 
ATOM   3938  O  O   . PRO A 1 612 ? 134.253 136.318 116.839 1.00 48.57  ? 587  PRO A O   1 
ATOM   3939  C  CB  . PRO A 1 612 ? 133.702 139.378 116.152 1.00 43.99  ? 587  PRO A CB  1 
ATOM   3940  C  CG  . PRO A 1 612 ? 135.129 139.396 115.746 1.00 44.66  ? 587  PRO A CG  1 
ATOM   3941  C  CD  . PRO A 1 612 ? 135.923 139.441 117.021 1.00 42.29  ? 587  PRO A CD  1 
ATOM   3942  N  N   . ARG A 1 613 ? 132.109 136.760 117.386 1.00 43.39  ? 588  ARG A N   1 
ATOM   3943  C  CA  . ARG A 1 613 ? 131.620 135.416 117.117 1.00 43.86  ? 588  ARG A CA  1 
ATOM   3944  C  C   . ARG A 1 613 ? 130.103 135.462 117.041 1.00 42.78  ? 588  ARG A C   1 
ATOM   3945  O  O   . ARG A 1 613 ? 129.456 136.230 117.757 1.00 44.43  ? 588  ARG A O   1 
ATOM   3946  C  CB  . ARG A 1 613 ? 132.072 134.418 118.189 1.00 45.85  ? 588  ARG A CB  1 
ATOM   3947  C  CG  . ARG A 1 613 ? 131.746 134.836 119.611 1.00 47.00  ? 588  ARG A CG  1 
ATOM   3948  C  CD  . ARG A 1 613 ? 132.443 133.942 120.622 1.00 44.56  ? 588  ARG A CD  1 
ATOM   3949  N  NE  . ARG A 1 613 ? 132.440 134.523 121.959 1.00 46.33  ? 588  ARG A NE  1 
ATOM   3950  C  CZ  . ARG A 1 613 ? 133.234 135.511 122.349 1.00 52.69  ? 588  ARG A CZ  1 
ATOM   3951  N  NH1 . ARG A 1 613 ? 134.119 136.051 121.528 1.00 50.99  ? 588  ARG A NH1 1 
ATOM   3952  N  NH2 . ARG A 1 613 ? 133.139 135.967 123.594 1.00 49.65  ? 588  ARG A NH2 1 
ATOM   3953  N  N   . VAL A 1 614 ? 129.543 134.631 116.164 1.00 32.93  ? 589  VAL A N   1 
ATOM   3954  C  CA  . VAL A 1 614 ? 128.099 134.591 115.945 1.00 28.68  ? 589  VAL A CA  1 
ATOM   3955  C  C   . VAL A 1 614 ? 127.493 133.718 117.040 1.00 29.85  ? 589  VAL A C   1 
ATOM   3956  O  O   . VAL A 1 614 ? 127.525 132.489 116.960 1.00 43.85  ? 589  VAL A O   1 
ATOM   3957  C  CB  . VAL A 1 614 ? 127.749 134.075 114.549 1.00 34.61  ? 589  VAL A CB  1 
ATOM   3958  C  CG1 . VAL A 1 614 ? 126.242 134.016 114.366 1.00 33.93  ? 589  VAL A CG1 1 
ATOM   3959  C  CG2 . VAL A 1 614 ? 128.380 134.962 113.493 1.00 37.40  ? 589  VAL A CG2 1 
ATOM   3960  N  N   . ARG A 1 615 ? 126.936 134.351 118.068 1.00 29.06  ? 590  ARG A N   1 
ATOM   3961  C  CA  . ARG A 1 615 ? 126.346 133.629 119.186 1.00 35.33  ? 590  ARG A CA  1 
ATOM   3962  C  C   . ARG A 1 615 ? 124.925 133.196 118.826 1.00 40.65  ? 590  ARG A C   1 
ATOM   3963  O  O   . ARG A 1 615 ? 124.481 133.322 117.681 1.00 42.45  ? 590  ARG A O   1 
ATOM   3964  C  CB  . ARG A 1 615 ? 126.395 134.484 120.447 1.00 38.58  ? 590  ARG A CB  1 
ATOM   3965  C  CG  . ARG A 1 615 ? 127.790 134.626 121.025 1.00 42.67  ? 590  ARG A CG  1 
ATOM   3966  C  CD  . ARG A 1 615 ? 127.769 134.581 122.540 1.00 47.22  ? 590  ARG A CD  1 
ATOM   3967  N  NE  . ARG A 1 615 ? 129.085 134.278 123.090 1.00 50.71  ? 590  ARG A NE  1 
ATOM   3968  C  CZ  . ARG A 1 615 ? 129.550 134.766 124.232 1.00 49.51  ? 590  ARG A CZ  1 
ATOM   3969  N  NH1 . ARG A 1 615 ? 128.833 135.593 124.973 1.00 46.20  ? 590  ARG A NH1 1 
ATOM   3970  N  NH2 . ARG A 1 615 ? 130.766 134.414 124.639 1.00 49.02  ? 590  ARG A NH2 1 
ATOM   3971  N  N   . ASP A 1 616 ? 124.187 132.682 119.808 1.00 39.89  ? 591  ASP A N   1 
ATOM   3972  C  CA  . ASP A 1 616 ? 122.892 132.061 119.560 1.00 34.88  ? 591  ASP A CA  1 
ATOM   3973  C  C   . ASP A 1 616 ? 121.738 132.804 120.212 1.00 40.35  ? 591  ASP A C   1 
ATOM   3974  O  O   . ASP A 1 616 ? 120.707 133.021 119.566 1.00 45.56  ? 591  ASP A O   1 
ATOM   3975  C  CB  . ASP A 1 616 ? 122.910 130.603 120.043 1.00 40.47  ? 591  ASP A CB  1 
ATOM   3976  C  CG  . ASP A 1 616 ? 121.977 129.714 119.247 1.00 49.05  ? 591  ASP A CG  1 
ATOM   3977  O  OD1 . ASP A 1 616 ? 122.105 129.676 118.005 1.00 49.50  ? 591  ASP A OD1 1 
ATOM   3978  O  OD2 . ASP A 1 616 ? 121.114 129.053 119.863 1.00 51.40  ? 591  ASP A OD2 1 
ATOM   3979  N  N   . ASN A 1 617 ? 121.866 133.185 121.481 1.00 44.11  ? 592  ASN A N   1 
ATOM   3980  C  CA  . ASN A 1 617 ? 120.797 133.887 122.179 1.00 37.92  ? 592  ASN A CA  1 
ATOM   3981  C  C   . ASN A 1 617 ? 121.414 134.892 123.138 1.00 42.26  ? 592  ASN A C   1 
ATOM   3982  O  O   . ASN A 1 617 ? 122.247 134.522 123.970 1.00 50.42  ? 592  ASN A O   1 
ATOM   3983  C  CB  . ASN A 1 617 ? 119.896 132.911 122.943 1.00 39.37  ? 592  ASN A CB  1 
ATOM   3984  C  CG  . ASN A 1 617 ? 118.857 132.258 122.056 1.00 45.94  ? 592  ASN A CG  1 
ATOM   3985  O  OD1 . ASN A 1 617 ? 119.168 131.363 121.271 1.00 48.49  ? 592  ASN A OD1 1 
ATOM   3986  N  ND2 . ASN A 1 617 ? 117.613 132.700 122.180 1.00 47.71  ? 592  ASN A ND2 1 
ATOM   3987  N  N   . TYR A 1 618 ? 121.004 136.153 123.023 1.00 35.02  ? 593  TYR A N   1 
ATOM   3988  C  CA  . TYR A 1 618 ? 121.525 137.218 123.874 1.00 42.18  ? 593  TYR A CA  1 
ATOM   3989  C  C   . TYR A 1 618 ? 120.636 137.361 125.102 1.00 41.42  ? 593  TYR A C   1 
ATOM   3990  O  O   . TYR A 1 618 ? 119.512 137.863 125.005 1.00 42.89  ? 593  TYR A O   1 
ATOM   3991  C  CB  . TYR A 1 618 ? 121.606 138.538 123.116 1.00 40.16  ? 593  TYR A CB  1 
ATOM   3992  C  CG  . TYR A 1 618 ? 122.274 139.629 123.917 1.00 33.92  ? 593  TYR A CG  1 
ATOM   3993  C  CD1 . TYR A 1 618 ? 123.482 139.401 124.558 1.00 39.56  ? 593  TYR A CD1 1 
ATOM   3994  C  CD2 . TYR A 1 618 ? 121.690 140.879 124.047 1.00 34.10  ? 593  TYR A CD2 1 
ATOM   3995  C  CE1 . TYR A 1 618 ? 124.094 140.389 125.298 1.00 37.90  ? 593  TYR A CE1 1 
ATOM   3996  C  CE2 . TYR A 1 618 ? 122.296 141.872 124.785 1.00 41.51  ? 593  TYR A CE2 1 
ATOM   3997  C  CZ  . TYR A 1 618 ? 123.496 141.622 125.409 1.00 41.11  ? 593  TYR A CZ  1 
ATOM   3998  O  OH  . TYR A 1 618 ? 124.104 142.611 126.144 1.00 46.40  ? 593  TYR A OH  1 
ATOM   3999  N  N   . ARG A 1 619 ? 121.151 136.938 126.255 1.00 33.62  ? 594  ARG A N   1 
ATOM   4000  C  CA  . ARG A 1 619 ? 120.463 137.063 127.538 1.00 24.41  ? 594  ARG A CA  1 
ATOM   4001  C  C   . ARG A 1 619 ? 119.031 136.541 127.441 1.00 30.73  ? 594  ARG A C   1 
ATOM   4002  O  O   . ARG A 1 619 ? 118.058 137.266 127.646 1.00 41.03  ? 594  ARG A O   1 
ATOM   4003  C  CB  . ARG A 1 619 ? 120.486 138.512 128.028 1.00 29.62  ? 594  ARG A CB  1 
ATOM   4004  C  CG  . ARG A 1 619 ? 121.702 138.861 128.863 1.00 28.45  ? 594  ARG A CG  1 
ATOM   4005  C  CD  . ARG A 1 619 ? 121.661 140.307 129.320 1.00 27.92  ? 594  ARG A CD  1 
ATOM   4006  N  NE  . ARG A 1 619 ? 122.749 140.612 130.240 1.00 36.39  ? 594  ARG A NE  1 
ATOM   4007  C  CZ  . ARG A 1 619 ? 122.658 140.538 131.561 1.00 38.27  ? 594  ARG A CZ  1 
ATOM   4008  N  NH1 . ARG A 1 619 ? 121.534 140.177 132.156 1.00 38.65  ? 594  ARG A NH1 1 
ATOM   4009  N  NH2 . ARG A 1 619 ? 123.721 140.834 132.302 1.00 39.88  ? 594  ARG A NH2 1 
ATOM   4010  N  N   . ALA A 1 620 ? 118.921 135.254 127.107 1.00 25.80  ? 595  ALA A N   1 
ATOM   4011  C  CA  . ALA A 1 620 ? 117.606 134.655 126.908 1.00 24.15  ? 595  ALA A CA  1 
ATOM   4012  C  C   . ALA A 1 620 ? 116.786 134.678 128.191 1.00 31.64  ? 595  ALA A C   1 
ATOM   4013  O  O   . ALA A 1 620 ? 115.581 134.952 128.160 1.00 38.87  ? 595  ALA A O   1 
ATOM   4014  C  CB  . ALA A 1 620 ? 117.752 133.227 126.389 1.00 27.02  ? 595  ALA A CB  1 
ATOM   4015  N  N   . ASN A 1 621 ? 117.424 134.402 129.330 1.00 33.64  ? 596  ASN A N   1 
ATOM   4016  C  CA  . ASN A 1 621 ? 116.689 134.311 130.588 1.00 32.73  ? 596  ASN A CA  1 
ATOM   4017  C  C   . ASN A 1 621 ? 116.060 135.648 130.965 1.00 42.05  ? 596  ASN A C   1 
ATOM   4018  O  O   . ASN A 1 621 ? 114.857 135.725 131.231 1.00 44.90  ? 596  ASN A O   1 
ATOM   4019  C  CB  . ASN A 1 621 ? 117.618 133.817 131.698 1.00 33.63  ? 596  ASN A CB  1 
ATOM   4020  C  CG  . ASN A 1 621 ? 116.865 133.398 132.944 1.00 45.91  ? 596  ASN A CG  1 
ATOM   4021  O  OD1 . ASN A 1 621 ? 115.638 133.311 132.941 1.00 49.71  ? 596  ASN A OD1 1 
ATOM   4022  N  ND2 . ASN A 1 621 ? 117.598 133.135 134.019 1.00 43.60  ? 596  ASN A ND2 1 
ATOM   4023  N  N   . LYS A 1 622 ? 116.855 136.721 130.975 1.00 35.82  ? 597  LYS A N   1 
ATOM   4024  C  CA  . LYS A 1 622 ? 116.333 138.016 131.404 1.00 32.54  ? 597  LYS A CA  1 
ATOM   4025  C  C   . LYS A 1 622 ? 115.371 138.603 130.378 1.00 39.94  ? 597  LYS A C   1 
ATOM   4026  O  O   . LYS A 1 622 ? 114.367 139.229 130.744 1.00 52.15  ? 597  LYS A O   1 
ATOM   4027  C  CB  . LYS A 1 622 ? 117.486 138.979 131.673 1.00 30.18  ? 597  LYS A CB  1 
ATOM   4028  C  CG  . LYS A 1 622 ? 118.667 138.336 132.373 1.00 37.87  ? 597  LYS A CG  1 
ATOM   4029  C  CD  . LYS A 1 622 ? 118.329 137.970 133.806 1.00 33.62  ? 597  LYS A CD  1 
ATOM   4030  C  CE  . LYS A 1 622 ? 119.548 137.433 134.535 1.00 33.65  ? 597  LYS A CE  1 
ATOM   4031  N  NZ  . LYS A 1 622 ? 119.214 136.964 135.906 1.00 44.92  ? 597  LYS A NZ  1 
ATOM   4032  N  N   . VAL A 1 623 ? 115.662 138.420 129.088 1.00 34.17  ? 598  VAL A N   1 
ATOM   4033  C  CA  . VAL A 1 623 ? 114.756 138.902 128.050 1.00 29.98  ? 598  VAL A CA  1 
ATOM   4034  C  C   . VAL A 1 623 ? 113.408 138.202 128.157 1.00 41.75  ? 598  VAL A C   1 
ATOM   4035  O  O   . VAL A 1 623 ? 112.351 138.841 128.079 1.00 51.65  ? 598  VAL A O   1 
ATOM   4036  C  CB  . VAL A 1 623 ? 115.389 138.714 126.659 1.00 28.08  ? 598  VAL A CB  1 
ATOM   4037  C  CG1 . VAL A 1 623 ? 114.318 138.621 125.587 1.00 25.44  ? 598  VAL A CG1 1 
ATOM   4038  C  CG2 . VAL A 1 623 ? 116.350 139.849 126.361 1.00 32.33  ? 598  VAL A CG2 1 
ATOM   4039  N  N   . ALA A 1 624 ? 113.421 136.880 128.347 1.00 34.33  ? 599  ALA A N   1 
ATOM   4040  C  CA  . ALA A 1 624 ? 112.172 136.152 128.528 1.00 33.88  ? 599  ALA A CA  1 
ATOM   4041  C  C   . ALA A 1 624 ? 111.476 136.548 129.822 1.00 35.98  ? 599  ALA A C   1 
ATOM   4042  O  O   . ALA A 1 624 ? 110.244 136.555 129.879 1.00 41.75  ? 599  ALA A O   1 
ATOM   4043  C  CB  . ALA A 1 624 ? 112.431 134.648 128.502 1.00 42.74  ? 599  ALA A CB  1 
ATOM   4044  N  N   . PHE A 1 625 ? 112.241 136.883 130.863 1.00 42.28  ? 600  PHE A N   1 
ATOM   4045  C  CA  . PHE A 1 625 ? 111.642 137.371 132.100 1.00 47.40  ? 600  PHE A CA  1 
ATOM   4046  C  C   . PHE A 1 625 ? 110.874 138.663 131.859 1.00 52.77  ? 600  PHE A C   1 
ATOM   4047  O  O   . PHE A 1 625 ? 109.741 138.825 132.327 1.00 56.87  ? 600  PHE A O   1 
ATOM   4048  C  CB  . PHE A 1 625 ? 112.730 137.579 133.155 1.00 49.04  ? 600  PHE A CB  1 
ATOM   4049  C  CG  . PHE A 1 625 ? 112.256 138.287 134.393 1.00 43.34  ? 600  PHE A CG  1 
ATOM   4050  C  CD1 . PHE A 1 625 ? 111.061 137.944 134.994 1.00 50.37  ? 600  PHE A CD1 1 
ATOM   4051  C  CD2 . PHE A 1 625 ? 113.016 139.292 134.960 1.00 46.33  ? 600  PHE A CD2 1 
ATOM   4052  C  CE1 . PHE A 1 625 ? 110.630 138.593 136.130 1.00 46.50  ? 600  PHE A CE1 1 
ATOM   4053  C  CE2 . PHE A 1 625 ? 112.588 139.944 136.096 1.00 46.68  ? 600  PHE A CE2 1 
ATOM   4054  C  CZ  . PHE A 1 625 ? 111.394 139.593 136.680 1.00 43.49  ? 600  PHE A CZ  1 
ATOM   4055  N  N   . TRP A 1 626 ? 111.475 139.596 131.124 1.00 53.28  ? 601  TRP A N   1 
ATOM   4056  C  CA  . TRP A 1 626 ? 110.827 140.881 130.895 1.00 46.70  ? 601  TRP A CA  1 
ATOM   4057  C  C   . TRP A 1 626 ? 109.713 140.817 129.860 1.00 51.10  ? 601  TRP A C   1 
ATOM   4058  O  O   . TRP A 1 626 ? 108.807 141.657 129.898 1.00 53.43  ? 601  TRP A O   1 
ATOM   4059  C  CB  . TRP A 1 626 ? 111.854 141.933 130.474 1.00 43.95  ? 601  TRP A CB  1 
ATOM   4060  C  CG  . TRP A 1 626 ? 112.676 142.433 131.612 1.00 39.22  ? 601  TRP A CG  1 
ATOM   4061  C  CD1 . TRP A 1 626 ? 114.021 142.312 131.762 1.00 47.94  ? 601  TRP A CD1 1 
ATOM   4062  C  CD2 . TRP A 1 626 ? 112.203 143.124 132.774 1.00 42.23  ? 601  TRP A CD2 1 
ATOM   4063  N  NE1 . TRP A 1 626 ? 114.420 142.891 132.940 1.00 46.51  ? 601  TRP A NE1 1 
ATOM   4064  C  CE2 . TRP A 1 626 ? 113.321 143.396 133.581 1.00 42.00  ? 601  TRP A CE2 1 
ATOM   4065  C  CE3 . TRP A 1 626 ? 110.942 143.541 133.208 1.00 49.65  ? 601  TRP A CE3 1 
ATOM   4066  C  CZ2 . TRP A 1 626 ? 113.218 144.065 134.795 1.00 48.22  ? 601  TRP A CZ2 1 
ATOM   4067  C  CZ3 . TRP A 1 626 ? 110.842 144.205 134.414 1.00 50.10  ? 601  TRP A CZ3 1 
ATOM   4068  C  CH2 . TRP A 1 626 ? 111.973 144.460 135.193 1.00 51.02  ? 601  TRP A CH2 1 
ATOM   4069  N  N   . LEU A 1 627 ? 109.749 139.853 128.940 1.00 46.18  ? 602  LEU A N   1 
ATOM   4070  C  CA  . LEU A 1 627 ? 108.751 139.798 127.879 1.00 40.16  ? 602  LEU A CA  1 
ATOM   4071  C  C   . LEU A 1 627 ? 107.619 138.814 128.140 1.00 51.63  ? 602  LEU A C   1 
ATOM   4072  O  O   . LEU A 1 627 ? 106.548 138.963 127.542 1.00 54.30  ? 602  LEU A O   1 
ATOM   4073  C  CB  . LEU A 1 627 ? 109.414 139.443 126.544 1.00 42.10  ? 602  LEU A CB  1 
ATOM   4074  C  CG  . LEU A 1 627 ? 110.403 140.462 125.979 1.00 45.33  ? 602  LEU A CG  1 
ATOM   4075  C  CD1 . LEU A 1 627 ? 111.018 139.944 124.691 1.00 43.00  ? 602  LEU A CD1 1 
ATOM   4076  C  CD2 . LEU A 1 627 ? 109.722 141.798 125.752 1.00 46.21  ? 602  LEU A CD2 1 
ATOM   4077  N  N   . GLU A 1 628 ? 107.815 137.820 129.002 1.00 48.86  ? 603  GLU A N   1 
ATOM   4078  C  CA  . GLU A 1 628 ? 106.828 136.762 129.180 1.00 36.88  ? 603  GLU A CA  1 
ATOM   4079  C  C   . GLU A 1 628 ? 106.302 136.641 130.601 1.00 34.84  ? 603  GLU A C   1 
ATOM   4080  O  O   . GLU A 1 628 ? 105.094 136.484 130.789 1.00 43.60  ? 603  GLU A O   1 
ATOM   4081  C  CB  . GLU A 1 628 ? 107.425 135.416 128.745 1.00 35.07  ? 603  GLU A CB  1 
ATOM   4082  C  CG  . GLU A 1 628 ? 108.181 135.479 127.428 1.00 38.21  ? 603  GLU A CG  1 
ATOM   4083  C  CD  . GLU A 1 628 ? 107.832 134.336 126.498 1.00 47.77  ? 603  GLU A CD  1 
ATOM   4084  O  OE1 . GLU A 1 628 ? 106.767 133.714 126.692 1.00 46.67  ? 603  GLU A OE1 1 
ATOM   4085  O  OE2 . GLU A 1 628 ? 108.622 134.061 125.570 1.00 48.18  ? 603  GLU A OE2 1 
ATOM   4086  N  N   . LEU A 1 629 ? 107.170 136.706 131.612 1.00 18.89  ? 604  LEU A N   1 
ATOM   4087  C  CA  . LEU A 1 629 ? 106.708 136.504 132.982 1.00 15.47  ? 604  LEU A CA  1 
ATOM   4088  C  C   . LEU A 1 629 ? 106.100 137.774 133.562 1.00 28.86  ? 604  LEU A C   1 
ATOM   4089  O  O   . LEU A 1 629 ? 105.013 137.734 134.150 1.00 46.36  ? 604  LEU A O   1 
ATOM   4090  C  CB  . LEU A 1 629 ? 107.856 136.014 133.866 1.00 26.20  ? 604  LEU A CB  1 
ATOM   4091  C  CG  . LEU A 1 629 ? 107.539 135.992 135.364 1.00 24.14  ? 604  LEU A CG  1 
ATOM   4092  C  CD1 . LEU A 1 629 ? 106.354 135.085 135.647 1.00 31.44  ? 604  LEU A CD1 1 
ATOM   4093  C  CD2 . LEU A 1 629 ? 108.740 135.563 136.180 1.00 24.46  ? 604  LEU A CD2 1 
ATOM   4094  N  N   . VAL A 1 630 ? 106.794 138.908 133.422 1.00 28.32  ? 605  VAL A N   1 
ATOM   4095  C  CA  . VAL A 1 630 ? 106.296 140.158 134.005 1.00 26.88  ? 605  VAL A CA  1 
ATOM   4096  C  C   . VAL A 1 630 ? 104.906 140.515 133.498 1.00 36.94  ? 605  VAL A C   1 
ATOM   4097  O  O   . VAL A 1 630 ? 104.067 140.933 134.310 1.00 40.99  ? 605  VAL A O   1 
ATOM   4098  C  CB  . VAL A 1 630 ? 107.324 141.280 133.807 1.00 27.39  ? 605  VAL A CB  1 
ATOM   4099  C  CG1 . VAL A 1 630 ? 106.661 142.640 133.920 1.00 34.34  ? 605  VAL A CG1 1 
ATOM   4100  C  CG2 . VAL A 1 630 ? 108.435 141.156 134.831 1.00 33.67  ? 605  VAL A CG2 1 
ATOM   4101  N  N   . PRO A 1 631 ? 104.580 140.389 132.205 1.00 33.23  ? 606  PRO A N   1 
ATOM   4102  C  CA  . PRO A 1 631 ? 103.184 140.616 131.796 1.00 32.82  ? 606  PRO A CA  1 
ATOM   4103  C  C   . PRO A 1 631 ? 102.188 139.709 132.499 1.00 36.22  ? 606  PRO A C   1 
ATOM   4104  O  O   . PRO A 1 631 ? 101.051 140.131 132.747 1.00 43.95  ? 606  PRO A O   1 
ATOM   4105  C  CB  . PRO A 1 631 ? 103.220 140.352 130.287 1.00 30.33  ? 606  PRO A CB  1 
ATOM   4106  C  CG  . PRO A 1 631 ? 104.592 140.722 129.894 1.00 30.18  ? 606  PRO A CG  1 
ATOM   4107  C  CD  . PRO A 1 631 ? 105.466 140.274 131.031 1.00 32.52  ? 606  PRO A CD  1 
ATOM   4108  N  N   . HIS A 1 632 ? 102.575 138.477 132.832 1.00 29.40  ? 607  HIS A N   1 
ATOM   4109  C  CA  . HIS A 1 632 ? 101.671 137.572 133.532 1.00 31.77  ? 607  HIS A CA  1 
ATOM   4110  C  C   . HIS A 1 632 ? 101.494 137.932 135.000 1.00 35.62  ? 607  HIS A C   1 
ATOM   4111  O  O   . HIS A 1 632 ? 100.596 137.383 135.647 1.00 44.54  ? 607  HIS A O   1 
ATOM   4112  C  CB  . HIS A 1 632 ? 102.169 136.131 133.418 1.00 26.19  ? 607  HIS A CB  1 
ATOM   4113  C  CG  . HIS A 1 632 ? 102.089 135.571 132.033 1.00 33.66  ? 607  HIS A CG  1 
ATOM   4114  N  ND1 . HIS A 1 632 ? 102.269 134.232 131.762 1.00 37.19  ? 607  HIS A ND1 1 
ATOM   4115  C  CD2 . HIS A 1 632 ? 101.851 136.167 130.841 1.00 34.92  ? 607  HIS A CD2 1 
ATOM   4116  C  CE1 . HIS A 1 632 ? 102.144 134.027 130.463 1.00 41.92  ? 607  HIS A CE1 1 
ATOM   4117  N  NE2 . HIS A 1 632 ? 101.891 135.185 129.881 1.00 39.41  ? 607  HIS A NE2 1 
ATOM   4118  N  N   . LEU A 1 633 ? 102.317 138.824 135.539 1.00 23.22  ? 608  LEU A N   1 
ATOM   4119  C  CA  . LEU A 1 633 ? 102.194 139.228 136.935 1.00 26.46  ? 608  LEU A CA  1 
ATOM   4120  C  C   . LEU A 1 633 ? 101.476 140.568 137.048 1.00 32.38  ? 608  LEU A C   1 
ATOM   4121  O  O   . LEU A 1 633 ? 100.724 140.957 136.155 1.00 28.86  ? 608  LEU A O   1 
ATOM   4122  C  CB  . LEU A 1 633 ? 103.571 139.310 137.598 1.00 20.60  ? 608  LEU A CB  1 
ATOM   4123  C  CG  . LEU A 1 633 ? 104.451 138.059 137.565 1.00 19.35  ? 608  LEU A CG  1 
ATOM   4124  C  CD1 . LEU A 1 633 ? 105.554 138.159 138.605 1.00 17.75  ? 608  LEU A CD1 1 
ATOM   4125  C  CD2 . LEU A 1 633 ? 103.624 136.807 137.786 1.00 29.55  ? 608  LEU A CD2 1 
ATOM   4126  N  N   . ARG B 1 82  ? 135.698 77.710  160.534 1.00 95.83  ? 40   ARG B N   1 
ATOM   4127  C  CA  . ARG B 1 82  ? 135.681 78.053  161.951 1.00 99.02  ? 40   ARG B CA  1 
ATOM   4128  C  C   . ARG B 1 82  ? 134.445 78.874  162.299 1.00 98.68  ? 40   ARG B C   1 
ATOM   4129  O  O   . ARG B 1 82  ? 134.062 79.779  161.558 1.00 98.10  ? 40   ARG B O   1 
ATOM   4130  C  CB  . ARG B 1 82  ? 136.949 78.818  162.333 1.00 98.32  ? 40   ARG B CB  1 
ATOM   4131  C  CG  . ARG B 1 82  ? 137.225 78.855  163.826 1.00 96.24  ? 40   ARG B CG  1 
ATOM   4132  C  CD  . ARG B 1 82  ? 138.316 79.859  164.155 1.00 96.61  ? 40   ARG B CD  1 
ATOM   4133  N  NE  . ARG B 1 82  ? 139.325 79.927  163.105 1.00 98.47  ? 40   ARG B NE  1 
ATOM   4134  C  CZ  . ARG B 1 82  ? 140.479 80.571  163.214 1.00 99.23  ? 40   ARG B CZ  1 
ATOM   4135  N  NH1 . ARG B 1 82  ? 140.805 81.222  164.318 1.00 98.42  ? 40   ARG B NH1 1 
ATOM   4136  N  NH2 . ARG B 1 82  ? 141.327 80.561  162.190 1.00 98.53  ? 40   ARG B NH2 1 
ATOM   4137  N  N   . PHE B 1 83  ? 133.823 78.553  163.436 1.00 87.06  ? 41   PHE B N   1 
ATOM   4138  C  CA  . PHE B 1 83  ? 132.609 79.215  163.912 1.00 84.60  ? 41   PHE B CA  1 
ATOM   4139  C  C   . PHE B 1 83  ? 132.935 79.887  165.241 1.00 84.49  ? 41   PHE B C   1 
ATOM   4140  O  O   . PHE B 1 83  ? 132.673 79.322  166.314 1.00 85.89  ? 41   PHE B O   1 
ATOM   4141  C  CB  . PHE B 1 83  ? 131.450 78.230  164.071 1.00 84.39  ? 41   PHE B CB  1 
ATOM   4142  C  CG  . PHE B 1 83  ? 130.858 77.748  162.770 1.00 84.97  ? 41   PHE B CG  1 
ATOM   4143  C  CD1 . PHE B 1 83  ? 131.438 78.065  161.554 1.00 83.31  ? 41   PHE B CD1 1 
ATOM   4144  C  CD2 . PHE B 1 83  ? 129.713 76.969  162.771 1.00 85.04  ? 41   PHE B CD2 1 
ATOM   4145  C  CE1 . PHE B 1 83  ? 130.892 77.617  160.368 1.00 85.05  ? 41   PHE B CE1 1 
ATOM   4146  C  CE2 . PHE B 1 83  ? 129.161 76.519  161.588 1.00 85.44  ? 41   PHE B CE2 1 
ATOM   4147  C  CZ  . PHE B 1 83  ? 129.752 76.843  160.386 1.00 85.47  ? 41   PHE B CZ  1 
ATOM   4148  N  N   . PRO B 1 84  ? 133.511 81.088  165.211 1.00 79.28  ? 42   PRO B N   1 
ATOM   4149  C  CA  . PRO B 1 84  ? 133.890 81.756  166.462 1.00 79.39  ? 42   PRO B CA  1 
ATOM   4150  C  C   . PRO B 1 84  ? 132.674 82.086  167.315 1.00 80.11  ? 42   PRO B C   1 
ATOM   4151  O  O   . PRO B 1 84  ? 131.587 82.361  166.804 1.00 82.69  ? 42   PRO B O   1 
ATOM   4152  C  CB  . PRO B 1 84  ? 134.604 83.024  165.983 1.00 76.09  ? 42   PRO B CB  1 
ATOM   4153  C  CG  . PRO B 1 84  ? 134.067 83.259  164.613 1.00 77.97  ? 42   PRO B CG  1 
ATOM   4154  C  CD  . PRO B 1 84  ? 133.855 81.897  164.030 1.00 78.32  ? 42   PRO B CD  1 
ATOM   4155  N  N   . VAL B 1 85  ? 132.873 82.056  168.630 1.00 81.37  ? 43   VAL B N   1 
ATOM   4156  C  CA  . VAL B 1 85  ? 131.821 82.318  169.605 1.00 82.01  ? 43   VAL B CA  1 
ATOM   4157  C  C   . VAL B 1 85  ? 132.215 83.545  170.414 1.00 84.26  ? 43   VAL B C   1 
ATOM   4158  O  O   . VAL B 1 85  ? 133.325 83.609  170.954 1.00 85.34  ? 43   VAL B O   1 
ATOM   4159  C  CB  . VAL B 1 85  ? 131.588 81.104  170.524 1.00 80.59  ? 43   VAL B CB  1 
ATOM   4160  C  CG1 . VAL B 1 85  ? 131.008 81.542  171.863 1.00 81.04  ? 43   VAL B CG1 1 
ATOM   4161  C  CG2 . VAL B 1 85  ? 130.678 80.094  169.845 1.00 81.45  ? 43   VAL B CG2 1 
ATOM   4162  N  N   . VAL B 1 86  ? 131.309 84.518  170.491 1.00 82.16  ? 44   VAL B N   1 
ATOM   4163  C  CA  . VAL B 1 86  ? 131.529 85.754  171.231 1.00 80.35  ? 44   VAL B CA  1 
ATOM   4164  C  C   . VAL B 1 86  ? 130.431 85.888  172.276 1.00 80.43  ? 44   VAL B C   1 
ATOM   4165  O  O   . VAL B 1 86  ? 129.245 85.734  171.960 1.00 80.81  ? 44   VAL B O   1 
ATOM   4166  C  CB  . VAL B 1 86  ? 131.552 86.979  170.300 1.00 74.32  ? 44   VAL B CB  1 
ATOM   4167  C  CG1 . VAL B 1 86  ? 131.655 88.258  171.112 1.00 75.90  ? 44   VAL B CG1 1 
ATOM   4168  C  CG2 . VAL B 1 86  ? 132.708 86.872  169.323 1.00 75.50  ? 44   VAL B CG2 1 
ATOM   4169  N  N   . ASN B 1 87  ? 130.826 86.168  173.514 1.00 86.71  ? 45   ASN B N   1 
ATOM   4170  C  CA  . ASN B 1 87  ? 129.886 86.305  174.619 1.00 86.78  ? 45   ASN B CA  1 
ATOM   4171  C  C   . ASN B 1 87  ? 129.428 87.755  174.722 1.00 86.94  ? 45   ASN B C   1 
ATOM   4172  O  O   . ASN B 1 87  ? 130.249 88.659  174.908 1.00 86.94  ? 45   ASN B O   1 
ATOM   4173  C  CB  . ASN B 1 87  ? 130.527 85.853  175.930 1.00 86.68  ? 45   ASN B CB  1 
ATOM   4174  C  CG  . ASN B 1 87  ? 129.856 86.460  177.147 1.00 88.54  ? 45   ASN B CG  1 
ATOM   4175  O  OD1 . ASN B 1 87  ? 128.858 85.939  177.645 1.00 89.25  ? 45   ASN B OD1 1 
ATOM   4176  N  ND2 . ASN B 1 87  ? 130.405 87.566  177.637 1.00 87.44  ? 45   ASN B ND2 1 
ATOM   4177  N  N   . THR B 1 88  ? 128.122 87.972  174.603 1.00 84.07  ? 46   THR B N   1 
ATOM   4178  C  CA  . THR B 1 88  ? 127.539 89.291  174.788 1.00 80.73  ? 46   THR B CA  1 
ATOM   4179  C  C   . THR B 1 88  ? 127.167 89.472  176.259 1.00 81.87  ? 46   THR B C   1 
ATOM   4180  O  O   . THR B 1 88  ? 127.518 88.657  177.116 1.00 82.35  ? 46   THR B O   1 
ATOM   4181  C  CB  . THR B 1 88  ? 126.335 89.474  173.867 1.00 77.89  ? 46   THR B CB  1 
ATOM   4182  O  OG1 . THR B 1 88  ? 125.173 88.899  174.477 1.00 78.48  ? 46   THR B OG1 1 
ATOM   4183  C  CG2 . THR B 1 88  ? 126.583 88.798  172.529 1.00 79.09  ? 46   THR B CG2 1 
ATOM   4184  N  N   . ALA B 1 89  ? 126.448 90.550  176.570 1.00 77.73  ? 47   ALA B N   1 
ATOM   4185  C  CA  . ALA B 1 89  ? 126.010 90.787  177.939 1.00 76.33  ? 47   ALA B CA  1 
ATOM   4186  C  C   . ALA B 1 89  ? 124.781 89.974  178.315 1.00 77.65  ? 47   ALA B C   1 
ATOM   4187  O  O   . ALA B 1 89  ? 124.439 89.910  179.500 1.00 78.54  ? 47   ALA B O   1 
ATOM   4188  C  CB  . ALA B 1 89  ? 125.725 92.275  178.154 1.00 76.71  ? 47   ALA B CB  1 
ATOM   4189  N  N   . TYR B 1 90  ? 124.113 89.353  177.343 1.00 81.74  ? 48   TYR B N   1 
ATOM   4190  C  CA  . TYR B 1 90  ? 122.945 88.527  177.605 1.00 85.03  ? 48   TYR B CA  1 
ATOM   4191  C  C   . TYR B 1 90  ? 123.181 87.051  177.319 1.00 85.66  ? 48   TYR B C   1 
ATOM   4192  O  O   . TYR B 1 90  ? 122.307 86.233  177.624 1.00 83.43  ? 48   TYR B O   1 
ATOM   4193  C  CB  . TYR B 1 90  ? 121.741 89.009  176.778 1.00 82.41  ? 48   TYR B CB  1 
ATOM   4194  C  CG  . TYR B 1 90  ? 121.518 90.507  176.797 1.00 81.79  ? 48   TYR B CG  1 
ATOM   4195  C  CD1 . TYR B 1 90  ? 122.259 91.352  175.980 1.00 83.15  ? 48   TYR B CD1 1 
ATOM   4196  C  CD2 . TYR B 1 90  ? 120.569 91.076  177.636 1.00 80.49  ? 48   TYR B CD2 1 
ATOM   4197  C  CE1 . TYR B 1 90  ? 122.057 92.719  175.995 1.00 82.33  ? 48   TYR B CE1 1 
ATOM   4198  C  CE2 . TYR B 1 90  ? 120.363 92.442  177.658 1.00 80.27  ? 48   TYR B CE2 1 
ATOM   4199  C  CZ  . TYR B 1 90  ? 121.109 93.258  176.836 1.00 81.37  ? 48   TYR B CZ  1 
ATOM   4200  O  OH  . TYR B 1 90  ? 120.907 94.619  176.853 1.00 78.72  ? 48   TYR B OH  1 
ATOM   4201  N  N   . GLY B 1 91  ? 124.322 86.693  176.746 1.00 90.80  ? 49   GLY B N   1 
ATOM   4202  C  CA  . GLY B 1 91  ? 124.597 85.305  176.427 1.00 89.65  ? 49   GLY B CA  1 
ATOM   4203  C  C   . GLY B 1 91  ? 125.760 85.205  175.456 1.00 89.39  ? 49   GLY B C   1 
ATOM   4204  O  O   . GLY B 1 91  ? 126.531 86.147  175.290 1.00 91.15  ? 49   GLY B O   1 
ATOM   4205  N  N   . ARG B 1 92  ? 125.861 84.038  174.827 1.00 89.56  ? 50   ARG B N   1 
ATOM   4206  C  CA  . ARG B 1 92  ? 126.904 83.744  173.856 1.00 87.71  ? 50   ARG B CA  1 
ATOM   4207  C  C   . ARG B 1 92  ? 126.266 83.414  172.515 1.00 89.78  ? 50   ARG B C   1 
ATOM   4208  O  O   . ARG B 1 92  ? 125.236 82.736  172.460 1.00 92.51  ? 50   ARG B O   1 
ATOM   4209  C  CB  . ARG B 1 92  ? 127.777 82.575  174.320 1.00 90.45  ? 50   ARG B CB  1 
ATOM   4210  C  CG  . ARG B 1 92  ? 127.963 82.499  175.826 1.00 92.35  ? 50   ARG B CG  1 
ATOM   4211  C  CD  . ARG B 1 92  ? 128.727 81.246  176.227 1.00 91.54  ? 50   ARG B CD  1 
ATOM   4212  N  NE  . ARG B 1 92  ? 130.048 81.177  175.612 1.00 93.51  ? 50   ARG B NE  1 
ATOM   4213  C  CZ  . ARG B 1 92  ? 131.107 81.856  176.031 1.00 92.43  ? 50   ARG B CZ  1 
ATOM   4214  N  NH1 . ARG B 1 92  ? 131.041 82.661  177.079 1.00 90.69  ? 50   ARG B NH1 1 
ATOM   4215  N  NH2 . ARG B 1 92  ? 132.262 81.719  175.386 1.00 90.83  ? 50   ARG B NH2 1 
ATOM   4216  N  N   . VAL B 1 93  ? 126.878 83.896  171.437 1.00 83.62  ? 51   VAL B N   1 
ATOM   4217  C  CA  . VAL B 1 93  ? 126.362 83.710  170.087 1.00 85.24  ? 51   VAL B CA  1 
ATOM   4218  C  C   . VAL B 1 93  ? 127.447 83.085  169.220 1.00 84.45  ? 51   VAL B C   1 
ATOM   4219  O  O   . VAL B 1 93  ? 128.629 83.426  169.344 1.00 84.04  ? 51   VAL B O   1 
ATOM   4220  C  CB  . VAL B 1 93  ? 125.872 85.040  169.476 1.00 81.65  ? 51   VAL B CB  1 
ATOM   4221  C  CG1 . VAL B 1 93  ? 124.611 85.510  170.179 1.00 82.95  ? 51   VAL B CG1 1 
ATOM   4222  C  CG2 . VAL B 1 93  ? 126.956 86.101  169.565 1.00 81.18  ? 51   VAL B CG2 1 
ATOM   4223  N  N   . ARG B 1 94  ? 127.042 82.168  168.346 1.00 86.25  ? 52   ARG B N   1 
ATOM   4224  C  CA  . ARG B 1 94  ? 127.941 81.553  167.378 1.00 85.10  ? 52   ARG B CA  1 
ATOM   4225  C  C   . ARG B 1 94  ? 127.776 82.229  166.025 1.00 84.61  ? 52   ARG B C   1 
ATOM   4226  O  O   . ARG B 1 94  ? 126.653 82.386  165.537 1.00 87.86  ? 52   ARG B O   1 
ATOM   4227  C  CB  . ARG B 1 94  ? 127.677 80.053  167.230 1.00 85.54  ? 52   ARG B CB  1 
ATOM   4228  C  CG  . ARG B 1 94  ? 128.805 79.335  166.492 1.00 85.17  ? 52   ARG B CG  1 
ATOM   4229  C  CD  . ARG B 1 94  ? 128.589 77.833  166.280 1.00 86.45  ? 52   ARG B CD  1 
ATOM   4230  N  NE  . ARG B 1 94  ? 127.609 77.200  167.156 1.00 89.78  ? 52   ARG B NE  1 
ATOM   4231  C  CZ  . ARG B 1 94  ? 127.771 76.999  168.457 1.00 88.62  ? 52   ARG B CZ  1 
ATOM   4232  N  NH1 . ARG B 1 94  ? 128.875 77.371  169.083 1.00 87.53  ? 52   ARG B NH1 1 
ATOM   4233  N  NH2 . ARG B 1 94  ? 126.808 76.390  169.142 1.00 87.54  ? 52   ARG B NH2 1 
ATOM   4234  N  N   . GLY B 1 95  ? 128.898 82.622  165.420 1.00 72.16  ? 53   GLY B N   1 
ATOM   4235  C  CA  . GLY B 1 95  ? 128.911 83.205  164.106 1.00 69.83  ? 53   GLY B CA  1 
ATOM   4236  C  C   . GLY B 1 95  ? 129.448 82.259  163.051 1.00 75.04  ? 53   GLY B C   1 
ATOM   4237  O  O   . GLY B 1 95  ? 129.482 81.034  163.226 1.00 81.94  ? 53   GLY B O   1 
ATOM   4238  N  N   . VAL B 1 96  ? 129.871 82.840  161.931 1.00 75.69  ? 54   VAL B N   1 
ATOM   4239  C  CA  . VAL B 1 96  ? 130.494 82.113  160.838 1.00 75.74  ? 54   VAL B CA  1 
ATOM   4240  C  C   . VAL B 1 96  ? 131.740 82.874  160.400 1.00 76.50  ? 54   VAL B C   1 
ATOM   4241  O  O   . VAL B 1 96  ? 132.074 83.921  160.949 1.00 78.00  ? 54   VAL B O   1 
ATOM   4242  C  CB  . VAL B 1 96  ? 129.533 81.901  159.651 1.00 76.91  ? 54   VAL B CB  1 
ATOM   4243  C  CG1 . VAL B 1 96  ? 128.598 80.741  159.931 1.00 78.85  ? 54   VAL B CG1 1 
ATOM   4244  C  CG2 . VAL B 1 96  ? 128.745 83.169  159.377 1.00 75.49  ? 54   VAL B CG2 1 
ATOM   4245  N  N   . ARG B 1 97  ? 132.428 82.332  159.401 1.00 85.65  ? 55   ARG B N   1 
ATOM   4246  C  CA  . ARG B 1 97  ? 133.651 82.924  158.868 1.00 86.82  ? 55   ARG B CA  1 
ATOM   4247  C  C   . ARG B 1 97  ? 133.605 82.944  157.347 1.00 85.73  ? 55   ARG B C   1 
ATOM   4248  O  O   . ARG B 1 97  ? 134.531 82.502  156.663 1.00 87.96  ? 55   ARG B O   1 
ATOM   4249  C  CB  . ARG B 1 97  ? 134.884 82.179  159.369 1.00 88.55  ? 55   ARG B CB  1 
ATOM   4250  C  CG  . ARG B 1 97  ? 136.144 83.027  159.392 1.00 85.70  ? 55   ARG B CG  1 
ATOM   4251  C  CD  . ARG B 1 97  ? 137.385 82.173  159.568 1.00 87.02  ? 55   ARG B CD  1 
ATOM   4252  N  NE  . ARG B 1 97  ? 138.599 82.901  159.219 1.00 87.18  ? 55   ARG B NE  1 
ATOM   4253  C  CZ  . ARG B 1 97  ? 139.284 83.659  160.063 1.00 87.82  ? 55   ARG B CZ  1 
ATOM   4254  N  NH1 . ARG B 1 97  ? 138.901 83.816  161.320 1.00 87.19  ? 55   ARG B NH1 1 
ATOM   4255  N  NH2 . ARG B 1 97  ? 140.382 84.277  159.636 1.00 86.71  ? 55   ARG B NH2 1 
ATOM   4256  N  N   . ARG B 1 98  ? 132.499 83.446  156.800 1.00 81.01  ? 56   ARG B N   1 
ATOM   4257  C  CA  . ARG B 1 98  ? 132.331 83.502  155.355 1.00 83.64  ? 56   ARG B CA  1 
ATOM   4258  C  C   . ARG B 1 98  ? 133.444 84.321  154.711 1.00 86.49  ? 56   ARG B C   1 
ATOM   4259  O  O   . ARG B 1 98  ? 133.814 85.391  155.200 1.00 84.82  ? 56   ARG B O   1 
ATOM   4260  C  CB  . ARG B 1 98  ? 130.969 84.103  155.007 1.00 83.23  ? 56   ARG B CB  1 
ATOM   4261  C  CG  . ARG B 1 98  ? 130.229 83.375  153.899 1.00 83.87  ? 56   ARG B CG  1 
ATOM   4262  C  CD  . ARG B 1 98  ? 129.769 82.001  154.353 1.00 85.17  ? 56   ARG B CD  1 
ATOM   4263  N  NE  . ARG B 1 98  ? 128.896 82.078  155.518 1.00 84.93  ? 56   ARG B NE  1 
ATOM   4264  C  CZ  . ARG B 1 98  ? 127.578 82.206  155.458 1.00 85.84  ? 56   ARG B CZ  1 
ATOM   4265  N  NH1 . ARG B 1 98  ? 126.942 82.283  154.301 1.00 86.70  ? 56   ARG B NH1 1 
ATOM   4266  N  NH2 . ARG B 1 98  ? 126.880 82.262  156.589 1.00 84.70  ? 56   ARG B NH2 1 
ATOM   4267  N  N   . GLU B 1 99  ? 133.979 83.806  153.609 1.00 99.12  ? 57   GLU B N   1 
ATOM   4268  C  CA  . GLU B 1 99  ? 135.063 84.446  152.881 1.00 99.38  ? 57   GLU B CA  1 
ATOM   4269  C  C   . GLU B 1 99  ? 134.528 85.090  151.608 1.00 100.28 ? 57   GLU B C   1 
ATOM   4270  O  O   . GLU B 1 99  ? 133.498 84.677  151.068 1.00 98.71  ? 57   GLU B O   1 
ATOM   4271  C  CB  . GLU B 1 99  ? 136.165 83.440  152.539 1.00 98.38  ? 57   GLU B CB  1 
ATOM   4272  C  CG  . GLU B 1 99  ? 137.238 83.318  153.608 1.00 100.54 ? 57   GLU B CG  1 
ATOM   4273  C  CD  . GLU B 1 99  ? 137.760 81.902  153.753 1.00 101.82 ? 57   GLU B CD  1 
ATOM   4274  O  OE1 . GLU B 1 99  ? 137.785 81.171  152.741 1.00 103.07 ? 57   GLU B OE1 1 
ATOM   4275  O  OE2 . GLU B 1 99  ? 138.144 81.521  154.878 1.00 99.62  ? 57   GLU B OE2 1 
ATOM   4276  N  N   . LEU B 1 100 ? 135.241 86.106  151.134 1.00 94.83  ? 58   LEU B N   1 
ATOM   4277  C  CA  . LEU B 1 100 ? 134.789 86.903  150.004 1.00 93.90  ? 58   LEU B CA  1 
ATOM   4278  C  C   . LEU B 1 100 ? 135.443 86.444  148.706 1.00 94.31  ? 58   LEU B C   1 
ATOM   4279  O  O   . LEU B 1 100 ? 136.536 85.871  148.703 1.00 93.71  ? 58   LEU B O   1 
ATOM   4280  C  CB  . LEU B 1 100 ? 135.085 88.383  150.241 1.00 91.51  ? 58   LEU B CB  1 
ATOM   4281  C  CG  . LEU B 1 100 ? 134.466 88.955  151.516 1.00 89.69  ? 58   LEU B CG  1 
ATOM   4282  C  CD1 . LEU B 1 100 ? 134.902 90.391  151.729 1.00 88.74  ? 58   LEU B CD1 1 
ATOM   4283  C  CD2 . LEU B 1 100 ? 132.954 88.853  151.454 1.00 91.26  ? 58   LEU B CD2 1 
ATOM   4284  N  N   . ASN B 1 101 ? 134.750 86.708  147.595 1.00 106.18 ? 59   ASN B N   1 
ATOM   4285  C  CA  . ASN B 1 101 ? 135.254 86.310  146.284 1.00 106.03 ? 59   ASN B CA  1 
ATOM   4286  C  C   . ASN B 1 101 ? 136.527 87.064  145.918 1.00 106.62 ? 59   ASN B C   1 
ATOM   4287  O  O   . ASN B 1 101 ? 137.450 86.485  145.335 1.00 106.07 ? 59   ASN B O   1 
ATOM   4288  C  CB  . ASN B 1 101 ? 134.177 86.530  145.222 1.00 103.55 ? 59   ASN B CB  1 
ATOM   4289  N  N   . ASN B 1 102 ? 136.593 88.353  146.245 1.00 106.70 ? 60   ASN B N   1 
ATOM   4290  C  CA  . ASN B 1 102 ? 137.724 89.173  145.841 1.00 105.32 ? 60   ASN B CA  1 
ATOM   4291  C  C   . ASN B 1 102 ? 138.990 88.748  146.586 1.00 106.17 ? 60   ASN B C   1 
ATOM   4292  O  O   . ASN B 1 102 ? 138.953 87.998  147.566 1.00 104.12 ? 60   ASN B O   1 
ATOM   4293  C  CB  . ASN B 1 102 ? 137.424 90.652  146.086 1.00 103.66 ? 60   ASN B CB  1 
ATOM   4294  C  CG  . ASN B 1 102 ? 138.314 91.573  145.272 1.00 104.82 ? 60   ASN B CG  1 
ATOM   4295  O  OD1 . ASN B 1 102 ? 139.536 91.432  145.268 1.00 105.81 ? 60   ASN B OD1 1 
ATOM   4296  N  ND2 . ASN B 1 102 ? 137.701 92.523  144.575 1.00 104.82 ? 60   ASN B ND2 1 
ATOM   4297  N  N   . GLU B 1 103 ? 140.129 89.244  146.102 1.00 115.99 ? 61   GLU B N   1 
ATOM   4298  C  CA  . GLU B 1 103 ? 141.432 88.835  146.612 1.00 116.18 ? 61   GLU B CA  1 
ATOM   4299  C  C   . GLU B 1 103 ? 141.964 89.771  147.691 1.00 113.94 ? 61   GLU B C   1 
ATOM   4300  O  O   . GLU B 1 103 ? 142.540 89.306  148.681 1.00 114.70 ? 61   GLU B O   1 
ATOM   4301  C  CB  . GLU B 1 103 ? 142.442 88.751  145.463 1.00 116.78 ? 61   GLU B CB  1 
ATOM   4302  C  CG  . GLU B 1 103 ? 142.027 87.830  144.323 1.00 117.13 ? 61   GLU B CG  1 
ATOM   4303  C  CD  . GLU B 1 103 ? 141.141 88.521  143.303 1.00 116.14 ? 61   GLU B CD  1 
ATOM   4304  O  OE1 . GLU B 1 103 ? 141.046 89.765  143.341 1.00 116.56 ? 61   GLU B OE1 1 
ATOM   4305  O  OE2 . GLU B 1 103 ? 140.539 87.819  142.463 1.00 115.71 ? 61   GLU B OE2 1 
ATOM   4306  N  N   . ILE B 1 104 ? 141.786 91.085  147.523 1.00 102.41 ? 62   ILE B N   1 
ATOM   4307  C  CA  . ILE B 1 104 ? 142.343 92.055  148.465 1.00 103.54 ? 62   ILE B CA  1 
ATOM   4308  C  C   . ILE B 1 104 ? 141.526 92.191  149.737 1.00 103.47 ? 62   ILE B C   1 
ATOM   4309  O  O   . ILE B 1 104 ? 141.871 93.015  150.595 1.00 102.76 ? 62   ILE B O   1 
ATOM   4310  C  CB  . ILE B 1 104 ? 142.481 93.443  147.806 1.00 105.08 ? 62   ILE B CB  1 
ATOM   4311  C  CG1 . ILE B 1 104 ? 141.102 94.056  147.554 1.00 104.67 ? 62   ILE B CG1 1 
ATOM   4312  C  CG2 . ILE B 1 104 ? 143.268 93.341  146.509 1.00 104.68 ? 62   ILE B CG2 1 
ATOM   4313  C  CD1 . ILE B 1 104 ? 141.149 95.411  146.882 1.00 102.35 ? 62   ILE B CD1 1 
ATOM   4314  N  N   . LEU B 1 105 ? 140.458 91.415  149.892 1.00 90.82  ? 63   LEU B N   1 
ATOM   4315  C  CA  . LEU B 1 105 ? 139.591 91.486  151.060 1.00 88.32  ? 63   LEU B CA  1 
ATOM   4316  C  C   . LEU B 1 105 ? 139.773 90.238  151.913 1.00 88.00  ? 63   LEU B C   1 
ATOM   4317  O  O   . LEU B 1 105 ? 139.745 89.117  151.396 1.00 88.47  ? 63   LEU B O   1 
ATOM   4318  C  CB  . LEU B 1 105 ? 138.126 91.632  150.645 1.00 87.64  ? 63   LEU B CB  1 
ATOM   4319  C  CG  . LEU B 1 105 ? 137.817 92.720  149.618 1.00 85.97  ? 63   LEU B CG  1 
ATOM   4320  C  CD1 . LEU B 1 105 ? 136.429 92.520  149.042 1.00 86.77  ? 63   LEU B CD1 1 
ATOM   4321  C  CD2 . LEU B 1 105 ? 137.946 94.098  150.242 1.00 82.21  ? 63   LEU B CD2 1 
ATOM   4322  N  N   . GLY B 1 106 ? 139.957 90.437  153.218 1.00 77.58  ? 64   GLY B N   1 
ATOM   4323  C  CA  . GLY B 1 106 ? 140.146 89.335  154.129 1.00 77.13  ? 64   GLY B CA  1 
ATOM   4324  C  C   . GLY B 1 106 ? 138.839 88.678  154.514 1.00 77.09  ? 64   GLY B C   1 
ATOM   4325  O  O   . GLY B 1 106 ? 137.750 89.052  154.060 1.00 79.15  ? 64   GLY B O   1 
ATOM   4326  N  N   . PRO B 1 107 ? 138.940 87.666  155.373 1.00 80.05  ? 65   PRO B N   1 
ATOM   4327  C  CA  . PRO B 1 107 ? 137.736 86.962  155.827 1.00 79.72  ? 65   PRO B CA  1 
ATOM   4328  C  C   . PRO B 1 107 ? 136.885 87.836  156.733 1.00 81.14  ? 65   PRO B C   1 
ATOM   4329  O  O   . PRO B 1 107 ? 137.374 88.759  157.389 1.00 79.99  ? 65   PRO B O   1 
ATOM   4330  C  CB  . PRO B 1 107 ? 138.290 85.748  156.586 1.00 80.37  ? 65   PRO B CB  1 
ATOM   4331  C  CG  . PRO B 1 107 ? 139.778 85.747  156.347 1.00 79.51  ? 65   PRO B CG  1 
ATOM   4332  C  CD  . PRO B 1 107 ? 140.160 87.144  156.005 1.00 79.56  ? 65   PRO B CD  1 
ATOM   4333  N  N   . VAL B 1 108 ? 135.589 87.531  156.762 1.00 69.99  ? 66   VAL B N   1 
ATOM   4334  C  CA  . VAL B 1 108 ? 134.608 88.305  157.512 1.00 63.84  ? 66   VAL B CA  1 
ATOM   4335  C  C   . VAL B 1 108 ? 133.823 87.366  158.417 1.00 66.79  ? 66   VAL B C   1 
ATOM   4336  O  O   . VAL B 1 108 ? 133.414 86.278  157.995 1.00 73.82  ? 66   VAL B O   1 
ATOM   4337  C  CB  . VAL B 1 108 ? 133.659 89.075  156.571 1.00 58.79  ? 66   VAL B CB  1 
ATOM   4338  C  CG1 . VAL B 1 108 ? 132.551 89.749  157.358 1.00 60.71  ? 66   VAL B CG1 1 
ATOM   4339  C  CG2 . VAL B 1 108 ? 134.435 90.096  155.766 1.00 62.60  ? 66   VAL B CG2 1 
ATOM   4340  N  N   . VAL B 1 109 ? 133.617 87.786  159.662 1.00 55.10  ? 67   VAL B N   1 
ATOM   4341  C  CA  . VAL B 1 109 ? 132.829 87.043  160.637 1.00 55.59  ? 67   VAL B CA  1 
ATOM   4342  C  C   . VAL B 1 109 ? 131.441 87.664  160.701 1.00 57.51  ? 67   VAL B C   1 
ATOM   4343  O  O   . VAL B 1 109 ? 131.305 88.884  160.858 1.00 65.12  ? 67   VAL B O   1 
ATOM   4344  C  CB  . VAL B 1 109 ? 133.505 87.051  162.018 1.00 59.07  ? 67   VAL B CB  1 
ATOM   4345  C  CG1 . VAL B 1 109 ? 132.707 86.226  163.004 1.00 59.54  ? 67   VAL B CG1 1 
ATOM   4346  C  CG2 . VAL B 1 109 ? 134.927 86.530  161.912 1.00 60.82  ? 67   VAL B CG2 1 
ATOM   4347  N  N   . GLN B 1 110 ? 130.408 86.833  160.574 1.00 52.50  ? 68   GLN B N   1 
ATOM   4348  C  CA  . GLN B 1 110 ? 129.031 87.304  160.463 1.00 51.40  ? 68   GLN B CA  1 
ATOM   4349  C  C   . GLN B 1 110 ? 128.197 86.712  161.593 1.00 57.90  ? 68   GLN B C   1 
ATOM   4350  O  O   . GLN B 1 110 ? 127.977 85.497  161.637 1.00 66.94  ? 68   GLN B O   1 
ATOM   4351  C  CB  . GLN B 1 110 ? 128.448 86.932  159.101 1.00 49.85  ? 68   GLN B CB  1 
ATOM   4352  C  CG  . GLN B 1 110 ? 129.342 87.297  157.930 1.00 52.62  ? 68   GLN B CG  1 
ATOM   4353  C  CD  . GLN B 1 110 ? 128.669 87.076  156.593 1.00 57.33  ? 68   GLN B CD  1 
ATOM   4354  O  OE1 . GLN B 1 110 ? 127.564 86.540  156.523 1.00 60.22  ? 68   GLN B OE1 1 
ATOM   4355  N  NE2 . GLN B 1 110 ? 129.333 87.488  155.521 1.00 56.30  ? 68   GLN B NE2 1 
ATOM   4356  N  N   . PHE B 1 111 ? 127.734 87.568  162.502 1.00 50.95  ? 69   PHE B N   1 
ATOM   4357  C  CA  . PHE B 1 111 ? 126.832 87.154  163.578 1.00 51.22  ? 69   PHE B CA  1 
ATOM   4358  C  C   . PHE B 1 111 ? 125.391 87.487  163.194 1.00 51.49  ? 69   PHE B C   1 
ATOM   4359  O  O   . PHE B 1 111 ? 124.721 88.318  163.807 1.00 51.44  ? 69   PHE B O   1 
ATOM   4360  C  CB  . PHE B 1 111 ? 127.225 87.821  164.892 1.00 47.66  ? 69   PHE B CB  1 
ATOM   4361  C  CG  . PHE B 1 111 ? 128.635 87.546  165.320 1.00 49.33  ? 69   PHE B CG  1 
ATOM   4362  C  CD1 . PHE B 1 111 ? 129.669 88.367  164.909 1.00 52.68  ? 69   PHE B CD1 1 
ATOM   4363  C  CD2 . PHE B 1 111 ? 128.926 86.469  166.137 1.00 53.79  ? 69   PHE B CD2 1 
ATOM   4364  C  CE1 . PHE B 1 111 ? 130.965 88.120  165.305 1.00 54.51  ? 69   PHE B CE1 1 
ATOM   4365  C  CE2 . PHE B 1 111 ? 130.222 86.216  166.535 1.00 56.01  ? 69   PHE B CE2 1 
ATOM   4366  C  CZ  . PHE B 1 111 ? 131.243 87.042  166.117 1.00 55.96  ? 69   PHE B CZ  1 
ATOM   4367  N  N   . LEU B 1 112 ? 124.919 86.809  162.152 1.00 50.50  ? 70   LEU B N   1 
ATOM   4368  C  CA  . LEU B 1 112 ? 123.610 87.110  161.588 1.00 49.77  ? 70   LEU B CA  1 
ATOM   4369  C  C   . LEU B 1 112 ? 122.491 86.720  162.547 1.00 51.57  ? 70   LEU B C   1 
ATOM   4370  O  O   . LEU B 1 112 ? 122.441 85.587  163.032 1.00 61.20  ? 70   LEU B O   1 
ATOM   4371  C  CB  . LEU B 1 112 ? 123.435 86.380  160.258 1.00 51.26  ? 70   LEU B CB  1 
ATOM   4372  C  CG  . LEU B 1 112 ? 123.767 87.129  158.967 1.00 51.38  ? 70   LEU B CG  1 
ATOM   4373  C  CD1 . LEU B 1 112 ? 125.006 87.987  159.129 1.00 50.20  ? 70   LEU B CD1 1 
ATOM   4374  C  CD2 . LEU B 1 112 ? 123.953 86.144  157.827 1.00 54.66  ? 70   LEU B CD2 1 
ATOM   4375  N  N   . GLY B 1 113 ? 121.586 87.659  162.811 1.00 38.23  ? 71   GLY B N   1 
ATOM   4376  C  CA  . GLY B 1 113 ? 120.354 87.351  163.508 1.00 40.58  ? 71   GLY B CA  1 
ATOM   4377  C  C   . GLY B 1 113 ? 120.373 87.465  165.015 1.00 42.16  ? 71   GLY B C   1 
ATOM   4378  O  O   . GLY B 1 113 ? 119.478 86.914  165.666 1.00 42.85  ? 71   GLY B O   1 
ATOM   4379  N  N   . VAL B 1 114 ? 121.348 88.151  165.595 1.00 41.91  ? 72   VAL B N   1 
ATOM   4380  C  CA  . VAL B 1 114 ? 121.371 88.287  167.058 1.00 42.97  ? 72   VAL B CA  1 
ATOM   4381  C  C   . VAL B 1 114 ? 120.274 89.255  167.494 1.00 41.63  ? 72   VAL B C   1 
ATOM   4382  O  O   . VAL B 1 114 ? 120.186 90.374  166.957 1.00 45.96  ? 72   VAL B O   1 
ATOM   4383  C  CB  . VAL B 1 114 ? 122.752 88.750  167.534 1.00 41.38  ? 72   VAL B CB  1 
ATOM   4384  C  CG1 . VAL B 1 114 ? 123.210 89.973  166.772 1.00 38.32  ? 72   VAL B CG1 1 
ATOM   4385  C  CG2 . VAL B 1 114 ? 122.728 89.040  169.024 1.00 40.13  ? 72   VAL B CG2 1 
ATOM   4386  N  N   . PRO B 1 115 ? 119.407 88.873  168.428 1.00 49.06  ? 73   PRO B N   1 
ATOM   4387  C  CA  . PRO B 1 115 ? 118.324 89.769  168.844 1.00 48.76  ? 73   PRO B CA  1 
ATOM   4388  C  C   . PRO B 1 115 ? 118.833 90.920  169.695 1.00 52.16  ? 73   PRO B C   1 
ATOM   4389  O  O   . PRO B 1 115 ? 119.911 90.867  170.290 1.00 55.59  ? 73   PRO B O   1 
ATOM   4390  C  CB  . PRO B 1 115 ? 117.399 88.852  169.651 1.00 46.24  ? 73   PRO B CB  1 
ATOM   4391  C  CG  . PRO B 1 115 ? 118.305 87.799  170.184 1.00 50.96  ? 73   PRO B CG  1 
ATOM   4392  C  CD  . PRO B 1 115 ? 119.358 87.580  169.131 1.00 52.70  ? 73   PRO B CD  1 
ATOM   4393  N  N   . TYR B 1 116 ? 118.024 91.981  169.749 1.00 51.24  ? 74   TYR B N   1 
ATOM   4394  C  CA  . TYR B 1 116 ? 118.354 93.140  170.566 1.00 51.43  ? 74   TYR B CA  1 
ATOM   4395  C  C   . TYR B 1 116 ? 117.186 93.674  171.384 1.00 51.56  ? 74   TYR B C   1 
ATOM   4396  O  O   . TYR B 1 116 ? 117.377 94.639  172.131 1.00 55.65  ? 74   TYR B O   1 
ATOM   4397  C  CB  . TYR B 1 116 ? 118.920 94.272  169.691 1.00 48.61  ? 74   TYR B CB  1 
ATOM   4398  C  CG  . TYR B 1 116 ? 117.947 94.840  168.683 1.00 50.80  ? 74   TYR B CG  1 
ATOM   4399  C  CD1 . TYR B 1 116 ? 117.812 94.274  167.425 1.00 48.98  ? 74   TYR B CD1 1 
ATOM   4400  C  CD2 . TYR B 1 116 ? 117.172 95.952  168.984 1.00 51.52  ? 74   TYR B CD2 1 
ATOM   4401  C  CE1 . TYR B 1 116 ? 116.931 94.792  166.499 1.00 51.43  ? 74   TYR B CE1 1 
ATOM   4402  C  CE2 . TYR B 1 116 ? 116.286 96.476  168.065 1.00 47.11  ? 74   TYR B CE2 1 
ATOM   4403  C  CZ  . TYR B 1 116 ? 116.170 95.892  166.825 1.00 49.48  ? 74   TYR B CZ  1 
ATOM   4404  O  OH  . TYR B 1 116 ? 115.290 96.409  165.904 1.00 54.09  ? 74   TYR B OH  1 
ATOM   4405  N  N   . ALA B 1 117 ? 115.996 93.088  171.278 1.00 55.97  ? 75   ALA B N   1 
ATOM   4406  C  CA  . ALA B 1 117 ? 114.859 93.532  172.072 1.00 59.44  ? 75   ALA B CA  1 
ATOM   4407  C  C   . ALA B 1 117 ? 113.835 92.410  172.142 1.00 65.49  ? 75   ALA B C   1 
ATOM   4408  O  O   . ALA B 1 117 ? 113.854 91.476  171.336 1.00 68.98  ? 75   ALA B O   1 
ATOM   4409  C  CB  . ALA B 1 117 ? 114.229 94.804  171.496 1.00 60.85  ? 75   ALA B CB  1 
ATOM   4410  N  N   . THR B 1 118 ? 112.941 92.516  173.121 1.00 74.89  ? 76   THR B N   1 
ATOM   4411  C  CA  . THR B 1 118 ? 111.907 91.507  173.296 1.00 74.63  ? 76   THR B CA  1 
ATOM   4412  C  C   . THR B 1 118 ? 110.931 91.543  172.121 1.00 74.08  ? 76   THR B C   1 
ATOM   4413  O  O   . THR B 1 118 ? 110.629 92.620  171.597 1.00 76.25  ? 76   THR B O   1 
ATOM   4414  C  CB  . THR B 1 118 ? 111.151 91.730  174.605 1.00 76.89  ? 76   THR B CB  1 
ATOM   4415  O  OG1 . THR B 1 118 ? 111.025 93.136  174.853 1.00 79.00  ? 76   THR B OG1 1 
ATOM   4416  C  CG2 . THR B 1 118 ? 111.889 91.078  175.763 1.00 74.56  ? 76   THR B CG2 1 
ATOM   4417  N  N   . PRO B 1 119 ? 110.428 90.392  171.685 1.00 74.74  ? 77   PRO B N   1 
ATOM   4418  C  CA  . PRO B 1 119 ? 109.500 90.363  170.550 1.00 77.25  ? 77   PRO B CA  1 
ATOM   4419  C  C   . PRO B 1 119 ? 108.202 91.074  170.884 1.00 79.16  ? 77   PRO B C   1 
ATOM   4420  O  O   . PRO B 1 119 ? 107.516 90.711  171.851 1.00 81.54  ? 77   PRO B O   1 
ATOM   4421  C  CB  . PRO B 1 119 ? 109.266 88.861  170.322 1.00 80.94  ? 77   PRO B CB  1 
ATOM   4422  C  CG  . PRO B 1 119 ? 110.417 88.183  170.986 1.00 78.83  ? 77   PRO B CG  1 
ATOM   4423  C  CD  . PRO B 1 119 ? 110.762 89.040  172.160 1.00 77.61  ? 77   PRO B CD  1 
ATOM   4424  N  N   . PRO B 1 120 ? 107.828 92.091  170.106 1.00 77.15  ? 78   PRO B N   1 
ATOM   4425  C  CA  . PRO B 1 120 ? 106.545 92.795  170.318 1.00 78.74  ? 78   PRO B CA  1 
ATOM   4426  C  C   . PRO B 1 120 ? 105.376 92.071  169.652 1.00 78.96  ? 78   PRO B C   1 
ATOM   4427  O  O   . PRO B 1 120 ? 104.881 92.432  168.586 1.00 77.82  ? 78   PRO B O   1 
ATOM   4428  C  CB  . PRO B 1 120 ? 106.812 94.164  169.690 1.00 74.14  ? 78   PRO B CB  1 
ATOM   4429  C  CG  . PRO B 1 120 ? 107.765 93.867  168.576 1.00 71.56  ? 78   PRO B CG  1 
ATOM   4430  C  CD  . PRO B 1 120 ? 108.606 92.685  169.006 1.00 72.27  ? 78   PRO B CD  1 
ATOM   4431  N  N   . LEU B 1 121 ? 104.912 91.009  170.308 1.00 83.08  ? 79   LEU B N   1 
ATOM   4432  C  CA  . LEU B 1 121 ? 103.914 90.110  169.743 1.00 83.25  ? 79   LEU B CA  1 
ATOM   4433  C  C   . LEU B 1 121 ? 102.523 90.304  170.328 1.00 83.91  ? 79   LEU B C   1 
ATOM   4434  O  O   . LEU B 1 121 ? 101.568 90.545  169.584 1.00 83.10  ? 79   LEU B O   1 
ATOM   4435  C  CB  . LEU B 1 121 ? 104.360 88.655  169.942 1.00 84.07  ? 79   LEU B CB  1 
ATOM   4436  C  CG  . LEU B 1 121 ? 105.201 88.043  168.821 1.00 83.04  ? 79   LEU B CG  1 
ATOM   4437  C  CD1 . LEU B 1 121 ? 105.954 86.823  169.319 1.00 81.32  ? 79   LEU B CD1 1 
ATOM   4438  C  CD2 . LEU B 1 121 ? 104.314 87.676  167.646 1.00 83.51  ? 79   LEU B CD2 1 
ATOM   4439  N  N   . GLY B 1 122 ? 102.378 90.205  171.647 1.00 93.51  ? 80   GLY B N   1 
ATOM   4440  C  CA  . GLY B 1 122 ? 101.066 90.263  172.261 1.00 95.02  ? 80   GLY B CA  1 
ATOM   4441  C  C   . GLY B 1 122 ? 100.667 91.648  172.722 1.00 93.29  ? 80   GLY B C   1 
ATOM   4442  O  O   . GLY B 1 122 ? 100.483 92.553  171.903 1.00 91.44  ? 80   GLY B O   1 
ATOM   4443  N  N   . ALA B 1 123 ? 100.524 91.825  174.037 1.00 96.63  ? 81   ALA B N   1 
ATOM   4444  C  CA  . ALA B 1 123 ? 100.181 93.128  174.590 1.00 96.81  ? 81   ALA B CA  1 
ATOM   4445  C  C   . ALA B 1 123 ? 101.312 94.137  174.456 1.00 95.68  ? 81   ALA B C   1 
ATOM   4446  O  O   . ALA B 1 123 ? 101.081 95.332  174.667 1.00 92.75  ? 81   ALA B O   1 
ATOM   4447  C  CB  . ALA B 1 123 ? 99.784  92.989  176.060 1.00 96.27  ? 81   ALA B CB  1 
ATOM   4448  N  N   . ARG B 1 124 ? 102.519 93.690  174.113 1.00 90.43  ? 82   ARG B N   1 
ATOM   4449  C  CA  . ARG B 1 124 ? 103.633 94.594  173.869 1.00 88.91  ? 82   ARG B CA  1 
ATOM   4450  C  C   . ARG B 1 124 ? 103.572 95.244  172.494 1.00 89.04  ? 82   ARG B C   1 
ATOM   4451  O  O   . ARG B 1 124 ? 104.404 96.108  172.200 1.00 87.69  ? 82   ARG B O   1 
ATOM   4452  C  CB  . ARG B 1 124 ? 104.958 93.849  174.034 1.00 87.10  ? 82   ARG B CB  1 
ATOM   4453  C  CG  . ARG B 1 124 ? 105.461 93.797  175.469 1.00 87.62  ? 82   ARG B CG  1 
ATOM   4454  C  CD  . ARG B 1 124 ? 106.713 92.944  175.595 1.00 86.99  ? 82   ARG B CD  1 
ATOM   4455  N  NE  . ARG B 1 124 ? 106.401 91.555  175.911 1.00 88.12  ? 82   ARG B NE  1 
ATOM   4456  C  CZ  . ARG B 1 124 ? 106.166 90.611  175.010 1.00 89.60  ? 82   ARG B CZ  1 
ATOM   4457  N  NH1 . ARG B 1 124 ? 106.196 90.870  173.714 1.00 87.20  ? 82   ARG B NH1 1 
ATOM   4458  N  NH2 . ARG B 1 124 ? 105.894 89.376  175.420 1.00 91.13  ? 82   ARG B NH2 1 
ATOM   4459  N  N   . ARG B 1 125 ? 102.628 94.840  171.647 1.00 85.93  ? 83   ARG B N   1 
ATOM   4460  C  CA  . ARG B 1 125 ? 102.421 95.527  170.381 1.00 82.00  ? 83   ARG B CA  1 
ATOM   4461  C  C   . ARG B 1 125 ? 101.976 96.961  170.639 1.00 82.78  ? 83   ARG B C   1 
ATOM   4462  O  O   . ARG B 1 125 ? 101.208 97.231  171.567 1.00 87.96  ? 83   ARG B O   1 
ATOM   4463  C  CB  . ARG B 1 125 ? 101.381 94.786  169.539 1.00 80.98  ? 83   ARG B CB  1 
ATOM   4464  C  CG  . ARG B 1 125 ? 101.069 95.444  168.205 1.00 81.87  ? 83   ARG B CG  1 
ATOM   4465  C  CD  . ARG B 1 125 ? 99.862  94.805  167.540 1.00 81.41  ? 83   ARG B CD  1 
ATOM   4466  N  NE  . ARG B 1 125 ? 100.155 93.466  167.044 1.00 82.25  ? 83   ARG B NE  1 
ATOM   4467  C  CZ  . ARG B 1 125 ? 99.268  92.678  166.452 1.00 81.12  ? 83   ARG B CZ  1 
ATOM   4468  N  NH1 . ARG B 1 125 ? 98.019  93.066  166.261 1.00 83.33  ? 83   ARG B NH1 1 
ATOM   4469  N  NH2 . ARG B 1 125 ? 99.645  91.471  166.040 1.00 80.84  ? 83   ARG B NH2 1 
ATOM   4470  N  N   . PHE B 1 126 ? 102.473 97.883  169.813 1.00 69.73  ? 84   PHE B N   1 
ATOM   4471  C  CA  . PHE B 1 126 ? 102.242 99.318  169.992 1.00 67.64  ? 84   PHE B CA  1 
ATOM   4472  C  C   . PHE B 1 126 ? 102.754 99.793  171.350 1.00 68.40  ? 84   PHE B C   1 
ATOM   4473  O  O   . PHE B 1 126 ? 102.153 100.652 171.998 1.00 66.74  ? 84   PHE B O   1 
ATOM   4474  C  CB  . PHE B 1 126 ? 100.765 99.677  169.808 1.00 67.39  ? 84   PHE B CB  1 
ATOM   4475  C  CG  . PHE B 1 126 ? 100.228 99.347  168.445 1.00 68.23  ? 84   PHE B CG  1 
ATOM   4476  C  CD1 . PHE B 1 126 ? 100.990 99.573  167.313 1.00 68.02  ? 84   PHE B CD1 1 
ATOM   4477  C  CD2 . PHE B 1 126 ? 98.960  98.813  168.297 1.00 70.86  ? 84   PHE B CD2 1 
ATOM   4478  C  CE1 . PHE B 1 126 ? 100.499 99.272  166.060 1.00 68.83  ? 84   PHE B CE1 1 
ATOM   4479  C  CE2 . PHE B 1 126 ? 98.464  98.509  167.045 1.00 69.31  ? 84   PHE B CE2 1 
ATOM   4480  C  CZ  . PHE B 1 126 ? 99.234  98.739  165.926 1.00 68.58  ? 84   PHE B CZ  1 
ATOM   4481  N  N   . GLN B 1 127 ? 103.873 99.222  171.784 1.00 78.85  ? 85   GLN B N   1 
ATOM   4482  C  CA  . GLN B 1 127 ? 104.578 99.627  172.988 1.00 79.16  ? 85   GLN B CA  1 
ATOM   4483  C  C   . GLN B 1 127 ? 106.067 99.724  172.693 1.00 78.54  ? 85   GLN B C   1 
ATOM   4484  O  O   . GLN B 1 127 ? 106.579 99.005  171.828 1.00 82.24  ? 85   GLN B O   1 
ATOM   4485  C  CB  . GLN B 1 127 ? 104.346 98.634  174.138 1.00 80.41  ? 85   GLN B CB  1 
ATOM   4486  C  CG  . GLN B 1 127 ? 102.907 98.552  174.618 1.00 80.94  ? 85   GLN B CG  1 
ATOM   4487  C  CD  . GLN B 1 127 ? 102.543 99.687  175.553 1.00 80.78  ? 85   GLN B CD  1 
ATOM   4488  O  OE1 . GLN B 1 127 ? 101.543 100.375 175.354 1.00 80.89  ? 85   GLN B OE1 1 
ATOM   4489  N  NE2 . GLN B 1 127 ? 103.356 99.887  176.584 1.00 80.74  ? 85   GLN B NE2 1 
ATOM   4490  N  N   . PRO B 1 128 ? 106.782 100.608 173.385 1.00 71.42  ? 86   PRO B N   1 
ATOM   4491  C  CA  . PRO B 1 128 ? 108.216 100.729 173.143 1.00 71.93  ? 86   PRO B CA  1 
ATOM   4492  C  C   . PRO B 1 128 ? 108.932 99.449  173.519 1.00 73.86  ? 86   PRO B C   1 
ATOM   4493  O  O   . PRO B 1 128 ? 108.509 98.725  174.441 1.00 79.08  ? 86   PRO B O   1 
ATOM   4494  C  CB  . PRO B 1 128 ? 108.631 101.897 174.050 1.00 73.63  ? 86   PRO B CB  1 
ATOM   4495  C  CG  . PRO B 1 128 ? 107.534 102.030 175.048 1.00 75.51  ? 86   PRO B CG  1 
ATOM   4496  C  CD  . PRO B 1 128 ? 106.292 101.613 174.341 1.00 72.87  ? 86   PRO B CD  1 
ATOM   4497  N  N   . PRO B 1 129 ? 110.024 99.125  172.832 1.00 65.13  ? 87   PRO B N   1 
ATOM   4498  C  CA  . PRO B 1 129 ? 110.740 97.881  173.125 1.00 68.76  ? 87   PRO B CA  1 
ATOM   4499  C  C   . PRO B 1 129 ? 111.492 97.959  174.444 1.00 69.39  ? 87   PRO B C   1 
ATOM   4500  O  O   . PRO B 1 129 ? 111.784 99.036  174.969 1.00 71.95  ? 87   PRO B O   1 
ATOM   4501  C  CB  . PRO B 1 129 ? 111.707 97.749  171.946 1.00 67.15  ? 87   PRO B CB  1 
ATOM   4502  C  CG  . PRO B 1 129 ? 111.987 99.160  171.568 1.00 64.30  ? 87   PRO B CG  1 
ATOM   4503  C  CD  . PRO B 1 129 ? 110.686 99.899  171.768 1.00 61.03  ? 87   PRO B CD  1 
ATOM   4504  N  N   . GLU B 1 130 ? 111.806 96.785  174.977 1.00 71.04  ? 88   GLU B N   1 
ATOM   4505  C  CA  . GLU B 1 130 ? 112.564 96.643  176.211 1.00 73.70  ? 88   GLU B CA  1 
ATOM   4506  C  C   . GLU B 1 130 ? 113.816 95.811  175.949 1.00 74.56  ? 88   GLU B C   1 
ATOM   4507  O  O   . GLU B 1 130 ? 114.077 95.371  174.828 1.00 74.74  ? 88   GLU B O   1 
ATOM   4508  C  CB  . GLU B 1 130 ? 111.709 96.006  177.310 1.00 75.61  ? 88   GLU B CB  1 
ATOM   4509  C  CG  . GLU B 1 130 ? 110.220 96.268  177.177 1.00 75.08  ? 88   GLU B CG  1 
ATOM   4510  C  CD  . GLU B 1 130 ? 109.400 95.450  178.154 1.00 79.92  ? 88   GLU B CD  1 
ATOM   4511  O  OE1 . GLU B 1 130 ? 109.504 95.700  179.373 1.00 77.55  ? 88   GLU B OE1 1 
ATOM   4512  O  OE2 . GLU B 1 130 ? 108.656 94.555  177.703 1.00 81.62  ? 88   GLU B OE2 1 
ATOM   4513  N  N   . ALA B 1 131 ? 114.595 95.601  177.006 1.00 75.83  ? 89   ALA B N   1 
ATOM   4514  C  CA  . ALA B 1 131 ? 115.797 94.794  176.897 1.00 75.92  ? 89   ALA B CA  1 
ATOM   4515  C  C   . ALA B 1 131 ? 115.431 93.338  176.608 1.00 79.16  ? 89   ALA B C   1 
ATOM   4516  O  O   . ALA B 1 131 ? 114.360 92.870  177.004 1.00 81.45  ? 89   ALA B O   1 
ATOM   4517  C  CB  . ALA B 1 131 ? 116.614 94.883  178.183 1.00 77.18  ? 89   ALA B CB  1 
ATOM   4518  N  N   . PRO B 1 132 ? 116.305 92.598  175.917 1.00 77.56  ? 90   PRO B N   1 
ATOM   4519  C  CA  . PRO B 1 132 ? 115.980 91.204  175.583 1.00 76.82  ? 90   PRO B CA  1 
ATOM   4520  C  C   . PRO B 1 132 ? 116.025 90.288  176.795 1.00 82.61  ? 90   PRO B C   1 
ATOM   4521  O  O   . PRO B 1 132 ? 116.297 90.732  177.914 1.00 83.77  ? 90   PRO B O   1 
ATOM   4522  C  CB  . PRO B 1 132 ? 117.055 90.818  174.555 1.00 73.25  ? 90   PRO B CB  1 
ATOM   4523  C  CG  . PRO B 1 132 ? 117.847 92.062  174.286 1.00 75.52  ? 90   PRO B CG  1 
ATOM   4524  C  CD  . PRO B 1 132 ? 117.640 92.980  175.435 1.00 76.37  ? 90   PRO B CD  1 
ATOM   4525  N  N   . ALA B 1 133 ? 115.759 89.005  176.578 1.00 95.31  ? 91   ALA B N   1 
ATOM   4526  C  CA  . ALA B 1 133 ? 115.813 87.997  177.626 1.00 92.49  ? 91   ALA B CA  1 
ATOM   4527  C  C   . ALA B 1 133 ? 117.061 87.148  177.436 1.00 93.90  ? 91   ALA B C   1 
ATOM   4528  O  O   . ALA B 1 133 ? 117.305 86.635  176.339 1.00 95.28  ? 91   ALA B O   1 
ATOM   4529  C  CB  . ALA B 1 133 ? 114.561 87.118  177.609 1.00 91.52  ? 91   ALA B CB  1 
ATOM   4530  N  N   . SER B 1 134 ? 117.847 87.009  178.500 1.00 100.91 ? 92   SER B N   1 
ATOM   4531  C  CA  . SER B 1 134 ? 119.073 86.227  178.431 1.00 99.79  ? 92   SER B CA  1 
ATOM   4532  C  C   . SER B 1 134 ? 118.759 84.758  178.175 1.00 102.12 ? 92   SER B C   1 
ATOM   4533  O  O   . SER B 1 134 ? 117.844 84.187  178.775 1.00 103.25 ? 92   SER B O   1 
ATOM   4534  C  CB  . SER B 1 134 ? 119.869 86.375  179.726 1.00 99.85  ? 92   SER B CB  1 
ATOM   4535  O  OG  . SER B 1 134 ? 119.014 86.330  180.855 1.00 101.85 ? 92   SER B OG  1 
ATOM   4536  N  N   . TRP B 1 135 ? 119.527 84.147  177.275 1.00 101.44 ? 93   TRP B N   1 
ATOM   4537  C  CA  . TRP B 1 135 ? 119.346 82.745  176.926 1.00 100.71 ? 93   TRP B CA  1 
ATOM   4538  C  C   . TRP B 1 135 ? 120.463 81.918  177.539 1.00 101.71 ? 93   TRP B C   1 
ATOM   4539  O  O   . TRP B 1 135 ? 121.644 82.187  177.274 1.00 99.96  ? 93   TRP B O   1 
ATOM   4540  C  CB  . TRP B 1 135 ? 119.312 82.558  175.408 1.00 100.59 ? 93   TRP B CB  1 
ATOM   4541  C  CG  . TRP B 1 135 ? 120.481 83.155  174.681 1.00 101.48 ? 93   TRP B CG  1 
ATOM   4542  C  CD1 . TRP B 1 135 ? 121.623 82.513  174.299 1.00 100.22 ? 93   TRP B CD1 1 
ATOM   4543  C  CD2 . TRP B 1 135 ? 120.615 84.510  174.236 1.00 102.13 ? 93   TRP B CD2 1 
ATOM   4544  N  NE1 . TRP B 1 135 ? 122.463 83.386  173.651 1.00 99.63  ? 93   TRP B NE1 1 
ATOM   4545  C  CE2 . TRP B 1 135 ? 121.867 84.618  173.599 1.00 101.71 ? 93   TRP B CE2 1 
ATOM   4546  C  CE3 . TRP B 1 135 ? 119.800 85.643  174.317 1.00 100.17 ? 93   TRP B CE3 1 
ATOM   4547  C  CZ2 . TRP B 1 135 ? 122.323 85.813  173.047 1.00 100.55 ? 93   TRP B CZ2 1 
ATOM   4548  C  CZ3 . TRP B 1 135 ? 120.255 86.828  173.769 1.00 100.43 ? 93   TRP B CZ3 1 
ATOM   4549  C  CH2 . TRP B 1 135 ? 121.504 86.904  173.142 1.00 100.46 ? 93   TRP B CH2 1 
ATOM   4550  N  N   . PRO B 1 136 ? 120.150 80.922  178.369 1.00 111.22 ? 94   PRO B N   1 
ATOM   4551  C  CA  . PRO B 1 136 ? 121.206 80.081  178.951 1.00 110.87 ? 94   PRO B CA  1 
ATOM   4552  C  C   . PRO B 1 136 ? 121.796 79.157  177.895 1.00 109.92 ? 94   PRO B C   1 
ATOM   4553  O  O   . PRO B 1 136 ? 121.095 78.319  177.324 1.00 109.31 ? 94   PRO B O   1 
ATOM   4554  C  CB  . PRO B 1 136 ? 120.474 79.302  180.049 1.00 110.08 ? 94   PRO B CB  1 
ATOM   4555  C  CG  . PRO B 1 136 ? 119.052 79.257  179.590 1.00 110.13 ? 94   PRO B CG  1 
ATOM   4556  C  CD  . PRO B 1 136 ? 118.804 80.525  178.819 1.00 109.92 ? 94   PRO B CD  1 
ATOM   4557  N  N   . GLY B 1 137 ? 123.093 79.319  177.633 1.00 100.31 ? 95   GLY B N   1 
ATOM   4558  C  CA  . GLY B 1 137 ? 123.793 78.500  176.666 1.00 100.35 ? 95   GLY B CA  1 
ATOM   4559  C  C   . GLY B 1 137 ? 124.363 79.335  175.531 1.00 99.52  ? 95   GLY B C   1 
ATOM   4560  O  O   . GLY B 1 137 ? 124.790 80.478  175.731 1.00 98.69  ? 95   GLY B O   1 
ATOM   4561  N  N   . VAL B 1 138 ? 124.370 78.744  174.339 1.00 94.63  ? 96   VAL B N   1 
ATOM   4562  C  CA  . VAL B 1 138 ? 124.918 79.372  173.144 1.00 94.07  ? 96   VAL B CA  1 
ATOM   4563  C  C   . VAL B 1 138 ? 123.829 79.390  172.080 1.00 95.71  ? 96   VAL B C   1 
ATOM   4564  O  O   . VAL B 1 138 ? 123.178 78.367  171.837 1.00 96.36  ? 96   VAL B O   1 
ATOM   4565  C  CB  . VAL B 1 138 ? 126.171 78.631  172.639 1.00 91.65  ? 96   VAL B CB  1 
ATOM   4566  C  CG1 . VAL B 1 138 ? 126.321 78.801  171.144 1.00 91.35  ? 96   VAL B CG1 1 
ATOM   4567  C  CG2 . VAL B 1 138 ? 127.420 79.110  173.368 1.00 92.18  ? 96   VAL B CG2 1 
ATOM   4568  N  N   . ARG B 1 139 ? 123.626 80.548  171.456 1.00 90.54  ? 97   ARG B N   1 
ATOM   4569  C  CA  . ARG B 1 139 ? 122.634 80.711  170.401 1.00 87.92  ? 97   ARG B CA  1 
ATOM   4570  C  C   . ARG B 1 139 ? 123.316 80.676  169.039 1.00 85.95  ? 97   ARG B C   1 
ATOM   4571  O  O   . ARG B 1 139 ? 124.266 81.426  168.795 1.00 86.55  ? 97   ARG B O   1 
ATOM   4572  C  CB  . ARG B 1 139 ? 121.870 82.025  170.566 1.00 87.17  ? 97   ARG B CB  1 
ATOM   4573  C  CG  . ARG B 1 139 ? 120.855 82.290  169.463 1.00 90.48  ? 97   ARG B CG  1 
ATOM   4574  C  CD  . ARG B 1 139 ? 120.266 83.689  169.569 1.00 89.07  ? 97   ARG B CD  1 
ATOM   4575  N  NE  . ARG B 1 139 ? 119.057 83.833  168.766 1.00 86.97  ? 97   ARG B NE  1 
ATOM   4576  C  CZ  . ARG B 1 139 ? 117.825 83.829  169.256 1.00 87.68  ? 97   ARG B CZ  1 
ATOM   4577  N  NH1 . ARG B 1 139 ? 117.598 83.701  170.553 1.00 89.08  ? 97   ARG B NH1 1 
ATOM   4578  N  NH2 . ARG B 1 139 ? 116.795 83.953  168.424 1.00 83.58  ? 97   ARG B NH2 1 
ATOM   4579  N  N   . ASN B 1 140 ? 122.824 79.809  168.157 1.00 102.03 ? 98   ASN B N   1 
ATOM   4580  C  CA  . ASN B 1 140 ? 123.346 79.711  166.798 1.00 101.37 ? 98   ASN B CA  1 
ATOM   4581  C  C   . ASN B 1 140 ? 122.837 80.898  165.991 1.00 103.81 ? 98   ASN B C   1 
ATOM   4582  O  O   . ASN B 1 140 ? 121.634 81.013  165.735 1.00 105.76 ? 98   ASN B O   1 
ATOM   4583  C  CB  . ASN B 1 140 ? 122.929 78.393  166.153 1.00 103.67 ? 98   ASN B CB  1 
ATOM   4584  C  CG  . ASN B 1 140 ? 123.603 77.194  166.785 1.00 108.23 ? 98   ASN B CG  1 
ATOM   4585  O  OD1 . ASN B 1 140 ? 124.794 77.228  167.095 1.00 107.62 ? 98   ASN B OD1 1 
ATOM   4586  N  ND2 . ASN B 1 140 ? 122.844 76.122  166.981 1.00 110.52 ? 98   ASN B ND2 1 
ATOM   4587  N  N   . ALA B 1 141 ? 123.747 81.781  165.590 1.00 81.75  ? 99   ALA B N   1 
ATOM   4588  C  CA  . ALA B 1 141 ? 123.415 82.968  164.805 1.00 74.87  ? 99   ALA B CA  1 
ATOM   4589  C  C   . ALA B 1 141 ? 124.085 82.831  163.442 1.00 74.70  ? 99   ALA B C   1 
ATOM   4590  O  O   . ALA B 1 141 ? 125.186 83.339  163.220 1.00 73.58  ? 99   ALA B O   1 
ATOM   4591  C  CB  . ALA B 1 141 ? 123.855 84.235  165.533 1.00 73.39  ? 99   ALA B CB  1 
ATOM   4592  N  N   . THR B 1 142 ? 123.416 82.142  162.532 1.00 79.05  ? 100  THR B N   1 
ATOM   4593  C  CA  . THR B 1 142 ? 123.930 81.944  161.180 1.00 80.00  ? 100  THR B CA  1 
ATOM   4594  C  C   . THR B 1 142 ? 122.925 82.310  160.100 1.00 80.98  ? 100  THR B C   1 
ATOM   4595  O  O   . THR B 1 142 ? 123.311 82.886  159.080 1.00 79.35  ? 100  THR B O   1 
ATOM   4596  C  CB  . THR B 1 142 ? 124.375 80.482  160.999 1.00 82.02  ? 100  THR B CB  1 
ATOM   4597  O  OG1 . THR B 1 142 ? 125.325 80.138  162.016 1.00 82.55  ? 100  THR B OG1 1 
ATOM   4598  C  CG2 . THR B 1 142 ? 125.006 80.276  159.631 1.00 82.18  ? 100  THR B CG2 1 
ATOM   4599  N  N   . THR B 1 143 ? 121.647 82.008  160.302 1.00 77.50  ? 101  THR B N   1 
ATOM   4600  C  CA  . THR B 1 143 ? 120.628 82.253  159.294 1.00 77.23  ? 101  THR B CA  1 
ATOM   4601  C  C   . THR B 1 143 ? 120.106 83.680  159.390 1.00 76.39  ? 101  THR B C   1 
ATOM   4602  O  O   . THR B 1 143 ? 120.099 84.291  160.462 1.00 77.93  ? 101  THR B O   1 
ATOM   4603  C  CB  . THR B 1 143 ? 119.469 81.267  159.443 1.00 80.60  ? 101  THR B CB  1 
ATOM   4604  O  OG1 . THR B 1 143 ? 118.947 81.338  160.775 1.00 80.88  ? 101  THR B OG1 1 
ATOM   4605  C  CG2 . THR B 1 143 ? 119.940 79.847  159.164 1.00 78.97  ? 101  THR B CG2 1 
ATOM   4606  N  N   . LEU B 1 144 ? 119.671 84.206  158.252 1.00 67.22  ? 102  LEU B N   1 
ATOM   4607  C  CA  . LEU B 1 144 ? 119.134 85.560  158.214 1.00 66.12  ? 102  LEU B CA  1 
ATOM   4608  C  C   . LEU B 1 144 ? 117.827 85.624  158.996 1.00 67.17  ? 102  LEU B C   1 
ATOM   4609  O  O   . LEU B 1 144 ? 116.949 84.775  158.799 1.00 67.58  ? 102  LEU B O   1 
ATOM   4610  C  CB  . LEU B 1 144 ? 118.914 86.007  156.771 1.00 63.65  ? 102  LEU B CB  1 
ATOM   4611  C  CG  . LEU B 1 144 ? 120.168 86.467  156.027 1.00 63.54  ? 102  LEU B CG  1 
ATOM   4612  C  CD1 . LEU B 1 144 ? 119.848 86.797  154.580 1.00 63.86  ? 102  LEU B CD1 1 
ATOM   4613  C  CD2 . LEU B 1 144 ? 120.784 87.664  156.726 1.00 59.76  ? 102  LEU B CD2 1 
ATOM   4614  N  N   . PRO B 1 145 ? 117.659 86.598  159.885 1.00 61.37  ? 103  PRO B N   1 
ATOM   4615  C  CA  . PRO B 1 145 ? 116.444 86.669  160.697 1.00 59.56  ? 103  PRO B CA  1 
ATOM   4616  C  C   . PRO B 1 145 ? 115.242 87.048  159.852 1.00 59.50  ? 103  PRO B C   1 
ATOM   4617  O  O   . PRO B 1 145 ? 115.393 87.621  158.763 1.00 59.64  ? 103  PRO B O   1 
ATOM   4618  C  CB  . PRO B 1 145 ? 116.772 87.762  161.723 1.00 57.85  ? 103  PRO B CB  1 
ATOM   4619  C  CG  . PRO B 1 145 ? 117.781 88.613  161.047 1.00 60.20  ? 103  PRO B CG  1 
ATOM   4620  C  CD  . PRO B 1 145 ? 118.597 87.691  160.189 1.00 59.88  ? 103  PRO B CD  1 
ATOM   4621  N  N   . PRO B 1 146 ? 114.032 86.734  160.314 1.00 61.89  ? 104  PRO B N   1 
ATOM   4622  C  CA  . PRO B 1 146 ? 112.835 87.098  159.549 1.00 61.00  ? 104  PRO B CA  1 
ATOM   4623  C  C   . PRO B 1 146 ? 112.669 88.607  159.447 1.00 60.15  ? 104  PRO B C   1 
ATOM   4624  O  O   . PRO B 1 146 ? 113.042 89.360  160.349 1.00 61.04  ? 104  PRO B O   1 
ATOM   4625  C  CB  . PRO B 1 146 ? 111.695 86.465  160.355 1.00 59.73  ? 104  PRO B CB  1 
ATOM   4626  C  CG  . PRO B 1 146 ? 112.242 86.305  161.730 1.00 59.97  ? 104  PRO B CG  1 
ATOM   4627  C  CD  . PRO B 1 146 ? 113.697 86.008  161.550 1.00 61.37  ? 104  PRO B CD  1 
ATOM   4628  N  N   . ALA B 1 147 ? 112.095 89.042  158.330 1.00 57.09  ? 105  ALA B N   1 
ATOM   4629  C  CA  . ALA B 1 147 ? 111.822 90.453  158.117 1.00 56.38  ? 105  ALA B CA  1 
ATOM   4630  C  C   . ALA B 1 147 ? 110.522 90.858  158.805 1.00 58.95  ? 105  ALA B C   1 
ATOM   4631  O  O   . ALA B 1 147 ? 109.653 90.030  159.089 1.00 67.38  ? 105  ALA B O   1 
ATOM   4632  C  CB  . ALA B 1 147 ? 111.746 90.769  156.624 1.00 52.30  ? 105  ALA B CB  1 
ATOM   4633  N  N   . CYS B 1 148 ? 110.401 92.153  159.079 1.00 55.63  ? 106  CYS B N   1 
ATOM   4634  C  CA  . CYS B 1 148 ? 109.198 92.669  159.710 1.00 54.77  ? 106  CYS B CA  1 
ATOM   4635  C  C   . CYS B 1 148 ? 108.026 92.622  158.730 1.00 57.80  ? 106  CYS B C   1 
ATOM   4636  O  O   . CYS B 1 148 ? 108.226 92.661  157.514 1.00 62.98  ? 106  CYS B O   1 
ATOM   4637  C  CB  . CYS B 1 148 ? 109.425 94.096  160.197 1.00 57.44  ? 106  CYS B CB  1 
ATOM   4638  S  SG  . CYS B 1 148 ? 110.561 94.213  161.595 1.00 68.08  ? 106  CYS B SG  1 
ATOM   4639  N  N   . PRO B 1 149 ? 106.794 92.522  159.235 1.00 59.63  ? 107  PRO B N   1 
ATOM   4640  C  CA  . PRO B 1 149 ? 105.640 92.399  158.335 1.00 61.04  ? 107  PRO B CA  1 
ATOM   4641  C  C   . PRO B 1 149 ? 105.518 93.598  157.407 1.00 60.07  ? 107  PRO B C   1 
ATOM   4642  O  O   . PRO B 1 149 ? 105.717 94.746  157.810 1.00 61.19  ? 107  PRO B O   1 
ATOM   4643  C  CB  . PRO B 1 149 ? 104.449 92.306  159.296 1.00 62.41  ? 107  PRO B CB  1 
ATOM   4644  C  CG  . PRO B 1 149 ? 105.034 91.845  160.587 1.00 61.74  ? 107  PRO B CG  1 
ATOM   4645  C  CD  . PRO B 1 149 ? 106.394 92.462  160.651 1.00 62.12  ? 107  PRO B CD  1 
ATOM   4646  N  N   . GLN B 1 150 ? 105.174 93.316  156.155 1.00 61.75  ? 108  GLN B N   1 
ATOM   4647  C  CA  . GLN B 1 150 ? 105.072 94.338  155.121 1.00 58.83  ? 108  GLN B CA  1 
ATOM   4648  C  C   . GLN B 1 150 ? 104.305 93.747  153.945 1.00 64.04  ? 108  GLN B C   1 
ATOM   4649  O  O   . GLN B 1 150 ? 103.840 92.605  153.992 1.00 70.65  ? 108  GLN B O   1 
ATOM   4650  C  CB  . GLN B 1 150 ? 106.456 94.836  154.700 1.00 59.46  ? 108  GLN B CB  1 
ATOM   4651  C  CG  . GLN B 1 150 ? 107.398 93.730  154.268 1.00 61.50  ? 108  GLN B CG  1 
ATOM   4652  C  CD  . GLN B 1 150 ? 108.849 94.080  154.510 1.00 61.72  ? 108  GLN B CD  1 
ATOM   4653  O  OE1 . GLN B 1 150 ? 109.526 94.611  153.632 1.00 59.44  ? 108  GLN B OE1 1 
ATOM   4654  N  NE2 . GLN B 1 150 ? 109.335 93.787  155.709 1.00 64.85  ? 108  GLN B NE2 1 
ATOM   4655  N  N   . ASN B 1 151 ? 104.179 94.538  152.879 1.00 75.46  ? 109  ASN B N   1 
ATOM   4656  C  CA  . ASN B 1 151 ? 103.433 94.110  151.697 1.00 75.39  ? 109  ASN B CA  1 
ATOM   4657  C  C   . ASN B 1 151 ? 104.075 94.774  150.483 1.00 75.90  ? 109  ASN B C   1 
ATOM   4658  O  O   . ASN B 1 151 ? 103.771 95.930  150.173 1.00 77.42  ? 109  ASN B O   1 
ATOM   4659  C  CB  . ASN B 1 151 ? 101.960 94.473  151.824 1.00 77.35  ? 109  ASN B CB  1 
ATOM   4660  C  CG  . ASN B 1 151 ? 101.093 93.767  150.802 1.00 79.40  ? 109  ASN B CG  1 
ATOM   4661  O  OD1 . ASN B 1 151 ? 101.588 93.235  149.809 1.00 81.49  ? 109  ASN B OD1 1 
ATOM   4662  N  ND2 . ASN B 1 151 ? 99.787  93.761  151.042 1.00 81.30  ? 109  ASN B ND2 1 
ATOM   4663  N  N   . LEU B 1 152 ? 104.959 94.039  149.804 1.00 75.54  ? 110  LEU B N   1 
ATOM   4664  C  CA  . LEU B 1 152 ? 105.613 94.584  148.619 1.00 74.53  ? 110  LEU B CA  1 
ATOM   4665  C  C   . LEU B 1 152 ? 104.653 94.659  147.439 1.00 77.19  ? 110  LEU B C   1 
ATOM   4666  O  O   . LEU B 1 152 ? 104.614 95.669  146.727 1.00 76.06  ? 110  LEU B O   1 
ATOM   4667  C  CB  . LEU B 1 152 ? 106.837 93.743  148.260 1.00 73.47  ? 110  LEU B CB  1 
ATOM   4668  C  CG  . LEU B 1 152 ? 108.068 93.901  149.153 1.00 74.07  ? 110  LEU B CG  1 
ATOM   4669  C  CD1 . LEU B 1 152 ? 109.334 93.641  148.359 1.00 76.64  ? 110  LEU B CD1 1 
ATOM   4670  C  CD2 . LEU B 1 152 ? 108.110 95.281  149.789 1.00 72.59  ? 110  LEU B CD2 1 
ATOM   4671  N  N   . HIS B 1 153 ? 103.871 93.605  147.216 1.00 89.79  ? 111  HIS B N   1 
ATOM   4672  C  CA  . HIS B 1 153 ? 102.930 93.561  146.097 1.00 89.52  ? 111  HIS B CA  1 
ATOM   4673  C  C   . HIS B 1 153 ? 101.595 94.194  146.494 1.00 88.22  ? 111  HIS B C   1 
ATOM   4674  O  O   . HIS B 1 153 ? 100.530 93.582  146.434 1.00 87.71  ? 111  HIS B O   1 
ATOM   4675  C  CB  . HIS B 1 153 ? 102.749 92.125  145.618 1.00 87.48  ? 111  HIS B CB  1 
ATOM   4676  C  CG  . HIS B 1 153 ? 103.973 91.544  144.981 1.00 91.17  ? 111  HIS B CG  1 
ATOM   4677  N  ND1 . HIS B 1 153 ? 104.279 91.729  143.650 1.00 90.55  ? 111  HIS B ND1 1 
ATOM   4678  C  CD2 . HIS B 1 153 ? 104.970 90.784  145.493 1.00 90.63  ? 111  HIS B CD2 1 
ATOM   4679  C  CE1 . HIS B 1 153 ? 105.410 91.107  143.369 1.00 89.33  ? 111  HIS B CE1 1 
ATOM   4680  N  NE2 . HIS B 1 153 ? 105.850 90.526  144.470 1.00 90.11  ? 111  HIS B NE2 1 
ATOM   4681  N  N   . GLY B 1 154 ? 101.678 95.454  146.909 1.00 85.28  ? 112  GLY B N   1 
ATOM   4682  C  CA  . GLY B 1 154 ? 100.530 96.236  147.303 1.00 84.29  ? 112  GLY B CA  1 
ATOM   4683  C  C   . GLY B 1 154 ? 100.562 97.609  146.657 1.00 87.89  ? 112  GLY B C   1 
ATOM   4684  O  O   . GLY B 1 154 ? 101.137 97.806  145.585 1.00 88.71  ? 112  GLY B O   1 
ATOM   4685  N  N   . ALA B 1 155 ? 99.929  98.562  147.330 1.00 84.10  ? 113  ALA B N   1 
ATOM   4686  C  CA  . ALA B 1 155 ? 99.873  99.943  146.852 1.00 83.19  ? 113  ALA B CA  1 
ATOM   4687  C  C   . ALA B 1 155 ? 100.978 100.777 147.497 1.00 81.71  ? 113  ALA B C   1 
ATOM   4688  O  O   . ALA B 1 155 ? 100.735 101.726 148.242 1.00 81.33  ? 113  ALA B O   1 
ATOM   4689  C  CB  . ALA B 1 155 ? 98.495  100.538 147.122 1.00 81.91  ? 113  ALA B CB  1 
ATOM   4690  N  N   . LEU B 1 156 ? 102.216 100.399 147.195 1.00 68.32  ? 114  LEU B N   1 
ATOM   4691  C  CA  . LEU B 1 156 ? 103.362 101.112 147.731 1.00 67.94  ? 114  LEU B CA  1 
ATOM   4692  C  C   . LEU B 1 156 ? 103.539 102.452 147.019 1.00 71.77  ? 114  LEU B C   1 
ATOM   4693  O  O   . LEU B 1 156 ? 103.268 102.568 145.821 1.00 72.21  ? 114  LEU B O   1 
ATOM   4694  C  CB  . LEU B 1 156 ? 104.631 100.278 147.577 1.00 64.13  ? 114  LEU B CB  1 
ATOM   4695  C  CG  . LEU B 1 156 ? 104.877 99.184  148.616 1.00 66.78  ? 114  LEU B CG  1 
ATOM   4696  C  CD1 . LEU B 1 156 ? 106.283 98.628  148.475 1.00 66.50  ? 114  LEU B CD1 1 
ATOM   4697  C  CD2 . LEU B 1 156 ? 104.646 99.715  150.020 1.00 67.69  ? 114  LEU B CD2 1 
ATOM   4698  N  N   . PRO B 1 157 ? 103.992 103.482 147.736 1.00 62.47  ? 115  PRO B N   1 
ATOM   4699  C  CA  . PRO B 1 157 ? 104.317 104.749 147.070 1.00 50.75  ? 115  PRO B CA  1 
ATOM   4700  C  C   . PRO B 1 157 ? 105.592 104.621 146.255 1.00 48.93  ? 115  PRO B C   1 
ATOM   4701  O  O   . PRO B 1 157 ? 106.690 104.586 146.816 1.00 57.12  ? 115  PRO B O   1 
ATOM   4702  C  CB  . PRO B 1 157 ? 104.488 105.735 148.235 1.00 44.56  ? 115  PRO B CB  1 
ATOM   4703  C  CG  . PRO B 1 157 ? 103.938 105.031 149.447 1.00 48.37  ? 115  PRO B CG  1 
ATOM   4704  C  CD  . PRO B 1 157 ? 104.135 103.575 149.196 1.00 55.44  ? 115  PRO B CD  1 
ATOM   4705  N  N   . ALA B 1 158 ? 105.459 104.553 144.931 1.00 37.63  ? 116  ALA B N   1 
ATOM   4706  C  CA  . ALA B 1 158 ? 106.614 104.312 144.077 1.00 40.64  ? 116  ALA B CA  1 
ATOM   4707  C  C   . ALA B 1 158 ? 107.480 105.548 143.883 1.00 38.22  ? 116  ALA B C   1 
ATOM   4708  O  O   . ALA B 1 158 ? 108.619 105.420 143.424 1.00 38.98  ? 116  ALA B O   1 
ATOM   4709  C  CB  . ALA B 1 158 ? 106.160 103.788 142.713 1.00 43.40  ? 116  ALA B CB  1 
ATOM   4710  N  N   . ILE B 1 159 ? 106.972 106.735 144.218 1.00 32.64  ? 117  ILE B N   1 
ATOM   4711  C  CA  . ILE B 1 159 ? 107.727 107.955 143.955 1.00 42.36  ? 117  ILE B CA  1 
ATOM   4712  C  C   . ILE B 1 159 ? 108.932 108.073 144.884 1.00 46.84  ? 117  ILE B C   1 
ATOM   4713  O  O   . ILE B 1 159 ? 109.977 108.602 144.487 1.00 49.28  ? 117  ILE B O   1 
ATOM   4714  C  CB  . ILE B 1 159 ? 106.802 109.184 144.054 1.00 37.86  ? 117  ILE B CB  1 
ATOM   4715  C  CG1 . ILE B 1 159 ? 107.536 110.443 143.591 1.00 36.76  ? 117  ILE B CG1 1 
ATOM   4716  C  CG2 . ILE B 1 159 ? 106.258 109.352 145.465 1.00 36.10  ? 117  ILE B CG2 1 
ATOM   4717  C  CD1 . ILE B 1 159 ? 108.159 110.307 142.222 1.00 34.84  ? 117  ILE B CD1 1 
ATOM   4718  N  N   . MET B 1 160 ? 108.822 107.581 146.118 1.00 39.35  ? 118  MET B N   1 
ATOM   4719  C  CA  . MET B 1 160 ? 109.879 107.736 147.108 1.00 33.33  ? 118  MET B CA  1 
ATOM   4720  C  C   . MET B 1 160 ? 110.796 106.525 147.219 1.00 39.33  ? 118  MET B C   1 
ATOM   4721  O  O   . MET B 1 160 ? 111.881 106.646 147.796 1.00 46.78  ? 118  MET B O   1 
ATOM   4722  C  CB  . MET B 1 160 ? 109.273 108.039 148.483 1.00 33.82  ? 118  MET B CB  1 
ATOM   4723  C  CG  . MET B 1 160 ? 107.979 107.300 148.768 1.00 39.17  ? 118  MET B CG  1 
ATOM   4724  S  SD  . MET B 1 160 ? 107.164 107.896 150.259 1.00 48.04  ? 118  MET B SD  1 
ATOM   4725  C  CE  . MET B 1 160 ? 108.540 107.917 151.403 1.00 41.68  ? 118  MET B CE  1 
ATOM   4726  N  N   . LEU B 1 161 ? 110.394 105.372 146.693 1.00 38.73  ? 119  LEU B N   1 
ATOM   4727  C  CA  . LEU B 1 161 ? 111.223 104.182 146.790 1.00 38.93  ? 119  LEU B CA  1 
ATOM   4728  C  C   . LEU B 1 161 ? 112.454 104.312 145.894 1.00 35.77  ? 119  LEU B C   1 
ATOM   4729  O  O   . LEU B 1 161 ? 112.419 105.004 144.873 1.00 37.36  ? 119  LEU B O   1 
ATOM   4730  C  CB  . LEU B 1 161 ? 110.427 102.942 146.396 1.00 35.69  ? 119  LEU B CB  1 
ATOM   4731  C  CG  . LEU B 1 161 ? 109.218 102.594 147.264 1.00 35.12  ? 119  LEU B CG  1 
ATOM   4732  C  CD1 . LEU B 1 161 ? 108.673 101.225 146.896 1.00 40.67  ? 119  LEU B CD1 1 
ATOM   4733  C  CD2 . LEU B 1 161 ? 109.575 102.653 148.733 1.00 33.87  ? 119  LEU B CD2 1 
ATOM   4734  N  N   . PRO B 1 162 ? 113.559 103.660 146.257 1.00 31.60  ? 120  PRO B N   1 
ATOM   4735  C  CA  . PRO B 1 162 ? 114.739 103.676 145.387 1.00 29.91  ? 120  PRO B CA  1 
ATOM   4736  C  C   . PRO B 1 162 ? 114.442 103.010 144.053 1.00 41.42  ? 120  PRO B C   1 
ATOM   4737  O  O   . PRO B 1 162 ? 113.585 102.131 143.950 1.00 58.34  ? 120  PRO B O   1 
ATOM   4738  C  CB  . PRO B 1 162 ? 115.786 102.892 146.187 1.00 33.87  ? 120  PRO B CB  1 
ATOM   4739  C  CG  . PRO B 1 162 ? 115.300 102.923 147.596 1.00 33.02  ? 120  PRO B CG  1 
ATOM   4740  C  CD  . PRO B 1 162 ? 113.809 102.926 147.507 1.00 39.78  ? 120  PRO B CD  1 
ATOM   4741  N  N   . VAL B 1 163 ? 115.160 103.452 143.019 1.00 27.98  ? 121  VAL B N   1 
ATOM   4742  C  CA  . VAL B 1 163 ? 114.885 102.978 141.667 1.00 30.86  ? 121  VAL B CA  1 
ATOM   4743  C  C   . VAL B 1 163 ? 115.170 101.485 141.543 1.00 42.85  ? 121  VAL B C   1 
ATOM   4744  O  O   . VAL B 1 163 ? 114.387 100.740 140.941 1.00 45.78  ? 121  VAL B O   1 
ATOM   4745  C  CB  . VAL B 1 163 ? 115.684 103.803 140.644 1.00 34.01  ? 121  VAL B CB  1 
ATOM   4746  C  CG1 . VAL B 1 163 ? 115.847 103.036 139.343 1.00 38.59  ? 121  VAL B CG1 1 
ATOM   4747  C  CG2 . VAL B 1 163 ? 114.987 105.127 140.392 1.00 37.79  ? 121  VAL B CG2 1 
ATOM   4748  N  N   . TRP B 1 164 ? 116.290 101.021 142.103 1.00 43.88  ? 122  TRP B N   1 
ATOM   4749  C  CA  . TRP B 1 164 ? 116.621 99.604  142.004 1.00 42.29  ? 122  TRP B CA  1 
ATOM   4750  C  C   . TRP B 1 164 ? 115.656 98.727  142.790 1.00 41.16  ? 122  TRP B C   1 
ATOM   4751  O  O   . TRP B 1 164 ? 115.523 97.541  142.474 1.00 52.12  ? 122  TRP B O   1 
ATOM   4752  C  CB  . TRP B 1 164 ? 118.060 99.359  142.468 1.00 39.47  ? 122  TRP B CB  1 
ATOM   4753  C  CG  . TRP B 1 164 ? 118.401 99.970  143.790 1.00 39.89  ? 122  TRP B CG  1 
ATOM   4754  C  CD1 . TRP B 1 164 ? 119.111 101.112 144.000 1.00 44.92  ? 122  TRP B CD1 1 
ATOM   4755  C  CD2 . TRP B 1 164 ? 118.081 99.454  145.088 1.00 39.10  ? 122  TRP B CD2 1 
ATOM   4756  N  NE1 . TRP B 1 164 ? 119.236 101.354 145.345 1.00 44.62  ? 122  TRP B NE1 1 
ATOM   4757  C  CE2 . TRP B 1 164 ? 118.613 100.348 146.035 1.00 41.47  ? 122  TRP B CE2 1 
ATOM   4758  C  CE3 . TRP B 1 164 ? 117.391 98.326  145.542 1.00 43.02  ? 122  TRP B CE3 1 
ATOM   4759  C  CZ2 . TRP B 1 164 ? 118.475 100.152 147.405 1.00 44.18  ? 122  TRP B CZ2 1 
ATOM   4760  C  CZ3 . TRP B 1 164 ? 117.253 98.136  146.900 1.00 39.24  ? 122  TRP B CZ3 1 
ATOM   4761  C  CH2 . TRP B 1 164 ? 117.793 99.042  147.816 1.00 37.48  ? 122  TRP B CH2 1 
ATOM   4762  N  N   . PHE B 1 165 ? 114.986 99.276  143.803 1.00 39.51  ? 123  PHE B N   1 
ATOM   4763  C  CA  . PHE B 1 165 ? 113.983 98.507  144.531 1.00 38.42  ? 123  PHE B CA  1 
ATOM   4764  C  C   . PHE B 1 165 ? 112.688 98.393  143.740 1.00 42.56  ? 123  PHE B C   1 
ATOM   4765  O  O   . PHE B 1 165 ? 112.032 97.347  143.765 1.00 52.17  ? 123  PHE B O   1 
ATOM   4766  C  CB  . PHE B 1 165 ? 113.722 99.143  145.897 1.00 43.13  ? 123  PHE B CB  1 
ATOM   4767  C  CG  . PHE B 1 165 ? 112.735 98.389  146.743 1.00 41.83  ? 123  PHE B CG  1 
ATOM   4768  C  CD1 . PHE B 1 165 ? 113.158 97.377  147.585 1.00 46.60  ? 123  PHE B CD1 1 
ATOM   4769  C  CD2 . PHE B 1 165 ? 111.388 98.702  146.708 1.00 42.07  ? 123  PHE B CD2 1 
ATOM   4770  C  CE1 . PHE B 1 165 ? 112.255 96.684  148.367 1.00 46.64  ? 123  PHE B CE1 1 
ATOM   4771  C  CE2 . PHE B 1 165 ? 110.481 98.012  147.486 1.00 46.64  ? 123  PHE B CE2 1 
ATOM   4772  C  CZ  . PHE B 1 165 ? 110.915 97.003  148.317 1.00 45.54  ? 123  PHE B CZ  1 
ATOM   4773  N  N   . THR B 1 166 ? 112.301 99.460  143.038 1.00 41.51  ? 124  THR B N   1 
ATOM   4774  C  CA  . THR B 1 166 ? 111.069 99.421  142.259 1.00 45.04  ? 124  THR B CA  1 
ATOM   4775  C  C   . THR B 1 166 ? 111.240 98.589  140.994 1.00 50.46  ? 124  THR B C   1 
ATOM   4776  O  O   . THR B 1 166 ? 110.346 97.816  140.628 1.00 53.08  ? 124  THR B O   1 
ATOM   4777  C  CB  . THR B 1 166 ? 110.623 100.840 141.911 1.00 41.30  ? 124  THR B CB  1 
ATOM   4778  O  OG1 . THR B 1 166 ? 110.320 101.554 143.115 1.00 45.62  ? 124  THR B OG1 1 
ATOM   4779  C  CG2 . THR B 1 166 ? 109.388 100.811 141.027 1.00 44.28  ? 124  THR B CG2 1 
ATOM   4780  N  N   . ASP B 1 167 ? 112.380 98.732  140.314 1.00 52.20  ? 125  ASP B N   1 
ATOM   4781  C  CA  . ASP B 1 167 ? 112.601 97.993  139.075 1.00 52.23  ? 125  ASP B CA  1 
ATOM   4782  C  C   . ASP B 1 167 ? 112.637 96.491  139.327 1.00 54.18  ? 125  ASP B C   1 
ATOM   4783  O  O   . ASP B 1 167 ? 111.916 95.722  138.682 1.00 57.89  ? 125  ASP B O   1 
ATOM   4784  C  CB  . ASP B 1 167 ? 113.898 98.458  138.414 1.00 48.20  ? 125  ASP B CB  1 
ATOM   4785  C  CG  . ASP B 1 167 ? 113.722 99.735  137.620 1.00 53.32  ? 125  ASP B CG  1 
ATOM   4786  O  OD1 . ASP B 1 167 ? 112.597 100.278 137.605 1.00 53.91  ? 125  ASP B OD1 1 
ATOM   4787  O  OD2 . ASP B 1 167 ? 114.709 100.198 137.011 1.00 54.57  ? 125  ASP B OD2 1 
ATOM   4788  N  N   . ASN B 1 168 ? 113.471 96.056  140.264 1.00 54.90  ? 126  ASN B N   1 
ATOM   4789  C  CA  . ASN B 1 168 ? 113.596 94.641  140.616 1.00 53.89  ? 126  ASN B CA  1 
ATOM   4790  C  C   . ASN B 1 168 ? 112.722 94.286  141.812 1.00 57.92  ? 126  ASN B C   1 
ATOM   4791  O  O   . ASN B 1 168 ? 113.200 93.763  142.818 1.00 58.04  ? 126  ASN B O   1 
ATOM   4792  C  CB  . ASN B 1 168 ? 115.055 94.297  140.883 1.00 53.50  ? 126  ASN B CB  1 
ATOM   4793  C  CG  . ASN B 1 168 ? 115.991 94.920  139.869 1.00 59.75  ? 126  ASN B CG  1 
ATOM   4794  O  OD1 . ASN B 1 168 ? 117.039 95.457  140.222 1.00 62.85  ? 126  ASN B OD1 1 
ATOM   4795  N  ND2 . ASN B 1 168 ? 115.615 94.852  138.597 1.00 60.65  ? 126  ASN B ND2 1 
ATOM   4796  N  N   . LEU B 1 169 ? 111.423 94.577  141.714 1.00 61.68  ? 127  LEU B N   1 
ATOM   4797  C  CA  . LEU B 1 169 ? 110.517 94.284  142.820 1.00 62.50  ? 127  LEU B CA  1 
ATOM   4798  C  C   . LEU B 1 169 ? 110.384 92.783  143.049 1.00 65.28  ? 127  LEU B C   1 
ATOM   4799  O  O   . LEU B 1 169 ? 110.324 92.329  144.197 1.00 68.20  ? 127  LEU B O   1 
ATOM   4800  C  CB  . LEU B 1 169 ? 109.149 94.910  142.559 1.00 63.38  ? 127  LEU B CB  1 
ATOM   4801  C  CG  . LEU B 1 169 ? 108.194 94.938  143.753 1.00 62.64  ? 127  LEU B CG  1 
ATOM   4802  C  CD1 . LEU B 1 169 ? 108.837 95.651  144.928 1.00 61.52  ? 127  LEU B CD1 1 
ATOM   4803  C  CD2 . LEU B 1 169 ? 106.882 95.603  143.375 1.00 63.59  ? 127  LEU B CD2 1 
ATOM   4804  N  N   . GLU B 1 170 ? 110.331 91.998  141.969 1.00 71.80  ? 128  GLU B N   1 
ATOM   4805  C  CA  . GLU B 1 170 ? 110.210 90.551  142.114 1.00 72.08  ? 128  GLU B CA  1 
ATOM   4806  C  C   . GLU B 1 170 ? 111.429 89.961  142.813 1.00 71.13  ? 128  GLU B C   1 
ATOM   4807  O  O   . GLU B 1 170 ? 111.295 89.092  143.683 1.00 70.47  ? 128  GLU B O   1 
ATOM   4808  C  CB  . GLU B 1 170 ? 110.009 89.900  140.746 1.00 73.37  ? 128  GLU B CB  1 
ATOM   4809  C  CG  . GLU B 1 170 ? 108.935 90.557  139.898 1.00 75.72  ? 128  GLU B CG  1 
ATOM   4810  C  CD  . GLU B 1 170 ? 109.513 91.383  138.767 1.00 78.80  ? 128  GLU B CD  1 
ATOM   4811  O  OE1 . GLU B 1 170 ? 110.748 91.559  138.730 1.00 79.06  ? 128  GLU B OE1 1 
ATOM   4812  O  OE2 . GLU B 1 170 ? 108.732 91.858  137.916 1.00 77.63  ? 128  GLU B OE2 1 
ATOM   4813  N  N   . ALA B 1 171 ? 112.627 90.417  142.443 1.00 69.52  ? 129  ALA B N   1 
ATOM   4814  C  CA  . ALA B 1 171 ? 113.836 89.930  143.099 1.00 68.17  ? 129  ALA B CA  1 
ATOM   4815  C  C   . ALA B 1 171 ? 113.917 90.415  144.541 1.00 70.20  ? 129  ALA B C   1 
ATOM   4816  O  O   . ALA B 1 171 ? 114.372 89.679  145.424 1.00 68.91  ? 129  ALA B O   1 
ATOM   4817  C  CB  . ALA B 1 171 ? 115.072 90.366  142.314 1.00 69.34  ? 129  ALA B CB  1 
ATOM   4818  N  N   . ALA B 1 172 ? 113.486 91.653  144.798 1.00 71.86  ? 130  ALA B N   1 
ATOM   4819  C  CA  . ALA B 1 172 ? 113.526 92.183  146.156 1.00 66.38  ? 130  ALA B CA  1 
ATOM   4820  C  C   . ALA B 1 172 ? 112.526 91.482  147.065 1.00 67.55  ? 130  ALA B C   1 
ATOM   4821  O  O   . ALA B 1 172 ? 112.740 91.413  148.280 1.00 69.33  ? 130  ALA B O   1 
ATOM   4822  C  CB  . ALA B 1 172 ? 113.266 93.688  146.143 1.00 61.58  ? 130  ALA B CB  1 
ATOM   4823  N  N   . ALA B 1 173 ? 111.432 90.963  146.504 1.00 71.05  ? 131  ALA B N   1 
ATOM   4824  C  CA  . ALA B 1 173 ? 110.444 90.246  147.299 1.00 70.92  ? 131  ALA B CA  1 
ATOM   4825  C  C   . ALA B 1 173 ? 110.962 88.915  147.826 1.00 71.37  ? 131  ALA B C   1 
ATOM   4826  O  O   . ALA B 1 173 ? 110.339 88.343  148.726 1.00 74.36  ? 131  ALA B O   1 
ATOM   4827  C  CB  . ALA B 1 173 ? 109.175 90.014  146.477 1.00 70.89  ? 131  ALA B CB  1 
ATOM   4828  N  N   . THR B 1 174 ? 112.073 88.409  147.285 1.00 75.93  ? 132  THR B N   1 
ATOM   4829  C  CA  . THR B 1 174 ? 112.648 87.167  147.791 1.00 76.55  ? 132  THR B CA  1 
ATOM   4830  C  C   . THR B 1 174 ? 113.099 87.319  149.238 1.00 77.19  ? 132  THR B C   1 
ATOM   4831  O  O   . THR B 1 174 ? 112.866 86.430  150.067 1.00 77.55  ? 132  THR B O   1 
ATOM   4832  C  CB  . THR B 1 174 ? 113.817 86.737  146.903 1.00 76.96  ? 132  THR B CB  1 
ATOM   4833  O  OG1 . THR B 1 174 ? 113.313 86.073  145.737 1.00 80.06  ? 132  THR B OG1 1 
ATOM   4834  C  CG2 . THR B 1 174 ? 114.754 85.799  147.650 1.00 73.37  ? 132  THR B CG2 1 
ATOM   4835  N  N   . TYR B 1 175 ? 113.736 88.446  149.565 1.00 73.15  ? 133  TYR B N   1 
ATOM   4836  C  CA  . TYR B 1 175 ? 114.243 88.649  150.918 1.00 70.23  ? 133  TYR B CA  1 
ATOM   4837  C  C   . TYR B 1 175 ? 113.109 88.731  151.933 1.00 71.54  ? 133  TYR B C   1 
ATOM   4838  O  O   . TYR B 1 175 ? 113.222 88.189  153.038 1.00 72.86  ? 133  TYR B O   1 
ATOM   4839  C  CB  . TYR B 1 175 ? 115.110 89.906  150.966 1.00 67.00  ? 133  TYR B CB  1 
ATOM   4840  C  CG  . TYR B 1 175 ? 116.293 89.850  150.029 1.00 67.19  ? 133  TYR B CG  1 
ATOM   4841  C  CD1 . TYR B 1 175 ? 117.505 89.317  150.443 1.00 67.90  ? 133  TYR B CD1 1 
ATOM   4842  C  CD2 . TYR B 1 175 ? 116.196 90.324  148.729 1.00 67.12  ? 133  TYR B CD2 1 
ATOM   4843  C  CE1 . TYR B 1 175 ? 118.588 89.261  149.589 1.00 67.07  ? 133  TYR B CE1 1 
ATOM   4844  C  CE2 . TYR B 1 175 ? 117.274 90.272  147.868 1.00 66.97  ? 133  TYR B CE2 1 
ATOM   4845  C  CZ  . TYR B 1 175 ? 118.467 89.740  148.303 1.00 65.37  ? 133  TYR B CZ  1 
ATOM   4846  O  OH  . TYR B 1 175 ? 119.544 89.686  147.450 1.00 66.13  ? 133  TYR B OH  1 
ATOM   4847  N  N   . VAL B 1 176 ? 112.015 89.404  151.585 1.00 78.37  ? 134  VAL B N   1 
ATOM   4848  C  CA  . VAL B 1 176 ? 110.843 89.482  152.460 1.00 78.95  ? 134  VAL B CA  1 
ATOM   4849  C  C   . VAL B 1 176 ? 109.928 88.308  152.104 1.00 80.65  ? 134  VAL B C   1 
ATOM   4850  O  O   . VAL B 1 176 ? 108.957 88.419  151.356 1.00 84.17  ? 134  VAL B O   1 
ATOM   4851  C  CB  . VAL B 1 176 ? 110.174 90.863  152.403 1.00 73.49  ? 134  VAL B CB  1 
ATOM   4852  C  CG1 . VAL B 1 176 ? 111.243 91.928  152.462 1.00 75.74  ? 134  VAL B CG1 1 
ATOM   4853  C  CG2 . VAL B 1 176 ? 109.421 91.117  151.103 1.00 73.75  ? 134  VAL B CG2 1 
ATOM   4854  N  N   . GLN B 1 177 ? 110.256 87.142  152.658 1.00 83.17  ? 135  GLN B N   1 
ATOM   4855  C  CA  . GLN B 1 177 ? 109.483 85.936  152.391 1.00 81.95  ? 135  GLN B CA  1 
ATOM   4856  C  C   . GLN B 1 177 ? 109.101 85.232  153.686 1.00 85.23  ? 135  GLN B C   1 
ATOM   4857  O  O   . GLN B 1 177 ? 108.098 84.513  153.737 1.00 86.90  ? 135  GLN B O   1 
ATOM   4858  C  CB  . GLN B 1 177 ? 110.269 84.986  151.486 1.00 83.33  ? 135  GLN B CB  1 
ATOM   4859  C  CG  . GLN B 1 177 ? 109.526 84.576  150.228 1.00 84.83  ? 135  GLN B CG  1 
ATOM   4860  C  CD  . GLN B 1 177 ? 110.195 83.423  149.509 1.00 87.31  ? 135  GLN B CD  1 
ATOM   4861  O  OE1 . GLN B 1 177 ? 111.383 83.163  149.698 1.00 87.15  ? 135  GLN B OE1 1 
ATOM   4862  N  NE2 . GLN B 1 177 ? 109.432 82.721  148.680 1.00 88.16  ? 135  GLN B NE2 1 
ATOM   4863  N  N   . ASN B 1 178 ? 109.896 85.430  154.735 1.00 82.66  ? 136  ASN B N   1 
ATOM   4864  C  CA  . ASN B 1 178 ? 109.650 84.828  156.043 1.00 83.42  ? 136  ASN B CA  1 
ATOM   4865  C  C   . ASN B 1 178 ? 109.150 85.858  157.047 1.00 81.91  ? 136  ASN B C   1 
ATOM   4866  O  O   . ASN B 1 178 ? 109.522 85.824  158.221 1.00 82.21  ? 136  ASN B O   1 
ATOM   4867  C  CB  . ASN B 1 178 ? 110.916 84.145  156.554 1.00 82.34  ? 136  ASN B CB  1 
ATOM   4868  C  CG  . ASN B 1 178 ? 110.633 83.127  157.644 1.00 86.79  ? 136  ASN B CG  1 
ATOM   4869  O  OD1 . ASN B 1 178 ? 109.481 82.905  158.017 1.00 88.10  ? 136  ASN B OD1 1 
ATOM   4870  N  ND2 . ASN B 1 178 ? 111.686 82.505  158.161 1.00 84.56  ? 136  ASN B ND2 1 
ATOM   4871  N  N   . GLN B 1 179 ? 108.308 86.789  156.603 1.00 74.47  ? 137  GLN B N   1 
ATOM   4872  C  CA  . GLN B 1 179 ? 107.877 87.888  157.459 1.00 72.81  ? 137  GLN B CA  1 
ATOM   4873  C  C   . GLN B 1 179 ? 107.150 87.374  158.694 1.00 72.26  ? 137  GLN B C   1 
ATOM   4874  O  O   . GLN B 1 179 ? 106.276 86.507  158.605 1.00 75.26  ? 137  GLN B O   1 
ATOM   4875  C  CB  . GLN B 1 179 ? 106.975 88.839  156.675 1.00 68.46  ? 137  GLN B CB  1 
ATOM   4876  C  CG  . GLN B 1 179 ? 107.355 88.989  155.215 1.00 71.18  ? 137  GLN B CG  1 
ATOM   4877  C  CD  . GLN B 1 179 ? 106.243 89.596  154.388 1.00 72.48  ? 137  GLN B CD  1 
ATOM   4878  O  OE1 . GLN B 1 179 ? 105.221 90.024  154.921 1.00 69.67  ? 137  GLN B OE1 1 
ATOM   4879  N  NE2 . GLN B 1 179 ? 106.437 89.637  153.075 1.00 74.93  ? 137  GLN B NE2 1 
ATOM   4880  N  N   . SER B 1 180 ? 107.519 87.916  159.852 1.00 70.16  ? 138  SER B N   1 
ATOM   4881  C  CA  . SER B 1 180 ? 106.874 87.577  161.111 1.00 72.58  ? 138  SER B CA  1 
ATOM   4882  C  C   . SER B 1 180 ? 106.876 88.810  162.000 1.00 70.55  ? 138  SER B C   1 
ATOM   4883  O  O   . SER B 1 180 ? 107.694 89.717  161.832 1.00 70.05  ? 138  SER B O   1 
ATOM   4884  C  CB  . SER B 1 180 ? 107.573 86.405  161.809 1.00 75.86  ? 138  SER B CB  1 
ATOM   4885  O  OG  . SER B 1 180 ? 106.739 85.835  162.803 1.00 76.27  ? 138  SER B OG  1 
ATOM   4886  N  N   . GLU B 1 181 ? 105.945 88.832  162.956 1.00 76.80  ? 139  GLU B N   1 
ATOM   4887  C  CA  . GLU B 1 181 ? 105.824 89.989  163.838 1.00 78.12  ? 139  GLU B CA  1 
ATOM   4888  C  C   . GLU B 1 181 ? 107.086 90.185  164.668 1.00 79.68  ? 139  GLU B C   1 
ATOM   4889  O  O   . GLU B 1 181 ? 107.539 91.319  164.865 1.00 77.89  ? 139  GLU B O   1 
ATOM   4890  C  CB  . GLU B 1 181 ? 104.602 89.840  164.741 1.00 78.68  ? 139  GLU B CB  1 
ATOM   4891  C  CG  . GLU B 1 181 ? 104.290 91.082  165.559 1.00 77.45  ? 139  GLU B CG  1 
ATOM   4892  C  CD  . GLU B 1 181 ? 102.814 91.220  165.874 1.00 81.39  ? 139  GLU B CD  1 
ATOM   4893  O  OE1 . GLU B 1 181 ? 102.095 90.200  165.827 1.00 82.35  ? 139  GLU B OE1 1 
ATOM   4894  O  OE2 . GLU B 1 181 ? 102.372 92.350  166.168 1.00 83.13  ? 139  GLU B OE2 1 
ATOM   4895  N  N   . ASP B 1 182 ? 107.668 89.095  165.161 1.00 74.67  ? 140  ASP B N   1 
ATOM   4896  C  CA  . ASP B 1 182 ? 108.929 89.162  165.891 1.00 68.59  ? 140  ASP B CA  1 
ATOM   4897  C  C   . ASP B 1 182 ? 110.052 89.281  164.868 1.00 68.38  ? 140  ASP B C   1 
ATOM   4898  O  O   . ASP B 1 182 ? 110.392 88.307  164.189 1.00 68.52  ? 140  ASP B O   1 
ATOM   4899  C  CB  . ASP B 1 182 ? 109.098 87.929  166.776 1.00 69.56  ? 140  ASP B CB  1 
ATOM   4900  C  CG  . ASP B 1 182 ? 110.554 87.586  167.044 1.00 72.14  ? 140  ASP B CG  1 
ATOM   4901  O  OD1 . ASP B 1 182 ? 111.358 88.509  167.297 1.00 69.49  ? 140  ASP B OD1 1 
ATOM   4902  O  OD2 . ASP B 1 182 ? 110.898 86.386  166.995 1.00 74.48  ? 140  ASP B OD2 1 
ATOM   4903  N  N   . CYS B 1 183 ? 110.621 90.481  164.744 1.00 62.34  ? 141  CYS B N   1 
ATOM   4904  C  CA  . CYS B 1 183 ? 111.671 90.717  163.763 1.00 61.98  ? 141  CYS B CA  1 
ATOM   4905  C  C   . CYS B 1 183 ? 112.803 91.578  164.306 1.00 59.12  ? 141  CYS B C   1 
ATOM   4906  O  O   . CYS B 1 183 ? 113.665 92.001  163.526 1.00 58.68  ? 141  CYS B O   1 
ATOM   4907  C  CB  . CYS B 1 183 ? 111.087 91.371  162.508 1.00 59.17  ? 141  CYS B CB  1 
ATOM   4908  S  SG  . CYS B 1 183 ? 109.959 92.738  162.852 1.00 64.10  ? 141  CYS B SG  1 
ATOM   4909  N  N   . LEU B 1 184 ? 112.835 91.848  165.610 1.00 53.57  ? 142  LEU B N   1 
ATOM   4910  C  CA  . LEU B 1 184 ? 113.846 92.724  166.199 1.00 52.02  ? 142  LEU B CA  1 
ATOM   4911  C  C   . LEU B 1 184 ? 115.162 91.958  166.304 1.00 54.47  ? 142  LEU B C   1 
ATOM   4912  O  O   . LEU B 1 184 ? 115.515 91.385  167.338 1.00 59.03  ? 142  LEU B O   1 
ATOM   4913  C  CB  . LEU B 1 184 ? 113.381 93.245  167.552 1.00 52.06  ? 142  LEU B CB  1 
ATOM   4914  C  CG  . LEU B 1 184 ? 112.010 93.925  167.551 1.00 53.11  ? 142  LEU B CG  1 
ATOM   4915  C  CD1 . LEU B 1 184 ? 111.743 94.610  168.878 1.00 53.51  ? 142  LEU B CD1 1 
ATOM   4916  C  CD2 . LEU B 1 184 ? 111.908 94.919  166.408 1.00 49.39  ? 142  LEU B CD2 1 
ATOM   4917  N  N   . TYR B 1 185 ? 115.901 91.954  165.196 1.00 44.73  ? 143  TYR B N   1 
ATOM   4918  C  CA  . TYR B 1 185 ? 117.221 91.347  165.133 1.00 45.60  ? 143  TYR B CA  1 
ATOM   4919  C  C   . TYR B 1 185 ? 118.142 92.250  164.327 1.00 45.94  ? 143  TYR B C   1 
ATOM   4920  O  O   . TYR B 1 185 ? 117.695 93.042  163.495 1.00 54.24  ? 143  TYR B O   1 
ATOM   4921  C  CB  . TYR B 1 185 ? 117.181 89.950  164.500 1.00 49.58  ? 143  TYR B CB  1 
ATOM   4922  C  CG  . TYR B 1 185 ? 116.189 88.998  165.127 1.00 48.85  ? 143  TYR B CG  1 
ATOM   4923  C  CD1 . TYR B 1 185 ? 116.540 88.221  166.222 1.00 47.81  ? 143  TYR B CD1 1 
ATOM   4924  C  CD2 . TYR B 1 185 ? 114.906 88.865  164.616 1.00 48.88  ? 143  TYR B CD2 1 
ATOM   4925  C  CE1 . TYR B 1 185 ? 115.639 87.348  166.796 1.00 48.53  ? 143  TYR B CE1 1 
ATOM   4926  C  CE2 . TYR B 1 185 ? 113.999 87.993  165.184 1.00 47.95  ? 143  TYR B CE2 1 
ATOM   4927  C  CZ  . TYR B 1 185 ? 114.371 87.237  166.272 1.00 50.33  ? 143  TYR B CZ  1 
ATOM   4928  O  OH  . TYR B 1 185 ? 113.471 86.368  166.841 1.00 59.17  ? 143  TYR B OH  1 
ATOM   4929  N  N   . LEU B 1 186 ? 119.441 92.124  164.583 1.00 38.30  ? 144  LEU B N   1 
ATOM   4930  C  CA  . LEU B 1 186 ? 120.458 92.840  163.830 1.00 38.24  ? 144  LEU B CA  1 
ATOM   4931  C  C   . LEU B 1 186 ? 121.568 91.878  163.436 1.00 41.77  ? 144  LEU B C   1 
ATOM   4932  O  O   . LEU B 1 186 ? 121.799 90.868  164.104 1.00 47.90  ? 144  LEU B O   1 
ATOM   4933  C  CB  . LEU B 1 186 ? 121.037 94.022  164.627 1.00 40.74  ? 144  LEU B CB  1 
ATOM   4934  C  CG  . LEU B 1 186 ? 121.613 93.763  166.019 1.00 39.74  ? 144  LEU B CG  1 
ATOM   4935  C  CD1 . LEU B 1 186 ? 123.117 93.584  165.958 1.00 42.15  ? 144  LEU B CD1 1 
ATOM   4936  C  CD2 . LEU B 1 186 ? 121.260 94.903  166.955 1.00 38.16  ? 144  LEU B CD2 1 
ATOM   4937  N  N   . ASN B 1 187 ? 122.247 92.196  162.338 1.00 35.55  ? 145  ASN B N   1 
ATOM   4938  C  CA  . ASN B 1 187 ? 123.330 91.385  161.804 1.00 34.39  ? 145  ASN B CA  1 
ATOM   4939  C  C   . ASN B 1 187 ? 124.618 92.194  161.829 1.00 34.44  ? 145  ASN B C   1 
ATOM   4940  O  O   . ASN B 1 187 ? 124.642 93.346  161.379 1.00 46.37  ? 145  ASN B O   1 
ATOM   4941  C  CB  . ASN B 1 187 ? 123.022 90.925  160.378 1.00 39.91  ? 145  ASN B CB  1 
ATOM   4942  C  CG  . ASN B 1 187 ? 121.537 90.792  160.117 1.00 42.65  ? 145  ASN B CG  1 
ATOM   4943  O  OD1 . ASN B 1 187 ? 120.839 90.051  160.806 1.00 44.62  ? 145  ASN B OD1 1 
ATOM   4944  N  ND2 . ASN B 1 187 ? 121.047 91.508  159.114 1.00 40.47  ? 145  ASN B ND2 1 
ATOM   4945  N  N   . LEU B 1 188 ? 125.680 91.587  162.351 1.00 37.43  ? 146  LEU B N   1 
ATOM   4946  C  CA  . LEU B 1 188 ? 126.985 92.221  162.468 1.00 40.55  ? 146  LEU B CA  1 
ATOM   4947  C  C   . LEU B 1 188 ? 127.955 91.573  161.492 1.00 44.49  ? 146  LEU B C   1 
ATOM   4948  O  O   . LEU B 1 188 ? 128.010 90.343  161.390 1.00 53.66  ? 146  LEU B O   1 
ATOM   4949  C  CB  . LEU B 1 188 ? 127.531 92.100  163.892 1.00 37.10  ? 146  LEU B CB  1 
ATOM   4950  C  CG  . LEU B 1 188 ? 126.733 92.745  165.022 1.00 36.29  ? 146  LEU B CG  1 
ATOM   4951  C  CD1 . LEU B 1 188 ? 126.260 91.688  165.997 1.00 38.12  ? 146  LEU B CD1 1 
ATOM   4952  C  CD2 . LEU B 1 188 ? 127.576 93.775  165.733 1.00 41.81  ? 146  LEU B CD2 1 
ATOM   4953  N  N   . TYR B 1 189 ? 128.717 92.399  160.781 1.00 39.29  ? 147  TYR B N   1 
ATOM   4954  C  CA  . TYR B 1 189 ? 129.785 91.942  159.904 1.00 39.21  ? 147  TYR B CA  1 
ATOM   4955  C  C   . TYR B 1 189 ? 131.086 92.548  160.405 1.00 45.44  ? 147  TYR B C   1 
ATOM   4956  O  O   . TYR B 1 189 ? 131.220 93.776  160.461 1.00 44.90  ? 147  TYR B O   1 
ATOM   4957  C  CB  . TYR B 1 189 ? 129.518 92.342  158.452 1.00 39.93  ? 147  TYR B CB  1 
ATOM   4958  C  CG  . TYR B 1 189 ? 128.139 91.966  157.958 1.00 42.61  ? 147  TYR B CG  1 
ATOM   4959  C  CD1 . TYR B 1 189 ? 127.059 92.818  158.139 1.00 43.29  ? 147  TYR B CD1 1 
ATOM   4960  C  CD2 . TYR B 1 189 ? 127.917 90.758  157.312 1.00 46.73  ? 147  TYR B CD2 1 
ATOM   4961  C  CE1 . TYR B 1 189 ? 125.800 92.479  157.691 1.00 42.24  ? 147  TYR B CE1 1 
ATOM   4962  C  CE2 . TYR B 1 189 ? 126.659 90.411  156.861 1.00 47.57  ? 147  TYR B CE2 1 
ATOM   4963  C  CZ  . TYR B 1 189 ? 125.605 91.276  157.052 1.00 42.51  ? 147  TYR B CZ  1 
ATOM   4964  O  OH  . TYR B 1 189 ? 124.350 90.936  156.605 1.00 45.38  ? 147  TYR B OH  1 
ATOM   4965  N  N   . VAL B 1 190 ? 132.033 91.689  160.769 1.00 53.71  ? 148  VAL B N   1 
ATOM   4966  C  CA  . VAL B 1 190 ? 133.275 92.089  161.417 1.00 50.32  ? 148  VAL B CA  1 
ATOM   4967  C  C   . VAL B 1 190 ? 134.428 91.661  160.522 1.00 52.37  ? 148  VAL B C   1 
ATOM   4968  O  O   . VAL B 1 190 ? 134.435 90.526  160.043 1.00 56.51  ? 148  VAL B O   1 
ATOM   4969  C  CB  . VAL B 1 190 ? 133.431 91.467  162.817 1.00 44.72  ? 148  VAL B CB  1 
ATOM   4970  C  CG1 . VAL B 1 190 ? 134.534 92.161  163.591 1.00 49.01  ? 148  VAL B CG1 1 
ATOM   4971  C  CG2 . VAL B 1 190 ? 132.117 91.532  163.578 1.00 42.10  ? 148  VAL B CG2 1 
ATOM   4972  N  N   . PRO B 1 191 ? 135.408 92.518  160.264 1.00 51.27  ? 149  PRO B N   1 
ATOM   4973  C  CA  . PRO B 1 191 ? 136.592 92.091  159.517 1.00 54.15  ? 149  PRO B CA  1 
ATOM   4974  C  C   . PRO B 1 191 ? 137.570 91.352  160.422 1.00 60.20  ? 149  PRO B C   1 
ATOM   4975  O  O   . PRO B 1 191 ? 137.414 91.292  161.641 1.00 59.89  ? 149  PRO B O   1 
ATOM   4976  C  CB  . PRO B 1 191 ? 137.182 93.409  159.020 1.00 49.88  ? 149  PRO B CB  1 
ATOM   4977  C  CG  . PRO B 1 191 ? 136.799 94.385  160.071 1.00 51.05  ? 149  PRO B CG  1 
ATOM   4978  C  CD  . PRO B 1 191 ? 135.457 93.950  160.601 1.00 50.90  ? 149  PRO B CD  1 
ATOM   4979  N  N   . THR B 1 192 ? 138.593 90.785  159.794 1.00 72.03  ? 150  THR B N   1 
ATOM   4980  C  CA  . THR B 1 192 ? 139.609 90.039  160.526 1.00 71.56  ? 150  THR B CA  1 
ATOM   4981  C  C   . THR B 1 192 ? 141.012 90.482  160.128 1.00 71.30  ? 150  THR B C   1 
ATOM   4982  O  O   . THR B 1 192 ? 141.637 91.290  160.816 1.00 70.48  ? 150  THR B O   1 
ATOM   4983  C  CB  . THR B 1 192 ? 139.471 88.525  160.293 1.00 69.68  ? 150  THR B CB  1 
ATOM   4984  O  OG1 . THR B 1 192 ? 139.189 88.276  158.911 1.00 69.97  ? 150  THR B OG1 1 
ATOM   4985  C  CG2 . THR B 1 192 ? 138.345 87.959  161.142 1.00 67.36  ? 150  THR B CG2 1 
ATOM   4986  N  N   . SER B 1 199 ? 143.266 101.807 162.682 1.00 103.27 ? 174  SER B N   1 
ATOM   4987  C  CA  . SER B 1 199 ? 144.579 101.484 163.226 1.00 105.41 ? 174  SER B CA  1 
ATOM   4988  C  C   . SER B 1 199 ? 144.466 100.968 164.658 1.00 106.43 ? 174  SER B C   1 
ATOM   4989  O  O   . SER B 1 199 ? 145.372 100.304 165.162 1.00 104.19 ? 174  SER B O   1 
ATOM   4990  C  CB  . SER B 1 199 ? 145.496 102.708 163.176 1.00 104.52 ? 174  SER B CB  1 
ATOM   4991  O  OG  . SER B 1 199 ? 145.413 103.354 161.917 1.00 103.18 ? 174  SER B OG  1 
ATOM   4992  N  N   . GLY B 1 200 ? 143.348 101.279 165.308 1.00 103.94 ? 175  GLY B N   1 
ATOM   4993  C  CA  . GLY B 1 200 ? 143.104 100.821 166.661 1.00 101.07 ? 175  GLY B CA  1 
ATOM   4994  C  C   . GLY B 1 200 ? 141.881 99.933  166.764 1.00 100.57 ? 175  GLY B C   1 
ATOM   4995  O  O   . GLY B 1 200 ? 141.702 99.021  165.952 1.00 101.33 ? 175  GLY B O   1 
ATOM   4996  N  N   . LYS B 1 201 ? 141.033 100.187 167.758 1.00 84.47  ? 176  LYS B N   1 
ATOM   4997  C  CA  . LYS B 1 201 ? 139.804 99.422  167.917 1.00 83.11  ? 176  LYS B CA  1 
ATOM   4998  C  C   . LYS B 1 201 ? 138.830 99.781  166.803 1.00 81.29  ? 176  LYS B C   1 
ATOM   4999  O  O   . LYS B 1 201 ? 138.653 100.959 166.477 1.00 83.85  ? 176  LYS B O   1 
ATOM   5000  C  CB  . LYS B 1 201 ? 139.183 99.686  169.288 1.00 79.19  ? 176  LYS B CB  1 
ATOM   5001  C  CG  . LYS B 1 201 ? 138.577 98.450  169.932 1.00 78.64  ? 176  LYS B CG  1 
ATOM   5002  C  CD  . LYS B 1 201 ? 138.579 98.554  171.448 1.00 79.84  ? 176  LYS B CD  1 
ATOM   5003  C  CE  . LYS B 1 201 ? 137.765 99.742  171.928 1.00 81.14  ? 176  LYS B CE  1 
ATOM   5004  N  NZ  . LYS B 1 201 ? 136.942 99.401  173.122 1.00 83.12  ? 176  LYS B NZ  1 
ATOM   5005  N  N   . LYS B 1 202 ? 138.203 98.764  166.220 1.00 60.33  ? 177  LYS B N   1 
ATOM   5006  C  CA  . LYS B 1 202 ? 137.404 98.965  165.021 1.00 59.42  ? 177  LYS B CA  1 
ATOM   5007  C  C   . LYS B 1 202 ? 136.161 99.797  165.330 1.00 61.35  ? 177  LYS B C   1 
ATOM   5008  O  O   . LYS B 1 202 ? 135.505 99.583  166.354 1.00 59.66  ? 177  LYS B O   1 
ATOM   5009  C  CB  . LYS B 1 202 ? 136.997 97.620  164.425 1.00 58.30  ? 177  LYS B CB  1 
ATOM   5010  C  CG  . LYS B 1 202 ? 138.171 96.703  164.135 1.00 62.22  ? 177  LYS B CG  1 
ATOM   5011  C  CD  . LYS B 1 202 ? 137.822 95.252  164.409 1.00 62.20  ? 177  LYS B CD  1 
ATOM   5012  C  CE  . LYS B 1 202 ? 138.352 94.345  163.316 1.00 61.39  ? 177  LYS B CE  1 
ATOM   5013  N  NZ  . LYS B 1 202 ? 139.806 94.556  163.087 1.00 64.97  ? 177  LYS B NZ  1 
ATOM   5014  N  N   . PRO B 1 203 ? 135.816 100.757 164.468 1.00 50.99  ? 178  PRO B N   1 
ATOM   5015  C  CA  . PRO B 1 203 ? 134.583 101.530 164.668 1.00 48.36  ? 178  PRO B CA  1 
ATOM   5016  C  C   . PRO B 1 203 ? 133.336 100.736 164.318 1.00 52.08  ? 178  PRO B C   1 
ATOM   5017  O  O   . PRO B 1 203 ? 133.426 99.574  163.909 1.00 62.01  ? 178  PRO B O   1 
ATOM   5018  C  CB  . PRO B 1 203 ? 134.764 102.728 163.724 1.00 44.56  ? 178  PRO B CB  1 
ATOM   5019  C  CG  . PRO B 1 203 ? 136.232 102.763 163.415 1.00 47.86  ? 178  PRO B CG  1 
ATOM   5020  C  CD  . PRO B 1 203 ? 136.653 101.333 163.406 1.00 47.44  ? 178  PRO B CD  1 
ATOM   5021  N  N   . VAL B 1 204 ? 132.168 101.353 164.473 1.00 37.15  ? 179  VAL B N   1 
ATOM   5022  C  CA  . VAL B 1 204 ? 130.889 100.716 164.188 1.00 35.87  ? 179  VAL B CA  1 
ATOM   5023  C  C   . VAL B 1 204 ? 130.105 101.609 163.239 1.00 38.27  ? 179  VAL B C   1 
ATOM   5024  O  O   . VAL B 1 204 ? 130.080 102.833 163.405 1.00 50.19  ? 179  VAL B O   1 
ATOM   5025  C  CB  . VAL B 1 204 ? 130.083 100.454 165.479 1.00 39.47  ? 179  VAL B CB  1 
ATOM   5026  C  CG1 . VAL B 1 204 ? 128.760 99.780  165.159 1.00 42.59  ? 179  VAL B CG1 1 
ATOM   5027  C  CG2 . VAL B 1 204 ? 130.893 99.612  166.448 1.00 43.02  ? 179  VAL B CG2 1 
ATOM   5028  N  N   . MET B 1 205 ? 129.477 100.999 162.235 1.00 39.11  ? 180  MET B N   1 
ATOM   5029  C  CA  . MET B 1 205 ? 128.637 101.708 161.271 1.00 41.39  ? 180  MET B CA  1 
ATOM   5030  C  C   . MET B 1 205 ? 127.278 101.017 161.220 1.00 42.23  ? 180  MET B C   1 
ATOM   5031  O  O   . MET B 1 205 ? 127.146 99.937  160.637 1.00 57.25  ? 180  MET B O   1 
ATOM   5032  C  CB  . MET B 1 205 ? 129.286 101.744 159.891 1.00 41.44  ? 180  MET B CB  1 
ATOM   5033  C  CG  . MET B 1 205 ? 130.673 102.351 159.866 1.00 44.22  ? 180  MET B CG  1 
ATOM   5034  S  SD  . MET B 1 205 ? 131.180 102.814 158.201 1.00 47.87  ? 180  MET B SD  1 
ATOM   5035  C  CE  . MET B 1 205 ? 129.744 103.729 157.658 1.00 44.85  ? 180  MET B CE  1 
ATOM   5036  N  N   . LEU B 1 206 ? 126.277 101.625 161.850 1.00 42.39  ? 181  LEU B N   1 
ATOM   5037  C  CA  . LEU B 1 206 ? 124.912 101.130 161.773 1.00 43.99  ? 181  LEU B CA  1 
ATOM   5038  C  C   . LEU B 1 206 ? 124.242 101.662 160.515 1.00 47.08  ? 181  LEU B C   1 
ATOM   5039  O  O   . LEU B 1 206 ? 124.447 102.815 160.128 1.00 61.35  ? 181  LEU B O   1 
ATOM   5040  C  CB  . LEU B 1 206 ? 124.123 101.553 163.012 1.00 44.26  ? 181  LEU B CB  1 
ATOM   5041  C  CG  . LEU B 1 206 ? 122.712 100.989 163.179 1.00 44.60  ? 181  LEU B CG  1 
ATOM   5042  C  CD1 . LEU B 1 206 ? 122.760 99.506  163.485 1.00 53.77  ? 181  LEU B CD1 1 
ATOM   5043  C  CD2 . LEU B 1 206 ? 121.970 101.732 164.274 1.00 48.63  ? 181  LEU B CD2 1 
ATOM   5044  N  N   . PHE B 1 207 ? 123.454 100.812 159.865 1.00 48.19  ? 182  PHE B N   1 
ATOM   5045  C  CA  . PHE B 1 207 ? 122.750 101.177 158.642 1.00 50.43  ? 182  PHE B CA  1 
ATOM   5046  C  C   . PHE B 1 207 ? 121.255 101.217 158.919 1.00 52.84  ? 182  PHE B C   1 
ATOM   5047  O  O   . PHE B 1 207 ? 120.681 100.229 159.386 1.00 60.41  ? 182  PHE B O   1 
ATOM   5048  C  CB  . PHE B 1 207 ? 123.059 100.198 157.511 1.00 49.92  ? 182  PHE B CB  1 
ATOM   5049  C  CG  . PHE B 1 207 ? 122.427 100.572 156.201 1.00 47.69  ? 182  PHE B CG  1 
ATOM   5050  C  CD1 . PHE B 1 207 ? 122.887 101.656 155.480 1.00 48.26  ? 182  PHE B CD1 1 
ATOM   5051  C  CD2 . PHE B 1 207 ? 121.370 99.841  155.693 1.00 55.05  ? 182  PHE B CD2 1 
ATOM   5052  C  CE1 . PHE B 1 207 ? 122.309 102.005 154.278 1.00 44.98  ? 182  PHE B CE1 1 
ATOM   5053  C  CE2 . PHE B 1 207 ? 120.789 100.187 154.492 1.00 52.49  ? 182  PHE B CE2 1 
ATOM   5054  C  CZ  . PHE B 1 207 ? 121.259 101.269 153.785 1.00 44.60  ? 182  PHE B CZ  1 
ATOM   5055  N  N   . LEU B 1 208 ? 120.627 102.353 158.620 1.00 44.75  ? 183  LEU B N   1 
ATOM   5056  C  CA  . LEU B 1 208 ? 119.191 102.546 158.822 1.00 42.53  ? 183  LEU B CA  1 
ATOM   5057  C  C   . LEU B 1 208 ? 118.516 102.470 157.456 1.00 50.60  ? 183  LEU B C   1 
ATOM   5058  O  O   . LEU B 1 208 ? 118.398 103.466 156.743 1.00 54.80  ? 183  LEU B O   1 
ATOM   5059  C  CB  . LEU B 1 208 ? 118.917 103.872 159.520 1.00 44.76  ? 183  LEU B CB  1 
ATOM   5060  C  CG  . LEU B 1 208 ? 118.804 103.828 161.043 1.00 41.63  ? 183  LEU B CG  1 
ATOM   5061  C  CD1 . LEU B 1 208 ? 120.167 103.651 161.676 1.00 49.56  ? 183  LEU B CD1 1 
ATOM   5062  C  CD2 . LEU B 1 208 ? 118.146 105.090 161.558 1.00 49.11  ? 183  LEU B CD2 1 
ATOM   5063  N  N   . HIS B 1 209 ? 118.061 101.272 157.099 1.00 46.79  ? 184  HIS B N   1 
ATOM   5064  C  CA  . HIS B 1 209 ? 117.505 101.023 155.778 1.00 44.17  ? 184  HIS B CA  1 
ATOM   5065  C  C   . HIS B 1 209 ? 116.117 101.647 155.649 1.00 44.67  ? 184  HIS B C   1 
ATOM   5066  O  O   . HIS B 1 209 ? 115.602 102.297 156.562 1.00 56.29  ? 184  HIS B O   1 
ATOM   5067  C  CB  . HIS B 1 209 ? 117.436 99.523  155.510 1.00 42.00  ? 184  HIS B CB  1 
ATOM   5068  C  CG  . HIS B 1 209 ? 116.517 98.790  156.436 1.00 42.58  ? 184  HIS B CG  1 
ATOM   5069  N  ND1 . HIS B 1 209 ? 115.175 98.620  156.171 1.00 41.23  ? 184  HIS B ND1 1 
ATOM   5070  C  CD2 . HIS B 1 209 ? 116.743 98.192  157.629 1.00 48.23  ? 184  HIS B CD2 1 
ATOM   5071  C  CE1 . HIS B 1 209 ? 114.616 97.944  157.158 1.00 47.12  ? 184  HIS B CE1 1 
ATOM   5072  N  NE2 . HIS B 1 209 ? 115.545 97.673  158.056 1.00 46.49  ? 184  HIS B NE2 1 
ATOM   5073  N  N   . GLY B 1 210 ? 115.504 101.437 154.486 1.00 36.17  ? 185  GLY B N   1 
ATOM   5074  C  CA  . GLY B 1 210 ? 114.133 101.847 154.261 1.00 33.29  ? 185  GLY B CA  1 
ATOM   5075  C  C   . GLY B 1 210 ? 113.965 102.975 153.265 1.00 39.24  ? 185  GLY B C   1 
ATOM   5076  O  O   . GLY B 1 210 ? 114.164 104.145 153.604 1.00 40.00  ? 185  GLY B O   1 
ATOM   5077  N  N   . GLY B 1 211 ? 113.599 102.634 152.028 1.00 36.27  ? 186  GLY B N   1 
ATOM   5078  C  CA  . GLY B 1 211 ? 113.246 103.665 151.066 1.00 36.55  ? 186  GLY B CA  1 
ATOM   5079  C  C   . GLY B 1 211 ? 112.015 104.441 151.490 1.00 37.16  ? 186  GLY B C   1 
ATOM   5080  O  O   . GLY B 1 211 ? 111.956 105.664 151.344 1.00 42.79  ? 186  GLY B O   1 
ATOM   5081  N  N   . SER B 1 212 ? 111.011 103.737 152.007 1.00 35.93  ? 187  SER B N   1 
ATOM   5082  C  CA  . SER B 1 212 ? 109.869 104.362 152.660 1.00 33.05  ? 187  SER B CA  1 
ATOM   5083  C  C   . SER B 1 212 ? 109.701 103.740 154.038 1.00 44.20  ? 187  SER B C   1 
ATOM   5084  O  O   . SER B 1 212 ? 110.579 103.004 154.499 1.00 53.87  ? 187  SER B O   1 
ATOM   5085  C  CB  . SER B 1 212 ? 108.595 104.195 151.833 1.00 33.21  ? 187  SER B CB  1 
ATOM   5086  O  OG  . SER B 1 212 ? 107.797 103.142 152.342 1.00 39.36  ? 187  SER B OG  1 
ATOM   5087  N  N   . TYR B 1 213 ? 108.586 104.020 154.705 1.00 34.35  ? 188  TYR B N   1 
ATOM   5088  C  CA  . TYR B 1 213 ? 108.343 103.497 156.040 1.00 35.15  ? 188  TYR B CA  1 
ATOM   5089  C  C   . TYR B 1 213 ? 107.479 102.242 156.037 1.00 44.19  ? 188  TYR B C   1 
ATOM   5090  O  O   . TYR B 1 213 ? 107.055 101.794 157.106 1.00 43.38  ? 188  TYR B O   1 
ATOM   5091  C  CB  . TYR B 1 213 ? 107.704 104.576 156.913 1.00 37.36  ? 188  TYR B CB  1 
ATOM   5092  C  CG  . TYR B 1 213 ? 108.583 105.787 157.116 1.00 36.43  ? 188  TYR B CG  1 
ATOM   5093  C  CD1 . TYR B 1 213 ? 109.598 105.782 158.062 1.00 38.54  ? 188  TYR B CD1 1 
ATOM   5094  C  CD2 . TYR B 1 213 ? 108.398 106.936 156.362 1.00 37.66  ? 188  TYR B CD2 1 
ATOM   5095  C  CE1 . TYR B 1 213 ? 110.403 106.887 158.250 1.00 31.61  ? 188  TYR B CE1 1 
ATOM   5096  C  CE2 . TYR B 1 213 ? 109.197 108.044 156.543 1.00 38.16  ? 188  TYR B CE2 1 
ATOM   5097  C  CZ  . TYR B 1 213 ? 110.197 108.014 157.488 1.00 37.04  ? 188  TYR B CZ  1 
ATOM   5098  O  OH  . TYR B 1 213 ? 110.993 109.119 157.671 1.00 44.24  ? 188  TYR B OH  1 
ATOM   5099  N  N   . MET B 1 214 ? 107.213 101.661 154.867 1.00 47.67  ? 189  MET B N   1 
ATOM   5100  C  CA  . MET B 1 214 ? 106.372 100.477 154.762 1.00 45.13  ? 189  MET B CA  1 
ATOM   5101  C  C   . MET B 1 214 ? 107.108 99.247  154.250 1.00 48.56  ? 189  MET B C   1 
ATOM   5102  O  O   . MET B 1 214 ? 106.490 98.184  154.128 1.00 53.96  ? 189  MET B O   1 
ATOM   5103  C  CB  . MET B 1 214 ? 105.172 100.754 153.845 1.00 46.61  ? 189  MET B CB  1 
ATOM   5104  C  CG  . MET B 1 214 ? 104.571 102.142 153.984 1.00 47.82  ? 189  MET B CG  1 
ATOM   5105  S  SD  . MET B 1 214 ? 103.206 102.215 155.155 1.00 58.88  ? 189  MET B SD  1 
ATOM   5106  C  CE  . MET B 1 214 ? 103.010 103.986 155.308 1.00 46.60  ? 189  MET B CE  1 
ATOM   5107  N  N   . GLU B 1 215 ? 108.401 99.351  153.951 1.00 44.93  ? 190  GLU B N   1 
ATOM   5108  C  CA  . GLU B 1 215 ? 109.107 98.277  153.267 1.00 47.69  ? 190  GLU B CA  1 
ATOM   5109  C  C   . GLU B 1 215 ? 110.585 98.323  153.622 1.00 52.95  ? 190  GLU B C   1 
ATOM   5110  O  O   . GLU B 1 215 ? 111.100 99.337  154.099 1.00 51.89  ? 190  GLU B O   1 
ATOM   5111  C  CB  . GLU B 1 215 ? 108.834 98.358  151.749 1.00 39.16  ? 190  GLU B CB  1 
ATOM   5112  C  CG  . GLU B 1 215 ? 109.388 99.572  150.946 1.00 47.18  ? 190  GLU B CG  1 
ATOM   5113  C  CD  . GLU B 1 215 ? 110.889 99.826  151.013 1.00 56.03  ? 190  GLU B CD  1 
ATOM   5114  O  OE1 . GLU B 1 215 ? 111.670 98.883  151.237 1.00 59.49  ? 190  GLU B OE1 1 
ATOM   5115  O  OE2 . GLU B 1 215 ? 111.293 100.995 150.855 1.00 55.37  ? 190  GLU B OE2 1 
ATOM   5116  N  N   . GLY B 1 216 ? 111.265 97.222  153.351 1.00 49.69  ? 191  GLY B N   1 
ATOM   5117  C  CA  . GLY B 1 216 ? 112.695 97.120  153.543 1.00 46.21  ? 191  GLY B CA  1 
ATOM   5118  C  C   . GLY B 1 216 ? 113.059 96.103  154.608 1.00 50.96  ? 191  GLY B C   1 
ATOM   5119  O  O   . GLY B 1 216 ? 112.272 95.792  155.512 1.00 54.54  ? 191  GLY B O   1 
ATOM   5120  N  N   . THR B 1 217 ? 114.270 95.565  154.494 1.00 48.07  ? 192  THR B N   1 
ATOM   5121  C  CA  . THR B 1 217 ? 114.815 94.679  155.510 1.00 43.64  ? 192  THR B CA  1 
ATOM   5122  C  C   . THR B 1 217 ? 116.332 94.754  155.439 1.00 46.57  ? 192  THR B C   1 
ATOM   5123  O  O   . THR B 1 217 ? 116.903 95.012  154.377 1.00 45.01  ? 192  THR B O   1 
ATOM   5124  C  CB  . THR B 1 217 ? 114.336 93.234  155.332 1.00 46.63  ? 192  THR B CB  1 
ATOM   5125  O  OG1 . THR B 1 217 ? 115.145 92.359  156.127 1.00 55.17  ? 192  THR B OG1 1 
ATOM   5126  C  CG2 . THR B 1 217 ? 114.437 92.814  153.880 1.00 51.85  ? 192  THR B CG2 1 
ATOM   5127  N  N   . GLY B 1 218 ? 116.976 94.527  156.582 1.00 52.11  ? 193  GLY B N   1 
ATOM   5128  C  CA  . GLY B 1 218 ? 118.421 94.632  156.648 1.00 49.84  ? 193  GLY B CA  1 
ATOM   5129  C  C   . GLY B 1 218 ? 119.165 93.502  155.974 1.00 49.17  ? 193  GLY B C   1 
ATOM   5130  O  O   . GLY B 1 218 ? 120.384 93.604  155.802 1.00 55.29  ? 193  GLY B O   1 
ATOM   5131  N  N   . ASN B 1 219 ? 118.466 92.435  155.590 1.00 44.23  ? 194  ASN B N   1 
ATOM   5132  C  CA  . ASN B 1 219 ? 119.091 91.320  154.893 1.00 46.56  ? 194  ASN B CA  1 
ATOM   5133  C  C   . ASN B 1 219 ? 119.374 91.626  153.430 1.00 49.44  ? 194  ASN B C   1 
ATOM   5134  O  O   . ASN B 1 219 ? 120.141 90.893  152.798 1.00 56.56  ? 194  ASN B O   1 
ATOM   5135  C  CB  . ASN B 1 219 ? 118.201 90.081  154.995 1.00 50.95  ? 194  ASN B CB  1 
ATOM   5136  C  CG  . ASN B 1 219 ? 117.663 89.864  156.394 1.00 54.14  ? 194  ASN B CG  1 
ATOM   5137  O  OD1 . ASN B 1 219 ? 118.241 90.332  157.374 1.00 56.09  ? 194  ASN B OD1 1 
ATOM   5138  N  ND2 . ASN B 1 219 ? 116.545 89.155  156.495 1.00 51.80  ? 194  ASN B ND2 1 
ATOM   5139  N  N   . MET B 1 220 ? 118.771 92.682  152.882 1.00 50.43  ? 195  MET B N   1 
ATOM   5140  C  CA  . MET B 1 220 ? 118.961 93.005  151.472 1.00 52.46  ? 195  MET B CA  1 
ATOM   5141  C  C   . MET B 1 220 ? 120.394 93.434  151.185 1.00 53.03  ? 195  MET B C   1 
ATOM   5142  O  O   . MET B 1 220 ? 120.962 93.068  150.150 1.00 55.41  ? 195  MET B O   1 
ATOM   5143  C  CB  . MET B 1 220 ? 117.976 94.097  151.059 1.00 48.57  ? 195  MET B CB  1 
ATOM   5144  C  CG  . MET B 1 220 ? 116.527 93.649  151.098 1.00 54.37  ? 195  MET B CG  1 
ATOM   5145  S  SD  . MET B 1 220 ? 115.387 94.796  150.309 1.00 61.75  ? 195  MET B SD  1 
ATOM   5146  C  CE  . MET B 1 220 ? 116.437 95.492  149.042 1.00 54.09  ? 195  MET B CE  1 
ATOM   5147  N  N   . PHE B 1 221 ? 120.995 94.205  152.086 1.00 49.50  ? 196  PHE B N   1 
ATOM   5148  C  CA  . PHE B 1 221 ? 122.338 94.739  151.897 1.00 46.67  ? 196  PHE B CA  1 
ATOM   5149  C  C   . PHE B 1 221 ? 123.335 93.886  152.668 1.00 50.63  ? 196  PHE B C   1 
ATOM   5150  O  O   . PHE B 1 221 ? 123.237 93.765  153.893 1.00 53.86  ? 196  PHE B O   1 
ATOM   5151  C  CB  . PHE B 1 221 ? 122.412 96.193  152.357 1.00 45.70  ? 196  PHE B CB  1 
ATOM   5152  C  CG  . PHE B 1 221 ? 121.290 97.044  151.849 1.00 45.79  ? 196  PHE B CG  1 
ATOM   5153  C  CD1 . PHE B 1 221 ? 121.311 97.542  150.559 1.00 47.63  ? 196  PHE B CD1 1 
ATOM   5154  C  CD2 . PHE B 1 221 ? 120.210 97.341  152.660 1.00 46.64  ? 196  PHE B CD2 1 
ATOM   5155  C  CE1 . PHE B 1 221 ? 120.279 98.324  150.090 1.00 48.88  ? 196  PHE B CE1 1 
ATOM   5156  C  CE2 . PHE B 1 221 ? 119.175 98.123  152.196 1.00 48.41  ? 196  PHE B CE2 1 
ATOM   5157  C  CZ  . PHE B 1 221 ? 119.209 98.615  150.910 1.00 50.69  ? 196  PHE B CZ  1 
ATOM   5158  N  N   . ASP B 1 222 ? 124.293 93.304  151.951 1.00 47.91  ? 197  ASP B N   1 
ATOM   5159  C  CA  . ASP B 1 222 ? 125.339 92.488  152.563 1.00 45.14  ? 197  ASP B CA  1 
ATOM   5160  C  C   . ASP B 1 222 ? 126.536 93.388  152.837 1.00 47.22  ? 197  ASP B C   1 
ATOM   5161  O  O   . ASP B 1 222 ? 127.261 93.776  151.918 1.00 44.50  ? 197  ASP B O   1 
ATOM   5162  C  CB  . ASP B 1 222 ? 125.710 91.319  151.658 1.00 48.77  ? 197  ASP B CB  1 
ATOM   5163  C  CG  . ASP B 1 222 ? 126.519 90.261  152.377 1.00 50.06  ? 197  ASP B CG  1 
ATOM   5164  O  OD1 . ASP B 1 222 ? 126.539 90.275  153.625 1.00 48.02  ? 197  ASP B OD1 1 
ATOM   5165  O  OD2 . ASP B 1 222 ? 127.135 89.415  151.696 1.00 51.43  ? 197  ASP B OD2 1 
ATOM   5166  N  N   . GLY B 1 223 ? 126.745 93.723  154.107 1.00 47.09  ? 198  GLY B N   1 
ATOM   5167  C  CA  . GLY B 1 223 ? 127.837 94.596  154.483 1.00 44.52  ? 198  GLY B CA  1 
ATOM   5168  C  C   . GLY B 1 223 ? 129.113 93.850  154.805 1.00 48.18  ? 198  GLY B C   1 
ATOM   5169  O  O   . GLY B 1 223 ? 129.910 94.297  155.634 1.00 50.02  ? 198  GLY B O   1 
ATOM   5170  N  N   . SER B 1 224 ? 129.318 92.705  154.155 1.00 49.07  ? 199  SER B N   1 
ATOM   5171  C  CA  . SER B 1 224 ? 130.538 91.931  154.344 1.00 45.15  ? 199  SER B CA  1 
ATOM   5172  C  C   . SER B 1 224 ? 131.699 92.447  153.508 1.00 47.01  ? 199  SER B C   1 
ATOM   5173  O  O   . SER B 1 224 ? 132.840 92.036  153.743 1.00 46.62  ? 199  SER B O   1 
ATOM   5174  C  CB  . SER B 1 224 ? 130.281 90.459  154.016 1.00 45.89  ? 199  SER B CB  1 
ATOM   5175  O  OG  . SER B 1 224 ? 130.262 90.246  152.615 1.00 44.41  ? 199  SER B OG  1 
ATOM   5176  N  N   . VAL B 1 225 ? 131.441 93.327  152.546 1.00 40.90  ? 200  VAL B N   1 
ATOM   5177  C  CA  . VAL B 1 225 ? 132.504 93.898  151.726 1.00 37.07  ? 200  VAL B CA  1 
ATOM   5178  C  C   . VAL B 1 225 ? 133.008 95.208  152.314 1.00 38.94  ? 200  VAL B C   1 
ATOM   5179  O  O   . VAL B 1 225 ? 134.219 95.434  152.395 1.00 45.23  ? 200  VAL B O   1 
ATOM   5180  C  CB  . VAL B 1 225 ? 132.000 94.087  150.283 1.00 36.43  ? 200  VAL B CB  1 
ATOM   5181  C  CG1 . VAL B 1 225 ? 133.167 94.160  149.323 1.00 36.51  ? 200  VAL B CG1 1 
ATOM   5182  C  CG2 . VAL B 1 225 ? 131.051 92.964  149.904 1.00 40.91  ? 200  VAL B CG2 1 
ATOM   5183  N  N   . LEU B 1 226 ? 132.087 96.080  152.728 1.00 42.37  ? 201  LEU B N   1 
ATOM   5184  C  CA  . LEU B 1 226 ? 132.477 97.327  153.375 1.00 35.98  ? 201  LEU B CA  1 
ATOM   5185  C  C   . LEU B 1 226 ? 133.215 97.061  154.679 1.00 41.76  ? 201  LEU B C   1 
ATOM   5186  O  O   . LEU B 1 226 ? 134.165 97.775  155.021 1.00 45.06  ? 201  LEU B O   1 
ATOM   5187  C  CB  . LEU B 1 226 ? 131.242 98.193  153.620 1.00 32.49  ? 201  LEU B CB  1 
ATOM   5188  C  CG  . LEU B 1 226 ? 131.439 99.505  154.379 1.00 33.81  ? 201  LEU B CG  1 
ATOM   5189  C  CD1 . LEU B 1 226 ? 132.341 100.436 153.601 1.00 38.56  ? 201  LEU B CD1 1 
ATOM   5190  C  CD2 . LEU B 1 226 ? 130.102 100.166 154.654 1.00 39.16  ? 201  LEU B CD2 1 
ATOM   5191  N  N   . ALA B 1 227 ? 132.788 96.040  155.425 1.00 39.59  ? 202  ALA B N   1 
ATOM   5192  C  CA  . ALA B 1 227 ? 133.457 95.706  156.677 1.00 40.14  ? 202  ALA B CA  1 
ATOM   5193  C  C   . ALA B 1 227 ? 134.888 95.246  156.437 1.00 43.93  ? 202  ALA B C   1 
ATOM   5194  O  O   . ALA B 1 227 ? 135.803 95.628  157.175 1.00 46.32  ? 202  ALA B O   1 
ATOM   5195  C  CB  . ALA B 1 227 ? 132.669 94.631  157.424 1.00 41.71  ? 202  ALA B CB  1 
ATOM   5196  N  N   . ALA B 1 228 ? 135.103 94.424  155.407 1.00 44.16  ? 203  ALA B N   1 
ATOM   5197  C  CA  . ALA B 1 228 ? 136.444 93.918  155.137 1.00 44.65  ? 203  ALA B CA  1 
ATOM   5198  C  C   . ALA B 1 228 ? 137.343 94.988  154.535 1.00 46.27  ? 203  ALA B C   1 
ATOM   5199  O  O   . ALA B 1 228 ? 138.548 95.007  154.809 1.00 47.97  ? 203  ALA B O   1 
ATOM   5200  C  CB  . ALA B 1 228 ? 136.375 92.708  154.209 1.00 43.55  ? 203  ALA B CB  1 
ATOM   5201  N  N   . TYR B 1 229 ? 136.784 95.879  153.715 1.00 41.16  ? 204  TYR B N   1 
ATOM   5202  C  CA  . TYR B 1 229 ? 137.603 96.899  153.068 1.00 38.11  ? 204  TYR B CA  1 
ATOM   5203  C  C   . TYR B 1 229 ? 138.075 97.945  154.070 1.00 40.85  ? 204  TYR B C   1 
ATOM   5204  O  O   . TYR B 1 229 ? 139.277 98.204  154.192 1.00 49.18  ? 204  TYR B O   1 
ATOM   5205  C  CB  . TYR B 1 229 ? 136.815 97.553  151.934 1.00 35.59  ? 204  TYR B CB  1 
ATOM   5206  C  CG  . TYR B 1 229 ? 137.631 98.458  151.040 1.00 37.84  ? 204  TYR B CG  1 
ATOM   5207  C  CD1 . TYR B 1 229 ? 137.914 99.766  151.411 1.00 38.33  ? 204  TYR B CD1 1 
ATOM   5208  C  CD2 . TYR B 1 229 ? 138.105 98.009  149.817 1.00 41.82  ? 204  TYR B CD2 1 
ATOM   5209  C  CE1 . TYR B 1 229 ? 138.654 100.594 150.594 1.00 39.76  ? 204  TYR B CE1 1 
ATOM   5210  C  CE2 . TYR B 1 229 ? 138.844 98.831  148.993 1.00 43.36  ? 204  TYR B CE2 1 
ATOM   5211  C  CZ  . TYR B 1 229 ? 139.116 100.122 149.387 1.00 39.97  ? 204  TYR B CZ  1 
ATOM   5212  O  OH  . TYR B 1 229 ? 139.854 100.944 148.569 1.00 41.48  ? 204  TYR B OH  1 
ATOM   5213  N  N   . GLY B 1 230 ? 137.145 98.557  154.794 1.00 34.32  ? 205  GLY B N   1 
ATOM   5214  C  CA  . GLY B 1 230 ? 137.465 99.632  155.706 1.00 39.46  ? 205  GLY B CA  1 
ATOM   5215  C  C   . GLY B 1 230 ? 137.810 99.234  157.120 1.00 39.70  ? 205  GLY B C   1 
ATOM   5216  O  O   . GLY B 1 230 ? 138.078 100.116 157.942 1.00 38.78  ? 205  GLY B O   1 
ATOM   5217  N  N   . ASN B 1 231 ? 137.815 97.938  157.432 1.00 44.51  ? 206  ASN B N   1 
ATOM   5218  C  CA  . ASN B 1 231 ? 138.096 97.450  158.784 1.00 48.49  ? 206  ASN B CA  1 
ATOM   5219  C  C   . ASN B 1 231 ? 137.146 98.067  159.809 1.00 50.07  ? 206  ASN B C   1 
ATOM   5220  O  O   . ASN B 1 231 ? 137.555 98.462  160.903 1.00 51.94  ? 206  ASN B O   1 
ATOM   5221  C  CB  . ASN B 1 231 ? 139.554 97.702  159.175 1.00 44.39  ? 206  ASN B CB  1 
ATOM   5222  C  CG  . ASN B 1 231 ? 140.480 96.595  158.716 1.00 52.37  ? 206  ASN B CG  1 
ATOM   5223  O  OD1 . ASN B 1 231 ? 140.249 95.962  157.687 1.00 54.14  ? 206  ASN B OD1 1 
ATOM   5224  N  ND2 . ASN B 1 231 ? 141.539 96.356  159.481 1.00 52.91  ? 206  ASN B ND2 1 
ATOM   5225  N  N   . VAL B 1 232 ? 135.865 98.151  159.454 1.00 43.63  ? 207  VAL B N   1 
ATOM   5226  C  CA  . VAL B 1 232 ? 134.841 98.739  160.309 1.00 42.99  ? 207  VAL B CA  1 
ATOM   5227  C  C   . VAL B 1 232 ? 133.707 97.736  160.468 1.00 40.31  ? 207  VAL B C   1 
ATOM   5228  O  O   . VAL B 1 232 ? 133.222 97.179  159.478 1.00 43.85  ? 207  VAL B O   1 
ATOM   5229  C  CB  . VAL B 1 232 ? 134.311 100.067 159.735 1.00 36.58  ? 207  VAL B CB  1 
ATOM   5230  C  CG1 . VAL B 1 232 ? 135.255 101.205 160.075 1.00 37.04  ? 207  VAL B CG1 1 
ATOM   5231  C  CG2 . VAL B 1 232 ? 134.129 99.960  158.232 1.00 31.69  ? 207  VAL B CG2 1 
ATOM   5232  N  N   . ILE B 1 233 ? 133.288 97.505  161.711 1.00 34.64  ? 208  ILE B N   1 
ATOM   5233  C  CA  . ILE B 1 233 ? 132.179 96.596  161.978 1.00 34.92  ? 208  ILE B CA  1 
ATOM   5234  C  C   . ILE B 1 233 ? 130.892 97.229  161.466 1.00 37.14  ? 208  ILE B C   1 
ATOM   5235  O  O   . ILE B 1 233 ? 130.507 98.319  161.903 1.00 47.53  ? 208  ILE B O   1 
ATOM   5236  C  CB  . ILE B 1 233 ? 132.081 96.278  163.474 1.00 37.73  ? 208  ILE B CB  1 
ATOM   5237  C  CG1 . ILE B 1 233 ? 133.341 95.557  163.950 1.00 43.42  ? 208  ILE B CG1 1 
ATOM   5238  C  CG2 . ILE B 1 233 ? 130.846 95.444  163.761 1.00 39.20  ? 208  ILE B CG2 1 
ATOM   5239  C  CD1 . ILE B 1 233 ? 133.338 95.238  165.425 1.00 41.88  ? 208  ILE B CD1 1 
ATOM   5240  N  N   . VAL B 1 234 ? 130.210 96.540  160.555 1.00 36.83  ? 209  VAL B N   1 
ATOM   5241  C  CA  . VAL B 1 234 ? 129.003 97.056  159.914 1.00 31.18  ? 209  VAL B CA  1 
ATOM   5242  C  C   . VAL B 1 234 ? 127.797 96.321  160.480 1.00 35.51  ? 209  VAL B C   1 
ATOM   5243  O  O   . VAL B 1 234 ? 127.746 95.087  160.453 1.00 48.08  ? 209  VAL B O   1 
ATOM   5244  C  CB  . VAL B 1 234 ? 129.068 96.910  158.385 1.00 28.53  ? 209  VAL B CB  1 
ATOM   5245  C  CG1 . VAL B 1 234 ? 127.741 97.294  157.761 1.00 35.28  ? 209  VAL B CG1 1 
ATOM   5246  C  CG2 . VAL B 1 234 ? 130.188 97.763  157.824 1.00 30.39  ? 209  VAL B CG2 1 
ATOM   5247  N  N   . VAL B 1 235 ? 126.822 97.075  160.982 1.00 27.60  ? 210  VAL B N   1 
ATOM   5248  C  CA  . VAL B 1 235 ? 125.655 96.515  161.652 1.00 31.44  ? 210  VAL B CA  1 
ATOM   5249  C  C   . VAL B 1 235 ? 124.411 96.930  160.882 1.00 34.63  ? 210  VAL B C   1 
ATOM   5250  O  O   . VAL B 1 235 ? 124.132 98.127  160.746 1.00 52.61  ? 210  VAL B O   1 
ATOM   5251  C  CB  . VAL B 1 235 ? 125.565 96.978  163.114 1.00 38.72  ? 210  VAL B CB  1 
ATOM   5252  C  CG1 . VAL B 1 235 ? 124.438 96.259  163.828 1.00 40.05  ? 210  VAL B CG1 1 
ATOM   5253  C  CG2 . VAL B 1 235 ? 126.887 96.758  163.823 1.00 37.51  ? 210  VAL B CG2 1 
ATOM   5254  N  N   . THR B 1 236 ? 123.651 95.947  160.407 1.00 29.50  ? 211  THR B N   1 
ATOM   5255  C  CA  . THR B 1 236 ? 122.398 96.195  159.703 1.00 34.36  ? 211  THR B CA  1 
ATOM   5256  C  C   . THR B 1 236 ? 121.251 95.608  160.512 1.00 39.39  ? 211  THR B C   1 
ATOM   5257  O  O   . THR B 1 236 ? 121.262 94.418  160.832 1.00 43.97  ? 211  THR B O   1 
ATOM   5258  C  CB  . THR B 1 236 ? 122.419 95.592  158.297 1.00 38.30  ? 211  THR B CB  1 
ATOM   5259  O  OG1 . THR B 1 236 ? 122.355 94.164  158.386 1.00 39.60  ? 211  THR B OG1 1 
ATOM   5260  C  CG2 . THR B 1 236 ? 123.689 95.993  157.566 1.00 35.00  ? 211  THR B CG2 1 
ATOM   5261  N  N   . LEU B 1 237 ? 120.258 96.432  160.824 1.00 43.16  ? 212  LEU B N   1 
ATOM   5262  C  CA  . LEU B 1 237 ? 119.204 96.055  161.754 1.00 41.50  ? 212  LEU B CA  1 
ATOM   5263  C  C   . LEU B 1 237 ? 117.875 95.868  161.032 1.00 42.57  ? 212  LEU B C   1 
ATOM   5264  O  O   . LEU B 1 237 ? 117.725 96.180  159.849 1.00 46.31  ? 212  LEU B O   1 
ATOM   5265  C  CB  . LEU B 1 237 ? 119.057 97.105  162.863 1.00 40.07  ? 212  LEU B CB  1 
ATOM   5266  C  CG  . LEU B 1 237 ? 118.119 98.291  162.614 1.00 35.17  ? 212  LEU B CG  1 
ATOM   5267  C  CD1 . LEU B 1 237 ? 117.979 99.130  163.868 1.00 40.59  ? 212  LEU B CD1 1 
ATOM   5268  C  CD2 . LEU B 1 237 ? 118.600 99.154  161.466 1.00 29.93  ? 212  LEU B CD2 1 
ATOM   5269  N  N   . ASN B 1 238 ? 116.905 95.341  161.778 1.00 39.51  ? 213  ASN B N   1 
ATOM   5270  C  CA  . ASN B 1 238 ? 115.519 95.248  161.345 1.00 38.52  ? 213  ASN B CA  1 
ATOM   5271  C  C   . ASN B 1 238 ? 114.644 95.892  162.408 1.00 42.51  ? 213  ASN B C   1 
ATOM   5272  O  O   . ASN B 1 238 ? 114.792 95.595  163.598 1.00 44.29  ? 213  ASN B O   1 
ATOM   5273  C  CB  . ASN B 1 238 ? 115.096 93.794  161.118 1.00 36.72  ? 213  ASN B CB  1 
ATOM   5274  C  CG  . ASN B 1 238 ? 115.802 93.160  159.940 1.00 39.51  ? 213  ASN B CG  1 
ATOM   5275  O  OD1 . ASN B 1 238 ? 116.284 93.853  159.047 1.00 44.90  ? 213  ASN B OD1 1 
ATOM   5276  N  ND2 . ASN B 1 238 ? 115.866 91.835  159.932 1.00 39.78  ? 213  ASN B ND2 1 
ATOM   5277  N  N   . TYR B 1 239 ? 113.740 96.770  161.984 1.00 44.68  ? 214  TYR B N   1 
ATOM   5278  C  CA  . TYR B 1 239 ? 112.879 97.500  162.901 1.00 40.54  ? 214  TYR B CA  1 
ATOM   5279  C  C   . TYR B 1 239 ? 111.447 97.471  162.389 1.00 41.66  ? 214  TYR B C   1 
ATOM   5280  O  O   . TYR B 1 239 ? 111.194 97.242  161.205 1.00 45.62  ? 214  TYR B O   1 
ATOM   5281  C  CB  . TYR B 1 239 ? 113.350 98.949  163.085 1.00 40.24  ? 214  TYR B CB  1 
ATOM   5282  C  CG  . TYR B 1 239 ? 113.388 99.764  161.811 1.00 44.67  ? 214  TYR B CG  1 
ATOM   5283  C  CD1 . TYR B 1 239 ? 114.506 99.749  160.987 1.00 44.83  ? 214  TYR B CD1 1 
ATOM   5284  C  CD2 . TYR B 1 239 ? 112.314 100.560 161.440 1.00 45.86  ? 214  TYR B CD2 1 
ATOM   5285  C  CE1 . TYR B 1 239 ? 114.547 100.495 159.826 1.00 40.98  ? 214  TYR B CE1 1 
ATOM   5286  C  CE2 . TYR B 1 239 ? 112.347 101.310 160.281 1.00 44.90  ? 214  TYR B CE2 1 
ATOM   5287  C  CZ  . TYR B 1 239 ? 113.466 101.274 159.479 1.00 39.17  ? 214  TYR B CZ  1 
ATOM   5288  O  OH  . TYR B 1 239 ? 113.501 102.021 158.324 1.00 39.62  ? 214  TYR B OH  1 
ATOM   5289  N  N   . ARG B 1 240 ? 110.511 97.702  163.308 1.00 44.37  ? 215  ARG B N   1 
ATOM   5290  C  CA  . ARG B 1 240 ? 109.095 97.660  162.969 1.00 44.76  ? 215  ARG B CA  1 
ATOM   5291  C  C   . ARG B 1 240 ? 108.770 98.690  161.895 1.00 47.89  ? 215  ARG B C   1 
ATOM   5292  O  O   . ARG B 1 240 ? 109.235 99.831  161.942 1.00 51.62  ? 215  ARG B O   1 
ATOM   5293  C  CB  . ARG B 1 240 ? 108.251 97.910  164.218 1.00 43.92  ? 215  ARG B CB  1 
ATOM   5294  C  CG  . ARG B 1 240 ? 108.030 96.672  165.066 1.00 42.40  ? 215  ARG B CG  1 
ATOM   5295  C  CD  . ARG B 1 240 ? 107.272 97.004  166.337 1.00 41.77  ? 215  ARG B CD  1 
ATOM   5296  N  NE  . ARG B 1 240 ? 108.134 97.624  167.336 1.00 46.24  ? 215  ARG B NE  1 
ATOM   5297  C  CZ  . ARG B 1 240 ? 107.714 98.070  168.511 1.00 48.62  ? 215  ARG B CZ  1 
ATOM   5298  N  NH1 . ARG B 1 240 ? 106.443 97.985  168.868 1.00 46.87  ? 215  ARG B NH1 1 
ATOM   5299  N  NH2 . ARG B 1 240 ? 108.591 98.615  169.349 1.00 48.28  ? 215  ARG B NH2 1 
ATOM   5300  N  N   . LEU B 1 241 ? 107.963 98.278  160.920 1.00 49.68  ? 216  LEU B N   1 
ATOM   5301  C  CA  . LEU B 1 241 ? 107.704 99.076  159.732 1.00 47.85  ? 216  LEU B CA  1 
ATOM   5302  C  C   . LEU B 1 241 ? 106.208 99.209  159.493 1.00 51.68  ? 216  LEU B C   1 
ATOM   5303  O  O   . LEU B 1 241 ? 105.426 98.312  159.818 1.00 50.95  ? 216  LEU B O   1 
ATOM   5304  C  CB  . LEU B 1 241 ? 108.357 98.454  158.492 1.00 43.47  ? 216  LEU B CB  1 
ATOM   5305  C  CG  . LEU B 1 241 ? 109.881 98.378  158.460 1.00 46.77  ? 216  LEU B CG  1 
ATOM   5306  C  CD1 . LEU B 1 241 ? 110.330 97.073  157.830 1.00 47.37  ? 216  LEU B CD1 1 
ATOM   5307  C  CD2 . LEU B 1 241 ? 110.453 99.562  157.702 1.00 48.54  ? 216  LEU B CD2 1 
ATOM   5308  N  N   . GLY B 1 242 ? 105.825 100.341 158.913 1.00 42.93  ? 217  GLY B N   1 
ATOM   5309  C  CA  . GLY B 1 242 ? 104.465 100.493 158.422 1.00 40.39  ? 217  GLY B CA  1 
ATOM   5310  C  C   . GLY B 1 242 ? 103.443 100.547 159.536 1.00 43.24  ? 217  GLY B C   1 
ATOM   5311  O  O   . GLY B 1 242 ? 103.532 101.363 160.460 1.00 46.98  ? 217  GLY B O   1 
ATOM   5312  N  N   . VAL B 1 243 ? 102.447 99.664  159.442 1.00 49.70  ? 218  VAL B N   1 
ATOM   5313  C  CA  . VAL B 1 243 ? 101.284 99.735  160.320 1.00 49.77  ? 218  VAL B CA  1 
ATOM   5314  C  C   . VAL B 1 243 ? 101.672 99.489  161.772 1.00 50.94  ? 218  VAL B C   1 
ATOM   5315  O  O   . VAL B 1 243 ? 101.258 100.230 162.671 1.00 56.21  ? 218  VAL B O   1 
ATOM   5316  C  CB  . VAL B 1 243 ? 100.212 98.739  159.849 1.00 53.31  ? 218  VAL B CB  1 
ATOM   5317  C  CG1 . VAL B 1 243 ? 98.872  99.101  160.438 1.00 49.96  ? 218  VAL B CG1 1 
ATOM   5318  C  CG2 . VAL B 1 243 ? 100.142 98.720  158.329 1.00 55.91  ? 218  VAL B CG2 1 
ATOM   5319  N  N   . LEU B 1 244 ? 102.466 98.451  162.031 1.00 45.83  ? 219  LEU B N   1 
ATOM   5320  C  CA  . LEU B 1 244 ? 102.783 98.080  163.403 1.00 45.11  ? 219  LEU B CA  1 
ATOM   5321  C  C   . LEU B 1 244 ? 103.854 98.960  164.030 1.00 48.54  ? 219  LEU B C   1 
ATOM   5322  O  O   . LEU B 1 244 ? 104.039 98.902  165.250 1.00 54.61  ? 219  LEU B O   1 
ATOM   5323  C  CB  . LEU B 1 244 ? 103.235 96.620  163.467 1.00 46.19  ? 219  LEU B CB  1 
ATOM   5324  C  CG  . LEU B 1 244 ? 102.375 95.591  162.735 1.00 50.47  ? 219  LEU B CG  1 
ATOM   5325  C  CD1 . LEU B 1 244 ? 103.030 95.208  161.423 1.00 52.66  ? 219  LEU B CD1 1 
ATOM   5326  C  CD2 . LEU B 1 244 ? 102.148 94.368  163.602 1.00 52.17  ? 219  LEU B CD2 1 
ATOM   5327  N  N   . GLY B 1 245 ? 104.554 99.767  163.240 1.00 43.54  ? 220  GLY B N   1 
ATOM   5328  C  CA  . GLY B 1 245 ? 105.679 100.518 163.756 1.00 42.79  ? 220  GLY B CA  1 
ATOM   5329  C  C   . GLY B 1 245 ? 105.420 101.989 164.002 1.00 46.65  ? 220  GLY B C   1 
ATOM   5330  O  O   . GLY B 1 245 ? 105.949 102.558 164.959 1.00 49.94  ? 220  GLY B O   1 
ATOM   5331  N  N   . PHE B 1 246 ? 104.618 102.625 163.148 1.00 46.91  ? 221  PHE B N   1 
ATOM   5332  C  CA  . PHE B 1 246 ? 104.433 104.070 163.210 1.00 46.32  ? 221  PHE B CA  1 
ATOM   5333  C  C   . PHE B 1 246 ? 102.969 104.473 163.354 1.00 47.06  ? 221  PHE B C   1 
ATOM   5334  O  O   . PHE B 1 246 ? 102.618 105.622 163.070 1.00 44.55  ? 221  PHE B O   1 
ATOM   5335  C  CB  . PHE B 1 246 ? 105.052 104.733 161.980 1.00 43.83  ? 221  PHE B CB  1 
ATOM   5336  C  CG  . PHE B 1 246 ? 106.523 104.468 161.828 1.00 38.72  ? 221  PHE B CG  1 
ATOM   5337  C  CD1 . PHE B 1 246 ? 107.429 104.982 162.736 1.00 40.45  ? 221  PHE B CD1 1 
ATOM   5338  C  CD2 . PHE B 1 246 ? 106.998 103.704 160.777 1.00 44.39  ? 221  PHE B CD2 1 
ATOM   5339  C  CE1 . PHE B 1 246 ? 108.781 104.739 162.600 1.00 44.61  ? 221  PHE B CE1 1 
ATOM   5340  C  CE2 . PHE B 1 246 ? 108.348 103.459 160.637 1.00 44.05  ? 221  PHE B CE2 1 
ATOM   5341  C  CZ  . PHE B 1 246 ? 109.240 103.977 161.549 1.00 41.26  ? 221  PHE B CZ  1 
ATOM   5342  N  N   . LEU B 1 247 ? 102.108 103.558 163.789 1.00 51.18  ? 222  LEU B N   1 
ATOM   5343  C  CA  . LEU B 1 247 ? 100.722 103.911 164.060 1.00 51.47  ? 222  LEU B CA  1 
ATOM   5344  C  C   . LEU B 1 247 ? 100.642 104.831 165.271 1.00 58.34  ? 222  LEU B C   1 
ATOM   5345  O  O   . LEU B 1 247 ? 101.325 104.621 166.276 1.00 62.65  ? 222  LEU B O   1 
ATOM   5346  C  CB  . LEU B 1 247 ? 99.888  102.654 164.298 1.00 52.74  ? 222  LEU B CB  1 
ATOM   5347  C  CG  . LEU B 1 247 ? 98.370  102.826 164.369 1.00 53.39  ? 222  LEU B CG  1 
ATOM   5348  C  CD1 . LEU B 1 247 ? 97.679  101.720 163.595 1.00 55.04  ? 222  LEU B CD1 1 
ATOM   5349  C  CD2 . LEU B 1 247 ? 97.894  102.844 165.812 1.00 56.51  ? 222  LEU B CD2 1 
ATOM   5350  N  N   . SER B 1 248 ? 99.800  105.856 165.174 1.00 62.09  ? 223  SER B N   1 
ATOM   5351  C  CA  . SER B 1 248 ? 99.650  106.809 166.264 1.00 61.27  ? 223  SER B CA  1 
ATOM   5352  C  C   . SER B 1 248 ? 98.292  107.484 166.157 1.00 63.33  ? 223  SER B C   1 
ATOM   5353  O  O   . SER B 1 248 ? 97.669  107.506 165.093 1.00 65.30  ? 223  SER B O   1 
ATOM   5354  C  CB  . SER B 1 248 ? 100.770 107.855 166.254 1.00 62.52  ? 223  SER B CB  1 
ATOM   5355  O  OG  . SER B 1 248 ? 100.649 108.740 167.353 1.00 67.34  ? 223  SER B OG  1 
ATOM   5356  N  N   . THR B 1 249 ? 97.843  108.035 167.285 1.00 77.25  ? 224  THR B N   1 
ATOM   5357  C  CA  . THR B 1 249 ? 96.583  108.758 167.355 1.00 77.56  ? 224  THR B CA  1 
ATOM   5358  C  C   . THR B 1 249 ? 96.720  110.168 167.908 1.00 76.96  ? 224  THR B C   1 
ATOM   5359  O  O   . THR B 1 249 ? 95.726  110.903 167.925 1.00 79.23  ? 224  THR B O   1 
ATOM   5360  C  CB  . THR B 1 249 ? 95.567  107.995 168.221 1.00 79.42  ? 224  THR B CB  1 
ATOM   5361  O  OG1 . THR B 1 249 ? 96.104  107.805 169.535 1.00 80.13  ? 224  THR B OG1 1 
ATOM   5362  C  CG2 . THR B 1 249 ? 95.249  106.642 167.611 1.00 76.68  ? 224  THR B CG2 1 
ATOM   5363  N  N   . GLY B 1 250 ? 97.907  110.568 168.357 1.00 78.52  ? 225  GLY B N   1 
ATOM   5364  C  CA  . GLY B 1 250 ? 98.105  111.839 169.009 1.00 79.66  ? 225  GLY B CA  1 
ATOM   5365  C  C   . GLY B 1 250 ? 97.848  111.812 170.502 1.00 83.34  ? 225  GLY B C   1 
ATOM   5366  O  O   . GLY B 1 250 ? 98.448  112.599 171.241 1.00 85.65  ? 225  GLY B O   1 
ATOM   5367  N  N   . ASP B 1 251 ? 96.971  110.923 170.961 1.00 96.15  ? 226  ASP B N   1 
ATOM   5368  C  CA  . ASP B 1 251 ? 96.685  110.774 172.381 1.00 97.16  ? 226  ASP B CA  1 
ATOM   5369  C  C   . ASP B 1 251 ? 97.754  109.891 173.022 1.00 96.02  ? 226  ASP B C   1 
ATOM   5370  O  O   . ASP B 1 251 ? 98.782  109.575 172.416 1.00 93.74  ? 226  ASP B O   1 
ATOM   5371  C  CB  . ASP B 1 251 ? 95.282  110.206 172.580 1.00 96.20  ? 226  ASP B CB  1 
ATOM   5372  C  CG  . ASP B 1 251 ? 94.223  110.991 171.832 1.00 96.93  ? 226  ASP B CG  1 
ATOM   5373  O  OD1 . ASP B 1 251 ? 94.311  112.236 171.807 1.00 99.16  ? 226  ASP B OD1 1 
ATOM   5374  O  OD2 . ASP B 1 251 ? 93.302  110.361 171.270 1.00 94.38  ? 226  ASP B OD2 1 
ATOM   5375  N  N   . GLN B 1 252 ? 97.522  109.480 174.265 1.00 104.48 ? 227  GLN B N   1 
ATOM   5376  C  CA  . GLN B 1 252 ? 98.432  108.584 174.964 1.00 104.73 ? 227  GLN B CA  1 
ATOM   5377  C  C   . GLN B 1 252 ? 98.115  107.114 174.727 1.00 105.02 ? 227  GLN B C   1 
ATOM   5378  O  O   . GLN B 1 252 ? 98.852  106.251 175.216 1.00 104.91 ? 227  GLN B O   1 
ATOM   5379  C  CB  . GLN B 1 252 ? 98.412  108.880 176.467 1.00 103.73 ? 227  GLN B CB  1 
ATOM   5380  C  CG  . GLN B 1 252 ? 99.065  110.199 176.843 1.00 104.18 ? 227  GLN B CG  1 
ATOM   5381  C  CD  . GLN B 1 252 ? 100.477 110.020 177.365 1.00 104.68 ? 227  GLN B CD  1 
ATOM   5382  O  OE1 . GLN B 1 252 ? 100.977 108.899 177.461 1.00 104.90 ? 227  GLN B OE1 1 
ATOM   5383  N  NE2 . GLN B 1 252 ? 101.128 111.126 177.705 1.00 104.35 ? 227  GLN B NE2 1 
ATOM   5384  N  N   . ALA B 1 253 ? 97.038  106.808 173.999 1.00 103.49 ? 228  ALA B N   1 
ATOM   5385  C  CA  . ALA B 1 253 ? 96.729  105.417 173.685 1.00 102.54 ? 228  ALA B CA  1 
ATOM   5386  C  C   . ALA B 1 253 ? 97.804  104.801 172.799 1.00 103.78 ? 228  ALA B C   1 
ATOM   5387  O  O   . ALA B 1 253 ? 98.211  103.653 173.008 1.00 103.57 ? 228  ALA B O   1 
ATOM   5388  C  CB  . ALA B 1 253 ? 95.360  105.321 173.015 1.00 102.23 ? 228  ALA B CB  1 
ATOM   5389  N  N   . ALA B 1 254 ? 98.276  105.551 171.802 1.00 88.96  ? 229  ALA B N   1 
ATOM   5390  C  CA  . ALA B 1 254 ? 99.343  105.082 170.919 1.00 85.14  ? 229  ALA B CA  1 
ATOM   5391  C  C   . ALA B 1 254 ? 100.170 106.303 170.527 1.00 83.24  ? 229  ALA B C   1 
ATOM   5392  O  O   . ALA B 1 254 ? 99.804  107.030 169.599 1.00 86.30  ? 229  ALA B O   1 
ATOM   5393  C  CB  . ALA B 1 254 ? 98.778  104.370 169.698 1.00 80.15  ? 229  ALA B CB  1 
ATOM   5394  N  N   . LYS B 1 255 ? 101.276 106.522 171.242 1.00 71.59  ? 230  LYS B N   1 
ATOM   5395  C  CA  . LYS B 1 255 ? 102.092 107.709 171.001 1.00 72.71  ? 230  LYS B CA  1 
ATOM   5396  C  C   . LYS B 1 255 ? 102.696 107.696 169.602 1.00 71.69  ? 230  LYS B C   1 
ATOM   5397  O  O   . LYS B 1 255 ? 102.706 108.723 168.913 1.00 72.29  ? 230  LYS B O   1 
ATOM   5398  C  CB  . LYS B 1 255 ? 103.188 107.812 172.060 1.00 74.28  ? 230  LYS B CB  1 
ATOM   5399  C  CG  . LYS B 1 255 ? 102.783 108.605 173.291 1.00 73.25  ? 230  LYS B CG  1 
ATOM   5400  C  CD  . LYS B 1 255 ? 102.792 110.099 173.018 1.00 74.95  ? 230  LYS B CD  1 
ATOM   5401  C  CE  . LYS B 1 255 ? 102.873 110.895 174.310 1.00 76.84  ? 230  LYS B CE  1 
ATOM   5402  N  NZ  . LYS B 1 255 ? 102.980 112.357 174.057 1.00 75.44  ? 230  LYS B NZ  1 
ATOM   5403  N  N   . GLY B 1 256 ? 103.202 106.549 169.164 1.00 60.71  ? 231  GLY B N   1 
ATOM   5404  C  CA  . GLY B 1 256 ? 103.770 106.418 167.837 1.00 62.43  ? 231  GLY B CA  1 
ATOM   5405  C  C   . GLY B 1 256 ? 105.286 106.372 167.857 1.00 67.87  ? 231  GLY B C   1 
ATOM   5406  O  O   . GLY B 1 256 ? 105.937 106.400 168.906 1.00 68.38  ? 231  GLY B O   1 
ATOM   5407  N  N   . ASN B 1 257 ? 105.843 106.305 166.646 1.00 57.44  ? 232  ASN B N   1 
ATOM   5408  C  CA  . ASN B 1 257 ? 107.288 106.213 166.429 1.00 49.70  ? 232  ASN B CA  1 
ATOM   5409  C  C   . ASN B 1 257 ? 107.893 105.034 167.191 1.00 54.43  ? 232  ASN B C   1 
ATOM   5410  O  O   . ASN B 1 257 ? 108.911 105.161 167.872 1.00 57.97  ? 232  ASN B O   1 
ATOM   5411  C  CB  . ASN B 1 257 ? 107.996 107.519 166.800 1.00 48.20  ? 232  ASN B CB  1 
ATOM   5412  C  CG  . ASN B 1 257 ? 107.114 108.731 166.619 1.00 53.99  ? 232  ASN B CG  1 
ATOM   5413  O  OD1 . ASN B 1 257 ? 106.627 109.001 165.523 1.00 58.33  ? 232  ASN B OD1 1 
ATOM   5414  N  ND2 . ASN B 1 257 ? 106.911 109.478 167.694 1.00 55.63  ? 232  ASN B ND2 1 
ATOM   5415  N  N   . TYR B 1 258 ? 107.250 103.871 167.073 1.00 53.53  ? 233  TYR B N   1 
ATOM   5416  C  CA  . TYR B 1 258 ? 107.832 102.668 167.657 1.00 54.36  ? 233  TYR B CA  1 
ATOM   5417  C  C   . TYR B 1 258 ? 109.015 102.171 166.839 1.00 52.53  ? 233  TYR B C   1 
ATOM   5418  O  O   . TYR B 1 258 ? 109.902 101.505 167.380 1.00 62.15  ? 233  TYR B O   1 
ATOM   5419  C  CB  . TYR B 1 258 ? 106.777 101.572 167.791 1.00 60.36  ? 233  TYR B CB  1 
ATOM   5420  C  CG  . TYR B 1 258 ? 105.498 102.032 168.449 1.00 59.63  ? 233  TYR B CG  1 
ATOM   5421  C  CD1 . TYR B 1 258 ? 105.477 102.395 169.787 1.00 58.88  ? 233  TYR B CD1 1 
ATOM   5422  C  CD2 . TYR B 1 258 ? 104.313 102.105 167.731 1.00 55.80  ? 233  TYR B CD2 1 
ATOM   5423  C  CE1 . TYR B 1 258 ? 104.314 102.818 170.392 1.00 60.34  ? 233  TYR B CE1 1 
ATOM   5424  C  CE2 . TYR B 1 258 ? 103.145 102.526 168.327 1.00 57.72  ? 233  TYR B CE2 1 
ATOM   5425  C  CZ  . TYR B 1 258 ? 103.151 102.881 169.657 1.00 63.12  ? 233  TYR B CZ  1 
ATOM   5426  O  OH  . TYR B 1 258 ? 101.987 103.302 170.256 1.00 66.94  ? 233  TYR B OH  1 
ATOM   5427  N  N   . GLY B 1 259 ? 109.050 102.481 165.543 1.00 35.80  ? 234  GLY B N   1 
ATOM   5428  C  CA  . GLY B 1 259 ? 110.217 102.138 164.747 1.00 38.79  ? 234  GLY B CA  1 
ATOM   5429  C  C   . GLY B 1 259 ? 111.453 102.910 165.167 1.00 42.88  ? 234  GLY B C   1 
ATOM   5430  O  O   . GLY B 1 259 ? 112.549 102.348 165.258 1.00 50.77  ? 234  GLY B O   1 
ATOM   5431  N  N   . LEU B 1 260 ? 111.294 104.208 165.433 1.00 40.70  ? 235  LEU B N   1 
ATOM   5432  C  CA  . LEU B 1 260 ? 112.415 105.000 165.925 1.00 41.20  ? 235  LEU B CA  1 
ATOM   5433  C  C   . LEU B 1 260 ? 112.868 104.513 167.294 1.00 43.61  ? 235  LEU B C   1 
ATOM   5434  O  O   . LEU B 1 260 ? 114.067 104.501 167.593 1.00 47.97  ? 235  LEU B O   1 
ATOM   5435  C  CB  . LEU B 1 260 ? 112.033 106.479 165.974 1.00 36.68  ? 235  LEU B CB  1 
ATOM   5436  C  CG  . LEU B 1 260 ? 111.796 107.157 164.624 1.00 37.17  ? 235  LEU B CG  1 
ATOM   5437  C  CD1 . LEU B 1 260 ? 111.359 108.596 164.817 1.00 43.38  ? 235  LEU B CD1 1 
ATOM   5438  C  CD2 . LEU B 1 260 ? 113.044 107.089 163.767 1.00 43.02  ? 235  LEU B CD2 1 
ATOM   5439  N  N   . LEU B 1 261 ? 111.922 104.103 168.141 1.00 39.25  ? 236  LEU B N   1 
ATOM   5440  C  CA  . LEU B 1 261 ? 112.286 103.545 169.439 1.00 40.15  ? 236  LEU B CA  1 
ATOM   5441  C  C   . LEU B 1 261 ? 113.023 102.219 169.284 1.00 44.42  ? 236  LEU B C   1 
ATOM   5442  O  O   . LEU B 1 261 ? 113.954 101.932 170.042 1.00 50.96  ? 236  LEU B O   1 
ATOM   5443  C  CB  . LEU B 1 261 ? 111.040 103.379 170.306 1.00 41.64  ? 236  LEU B CB  1 
ATOM   5444  C  CG  . LEU B 1 261 ? 110.420 104.692 170.789 1.00 43.77  ? 236  LEU B CG  1 
ATOM   5445  C  CD1 . LEU B 1 261 ? 109.071 104.452 171.444 1.00 48.73  ? 236  LEU B CD1 1 
ATOM   5446  C  CD2 . LEU B 1 261 ? 111.360 105.407 171.744 1.00 39.48  ? 236  LEU B CD2 1 
ATOM   5447  N  N   . ASP B 1 262 ? 112.627 101.401 168.306 1.00 49.09  ? 237  ASP B N   1 
ATOM   5448  C  CA  . ASP B 1 262 ? 113.362 100.170 168.025 1.00 50.02  ? 237  ASP B CA  1 
ATOM   5449  C  C   . ASP B 1 262 ? 114.783 100.473 167.567 1.00 52.48  ? 237  ASP B C   1 
ATOM   5450  O  O   . ASP B 1 262 ? 115.738 99.807  167.987 1.00 59.83  ? 237  ASP B O   1 
ATOM   5451  C  CB  . ASP B 1 262 ? 112.629 99.348  166.965 1.00 48.89  ? 237  ASP B CB  1 
ATOM   5452  C  CG  . ASP B 1 262 ? 111.326 98.765  167.475 1.00 57.28  ? 237  ASP B CG  1 
ATOM   5453  O  OD1 . ASP B 1 262 ? 110.911 99.122  168.596 1.00 54.19  ? 237  ASP B OD1 1 
ATOM   5454  O  OD2 . ASP B 1 262 ? 110.714 97.952  166.752 1.00 56.33  ? 237  ASP B OD2 1 
ATOM   5455  N  N   . GLN B 1 263 ? 114.941 101.475 166.700 1.00 37.36  ? 238  GLN B N   1 
ATOM   5456  C  CA  . GLN B 1 263 ? 116.274 101.861 166.246 1.00 30.73  ? 238  GLN B CA  1 
ATOM   5457  C  C   . GLN B 1 263 ? 117.124 102.373 167.403 1.00 33.87  ? 238  GLN B C   1 
ATOM   5458  O  O   . GLN B 1 263 ? 118.319 102.066 167.492 1.00 39.51  ? 238  GLN B O   1 
ATOM   5459  C  CB  . GLN B 1 263 ? 116.166 102.919 165.150 1.00 30.48  ? 238  GLN B CB  1 
ATOM   5460  C  CG  . GLN B 1 263 ? 115.657 102.385 163.828 1.00 36.71  ? 238  GLN B CG  1 
ATOM   5461  C  CD  . GLN B 1 263 ? 115.324 103.489 162.851 1.00 35.45  ? 238  GLN B CD  1 
ATOM   5462  O  OE1 . GLN B 1 263 ? 115.231 104.655 163.227 1.00 38.64  ? 238  GLN B OE1 1 
ATOM   5463  N  NE2 . GLN B 1 263 ? 115.138 103.127 161.589 1.00 33.24  ? 238  GLN B NE2 1 
ATOM   5464  N  N   . ILE B 1 264 ? 116.524 103.156 168.300 1.00 32.00  ? 239  ILE B N   1 
ATOM   5465  C  CA  . ILE B 1 264 ? 117.255 103.666 169.455 1.00 36.33  ? 239  ILE B CA  1 
ATOM   5466  C  C   . ILE B 1 264 ? 117.637 102.526 170.393 1.00 42.26  ? 239  ILE B C   1 
ATOM   5467  O  O   . ILE B 1 264 ? 118.726 102.524 170.979 1.00 43.48  ? 239  ILE B O   1 
ATOM   5468  C  CB  . ILE B 1 264 ? 116.423 104.747 170.168 1.00 37.96  ? 239  ILE B CB  1 
ATOM   5469  C  CG1 . ILE B 1 264 ? 116.381 106.018 169.321 1.00 37.44  ? 239  ILE B CG1 1 
ATOM   5470  C  CG2 . ILE B 1 264 ? 116.993 105.053 171.540 1.00 38.83  ? 239  ILE B CG2 1 
ATOM   5471  C  CD1 . ILE B 1 264 ? 115.383 107.041 169.802 1.00 39.75  ? 239  ILE B CD1 1 
ATOM   5472  N  N   . GLN B 1 265 ? 116.754 101.536 170.548 1.00 44.04  ? 240  GLN B N   1 
ATOM   5473  C  CA  . GLN B 1 265 ? 117.088 100.363 171.349 1.00 38.58  ? 240  GLN B CA  1 
ATOM   5474  C  C   . GLN B 1 265 ? 118.248 99.590  170.735 1.00 41.57  ? 240  GLN B C   1 
ATOM   5475  O  O   . GLN B 1 265 ? 119.129 99.104  171.452 1.00 50.78  ? 240  GLN B O   1 
ATOM   5476  C  CB  . GLN B 1 265 ? 115.862 99.463  171.498 1.00 37.14  ? 240  GLN B CB  1 
ATOM   5477  C  CG  . GLN B 1 265 ? 116.153 98.114  172.133 1.00 42.05  ? 240  GLN B CG  1 
ATOM   5478  C  CD  . GLN B 1 265 ? 116.696 98.235  173.542 1.00 46.92  ? 240  GLN B CD  1 
ATOM   5479  O  OE1 . GLN B 1 265 ? 116.307 99.127  174.295 1.00 48.36  ? 240  GLN B OE1 1 
ATOM   5480  N  NE2 . GLN B 1 265 ? 117.601 97.335  173.906 1.00 45.91  ? 240  GLN B NE2 1 
ATOM   5481  N  N   . ALA B 1 266 ? 118.259 99.458  169.407 1.00 36.61  ? 241  ALA B N   1 
ATOM   5482  C  CA  . ALA B 1 266 ? 119.383 98.806  168.741 1.00 34.79  ? 241  ALA B CA  1 
ATOM   5483  C  C   . ALA B 1 266 ? 120.674 99.587  168.951 1.00 32.58  ? 241  ALA B C   1 
ATOM   5484  O  O   . ALA B 1 266 ? 121.739 98.996  169.165 1.00 42.85  ? 241  ALA B O   1 
ATOM   5485  C  CB  . ALA B 1 266 ? 119.091 98.643  167.252 1.00 36.97  ? 241  ALA B CB  1 
ATOM   5486  N  N   . LEU B 1 267 ? 120.598 100.917 168.888 1.00 33.66  ? 242  LEU B N   1 
ATOM   5487  C  CA  . LEU B 1 267 ? 121.776 101.739 169.147 1.00 33.03  ? 242  LEU B CA  1 
ATOM   5488  C  C   . LEU B 1 267 ? 122.271 101.557 170.576 1.00 36.50  ? 242  LEU B C   1 
ATOM   5489  O  O   . LEU B 1 267 ? 123.480 101.497 170.818 1.00 42.43  ? 242  LEU B O   1 
ATOM   5490  C  CB  . LEU B 1 267 ? 121.467 103.209 168.872 1.00 36.79  ? 242  LEU B CB  1 
ATOM   5491  C  CG  . LEU B 1 267 ? 121.760 103.708 167.457 1.00 35.38  ? 242  LEU B CG  1 
ATOM   5492  C  CD1 . LEU B 1 267 ? 121.165 105.086 167.241 1.00 34.73  ? 242  LEU B CD1 1 
ATOM   5493  C  CD2 . LEU B 1 267 ? 123.256 103.722 167.203 1.00 33.82  ? 242  LEU B CD2 1 
ATOM   5494  N  N   . ARG B 1 268 ? 121.349 101.473 171.538 1.00 41.31  ? 243  ARG B N   1 
ATOM   5495  C  CA  . ARG B 1 268 ? 121.736 101.241 172.927 1.00 45.58  ? 243  ARG B CA  1 
ATOM   5496  C  C   . ARG B 1 268 ? 122.389 99.875  173.099 1.00 41.79  ? 243  ARG B C   1 
ATOM   5497  O  O   . ARG B 1 268 ? 123.383 99.736  173.826 1.00 48.75  ? 243  ARG B O   1 
ATOM   5498  C  CB  . ARG B 1 268 ? 120.514 101.368 173.835 1.00 40.43  ? 243  ARG B CB  1 
ATOM   5499  C  CG  . ARG B 1 268 ? 120.844 101.602 175.295 1.00 42.53  ? 243  ARG B CG  1 
ATOM   5500  C  CD  . ARG B 1 268 ? 119.583 101.649 176.139 1.00 44.46  ? 243  ARG B CD  1 
ATOM   5501  N  NE  . ARG B 1 268 ? 118.464 102.247 175.421 1.00 46.75  ? 243  ARG B NE  1 
ATOM   5502  C  CZ  . ARG B 1 268 ? 118.195 103.545 175.401 1.00 48.77  ? 243  ARG B CZ  1 
ATOM   5503  N  NH1 . ARG B 1 268 ? 118.953 104.417 176.044 1.00 46.99  ? 243  ARG B NH1 1 
ATOM   5504  N  NH2 . ARG B 1 268 ? 117.139 103.978 174.720 1.00 47.52  ? 243  ARG B NH2 1 
ATOM   5505  N  N   . TRP B 1 269 ? 121.833 98.852  172.447 1.00 39.46  ? 244  TRP B N   1 
ATOM   5506  C  CA  . TRP B 1 269 ? 122.427 97.521  172.496 1.00 39.02  ? 244  TRP B CA  1 
ATOM   5507  C  C   . TRP B 1 269 ? 123.834 97.533  171.918 1.00 39.94  ? 244  TRP B C   1 
ATOM   5508  O  O   . TRP B 1 269 ? 124.748 96.916  172.475 1.00 47.11  ? 244  TRP B O   1 
ATOM   5509  C  CB  . TRP B 1 269 ? 121.541 96.527  171.742 1.00 41.85  ? 244  TRP B CB  1 
ATOM   5510  C  CG  . TRP B 1 269 ? 121.947 95.091  171.896 1.00 46.93  ? 244  TRP B CG  1 
ATOM   5511  C  CD1 . TRP B 1 269 ? 121.403 94.175  172.748 1.00 48.98  ? 244  TRP B CD1 1 
ATOM   5512  C  CD2 . TRP B 1 269 ? 122.965 94.398  171.161 1.00 47.14  ? 244  TRP B CD2 1 
ATOM   5513  N  NE1 . TRP B 1 269 ? 122.027 92.961  172.600 1.00 47.69  ? 244  TRP B NE1 1 
ATOM   5514  C  CE2 . TRP B 1 269 ? 122.989 93.071  171.631 1.00 47.85  ? 244  TRP B CE2 1 
ATOM   5515  C  CE3 . TRP B 1 269 ? 123.862 94.773  170.156 1.00 44.38  ? 244  TRP B CE3 1 
ATOM   5516  C  CZ2 . TRP B 1 269 ? 123.872 92.119  171.132 1.00 47.97  ? 244  TRP B CZ2 1 
ATOM   5517  C  CZ3 . TRP B 1 269 ? 124.739 93.826  169.663 1.00 45.56  ? 244  TRP B CZ3 1 
ATOM   5518  C  CH2 . TRP B 1 269 ? 124.737 92.515  170.150 1.00 47.27  ? 244  TRP B CH2 1 
ATOM   5519  N  N   . LEU B 1 270 ? 124.027 98.233  170.798 1.00 42.03  ? 245  LEU B N   1 
ATOM   5520  C  CA  . LEU B 1 270 ? 125.364 98.362  170.229 1.00 39.68  ? 245  LEU B CA  1 
ATOM   5521  C  C   . LEU B 1 270 ? 126.300 99.094  171.181 1.00 46.02  ? 245  LEU B C   1 
ATOM   5522  O  O   . LEU B 1 270 ? 127.455 98.696  171.358 1.00 46.44  ? 245  LEU B O   1 
ATOM   5523  C  CB  . LEU B 1 270 ? 125.293 99.087  168.886 1.00 41.66  ? 245  LEU B CB  1 
ATOM   5524  C  CG  . LEU B 1 270 ? 124.928 98.245  167.665 1.00 39.81  ? 245  LEU B CG  1 
ATOM   5525  C  CD1 . LEU B 1 270 ? 125.316 98.967  166.388 1.00 40.24  ? 245  LEU B CD1 1 
ATOM   5526  C  CD2 . LEU B 1 270 ? 125.602 96.887  167.737 1.00 45.38  ? 245  LEU B CD2 1 
ATOM   5527  N  N   . SER B 1 271 ? 125.815 100.167 171.809 1.00 46.01  ? 246  SER B N   1 
ATOM   5528  C  CA  . SER B 1 271 ? 126.662 100.954 172.698 1.00 44.01  ? 246  SER B CA  1 
ATOM   5529  C  C   . SER B 1 271 ? 127.119 100.138 173.900 1.00 47.18  ? 246  SER B C   1 
ATOM   5530  O  O   . SER B 1 271 ? 128.278 100.232 174.318 1.00 42.14  ? 246  SER B O   1 
ATOM   5531  C  CB  . SER B 1 271 ? 125.917 102.207 173.154 1.00 37.45  ? 246  SER B CB  1 
ATOM   5532  O  OG  . SER B 1 271 ? 126.559 102.809 174.264 1.00 44.14  ? 246  SER B OG  1 
ATOM   5533  N  N   . GLU B 1 272 ? 126.226 99.331  174.470 1.00 53.35  ? 247  GLU B N   1 
ATOM   5534  C  CA  . GLU B 1 272 ? 126.542 98.585  175.681 1.00 49.77  ? 247  GLU B CA  1 
ATOM   5535  C  C   . GLU B 1 272 ? 126.955 97.141  175.421 1.00 53.42  ? 247  GLU B C   1 
ATOM   5536  O  O   . GLU B 1 272 ? 127.159 96.393  176.382 1.00 57.24  ? 247  GLU B O   1 
ATOM   5537  C  CB  . GLU B 1 272 ? 125.351 98.614  176.645 1.00 49.25  ? 247  GLU B CB  1 
ATOM   5538  C  CG  . GLU B 1 272 ? 124.212 97.683  176.271 1.00 52.96  ? 247  GLU B CG  1 
ATOM   5539  C  CD  . GLU B 1 272 ? 122.961 97.943  177.086 1.00 59.24  ? 247  GLU B CD  1 
ATOM   5540  O  OE1 . GLU B 1 272 ? 122.806 99.072  177.595 1.00 60.12  ? 247  GLU B OE1 1 
ATOM   5541  O  OE2 . GLU B 1 272 ? 122.133 97.017  177.219 1.00 57.90  ? 247  GLU B OE2 1 
ATOM   5542  N  N   . ASN B 1 273 ? 127.089 96.724  174.159 1.00 53.55  ? 248  ASN B N   1 
ATOM   5543  C  CA  . ASN B 1 273 ? 127.430 95.337  173.869 1.00 51.15  ? 248  ASN B CA  1 
ATOM   5544  C  C   . ASN B 1 273 ? 128.449 95.145  172.754 1.00 56.48  ? 248  ASN B C   1 
ATOM   5545  O  O   . ASN B 1 273 ? 128.791 93.995  172.461 1.00 58.18  ? 248  ASN B O   1 
ATOM   5546  C  CB  . ASN B 1 273 ? 126.160 94.545  173.521 1.00 53.81  ? 248  ASN B CB  1 
ATOM   5547  C  CG  . ASN B 1 273 ? 125.598 93.795  174.709 1.00 56.50  ? 248  ASN B CG  1 
ATOM   5548  O  OD1 . ASN B 1 273 ? 125.929 92.632  174.935 1.00 63.45  ? 248  ASN B OD1 1 
ATOM   5549  N  ND2 . ASN B 1 273 ? 124.742 94.458  175.476 1.00 55.38  ? 248  ASN B ND2 1 
ATOM   5550  N  N   . ILE B 1 274 ? 128.942 96.211  172.118 1.00 58.03  ? 249  ILE B N   1 
ATOM   5551  C  CA  . ILE B 1 274 ? 129.870 96.039  170.999 1.00 55.36  ? 249  ILE B CA  1 
ATOM   5552  C  C   . ILE B 1 274 ? 131.312 95.870  171.444 1.00 58.83  ? 249  ILE B C   1 
ATOM   5553  O  O   . ILE B 1 274 ? 132.160 95.489  170.627 1.00 60.94  ? 249  ILE B O   1 
ATOM   5554  C  CB  . ILE B 1 274 ? 129.778 97.222  170.016 1.00 55.56  ? 249  ILE B CB  1 
ATOM   5555  C  CG1 . ILE B 1 274 ? 130.192 96.787  168.610 1.00 54.67  ? 249  ILE B CG1 1 
ATOM   5556  C  CG2 . ILE B 1 274 ? 130.628 98.387  170.494 1.00 57.81  ? 249  ILE B CG2 1 
ATOM   5557  C  CD1 . ILE B 1 274 ? 129.529 95.517  168.154 1.00 54.07  ? 249  ILE B CD1 1 
ATOM   5558  N  N   . ALA B 1 275 ? 131.619 96.132  172.716 1.00 63.84  ? 250  ALA B N   1 
ATOM   5559  C  CA  . ALA B 1 275 ? 132.991 95.978  173.186 1.00 63.08  ? 250  ALA B CA  1 
ATOM   5560  C  C   . ALA B 1 275 ? 133.447 94.526  173.126 1.00 65.61  ? 250  ALA B C   1 
ATOM   5561  O  O   . ALA B 1 275 ? 134.645 94.258  172.979 1.00 68.23  ? 250  ALA B O   1 
ATOM   5562  C  CB  . ALA B 1 275 ? 133.122 96.518  174.610 1.00 62.67  ? 250  ALA B CB  1 
ATOM   5563  N  N   . HIS B 1 276 ? 132.513 93.580  173.234 1.00 65.14  ? 251  HIS B N   1 
ATOM   5564  C  CA  . HIS B 1 276 ? 132.873 92.167  173.201 1.00 63.02  ? 251  HIS B CA  1 
ATOM   5565  C  C   . HIS B 1 276 ? 133.218 91.693  171.796 1.00 64.78  ? 251  HIS B C   1 
ATOM   5566  O  O   . HIS B 1 276 ? 134.081 90.823  171.636 1.00 67.58  ? 251  HIS B O   1 
ATOM   5567  C  CB  . HIS B 1 276 ? 131.736 91.323  173.777 1.00 62.28  ? 251  HIS B CB  1 
ATOM   5568  C  CG  . HIS B 1 276 ? 131.203 91.834  175.080 1.00 65.07  ? 251  HIS B CG  1 
ATOM   5569  N  ND1 . HIS B 1 276 ? 129.943 91.522  175.541 1.00 68.06  ? 251  HIS B ND1 1 
ATOM   5570  C  CD2 . HIS B 1 276 ? 131.762 92.628  176.023 1.00 63.46  ? 251  HIS B CD2 1 
ATOM   5571  C  CE1 . HIS B 1 276 ? 129.746 92.107  176.709 1.00 66.78  ? 251  HIS B CE1 1 
ATOM   5572  N  NE2 . HIS B 1 276 ? 130.835 92.785  177.024 1.00 65.63  ? 251  HIS B NE2 1 
ATOM   5573  N  N   . PHE B 1 277 ? 132.565 92.245  170.773 1.00 62.41  ? 252  PHE B N   1 
ATOM   5574  C  CA  . PHE B 1 277 ? 132.856 91.877  169.394 1.00 61.12  ? 252  PHE B CA  1 
ATOM   5575  C  C   . PHE B 1 277 ? 134.098 92.568  168.848 1.00 63.15  ? 252  PHE B C   1 
ATOM   5576  O  O   . PHE B 1 277 ? 134.510 92.265  167.723 1.00 61.78  ? 252  PHE B O   1 
ATOM   5577  C  CB  . PHE B 1 277 ? 131.661 92.196  168.490 1.00 56.14  ? 252  PHE B CB  1 
ATOM   5578  C  CG  . PHE B 1 277 ? 130.437 91.373  168.782 1.00 58.16  ? 252  PHE B CG  1 
ATOM   5579  C  CD1 . PHE B 1 277 ? 129.626 91.665  169.865 1.00 63.44  ? 252  PHE B CD1 1 
ATOM   5580  C  CD2 . PHE B 1 277 ? 130.096 90.309  167.966 1.00 60.73  ? 252  PHE B CD2 1 
ATOM   5581  C  CE1 . PHE B 1 277 ? 128.501 90.910  170.130 1.00 62.50  ? 252  PHE B CE1 1 
ATOM   5582  C  CE2 . PHE B 1 277 ? 128.972 89.551  168.227 1.00 63.95  ? 252  PHE B CE2 1 
ATOM   5583  C  CZ  . PHE B 1 277 ? 128.174 89.852  169.311 1.00 62.84  ? 252  PHE B CZ  1 
ATOM   5584  N  N   . GLY B 1 278 ? 134.697 93.481  169.609 1.00 64.88  ? 253  GLY B N   1 
ATOM   5585  C  CA  . GLY B 1 278 ? 135.868 94.208  169.170 1.00 64.79  ? 253  GLY B CA  1 
ATOM   5586  C  C   . GLY B 1 278 ? 135.608 95.624  168.711 1.00 65.23  ? 253  GLY B C   1 
ATOM   5587  O  O   . GLY B 1 278 ? 136.560 96.318  168.334 1.00 68.25  ? 253  GLY B O   1 
ATOM   5588  N  N   . GLY B 1 279 ? 134.355 96.076  168.730 1.00 65.15  ? 254  GLY B N   1 
ATOM   5589  C  CA  . GLY B 1 279 ? 134.039 97.415  168.286 1.00 67.41  ? 254  GLY B CA  1 
ATOM   5590  C  C   . GLY B 1 279 ? 134.308 98.470  169.342 1.00 69.81  ? 254  GLY B C   1 
ATOM   5591  O  O   . GLY B 1 279 ? 134.520 98.184  170.519 1.00 68.61  ? 254  GLY B O   1 
ATOM   5592  N  N   . ASP B 1 280 ? 134.296 99.725  168.891 1.00 68.12  ? 255  ASP B N   1 
ATOM   5593  C  CA  . ASP B 1 280 ? 134.503 100.865 169.769 1.00 68.68  ? 255  ASP B CA  1 
ATOM   5594  C  C   . ASP B 1 280 ? 133.164 101.510 170.078 1.00 68.22  ? 255  ASP B C   1 
ATOM   5595  O  O   . ASP B 1 280 ? 132.500 101.999 169.151 1.00 69.92  ? 255  ASP B O   1 
ATOM   5596  C  CB  . ASP B 1 280 ? 135.439 101.878 169.118 1.00 69.25  ? 255  ASP B CB  1 
ATOM   5597  C  CG  . ASP B 1 280 ? 136.171 102.737 170.133 1.00 72.97  ? 255  ASP B CG  1 
ATOM   5598  O  OD1 . ASP B 1 280 ? 135.655 102.912 171.256 1.00 70.90  ? 255  ASP B OD1 1 
ATOM   5599  O  OD2 . ASP B 1 280 ? 137.266 103.240 169.807 1.00 73.29  ? 255  ASP B OD2 1 
ATOM   5600  N  N   . PRO B 1 281 ? 132.724 101.542 171.336 1.00 69.13  ? 256  PRO B N   1 
ATOM   5601  C  CA  . PRO B 1 281 ? 131.438 102.167 171.666 1.00 68.71  ? 256  PRO B CA  1 
ATOM   5602  C  C   . PRO B 1 281 ? 131.461 103.687 171.687 1.00 69.70  ? 256  PRO B C   1 
ATOM   5603  O  O   . PRO B 1 281 ? 130.506 104.292 172.182 1.00 71.20  ? 256  PRO B O   1 
ATOM   5604  C  CB  . PRO B 1 281 ? 131.136 101.611 173.066 1.00 68.30  ? 256  PRO B CB  1 
ATOM   5605  C  CG  . PRO B 1 281 ? 132.456 101.267 173.647 1.00 69.80  ? 256  PRO B CG  1 
ATOM   5606  C  CD  . PRO B 1 281 ? 133.424 101.024 172.524 1.00 70.86  ? 256  PRO B CD  1 
ATOM   5607  N  N   . GLU B 1 282 ? 132.514 104.318 171.169 1.00 67.23  ? 257  GLU B N   1 
ATOM   5608  C  CA  . GLU B 1 282 ? 132.616 105.772 171.135 1.00 65.70  ? 257  GLU B CA  1 
ATOM   5609  C  C   . GLU B 1 282 ? 132.752 106.310 169.716 1.00 65.11  ? 257  GLU B C   1 
ATOM   5610  O  O   . GLU B 1 282 ? 132.947 107.518 169.539 1.00 64.14  ? 257  GLU B O   1 
ATOM   5611  C  CB  . GLU B 1 282 ? 133.800 106.238 171.990 1.00 65.26  ? 257  GLU B CB  1 
ATOM   5612  C  CG  . GLU B 1 282 ? 133.598 107.585 172.666 1.00 66.49  ? 257  GLU B CG  1 
ATOM   5613  C  CD  . GLU B 1 282 ? 132.698 107.501 173.884 1.00 67.88  ? 257  GLU B CD  1 
ATOM   5614  O  OE1 . GLU B 1 282 ? 132.384 106.373 174.317 1.00 69.43  ? 257  GLU B OE1 1 
ATOM   5615  O  OE2 . GLU B 1 282 ? 132.306 108.564 174.409 1.00 65.70  ? 257  GLU B OE2 1 
ATOM   5616  N  N   . ARG B 1 283 ? 132.661 105.450 168.704 1.00 57.95  ? 258  ARG B N   1 
ATOM   5617  C  CA  . ARG B 1 283 ? 132.799 105.835 167.301 1.00 57.79  ? 258  ARG B CA  1 
ATOM   5618  C  C   . ARG B 1 283 ? 131.693 105.200 166.468 1.00 59.24  ? 258  ARG B C   1 
ATOM   5619  O  O   . ARG B 1 283 ? 131.930 104.636 165.398 1.00 63.24  ? 258  ARG B O   1 
ATOM   5620  C  CB  . ARG B 1 283 ? 134.171 105.440 166.761 1.00 55.25  ? 258  ARG B CB  1 
ATOM   5621  C  CG  . ARG B 1 283 ? 135.342 106.026 167.532 1.00 57.94  ? 258  ARG B CG  1 
ATOM   5622  C  CD  . ARG B 1 283 ? 136.577 106.150 166.655 1.00 56.26  ? 258  ARG B CD  1 
ATOM   5623  N  NE  . ARG B 1 283 ? 137.291 104.884 166.541 1.00 56.78  ? 258  ARG B NE  1 
ATOM   5624  C  CZ  . ARG B 1 283 ? 138.470 104.739 165.954 1.00 56.76  ? 258  ARG B CZ  1 
ATOM   5625  N  NH1 . ARG B 1 283 ? 139.103 105.767 165.413 1.00 56.97  ? 258  ARG B NH1 1 
ATOM   5626  N  NH2 . ARG B 1 283 ? 139.029 103.534 165.908 1.00 58.78  ? 258  ARG B NH2 1 
ATOM   5627  N  N   . ILE B 1 284 ? 130.457 105.289 166.954 1.00 50.16  ? 259  ILE B N   1 
ATOM   5628  C  CA  . ILE B 1 284 ? 129.319 104.627 166.324 1.00 42.22  ? 259  ILE B CA  1 
ATOM   5629  C  C   . ILE B 1 284 ? 128.690 105.609 165.340 1.00 38.84  ? 259  ILE B C   1 
ATOM   5630  O  O   . ILE B 1 284 ? 127.954 106.515 165.731 1.00 47.48  ? 259  ILE B O   1 
ATOM   5631  C  CB  . ILE B 1 284 ? 128.305 104.140 167.359 1.00 42.90  ? 259  ILE B CB  1 
ATOM   5632  C  CG1 . ILE B 1 284 ? 128.980 103.215 168.372 1.00 45.51  ? 259  ILE B CG1 1 
ATOM   5633  C  CG2 . ILE B 1 284 ? 127.147 103.431 166.677 1.00 40.03  ? 259  ILE B CG2 1 
ATOM   5634  C  CD1 . ILE B 1 284 ? 128.036 102.661 169.413 1.00 46.04  ? 259  ILE B CD1 1 
ATOM   5635  N  N   . THR B 1 285 ? 128.983 105.428 164.057 1.00 32.50  ? 260  THR B N   1 
ATOM   5636  C  CA  . THR B 1 285 ? 128.316 106.181 163.007 1.00 34.22  ? 260  THR B CA  1 
ATOM   5637  C  C   . THR B 1 285 ? 127.000 105.505 162.644 1.00 42.02  ? 260  THR B C   1 
ATOM   5638  O  O   . THR B 1 285 ? 126.857 104.287 162.760 1.00 61.42  ? 260  THR B O   1 
ATOM   5639  C  CB  . THR B 1 285 ? 129.210 106.278 161.770 1.00 36.70  ? 260  THR B CB  1 
ATOM   5640  O  OG1 . THR B 1 285 ? 130.535 106.649 162.167 1.00 51.71  ? 260  THR B OG1 1 
ATOM   5641  C  CG2 . THR B 1 285 ? 128.679 107.310 160.793 1.00 43.11  ? 260  THR B CG2 1 
ATOM   5642  N  N   . ILE B 1 286 ? 126.028 106.307 162.216 1.00 38.19  ? 261  ILE B N   1 
ATOM   5643  C  CA  . ILE B 1 286 ? 124.768 105.799 161.686 1.00 34.27  ? 261  ILE B CA  1 
ATOM   5644  C  C   . ILE B 1 286 ? 124.541 106.430 160.322 1.00 38.64  ? 261  ILE B C   1 
ATOM   5645  O  O   . ILE B 1 286 ? 124.661 107.650 160.170 1.00 60.28  ? 261  ILE B O   1 
ATOM   5646  C  CB  . ILE B 1 286 ? 123.579 106.083 162.624 1.00 36.74  ? 261  ILE B CB  1 
ATOM   5647  C  CG1 . ILE B 1 286 ? 123.533 107.556 163.026 1.00 41.47  ? 261  ILE B CG1 1 
ATOM   5648  C  CG2 . ILE B 1 286 ? 123.655 105.205 163.857 1.00 50.73  ? 261  ILE B CG2 1 
ATOM   5649  C  CD1 . ILE B 1 286 ? 122.258 107.946 163.733 1.00 45.87  ? 261  ILE B CD1 1 
ATOM   5650  N  N   . PHE B 1 287 ? 124.229 105.602 159.328 1.00 41.55  ? 262  PHE B N   1 
ATOM   5651  C  CA  . PHE B 1 287 ? 124.019 106.095 157.977 1.00 46.56  ? 262  PHE B CA  1 
ATOM   5652  C  C   . PHE B 1 287 ? 122.871 105.338 157.331 1.00 47.74  ? 262  PHE B C   1 
ATOM   5653  O  O   . PHE B 1 287 ? 122.537 104.218 157.723 1.00 64.14  ? 262  PHE B O   1 
ATOM   5654  C  CB  . PHE B 1 287 ? 125.292 105.984 157.123 1.00 52.08  ? 262  PHE B CB  1 
ATOM   5655  C  CG  . PHE B 1 287 ? 125.637 104.585 156.700 1.00 51.54  ? 262  PHE B CG  1 
ATOM   5656  C  CD1 . PHE B 1 287 ? 125.956 103.619 157.634 1.00 55.19  ? 262  PHE B CD1 1 
ATOM   5657  C  CD2 . PHE B 1 287 ? 125.672 104.248 155.358 1.00 52.47  ? 262  PHE B CD2 1 
ATOM   5658  C  CE1 . PHE B 1 287 ? 126.281 102.338 157.242 1.00 52.76  ? 262  PHE B CE1 1 
ATOM   5659  C  CE2 . PHE B 1 287 ? 126.001 102.970 154.960 1.00 51.09  ? 262  PHE B CE2 1 
ATOM   5660  C  CZ  . PHE B 1 287 ? 126.305 102.013 155.904 1.00 51.45  ? 262  PHE B CZ  1 
ATOM   5661  N  N   . GLY B 1 288 ? 122.261 105.972 156.338 1.00 20.38  ? 263  GLY B N   1 
ATOM   5662  C  CA  . GLY B 1 288 ? 121.144 105.369 155.640 1.00 27.65  ? 263  GLY B CA  1 
ATOM   5663  C  C   . GLY B 1 288 ? 120.738 106.211 154.456 1.00 25.13  ? 263  GLY B C   1 
ATOM   5664  O  O   . GLY B 1 288 ? 121.096 107.389 154.355 1.00 35.44  ? 263  GLY B O   1 
ATOM   5665  N  N   . SER B 1 289 ? 119.984 105.588 153.556 1.00 21.53  ? 264  SER B N   1 
ATOM   5666  C  CA  . SER B 1 289 ? 119.507 106.239 152.347 1.00 21.12  ? 264  SER B CA  1 
ATOM   5667  C  C   . SER B 1 289 ? 117.986 106.275 152.342 1.00 29.87  ? 264  SER B C   1 
ATOM   5668  O  O   . SER B 1 289 ? 117.322 105.509 153.045 1.00 38.13  ? 264  SER B O   1 
ATOM   5669  C  CB  . SER B 1 289 ? 120.017 105.522 151.090 1.00 28.50  ? 264  SER B CB  1 
ATOM   5670  O  OG  . SER B 1 289 ? 119.259 105.892 149.952 1.00 31.59  ? 264  SER B OG  1 
ATOM   5671  N  N   . GLY B 1 290 ? 117.440 107.177 151.531 1.00 24.91  ? 265  GLY B N   1 
ATOM   5672  C  CA  . GLY B 1 290 ? 116.002 107.307 151.426 1.00 22.62  ? 265  GLY B CA  1 
ATOM   5673  C  C   . GLY B 1 290 ? 115.381 107.778 152.727 1.00 22.14  ? 265  GLY B C   1 
ATOM   5674  O  O   . GLY B 1 290 ? 115.985 108.520 153.508 1.00 27.49  ? 265  GLY B O   1 
ATOM   5675  N  N   . ALA B 1 291 ? 114.146 107.328 152.966 1.00 20.98  ? 266  ALA B N   1 
ATOM   5676  C  CA  . ALA B 1 291 ? 113.434 107.728 154.176 1.00 25.06  ? 266  ALA B CA  1 
ATOM   5677  C  C   . ALA B 1 291 ? 114.152 107.259 155.432 1.00 28.03  ? 266  ALA B C   1 
ATOM   5678  O  O   . ALA B 1 291 ? 114.001 107.871 156.495 1.00 30.59  ? 266  ALA B O   1 
ATOM   5679  C  CB  . ALA B 1 291 ? 112.004 107.191 154.153 1.00 26.72  ? 266  ALA B CB  1 
ATOM   5680  N  N   . GLY B 1 292 ? 114.934 106.183 155.333 1.00 17.86  ? 267  GLY B N   1 
ATOM   5681  C  CA  . GLY B 1 292 ? 115.756 105.778 156.460 1.00 10.92  ? 267  GLY B CA  1 
ATOM   5682  C  C   . GLY B 1 292 ? 116.703 106.876 156.899 1.00 25.92  ? 267  GLY B C   1 
ATOM   5683  O  O   . GLY B 1 292 ? 116.895 107.101 158.097 1.00 27.29  ? 267  GLY B O   1 
ATOM   5684  N  N   . ALA B 1 293 ? 117.292 107.588 155.933 1.00 26.21  ? 268  ALA B N   1 
ATOM   5685  C  CA  . ALA B 1 293 ? 118.126 108.739 156.263 1.00 16.90  ? 268  ALA B CA  1 
ATOM   5686  C  C   . ALA B 1 293 ? 117.339 109.771 157.056 1.00 20.76  ? 268  ALA B C   1 
ATOM   5687  O  O   . ALA B 1 293 ? 117.885 110.417 157.959 1.00 33.87  ? 268  ALA B O   1 
ATOM   5688  C  CB  . ALA B 1 293 ? 118.691 109.364 154.990 1.00 23.54  ? 268  ALA B CB  1 
ATOM   5689  N  N   . SER B 1 294 ? 116.051 109.927 156.743 1.00 18.84  ? 269  SER B N   1 
ATOM   5690  C  CA  . SER B 1 294 ? 115.201 110.811 157.532 1.00 15.91  ? 269  SER B CA  1 
ATOM   5691  C  C   . SER B 1 294 ? 115.224 110.405 158.997 1.00 26.09  ? 269  SER B C   1 
ATOM   5692  O  O   . SER B 1 294 ? 115.384 111.252 159.886 1.00 31.72  ? 269  SER B O   1 
ATOM   5693  C  CB  . SER B 1 294 ? 113.773 110.789 156.989 1.00 13.01  ? 269  SER B CB  1 
ATOM   5694  O  OG  . SER B 1 294 ? 113.690 111.460 155.745 1.00 28.66  ? 269  SER B OG  1 
ATOM   5695  N  N   . CYS B 1 295 ? 115.105 109.101 159.264 1.00 23.66  ? 270  CYS B N   1 
ATOM   5696  C  CA  . CYS B 1 295 ? 115.217 108.609 160.632 1.00 16.48  ? 270  CYS B CA  1 
ATOM   5697  C  C   . CYS B 1 295 ? 116.509 109.089 161.274 1.00 22.17  ? 270  CYS B C   1 
ATOM   5698  O  O   . CYS B 1 295 ? 116.506 109.555 162.420 1.00 30.35  ? 270  CYS B O   1 
ATOM   5699  C  CB  . CYS B 1 295 ? 115.144 107.082 160.651 1.00 10.22  ? 270  CYS B CB  1 
ATOM   5700  S  SG  . CYS B 1 295 ? 113.550 106.403 160.148 1.00 33.23  ? 270  CYS B SG  1 
ATOM   5701  N  N   . VAL B 1 296 ? 117.616 109.032 160.527 1.00 22.61  ? 271  VAL B N   1 
ATOM   5702  C  CA  . VAL B 1 296 ? 118.892 109.515 161.047 1.00 19.76  ? 271  VAL B CA  1 
ATOM   5703  C  C   . VAL B 1 296 ? 118.755 110.958 161.509 1.00 30.26  ? 271  VAL B C   1 
ATOM   5704  O  O   . VAL B 1 296 ? 119.128 111.307 162.636 1.00 37.21  ? 271  VAL B O   1 
ATOM   5705  C  CB  . VAL B 1 296 ? 119.996 109.366 159.986 1.00 9.21   ? 271  VAL B CB  1 
ATOM   5706  C  CG1 . VAL B 1 296 ? 121.184 110.240 160.332 1.00 6.92   ? 271  VAL B CG1 1 
ATOM   5707  C  CG2 . VAL B 1 296 ? 120.418 107.917 159.863 1.00 28.60  ? 271  VAL B CG2 1 
ATOM   5708  N  N   . ASN B 1 297 ? 118.171 111.809 160.662 1.00 26.27  ? 272  ASN B N   1 
ATOM   5709  C  CA  . ASN B 1 297 ? 117.935 113.187 161.071 1.00 20.59  ? 272  ASN B CA  1 
ATOM   5710  C  C   . ASN B 1 297 ? 116.989 113.239 162.262 1.00 25.00  ? 272  ASN B C   1 
ATOM   5711  O  O   . ASN B 1 297 ? 117.238 113.965 163.232 1.00 36.28  ? 272  ASN B O   1 
ATOM   5712  C  CB  . ASN B 1 297 ? 117.383 113.997 159.900 1.00 19.61  ? 272  ASN B CB  1 
ATOM   5713  C  CG  . ASN B 1 297 ? 118.477 114.603 159.048 1.00 30.30  ? 272  ASN B CG  1 
ATOM   5714  O  OD1 . ASN B 1 297 ? 118.620 115.822 158.977 1.00 34.78  ? 272  ASN B OD1 1 
ATOM   5715  N  ND2 . ASN B 1 297 ? 119.259 113.752 158.396 1.00 22.03  ? 272  ASN B ND2 1 
ATOM   5716  N  N   . LEU B 1 298 ? 115.923 112.439 162.228 1.00 21.27  ? 273  LEU B N   1 
ATOM   5717  C  CA  . LEU B 1 298 ? 115.013 112.373 163.361 1.00 24.62  ? 273  LEU B CA  1 
ATOM   5718  C  C   . LEU B 1 298 ? 115.657 111.730 164.579 1.00 27.93  ? 273  LEU B C   1 
ATOM   5719  O  O   . LEU B 1 298 ? 115.111 111.845 165.680 1.00 31.67  ? 273  LEU B O   1 
ATOM   5720  C  CB  . LEU B 1 298 ? 113.743 111.618 162.971 1.00 23.60  ? 273  LEU B CB  1 
ATOM   5721  C  CG  . LEU B 1 298 ? 112.908 112.282 161.875 1.00 15.27  ? 273  LEU B CG  1 
ATOM   5722  C  CD1 . LEU B 1 298 ? 112.122 111.250 161.090 1.00 18.69  ? 273  LEU B CD1 1 
ATOM   5723  C  CD2 . LEU B 1 298 ? 111.977 113.318 162.472 1.00 27.51  ? 273  LEU B CD2 1 
ATOM   5724  N  N   . LEU B 1 299 ? 116.797 111.061 164.410 1.00 27.17  ? 274  LEU B N   1 
ATOM   5725  C  CA  . LEU B 1 299 ? 117.551 110.542 165.539 1.00 25.41  ? 274  LEU B CA  1 
ATOM   5726  C  C   . LEU B 1 299 ? 118.548 111.551 166.089 1.00 29.22  ? 274  LEU B C   1 
ATOM   5727  O  O   . LEU B 1 299 ? 119.172 111.283 167.120 1.00 36.67  ? 274  LEU B O   1 
ATOM   5728  C  CB  . LEU B 1 299 ? 118.288 109.258 165.144 1.00 22.17  ? 274  LEU B CB  1 
ATOM   5729  C  CG  . LEU B 1 299 ? 117.451 107.978 165.104 1.00 18.68  ? 274  LEU B CG  1 
ATOM   5730  C  CD1 . LEU B 1 299 ? 118.342 106.752 165.169 1.00 26.22  ? 274  LEU B CD1 1 
ATOM   5731  C  CD2 . LEU B 1 299 ? 116.432 107.964 166.228 1.00 26.42  ? 274  LEU B CD2 1 
ATOM   5732  N  N   . ILE B 1 300 ? 118.713 112.695 165.429 1.00 28.01  ? 275  ILE B N   1 
ATOM   5733  C  CA  . ILE B 1 300 ? 119.624 113.725 165.917 1.00 30.36  ? 275  ILE B CA  1 
ATOM   5734  C  C   . ILE B 1 300 ? 118.906 114.712 166.827 1.00 33.73  ? 275  ILE B C   1 
ATOM   5735  O  O   . ILE B 1 300 ? 119.441 115.112 167.864 1.00 42.40  ? 275  ILE B O   1 
ATOM   5736  C  CB  . ILE B 1 300 ? 120.296 114.435 164.724 1.00 28.48  ? 275  ILE B CB  1 
ATOM   5737  C  CG1 . ILE B 1 300 ? 121.357 113.528 164.102 1.00 33.44  ? 275  ILE B CG1 1 
ATOM   5738  C  CG2 . ILE B 1 300 ? 120.912 115.751 165.156 1.00 28.97  ? 275  ILE B CG2 1 
ATOM   5739  C  CD1 . ILE B 1 300 ? 122.169 114.192 163.024 1.00 22.29  ? 275  ILE B CD1 1 
ATOM   5740  N  N   . LEU B 1 301 ? 117.684 115.101 166.469 1.00 37.62  ? 276  LEU B N   1 
ATOM   5741  C  CA  . LEU B 1 301 ? 116.913 116.044 167.267 1.00 41.32  ? 276  LEU B CA  1 
ATOM   5742  C  C   . LEU B 1 301 ? 116.248 115.395 168.473 1.00 46.80  ? 276  LEU B C   1 
ATOM   5743  O  O   . LEU B 1 301 ? 115.648 116.108 169.285 1.00 53.12  ? 276  LEU B O   1 
ATOM   5744  C  CB  . LEU B 1 301 ? 115.851 116.720 166.396 1.00 36.98  ? 276  LEU B CB  1 
ATOM   5745  C  CG  . LEU B 1 301 ? 116.188 116.886 164.913 1.00 37.65  ? 276  LEU B CG  1 
ATOM   5746  C  CD1 . LEU B 1 301 ? 114.969 117.346 164.138 1.00 38.99  ? 276  LEU B CD1 1 
ATOM   5747  C  CD2 . LEU B 1 301 ? 117.337 117.860 164.724 1.00 35.84  ? 276  LEU B CD2 1 
ATOM   5748  N  N   . SER B 1 302 ? 116.340 114.076 168.611 1.00 47.40  ? 277  SER B N   1 
ATOM   5749  C  CA  . SER B 1 302 ? 115.721 113.363 169.720 1.00 45.94  ? 277  SER B CA  1 
ATOM   5750  C  C   . SER B 1 302 ? 116.693 113.269 170.887 1.00 50.00  ? 277  SER B C   1 
ATOM   5751  O  O   . SER B 1 302 ? 117.861 112.913 170.703 1.00 52.34  ? 277  SER B O   1 
ATOM   5752  C  CB  . SER B 1 302 ? 115.291 111.963 169.283 1.00 50.96  ? 277  SER B CB  1 
ATOM   5753  O  OG  . SER B 1 302 ? 114.132 112.018 168.471 1.00 51.50  ? 277  SER B OG  1 
ATOM   5754  N  N   . HIS B 1 303 ? 116.207 113.587 172.087 1.00 66.40  ? 278  HIS B N   1 
ATOM   5755  C  CA  . HIS B 1 303 ? 117.030 113.486 173.285 1.00 68.68  ? 278  HIS B CA  1 
ATOM   5756  C  C   . HIS B 1 303 ? 117.178 112.055 173.782 1.00 70.89  ? 278  HIS B C   1 
ATOM   5757  O  O   . HIS B 1 303 ? 117.985 111.814 174.686 1.00 74.48  ? 278  HIS B O   1 
ATOM   5758  C  CB  . HIS B 1 303 ? 116.453 114.358 174.405 1.00 68.67  ? 278  HIS B CB  1 
ATOM   5759  C  CG  . HIS B 1 303 ? 114.966 114.264 174.545 1.00 71.27  ? 278  HIS B CG  1 
ATOM   5760  N  ND1 . HIS B 1 303 ? 114.094 114.859 173.659 1.00 70.89  ? 278  HIS B ND1 1 
ATOM   5761  C  CD2 . HIS B 1 303 ? 114.196 113.649 175.474 1.00 71.63  ? 278  HIS B CD2 1 
ATOM   5762  C  CE1 . HIS B 1 303 ? 112.852 114.612 174.034 1.00 71.00  ? 278  HIS B CE1 1 
ATOM   5763  N  NE2 . HIS B 1 303 ? 112.886 113.880 175.132 1.00 73.12  ? 278  HIS B NE2 1 
ATOM   5764  N  N   . HIS B 1 304 ? 116.418 111.109 173.225 1.00 68.28  ? 279  HIS B N   1 
ATOM   5765  C  CA  . HIS B 1 304 ? 116.581 109.710 173.607 1.00 65.38  ? 279  HIS B CA  1 
ATOM   5766  C  C   . HIS B 1 304 ? 117.965 109.198 173.235 1.00 66.64  ? 279  HIS B C   1 
ATOM   5767  O  O   . HIS B 1 304 ? 118.612 108.501 174.025 1.00 67.44  ? 279  HIS B O   1 
ATOM   5768  C  CB  . HIS B 1 304 ? 115.500 108.857 172.944 1.00 64.36  ? 279  HIS B CB  1 
ATOM   5769  C  CG  . HIS B 1 304 ? 114.136 109.040 173.532 1.00 64.65  ? 279  HIS B CG  1 
ATOM   5770  N  ND1 . HIS B 1 304 ? 113.366 107.984 173.967 1.00 69.57  ? 279  HIS B ND1 1 
ATOM   5771  C  CD2 . HIS B 1 304 ? 113.404 110.157 173.755 1.00 67.00  ? 279  HIS B CD2 1 
ATOM   5772  C  CE1 . HIS B 1 304 ? 112.218 108.442 174.434 1.00 68.75  ? 279  HIS B CE1 1 
ATOM   5773  N  NE2 . HIS B 1 304 ? 112.216 109.757 174.316 1.00 67.70  ? 279  HIS B NE2 1 
ATOM   5774  N  N   . SER B 1 305 ? 118.435 109.534 172.036 1.00 60.86  ? 280  SER B N   1 
ATOM   5775  C  CA  . SER B 1 305 ? 119.754 109.115 171.568 1.00 59.55  ? 280  SER B CA  1 
ATOM   5776  C  C   . SER B 1 305 ? 120.762 110.238 171.804 1.00 55.68  ? 280  SER B C   1 
ATOM   5777  O  O   . SER B 1 305 ? 121.230 110.910 170.885 1.00 56.02  ? 280  SER B O   1 
ATOM   5778  C  CB  . SER B 1 305 ? 119.689 108.717 170.097 1.00 57.99  ? 280  SER B CB  1 
ATOM   5779  O  OG  . SER B 1 305 ? 119.715 109.863 169.265 1.00 54.80  ? 280  SER B OG  1 
ATOM   5780  N  N   . GLU B 1 306 ? 121.092 110.432 173.081 1.00 62.44  ? 281  GLU B N   1 
ATOM   5781  C  CA  . GLU B 1 306 ? 122.002 111.509 173.456 1.00 66.32  ? 281  GLU B CA  1 
ATOM   5782  C  C   . GLU B 1 306 ? 123.457 111.106 173.243 1.00 69.80  ? 281  GLU B C   1 
ATOM   5783  O  O   . GLU B 1 306 ? 124.167 111.706 172.429 1.00 70.25  ? 281  GLU B O   1 
ATOM   5784  C  CB  . GLU B 1 306 ? 121.760 111.910 174.913 1.00 68.32  ? 281  GLU B CB  1 
ATOM   5785  C  CG  . GLU B 1 306 ? 122.626 113.060 175.391 1.00 68.91  ? 281  GLU B CG  1 
ATOM   5786  C  CD  . GLU B 1 306 ? 122.008 113.807 176.555 1.00 71.09  ? 281  GLU B CD  1 
ATOM   5787  O  OE1 . GLU B 1 306 ? 120.816 113.572 176.847 1.00 72.24  ? 281  GLU B OE1 1 
ATOM   5788  O  OE2 . GLU B 1 306 ? 122.713 114.628 177.179 1.00 70.33  ? 281  GLU B OE2 1 
ATOM   5789  N  N   . GLY B 1 307 ? 123.916 110.086 173.966 1.00 62.73  ? 282  GLY B N   1 
ATOM   5790  C  CA  . GLY B 1 307 ? 125.277 109.605 173.848 1.00 59.51  ? 282  GLY B CA  1 
ATOM   5791  C  C   . GLY B 1 307 ? 125.446 108.289 173.127 1.00 59.17  ? 282  GLY B C   1 
ATOM   5792  O  O   . GLY B 1 307 ? 126.530 107.695 173.204 1.00 61.65  ? 282  GLY B O   1 
ATOM   5793  N  N   . LEU B 1 308 ? 124.420 107.801 172.426 1.00 40.58  ? 283  LEU B N   1 
ATOM   5794  C  CA  . LEU B 1 308 ? 124.510 106.485 171.803 1.00 40.24  ? 283  LEU B CA  1 
ATOM   5795  C  C   . LEU B 1 308 ? 125.443 106.497 170.598 1.00 43.73  ? 283  LEU B C   1 
ATOM   5796  O  O   . LEU B 1 308 ? 126.271 105.593 170.441 1.00 51.94  ? 283  LEU B O   1 
ATOM   5797  C  CB  . LEU B 1 308 ? 123.118 106.001 171.402 1.00 42.72  ? 283  LEU B CB  1 
ATOM   5798  C  CG  . LEU B 1 308 ? 122.060 106.019 172.506 1.00 45.10  ? 283  LEU B CG  1 
ATOM   5799  C  CD1 . LEU B 1 308 ? 120.777 105.361 172.031 1.00 43.46  ? 283  LEU B CD1 1 
ATOM   5800  C  CD2 . LEU B 1 308 ? 122.579 105.338 173.760 1.00 45.78  ? 283  LEU B CD2 1 
ATOM   5801  N  N   . PHE B 1 309 ? 125.332 107.509 169.742 1.00 39.26  ? 284  PHE B N   1 
ATOM   5802  C  CA  . PHE B 1 309 ? 126.138 107.600 168.533 1.00 41.29  ? 284  PHE B CA  1 
ATOM   5803  C  C   . PHE B 1 309 ? 126.845 108.948 168.490 1.00 43.46  ? 284  PHE B C   1 
ATOM   5804  O  O   . PHE B 1 309 ? 126.535 109.864 169.256 1.00 50.75  ? 284  PHE B O   1 
ATOM   5805  C  CB  . PHE B 1 309 ? 125.288 107.396 167.271 1.00 40.97  ? 284  PHE B CB  1 
ATOM   5806  C  CG  . PHE B 1 309 ? 124.297 108.493 167.018 1.00 39.38  ? 284  PHE B CG  1 
ATOM   5807  C  CD1 . PHE B 1 309 ? 123.123 108.567 167.743 1.00 43.76  ? 284  PHE B CD1 1 
ATOM   5808  C  CD2 . PHE B 1 309 ? 124.539 109.449 166.049 1.00 39.89  ? 284  PHE B CD2 1 
ATOM   5809  C  CE1 . PHE B 1 309 ? 122.212 109.574 167.508 1.00 44.49  ? 284  PHE B CE1 1 
ATOM   5810  C  CE2 . PHE B 1 309 ? 123.631 110.458 165.810 1.00 39.45  ? 284  PHE B CE2 1 
ATOM   5811  C  CZ  . PHE B 1 309 ? 122.466 110.520 166.540 1.00 39.20  ? 284  PHE B CZ  1 
ATOM   5812  N  N   . GLN B 1 310 ? 127.812 109.058 167.583 1.00 41.18  ? 285  GLN B N   1 
ATOM   5813  C  CA  . GLN B 1 310 ? 128.651 110.246 167.477 1.00 41.70  ? 285  GLN B CA  1 
ATOM   5814  C  C   . GLN B 1 310 ? 128.532 110.963 166.143 1.00 42.20  ? 285  GLN B C   1 
ATOM   5815  O  O   . GLN B 1 310 ? 128.541 112.195 166.113 1.00 49.28  ? 285  GLN B O   1 
ATOM   5816  C  CB  . GLN B 1 310 ? 130.123 109.877 167.715 1.00 43.83  ? 285  GLN B CB  1 
ATOM   5817  C  CG  . GLN B 1 310 ? 130.523 109.826 169.179 1.00 45.33  ? 285  GLN B CG  1 
ATOM   5818  C  CD  . GLN B 1 310 ? 130.095 108.543 169.862 1.00 51.69  ? 285  GLN B CD  1 
ATOM   5819  O  OE1 . GLN B 1 310 ? 129.442 107.692 169.261 1.00 50.82  ? 285  GLN B OE1 1 
ATOM   5820  N  NE2 . GLN B 1 310 ? 130.460 108.400 171.130 1.00 52.70  ? 285  GLN B NE2 1 
ATOM   5821  N  N   . LYS B 1 311 ? 128.425 110.234 165.039 1.00 35.30  ? 286  LYS B N   1 
ATOM   5822  C  CA  . LYS B 1 311 ? 128.393 110.816 163.705 1.00 36.63  ? 286  LYS B CA  1 
ATOM   5823  C  C   . LYS B 1 311 ? 127.105 110.414 162.995 1.00 40.69  ? 286  LYS B C   1 
ATOM   5824  O  O   . LYS B 1 311 ? 126.290 109.656 163.521 1.00 49.58  ? 286  LYS B O   1 
ATOM   5825  C  CB  . LYS B 1 311 ? 129.618 110.384 162.896 1.00 38.95  ? 286  LYS B CB  1 
ATOM   5826  C  CG  . LYS B 1 311 ? 130.929 110.537 163.641 1.00 42.14  ? 286  LYS B CG  1 
ATOM   5827  C  CD  . LYS B 1 311 ? 131.987 109.608 163.084 1.00 44.25  ? 286  LYS B CD  1 
ATOM   5828  C  CE  . LYS B 1 311 ? 133.256 109.677 163.907 1.00 43.23  ? 286  LYS B CE  1 
ATOM   5829  N  NZ  . LYS B 1 311 ? 133.693 111.082 164.117 1.00 43.69  ? 286  LYS B NZ  1 
ATOM   5830  N  N   . ALA B 1 312 ? 126.931 110.932 161.781 1.00 40.04  ? 287  ALA B N   1 
ATOM   5831  C  CA  . ALA B 1 312 ? 125.735 110.650 160.997 1.00 33.63  ? 287  ALA B CA  1 
ATOM   5832  C  C   . ALA B 1 312 ? 126.025 110.940 159.534 1.00 34.35  ? 287  ALA B C   1 
ATOM   5833  O  O   . ALA B 1 312 ? 126.562 112.002 159.209 1.00 55.43  ? 287  ALA B O   1 
ATOM   5834  C  CB  . ALA B 1 312 ? 124.548 111.485 161.482 1.00 46.33  ? 287  ALA B CB  1 
ATOM   5835  N  N   . ILE B 1 313 ? 125.669 110.002 158.662 1.00 39.29  ? 288  ILE B N   1 
ATOM   5836  C  CA  . ILE B 1 313 ? 125.846 110.145 157.221 1.00 45.54  ? 288  ILE B CA  1 
ATOM   5837  C  C   . ILE B 1 313 ? 124.464 110.019 156.597 1.00 50.29  ? 288  ILE B C   1 
ATOM   5838  O  O   . ILE B 1 313 ? 123.998 108.908 156.320 1.00 59.82  ? 288  ILE B O   1 
ATOM   5839  C  CB  . ILE B 1 313 ? 126.809 109.102 156.645 1.00 43.57  ? 288  ILE B CB  1 
ATOM   5840  C  CG1 . ILE B 1 313 ? 128.139 109.116 157.398 1.00 51.10  ? 288  ILE B CG1 1 
ATOM   5841  C  CG2 . ILE B 1 313 ? 127.029 109.342 155.162 1.00 49.69  ? 288  ILE B CG2 1 
ATOM   5842  C  CD1 . ILE B 1 313 ? 129.056 107.972 157.028 1.00 49.59  ? 288  ILE B CD1 1 
ATOM   5843  N  N   . ALA B 1 314 ? 123.803 111.149 156.368 1.00 31.54  ? 289  ALA B N   1 
ATOM   5844  C  CA  . ALA B 1 314 ? 122.469 111.172 155.780 1.00 24.44  ? 289  ALA B CA  1 
ATOM   5845  C  C   . ALA B 1 314 ? 122.604 111.453 154.290 1.00 22.82  ? 289  ALA B C   1 
ATOM   5846  O  O   . ALA B 1 314 ? 122.920 112.577 153.892 1.00 48.72  ? 289  ALA B O   1 
ATOM   5847  C  CB  . ALA B 1 314 ? 121.592 112.221 156.459 1.00 28.92  ? 289  ALA B CB  1 
ATOM   5848  N  N   . GLN B 1 315 ? 122.360 110.438 153.469 1.00 3.52   ? 290  GLN B N   1 
ATOM   5849  C  CA  . GLN B 1 315 ? 122.483 110.549 152.023 1.00 19.89  ? 290  GLN B CA  1 
ATOM   5850  C  C   . GLN B 1 315 ? 121.110 110.440 151.376 1.00 25.72  ? 290  GLN B C   1 
ATOM   5851  O  O   . GLN B 1 315 ? 120.372 109.483 151.631 1.00 33.08  ? 290  GLN B O   1 
ATOM   5852  C  CB  . GLN B 1 315 ? 123.427 109.477 151.473 1.00 20.60  ? 290  GLN B CB  1 
ATOM   5853  C  CG  . GLN B 1 315 ? 123.155 108.078 151.990 1.00 29.78  ? 290  GLN B CG  1 
ATOM   5854  C  CD  . GLN B 1 315 ? 124.348 107.157 151.841 1.00 27.39  ? 290  GLN B CD  1 
ATOM   5855  O  OE1 . GLN B 1 315 ? 125.475 107.524 152.168 1.00 26.37  ? 290  GLN B OE1 1 
ATOM   5856  N  NE2 . GLN B 1 315 ? 124.104 105.953 151.343 1.00 22.36  ? 290  GLN B NE2 1 
ATOM   5857  N  N   . SER B 1 316 ? 120.776 111.426 150.540 1.00 20.61  ? 291  SER B N   1 
ATOM   5858  C  CA  . SER B 1 316 ? 119.499 111.473 149.825 1.00 17.54  ? 291  SER B CA  1 
ATOM   5859  C  C   . SER B 1 316 ? 118.318 111.377 150.790 1.00 30.48  ? 291  SER B C   1 
ATOM   5860  O  O   . SER B 1 316 ? 117.370 110.620 150.576 1.00 42.34  ? 291  SER B O   1 
ATOM   5861  C  CB  . SER B 1 316 ? 119.426 110.377 148.760 1.00 23.47  ? 291  SER B CB  1 
ATOM   5862  O  OG  . SER B 1 316 ? 120.543 110.433 147.893 1.00 37.49  ? 291  SER B OG  1 
ATOM   5863  N  N   . GLY B 1 317 ? 118.382 112.157 151.865 1.00 27.33  ? 292  GLY B N   1 
ATOM   5864  C  CA  . GLY B 1 317 ? 117.316 112.157 152.848 1.00 25.61  ? 292  GLY B CA  1 
ATOM   5865  C  C   . GLY B 1 317 ? 117.373 113.322 153.813 1.00 29.23  ? 292  GLY B C   1 
ATOM   5866  O  O   . GLY B 1 317 ? 118.457 113.807 154.148 1.00 31.88  ? 292  GLY B O   1 
ATOM   5867  N  N   . THR B 1 318 ? 116.208 113.771 154.273 1.00 22.46  ? 293  THR B N   1 
ATOM   5868  C  CA  . THR B 1 318 ? 116.112 114.887 155.203 1.00 17.28  ? 293  THR B CA  1 
ATOM   5869  C  C   . THR B 1 318 ? 114.891 114.688 156.088 1.00 26.04  ? 293  THR B C   1 
ATOM   5870  O  O   . THR B 1 318 ? 114.051 113.821 155.840 1.00 33.12  ? 293  THR B O   1 
ATOM   5871  C  CB  . THR B 1 318 ? 116.021 116.230 154.470 1.00 22.62  ? 293  THR B CB  1 
ATOM   5872  O  OG1 . THR B 1 318 ? 115.261 116.069 153.266 1.00 34.20  ? 293  THR B OG1 1 
ATOM   5873  C  CG2 . THR B 1 318 ? 117.402 116.756 154.132 1.00 32.42  ? 293  THR B CG2 1 
ATOM   5874  N  N   . ALA B 1 319 ? 114.804 115.506 157.135 1.00 23.66  ? 294  ALA B N   1 
ATOM   5875  C  CA  . ALA B 1 319 ? 113.662 115.502 158.037 1.00 19.16  ? 294  ALA B CA  1 
ATOM   5876  C  C   . ALA B 1 319 ? 112.732 116.684 157.807 1.00 27.00  ? 294  ALA B C   1 
ATOM   5877  O  O   . ALA B 1 319 ? 111.816 116.902 158.606 1.00 35.54  ? 294  ALA B O   1 
ATOM   5878  C  CB  . ALA B 1 319 ? 114.135 115.492 159.491 1.00 24.04  ? 294  ALA B CB  1 
ATOM   5879  N  N   . ILE B 1 320 ? 112.942 117.450 156.737 1.00 26.42  ? 295  ILE B N   1 
ATOM   5880  C  CA  . ILE B 1 320 ? 112.151 118.639 156.460 1.00 26.97  ? 295  ILE B CA  1 
ATOM   5881  C  C   . ILE B 1 320 ? 111.483 118.578 155.094 1.00 30.47  ? 295  ILE B C   1 
ATOM   5882  O  O   . ILE B 1 320 ? 110.977 119.590 154.610 1.00 33.18  ? 295  ILE B O   1 
ATOM   5883  C  CB  . ILE B 1 320 ? 113.001 119.917 156.592 1.00 24.12  ? 295  ILE B CB  1 
ATOM   5884  C  CG1 . ILE B 1 320 ? 114.319 119.763 155.839 1.00 22.89  ? 295  ILE B CG1 1 
ATOM   5885  C  CG2 . ILE B 1 320 ? 113.279 120.214 158.048 1.00 31.82  ? 295  ILE B CG2 1 
ATOM   5886  C  CD1 . ILE B 1 320 ? 115.218 120.969 155.951 1.00 24.15  ? 295  ILE B CD1 1 
ATOM   5887  N  N   . SER B 1 321 ? 111.471 117.410 154.458 1.00 22.06  ? 296  SER B N   1 
ATOM   5888  C  CA  . SER B 1 321 ? 110.791 117.252 153.184 1.00 21.93  ? 296  SER B CA  1 
ATOM   5889  C  C   . SER B 1 321 ? 109.302 117.009 153.418 1.00 31.78  ? 296  SER B C   1 
ATOM   5890  O  O   . SER B 1 321 ? 108.817 116.989 154.553 1.00 32.96  ? 296  SER B O   1 
ATOM   5891  C  CB  . SER B 1 321 ? 111.423 116.117 152.383 1.00 22.46  ? 296  SER B CB  1 
ATOM   5892  O  OG  . SER B 1 321 ? 111.203 114.869 153.012 1.00 33.56  ? 296  SER B OG  1 
ATOM   5893  N  N   . SER B 1 322 ? 108.559 116.824 152.326 1.00 34.55  ? 297  SER B N   1 
ATOM   5894  C  CA  . SER B 1 322 ? 107.116 116.649 152.444 1.00 27.97  ? 297  SER B CA  1 
ATOM   5895  C  C   . SER B 1 322 ? 106.750 115.270 152.978 1.00 30.40  ? 297  SER B C   1 
ATOM   5896  O  O   . SER B 1 322 ? 105.735 115.125 153.668 1.00 37.33  ? 297  SER B O   1 
ATOM   5897  C  CB  . SER B 1 322 ? 106.445 116.890 151.093 1.00 26.43  ? 297  SER B CB  1 
ATOM   5898  O  OG  . SER B 1 322 ? 107.275 116.460 150.029 1.00 33.48  ? 297  SER B OG  1 
ATOM   5899  N  N   . TRP B 1 323 ? 107.556 114.252 152.679 1.00 26.93  ? 298  TRP B N   1 
ATOM   5900  C  CA  . TRP B 1 323 ? 107.264 112.876 153.064 1.00 32.55  ? 298  TRP B CA  1 
ATOM   5901  C  C   . TRP B 1 323 ? 108.200 112.365 154.154 1.00 32.88  ? 298  TRP B C   1 
ATOM   5902  O  O   . TRP B 1 323 ? 108.553 111.184 154.170 1.00 34.90  ? 298  TRP B O   1 
ATOM   5903  C  CB  . TRP B 1 323 ? 107.327 111.961 151.843 1.00 31.97  ? 298  TRP B CB  1 
ATOM   5904  C  CG  . TRP B 1 323 ? 108.570 112.129 151.025 1.00 34.06  ? 298  TRP B CG  1 
ATOM   5905  C  CD1 . TRP B 1 323 ? 109.840 112.323 151.486 1.00 37.54  ? 298  TRP B CD1 1 
ATOM   5906  C  CD2 . TRP B 1 323 ? 108.661 112.116 149.598 1.00 28.98  ? 298  TRP B CD2 1 
ATOM   5907  N  NE1 . TRP B 1 323 ? 110.714 112.433 150.435 1.00 28.77  ? 298  TRP B NE1 1 
ATOM   5908  C  CE2 . TRP B 1 323 ? 110.014 112.309 149.264 1.00 23.65  ? 298  TRP B CE2 1 
ATOM   5909  C  CE3 . TRP B 1 323 ? 107.729 111.959 148.569 1.00 33.24  ? 298  TRP B CE3 1 
ATOM   5910  C  CZ2 . TRP B 1 323 ? 110.456 112.350 147.949 1.00 28.74  ? 298  TRP B CZ2 1 
ATOM   5911  C  CZ3 . TRP B 1 323 ? 108.172 111.999 147.264 1.00 35.17  ? 298  TRP B CZ3 1 
ATOM   5912  C  CH2 . TRP B 1 323 ? 109.523 112.192 146.965 1.00 29.52  ? 298  TRP B CH2 1 
ATOM   5913  N  N   . SER B 1 324 ? 108.612 113.237 155.071 1.00 27.31  ? 299  SER B N   1 
ATOM   5914  C  CA  . SER B 1 324 ? 109.510 112.848 156.151 1.00 18.81  ? 299  SER B CA  1 
ATOM   5915  C  C   . SER B 1 324 ? 108.786 112.602 157.465 1.00 26.92  ? 299  SER B C   1 
ATOM   5916  O  O   . SER B 1 324 ? 109.123 111.655 158.182 1.00 35.28  ? 299  SER B O   1 
ATOM   5917  C  CB  . SER B 1 324 ? 110.585 113.917 156.356 1.00 29.89  ? 299  SER B CB  1 
ATOM   5918  O  OG  . SER B 1 324 ? 111.612 113.795 155.389 1.00 43.95  ? 299  SER B OG  1 
ATOM   5919  N  N   . VAL B 1 325 ? 107.801 113.430 157.799 1.00 34.02  ? 300  VAL B N   1 
ATOM   5920  C  CA  . VAL B 1 325 ? 107.042 113.295 159.034 1.00 29.77  ? 300  VAL B CA  1 
ATOM   5921  C  C   . VAL B 1 325 ? 105.562 113.235 158.688 1.00 34.94  ? 300  VAL B C   1 
ATOM   5922  O  O   . VAL B 1 325 ? 105.111 113.815 157.696 1.00 39.61  ? 300  VAL B O   1 
ATOM   5923  C  CB  . VAL B 1 325 ? 107.325 114.456 160.015 1.00 31.64  ? 300  VAL B CB  1 
ATOM   5924  C  CG1 . VAL B 1 325 ? 106.954 114.064 161.433 1.00 33.81  ? 300  VAL B CG1 1 
ATOM   5925  C  CG2 . VAL B 1 325 ? 108.781 114.875 159.942 1.00 33.43  ? 300  VAL B CG2 1 
ATOM   5926  N  N   . ASN B 1 326 ? 104.803 112.521 159.515 1.00 44.05  ? 301  ASN B N   1 
ATOM   5927  C  CA  . ASN B 1 326 ? 103.355 112.421 159.372 1.00 39.78  ? 301  ASN B CA  1 
ATOM   5928  C  C   . ASN B 1 326 ? 102.720 113.408 160.345 1.00 47.80  ? 301  ASN B C   1 
ATOM   5929  O  O   . ASN B 1 326 ? 102.819 113.237 161.564 1.00 50.96  ? 301  ASN B O   1 
ATOM   5930  C  CB  . ASN B 1 326 ? 102.878 110.996 159.636 1.00 38.79  ? 301  ASN B CB  1 
ATOM   5931  C  CG  . ASN B 1 326 ? 101.381 110.845 159.481 1.00 43.87  ? 301  ASN B CG  1 
ATOM   5932  O  OD1 . ASN B 1 326 ? 100.732 111.642 158.805 1.00 47.80  ? 301  ASN B OD1 1 
ATOM   5933  N  ND2 . ASN B 1 326 ? 100.822 109.816 160.106 1.00 44.37  ? 301  ASN B ND2 1 
ATOM   5934  N  N   . TYR B 1 327 ? 102.071 114.439 159.806 1.00 50.38  ? 302  TYR B N   1 
ATOM   5935  C  CA  . TYR B 1 327 ? 101.543 115.516 160.631 1.00 49.30  ? 302  TYR B CA  1 
ATOM   5936  C  C   . TYR B 1 327 ? 100.083 115.322 161.014 1.00 52.53  ? 302  TYR B C   1 
ATOM   5937  O  O   . TYR B 1 327 ? 99.610  115.986 161.943 1.00 59.17  ? 302  TYR B O   1 
ATOM   5938  C  CB  . TYR B 1 327 ? 101.706 116.856 159.908 1.00 49.22  ? 302  TYR B CB  1 
ATOM   5939  C  CG  . TYR B 1 327 ? 103.109 117.412 159.983 1.00 53.17  ? 302  TYR B CG  1 
ATOM   5940  C  CD1 . TYR B 1 327 ? 103.828 117.374 161.169 1.00 52.51  ? 302  TYR B CD1 1 
ATOM   5941  C  CD2 . TYR B 1 327 ? 103.717 117.968 158.867 1.00 52.27  ? 302  TYR B CD2 1 
ATOM   5942  C  CE1 . TYR B 1 327 ? 105.111 117.877 161.242 1.00 51.84  ? 302  TYR B CE1 1 
ATOM   5943  C  CE2 . TYR B 1 327 ? 104.999 118.473 158.930 1.00 54.34  ? 302  TYR B CE2 1 
ATOM   5944  C  CZ  . TYR B 1 327 ? 105.691 118.425 160.120 1.00 56.96  ? 302  TYR B CZ  1 
ATOM   5945  O  OH  . TYR B 1 327 ? 106.970 118.928 160.188 1.00 59.70  ? 302  TYR B OH  1 
ATOM   5946  N  N   . GLN B 1 328 ? 99.361  114.438 160.329 1.00 49.02  ? 303  GLN B N   1 
ATOM   5947  C  CA  . GLN B 1 328 ? 97.963  114.139 160.639 1.00 47.36  ? 303  GLN B CA  1 
ATOM   5948  C  C   . GLN B 1 328 ? 97.817  112.630 160.779 1.00 51.80  ? 303  GLN B C   1 
ATOM   5949  O  O   . GLN B 1 328 ? 97.340  111.950 159.861 1.00 52.70  ? 303  GLN B O   1 
ATOM   5950  C  CB  . GLN B 1 328 ? 97.023  114.693 159.568 1.00 48.83  ? 303  GLN B CB  1 
ATOM   5951  C  CG  . GLN B 1 328 ? 97.596  114.682 158.164 1.00 55.07  ? 303  GLN B CG  1 
ATOM   5952  C  CD  . GLN B 1 328 ? 96.670  115.332 157.158 1.00 55.93  ? 303  GLN B CD  1 
ATOM   5953  O  OE1 . GLN B 1 328 ? 95.508  115.605 157.454 1.00 57.30  ? 303  GLN B OE1 1 
ATOM   5954  N  NE2 . GLN B 1 328 ? 97.182  115.582 155.958 1.00 53.38  ? 303  GLN B NE2 1 
ATOM   5955  N  N   . PRO B 1 329 ? 98.221  112.071 161.918 1.00 53.19  ? 304  PRO B N   1 
ATOM   5956  C  CA  . PRO B 1 329 ? 98.152  110.615 162.089 1.00 53.69  ? 304  PRO B CA  1 
ATOM   5957  C  C   . PRO B 1 329 ? 96.754  110.126 162.431 1.00 58.38  ? 304  PRO B C   1 
ATOM   5958  O  O   . PRO B 1 329 ? 96.405  108.977 162.140 1.00 61.96  ? 304  PRO B O   1 
ATOM   5959  C  CB  . PRO B 1 329 ? 99.129  110.360 163.240 1.00 51.33  ? 304  PRO B CB  1 
ATOM   5960  C  CG  . PRO B 1 329 ? 99.049  111.603 164.058 1.00 50.65  ? 304  PRO B CG  1 
ATOM   5961  C  CD  . PRO B 1 329 ? 98.790  112.741 163.100 1.00 52.03  ? 304  PRO B CD  1 
ATOM   5962  N  N   . LEU B 1 330 ? 95.950  110.992 163.054 1.00 58.41  ? 305  LEU B N   1 
ATOM   5963  C  CA  . LEU B 1 330 ? 94.631  110.576 163.519 1.00 57.21  ? 305  LEU B CA  1 
ATOM   5964  C  C   . LEU B 1 330 ? 93.723  110.187 162.361 1.00 59.76  ? 305  LEU B C   1 
ATOM   5965  O  O   . LEU B 1 330 ? 93.000  109.188 162.443 1.00 63.66  ? 305  LEU B O   1 
ATOM   5966  C  CB  . LEU B 1 330 ? 93.992  111.688 164.350 1.00 58.29  ? 305  LEU B CB  1 
ATOM   5967  C  CG  . LEU B 1 330 ? 92.880  111.251 165.307 1.00 61.44  ? 305  LEU B CG  1 
ATOM   5968  C  CD1 . LEU B 1 330 ? 93.257  109.970 166.030 1.00 60.82  ? 305  LEU B CD1 1 
ATOM   5969  C  CD2 . LEU B 1 330 ? 92.561  112.355 166.302 1.00 61.14  ? 305  LEU B CD2 1 
ATOM   5970  N  N   . LYS B 1 331 ? 93.746  110.959 161.273 1.00 53.57  ? 306  LYS B N   1 
ATOM   5971  C  CA  . LYS B 1 331 ? 92.867  110.671 160.144 1.00 54.14  ? 306  LYS B CA  1 
ATOM   5972  C  C   . LYS B 1 331 ? 93.166  109.301 159.549 1.00 56.52  ? 306  LYS B C   1 
ATOM   5973  O  O   . LYS B 1 331 ? 92.258  108.485 159.346 1.00 61.95  ? 306  LYS B O   1 
ATOM   5974  C  CB  . LYS B 1 331 ? 93.006  111.758 159.079 1.00 54.37  ? 306  LYS B CB  1 
ATOM   5975  C  CG  . LYS B 1 331 ? 92.293  111.435 157.777 1.00 58.76  ? 306  LYS B CG  1 
ATOM   5976  C  CD  . LYS B 1 331 ? 93.051  111.979 156.579 1.00 54.77  ? 306  LYS B CD  1 
ATOM   5977  C  CE  . LYS B 1 331 ? 93.082  113.496 156.587 1.00 55.66  ? 306  LYS B CE  1 
ATOM   5978  N  NZ  . LYS B 1 331 ? 93.657  114.039 155.326 1.00 56.79  ? 306  LYS B NZ  1 
ATOM   5979  N  N   . TYR B 1 332 ? 94.442  109.024 159.278 1.00 55.52  ? 307  TYR B N   1 
ATOM   5980  C  CA  . TYR B 1 332 ? 94.801  107.752 158.660 1.00 60.60  ? 307  TYR B CA  1 
ATOM   5981  C  C   . TYR B 1 332 ? 94.616  106.594 159.631 1.00 56.58  ? 307  TYR B C   1 
ATOM   5982  O  O   . TYR B 1 332 ? 94.223  105.494 159.224 1.00 56.48  ? 307  TYR B O   1 
ATOM   5983  C  CB  . TYR B 1 332 ? 96.235  107.811 158.143 1.00 55.61  ? 307  TYR B CB  1 
ATOM   5984  C  CG  . TYR B 1 332 ? 96.403  108.769 156.990 1.00 52.55  ? 307  TYR B CG  1 
ATOM   5985  C  CD1 . TYR B 1 332 ? 96.110  108.380 155.693 1.00 52.68  ? 307  TYR B CD1 1 
ATOM   5986  C  CD2 . TYR B 1 332 ? 96.843  110.067 157.201 1.00 54.89  ? 307  TYR B CD2 1 
ATOM   5987  C  CE1 . TYR B 1 332 ? 96.255  109.254 154.636 1.00 54.77  ? 307  TYR B CE1 1 
ATOM   5988  C  CE2 . TYR B 1 332 ? 96.994  110.949 156.150 1.00 57.79  ? 307  TYR B CE2 1 
ATOM   5989  C  CZ  . TYR B 1 332 ? 96.699  110.537 154.869 1.00 57.80  ? 307  TYR B CZ  1 
ATOM   5990  O  OH  . TYR B 1 332 ? 96.847  111.411 153.817 1.00 56.96  ? 307  TYR B OH  1 
ATOM   5991  N  N   . THR B 1 333 ? 94.886  106.819 160.919 1.00 57.02  ? 308  THR B N   1 
ATOM   5992  C  CA  . THR B 1 333 ? 94.656  105.770 161.907 1.00 60.55  ? 308  THR B CA  1 
ATOM   5993  C  C   . THR B 1 333 ? 93.179  105.407 161.987 1.00 64.00  ? 308  THR B C   1 
ATOM   5994  O  O   . THR B 1 333 ? 92.825  104.224 162.025 1.00 63.62  ? 308  THR B O   1 
ATOM   5995  C  CB  . THR B 1 333 ? 95.176  106.209 163.275 1.00 60.68  ? 308  THR B CB  1 
ATOM   5996  O  OG1 . THR B 1 333 ? 96.598  106.369 163.217 1.00 60.86  ? 308  THR B OG1 1 
ATOM   5997  C  CG2 . THR B 1 333 ? 94.838  105.168 164.327 1.00 58.40  ? 308  THR B CG2 1 
ATOM   5998  N  N   . ARG B 1 334 ? 92.299  106.412 162.000 1.00 73.81  ? 309  ARG B N   1 
ATOM   5999  C  CA  . ARG B 1 334 ? 90.866  106.139 162.037 1.00 71.38  ? 309  ARG B CA  1 
ATOM   6000  C  C   . ARG B 1 334 ? 90.394  105.484 160.745 1.00 71.49  ? 309  ARG B C   1 
ATOM   6001  O  O   . ARG B 1 334 ? 89.513  104.617 160.772 1.00 76.91  ? 309  ARG B O   1 
ATOM   6002  C  CB  . ARG B 1 334 ? 90.091  107.427 162.305 1.00 73.84  ? 309  ARG B CB  1 
ATOM   6003  C  CG  . ARG B 1 334 ? 90.314  108.001 163.694 1.00 72.68  ? 309  ARG B CG  1 
ATOM   6004  C  CD  . ARG B 1 334 ? 89.511  109.274 163.905 1.00 73.47  ? 309  ARG B CD  1 
ATOM   6005  N  NE  . ARG B 1 334 ? 88.087  109.007 164.067 1.00 77.71  ? 309  ARG B NE  1 
ATOM   6006  C  CZ  . ARG B 1 334 ? 87.541  108.459 165.145 1.00 80.24  ? 309  ARG B CZ  1 
ATOM   6007  N  NH1 . ARG B 1 334 ? 88.272  108.118 166.194 1.00 79.69  ? 309  ARG B NH1 1 
ATOM   6008  N  NH2 . ARG B 1 334 ? 86.228  108.253 165.173 1.00 79.43  ? 309  ARG B NH2 1 
ATOM   6009  N  N   . LEU B 1 335 ? 90.959  105.885 159.604 1.00 64.23  ? 310  LEU B N   1 
ATOM   6010  C  CA  . LEU B 1 335 ? 90.605  105.240 158.344 1.00 66.29  ? 310  LEU B CA  1 
ATOM   6011  C  C   . LEU B 1 335 ? 90.988  103.764 158.360 1.00 66.83  ? 310  LEU B C   1 
ATOM   6012  O  O   . LEU B 1 335 ? 90.199  102.902 157.952 1.00 70.59  ? 310  LEU B O   1 
ATOM   6013  C  CB  . LEU B 1 335 ? 91.282  105.967 157.181 1.00 66.67  ? 310  LEU B CB  1 
ATOM   6014  C  CG  . LEU B 1 335 ? 90.590  105.964 155.816 1.00 68.42  ? 310  LEU B CG  1 
ATOM   6015  C  CD1 . LEU B 1 335 ? 91.130  107.096 154.957 1.00 64.87  ? 310  LEU B CD1 1 
ATOM   6016  C  CD2 . LEU B 1 335 ? 90.759  104.630 155.105 1.00 67.35  ? 310  LEU B CD2 1 
ATOM   6017  N  N   . LEU B 1 336 ? 92.193  103.454 158.843 1.00 64.20  ? 311  LEU B N   1 
ATOM   6018  C  CA  . LEU B 1 336 ? 92.612  102.062 158.961 1.00 65.69  ? 311  LEU B CA  1 
ATOM   6019  C  C   . LEU B 1 336 ? 91.723  101.297 159.932 1.00 68.69  ? 311  LEU B C   1 
ATOM   6020  O  O   . LEU B 1 336 ? 91.361  100.143 159.677 1.00 72.19  ? 311  LEU B O   1 
ATOM   6021  C  CB  . LEU B 1 336 ? 94.067  101.988 159.413 1.00 66.98  ? 311  LEU B CB  1 
ATOM   6022  C  CG  . LEU B 1 336 ? 94.541  100.586 159.791 1.00 64.66  ? 311  LEU B CG  1 
ATOM   6023  C  CD1 . LEU B 1 336 ? 94.801  99.743  158.551 1.00 62.05  ? 311  LEU B CD1 1 
ATOM   6024  C  CD2 . LEU B 1 336 ? 95.762  100.661 160.676 1.00 64.46  ? 311  LEU B CD2 1 
ATOM   6025  N  N   . ALA B 1 337 ? 91.374  101.920 161.059 1.00 78.27  ? 312  ALA B N   1 
ATOM   6026  C  CA  . ALA B 1 337 ? 90.519  101.259 162.039 1.00 77.19  ? 312  ALA B CA  1 
ATOM   6027  C  C   . ALA B 1 337 ? 89.149  100.948 161.452 1.00 77.42  ? 312  ALA B C   1 
ATOM   6028  O  O   . ALA B 1 337 ? 88.596  99.867  161.684 1.00 80.14  ? 312  ALA B O   1 
ATOM   6029  C  CB  . ALA B 1 337 ? 90.390  102.130 163.287 1.00 80.10  ? 312  ALA B CB  1 
ATOM   6030  N  N   . ALA B 1 338 ? 88.586  101.886 160.688 1.00 81.16  ? 313  ALA B N   1 
ATOM   6031  C  CA  . ALA B 1 338 ? 87.309  101.637 160.028 1.00 81.02  ? 313  ALA B CA  1 
ATOM   6032  C  C   . ALA B 1 338 ? 87.428  100.525 158.995 1.00 83.05  ? 313  ALA B C   1 
ATOM   6033  O  O   . ALA B 1 338 ? 86.537  99.676  158.880 1.00 86.65  ? 313  ALA B O   1 
ATOM   6034  C  CB  . ALA B 1 338 ? 86.794  102.921 159.379 1.00 79.77  ? 313  ALA B CB  1 
ATOM   6035  N  N   . LYS B 1 339 ? 88.523  100.510 158.234 1.00 79.79  ? 314  LYS B N   1 
ATOM   6036  C  CA  . LYS B 1 339 ? 88.700  99.496  157.203 1.00 78.23  ? 314  LYS B CA  1 
ATOM   6037  C  C   . LYS B 1 339 ? 89.080  98.130  157.765 1.00 75.22  ? 314  LYS B C   1 
ATOM   6038  O  O   . LYS B 1 339 ? 88.997  97.137  157.035 1.00 76.78  ? 314  LYS B O   1 
ATOM   6039  C  CB  . LYS B 1 339 ? 89.762  99.952  156.197 1.00 76.83  ? 314  LYS B CB  1 
ATOM   6040  C  CG  . LYS B 1 339 ? 89.646  99.299  154.827 1.00 77.82  ? 314  LYS B CG  1 
ATOM   6041  C  CD  . LYS B 1 339 ? 90.951  99.389  154.053 1.00 74.93  ? 314  LYS B CD  1 
ATOM   6042  C  CE  . LYS B 1 339 ? 91.407  100.829 153.907 1.00 75.92  ? 314  LYS B CE  1 
ATOM   6043  N  NZ  . LYS B 1 339 ? 90.469  101.623 153.067 1.00 76.50  ? 314  LYS B NZ  1 
ATOM   6044  N  N   . VAL B 1 340 ? 89.481  98.050  159.033 1.00 81.77  ? 315  VAL B N   1 
ATOM   6045  C  CA  . VAL B 1 340 ? 89.934  96.789  159.610 1.00 83.79  ? 315  VAL B CA  1 
ATOM   6046  C  C   . VAL B 1 340 ? 88.825  96.163  160.447 1.00 85.88  ? 315  VAL B C   1 
ATOM   6047  O  O   . VAL B 1 340 ? 88.851  94.960  160.727 1.00 85.92  ? 315  VAL B O   1 
ATOM   6048  C  CB  . VAL B 1 340 ? 91.216  96.984  160.441 1.00 83.76  ? 315  VAL B CB  1 
ATOM   6049  C  CG1 . VAL B 1 340 ? 90.882  97.397  161.866 1.00 84.50  ? 315  VAL B CG1 1 
ATOM   6050  C  CG2 . VAL B 1 340 ? 92.051  95.714  160.429 1.00 81.95  ? 315  VAL B CG2 1 
ATOM   6051  N  N   . GLY B 1 341 ? 87.846  96.968  160.856 1.00 102.41 ? 316  GLY B N   1 
ATOM   6052  C  CA  . GLY B 1 341 ? 86.676  96.422  161.516 1.00 103.03 ? 316  GLY B CA  1 
ATOM   6053  C  C   . GLY B 1 341 ? 86.179  97.151  162.748 1.00 104.54 ? 316  GLY B C   1 
ATOM   6054  O  O   . GLY B 1 341 ? 84.967  97.196  162.983 1.00 105.30 ? 316  GLY B O   1 
ATOM   6055  N  N   . CYS B 1 342 ? 87.077  97.731  163.543 1.00 117.92 ? 317  CYS B N   1 
ATOM   6056  C  CA  . CYS B 1 342 ? 86.682  98.415  164.769 1.00 118.92 ? 317  CYS B CA  1 
ATOM   6057  C  C   . CYS B 1 342 ? 87.095  99.875  164.696 1.00 117.48 ? 317  CYS B C   1 
ATOM   6058  O  O   . CYS B 1 342 ? 88.275  100.180 164.500 1.00 117.14 ? 317  CYS B O   1 
ATOM   6059  C  CB  . CYS B 1 342 ? 87.298  97.761  166.011 1.00 119.17 ? 317  CYS B CB  1 
ATOM   6060  S  SG  . CYS B 1 342 ? 89.023  97.258  165.864 1.00 123.96 ? 317  CYS B SG  1 
ATOM   6061  N  N   . ASP B 1 343 ? 86.127  100.770 164.872 1.00 110.55 ? 318  ASP B N   1 
ATOM   6062  C  CA  . ASP B 1 343 ? 86.333  102.213 164.798 1.00 110.99 ? 318  ASP B CA  1 
ATOM   6063  C  C   . ASP B 1 343 ? 85.664  102.905 165.978 1.00 112.67 ? 318  ASP B C   1 
ATOM   6064  O  O   . ASP B 1 343 ? 84.897  103.857 165.821 1.00 112.76 ? 318  ASP B O   1 
ATOM   6065  C  CB  . ASP B 1 343 ? 85.817  102.774 163.477 1.00 110.77 ? 318  ASP B CB  1 
ATOM   6066  C  CG  . ASP B 1 343 ? 86.594  103.992 163.021 1.00 109.77 ? 318  ASP B CG  1 
ATOM   6067  O  OD1 . ASP B 1 343 ? 87.715  104.207 163.528 1.00 108.08 ? 318  ASP B OD1 1 
ATOM   6068  O  OD2 . ASP B 1 343 ? 86.085  104.736 162.156 1.00 110.68 ? 318  ASP B OD2 1 
ATOM   6069  N  N   . ARG B 1 344 ? 85.941  102.411 167.184 1.00 123.38 ? 319  ARG B N   1 
ATOM   6070  C  CA  . ARG B 1 344 ? 85.373  103.001 168.389 1.00 122.56 ? 319  ARG B CA  1 
ATOM   6071  C  C   . ARG B 1 344 ? 85.761  104.469 168.506 1.00 123.61 ? 319  ARG B C   1 
ATOM   6072  O  O   . ARG B 1 344 ? 86.874  104.866 168.149 1.00 124.32 ? 319  ARG B O   1 
ATOM   6073  C  CB  . ARG B 1 344 ? 85.844  102.234 169.625 1.00 122.71 ? 319  ARG B CB  1 
ATOM   6074  C  CG  . ARG B 1 344 ? 85.924  100.729 169.436 1.00 122.89 ? 319  ARG B CG  1 
ATOM   6075  C  CD  . ARG B 1 344 ? 84.592  100.063 169.742 1.00 122.35 ? 319  ARG B CD  1 
ATOM   6076  N  NE  . ARG B 1 344 ? 84.635  98.625  169.502 1.00 124.32 ? 319  ARG B NE  1 
ATOM   6077  C  CZ  . ARG B 1 344 ? 84.575  98.065  168.303 1.00 124.58 ? 319  ARG B CZ  1 
ATOM   6078  N  NH1 . ARG B 1 344 ? 84.429  98.791  167.207 1.00 124.25 ? 319  ARG B NH1 1 
ATOM   6079  N  NH2 . ARG B 1 344 ? 84.656  96.741  168.200 1.00 124.16 ? 319  ARG B NH2 1 
ATOM   6080  N  N   . GLU B 1 345 ? 84.823  105.280 169.002 1.00 131.74 ? 320  GLU B N   1 
ATOM   6081  C  CA  . GLU B 1 345 ? 85.060  106.717 169.104 1.00 131.62 ? 320  GLU B CA  1 
ATOM   6082  C  C   . GLU B 1 345 ? 86.221  107.023 170.042 1.00 132.28 ? 320  GLU B C   1 
ATOM   6083  O  O   . GLU B 1 345 ? 87.061  107.880 169.742 1.00 131.41 ? 320  GLU B O   1 
ATOM   6084  C  CB  . GLU B 1 345 ? 83.789  107.425 169.571 1.00 131.98 ? 320  GLU B CB  1 
ATOM   6085  C  CG  . GLU B 1 345 ? 83.856  108.941 169.491 1.00 131.94 ? 320  GLU B CG  1 
ATOM   6086  C  CD  . GLU B 1 345 ? 84.010  109.445 168.070 1.00 132.64 ? 320  GLU B CD  1 
ATOM   6087  O  OE1 . GLU B 1 345 ? 83.470  108.802 167.146 1.00 132.77 ? 320  GLU B OE1 1 
ATOM   6088  O  OE2 . GLU B 1 345 ? 84.671  110.487 167.876 1.00 132.93 ? 320  GLU B OE2 1 
ATOM   6089  N  N   . ASP B 1 346 ? 86.285  106.339 171.181 1.00 131.13 ? 321  ASP B N   1 
ATOM   6090  C  CA  . ASP B 1 346 ? 87.406  106.520 172.092 1.00 131.19 ? 321  ASP B CA  1 
ATOM   6091  C  C   . ASP B 1 346 ? 88.644  105.837 171.525 1.00 132.71 ? 321  ASP B C   1 
ATOM   6092  O  O   . ASP B 1 346 ? 88.589  104.677 171.104 1.00 132.50 ? 321  ASP B O   1 
ATOM   6093  C  CB  . ASP B 1 346 ? 87.069  105.961 173.472 1.00 130.41 ? 321  ASP B CB  1 
ATOM   6094  C  CG  . ASP B 1 346 ? 87.929  106.560 174.568 1.00 131.80 ? 321  ASP B CG  1 
ATOM   6095  O  OD1 . ASP B 1 346 ? 88.805  107.391 174.250 1.00 131.21 ? 321  ASP B OD1 1 
ATOM   6096  O  OD2 . ASP B 1 346 ? 87.728  106.201 175.748 1.00 132.36 ? 321  ASP B OD2 1 
ATOM   6097  N  N   . SER B 1 347 ? 89.765  106.563 171.513 1.00 121.30 ? 322  SER B N   1 
ATOM   6098  C  CA  . SER B 1 347 ? 90.980  106.044 170.892 1.00 118.99 ? 322  SER B CA  1 
ATOM   6099  C  C   . SER B 1 347 ? 91.524  104.828 171.630 1.00 118.64 ? 322  SER B C   1 
ATOM   6100  O  O   . SER B 1 347 ? 92.080  103.922 170.997 1.00 117.82 ? 322  SER B O   1 
ATOM   6101  C  CB  . SER B 1 347 ? 92.041  107.142 170.823 1.00 118.16 ? 322  SER B CB  1 
ATOM   6102  O  OG  . SER B 1 347 ? 91.540  108.295 170.169 1.00 117.30 ? 322  SER B OG  1 
ATOM   6103  N  N   . THR B 1 348 ? 91.385  104.792 172.958 1.00 119.08 ? 323  THR B N   1 
ATOM   6104  C  CA  . THR B 1 348 ? 91.929  103.676 173.727 1.00 119.05 ? 323  THR B CA  1 
ATOM   6105  C  C   . THR B 1 348 ? 91.266  102.359 173.341 1.00 118.46 ? 323  THR B C   1 
ATOM   6106  O  O   . THR B 1 348 ? 91.946  101.339 173.180 1.00 117.21 ? 323  THR B O   1 
ATOM   6107  C  CB  . THR B 1 348 ? 91.763  103.939 175.224 1.00 118.22 ? 323  THR B CB  1 
ATOM   6108  O  OG1 . THR B 1 348 ? 92.197  105.270 175.528 1.00 118.34 ? 323  THR B OG1 1 
ATOM   6109  C  CG2 . THR B 1 348 ? 92.586  102.947 176.031 1.00 117.47 ? 323  THR B CG2 1 
ATOM   6110  N  N   . GLU B 1 349 ? 89.941  102.362 173.184 1.00 120.90 ? 324  GLU B N   1 
ATOM   6111  C  CA  . GLU B 1 349 ? 89.240  101.142 172.793 1.00 120.82 ? 324  GLU B CA  1 
ATOM   6112  C  C   . GLU B 1 349 ? 89.643  100.697 171.393 1.00 122.25 ? 324  GLU B C   1 
ATOM   6113  O  O   . GLU B 1 349 ? 89.814  99.498  171.141 1.00 122.89 ? 324  GLU B O   1 
ATOM   6114  C  CB  . GLU B 1 349 ? 87.729  101.355 172.876 1.00 120.54 ? 324  GLU B CB  1 
ATOM   6115  C  CG  . GLU B 1 349 ? 87.290  102.350 173.941 1.00 121.45 ? 324  GLU B CG  1 
ATOM   6116  C  CD  . GLU B 1 349 ? 87.625  101.900 175.352 1.00 121.74 ? 324  GLU B CD  1 
ATOM   6117  O  OE1 . GLU B 1 349 ? 87.755  100.678 175.578 1.00 121.85 ? 324  GLU B OE1 1 
ATOM   6118  O  OE2 . GLU B 1 349 ? 87.757  102.771 176.236 1.00 121.22 ? 324  GLU B OE2 1 
ATOM   6119  N  N   . ALA B 1 350 ? 89.794  101.648 170.467 1.00 119.39 ? 325  ALA B N   1 
ATOM   6120  C  CA  . ALA B 1 350 ? 90.215  101.304 169.114 1.00 119.00 ? 325  ALA B CA  1 
ATOM   6121  C  C   . ALA B 1 350 ? 91.613  100.698 169.108 1.00 119.04 ? 325  ALA B C   1 
ATOM   6122  O  O   . ALA B 1 350 ? 91.867  99.713  168.406 1.00 117.88 ? 325  ALA B O   1 
ATOM   6123  C  CB  . ALA B 1 350 ? 90.160  102.539 168.215 1.00 117.81 ? 325  ALA B CB  1 
ATOM   6124  N  N   . VAL B 1 351 ? 92.532  101.271 169.888 1.00 111.93 ? 326  VAL B N   1 
ATOM   6125  C  CA  . VAL B 1 351 ? 93.882  100.721 169.970 1.00 109.84 ? 326  VAL B CA  1 
ATOM   6126  C  C   . VAL B 1 351 ? 93.857  99.331  170.595 1.00 111.68 ? 326  VAL B C   1 
ATOM   6127  O  O   . VAL B 1 351 ? 94.570  98.421  170.150 1.00 112.98 ? 326  VAL B O   1 
ATOM   6128  C  CB  . VAL B 1 351 ? 94.801  101.680 170.748 1.00 110.43 ? 326  VAL B CB  1 
ATOM   6129  C  CG1 . VAL B 1 351 ? 96.130  101.012 171.065 1.00 110.16 ? 326  VAL B CG1 1 
ATOM   6130  C  CG2 . VAL B 1 351 ? 95.022  102.957 169.955 1.00 110.78 ? 326  VAL B CG2 1 
ATOM   6131  N  N   . GLU B 1 352 ? 93.041  99.142  171.635 1.00 113.70 ? 327  GLU B N   1 
ATOM   6132  C  CA  . GLU B 1 352 ? 92.951  97.833  172.273 1.00 112.93 ? 327  GLU B CA  1 
ATOM   6133  C  C   . GLU B 1 352 ? 92.414  96.785  171.306 1.00 112.98 ? 327  GLU B C   1 
ATOM   6134  O  O   . GLU B 1 352 ? 92.890  95.644  171.291 1.00 113.23 ? 327  GLU B O   1 
ATOM   6135  C  CB  . GLU B 1 352 ? 92.075  97.917  173.522 1.00 112.42 ? 327  GLU B CB  1 
ATOM   6136  C  CG  . GLU B 1 352 ? 92.855  98.052  174.823 1.00 113.81 ? 327  GLU B CG  1 
ATOM   6137  C  CD  . GLU B 1 352 ? 93.832  96.913  175.051 1.00 114.43 ? 327  GLU B CD  1 
ATOM   6138  O  OE1 . GLU B 1 352 ? 93.522  95.768  174.658 1.00 114.17 ? 327  GLU B OE1 1 
ATOM   6139  O  OE2 . GLU B 1 352 ? 94.912  97.164  175.627 1.00 113.93 ? 327  GLU B OE2 1 
ATOM   6140  N  N   . CYS B 1 353 ? 91.415  97.149  170.497 1.00 113.76 ? 328  CYS B N   1 
ATOM   6141  C  CA  . CYS B 1 353 ? 90.927  96.221  169.481 1.00 113.96 ? 328  CYS B CA  1 
ATOM   6142  C  C   . CYS B 1 353 ? 91.994  95.942  168.430 1.00 114.75 ? 328  CYS B C   1 
ATOM   6143  O  O   . CYS B 1 353 ? 92.165  94.795  168.001 1.00 115.78 ? 328  CYS B O   1 
ATOM   6144  C  CB  . CYS B 1 353 ? 89.664  96.762  168.813 1.00 115.29 ? 328  CYS B CB  1 
ATOM   6145  S  SG  . CYS B 1 353 ? 89.220  95.846  167.311 1.00 125.39 ? 328  CYS B SG  1 
ATOM   6146  N  N   . LEU B 1 354 ? 92.715  96.981  167.999 1.00 105.13 ? 329  LEU B N   1 
ATOM   6147  C  CA  . LEU B 1 354 ? 93.763  96.800  167.000 1.00 104.36 ? 329  LEU B CA  1 
ATOM   6148  C  C   . LEU B 1 354 ? 94.857  95.869  167.501 1.00 103.12 ? 329  LEU B C   1 
ATOM   6149  O  O   . LEU B 1 354 ? 95.461  95.136  166.710 1.00 102.61 ? 329  LEU B O   1 
ATOM   6150  C  CB  . LEU B 1 354 ? 94.355  98.154  166.611 1.00 101.92 ? 329  LEU B CB  1 
ATOM   6151  C  CG  . LEU B 1 354 ? 93.657  98.905  165.476 1.00 103.51 ? 329  LEU B CG  1 
ATOM   6152  C  CD1 . LEU B 1 354 ? 94.171  100.332 165.383 1.00 102.51 ? 329  LEU B CD1 1 
ATOM   6153  C  CD2 . LEU B 1 354 ? 93.844  98.178  164.155 1.00 102.27 ? 329  LEU B CD2 1 
ATOM   6154  N  N   . ARG B 1 355 ? 95.125  95.883  168.807 1.00 95.06  ? 330  ARG B N   1 
ATOM   6155  C  CA  . ARG B 1 355 ? 96.112  94.971  169.373 1.00 93.45  ? 330  ARG B CA  1 
ATOM   6156  C  C   . ARG B 1 355 ? 95.673  93.513  169.315 1.00 94.55  ? 330  ARG B C   1 
ATOM   6157  O  O   . ARG B 1 355 ? 96.500  92.628  169.557 1.00 94.30  ? 330  ARG B O   1 
ATOM   6158  C  CB  . ARG B 1 355 ? 96.425  95.357  170.819 1.00 93.61  ? 330  ARG B CB  1 
ATOM   6159  C  CG  . ARG B 1 355 ? 97.120  96.698  170.961 1.00 92.70  ? 330  ARG B CG  1 
ATOM   6160  C  CD  . ARG B 1 355 ? 97.804  96.834  172.309 1.00 91.57  ? 330  ARG B CD  1 
ATOM   6161  N  NE  . ARG B 1 355 ? 98.036  98.231  172.654 1.00 91.93  ? 330  ARG B NE  1 
ATOM   6162  C  CZ  . ARG B 1 355 ? 98.690  98.638  173.734 1.00 94.66  ? 330  ARG B CZ  1 
ATOM   6163  N  NH1 . ARG B 1 355 ? 99.195  97.776  174.601 1.00 93.57  ? 330  ARG B NH1 1 
ATOM   6164  N  NH2 . ARG B 1 355 ? 98.840  99.941  173.948 1.00 94.88  ? 330  ARG B NH2 1 
ATOM   6165  N  N   . ARG B 1 356 ? 94.405  93.241  169.005 1.00 105.55 ? 331  ARG B N   1 
ATOM   6166  C  CA  . ARG B 1 356 ? 93.916  91.872  168.915 1.00 104.73 ? 331  ARG B CA  1 
ATOM   6167  C  C   . ARG B 1 356 ? 93.999  91.294  167.509 1.00 105.32 ? 331  ARG B C   1 
ATOM   6168  O  O   . ARG B 1 356 ? 94.090  90.070  167.364 1.00 105.36 ? 331  ARG B O   1 
ATOM   6169  C  CB  . ARG B 1 356 ? 92.466  91.795  169.404 1.00 105.78 ? 331  ARG B CB  1 
ATOM   6170  C  CG  . ARG B 1 356 ? 92.292  92.093  170.883 1.00 106.48 ? 331  ARG B CG  1 
ATOM   6171  C  CD  . ARG B 1 356 ? 91.122  91.319  171.464 1.00 106.84 ? 331  ARG B CD  1 
ATOM   6172  N  NE  . ARG B 1 356 ? 89.842  91.805  170.963 1.00 105.92 ? 331  ARG B NE  1 
ATOM   6173  C  CZ  . ARG B 1 356 ? 89.134  92.772  171.530 1.00 105.37 ? 331  ARG B CZ  1 
ATOM   6174  N  NH1 . ARG B 1 356 ? 89.549  93.378  172.630 1.00 105.66 ? 331  ARG B NH1 1 
ATOM   6175  N  NH2 . ARG B 1 356 ? 87.979  93.138  170.981 1.00 105.00 ? 331  ARG B NH2 1 
ATOM   6176  N  N   . LYS B 1 357 ? 93.963  92.134  166.478 1.00 105.52 ? 332  LYS B N   1 
ATOM   6177  C  CA  . LYS B 1 357 ? 94.076  91.649  165.111 1.00 103.77 ? 332  LYS B CA  1 
ATOM   6178  C  C   . LYS B 1 357 ? 95.466  91.075  164.858 1.00 104.90 ? 332  LYS B C   1 
ATOM   6179  O  O   . LYS B 1 357 ? 96.476  91.604  165.330 1.00 107.52 ? 332  LYS B O   1 
ATOM   6180  C  CB  . LYS B 1 357 ? 93.789  92.775  164.118 1.00 102.83 ? 332  LYS B CB  1 
ATOM   6181  C  CG  . LYS B 1 357 ? 92.464  92.642  163.386 1.00 103.93 ? 332  LYS B CG  1 
ATOM   6182  C  CD  . LYS B 1 357 ? 91.288  92.755  164.340 1.00 104.08 ? 332  LYS B CD  1 
ATOM   6183  C  CE  . LYS B 1 357 ? 89.986  92.366  163.657 1.00 104.79 ? 332  LYS B CE  1 
ATOM   6184  N  NZ  . LYS B 1 357 ? 88.822  92.462  164.581 1.00 104.72 ? 332  LYS B NZ  1 
ATOM   6185  N  N   . SER B 1 358 ? 95.511  89.980  164.104 1.00 96.20  ? 333  SER B N   1 
ATOM   6186  C  CA  . SER B 1 358 ? 96.786  89.355  163.788 1.00 97.66  ? 333  SER B CA  1 
ATOM   6187  C  C   . SER B 1 358 ? 97.586  90.234  162.834 1.00 97.25  ? 333  SER B C   1 
ATOM   6188  O  O   . SER B 1 358 ? 97.042  91.100  162.146 1.00 97.84  ? 333  SER B O   1 
ATOM   6189  C  CB  . SER B 1 358 ? 96.575  87.968  163.183 1.00 96.99  ? 333  SER B CB  1 
ATOM   6190  O  OG  . SER B 1 358 ? 97.790  87.446  162.673 1.00 97.35  ? 333  SER B OG  1 
ATOM   6191  N  N   . SER B 1 359 ? 98.898  89.989  162.793 1.00 87.10  ? 334  SER B N   1 
ATOM   6192  C  CA  . SER B 1 359 ? 99.826  90.911  162.147 1.00 85.49  ? 334  SER B CA  1 
ATOM   6193  C  C   . SER B 1 359 ? 99.592  91.055  160.648 1.00 87.10  ? 334  SER B C   1 
ATOM   6194  O  O   . SER B 1 359 ? 100.042 92.044  160.061 1.00 88.28  ? 334  SER B O   1 
ATOM   6195  C  CB  . SER B 1 359 ? 101.265 90.462  162.400 1.00 85.35  ? 334  SER B CB  1 
ATOM   6196  O  OG  . SER B 1 359 ? 101.536 89.233  161.750 1.00 88.82  ? 334  SER B OG  1 
ATOM   6197  N  N   . ARG B 1 360 ? 98.909  90.106  160.010 1.00 86.30  ? 335  ARG B N   1 
ATOM   6198  C  CA  . ARG B 1 360 ? 98.779  90.146  158.559 1.00 85.49  ? 335  ARG B CA  1 
ATOM   6199  C  C   . ARG B 1 360 ? 97.475  90.770  158.078 1.00 83.96  ? 335  ARG B C   1 
ATOM   6200  O  O   . ARG B 1 360 ? 97.407  91.200  156.921 1.00 83.58  ? 335  ARG B O   1 
ATOM   6201  C  CB  . ARG B 1 360 ? 98.909  88.736  157.974 1.00 84.23  ? 335  ARG B CB  1 
ATOM   6202  C  CG  . ARG B 1 360 ? 100.337 88.215  157.936 1.00 83.65  ? 335  ARG B CG  1 
ATOM   6203  C  CD  . ARG B 1 360 ? 101.276 89.205  157.260 1.00 85.11  ? 335  ARG B CD  1 
ATOM   6204  N  NE  . ARG B 1 360 ? 101.433 88.937  155.835 1.00 86.52  ? 335  ARG B NE  1 
ATOM   6205  C  CZ  . ARG B 1 360 ? 101.288 89.848  154.883 1.00 84.63  ? 335  ARG B CZ  1 
ATOM   6206  N  NH1 . ARG B 1 360 ? 100.980 91.103  155.167 1.00 83.40  ? 335  ARG B NH1 1 
ATOM   6207  N  NH2 . ARG B 1 360 ? 101.455 89.491  153.613 1.00 84.59  ? 335  ARG B NH2 1 
ATOM   6208  N  N   . GLU B 1 361 ? 96.442  90.831  158.920 1.00 89.36  ? 336  GLU B N   1 
ATOM   6209  C  CA  . GLU B 1 361 ? 95.186  91.431  158.482 1.00 89.65  ? 336  GLU B CA  1 
ATOM   6210  C  C   . GLU B 1 361 ? 95.255  92.954  158.453 1.00 91.13  ? 336  GLU B C   1 
ATOM   6211  O  O   . GLU B 1 361 ? 94.696  93.580  157.546 1.00 93.45  ? 336  GLU B O   1 
ATOM   6212  C  CB  . GLU B 1 361 ? 94.031  90.965  159.370 1.00 90.05  ? 336  GLU B CB  1 
ATOM   6213  C  CG  . GLU B 1 361 ? 93.500  89.582  159.018 1.00 91.58  ? 336  GLU B CG  1 
ATOM   6214  C  CD  . GLU B 1 361 ? 94.254  88.470  159.710 1.00 92.28  ? 336  GLU B CD  1 
ATOM   6215  O  OE1 . GLU B 1 361 ? 94.755  88.706  160.826 1.00 91.37  ? 336  GLU B OE1 1 
ATOM   6216  O  OE2 . GLU B 1 361 ? 94.345  87.362  159.140 1.00 91.46  ? 336  GLU B OE2 1 
ATOM   6217  N  N   . LEU B 1 362 ? 95.928  93.569  159.422 1.00 80.41  ? 337  LEU B N   1 
ATOM   6218  C  CA  . LEU B 1 362 ? 96.011  95.023  159.477 1.00 77.71  ? 337  LEU B CA  1 
ATOM   6219  C  C   . LEU B 1 362 ? 97.154  95.581  158.641 1.00 73.98  ? 337  LEU B C   1 
ATOM   6220  O  O   . LEU B 1 362 ? 97.323  96.803  158.585 1.00 76.00  ? 337  LEU B O   1 
ATOM   6221  C  CB  . LEU B 1 362 ? 96.149  95.506  160.927 1.00 77.35  ? 337  LEU B CB  1 
ATOM   6222  C  CG  . LEU B 1 362 ? 97.516  95.496  161.615 1.00 73.85  ? 337  LEU B CG  1 
ATOM   6223  C  CD1 . LEU B 1 362 ? 97.434  96.218  162.952 1.00 74.62  ? 337  LEU B CD1 1 
ATOM   6224  C  CD2 . LEU B 1 362 ? 98.037  94.089  161.811 1.00 75.89  ? 337  LEU B CD2 1 
ATOM   6225  N  N   . VAL B 1 363 ? 97.936  94.722  157.994 1.00 75.23  ? 338  VAL B N   1 
ATOM   6226  C  CA  . VAL B 1 363 ? 98.981  95.175  157.081 1.00 76.24  ? 338  VAL B CA  1 
ATOM   6227  C  C   . VAL B 1 363 ? 98.496  95.157  155.638 1.00 78.82  ? 338  VAL B C   1 
ATOM   6228  O  O   . VAL B 1 363 ? 98.815  96.057  154.857 1.00 79.85  ? 338  VAL B O   1 
ATOM   6229  C  CB  . VAL B 1 363 ? 100.245 94.312  157.265 1.00 77.59  ? 338  VAL B CB  1 
ATOM   6230  C  CG1 . VAL B 1 363 ? 101.163 94.432  156.060 1.00 78.07  ? 338  VAL B CG1 1 
ATOM   6231  C  CG2 . VAL B 1 363 ? 100.975 94.720  158.527 1.00 76.08  ? 338  VAL B CG2 1 
ATOM   6232  N  N   . ASP B 1 364 ? 97.701  94.150  155.273 1.00 87.49  ? 339  ASP B N   1 
ATOM   6233  C  CA  . ASP B 1 364 ? 97.192  94.029  153.913 1.00 87.69  ? 339  ASP B CA  1 
ATOM   6234  C  C   . ASP B 1 364 ? 96.194  95.122  153.554 1.00 84.79  ? 339  ASP B C   1 
ATOM   6235  O  O   . ASP B 1 364 ? 95.851  95.254  152.374 1.00 84.31  ? 339  ASP B O   1 
ATOM   6236  C  CB  . ASP B 1 364 ? 96.545  92.657  153.719 1.00 86.27  ? 339  ASP B CB  1 
ATOM   6237  C  CG  . ASP B 1 364 ? 97.344  91.764  152.793 1.00 86.67  ? 339  ASP B CG  1 
ATOM   6238  O  OD1 . ASP B 1 364 ? 98.211  92.287  152.064 1.00 89.40  ? 339  ASP B OD1 1 
ATOM   6239  O  OD2 . ASP B 1 364 ? 97.107  90.538  152.796 1.00 86.25  ? 339  ASP B OD2 1 
ATOM   6240  N  N   . GLN B 1 365 ? 95.719  95.893  154.529 1.00 82.64  ? 340  GLN B N   1 
ATOM   6241  C  CA  . GLN B 1 365 ? 94.799  96.983  154.237 1.00 83.08  ? 340  GLN B CA  1 
ATOM   6242  C  C   . GLN B 1 365 ? 95.473  98.023  153.352 1.00 84.58  ? 340  GLN B C   1 
ATOM   6243  O  O   . GLN B 1 365 ? 96.663  98.315  153.500 1.00 85.83  ? 340  GLN B O   1 
ATOM   6244  C  CB  . GLN B 1 365 ? 94.312  97.629  155.533 1.00 83.66  ? 340  GLN B CB  1 
ATOM   6245  C  CG  . GLN B 1 365 ? 93.815  96.639  156.572 1.00 85.46  ? 340  GLN B CG  1 
ATOM   6246  C  CD  . GLN B 1 365 ? 92.591  95.877  156.110 1.00 85.53  ? 340  GLN B CD  1 
ATOM   6247  O  OE1 . GLN B 1 365 ? 91.757  96.406  155.376 1.00 85.31  ? 340  GLN B OE1 1 
ATOM   6248  N  NE2 . GLN B 1 365 ? 92.477  94.625  156.536 1.00 85.63  ? 340  GLN B NE2 1 
ATOM   6249  N  N   . ASP B 1 366 ? 94.701  98.584  152.425 1.00 83.88  ? 341  ASP B N   1 
ATOM   6250  C  CA  . ASP B 1 366 ? 95.208  99.551  151.453 1.00 83.16  ? 341  ASP B CA  1 
ATOM   6251  C  C   . ASP B 1 366 ? 94.770  100.941 151.903 1.00 83.88  ? 341  ASP B C   1 
ATOM   6252  O  O   . ASP B 1 366 ? 93.726  101.448 151.492 1.00 85.21  ? 341  ASP B O   1 
ATOM   6253  C  CB  . ASP B 1 366 ? 94.703  99.219  150.053 1.00 83.72  ? 341  ASP B CB  1 
ATOM   6254  C  CG  . ASP B 1 366 ? 95.435  99.984  148.965 1.00 86.57  ? 341  ASP B CG  1 
ATOM   6255  O  OD1 . ASP B 1 366 ? 96.024  101.043 149.264 1.00 84.72  ? 341  ASP B OD1 1 
ATOM   6256  O  OD2 . ASP B 1 366 ? 95.424  99.520  147.806 1.00 86.78  ? 341  ASP B OD2 1 
ATOM   6257  N  N   . VAL B 1 367 ? 95.580  101.559 152.756 1.00 68.14  ? 342  VAL B N   1 
ATOM   6258  C  CA  . VAL B 1 367 ? 95.352  102.926 153.210 1.00 67.11  ? 342  VAL B CA  1 
ATOM   6259  C  C   . VAL B 1 367 ? 96.278  103.829 152.407 1.00 66.24  ? 342  VAL B C   1 
ATOM   6260  O  O   . VAL B 1 367 ? 97.496  103.834 152.618 1.00 68.41  ? 342  VAL B O   1 
ATOM   6261  C  CB  . VAL B 1 367 ? 95.593  103.072 154.717 1.00 65.78  ? 342  VAL B CB  1 
ATOM   6262  C  CG1 . VAL B 1 367 ? 95.418  104.519 155.141 1.00 65.33  ? 342  VAL B CG1 1 
ATOM   6263  C  CG2 . VAL B 1 367 ? 94.649  102.169 155.492 1.00 67.85  ? 342  VAL B CG2 1 
ATOM   6264  N  N   . GLN B 1 368 ? 95.702  104.598 151.484 1.00 56.92  ? 343  GLN B N   1 
ATOM   6265  C  CA  . GLN B 1 368 ? 96.482  105.412 150.565 1.00 56.90  ? 343  GLN B CA  1 
ATOM   6266  C  C   . GLN B 1 368 ? 96.607  106.828 151.098 1.00 57.78  ? 343  GLN B C   1 
ATOM   6267  O  O   . GLN B 1 368 ? 95.582  107.463 151.389 1.00 57.25  ? 343  GLN B O   1 
ATOM   6268  C  CB  . GLN B 1 368 ? 95.836  105.427 149.185 1.00 55.06  ? 343  GLN B CB  1 
ATOM   6269  C  CG  . GLN B 1 368 ? 96.819  105.617 148.043 1.00 58.48  ? 343  GLN B CG  1 
ATOM   6270  C  CD  . GLN B 1 368 ? 97.534  104.336 147.665 1.00 60.68  ? 343  GLN B CD  1 
ATOM   6271  O  OE1 . GLN B 1 368 ? 97.419  103.322 148.350 1.00 60.35  ? 343  GLN B OE1 1 
ATOM   6272  N  NE2 . GLN B 1 368 ? 98.279  104.377 146.567 1.00 60.96  ? 343  GLN B NE2 1 
ATOM   6273  N  N   . PRO B 1 369 ? 97.816  107.357 151.247 1.00 46.09  ? 344  PRO B N   1 
ATOM   6274  C  CA  . PRO B 1 369 ? 97.976  108.757 151.638 1.00 39.67  ? 344  PRO B CA  1 
ATOM   6275  C  C   . PRO B 1 369 ? 97.895  109.676 150.427 1.00 42.44  ? 344  PRO B C   1 
ATOM   6276  O  O   . PRO B 1 369 ? 97.919  109.241 149.275 1.00 41.32  ? 344  PRO B O   1 
ATOM   6277  C  CB  . PRO B 1 369 ? 99.373  108.780 152.259 1.00 37.90  ? 344  PRO B CB  1 
ATOM   6278  C  CG  . PRO B 1 369 ? 100.119 107.747 151.477 1.00 35.79  ? 344  PRO B CG  1 
ATOM   6279  C  CD  . PRO B 1 369 ? 99.115  106.678 151.092 1.00 43.43  ? 344  PRO B CD  1 
ATOM   6280  N  N   . ALA B 1 370 ? 97.791  110.971 150.711 1.00 36.48  ? 345  ALA B N   1 
ATOM   6281  C  CA  . ALA B 1 370 ? 97.823  111.964 149.650 1.00 33.56  ? 345  ALA B CA  1 
ATOM   6282  C  C   . ALA B 1 370 ? 99.173  111.924 148.940 1.00 37.35  ? 345  ALA B C   1 
ATOM   6283  O  O   . ALA B 1 370 ? 100.182 111.481 149.493 1.00 48.04  ? 345  ALA B O   1 
ATOM   6284  C  CB  . ALA B 1 370 ? 97.557  113.360 150.210 1.00 30.88  ? 345  ALA B CB  1 
ATOM   6285  N  N   . ARG B 1 371 ? 99.180  112.384 147.692 1.00 30.97  ? 346  ARG B N   1 
ATOM   6286  C  CA  . ARG B 1 371 ? 100.392 112.317 146.888 1.00 30.81  ? 346  ARG B CA  1 
ATOM   6287  C  C   . ARG B 1 371 ? 101.500 113.152 147.519 1.00 38.40  ? 346  ARG B C   1 
ATOM   6288  O  O   . ARG B 1 371 ? 101.250 114.217 148.090 1.00 45.90  ? 346  ARG B O   1 
ATOM   6289  C  CB  . ARG B 1 371 ? 100.111 112.793 145.463 1.00 34.26  ? 346  ARG B CB  1 
ATOM   6290  C  CG  . ARG B 1 371 ? 99.690  111.677 144.519 1.00 34.63  ? 346  ARG B CG  1 
ATOM   6291  C  CD  . ARG B 1 371 ? 99.437  112.191 143.110 1.00 36.35  ? 346  ARG B CD  1 
ATOM   6292  N  NE  . ARG B 1 371 ? 100.661 112.642 142.459 1.00 33.73  ? 346  ARG B NE  1 
ATOM   6293  C  CZ  . ARG B 1 371 ? 101.586 111.833 141.960 1.00 39.74  ? 346  ARG B CZ  1 
ATOM   6294  N  NH1 . ARG B 1 371 ? 101.460 110.518 142.019 1.00 39.69  ? 346  ARG B NH1 1 
ATOM   6295  N  NH2 . ARG B 1 371 ? 102.666 112.357 141.387 1.00 36.93  ? 346  ARG B NH2 1 
ATOM   6296  N  N   . TYR B 1 372 ? 102.730 112.643 147.425 1.00 36.41  ? 347  TYR B N   1 
ATOM   6297  C  CA  . TYR B 1 372 ? 103.916 113.279 148.003 1.00 32.38  ? 347  TYR B CA  1 
ATOM   6298  C  C   . TYR B 1 372 ? 103.808 113.413 149.519 1.00 41.13  ? 347  TYR B C   1 
ATOM   6299  O  O   . TYR B 1 372 ? 104.389 114.324 150.114 1.00 50.51  ? 347  TYR B O   1 
ATOM   6300  C  CB  . TYR B 1 372 ? 104.188 114.645 147.365 1.00 29.14  ? 347  TYR B CB  1 
ATOM   6301  C  CG  . TYR B 1 372 ? 104.153 114.637 145.855 1.00 31.71  ? 347  TYR B CG  1 
ATOM   6302  C  CD1 . TYR B 1 372 ? 104.684 113.579 145.135 1.00 36.38  ? 347  TYR B CD1 1 
ATOM   6303  C  CD2 . TYR B 1 372 ? 103.586 115.688 145.151 1.00 31.06  ? 347  TYR B CD2 1 
ATOM   6304  C  CE1 . TYR B 1 372 ? 104.652 113.568 143.757 1.00 37.81  ? 347  TYR B CE1 1 
ATOM   6305  C  CE2 . TYR B 1 372 ? 103.549 115.685 143.773 1.00 34.04  ? 347  TYR B CE2 1 
ATOM   6306  C  CZ  . TYR B 1 372 ? 104.084 114.623 143.082 1.00 36.67  ? 347  TYR B CZ  1 
ATOM   6307  O  OH  . TYR B 1 372 ? 104.050 114.615 141.707 1.00 39.67  ? 347  TYR B OH  1 
ATOM   6308  N  N   . HIS B 1 373 ? 103.064 112.512 150.157 1.00 30.53  ? 348  HIS B N   1 
ATOM   6309  C  CA  . HIS B 1 373 ? 102.945 112.454 151.608 1.00 28.43  ? 348  HIS B CA  1 
ATOM   6310  C  C   . HIS B 1 373 ? 103.052 111.001 152.055 1.00 38.03  ? 348  HIS B C   1 
ATOM   6311  O  O   . HIS B 1 373 ? 103.252 110.092 151.245 1.00 41.09  ? 348  HIS B O   1 
ATOM   6312  C  CB  . HIS B 1 373 ? 101.630 113.077 152.093 1.00 23.59  ? 348  HIS B CB  1 
ATOM   6313  C  CG  . HIS B 1 373 ? 101.553 114.560 151.909 1.00 31.98  ? 348  HIS B CG  1 
ATOM   6314  N  ND1 . HIS B 1 373 ? 101.608 115.163 150.671 1.00 39.47  ? 348  HIS B ND1 1 
ATOM   6315  C  CD2 . HIS B 1 373 ? 101.423 115.563 152.809 1.00 36.95  ? 348  HIS B CD2 1 
ATOM   6316  C  CE1 . HIS B 1 373 ? 101.517 116.473 150.816 1.00 34.88  ? 348  HIS B CE1 1 
ATOM   6317  N  NE2 . HIS B 1 373 ? 101.404 116.742 152.104 1.00 39.40  ? 348  HIS B NE2 1 
ATOM   6318  N  N   . ILE B 1 374 ? 102.916 110.783 153.361 1.00 35.37  ? 349  ILE B N   1 
ATOM   6319  C  CA  . ILE B 1 374 ? 102.969 109.448 153.941 1.00 31.93  ? 349  ILE B CA  1 
ATOM   6320  C  C   . ILE B 1 374 ? 101.763 109.250 154.846 1.00 37.68  ? 349  ILE B C   1 
ATOM   6321  O  O   . ILE B 1 374 ? 101.210 110.207 155.398 1.00 40.26  ? 349  ILE B O   1 
ATOM   6322  C  CB  . ILE B 1 374 ? 104.274 109.206 154.729 1.00 28.30  ? 349  ILE B CB  1 
ATOM   6323  C  CG1 . ILE B 1 374 ? 104.531 110.359 155.698 1.00 33.26  ? 349  ILE B CG1 1 
ATOM   6324  C  CG2 . ILE B 1 374 ? 105.445 109.023 153.782 1.00 30.37  ? 349  ILE B CG2 1 
ATOM   6325  C  CD1 . ILE B 1 374 ? 105.428 109.992 156.853 1.00 35.02  ? 349  ILE B CD1 1 
ATOM   6326  N  N   . ALA B 1 375 ? 101.358 107.990 154.999 1.00 40.47  ? 350  ALA B N   1 
ATOM   6327  C  CA  . ALA B 1 375 ? 100.241 107.638 155.869 1.00 38.45  ? 350  ALA B CA  1 
ATOM   6328  C  C   . ALA B 1 375 ? 100.727 107.246 157.261 1.00 41.04  ? 350  ALA B C   1 
ATOM   6329  O  O   . ALA B 1 375 ? 100.311 107.837 158.262 1.00 48.34  ? 350  ALA B O   1 
ATOM   6330  C  CB  . ALA B 1 375 ? 99.423  106.504 155.243 1.00 42.51  ? 350  ALA B CB  1 
ATOM   6331  N  N   . PHE B 1 376 ? 101.607 106.252 157.336 1.00 41.75  ? 351  PHE B N   1 
ATOM   6332  C  CA  . PHE B 1 376 ? 102.170 105.779 158.596 1.00 41.00  ? 351  PHE B CA  1 
ATOM   6333  C  C   . PHE B 1 376 ? 103.662 106.086 158.598 1.00 39.17  ? 351  PHE B C   1 
ATOM   6334  O  O   . PHE B 1 376 ? 104.425 105.504 157.820 1.00 45.65  ? 351  PHE B O   1 
ATOM   6335  C  CB  . PHE B 1 376 ? 101.909 104.287 158.784 1.00 45.19  ? 351  PHE B CB  1 
ATOM   6336  C  CG  . PHE B 1 376 ? 100.451 103.929 158.819 1.00 46.53  ? 351  PHE B CG  1 
ATOM   6337  C  CD1 . PHE B 1 376 ? 99.661  104.296 159.894 1.00 46.63  ? 351  PHE B CD1 1 
ATOM   6338  C  CD2 . PHE B 1 376 ? 99.870  103.230 157.775 1.00 46.90  ? 351  PHE B CD2 1 
ATOM   6339  C  CE1 . PHE B 1 376 ? 98.320  103.970 159.928 1.00 45.44  ? 351  PHE B CE1 1 
ATOM   6340  C  CE2 . PHE B 1 376 ? 98.531  102.901 157.805 1.00 46.58  ? 351  PHE B CE2 1 
ATOM   6341  C  CZ  . PHE B 1 376 ? 97.755  103.272 158.883 1.00 46.58  ? 351  PHE B CZ  1 
ATOM   6342  N  N   . GLY B 1 377 ? 104.072 106.998 159.473 1.00 32.57  ? 352  GLY B N   1 
ATOM   6343  C  CA  . GLY B 1 377 ? 105.452 107.401 159.578 1.00 33.29  ? 352  GLY B CA  1 
ATOM   6344  C  C   . GLY B 1 377 ? 105.724 108.059 160.913 1.00 40.35  ? 352  GLY B C   1 
ATOM   6345  O  O   . GLY B 1 377 ? 104.912 107.985 161.839 1.00 52.65  ? 352  GLY B O   1 
ATOM   6346  N  N   . PRO B 1 378 ? 106.881 108.704 161.044 1.00 28.58  ? 353  PRO B N   1 
ATOM   6347  C  CA  . PRO B 1 378 ? 107.184 109.416 162.290 1.00 30.96  ? 353  PRO B CA  1 
ATOM   6348  C  C   . PRO B 1 378 ? 106.144 110.488 162.574 1.00 38.23  ? 353  PRO B C   1 
ATOM   6349  O  O   . PRO B 1 378 ? 105.640 111.148 161.664 1.00 46.26  ? 353  PRO B O   1 
ATOM   6350  C  CB  . PRO B 1 378 ? 108.565 110.024 162.022 1.00 27.97  ? 353  PRO B CB  1 
ATOM   6351  C  CG  . PRO B 1 378 ? 109.155 109.152 160.971 1.00 29.58  ? 353  PRO B CG  1 
ATOM   6352  C  CD  . PRO B 1 378 ? 108.009 108.738 160.102 1.00 28.77  ? 353  PRO B CD  1 
ATOM   6353  N  N   . VAL B 1 379 ? 105.813 110.646 163.853 1.00 40.14  ? 354  VAL B N   1 
ATOM   6354  C  CA  . VAL B 1 379 ? 104.776 111.571 164.294 1.00 40.75  ? 354  VAL B CA  1 
ATOM   6355  C  C   . VAL B 1 379 ? 105.357 112.463 165.380 1.00 49.36  ? 354  VAL B C   1 
ATOM   6356  O  O   . VAL B 1 379 ? 106.029 111.976 166.295 1.00 53.91  ? 354  VAL B O   1 
ATOM   6357  C  CB  . VAL B 1 379 ? 103.531 110.829 164.818 1.00 48.05  ? 354  VAL B CB  1 
ATOM   6358  C  CG1 . VAL B 1 379 ? 102.451 111.821 165.207 1.00 53.30  ? 354  VAL B CG1 1 
ATOM   6359  C  CG2 . VAL B 1 379 ? 103.010 109.856 163.775 1.00 47.76  ? 354  VAL B CG2 1 
ATOM   6360  N  N   . VAL B 1 380 ? 105.098 113.763 165.278 1.00 51.91  ? 355  VAL B N   1 
ATOM   6361  C  CA  . VAL B 1 380 ? 105.547 114.715 166.289 1.00 53.79  ? 355  VAL B CA  1 
ATOM   6362  C  C   . VAL B 1 380 ? 104.653 114.584 167.517 1.00 56.04  ? 355  VAL B C   1 
ATOM   6363  O  O   . VAL B 1 380 ? 103.460 114.901 167.470 1.00 58.51  ? 355  VAL B O   1 
ATOM   6364  C  CB  . VAL B 1 380 ? 105.543 116.149 165.741 1.00 51.56  ? 355  VAL B CB  1 
ATOM   6365  C  CG1 . VAL B 1 380 ? 106.779 116.384 164.900 1.00 53.53  ? 355  VAL B CG1 1 
ATOM   6366  C  CG2 . VAL B 1 380 ? 104.298 116.399 164.907 1.00 53.26  ? 355  VAL B CG2 1 
ATOM   6367  N  N   . ASP B 1 381 ? 105.223 114.108 168.611 1.00 67.96  ? 356  ASP B N   1 
ATOM   6368  C  CA  . ASP B 1 381 ? 104.460 113.878 169.833 1.00 69.50  ? 356  ASP B CA  1 
ATOM   6369  C  C   . ASP B 1 381 ? 105.039 114.587 171.046 1.00 73.37  ? 356  ASP B C   1 
ATOM   6370  O  O   . ASP B 1 381 ? 104.279 115.101 171.870 1.00 77.68  ? 356  ASP B O   1 
ATOM   6371  C  CB  . ASP B 1 381 ? 104.372 112.372 170.108 1.00 69.11  ? 356  ASP B CB  1 
ATOM   6372  C  CG  . ASP B 1 381 ? 105.727 111.699 170.078 1.00 75.69  ? 356  ASP B CG  1 
ATOM   6373  O  OD1 . ASP B 1 381 ? 106.534 111.939 171.000 1.00 74.78  ? 356  ASP B OD1 1 
ATOM   6374  O  OD2 . ASP B 1 381 ? 105.989 110.935 169.128 1.00 79.00  ? 356  ASP B OD2 1 
ATOM   6375  N  N   . GLY B 1 382 ? 106.362 114.629 171.178 1.00 71.36  ? 357  GLY B N   1 
ATOM   6376  C  CA  . GLY B 1 382 ? 106.985 115.243 172.333 1.00 73.56  ? 357  GLY B CA  1 
ATOM   6377  C  C   . GLY B 1 382 ? 107.981 114.332 173.020 1.00 76.99  ? 357  GLY B C   1 
ATOM   6378  O  O   . GLY B 1 382 ? 108.905 114.804 173.689 1.00 76.27  ? 357  GLY B O   1 
ATOM   6379  N  N   . ASP B 1 383 ? 107.803 113.020 172.864 1.00 80.07  ? 358  ASP B N   1 
ATOM   6380  C  CA  . ASP B 1 383 ? 108.727 112.065 173.467 1.00 80.11  ? 358  ASP B CA  1 
ATOM   6381  C  C   . ASP B 1 383 ? 109.970 111.881 172.603 1.00 77.41  ? 358  ASP B C   1 
ATOM   6382  O  O   . ASP B 1 383 ? 111.089 112.179 173.034 1.00 76.27  ? 358  ASP B O   1 
ATOM   6383  C  CB  . ASP B 1 383 ? 108.023 110.724 173.693 1.00 79.45  ? 358  ASP B CB  1 
ATOM   6384  C  CG  . ASP B 1 383 ? 108.758 109.836 174.679 1.00 81.65  ? 358  ASP B CG  1 
ATOM   6385  O  OD1 . ASP B 1 383 ? 109.761 110.297 175.264 1.00 82.45  ? 358  ASP B OD1 1 
ATOM   6386  O  OD2 . ASP B 1 383 ? 108.333 108.677 174.868 1.00 80.54  ? 358  ASP B OD2 1 
ATOM   6387  N  N   . VAL B 1 384 ? 109.789 111.398 171.378 1.00 67.52  ? 359  VAL B N   1 
ATOM   6388  C  CA  . VAL B 1 384 ? 110.910 111.198 170.465 1.00 69.47  ? 359  VAL B CA  1 
ATOM   6389  C  C   . VAL B 1 384 ? 111.186 112.453 169.651 1.00 72.42  ? 359  VAL B C   1 
ATOM   6390  O  O   . VAL B 1 384 ? 112.320 112.934 169.595 1.00 76.49  ? 359  VAL B O   1 
ATOM   6391  C  CB  . VAL B 1 384 ? 110.638 109.984 169.552 1.00 70.76  ? 359  VAL B CB  1 
ATOM   6392  C  CG1 . VAL B 1 384 ? 111.823 109.736 168.635 1.00 65.57  ? 359  VAL B CG1 1 
ATOM   6393  C  CG2 . VAL B 1 384 ? 110.339 108.754 170.386 1.00 69.88  ? 359  VAL B CG2 1 
ATOM   6394  N  N   . VAL B 1 385 ? 110.159 113.005 169.015 1.00 66.34  ? 360  VAL B N   1 
ATOM   6395  C  CA  . VAL B 1 385 ? 110.297 114.249 168.265 1.00 64.92  ? 360  VAL B CA  1 
ATOM   6396  C  C   . VAL B 1 385 ? 109.529 115.328 169.020 1.00 67.41  ? 360  VAL B C   1 
ATOM   6397  O  O   . VAL B 1 385 ? 108.292 115.360 168.962 1.00 72.07  ? 360  VAL B O   1 
ATOM   6398  C  CB  . VAL B 1 385 ? 109.789 114.094 166.823 1.00 61.24  ? 360  VAL B CB  1 
ATOM   6399  C  CG1 . VAL B 1 385 ? 110.373 115.177 165.938 1.00 61.59  ? 360  VAL B CG1 1 
ATOM   6400  C  CG2 . VAL B 1 385 ? 110.137 112.717 166.284 1.00 58.91  ? 360  VAL B CG2 1 
ATOM   6401  N  N   . PRO B 1 386 ? 110.215 116.216 169.752 1.00 59.73  ? 361  PRO B N   1 
ATOM   6402  C  CA  . PRO B 1 386 ? 109.508 117.216 170.568 1.00 60.04  ? 361  PRO B CA  1 
ATOM   6403  C  C   . PRO B 1 386 ? 108.592 118.115 169.754 1.00 60.80  ? 361  PRO B C   1 
ATOM   6404  O  O   . PRO B 1 386 ? 107.390 118.196 170.025 1.00 63.11  ? 361  PRO B O   1 
ATOM   6405  C  CB  . PRO B 1 386 ? 110.651 118.015 171.208 1.00 62.25  ? 361  PRO B CB  1 
ATOM   6406  C  CG  . PRO B 1 386 ? 111.824 117.095 171.177 1.00 60.89  ? 361  PRO B CG  1 
ATOM   6407  C  CD  . PRO B 1 386 ? 111.674 116.285 169.928 1.00 57.71  ? 361  PRO B CD  1 
ATOM   6408  N  N   . ASP B 1 387 ? 109.149 118.793 168.757 1.00 58.80  ? 362  ASP B N   1 
ATOM   6409  C  CA  . ASP B 1 387 ? 108.385 119.631 167.845 1.00 59.04  ? 362  ASP B CA  1 
ATOM   6410  C  C   . ASP B 1 387 ? 108.680 119.182 166.420 1.00 60.61  ? 362  ASP B C   1 
ATOM   6411  O  O   . ASP B 1 387 ? 109.401 118.207 166.194 1.00 61.88  ? 362  ASP B O   1 
ATOM   6412  C  CB  . ASP B 1 387 ? 108.718 121.115 168.042 1.00 56.00  ? 362  ASP B CB  1 
ATOM   6413  C  CG  . ASP B 1 387 ? 107.510 122.009 167.863 1.00 63.21  ? 362  ASP B CG  1 
ATOM   6414  O  OD1 . ASP B 1 387 ? 106.799 121.853 166.850 1.00 66.97  ? 362  ASP B OD1 1 
ATOM   6415  O  OD2 . ASP B 1 387 ? 107.271 122.870 168.735 1.00 65.27  ? 362  ASP B OD2 1 
ATOM   6416  N  N   . ASP B 1 388 ? 108.117 119.892 165.449 1.00 55.63  ? 363  ASP B N   1 
ATOM   6417  C  CA  . ASP B 1 388 ? 108.373 119.541 164.061 1.00 52.26  ? 363  ASP B CA  1 
ATOM   6418  C  C   . ASP B 1 388 ? 109.852 119.751 163.744 1.00 51.56  ? 363  ASP B C   1 
ATOM   6419  O  O   . ASP B 1 388 ? 110.469 120.692 164.257 1.00 54.82  ? 363  ASP B O   1 
ATOM   6420  C  CB  . ASP B 1 388 ? 107.498 120.368 163.117 1.00 51.09  ? 363  ASP B CB  1 
ATOM   6421  C  CG  . ASP B 1 388 ? 107.716 121.853 163.271 1.00 58.03  ? 363  ASP B CG  1 
ATOM   6422  O  OD1 . ASP B 1 388 ? 108.023 122.291 164.396 1.00 62.26  ? 363  ASP B OD1 1 
ATOM   6423  O  OD2 . ASP B 1 388 ? 107.577 122.582 162.267 1.00 61.73  ? 363  ASP B OD2 1 
ATOM   6424  N  N   . PRO B 1 389 ? 110.455 118.885 162.926 1.00 48.67  ? 364  PRO B N   1 
ATOM   6425  C  CA  . PRO B 1 389 ? 111.907 118.976 162.706 1.00 46.36  ? 364  PRO B CA  1 
ATOM   6426  C  C   . PRO B 1 389 ? 112.360 120.295 162.110 1.00 47.08  ? 364  PRO B C   1 
ATOM   6427  O  O   . PRO B 1 389 ? 113.495 120.714 162.366 1.00 50.82  ? 364  PRO B O   1 
ATOM   6428  C  CB  . PRO B 1 389 ? 112.189 117.804 161.756 1.00 44.98  ? 364  PRO B CB  1 
ATOM   6429  C  CG  . PRO B 1 389 ? 111.048 116.870 161.954 1.00 46.90  ? 364  PRO B CG  1 
ATOM   6430  C  CD  . PRO B 1 389 ? 109.862 117.738 162.224 1.00 51.57  ? 364  PRO B CD  1 
ATOM   6431  N  N   . GLU B 1 390 ? 111.516 120.961 161.320 1.00 49.35  ? 365  GLU B N   1 
ATOM   6432  C  CA  . GLU B 1 390 ? 111.920 122.223 160.708 1.00 44.65  ? 365  GLU B CA  1 
ATOM   6433  C  C   . GLU B 1 390 ? 112.206 123.282 161.765 1.00 49.07  ? 365  GLU B C   1 
ATOM   6434  O  O   . GLU B 1 390 ? 113.223 123.980 161.701 1.00 51.26  ? 365  GLU B O   1 
ATOM   6435  C  CB  . GLU B 1 390 ? 110.839 122.702 159.739 1.00 48.60  ? 365  GLU B CB  1 
ATOM   6436  C  CG  . GLU B 1 390 ? 110.990 124.149 159.303 1.00 52.96  ? 365  GLU B CG  1 
ATOM   6437  C  CD  . GLU B 1 390 ? 112.054 124.333 158.240 1.00 57.95  ? 365  GLU B CD  1 
ATOM   6438  O  OE1 . GLU B 1 390 ? 113.254 124.323 158.587 1.00 53.75  ? 365  GLU B OE1 1 
ATOM   6439  O  OE2 . GLU B 1 390 ? 111.690 124.488 157.056 1.00 58.66  ? 365  GLU B OE2 1 
ATOM   6440  N  N   . ILE B 1 391 ? 111.320 123.410 162.753 1.00 55.55  ? 366  ILE B N   1 
ATOM   6441  C  CA  . ILE B 1 391 ? 111.515 124.403 163.806 1.00 54.66  ? 366  ILE B CA  1 
ATOM   6442  C  C   . ILE B 1 391 ? 112.671 124.003 164.716 1.00 55.67  ? 366  ILE B C   1 
ATOM   6443  O  O   . ILE B 1 391 ? 113.449 124.854 165.164 1.00 56.60  ? 366  ILE B O   1 
ATOM   6444  C  CB  . ILE B 1 391 ? 110.209 124.601 164.596 1.00 50.31  ? 366  ILE B CB  1 
ATOM   6445  C  CG1 . ILE B 1 391 ? 109.179 125.343 163.744 1.00 55.90  ? 366  ILE B CG1 1 
ATOM   6446  C  CG2 . ILE B 1 391 ? 110.463 125.355 165.889 1.00 46.99  ? 366  ILE B CG2 1 
ATOM   6447  C  CD1 . ILE B 1 391 ? 109.663 126.678 163.226 1.00 55.68  ? 366  ILE B CD1 1 
ATOM   6448  N  N   . LEU B 1 392 ? 112.807 122.704 164.995 1.00 55.91  ? 367  LEU B N   1 
ATOM   6449  C  CA  . LEU B 1 392 ? 113.779 122.249 165.985 1.00 51.71  ? 367  LEU B CA  1 
ATOM   6450  C  C   . LEU B 1 392 ? 115.208 122.587 165.576 1.00 51.28  ? 367  LEU B C   1 
ATOM   6451  O  O   . LEU B 1 392 ? 116.006 123.037 166.405 1.00 57.42  ? 367  LEU B O   1 
ATOM   6452  C  CB  . LEU B 1 392 ? 113.633 120.745 166.207 1.00 50.15  ? 367  LEU B CB  1 
ATOM   6453  C  CG  . LEU B 1 392 ? 112.727 120.317 167.361 1.00 51.46  ? 367  LEU B CG  1 
ATOM   6454  C  CD1 . LEU B 1 392 ? 112.885 118.834 167.638 1.00 49.57  ? 367  LEU B CD1 1 
ATOM   6455  C  CD2 . LEU B 1 392 ? 113.025 121.133 168.606 1.00 53.22  ? 367  LEU B CD2 1 
ATOM   6456  N  N   . MET B 1 393 ? 115.553 122.378 164.304 1.00 42.68  ? 368  MET B N   1 
ATOM   6457  C  CA  . MET B 1 393 ? 116.926 122.607 163.873 1.00 45.98  ? 368  MET B CA  1 
ATOM   6458  C  C   . MET B 1 393 ? 117.257 124.084 163.714 1.00 50.72  ? 368  MET B C   1 
ATOM   6459  O  O   . MET B 1 393 ? 118.441 124.437 163.691 1.00 55.12  ? 368  MET B O   1 
ATOM   6460  C  CB  . MET B 1 393 ? 117.206 121.871 162.561 1.00 44.83  ? 368  MET B CB  1 
ATOM   6461  C  CG  . MET B 1 393 ? 116.165 122.086 161.484 1.00 50.48  ? 368  MET B CG  1 
ATOM   6462  S  SD  . MET B 1 393 ? 116.476 121.082 160.020 1.00 58.21  ? 368  MET B SD  1 
ATOM   6463  C  CE  . MET B 1 393 ? 116.867 119.504 160.770 1.00 39.74  ? 368  MET B CE  1 
ATOM   6464  N  N   . GLN B 1 394 ? 116.250 124.953 163.599 1.00 54.79  ? 369  GLN B N   1 
ATOM   6465  C  CA  . GLN B 1 394 ? 116.522 126.386 163.539 1.00 55.43  ? 369  GLN B CA  1 
ATOM   6466  C  C   . GLN B 1 394 ? 117.117 126.885 164.849 1.00 59.47  ? 369  GLN B C   1 
ATOM   6467  O  O   . GLN B 1 394 ? 118.118 127.611 164.854 1.00 59.15  ? 369  GLN B O   1 
ATOM   6468  C  CB  . GLN B 1 394 ? 115.243 127.155 163.207 1.00 53.15  ? 369  GLN B CB  1 
ATOM   6469  C  CG  . GLN B 1 394 ? 114.591 126.753 161.900 1.00 54.14  ? 369  GLN B CG  1 
ATOM   6470  C  CD  . GLN B 1 394 ? 114.443 127.914 160.941 1.00 60.53  ? 369  GLN B CD  1 
ATOM   6471  O  OE1 . GLN B 1 394 ? 115.196 128.885 161.004 1.00 61.32  ? 369  GLN B OE1 1 
ATOM   6472  N  NE2 . GLN B 1 394 ? 113.466 127.822 160.047 1.00 58.97  ? 369  GLN B NE2 1 
ATOM   6473  N  N   . GLN B 1 395 ? 116.513 126.506 165.971 1.00 64.57  ? 370  GLN B N   1 
ATOM   6474  C  CA  . GLN B 1 395 ? 116.963 126.959 167.287 1.00 61.79  ? 370  GLN B CA  1 
ATOM   6475  C  C   . GLN B 1 395 ? 117.936 125.974 167.929 1.00 59.70  ? 370  GLN B C   1 
ATOM   6476  O  O   . GLN B 1 395 ? 117.777 125.583 169.084 1.00 66.51  ? 370  GLN B O   1 
ATOM   6477  C  CB  . GLN B 1 395 ? 115.755 127.198 168.183 1.00 63.26  ? 370  GLN B CB  1 
ATOM   6478  C  CG  . GLN B 1 395 ? 114.554 127.760 167.446 1.00 62.87  ? 370  GLN B CG  1 
ATOM   6479  C  CD  . GLN B 1 395 ? 113.240 127.362 168.083 1.00 68.22  ? 370  GLN B CD  1 
ATOM   6480  O  OE1 . GLN B 1 395 ? 113.196 126.488 168.949 1.00 67.29  ? 370  GLN B OE1 1 
ATOM   6481  N  NE2 . GLN B 1 395 ? 112.158 128.002 167.656 1.00 69.71  ? 370  GLN B NE2 1 
ATOM   6482  N  N   . GLY B 1 396 ? 118.961 125.583 167.172 1.00 56.54  ? 371  GLY B N   1 
ATOM   6483  C  CA  . GLY B 1 396 ? 120.067 124.774 167.656 1.00 60.37  ? 371  GLY B CA  1 
ATOM   6484  C  C   . GLY B 1 396 ? 119.751 123.654 168.627 1.00 61.49  ? 371  GLY B C   1 
ATOM   6485  O  O   . GLY B 1 396 ? 120.421 123.524 169.655 1.00 66.61  ? 371  GLY B O   1 
ATOM   6486  N  N   . GLU B 1 397 ? 118.747 122.839 168.325 1.00 57.71  ? 372  GLU B N   1 
ATOM   6487  C  CA  . GLU B 1 397 ? 118.365 121.732 169.202 1.00 56.66  ? 372  GLU B CA  1 
ATOM   6488  C  C   . GLU B 1 397 ? 119.007 120.425 168.739 1.00 56.90  ? 372  GLU B C   1 
ATOM   6489  O  O   . GLU B 1 397 ? 118.342 119.471 168.339 1.00 57.74  ? 372  GLU B O   1 
ATOM   6490  C  CB  . GLU B 1 397 ? 116.846 121.613 169.273 1.00 58.07  ? 372  GLU B CB  1 
ATOM   6491  C  CG  . GLU B 1 397 ? 116.162 122.855 169.814 1.00 61.69  ? 372  GLU B CG  1 
ATOM   6492  C  CD  . GLU B 1 397 ? 115.707 122.690 171.250 1.00 65.34  ? 372  GLU B CD  1 
ATOM   6493  O  OE1 . GLU B 1 397 ? 115.055 121.671 171.555 1.00 67.14  ? 372  GLU B OE1 1 
ATOM   6494  O  OE2 . GLU B 1 397 ? 116.005 123.580 172.074 1.00 67.18  ? 372  GLU B OE2 1 
ATOM   6495  N  N   . PHE B 1 398 ? 120.336 120.400 168.800 1.00 52.98  ? 373  PHE B N   1 
ATOM   6496  C  CA  . PHE B 1 398 ? 121.110 119.206 168.489 1.00 51.74  ? 373  PHE B CA  1 
ATOM   6497  C  C   . PHE B 1 398 ? 122.446 119.307 169.211 1.00 52.91  ? 373  PHE B C   1 
ATOM   6498  O  O   . PHE B 1 398 ? 122.836 120.378 169.680 1.00 58.37  ? 373  PHE B O   1 
ATOM   6499  C  CB  . PHE B 1 398 ? 121.306 119.019 166.978 1.00 54.63  ? 373  PHE B CB  1 
ATOM   6500  C  CG  . PHE B 1 398 ? 121.387 120.305 166.203 1.00 49.30  ? 373  PHE B CG  1 
ATOM   6501  C  CD1 . PHE B 1 398 ? 120.239 120.938 165.757 1.00 45.85  ? 373  PHE B CD1 1 
ATOM   6502  C  CD2 . PHE B 1 398 ? 122.613 120.872 165.908 1.00 49.11  ? 373  PHE B CD2 1 
ATOM   6503  C  CE1 . PHE B 1 398 ? 120.313 122.114 165.044 1.00 46.28  ? 373  PHE B CE1 1 
ATOM   6504  C  CE2 . PHE B 1 398 ? 122.692 122.048 165.193 1.00 50.51  ? 373  PHE B CE2 1 
ATOM   6505  C  CZ  . PHE B 1 398 ? 121.541 122.670 164.761 1.00 45.90  ? 373  PHE B CZ  1 
ATOM   6506  N  N   . LEU B 1 399 ? 123.144 118.176 169.295 1.00 50.99  ? 374  LEU B N   1 
ATOM   6507  C  CA  . LEU B 1 399 ? 124.306 118.034 170.165 1.00 54.99  ? 374  LEU B CA  1 
ATOM   6508  C  C   . LEU B 1 399 ? 125.610 117.877 169.386 1.00 53.48  ? 374  LEU B C   1 
ATOM   6509  O  O   . LEU B 1 399 ? 126.478 117.086 169.760 1.00 51.87  ? 374  LEU B O   1 
ATOM   6510  C  CB  . LEU B 1 399 ? 124.118 116.858 171.118 1.00 54.84  ? 374  LEU B CB  1 
ATOM   6511  C  CG  . LEU B 1 399 ? 122.963 116.981 172.111 1.00 53.93  ? 374  LEU B CG  1 
ATOM   6512  C  CD1 . LEU B 1 399 ? 122.962 115.807 173.071 1.00 54.78  ? 374  LEU B CD1 1 
ATOM   6513  C  CD2 . LEU B 1 399 ? 123.037 118.294 172.869 1.00 56.17  ? 374  LEU B CD2 1 
ATOM   6514  N  N   . ASN B 1 400 ? 125.761 118.633 168.298 1.00 45.94  ? 375  ASN B N   1 
ATOM   6515  C  CA  . ASN B 1 400 ? 127.035 118.770 167.589 1.00 50.61  ? 375  ASN B CA  1 
ATOM   6516  C  C   . ASN B 1 400 ? 127.564 117.416 167.104 1.00 52.86  ? 375  ASN B C   1 
ATOM   6517  O  O   . ASN B 1 400 ? 128.609 116.931 167.542 1.00 53.30  ? 375  ASN B O   1 
ATOM   6518  C  CB  . ASN B 1 400 ? 128.067 119.481 168.472 1.00 50.39  ? 375  ASN B CB  1 
ATOM   6519  C  CG  . ASN B 1 400 ? 129.299 119.911 167.702 1.00 52.67  ? 375  ASN B CG  1 
ATOM   6520  O  OD1 . ASN B 1 400 ? 129.393 121.050 167.247 1.00 50.86  ? 375  ASN B OD1 1 
ATOM   6521  N  ND2 . ASN B 1 400 ? 130.254 119.000 167.555 1.00 53.99  ? 375  ASN B ND2 1 
ATOM   6522  N  N   . TYR B 1 401 ? 126.817 116.809 166.188 1.00 50.95  ? 376  TYR B N   1 
ATOM   6523  C  CA  . TYR B 1 401 ? 127.217 115.559 165.555 1.00 42.50  ? 376  TYR B CA  1 
ATOM   6524  C  C   . TYR B 1 401 ? 127.908 115.858 164.232 1.00 45.64  ? 376  TYR B C   1 
ATOM   6525  O  O   . TYR B 1 401 ? 127.399 116.644 163.427 1.00 48.13  ? 376  TYR B O   1 
ATOM   6526  C  CB  . TYR B 1 401 ? 126.011 114.650 165.309 1.00 39.51  ? 376  TYR B CB  1 
ATOM   6527  C  CG  . TYR B 1 401 ? 125.210 114.315 166.543 1.00 43.48  ? 376  TYR B CG  1 
ATOM   6528  C  CD1 . TYR B 1 401 ? 125.519 113.206 167.315 1.00 48.04  ? 376  TYR B CD1 1 
ATOM   6529  C  CD2 . TYR B 1 401 ? 124.136 115.102 166.928 1.00 47.88  ? 376  TYR B CD2 1 
ATOM   6530  C  CE1 . TYR B 1 401 ? 124.785 112.895 168.441 1.00 43.50  ? 376  TYR B CE1 1 
ATOM   6531  C  CE2 . TYR B 1 401 ? 123.397 114.799 168.052 1.00 49.33  ? 376  TYR B CE2 1 
ATOM   6532  C  CZ  . TYR B 1 401 ? 123.725 113.695 168.804 1.00 46.43  ? 376  TYR B CZ  1 
ATOM   6533  O  OH  . TYR B 1 401 ? 122.990 113.390 169.925 1.00 49.62  ? 376  TYR B OH  1 
ATOM   6534  N  N   . ASP B 1 402 ? 129.068 115.240 164.015 1.00 46.33  ? 377  ASP B N   1 
ATOM   6535  C  CA  . ASP B 1 402 ? 129.710 115.312 162.709 1.00 43.56  ? 377  ASP B CA  1 
ATOM   6536  C  C   . ASP B 1 402 ? 128.782 114.717 161.660 1.00 48.51  ? 377  ASP B C   1 
ATOM   6537  O  O   . ASP B 1 402 ? 128.280 113.602 161.823 1.00 62.43  ? 377  ASP B O   1 
ATOM   6538  C  CB  . ASP B 1 402 ? 131.041 114.564 162.728 1.00 41.84  ? 377  ASP B CB  1 
ATOM   6539  C  CG  . ASP B 1 402 ? 131.945 115.016 163.853 1.00 48.51  ? 377  ASP B CG  1 
ATOM   6540  O  OD1 . ASP B 1 402 ? 131.528 115.900 164.628 1.00 54.34  ? 377  ASP B OD1 1 
ATOM   6541  O  OD2 . ASP B 1 402 ? 133.072 114.491 163.963 1.00 43.25  ? 377  ASP B OD2 1 
ATOM   6542  N  N   . MET B 1 403 ? 128.558 115.457 160.578 1.00 42.00  ? 378  MET B N   1 
ATOM   6543  C  CA  . MET B 1 403 ? 127.480 115.138 159.655 1.00 41.20  ? 378  MET B CA  1 
ATOM   6544  C  C   . MET B 1 403 ? 127.962 115.189 158.211 1.00 35.44  ? 378  MET B C   1 
ATOM   6545  O  O   . MET B 1 403 ? 128.784 116.035 157.844 1.00 50.62  ? 378  MET B O   1 
ATOM   6546  C  CB  . MET B 1 403 ? 126.301 116.095 159.873 1.00 44.38  ? 378  MET B CB  1 
ATOM   6547  C  CG  . MET B 1 403 ? 125.269 116.075 158.776 1.00 48.81  ? 378  MET B CG  1 
ATOM   6548  S  SD  . MET B 1 403 ? 123.649 116.683 159.270 1.00 58.09  ? 378  MET B SD  1 
ATOM   6549  C  CE  . MET B 1 403 ? 122.803 115.143 159.610 1.00 48.30  ? 378  MET B CE  1 
ATOM   6550  N  N   . LEU B 1 404 ? 127.439 114.274 157.394 1.00 38.21  ? 379  LEU B N   1 
ATOM   6551  C  CA  . LEU B 1 404 ? 127.806 114.153 155.984 1.00 48.00  ? 379  LEU B CA  1 
ATOM   6552  C  C   . LEU B 1 404 ? 126.519 114.014 155.174 1.00 50.19  ? 379  LEU B C   1 
ATOM   6553  O  O   . LEU B 1 404 ? 125.932 112.930 155.113 1.00 61.83  ? 379  LEU B O   1 
ATOM   6554  C  CB  . LEU B 1 404 ? 128.740 112.964 155.769 1.00 49.99  ? 379  LEU B CB  1 
ATOM   6555  C  CG  . LEU B 1 404 ? 129.547 112.859 154.473 1.00 45.00  ? 379  LEU B CG  1 
ATOM   6556  C  CD1 . LEU B 1 404 ? 130.804 112.043 154.712 1.00 42.28  ? 379  LEU B CD1 1 
ATOM   6557  C  CD2 . LEU B 1 404 ? 128.727 112.240 153.359 1.00 50.41  ? 379  LEU B CD2 1 
ATOM   6558  N  N   . ILE B 1 405 ? 126.088 115.105 154.549 1.00 34.68  ? 380  ILE B N   1 
ATOM   6559  C  CA  . ILE B 1 405 ? 124.885 115.112 153.734 1.00 31.70  ? 380  ILE B CA  1 
ATOM   6560  C  C   . ILE B 1 405 ? 125.295 114.916 152.280 1.00 36.82  ? 380  ILE B C   1 
ATOM   6561  O  O   . ILE B 1 405 ? 126.433 115.178 151.881 1.00 57.52  ? 380  ILE B O   1 
ATOM   6562  C  CB  . ILE B 1 405 ? 124.064 116.419 153.908 1.00 40.88  ? 380  ILE B CB  1 
ATOM   6563  C  CG1 . ILE B 1 405 ? 123.793 116.718 155.377 1.00 39.95  ? 380  ILE B CG1 1 
ATOM   6564  C  CG2 . ILE B 1 405 ? 122.727 116.352 153.193 1.00 48.99  ? 380  ILE B CG2 1 
ATOM   6565  C  CD1 . ILE B 1 405 ? 124.648 117.820 155.906 1.00 50.96  ? 380  ILE B CD1 1 
ATOM   6566  N  N   . GLY B 1 406 ? 124.354 114.449 151.467 1.00 23.94  ? 381  GLY B N   1 
ATOM   6567  C  CA  . GLY B 1 406 ? 124.616 114.331 150.048 1.00 34.23  ? 381  GLY B CA  1 
ATOM   6568  C  C   . GLY B 1 406 ? 123.347 114.166 149.251 1.00 39.71  ? 381  GLY B C   1 
ATOM   6569  O  O   . GLY B 1 406 ? 122.289 113.815 149.781 1.00 50.41  ? 381  GLY B O   1 
ATOM   6570  N  N   . VAL B 1 407 ? 123.472 114.429 147.953 1.00 33.70  ? 382  VAL B N   1 
ATOM   6571  C  CA  . VAL B 1 407 ? 122.377 114.289 147.002 1.00 14.60  ? 382  VAL B CA  1 
ATOM   6572  C  C   . VAL B 1 407 ? 122.931 113.677 145.723 1.00 27.15  ? 382  VAL B C   1 
ATOM   6573  O  O   . VAL B 1 407 ? 124.141 113.557 145.544 1.00 46.78  ? 382  VAL B O   1 
ATOM   6574  C  CB  . VAL B 1 407 ? 121.687 115.633 146.696 1.00 18.14  ? 382  VAL B CB  1 
ATOM   6575  C  CG1 . VAL B 1 407 ? 120.935 116.133 147.912 1.00 32.69  ? 382  VAL B CG1 1 
ATOM   6576  C  CG2 . VAL B 1 407 ? 122.710 116.655 146.250 1.00 29.67  ? 382  VAL B CG2 1 
ATOM   6577  N  N   . ASN B 1 408 ? 122.029 113.276 144.838 1.00 23.98  ? 383  ASN B N   1 
ATOM   6578  C  CA  . ASN B 1 408 ? 122.395 112.816 143.507 1.00 24.04  ? 383  ASN B CA  1 
ATOM   6579  C  C   . ASN B 1 408 ? 122.023 113.892 142.493 1.00 27.69  ? 383  ASN B C   1 
ATOM   6580  O  O   . ASN B 1 408 ? 121.439 114.923 142.833 1.00 39.40  ? 383  ASN B O   1 
ATOM   6581  C  CB  . ASN B 1 408 ? 121.721 111.480 143.187 1.00 27.17  ? 383  ASN B CB  1 
ATOM   6582  C  CG  . ASN B 1 408 ? 121.987 110.427 144.244 1.00 27.37  ? 383  ASN B CG  1 
ATOM   6583  O  OD1 . ASN B 1 408 ? 122.489 110.729 145.324 1.00 30.94  ? 383  ASN B OD1 1 
ATOM   6584  N  ND2 . ASN B 1 408 ? 121.651 109.182 143.936 1.00 32.11  ? 383  ASN B ND2 1 
ATOM   6585  N  N   . GLN B 1 409 ? 122.380 113.651 141.231 1.00 35.20  ? 384  GLN B N   1 
ATOM   6586  C  CA  . GLN B 1 409 ? 122.119 114.648 140.198 1.00 38.36  ? 384  GLN B CA  1 
ATOM   6587  C  C   . GLN B 1 409 ? 120.625 114.773 139.931 1.00 46.35  ? 384  GLN B C   1 
ATOM   6588  O  O   . GLN B 1 409 ? 120.023 115.825 140.173 1.00 51.44  ? 384  GLN B O   1 
ATOM   6589  C  CB  . GLN B 1 409 ? 122.868 114.283 138.917 1.00 39.35  ? 384  GLN B CB  1 
ATOM   6590  C  CG  . GLN B 1 409 ? 122.455 115.097 137.706 1.00 40.61  ? 384  GLN B CG  1 
ATOM   6591  C  CD  . GLN B 1 409 ? 123.123 114.617 136.437 1.00 46.28  ? 384  GLN B CD  1 
ATOM   6592  O  OE1 . GLN B 1 409 ? 123.892 113.656 136.453 1.00 49.36  ? 384  GLN B OE1 1 
ATOM   6593  N  NE2 . GLN B 1 409 ? 122.849 115.295 135.329 1.00 44.12  ? 384  GLN B NE2 1 
ATOM   6594  N  N   . GLY B 1 410 ? 120.010 113.708 139.429 1.00 30.86  ? 385  GLY B N   1 
ATOM   6595  C  CA  . GLY B 1 410 ? 118.571 113.693 139.274 1.00 30.23  ? 385  GLY B CA  1 
ATOM   6596  C  C   . GLY B 1 410 ? 117.940 112.505 139.965 1.00 29.94  ? 385  GLY B C   1 
ATOM   6597  O  O   . GLY B 1 410 ? 118.069 111.372 139.497 1.00 44.18  ? 385  GLY B O   1 
ATOM   6598  N  N   . GLU B 1 411 ? 117.227 112.753 141.060 1.00 28.49  ? 386  GLU B N   1 
ATOM   6599  C  CA  . GLU B 1 411 ? 116.645 111.674 141.844 1.00 33.71  ? 386  GLU B CA  1 
ATOM   6600  C  C   . GLU B 1 411 ? 115.155 111.501 141.607 1.00 31.30  ? 386  GLU B C   1 
ATOM   6601  O  O   . GLU B 1 411 ? 114.617 110.425 141.883 1.00 40.55  ? 386  GLU B O   1 
ATOM   6602  C  CB  . GLU B 1 411 ? 116.894 111.905 143.337 1.00 31.29  ? 386  GLU B CB  1 
ATOM   6603  C  CG  . GLU B 1 411 ? 118.153 112.693 143.639 1.00 31.97  ? 386  GLU B CG  1 
ATOM   6604  C  CD  . GLU B 1 411 ? 118.572 112.578 145.087 1.00 44.29  ? 386  GLU B CD  1 
ATOM   6605  O  OE1 . GLU B 1 411 ? 119.786 112.543 145.360 1.00 51.18  ? 386  GLU B OE1 1 
ATOM   6606  O  OE2 . GLU B 1 411 ? 117.687 112.476 145.955 1.00 40.39  ? 386  GLU B OE2 1 
ATOM   6607  N  N   . GLY B 1 412 ? 114.476 112.529 141.110 1.00 17.21  ? 387  GLY B N   1 
ATOM   6608  C  CA  . GLY B 1 412 ? 113.063 112.416 140.817 1.00 16.59  ? 387  GLY B CA  1 
ATOM   6609  C  C   . GLY B 1 412 ? 112.814 111.750 139.481 1.00 24.42  ? 387  GLY B C   1 
ATOM   6610  O  O   . GLY B 1 412 ? 111.992 112.220 138.690 1.00 35.08  ? 387  GLY B O   1 
ATOM   6611  N  N   . LEU B 1 413 ? 113.528 110.654 139.217 1.00 26.84  ? 388  LEU B N   1 
ATOM   6612  C  CA  . LEU B 1 413 ? 113.394 109.959 137.943 1.00 26.78  ? 388  LEU B CA  1 
ATOM   6613  C  C   . LEU B 1 413 ? 111.989 109.416 137.728 1.00 31.24  ? 388  LEU B C   1 
ATOM   6614  O  O   . LEU B 1 413 ? 111.583 109.216 136.579 1.00 35.69  ? 388  LEU B O   1 
ATOM   6615  C  CB  . LEU B 1 413 ? 114.415 108.823 137.860 1.00 31.82  ? 388  LEU B CB  1 
ATOM   6616  C  CG  . LEU B 1 413 ? 114.611 108.173 136.490 1.00 29.51  ? 388  LEU B CG  1 
ATOM   6617  C  CD1 . LEU B 1 413 ? 114.920 109.227 135.446 1.00 24.54  ? 388  LEU B CD1 1 
ATOM   6618  C  CD2 . LEU B 1 413 ? 115.710 107.127 136.538 1.00 40.23  ? 388  LEU B CD2 1 
ATOM   6619  N  N   . LYS B 1 414 ? 111.238 109.181 138.799 1.00 28.49  ? 389  LYS B N   1 
ATOM   6620  C  CA  . LYS B 1 414 ? 109.871 108.695 138.691 1.00 27.34  ? 389  LYS B CA  1 
ATOM   6621  C  C   . LYS B 1 414 ? 108.849 109.820 138.607 1.00 32.77  ? 389  LYS B C   1 
ATOM   6622  O  O   . LYS B 1 414 ? 107.656 109.541 138.448 1.00 37.86  ? 389  LYS B O   1 
ATOM   6623  C  CB  . LYS B 1 414 ? 109.545 107.778 139.871 1.00 28.06  ? 389  LYS B CB  1 
ATOM   6624  C  CG  . LYS B 1 414 ? 110.502 106.608 140.000 1.00 31.09  ? 389  LYS B CG  1 
ATOM   6625  C  CD  . LYS B 1 414 ? 109.786 105.346 140.434 1.00 32.44  ? 389  LYS B CD  1 
ATOM   6626  C  CE  . LYS B 1 414 ? 110.647 104.124 140.176 1.00 40.78  ? 389  LYS B CE  1 
ATOM   6627  N  NZ  . LYS B 1 414 ? 111.160 104.096 138.778 1.00 37.61  ? 389  LYS B NZ  1 
ATOM   6628  N  N   . PHE B 1 415 ? 109.281 111.078 138.720 1.00 29.66  ? 390  PHE B N   1 
ATOM   6629  C  CA  . PHE B 1 415 ? 108.387 112.188 138.410 1.00 25.05  ? 390  PHE B CA  1 
ATOM   6630  C  C   . PHE B 1 415 ? 107.982 112.155 136.944 1.00 34.64  ? 390  PHE B C   1 
ATOM   6631  O  O   . PHE B 1 415 ? 106.813 112.377 136.608 1.00 45.81  ? 390  PHE B O   1 
ATOM   6632  C  CB  . PHE B 1 415 ? 109.057 113.517 138.753 1.00 24.17  ? 390  PHE B CB  1 
ATOM   6633  C  CG  . PHE B 1 415 ? 108.110 114.681 138.788 1.00 28.02  ? 390  PHE B CG  1 
ATOM   6634  C  CD1 . PHE B 1 415 ? 106.823 114.528 139.268 1.00 33.99  ? 390  PHE B CD1 1 
ATOM   6635  C  CD2 . PHE B 1 415 ? 108.508 115.927 138.340 1.00 29.60  ? 390  PHE B CD2 1 
ATOM   6636  C  CE1 . PHE B 1 415 ? 105.951 115.597 139.302 1.00 31.40  ? 390  PHE B CE1 1 
ATOM   6637  C  CE2 . PHE B 1 415 ? 107.641 116.998 138.372 1.00 25.81  ? 390  PHE B CE2 1 
ATOM   6638  C  CZ  . PHE B 1 415 ? 106.362 116.833 138.854 1.00 26.31  ? 390  PHE B CZ  1 
ATOM   6639  N  N   . VAL B 1 416 ? 108.936 111.878 136.058 1.00 37.00  ? 391  VAL B N   1 
ATOM   6640  C  CA  . VAL B 1 416 ? 108.647 111.693 134.643 1.00 37.89  ? 391  VAL B CA  1 
ATOM   6641  C  C   . VAL B 1 416 ? 108.763 110.213 134.300 1.00 44.20  ? 391  VAL B C   1 
ATOM   6642  O  O   . VAL B 1 416 ? 109.838 109.722 133.936 1.00 44.62  ? 391  VAL B O   1 
ATOM   6643  C  CB  . VAL B 1 416 ? 109.575 112.558 133.768 1.00 29.92  ? 391  VAL B CB  1 
ATOM   6644  C  CG1 . VAL B 1 416 ? 109.085 113.990 133.754 1.00 38.06  ? 391  VAL B CG1 1 
ATOM   6645  C  CG2 . VAL B 1 416 ? 111.001 112.515 134.295 1.00 27.68  ? 391  VAL B CG2 1 
ATOM   6646  N  N   . GLU B 1 417 ? 107.650 109.491 134.414 1.00 50.50  ? 392  GLU B N   1 
ATOM   6647  C  CA  . GLU B 1 417 ? 107.609 108.077 134.069 1.00 50.65  ? 392  GLU B CA  1 
ATOM   6648  C  C   . GLU B 1 417 ? 106.504 107.838 133.052 1.00 55.25  ? 392  GLU B C   1 
ATOM   6649  O  O   . GLU B 1 417 ? 106.607 106.943 132.207 1.00 55.55  ? 392  GLU B O   1 
ATOM   6650  C  CB  . GLU B 1 417 ? 107.394 107.217 135.316 1.00 47.07  ? 392  GLU B CB  1 
ATOM   6651  N  N   . ASP B 1 418 ? 105.440 108.638 133.131 1.00 72.57  ? 393  ASP B N   1 
ATOM   6652  C  CA  . ASP B 1 418 ? 104.374 108.583 132.142 1.00 74.15  ? 393  ASP B CA  1 
ATOM   6653  C  C   . ASP B 1 418 ? 104.805 109.126 130.787 1.00 74.70  ? 393  ASP B C   1 
ATOM   6654  O  O   . ASP B 1 418 ? 104.108 108.891 129.794 1.00 74.28  ? 393  ASP B O   1 
ATOM   6655  C  CB  . ASP B 1 418 ? 103.153 109.356 132.644 1.00 71.29  ? 393  ASP B CB  1 
ATOM   6656  N  N   . SER B 1 419 ? 105.925 109.841 130.723 1.00 67.44  ? 394  SER B N   1 
ATOM   6657  C  CA  . SER B 1 419 ? 106.450 110.413 129.488 1.00 66.05  ? 394  SER B CA  1 
ATOM   6658  C  C   . SER B 1 419 ? 107.943 110.139 129.374 1.00 68.50  ? 394  SER B C   1 
ATOM   6659  O  O   . SER B 1 419 ? 108.741 111.017 129.043 1.00 70.35  ? 394  SER B O   1 
ATOM   6660  C  CB  . SER B 1 419 ? 106.172 111.911 129.422 1.00 66.97  ? 394  SER B CB  1 
ATOM   6661  O  OG  . SER B 1 419 ? 107.017 112.622 130.308 1.00 70.03  ? 394  SER B OG  1 
ATOM   6662  N  N   . ALA B 1 420 ? 108.340 108.898 129.654 1.00 71.75  ? 395  ALA B N   1 
ATOM   6663  C  CA  . ALA B 1 420 ? 109.738 108.500 129.587 1.00 72.37  ? 395  ALA B CA  1 
ATOM   6664  C  C   . ALA B 1 420 ? 110.036 107.520 128.462 1.00 73.73  ? 395  ALA B C   1 
ATOM   6665  O  O   . ALA B 1 420 ? 111.212 107.242 128.204 1.00 71.89  ? 395  ALA B O   1 
ATOM   6666  C  CB  . ALA B 1 420 ? 110.182 107.884 130.922 1.00 71.17  ? 395  ALA B CB  1 
ATOM   6667  N  N   . GLU B 1 421 ? 109.015 106.993 127.792 1.00 82.03  ? 396  GLU B N   1 
ATOM   6668  C  CA  . GLU B 1 421 ? 109.179 106.051 126.693 1.00 81.46  ? 396  GLU B CA  1 
ATOM   6669  C  C   . GLU B 1 421 ? 108.639 106.634 125.394 1.00 81.80  ? 396  GLU B C   1 
ATOM   6670  O  O   . GLU B 1 421 ? 107.975 105.951 124.611 1.00 80.78  ? 396  GLU B O   1 
ATOM   6671  C  CB  . GLU B 1 421 ? 108.500 104.721 127.011 1.00 79.60  ? 396  GLU B CB  1 
ATOM   6672  N  N   . SER B 1 422 ? 108.919 107.912 125.151 1.00 89.62  ? 397  SER B N   1 
ATOM   6673  C  CA  . SER B 1 422 ? 108.453 108.609 123.963 1.00 89.95  ? 397  SER B CA  1 
ATOM   6674  C  C   . SER B 1 422 ? 109.644 109.121 123.164 1.00 91.42  ? 397  SER B C   1 
ATOM   6675  O  O   . SER B 1 422 ? 110.718 109.378 123.716 1.00 89.24  ? 397  SER B O   1 
ATOM   6676  C  CB  . SER B 1 422 ? 107.528 109.776 124.330 1.00 87.58  ? 397  SER B CB  1 
ATOM   6677  O  OG  . SER B 1 422 ? 106.780 110.205 123.206 1.00 87.69  ? 397  SER B OG  1 
ATOM   6678  N  N   . GLU B 1 423 ? 109.442 109.258 121.851 1.00 96.98  ? 398  GLU B N   1 
ATOM   6679  C  CA  . GLU B 1 423 ? 110.517 109.731 120.983 1.00 96.65  ? 398  GLU B CA  1 
ATOM   6680  C  C   . GLU B 1 423 ? 110.941 111.146 121.351 1.00 96.42  ? 398  GLU B C   1 
ATOM   6681  O  O   . GLU B 1 423 ? 112.139 111.446 121.419 1.00 94.48  ? 398  GLU B O   1 
ATOM   6682  C  CB  . GLU B 1 423 ? 110.077 109.664 119.520 1.00 95.77  ? 398  GLU B CB  1 
ATOM   6683  N  N   . ASP B 1 424 ? 109.977 112.029 121.592 1.00 93.99  ? 399  ASP B N   1 
ATOM   6684  C  CA  . ASP B 1 424 ? 110.265 113.381 122.041 1.00 92.42  ? 399  ASP B CA  1 
ATOM   6685  C  C   . ASP B 1 424 ? 110.227 113.421 123.568 1.00 94.72  ? 399  ASP B C   1 
ATOM   6686  O  O   . ASP B 1 424 ? 110.166 112.387 124.238 1.00 96.11  ? 399  ASP B O   1 
ATOM   6687  C  CB  . ASP B 1 424 ? 109.284 114.369 121.412 1.00 91.43  ? 399  ASP B CB  1 
ATOM   6688  C  CG  . ASP B 1 424 ? 107.863 114.176 121.906 1.00 91.57  ? 399  ASP B CG  1 
ATOM   6689  O  OD1 . ASP B 1 424 ? 107.517 113.047 122.312 1.00 90.98  ? 399  ASP B OD1 1 
ATOM   6690  O  OD2 . ASP B 1 424 ? 107.090 115.157 121.886 1.00 92.35  ? 399  ASP B OD2 1 
ATOM   6691  N  N   . GLY B 1 425 ? 110.262 114.622 124.135 1.00 81.17  ? 400  GLY B N   1 
ATOM   6692  C  CA  . GLY B 1 425 ? 110.215 114.767 125.575 1.00 76.78  ? 400  GLY B CA  1 
ATOM   6693  C  C   . GLY B 1 425 ? 108.813 114.999 126.096 1.00 74.59  ? 400  GLY B C   1 
ATOM   6694  O  O   . GLY B 1 425 ? 107.951 114.121 125.996 1.00 76.96  ? 400  GLY B O   1 
ATOM   6695  N  N   . VAL B 1 426 ? 108.575 116.181 126.655 1.00 57.35  ? 401  VAL B N   1 
ATOM   6696  C  CA  . VAL B 1 426 ? 107.279 116.560 127.204 1.00 57.66  ? 401  VAL B CA  1 
ATOM   6697  C  C   . VAL B 1 426 ? 106.757 117.754 126.419 1.00 59.29  ? 401  VAL B C   1 
ATOM   6698  O  O   . VAL B 1 426 ? 107.459 118.762 126.270 1.00 61.32  ? 401  VAL B O   1 
ATOM   6699  C  CB  . VAL B 1 426 ? 107.377 116.886 128.704 1.00 57.26  ? 401  VAL B CB  1 
ATOM   6700  C  CG1 . VAL B 1 426 ? 106.021 117.285 129.249 1.00 57.30  ? 401  VAL B CG1 1 
ATOM   6701  C  CG2 . VAL B 1 426 ? 107.923 115.695 129.467 1.00 52.76  ? 401  VAL B CG2 1 
ATOM   6702  N  N   . SER B 1 427 ? 105.533 117.640 125.913 1.00 54.15  ? 402  SER B N   1 
ATOM   6703  C  CA  . SER B 1 427 ? 104.919 118.745 125.196 1.00 58.69  ? 402  SER B CA  1 
ATOM   6704  C  C   . SER B 1 427 ? 104.542 119.863 126.164 1.00 61.23  ? 402  SER B C   1 
ATOM   6705  O  O   . SER B 1 427 ? 104.471 119.672 127.381 1.00 63.60  ? 402  SER B O   1 
ATOM   6706  C  CB  . SER B 1 427 ? 103.684 118.269 124.431 1.00 61.89  ? 402  SER B CB  1 
ATOM   6707  O  OG  . SER B 1 427 ? 102.677 117.816 125.317 1.00 62.04  ? 402  SER B OG  1 
ATOM   6708  N  N   . ALA B 1 428 ? 104.305 121.051 125.603 1.00 57.51  ? 403  ALA B N   1 
ATOM   6709  C  CA  . ALA B 1 428 ? 103.952 122.201 126.430 1.00 55.15  ? 403  ALA B CA  1 
ATOM   6710  C  C   . ALA B 1 428 ? 102.639 121.971 127.166 1.00 56.21  ? 403  ALA B C   1 
ATOM   6711  O  O   . ALA B 1 428 ? 102.512 122.313 128.348 1.00 58.32  ? 403  ALA B O   1 
ATOM   6712  C  CB  . ALA B 1 428 ? 103.874 123.462 125.571 1.00 55.53  ? 403  ALA B CB  1 
ATOM   6713  N  N   . SER B 1 429 ? 101.652 121.386 126.484 1.00 55.45  ? 404  SER B N   1 
ATOM   6714  C  CA  . SER B 1 429 ? 100.380 121.081 127.128 1.00 54.02  ? 404  SER B CA  1 
ATOM   6715  C  C   . SER B 1 429 ? 100.531 120.049 128.236 1.00 52.88  ? 404  SER B C   1 
ATOM   6716  O  O   . SER B 1 429 ? 99.676  119.982 129.126 1.00 55.92  ? 404  SER B O   1 
ATOM   6717  C  CB  . SER B 1 429 ? 99.371  120.588 126.090 1.00 59.32  ? 404  SER B CB  1 
ATOM   6718  O  OG  . SER B 1 429 ? 99.172  121.552 125.070 1.00 61.96  ? 404  SER B OG  1 
ATOM   6719  N  N   . ALA B 1 430 ? 101.593 119.244 128.202 1.00 49.43  ? 405  ALA B N   1 
ATOM   6720  C  CA  . ALA B 1 430 ? 101.858 118.289 129.269 1.00 50.74  ? 405  ALA B CA  1 
ATOM   6721  C  C   . ALA B 1 430 ? 102.765 118.860 130.349 1.00 53.24  ? 405  ALA B C   1 
ATOM   6722  O  O   . ALA B 1 430 ? 102.593 118.528 131.526 1.00 54.44  ? 405  ALA B O   1 
ATOM   6723  C  CB  . ALA B 1 430 ? 102.477 117.013 128.696 1.00 48.83  ? 405  ALA B CB  1 
ATOM   6724  N  N   . PHE B 1 431 ? 103.721 119.715 129.979 1.00 46.20  ? 406  PHE B N   1 
ATOM   6725  C  CA  . PHE B 1 431 ? 104.531 120.404 130.980 1.00 39.71  ? 406  PHE B CA  1 
ATOM   6726  C  C   . PHE B 1 431 ? 103.667 121.296 131.861 1.00 41.31  ? 406  PHE B C   1 
ATOM   6727  O  O   . PHE B 1 431 ? 103.818 121.307 133.091 1.00 50.61  ? 406  PHE B O   1 
ATOM   6728  C  CB  . PHE B 1 431 ? 105.621 121.220 130.284 1.00 44.14  ? 406  PHE B CB  1 
ATOM   6729  C  CG  . PHE B 1 431 ? 106.578 121.894 131.224 1.00 48.00  ? 406  PHE B CG  1 
ATOM   6730  C  CD1 . PHE B 1 431 ? 107.623 121.189 131.795 1.00 47.67  ? 406  PHE B CD1 1 
ATOM   6731  C  CD2 . PHE B 1 431 ? 106.445 123.238 131.523 1.00 49.46  ? 406  PHE B CD2 1 
ATOM   6732  C  CE1 . PHE B 1 431 ? 108.509 121.811 132.653 1.00 45.59  ? 406  PHE B CE1 1 
ATOM   6733  C  CE2 . PHE B 1 431 ? 107.328 123.862 132.381 1.00 48.31  ? 406  PHE B CE2 1 
ATOM   6734  C  CZ  . PHE B 1 431 ? 108.360 123.148 132.947 1.00 43.47  ? 406  PHE B CZ  1 
ATOM   6735  N  N   . ASP B 1 432 ? 102.746 122.043 131.247 1.00 36.62  ? 407  ASP B N   1 
ATOM   6736  C  CA  . ASP B 1 432 ? 101.832 122.884 132.011 1.00 35.95  ? 407  ASP B CA  1 
ATOM   6737  C  C   . ASP B 1 432 ? 100.998 122.044 132.968 1.00 38.24  ? 407  ASP B C   1 
ATOM   6738  O  O   . ASP B 1 432 ? 100.835 122.393 134.143 1.00 46.01  ? 407  ASP B O   1 
ATOM   6739  C  CB  . ASP B 1 432 ? 100.921 123.659 131.059 1.00 45.44  ? 407  ASP B CB  1 
ATOM   6740  C  CG  . ASP B 1 432 ? 101.406 125.067 130.803 1.00 52.24  ? 407  ASP B CG  1 
ATOM   6741  O  OD1 . ASP B 1 432 ? 102.627 125.295 130.892 1.00 51.89  ? 407  ASP B OD1 1 
ATOM   6742  O  OD2 . ASP B 1 432 ? 100.566 125.945 130.511 1.00 52.34  ? 407  ASP B OD2 1 
ATOM   6743  N  N   . PHE B 1 433 ? 100.468 120.923 132.475 1.00 40.06  ? 408  PHE B N   1 
ATOM   6744  C  CA  . PHE B 1 433 ? 99.633  120.057 133.300 1.00 40.48  ? 408  PHE B CA  1 
ATOM   6745  C  C   . PHE B 1 433 ? 100.422 119.466 134.460 1.00 44.76  ? 408  PHE B C   1 
ATOM   6746  O  O   . PHE B 1 433 ? 99.926  119.408 135.592 1.00 45.01  ? 408  PHE B O   1 
ATOM   6747  C  CB  . PHE B 1 433 ? 99.031  118.951 132.434 1.00 38.48  ? 408  PHE B CB  1 
ATOM   6748  C  CG  . PHE B 1 433 ? 98.140  118.008 133.183 1.00 40.44  ? 408  PHE B CG  1 
ATOM   6749  C  CD1 . PHE B 1 433 ? 96.921  118.434 133.680 1.00 44.62  ? 408  PHE B CD1 1 
ATOM   6750  C  CD2 . PHE B 1 433 ? 98.517  116.691 133.380 1.00 42.34  ? 408  PHE B CD2 1 
ATOM   6751  C  CE1 . PHE B 1 433 ? 96.097  117.565 134.366 1.00 45.41  ? 408  PHE B CE1 1 
ATOM   6752  C  CE2 . PHE B 1 433 ? 97.697  115.818 134.064 1.00 45.16  ? 408  PHE B CE2 1 
ATOM   6753  C  CZ  . PHE B 1 433 ? 96.485  116.255 134.557 1.00 46.28  ? 408  PHE B CZ  1 
ATOM   6754  N  N   . THR B 1 434 ? 101.654 119.021 134.200 1.00 39.75  ? 409  THR B N   1 
ATOM   6755  C  CA  . THR B 1 434 ? 102.469 118.435 135.259 1.00 33.64  ? 409  THR B CA  1 
ATOM   6756  C  C   . THR B 1 434 ? 102.806 119.465 136.329 1.00 31.07  ? 409  THR B C   1 
ATOM   6757  O  O   . THR B 1 434 ? 102.705 119.178 137.528 1.00 37.97  ? 409  THR B O   1 
ATOM   6758  C  CB  . THR B 1 434 ? 103.743 117.834 134.667 1.00 32.25  ? 409  THR B CB  1 
ATOM   6759  O  OG1 . THR B 1 434 ? 103.447 116.553 134.098 1.00 38.45  ? 409  THR B OG1 1 
ATOM   6760  C  CG2 . THR B 1 434 ? 104.799 117.660 135.741 1.00 35.02  ? 409  THR B CG2 1 
ATOM   6761  N  N   . VAL B 1 435 ? 103.190 120.677 135.920 1.00 34.50  ? 410  VAL B N   1 
ATOM   6762  C  CA  . VAL B 1 435 ? 103.520 121.707 136.902 1.00 34.28  ? 410  VAL B CA  1 
ATOM   6763  C  C   . VAL B 1 435 ? 102.281 122.108 137.697 1.00 37.00  ? 410  VAL B C   1 
ATOM   6764  O  O   . VAL B 1 435 ? 102.351 122.328 138.914 1.00 42.30  ? 410  VAL B O   1 
ATOM   6765  C  CB  . VAL B 1 435 ? 104.175 122.914 136.207 1.00 31.59  ? 410  VAL B CB  1 
ATOM   6766  C  CG1 . VAL B 1 435 ? 104.114 124.142 137.093 1.00 30.47  ? 410  VAL B CG1 1 
ATOM   6767  C  CG2 . VAL B 1 435 ? 105.614 122.592 135.850 1.00 27.84  ? 410  VAL B CG2 1 
ATOM   6768  N  N   . SER B 1 436 ? 101.125 122.196 137.032 1.00 33.72  ? 411  SER B N   1 
ATOM   6769  C  CA  . SER B 1 436 ? 99.894  122.538 137.737 1.00 31.35  ? 411  SER B CA  1 
ATOM   6770  C  C   . SER B 1 436 ? 99.518  121.465 138.750 1.00 41.38  ? 411  SER B C   1 
ATOM   6771  O  O   . SER B 1 436 ? 99.108  121.779 139.873 1.00 49.25  ? 411  SER B O   1 
ATOM   6772  C  CB  . SER B 1 436 ? 98.760  122.753 136.737 1.00 40.08  ? 411  SER B CB  1 
ATOM   6773  O  OG  . SER B 1 436 ? 99.154  123.642 135.708 1.00 49.50  ? 411  SER B OG  1 
ATOM   6774  N  N   . ASN B 1 437 ? 99.648  120.190 138.371 1.00 37.46  ? 412  ASN B N   1 
ATOM   6775  C  CA  . ASN B 1 437 ? 99.375  119.106 139.310 1.00 39.00  ? 412  ASN B CA  1 
ATOM   6776  C  C   . ASN B 1 437 ? 100.343 119.141 140.484 1.00 41.62  ? 412  ASN B C   1 
ATOM   6777  O  O   . ASN B 1 437 ? 99.950  118.905 141.631 1.00 38.87  ? 412  ASN B O   1 
ATOM   6778  C  CB  . ASN B 1 437 ? 99.455  117.758 138.596 1.00 37.17  ? 412  ASN B CB  1 
ATOM   6779  C  CG  . ASN B 1 437 ? 98.172  117.400 137.881 1.00 43.76  ? 412  ASN B CG  1 
ATOM   6780  O  OD1 . ASN B 1 437 ? 97.217  118.176 137.869 1.00 45.71  ? 412  ASN B OD1 1 
ATOM   6781  N  ND2 . ASN B 1 437 ? 98.141  116.217 137.282 1.00 41.27  ? 412  ASN B ND2 1 
ATOM   6782  N  N   . PHE B 1 438 ? 101.618 119.422 140.209 1.00 41.39  ? 413  PHE B N   1 
ATOM   6783  C  CA  . PHE B 1 438 ? 102.613 119.546 141.267 1.00 32.36  ? 413  PHE B CA  1 
ATOM   6784  C  C   . PHE B 1 438 ? 102.214 120.625 142.268 1.00 37.84  ? 413  PHE B C   1 
ATOM   6785  O  O   . PHE B 1 438 ? 102.197 120.390 143.484 1.00 48.18  ? 413  PHE B O   1 
ATOM   6786  C  CB  . PHE B 1 438 ? 103.972 119.849 140.631 1.00 34.96  ? 413  PHE B CB  1 
ATOM   6787  C  CG  . PHE B 1 438 ? 105.076 120.105 141.611 1.00 36.10  ? 413  PHE B CG  1 
ATOM   6788  C  CD1 . PHE B 1 438 ? 105.335 121.386 142.067 1.00 34.56  ? 413  PHE B CD1 1 
ATOM   6789  C  CD2 . PHE B 1 438 ? 105.879 119.069 142.049 1.00 41.31  ? 413  PHE B CD2 1 
ATOM   6790  C  CE1 . PHE B 1 438 ? 106.356 121.621 142.957 1.00 35.78  ? 413  PHE B CE1 1 
ATOM   6791  C  CE2 . PHE B 1 438 ? 106.903 119.301 142.938 1.00 36.43  ? 413  PHE B CE2 1 
ATOM   6792  C  CZ  . PHE B 1 438 ? 107.141 120.578 143.390 1.00 38.79  ? 413  PHE B CZ  1 
ATOM   6793  N  N   . VAL B 1 439 ? 101.864 121.812 141.766 1.00 35.78  ? 414  VAL B N   1 
ATOM   6794  C  CA  . VAL B 1 439 ? 101.481 122.913 142.648 1.00 35.91  ? 414  VAL B CA  1 
ATOM   6795  C  C   . VAL B 1 439 ? 100.223 122.564 143.432 1.00 42.24  ? 414  VAL B C   1 
ATOM   6796  O  O   . VAL B 1 439 ? 100.130 122.831 144.636 1.00 47.93  ? 414  VAL B O   1 
ATOM   6797  C  CB  . VAL B 1 439 ? 101.298 124.210 141.839 1.00 31.23  ? 414  VAL B CB  1 
ATOM   6798  C  CG1 . VAL B 1 439 ? 100.789 125.325 142.733 1.00 32.52  ? 414  VAL B CG1 1 
ATOM   6799  C  CG2 . VAL B 1 439 ? 102.602 124.612 141.190 1.00 35.04  ? 414  VAL B CG2 1 
ATOM   6800  N  N   . ASP B 1 440 ? 99.234  121.964 142.764 1.00 41.41  ? 415  ASP B N   1 
ATOM   6801  C  CA  . ASP B 1 440 ? 97.984  121.627 143.439 1.00 41.17  ? 415  ASP B CA  1 
ATOM   6802  C  C   . ASP B 1 440 ? 98.207  120.605 144.546 1.00 46.88  ? 415  ASP B C   1 
ATOM   6803  O  O   . ASP B 1 440 ? 97.635  120.725 145.635 1.00 49.60  ? 415  ASP B O   1 
ATOM   6804  C  CB  . ASP B 1 440 ? 96.968  121.103 142.425 1.00 38.98  ? 415  ASP B CB  1 
ATOM   6805  C  CG  . ASP B 1 440 ? 95.981  122.165 141.987 1.00 48.72  ? 415  ASP B CG  1 
ATOM   6806  O  OD1 . ASP B 1 440 ? 95.684  123.071 142.794 1.00 53.24  ? 415  ASP B OD1 1 
ATOM   6807  O  OD2 . ASP B 1 440 ? 95.501  122.093 140.836 1.00 51.33  ? 415  ASP B OD2 1 
ATOM   6808  N  N   . ASN B 1 441 ? 99.035  119.591 144.286 1.00 40.04  ? 416  ASN B N   1 
ATOM   6809  C  CA  . ASN B 1 441 ? 99.232  118.532 145.268 1.00 36.55  ? 416  ASN B CA  1 
ATOM   6810  C  C   . ASN B 1 441 ? 100.086 119.002 146.437 1.00 42.31  ? 416  ASN B C   1 
ATOM   6811  O  O   . ASN B 1 441 ? 99.829  118.626 147.587 1.00 47.53  ? 416  ASN B O   1 
ATOM   6812  C  CB  . ASN B 1 441 ? 99.865  117.311 144.604 1.00 34.29  ? 416  ASN B CB  1 
ATOM   6813  C  CG  . ASN B 1 441 ? 98.884  116.540 143.747 1.00 46.65  ? 416  ASN B CG  1 
ATOM   6814  O  OD1 . ASN B 1 441 ? 97.730  116.345 144.126 1.00 49.67  ? 416  ASN B OD1 1 
ATOM   6815  N  ND2 . ASN B 1 441 ? 99.339  116.096 142.582 1.00 50.05  ? 416  ASN B ND2 1 
ATOM   6816  N  N   . LEU B 1 442 ? 101.104 119.822 146.175 1.00 41.90  ? 417  LEU B N   1 
ATOM   6817  C  CA  . LEU B 1 442 ? 102.059 120.151 147.230 1.00 40.65  ? 417  LEU B CA  1 
ATOM   6818  C  C   . LEU B 1 442 ? 101.699 121.437 147.971 1.00 44.91  ? 417  LEU B C   1 
ATOM   6819  O  O   . LEU B 1 442 ? 101.498 121.419 149.189 1.00 48.62  ? 417  LEU B O   1 
ATOM   6820  C  CB  . LEU B 1 442 ? 103.471 120.233 146.644 1.00 32.86  ? 417  LEU B CB  1 
ATOM   6821  C  CG  . LEU B 1 442 ? 104.269 118.957 146.907 1.00 39.30  ? 417  LEU B CG  1 
ATOM   6822  C  CD1 . LEU B 1 442 ? 105.578 118.960 146.153 1.00 45.03  ? 417  LEU B CD1 1 
ATOM   6823  C  CD2 . LEU B 1 442 ? 104.510 118.798 148.396 1.00 44.66  ? 417  LEU B CD2 1 
ATOM   6824  N  N   . TYR B 1 443 ? 101.616 122.559 147.256 1.00 53.50  ? 418  TYR B N   1 
ATOM   6825  C  CA  . TYR B 1 443 ? 101.399 123.836 147.930 1.00 53.36  ? 418  TYR B CA  1 
ATOM   6826  C  C   . TYR B 1 443 ? 99.925  124.058 148.250 1.00 56.58  ? 418  TYR B C   1 
ATOM   6827  O  O   . TYR B 1 443 ? 99.539  124.133 149.421 1.00 57.73  ? 418  TYR B O   1 
ATOM   6828  C  CB  . TYR B 1 443 ? 101.954 124.978 147.075 1.00 50.20  ? 418  TYR B CB  1 
ATOM   6829  C  CG  . TYR B 1 443 ? 103.456 125.094 147.161 1.00 50.63  ? 418  TYR B CG  1 
ATOM   6830  C  CD1 . TYR B 1 443 ? 104.056 125.842 148.163 1.00 52.70  ? 418  TYR B CD1 1 
ATOM   6831  C  CD2 . TYR B 1 443 ? 104.275 124.441 146.252 1.00 51.52  ? 418  TYR B CD2 1 
ATOM   6832  C  CE1 . TYR B 1 443 ? 105.427 125.945 148.252 1.00 48.53  ? 418  TYR B CE1 1 
ATOM   6833  C  CE2 . TYR B 1 443 ? 105.647 124.538 146.333 1.00 51.49  ? 418  TYR B CE2 1 
ATOM   6834  C  CZ  . TYR B 1 443 ? 106.217 125.292 147.334 1.00 49.60  ? 418  TYR B CZ  1 
ATOM   6835  O  OH  . TYR B 1 443 ? 107.585 125.391 147.420 1.00 54.84  ? 418  TYR B OH  1 
ATOM   6836  N  N   . GLY B 1 444 ? 99.087  124.153 147.221 1.00 65.55  ? 419  GLY B N   1 
ATOM   6837  C  CA  . GLY B 1 444 ? 97.657  124.299 147.416 1.00 66.24  ? 419  GLY B CA  1 
ATOM   6838  C  C   . GLY B 1 444 ? 97.252  125.507 148.236 1.00 68.87  ? 419  GLY B C   1 
ATOM   6839  O  O   . GLY B 1 444 ? 96.436  125.389 149.156 1.00 67.76  ? 419  GLY B O   1 
ATOM   6840  N  N   . TYR B 1 445 ? 97.816  126.674 147.922 1.00 87.37  ? 420  TYR B N   1 
ATOM   6841  C  CA  . TYR B 1 445 ? 97.517  127.889 148.668 1.00 86.06  ? 420  TYR B CA  1 
ATOM   6842  C  C   . TYR B 1 445 ? 96.325  128.591 148.031 1.00 89.41  ? 420  TYR B C   1 
ATOM   6843  O  O   . TYR B 1 445 ? 96.439  129.063 146.889 1.00 88.11  ? 420  TYR B O   1 
ATOM   6844  C  CB  . TYR B 1 445 ? 98.725  128.813 148.695 1.00 85.97  ? 420  TYR B CB  1 
ATOM   6845  N  N   . PRO B 1 446 ? 95.178  128.679 148.707 1.00 108.43 ? 421  PRO B N   1 
ATOM   6846  C  CA  . PRO B 1 446 ? 94.029  129.382 148.112 1.00 106.96 ? 421  PRO B CA  1 
ATOM   6847  C  C   . PRO B 1 446 ? 94.278  130.860 147.875 1.00 105.58 ? 421  PRO B C   1 
ATOM   6848  O  O   . PRO B 1 446 ? 93.660  131.444 146.976 1.00 106.46 ? 421  PRO B O   1 
ATOM   6849  C  CB  . PRO B 1 446 ? 92.909  129.158 149.139 1.00 106.75 ? 421  PRO B CB  1 
ATOM   6850  C  CG  . PRO B 1 446 ? 93.364  128.002 149.977 1.00 107.70 ? 421  PRO B CG  1 
ATOM   6851  C  CD  . PRO B 1 446 ? 94.854  128.098 150.020 1.00 107.39 ? 421  PRO B CD  1 
ATOM   6852  N  N   . GLU B 1 447 ? 95.159  131.486 148.660 1.00 95.08  ? 422  GLU B N   1 
ATOM   6853  C  CA  . GLU B 1 447 ? 95.393  132.920 148.520 1.00 95.06  ? 422  GLU B CA  1 
ATOM   6854  C  C   . GLU B 1 447 ? 95.955  133.256 147.145 1.00 94.32  ? 422  GLU B C   1 
ATOM   6855  O  O   . GLU B 1 447 ? 95.430  134.128 146.443 1.00 94.58  ? 422  GLU B O   1 
ATOM   6856  C  CB  . GLU B 1 447 ? 96.336  133.406 149.622 1.00 95.18  ? 422  GLU B CB  1 
ATOM   6857  N  N   . GLY B 1 448 ? 97.020  132.571 146.740 1.00 81.91  ? 423  GLY B N   1 
ATOM   6858  C  CA  . GLY B 1 448 ? 97.573  132.788 145.420 1.00 81.14  ? 423  GLY B CA  1 
ATOM   6859  C  C   . GLY B 1 448 ? 98.265  131.574 144.841 1.00 80.07  ? 423  GLY B C   1 
ATOM   6860  O  O   . GLY B 1 448 ? 99.218  131.048 145.423 1.00 81.88  ? 423  GLY B O   1 
ATOM   6861  N  N   . LYS B 1 449 ? 97.791  131.127 143.680 1.00 72.26  ? 424  LYS B N   1 
ATOM   6862  C  CA  . LYS B 1 449 ? 98.435  130.049 142.943 1.00 71.08  ? 424  LYS B CA  1 
ATOM   6863  C  C   . LYS B 1 449 ? 98.579  130.345 141.461 1.00 69.64  ? 424  LYS B C   1 
ATOM   6864  O  O   . LYS B 1 449 ? 99.344  129.649 140.788 1.00 71.56  ? 424  LYS B O   1 
ATOM   6865  C  CB  . LYS B 1 449 ? 97.661  128.734 143.116 1.00 70.75  ? 424  LYS B CB  1 
ATOM   6866  N  N   . ASP B 1 450 ? 97.877  131.346 140.929 1.00 72.65  ? 425  ASP B N   1 
ATOM   6867  C  CA  . ASP B 1 450 ? 98.077  131.772 139.552 1.00 73.18  ? 425  ASP B CA  1 
ATOM   6868  C  C   . ASP B 1 450 ? 99.373  132.546 139.367 1.00 75.36  ? 425  ASP B C   1 
ATOM   6869  O  O   . ASP B 1 450 ? 99.757  132.811 138.224 1.00 74.03  ? 425  ASP B O   1 
ATOM   6870  C  CB  . ASP B 1 450 ? 96.890  132.621 139.093 1.00 76.63  ? 425  ASP B CB  1 
ATOM   6871  C  CG  . ASP B 1 450 ? 96.378  133.544 140.182 1.00 79.16  ? 425  ASP B CG  1 
ATOM   6872  O  OD1 . ASP B 1 450 ? 96.916  133.493 141.308 1.00 76.98  ? 425  ASP B OD1 1 
ATOM   6873  O  OD2 . ASP B 1 450 ? 95.437  134.320 139.913 1.00 78.75  ? 425  ASP B OD2 1 
ATOM   6874  N  N   . VAL B 1 451 ? 100.041 132.924 140.452 1.00 57.55  ? 426  VAL B N   1 
ATOM   6875  C  CA  . VAL B 1 451 ? 101.340 133.577 140.384 1.00 48.30  ? 426  VAL B CA  1 
ATOM   6876  C  C   . VAL B 1 451 ? 102.474 132.586 140.609 1.00 51.38  ? 426  VAL B C   1 
ATOM   6877  O  O   . VAL B 1 451 ? 103.479 132.620 139.900 1.00 59.64  ? 426  VAL B O   1 
ATOM   6878  C  CB  . VAL B 1 451 ? 101.408 134.736 141.401 1.00 43.73  ? 426  VAL B CB  1 
ATOM   6879  C  CG1 . VAL B 1 451 ? 102.790 135.363 141.403 1.00 45.15  ? 426  VAL B CG1 1 
ATOM   6880  C  CG2 . VAL B 1 451 ? 100.347 135.776 141.089 1.00 50.91  ? 426  VAL B CG2 1 
ATOM   6881  N  N   . LEU B 1 452 ? 102.319 131.695 141.592 1.00 43.29  ? 427  LEU B N   1 
ATOM   6882  C  CA  . LEU B 1 452 ? 103.364 130.721 141.890 1.00 40.91  ? 427  LEU B CA  1 
ATOM   6883  C  C   . LEU B 1 452 ? 103.578 129.762 140.725 1.00 41.87  ? 427  LEU B C   1 
ATOM   6884  O  O   . LEU B 1 452 ? 104.721 129.429 140.384 1.00 48.33  ? 427  LEU B O   1 
ATOM   6885  C  CB  . LEU B 1 452 ? 103.005 129.953 143.161 1.00 39.93  ? 427  LEU B CB  1 
ATOM   6886  C  CG  . LEU B 1 452 ? 104.052 129.001 143.735 1.00 35.37  ? 427  LEU B CG  1 
ATOM   6887  C  CD1 . LEU B 1 452 ? 105.417 129.656 143.736 1.00 39.56  ? 427  LEU B CD1 1 
ATOM   6888  C  CD2 . LEU B 1 452 ? 103.660 128.575 145.137 1.00 43.33  ? 427  LEU B CD2 1 
ATOM   6889  N  N   . ARG B 1 453 ? 102.490 129.312 140.097 1.00 38.22  ? 428  ARG B N   1 
ATOM   6890  C  CA  . ARG B 1 453 ? 102.613 128.364 138.996 1.00 35.01  ? 428  ARG B CA  1 
ATOM   6891  C  C   . ARG B 1 453 ? 103.409 128.965 137.845 1.00 41.92  ? 428  ARG B C   1 
ATOM   6892  O  O   . ARG B 1 453 ? 104.314 128.324 137.300 1.00 51.62  ? 428  ARG B O   1 
ATOM   6893  C  CB  . ARG B 1 453 ? 101.227 127.926 138.526 1.00 38.38  ? 428  ARG B CB  1 
ATOM   6894  C  CG  . ARG B 1 453 ? 101.225 127.196 137.195 1.00 42.29  ? 428  ARG B CG  1 
ATOM   6895  C  CD  . ARG B 1 453 ? 99.847  126.644 136.859 1.00 47.75  ? 428  ARG B CD  1 
ATOM   6896  N  NE  . ARG B 1 453 ? 98.860  127.700 136.669 1.00 48.72  ? 428  ARG B NE  1 
ATOM   6897  C  CZ  . ARG B 1 453 ? 97.904  127.998 137.537 1.00 50.52  ? 428  ARG B CZ  1 
ATOM   6898  N  NH1 . ARG B 1 453 ? 97.772  127.334 138.674 1.00 47.37  ? 428  ARG B NH1 1 
ATOM   6899  N  NH2 . ARG B 1 453 ? 97.059  128.986 137.259 1.00 48.81  ? 428  ARG B NH2 1 
ATOM   6900  N  N   . GLU B 1 454 ? 103.110 130.215 137.486 1.00 42.14  ? 429  GLU B N   1 
ATOM   6901  C  CA  . GLU B 1 454 ? 103.805 130.844 136.368 1.00 39.50  ? 429  GLU B CA  1 
ATOM   6902  C  C   . GLU B 1 454 ? 105.279 131.073 136.677 1.00 39.94  ? 429  GLU B C   1 
ATOM   6903  O  O   . GLU B 1 454 ? 106.131 130.899 135.799 1.00 41.39  ? 429  GLU B O   1 
ATOM   6904  C  CB  . GLU B 1 454 ? 103.125 132.160 135.994 1.00 34.86  ? 429  GLU B CB  1 
ATOM   6905  C  CG  . GLU B 1 454 ? 101.616 132.063 135.859 1.00 45.72  ? 429  GLU B CG  1 
ATOM   6906  C  CD  . GLU B 1 454 ? 101.170 131.600 134.484 1.00 53.59  ? 429  GLU B CD  1 
ATOM   6907  O  OE1 . GLU B 1 454 ? 101.985 130.990 133.760 1.00 55.95  ? 429  GLU B OE1 1 
ATOM   6908  O  OE2 . GLU B 1 454 ? 99.999  131.845 134.126 1.00 49.85  ? 429  GLU B OE2 1 
ATOM   6909  N  N   . THR B 1 455 ? 105.611 131.458 137.912 1.00 36.86  ? 430  THR B N   1 
ATOM   6910  C  CA  . THR B 1 455 ? 107.011 131.749 138.207 1.00 31.86  ? 430  THR B CA  1 
ATOM   6911  C  C   . THR B 1 455 ? 107.837 130.471 138.308 1.00 35.38  ? 430  THR B C   1 
ATOM   6912  O  O   . THR B 1 455 ? 108.991 130.444 137.861 1.00 42.46  ? 430  THR B O   1 
ATOM   6913  C  CB  . THR B 1 455 ? 107.144 132.594 139.477 1.00 30.61  ? 430  THR B CB  1 
ATOM   6914  O  OG1 . THR B 1 455 ? 108.532 132.809 139.759 1.00 35.84  ? 430  THR B OG1 1 
ATOM   6915  C  CG2 . THR B 1 455 ? 106.511 131.917 140.664 1.00 33.69  ? 430  THR B CG2 1 
ATOM   6916  N  N   . ILE B 1 456 ? 107.275 129.391 138.862 1.00 35.29  ? 431  ILE B N   1 
ATOM   6917  C  CA  . ILE B 1 456 ? 108.036 128.144 138.856 1.00 28.69  ? 431  ILE B CA  1 
ATOM   6918  C  C   . ILE B 1 456 ? 108.011 127.472 137.491 1.00 32.24  ? 431  ILE B C   1 
ATOM   6919  O  O   . ILE B 1 456 ? 108.826 126.577 137.237 1.00 40.96  ? 431  ILE B O   1 
ATOM   6920  C  CB  . ILE B 1 456 ? 107.561 127.137 139.919 1.00 23.55  ? 431  ILE B CB  1 
ATOM   6921  C  CG1 . ILE B 1 456 ? 106.389 126.306 139.402 1.00 30.29  ? 431  ILE B CG1 1 
ATOM   6922  C  CG2 . ILE B 1 456 ? 107.224 127.831 141.222 1.00 35.58  ? 431  ILE B CG2 1 
ATOM   6923  C  CD1 . ILE B 1 456 ? 106.022 125.175 140.320 1.00 41.50  ? 431  ILE B CD1 1 
ATOM   6924  N  N   . LYS B 1 457 ? 107.098 127.871 136.605 1.00 37.44  ? 432  LYS B N   1 
ATOM   6925  C  CA  . LYS B 1 457 ? 107.176 127.434 135.217 1.00 35.59  ? 432  LYS B CA  1 
ATOM   6926  C  C   . LYS B 1 457 ? 108.272 128.173 134.464 1.00 33.44  ? 432  LYS B C   1 
ATOM   6927  O  O   . LYS B 1 457 ? 109.008 127.569 133.677 1.00 35.56  ? 432  LYS B O   1 
ATOM   6928  C  CB  . LYS B 1 457 ? 105.830 127.647 134.531 1.00 34.06  ? 432  LYS B CB  1 
ATOM   6929  C  CG  . LYS B 1 457 ? 105.559 126.709 133.382 1.00 30.96  ? 432  LYS B CG  1 
ATOM   6930  C  CD  . LYS B 1 457 ? 104.377 127.195 132.572 1.00 33.82  ? 432  LYS B CD  1 
ATOM   6931  C  CE  . LYS B 1 457 ? 103.152 127.397 133.447 1.00 36.33  ? 432  LYS B CE  1 
ATOM   6932  N  NZ  . LYS B 1 457 ? 102.882 126.216 134.311 1.00 41.69  ? 432  LYS B NZ  1 
ATOM   6933  N  N   . PHE B 1 458 ? 108.386 129.482 134.690 1.00 37.12  ? 433  PHE B N   1 
ATOM   6934  C  CA  . PHE B 1 458 ? 109.410 130.270 134.014 1.00 42.29  ? 433  PHE B CA  1 
ATOM   6935  C  C   . PHE B 1 458 ? 110.802 129.927 134.524 1.00 43.94  ? 433  PHE B C   1 
ATOM   6936  O  O   . PHE B 1 458 ? 111.766 129.918 133.750 1.00 53.75  ? 433  PHE B O   1 
ATOM   6937  C  CB  . PHE B 1 458 ? 109.135 131.761 134.197 1.00 34.70  ? 433  PHE B CB  1 
ATOM   6938  C  CG  . PHE B 1 458 ? 110.362 132.616 134.078 1.00 28.87  ? 433  PHE B CG  1 
ATOM   6939  C  CD1 . PHE B 1 458 ? 110.905 132.902 132.841 1.00 30.16  ? 433  PHE B CD1 1 
ATOM   6940  C  CD2 . PHE B 1 458 ? 110.985 133.117 135.207 1.00 39.63  ? 433  PHE B CD2 1 
ATOM   6941  C  CE1 . PHE B 1 458 ? 112.035 133.681 132.730 1.00 37.45  ? 433  PHE B CE1 1 
ATOM   6942  C  CE2 . PHE B 1 458 ? 112.117 133.894 135.100 1.00 41.68  ? 433  PHE B CE2 1 
ATOM   6943  C  CZ  . PHE B 1 458 ? 112.643 134.175 133.861 1.00 36.10  ? 433  PHE B CZ  1 
ATOM   6944  N  N   . MET B 1 459 ? 110.936 129.669 135.825 1.00 34.95  ? 434  MET B N   1 
ATOM   6945  C  CA  . MET B 1 459 ? 112.257 129.396 136.378 1.00 29.44  ? 434  MET B CA  1 
ATOM   6946  C  C   . MET B 1 459 ? 112.822 128.083 135.852 1.00 38.58  ? 434  MET B C   1 
ATOM   6947  O  O   . MET B 1 459 ? 114.010 128.002 135.523 1.00 47.49  ? 434  MET B O   1 
ATOM   6948  C  CB  . MET B 1 459 ? 112.195 129.383 137.904 1.00 35.83  ? 434  MET B CB  1 
ATOM   6949  C  CG  . MET B 1 459 ? 113.514 129.718 138.568 1.00 41.07  ? 434  MET B CG  1 
ATOM   6950  S  SD  . MET B 1 459 ? 113.828 131.491 138.603 1.00 51.98  ? 434  MET B SD  1 
ATOM   6951  C  CE  . MET B 1 459 ? 115.618 131.513 138.610 1.00 43.74  ? 434  MET B CE  1 
ATOM   6952  N  N   . TYR B 1 460 ? 111.992 127.048 135.763 1.00 40.23  ? 435  TYR B N   1 
ATOM   6953  C  CA  . TYR B 1 460 ? 112.448 125.721 135.347 1.00 45.54  ? 435  TYR B CA  1 
ATOM   6954  C  C   . TYR B 1 460 ? 112.142 125.469 133.871 1.00 48.63  ? 435  TYR B C   1 
ATOM   6955  O  O   . TYR B 1 460 ? 111.367 124.586 133.507 1.00 49.18  ? 435  TYR B O   1 
ATOM   6956  C  CB  . TYR B 1 460 ? 111.823 124.650 136.235 1.00 41.59  ? 435  TYR B CB  1 
ATOM   6957  C  CG  . TYR B 1 460 ? 112.468 124.563 137.594 1.00 42.10  ? 435  TYR B CG  1 
ATOM   6958  C  CD1 . TYR B 1 460 ? 113.630 123.832 137.785 1.00 44.05  ? 435  TYR B CD1 1 
ATOM   6959  C  CD2 . TYR B 1 460 ? 111.924 125.225 138.684 1.00 45.22  ? 435  TYR B CD2 1 
ATOM   6960  C  CE1 . TYR B 1 460 ? 114.226 123.756 139.023 1.00 43.40  ? 435  TYR B CE1 1 
ATOM   6961  C  CE2 . TYR B 1 460 ? 112.514 125.155 139.926 1.00 45.03  ? 435  TYR B CE2 1 
ATOM   6962  C  CZ  . TYR B 1 460 ? 113.664 124.419 140.089 1.00 46.29  ? 435  TYR B CZ  1 
ATOM   6963  O  OH  . TYR B 1 460 ? 114.255 124.346 141.326 1.00 52.59  ? 435  TYR B OH  1 
ATOM   6964  N  N   . THR B 1 461 ? 112.776 126.265 133.013 1.00 32.90  ? 436  THR B N   1 
ATOM   6965  C  CA  . THR B 1 461 ? 112.734 126.022 131.579 1.00 33.79  ? 436  THR B CA  1 
ATOM   6966  C  C   . THR B 1 461 ? 113.944 126.688 130.941 1.00 38.56  ? 436  THR B C   1 
ATOM   6967  O  O   . THR B 1 461 ? 114.345 127.781 131.349 1.00 43.53  ? 436  THR B O   1 
ATOM   6968  C  CB  . THR B 1 461 ? 111.440 126.542 130.939 1.00 31.79  ? 436  THR B CB  1 
ATOM   6969  O  OG1 . THR B 1 461 ? 111.544 126.455 129.513 1.00 34.56  ? 436  THR B OG1 1 
ATOM   6970  C  CG2 . THR B 1 461 ? 111.186 127.981 131.328 1.00 32.58  ? 436  THR B CG2 1 
ATOM   6971  N  N   . ASP B 1 462 ? 114.527 126.017 129.952 1.00 43.99  ? 437  ASP B N   1 
ATOM   6972  C  CA  . ASP B 1 462 ? 115.702 126.524 129.253 1.00 44.89  ? 437  ASP B CA  1 
ATOM   6973  C  C   . ASP B 1 462 ? 115.231 127.390 128.092 1.00 52.85  ? 437  ASP B C   1 
ATOM   6974  O  O   . ASP B 1 462 ? 114.605 126.892 127.151 1.00 59.78  ? 437  ASP B O   1 
ATOM   6975  C  CB  . ASP B 1 462 ? 116.578 125.373 128.765 1.00 42.00  ? 437  ASP B CB  1 
ATOM   6976  C  CG  . ASP B 1 462 ? 117.976 125.823 128.392 1.00 51.82  ? 437  ASP B CG  1 
ATOM   6977  O  OD1 . ASP B 1 462 ? 118.235 127.045 128.408 1.00 53.03  ? 437  ASP B OD1 1 
ATOM   6978  O  OD2 . ASP B 1 462 ? 118.818 124.955 128.081 1.00 57.53  ? 437  ASP B OD2 1 
ATOM   6979  N  N   . TRP B 1 463 ? 115.530 128.687 128.156 1.00 45.44  ? 438  TRP B N   1 
ATOM   6980  C  CA  . TRP B 1 463 ? 115.067 129.613 127.132 1.00 39.82  ? 438  TRP B CA  1 
ATOM   6981  C  C   . TRP B 1 463 ? 115.956 129.633 125.897 1.00 47.63  ? 438  TRP B C   1 
ATOM   6982  O  O   . TRP B 1 463 ? 115.543 130.179 124.869 1.00 56.40  ? 438  TRP B O   1 
ATOM   6983  C  CB  . TRP B 1 463 ? 114.950 131.021 127.717 1.00 43.65  ? 438  TRP B CB  1 
ATOM   6984  C  CG  . TRP B 1 463 ? 113.868 131.131 128.744 1.00 41.18  ? 438  TRP B CG  1 
ATOM   6985  C  CD1 . TRP B 1 463 ? 114.027 131.213 130.094 1.00 44.96  ? 438  TRP B CD1 1 
ATOM   6986  C  CD2 . TRP B 1 463 ? 112.458 131.151 128.504 1.00 41.45  ? 438  TRP B CD2 1 
ATOM   6987  N  NE1 . TRP B 1 463 ? 112.803 131.292 130.711 1.00 45.44  ? 438  TRP B NE1 1 
ATOM   6988  C  CE2 . TRP B 1 463 ? 111.823 131.256 129.755 1.00 39.20  ? 438  TRP B CE2 1 
ATOM   6989  C  CE3 . TRP B 1 463 ? 111.670 131.095 127.353 1.00 49.87  ? 438  TRP B CE3 1 
ATOM   6990  C  CZ2 . TRP B 1 463 ? 110.439 131.305 129.887 1.00 40.32  ? 438  TRP B CZ2 1 
ATOM   6991  C  CZ3 . TRP B 1 463 ? 110.296 131.145 127.486 1.00 47.60  ? 438  TRP B CZ3 1 
ATOM   6992  C  CH2 . TRP B 1 463 ? 109.694 131.249 128.743 1.00 41.46  ? 438  TRP B CH2 1 
ATOM   6993  N  N   . ALA B 1 464 ? 117.158 129.058 125.966 1.00 49.94  ? 439  ALA B N   1 
ATOM   6994  C  CA  . ALA B 1 464 ? 117.976 128.901 124.771 1.00 56.01  ? 439  ALA B CA  1 
ATOM   6995  C  C   . ALA B 1 464 ? 117.475 127.779 123.872 1.00 56.81  ? 439  ALA B C   1 
ATOM   6996  O  O   . ALA B 1 464 ? 117.783 127.775 122.675 1.00 53.70  ? 439  ALA B O   1 
ATOM   6997  C  CB  . ALA B 1 464 ? 119.433 128.644 125.156 1.00 52.09  ? 439  ALA B CB  1 
ATOM   6998  N  N   . ASP B 1 465 ? 116.715 126.837 124.421 1.00 57.16  ? 440  ASP B N   1 
ATOM   6999  C  CA  . ASP B 1 465 ? 116.117 125.724 123.690 1.00 53.32  ? 440  ASP B CA  1 
ATOM   7000  C  C   . ASP B 1 465 ? 114.655 125.574 124.087 1.00 56.72  ? 440  ASP B C   1 
ATOM   7001  O  O   . ASP B 1 465 ? 114.182 124.494 124.445 1.00 62.59  ? 440  ASP B O   1 
ATOM   7002  C  CB  . ASP B 1 465 ? 116.891 124.433 123.932 1.00 58.90  ? 440  ASP B CB  1 
ATOM   7003  C  CG  . ASP B 1 465 ? 117.652 123.973 122.705 1.00 67.26  ? 440  ASP B CG  1 
ATOM   7004  O  OD1 . ASP B 1 465 ? 117.524 124.624 121.647 1.00 70.61  ? 440  ASP B OD1 1 
ATOM   7005  O  OD2 . ASP B 1 465 ? 118.377 122.960 122.796 1.00 68.73  ? 440  ASP B OD2 1 
ATOM   7006  N  N   . ARG B 1 466 ? 113.928 126.694 124.041 1.00 54.56  ? 441  ARG B N   1 
ATOM   7007  C  CA  . ARG B 1 466 ? 112.562 126.745 124.555 1.00 56.81  ? 441  ARG B CA  1 
ATOM   7008  C  C   . ARG B 1 466 ? 111.652 125.721 123.889 1.00 58.92  ? 441  ARG B C   1 
ATOM   7009  O  O   . ARG B 1 466 ? 110.742 125.189 124.536 1.00 58.32  ? 441  ARG B O   1 
ATOM   7010  C  CB  . ARG B 1 466 ? 112.008 128.158 124.371 1.00 56.56  ? 441  ARG B CB  1 
ATOM   7011  C  CG  . ARG B 1 466 ? 110.511 128.305 124.576 1.00 58.10  ? 441  ARG B CG  1 
ATOM   7012  C  CD  . ARG B 1 466 ? 109.980 129.600 123.961 1.00 57.28  ? 441  ARG B CD  1 
ATOM   7013  N  NE  . ARG B 1 466 ? 110.806 130.762 124.270 1.00 56.18  ? 441  ARG B NE  1 
ATOM   7014  C  CZ  . ARG B 1 466 ? 111.706 131.288 123.449 1.00 59.77  ? 441  ARG B CZ  1 
ATOM   7015  N  NH1 . ARG B 1 466 ? 111.929 130.776 122.250 1.00 61.74  ? 441  ARG B NH1 1 
ATOM   7016  N  NH2 . ARG B 1 466 ? 112.402 132.350 123.842 1.00 57.61  ? 441  ARG B NH2 1 
ATOM   7017  N  N   . ASP B 1 467 ? 111.880 125.419 122.611 1.00 65.04  ? 442  ASP B N   1 
ATOM   7018  C  CA  . ASP B 1 467 ? 111.051 124.471 121.876 1.00 61.64  ? 442  ASP B CA  1 
ATOM   7019  C  C   . ASP B 1 467 ? 111.763 123.146 121.624 1.00 64.46  ? 442  ASP B C   1 
ATOM   7020  O  O   . ASP B 1 467 ? 111.426 122.439 120.669 1.00 66.81  ? 442  ASP B O   1 
ATOM   7021  C  CB  . ASP B 1 467 ? 110.591 125.084 120.554 1.00 59.40  ? 442  ASP B CB  1 
ATOM   7022  N  N   . ASN B 1 468 ? 112.745 122.798 122.460 1.00 66.03  ? 443  ASN B N   1 
ATOM   7023  C  CA  . ASN B 1 468 ? 113.478 121.550 122.264 1.00 61.91  ? 443  ASN B CA  1 
ATOM   7024  C  C   . ASN B 1 468 ? 112.573 120.338 122.444 1.00 61.06  ? 443  ASN B C   1 
ATOM   7025  O  O   . ASN B 1 468 ? 112.661 119.370 121.681 1.00 66.95  ? 443  ASN B O   1 
ATOM   7026  C  CB  . ASN B 1 468 ? 114.662 121.479 123.227 1.00 63.51  ? 443  ASN B CB  1 
ATOM   7027  C  CG  . ASN B 1 468 ? 115.752 120.540 122.746 1.00 64.71  ? 443  ASN B CG  1 
ATOM   7028  O  OD1 . ASN B 1 468 ? 115.473 119.498 122.154 1.00 66.84  ? 443  ASN B OD1 1 
ATOM   7029  N  ND2 . ASN B 1 468 ? 117.002 120.905 123.001 1.00 64.53  ? 443  ASN B ND2 1 
ATOM   7030  N  N   . GLY B 1 469 ? 111.699 120.371 123.445 1.00 62.26  ? 444  GLY B N   1 
ATOM   7031  C  CA  . GLY B 1 469 ? 110.838 119.238 123.721 1.00 65.07  ? 444  GLY B CA  1 
ATOM   7032  C  C   . GLY B 1 469 ? 111.509 118.201 124.596 1.00 64.94  ? 444  GLY B C   1 
ATOM   7033  O  O   . GLY B 1 469 ? 111.013 117.876 125.679 1.00 62.54  ? 444  GLY B O   1 
ATOM   7034  N  N   . GLU B 1 470 ? 112.642 117.671 124.132 1.00 70.09  ? 445  GLU B N   1 
ATOM   7035  C  CA  . GLU B 1 470 ? 113.400 116.723 124.942 1.00 66.56  ? 445  GLU B CA  1 
ATOM   7036  C  C   . GLU B 1 470 ? 113.969 117.397 126.183 1.00 70.30  ? 445  GLU B C   1 
ATOM   7037  O  O   . GLU B 1 470 ? 114.041 116.782 127.254 1.00 71.27  ? 445  GLU B O   1 
ATOM   7038  C  CB  . GLU B 1 470 ? 114.514 116.093 124.105 1.00 66.78  ? 445  GLU B CB  1 
ATOM   7039  C  CG  . GLU B 1 470 ? 115.579 115.363 124.909 1.00 68.15  ? 445  GLU B CG  1 
ATOM   7040  C  CD  . GLU B 1 470 ? 116.784 116.232 125.211 1.00 73.50  ? 445  GLU B CD  1 
ATOM   7041  O  OE1 . GLU B 1 470 ? 117.454 116.677 124.255 1.00 74.55  ? 445  GLU B OE1 1 
ATOM   7042  O  OE2 . GLU B 1 470 ? 117.060 116.473 126.406 1.00 73.56  ? 445  GLU B OE2 1 
ATOM   7043  N  N   . MET B 1 471 ? 114.368 118.664 126.065 1.00 70.60  ? 446  MET B N   1 
ATOM   7044  C  CA  . MET B 1 471 ? 114.888 119.405 127.207 1.00 65.22  ? 446  MET B CA  1 
ATOM   7045  C  C   . MET B 1 471 ? 113.704 119.967 127.992 1.00 66.60  ? 446  MET B C   1 
ATOM   7046  O  O   . MET B 1 471 ? 113.622 121.169 128.266 1.00 67.74  ? 446  MET B O   1 
ATOM   7047  C  CB  . MET B 1 471 ? 115.859 120.496 126.731 1.00 65.42  ? 446  MET B CB  1 
ATOM   7048  C  CG  . MET B 1 471 ? 116.450 121.402 127.812 1.00 69.48  ? 446  MET B CG  1 
ATOM   7049  S  SD  . MET B 1 471 ? 118.073 120.862 128.377 1.00 82.80  ? 446  MET B SD  1 
ATOM   7050  C  CE  . MET B 1 471 ? 119.131 121.696 127.197 1.00 66.99  ? 446  MET B CE  1 
ATOM   7051  N  N   . ARG B 1 472 ? 112.748 119.099 128.312 1.00 48.10  ? 447  ARG B N   1 
ATOM   7052  C  CA  . ARG B 1 472 ? 111.686 119.436 129.248 1.00 44.26  ? 447  ARG B CA  1 
ATOM   7053  C  C   . ARG B 1 472 ? 111.580 118.324 130.281 1.00 49.10  ? 447  ARG B C   1 
ATOM   7054  O  O   . ARG B 1 472 ? 111.245 118.573 131.443 1.00 58.82  ? 447  ARG B O   1 
ATOM   7055  C  CB  . ARG B 1 472 ? 110.360 119.651 128.518 1.00 46.17  ? 447  ARG B CB  1 
ATOM   7056  C  CG  . ARG B 1 472 ? 109.651 120.933 128.920 1.00 45.48  ? 447  ARG B CG  1 
ATOM   7057  C  CD  . ARG B 1 472 ? 108.605 121.345 127.901 1.00 53.21  ? 447  ARG B CD  1 
ATOM   7058  N  NE  . ARG B 1 472 ? 109.177 121.544 126.575 1.00 58.03  ? 447  ARG B NE  1 
ATOM   7059  C  CZ  . ARG B 1 472 ? 108.471 121.848 125.495 1.00 56.67  ? 447  ARG B CZ  1 
ATOM   7060  N  NH1 . ARG B 1 472 ? 107.158 121.993 125.546 1.00 49.12  ? 447  ARG B NH1 1 
ATOM   7061  N  NH2 . ARG B 1 472 ? 109.099 122.013 124.334 1.00 57.53  ? 447  ARG B NH2 1 
ATOM   7062  N  N   . ARG B 1 473 ? 111.895 117.095 129.867 1.00 49.73  ? 448  ARG B N   1 
ATOM   7063  C  CA  . ARG B 1 473 ? 112.035 116.006 130.826 1.00 47.92  ? 448  ARG B CA  1 
ATOM   7064  C  C   . ARG B 1 473 ? 113.143 116.308 131.823 1.00 49.38  ? 448  ARG B C   1 
ATOM   7065  O  O   . ARG B 1 473 ? 112.982 116.094 133.032 1.00 57.55  ? 448  ARG B O   1 
ATOM   7066  C  CB  . ARG B 1 473 ? 112.329 114.697 130.095 1.00 51.10  ? 448  ARG B CB  1 
ATOM   7067  C  CG  . ARG B 1 473 ? 111.110 113.983 129.551 1.00 54.39  ? 448  ARG B CG  1 
ATOM   7068  C  CD  . ARG B 1 473 ? 111.501 112.662 128.916 1.00 56.57  ? 448  ARG B CD  1 
ATOM   7069  N  NE  . ARG B 1 473 ? 112.827 112.725 128.313 1.00 59.48  ? 448  ARG B NE  1 
ATOM   7070  C  CZ  . ARG B 1 473 ? 113.361 111.763 127.574 1.00 60.98  ? 448  ARG B CZ  1 
ATOM   7071  N  NH1 . ARG B 1 473 ? 112.705 110.643 127.319 1.00 62.27  ? 448  ARG B NH1 1 
ATOM   7072  N  NH2 . ARG B 1 473 ? 114.583 111.930 127.076 1.00 57.52  ? 448  ARG B NH2 1 
ATOM   7073  N  N   . LYS B 1 474 ? 114.275 116.815 131.331 1.00 40.50  ? 449  LYS B N   1 
ATOM   7074  C  CA  . LYS B 1 474 ? 115.379 117.170 132.213 1.00 37.05  ? 449  LYS B CA  1 
ATOM   7075  C  C   . LYS B 1 474 ? 114.963 118.252 133.199 1.00 42.00  ? 449  LYS B C   1 
ATOM   7076  O  O   . LYS B 1 474 ? 115.283 118.171 134.389 1.00 47.94  ? 449  LYS B O   1 
ATOM   7077  C  CB  . LYS B 1 474 ? 116.580 117.632 131.390 1.00 39.84  ? 449  LYS B CB  1 
ATOM   7078  C  CG  . LYS B 1 474 ? 117.578 116.535 131.067 1.00 45.33  ? 449  LYS B CG  1 
ATOM   7079  C  CD  . LYS B 1 474 ? 118.280 116.030 132.315 1.00 45.95  ? 449  LYS B CD  1 
ATOM   7080  C  CE  . LYS B 1 474 ? 119.237 114.897 131.984 1.00 45.13  ? 449  LYS B CE  1 
ATOM   7081  N  NZ  . LYS B 1 474 ? 120.265 115.315 130.990 1.00 50.14  ? 449  LYS B NZ  1 
ATOM   7082  N  N   . THR B 1 475 ? 114.233 119.265 132.727 1.00 36.61  ? 450  THR B N   1 
ATOM   7083  C  CA  . THR B 1 475 ? 113.841 120.358 133.611 1.00 33.07  ? 450  THR B CA  1 
ATOM   7084  C  C   . THR B 1 475 ? 112.800 119.908 134.629 1.00 37.64  ? 450  THR B C   1 
ATOM   7085  O  O   . THR B 1 475 ? 112.824 120.354 135.777 1.00 48.33  ? 450  THR B O   1 
ATOM   7086  C  CB  . THR B 1 475 ? 113.316 121.539 132.798 1.00 33.00  ? 450  THR B CB  1 
ATOM   7087  O  OG1 . THR B 1 475 ? 112.090 121.170 132.155 1.00 45.35  ? 450  THR B OG1 1 
ATOM   7088  C  CG2 . THR B 1 475 ? 114.332 121.950 131.747 1.00 36.50  ? 450  THR B CG2 1 
ATOM   7089  N  N   . LEU B 1 476 ? 111.884 119.019 134.237 1.00 30.95  ? 451  LEU B N   1 
ATOM   7090  C  CA  . LEU B 1 476 ? 110.909 118.501 135.193 1.00 31.36  ? 451  LEU B CA  1 
ATOM   7091  C  C   . LEU B 1 476 ? 111.580 117.642 136.259 1.00 34.84  ? 451  LEU B C   1 
ATOM   7092  O  O   . LEU B 1 476 ? 111.263 117.751 137.455 1.00 38.08  ? 451  LEU B O   1 
ATOM   7093  C  CB  . LEU B 1 476 ? 109.840 117.699 134.455 1.00 30.00  ? 451  LEU B CB  1 
ATOM   7094  C  CG  . LEU B 1 476 ? 108.613 118.486 134.003 1.00 26.44  ? 451  LEU B CG  1 
ATOM   7095  C  CD1 . LEU B 1 476 ? 107.575 117.553 133.411 1.00 31.13  ? 451  LEU B CD1 1 
ATOM   7096  C  CD2 . LEU B 1 476 ? 108.037 119.275 135.162 1.00 34.83  ? 451  LEU B CD2 1 
ATOM   7097  N  N   . LEU B 1 477 ? 112.510 116.778 135.842 1.00 31.27  ? 452  LEU B N   1 
ATOM   7098  C  CA  . LEU B 1 477 ? 113.261 115.978 136.801 1.00 27.63  ? 452  LEU B CA  1 
ATOM   7099  C  C   . LEU B 1 477 ? 114.067 116.869 137.737 1.00 35.25  ? 452  LEU B C   1 
ATOM   7100  O  O   . LEU B 1 477 ? 114.123 116.621 138.949 1.00 40.07  ? 452  LEU B O   1 
ATOM   7101  C  CB  . LEU B 1 477 ? 114.167 115.002 136.053 1.00 16.71  ? 452  LEU B CB  1 
ATOM   7102  C  CG  . LEU B 1 477 ? 115.456 114.543 136.729 1.00 26.78  ? 452  LEU B CG  1 
ATOM   7103  C  CD1 . LEU B 1 477 ? 115.147 113.588 137.862 1.00 31.66  ? 452  LEU B CD1 1 
ATOM   7104  C  CD2 . LEU B 1 477 ? 116.381 113.892 135.716 1.00 33.03  ? 452  LEU B CD2 1 
ATOM   7105  N  N   . ALA B 1 478 ? 114.685 117.921 137.195 1.00 28.15  ? 453  ALA B N   1 
ATOM   7106  C  CA  . ALA B 1 478 ? 115.416 118.869 138.026 1.00 30.33  ? 453  ALA B CA  1 
ATOM   7107  C  C   . ALA B 1 478 ? 114.486 119.590 138.990 1.00 34.17  ? 453  ALA B C   1 
ATOM   7108  O  O   . ALA B 1 478 ? 114.859 119.855 140.134 1.00 43.77  ? 453  ALA B O   1 
ATOM   7109  C  CB  . ALA B 1 478 ? 116.162 119.871 137.147 1.00 28.13  ? 453  ALA B CB  1 
ATOM   7110  N  N   . LEU B 1 479 ? 113.273 119.919 138.545 1.00 31.66  ? 454  LEU B N   1 
ATOM   7111  C  CA  . LEU B 1 479 ? 112.298 120.562 139.420 1.00 36.36  ? 454  LEU B CA  1 
ATOM   7112  C  C   . LEU B 1 479 ? 111.977 119.680 140.617 1.00 33.34  ? 454  LEU B C   1 
ATOM   7113  O  O   . LEU B 1 479 ? 112.042 120.125 141.772 1.00 42.93  ? 454  LEU B O   1 
ATOM   7114  C  CB  . LEU B 1 479 ? 111.030 120.880 138.623 1.00 34.87  ? 454  LEU B CB  1 
ATOM   7115  C  CG  . LEU B 1 479 ? 109.674 121.054 139.315 1.00 31.53  ? 454  LEU B CG  1 
ATOM   7116  C  CD1 . LEU B 1 479 ? 109.721 122.099 140.408 1.00 38.12  ? 454  LEU B CD1 1 
ATOM   7117  C  CD2 . LEU B 1 479 ? 108.602 121.399 138.298 1.00 34.95  ? 454  LEU B CD2 1 
ATOM   7118  N  N   . PHE B 1 480 ? 111.635 118.416 140.360 1.00 28.65  ? 455  PHE B N   1 
ATOM   7119  C  CA  . PHE B 1 480 ? 111.298 117.525 141.467 1.00 31.41  ? 455  PHE B CA  1 
ATOM   7120  C  C   . PHE B 1 480 ? 112.495 117.305 142.384 1.00 35.75  ? 455  PHE B C   1 
ATOM   7121  O  O   . PHE B 1 480 ? 112.363 117.357 143.615 1.00 42.36  ? 455  PHE B O   1 
ATOM   7122  C  CB  . PHE B 1 480 ? 110.777 116.189 140.946 1.00 32.29  ? 455  PHE B CB  1 
ATOM   7123  C  CG  . PHE B 1 480 ? 109.953 115.437 141.949 1.00 31.89  ? 455  PHE B CG  1 
ATOM   7124  C  CD1 . PHE B 1 480 ? 108.921 116.065 142.624 1.00 32.72  ? 455  PHE B CD1 1 
ATOM   7125  C  CD2 . PHE B 1 480 ? 110.218 114.109 142.230 1.00 35.96  ? 455  PHE B CD2 1 
ATOM   7126  C  CE1 . PHE B 1 480 ? 108.164 115.379 143.551 1.00 39.97  ? 455  PHE B CE1 1 
ATOM   7127  C  CE2 . PHE B 1 480 ? 109.466 113.421 143.157 1.00 34.71  ? 455  PHE B CE2 1 
ATOM   7128  C  CZ  . PHE B 1 480 ? 108.437 114.056 143.817 1.00 34.97  ? 455  PHE B CZ  1 
ATOM   7129  N  N   . THR B 1 481 ? 113.677 117.075 141.804 1.00 30.85  ? 456  THR B N   1 
ATOM   7130  C  CA  . THR B 1 481 ? 114.870 116.846 142.611 1.00 26.65  ? 456  THR B CA  1 
ATOM   7131  C  C   . THR B 1 481 ? 115.201 118.062 143.465 1.00 31.98  ? 456  THR B C   1 
ATOM   7132  O  O   . THR B 1 481 ? 115.539 117.928 144.647 1.00 36.63  ? 456  THR B O   1 
ATOM   7133  C  CB  . THR B 1 481 ? 116.047 116.488 141.704 1.00 29.83  ? 456  THR B CB  1 
ATOM   7134  O  OG1 . THR B 1 481 ? 115.843 115.184 141.149 1.00 38.95  ? 456  THR B OG1 1 
ATOM   7135  C  CG2 . THR B 1 481 ? 117.349 116.499 142.482 1.00 31.47  ? 456  THR B CG2 1 
ATOM   7136  N  N   . ASP B 1 482 ? 115.102 119.260 142.887 1.00 32.31  ? 457  ASP B N   1 
ATOM   7137  C  CA  . ASP B 1 482 ? 115.416 120.477 143.620 1.00 28.74  ? 457  ASP B CA  1 
ATOM   7138  C  C   . ASP B 1 482 ? 114.434 120.711 144.755 1.00 33.79  ? 457  ASP B C   1 
ATOM   7139  O  O   . ASP B 1 482 ? 114.838 121.093 145.857 1.00 41.61  ? 457  ASP B O   1 
ATOM   7140  C  CB  . ASP B 1 482 ? 115.423 121.672 142.669 1.00 27.23  ? 457  ASP B CB  1 
ATOM   7141  C  CG  . ASP B 1 482 ? 116.695 121.763 141.860 1.00 38.14  ? 457  ASP B CG  1 
ATOM   7142  O  OD1 . ASP B 1 482 ? 117.725 121.226 142.312 1.00 45.92  ? 457  ASP B OD1 1 
ATOM   7143  O  OD2 . ASP B 1 482 ? 116.664 122.370 140.771 1.00 39.16  ? 457  ASP B OD2 1 
ATOM   7144  N  N   . HIS B 1 483 ? 113.138 120.493 144.515 1.00 41.57  ? 458  HIS B N   1 
ATOM   7145  C  CA  . HIS B 1 483 ? 112.183 120.780 145.579 1.00 42.40  ? 458  HIS B CA  1 
ATOM   7146  C  C   . HIS B 1 483 ? 112.264 119.752 146.698 1.00 49.02  ? 458  HIS B C   1 
ATOM   7147  O  O   . HIS B 1 483 ? 112.257 120.117 147.879 1.00 56.47  ? 458  HIS B O   1 
ATOM   7148  C  CB  . HIS B 1 483 ? 110.757 120.845 145.047 1.00 47.83  ? 458  HIS B CB  1 
ATOM   7149  C  CG  . HIS B 1 483 ? 109.762 121.248 146.090 1.00 46.06  ? 458  HIS B CG  1 
ATOM   7150  N  ND1 . HIS B 1 483 ? 108.479 120.751 146.135 1.00 48.98  ? 458  HIS B ND1 1 
ATOM   7151  C  CD2 . HIS B 1 483 ? 109.872 122.098 147.137 1.00 49.65  ? 458  HIS B CD2 1 
ATOM   7152  C  CE1 . HIS B 1 483 ? 107.839 121.282 147.161 1.00 49.31  ? 458  HIS B CE1 1 
ATOM   7153  N  NE2 . HIS B 1 483 ? 108.662 122.103 147.786 1.00 47.28  ? 458  HIS B NE2 1 
ATOM   7154  N  N   . GLN B 1 484 ? 112.339 118.465 146.357 1.00 45.74  ? 459  GLN B N   1 
ATOM   7155  C  CA  . GLN B 1 484 ? 112.182 117.440 147.382 1.00 33.35  ? 459  GLN B CA  1 
ATOM   7156  C  C   . GLN B 1 484 ? 113.491 116.994 148.015 1.00 35.70  ? 459  GLN B C   1 
ATOM   7157  O  O   . GLN B 1 484 ? 113.503 116.654 149.203 1.00 45.01  ? 459  GLN B O   1 
ATOM   7158  C  CB  . GLN B 1 484 ? 111.456 116.223 146.802 1.00 30.08  ? 459  GLN B CB  1 
ATOM   7159  C  CG  . GLN B 1 484 ? 110.041 116.521 146.357 1.00 38.15  ? 459  GLN B CG  1 
ATOM   7160  C  CD  . GLN B 1 484 ? 109.040 116.370 147.483 1.00 38.55  ? 459  GLN B CD  1 
ATOM   7161  O  OE1 . GLN B 1 484 ? 108.685 117.341 148.148 1.00 40.02  ? 459  GLN B OE1 1 
ATOM   7162  N  NE2 . GLN B 1 484 ? 108.577 115.147 147.701 1.00 46.32  ? 459  GLN B NE2 1 
ATOM   7163  N  N   . TRP B 1 485 ? 114.593 116.990 147.272 1.00 34.19  ? 460  TRP B N   1 
ATOM   7164  C  CA  . TRP B 1 485 ? 115.826 116.396 147.769 1.00 25.68  ? 460  TRP B CA  1 
ATOM   7165  C  C   . TRP B 1 485 ? 116.991 117.364 147.904 1.00 18.72  ? 460  TRP B C   1 
ATOM   7166  O  O   . TRP B 1 485 ? 117.791 117.204 148.826 1.00 27.40  ? 460  TRP B O   1 
ATOM   7167  C  CB  . TRP B 1 485 ? 116.263 115.244 146.858 1.00 29.07  ? 460  TRP B CB  1 
ATOM   7168  C  CG  . TRP B 1 485 ? 115.503 113.984 147.083 1.00 32.00  ? 460  TRP B CG  1 
ATOM   7169  C  CD1 . TRP B 1 485 ? 115.620 113.133 148.141 1.00 32.45  ? 460  TRP B CD1 1 
ATOM   7170  C  CD2 . TRP B 1 485 ? 114.522 113.413 146.214 1.00 27.46  ? 460  TRP B CD2 1 
ATOM   7171  N  NE1 . TRP B 1 485 ? 114.763 112.072 147.989 1.00 26.68  ? 460  TRP B NE1 1 
ATOM   7172  C  CE2 . TRP B 1 485 ? 114.077 112.222 146.813 1.00 31.52  ? 460  TRP B CE2 1 
ATOM   7173  C  CE3 . TRP B 1 485 ? 113.970 113.799 144.991 1.00 30.63  ? 460  TRP B CE3 1 
ATOM   7174  C  CZ2 . TRP B 1 485 ? 113.111 111.412 146.229 1.00 35.61  ? 460  TRP B CZ2 1 
ATOM   7175  C  CZ3 . TRP B 1 485 ? 113.011 112.995 144.415 1.00 28.15  ? 460  TRP B CZ3 1 
ATOM   7176  C  CH2 . TRP B 1 485 ? 112.589 111.817 145.034 1.00 27.95  ? 460  TRP B CH2 1 
ATOM   7177  N  N   . VAL B 1 486 ? 117.118 118.349 147.021 1.00 11.28  ? 461  VAL B N   1 
ATOM   7178  C  CA  . VAL B 1 486 ? 118.292 119.219 147.029 1.00 19.35  ? 461  VAL B CA  1 
ATOM   7179  C  C   . VAL B 1 486 ? 118.100 120.408 147.960 1.00 25.96  ? 461  VAL B C   1 
ATOM   7180  O  O   . VAL B 1 486 ? 118.966 120.704 148.788 1.00 36.82  ? 461  VAL B O   1 
ATOM   7181  C  CB  . VAL B 1 486 ? 118.627 119.673 145.592 1.00 23.03  ? 461  VAL B CB  1 
ATOM   7182  C  CG1 . VAL B 1 486 ? 119.502 120.914 145.614 1.00 5.67   ? 461  VAL B CG1 1 
ATOM   7183  C  CG2 . VAL B 1 486 ? 119.317 118.552 144.834 1.00 27.06  ? 461  VAL B CG2 1 
ATOM   7184  N  N   . ALA B 1 487 ? 116.975 121.112 147.841 1.00 31.12  ? 462  ALA B N   1 
ATOM   7185  C  CA  . ALA B 1 487 ? 116.726 122.250 148.725 1.00 26.05  ? 462  ALA B CA  1 
ATOM   7186  C  C   . ALA B 1 487 ? 116.648 121.851 150.193 1.00 29.18  ? 462  ALA B C   1 
ATOM   7187  O  O   . ALA B 1 487 ? 117.263 122.541 151.024 1.00 40.50  ? 462  ALA B O   1 
ATOM   7188  C  CB  . ALA B 1 487 ? 115.464 122.995 148.278 1.00 22.54  ? 462  ALA B CB  1 
ATOM   7189  N  N   . PRO B 1 488 ? 115.915 120.801 150.594 1.00 14.30  ? 463  PRO B N   1 
ATOM   7190  C  CA  . PRO B 1 488 ? 115.959 120.407 152.012 1.00 11.29  ? 463  PRO B CA  1 
ATOM   7191  C  C   . PRO B 1 488 ? 117.344 120.009 152.489 1.00 23.33  ? 463  PRO B C   1 
ATOM   7192  O  O   . PRO B 1 488 ? 117.713 120.319 153.628 1.00 31.75  ? 463  PRO B O   1 
ATOM   7193  C  CB  . PRO B 1 488 ? 114.977 119.230 152.073 1.00 19.18  ? 463  PRO B CB  1 
ATOM   7194  C  CG  . PRO B 1 488 ? 114.047 119.472 150.951 1.00 20.66  ? 463  PRO B CG  1 
ATOM   7195  C  CD  . PRO B 1 488 ? 114.915 120.007 149.857 1.00 25.28  ? 463  PRO B CD  1 
ATOM   7196  N  N   . ALA B 1 489 ? 118.129 119.335 151.645 1.00 21.33  ? 464  ALA B N   1 
ATOM   7197  C  CA  . ALA B 1 489 ? 119.479 118.951 152.043 1.00 9.75   ? 464  ALA B CA  1 
ATOM   7198  C  C   . ALA B 1 489 ? 120.359 120.174 152.257 1.00 24.09  ? 464  ALA B C   1 
ATOM   7199  O  O   . ALA B 1 489 ? 121.095 120.254 153.247 1.00 36.09  ? 464  ALA B O   1 
ATOM   7200  C  CB  . ALA B 1 489 ? 120.094 118.023 150.998 1.00 6.44   ? 464  ALA B CB  1 
ATOM   7201  N  N   . VAL B 1 490 ? 120.288 121.146 151.345 1.00 21.51  ? 465  VAL B N   1 
ATOM   7202  C  CA  . VAL B 1 490 ? 121.077 122.364 151.503 1.00 10.83  ? 465  VAL B CA  1 
ATOM   7203  C  C   . VAL B 1 490 ? 120.625 123.132 152.738 1.00 19.54  ? 465  VAL B C   1 
ATOM   7204  O  O   . VAL B 1 490 ? 121.449 123.662 153.494 1.00 34.17  ? 465  VAL B O   1 
ATOM   7205  C  CB  . VAL B 1 490 ? 120.992 123.227 150.231 1.00 4.00   ? 465  VAL B CB  1 
ATOM   7206  C  CG1 . VAL B 1 490 ? 121.497 124.629 150.504 1.00 16.29  ? 465  VAL B CG1 1 
ATOM   7207  C  CG2 . VAL B 1 490 ? 121.789 122.590 149.111 1.00 9.88   ? 465  VAL B CG2 1 
ATOM   7208  N  N   . ALA B 1 491 ? 119.311 123.199 152.970 1.00 17.09  ? 466  ALA B N   1 
ATOM   7209  C  CA  . ALA B 1 491 ? 118.803 123.915 154.134 1.00 17.20  ? 466  ALA B CA  1 
ATOM   7210  C  C   . ALA B 1 491 ? 119.266 123.270 155.434 1.00 20.88  ? 466  ALA B C   1 
ATOM   7211  O  O   . ALA B 1 491 ? 119.698 123.967 156.359 1.00 28.33  ? 466  ALA B O   1 
ATOM   7212  C  CB  . ALA B 1 491 ? 117.278 123.984 154.085 1.00 18.88  ? 466  ALA B CB  1 
ATOM   7213  N  N   . THR B 1 492 ? 119.194 121.939 155.526 1.00 21.45  ? 467  THR B N   1 
ATOM   7214  C  CA  . THR B 1 492 ? 119.625 121.291 156.759 1.00 22.42  ? 467  THR B CA  1 
ATOM   7215  C  C   . THR B 1 492 ? 121.137 121.370 156.930 1.00 24.12  ? 467  THR B C   1 
ATOM   7216  O  O   . THR B 1 492 ? 121.620 121.498 158.060 1.00 34.85  ? 467  THR B O   1 
ATOM   7217  C  CB  . THR B 1 492 ? 119.138 119.838 156.814 1.00 17.21  ? 467  THR B CB  1 
ATOM   7218  O  OG1 . THR B 1 492 ? 119.386 119.303 158.119 1.00 26.15  ? 467  THR B OG1 1 
ATOM   7219  C  CG2 . THR B 1 492 ? 119.840 118.975 155.791 1.00 18.30  ? 467  THR B CG2 1 
ATOM   7220  N  N   . ALA B 1 493 ? 121.898 121.341 155.831 1.00 15.02  ? 468  ALA B N   1 
ATOM   7221  C  CA  . ALA B 1 493 ? 123.340 121.527 155.937 1.00 12.65  ? 468  ALA B CA  1 
ATOM   7222  C  C   . ALA B 1 493 ? 123.677 122.921 156.449 1.00 16.13  ? 468  ALA B C   1 
ATOM   7223  O  O   . ALA B 1 493 ? 124.570 123.081 157.288 1.00 27.92  ? 468  ALA B O   1 
ATOM   7224  C  CB  . ALA B 1 493 ? 124.003 121.272 154.584 1.00 7.29   ? 468  ALA B CB  1 
ATOM   7225  N  N   . LYS B 1 494 ? 122.973 123.943 155.957 1.00 23.15  ? 469  LYS B N   1 
ATOM   7226  C  CA  . LYS B 1 494 ? 123.220 125.302 156.430 1.00 23.79  ? 469  LYS B CA  1 
ATOM   7227  C  C   . LYS B 1 494 ? 122.820 125.468 157.891 1.00 30.64  ? 469  LYS B C   1 
ATOM   7228  O  O   . LYS B 1 494 ? 123.534 126.119 158.661 1.00 40.06  ? 469  LYS B O   1 
ATOM   7229  C  CB  . LYS B 1 494 ? 122.479 126.313 155.557 1.00 18.58  ? 469  LYS B CB  1 
ATOM   7230  C  CG  . LYS B 1 494 ? 123.017 126.419 154.144 1.00 28.08  ? 469  LYS B CG  1 
ATOM   7231  C  CD  . LYS B 1 494 ? 122.498 127.662 153.439 1.00 30.32  ? 469  LYS B CD  1 
ATOM   7232  C  CE  . LYS B 1 494 ? 121.009 127.855 153.664 1.00 36.51  ? 469  LYS B CE  1 
ATOM   7233  N  NZ  . LYS B 1 494 ? 120.508 129.094 153.010 1.00 32.93  ? 469  LYS B NZ  1 
ATOM   7234  N  N   . LEU B 1 495 ? 121.681 124.897 158.292 1.00 24.47  ? 470  LEU B N   1 
ATOM   7235  C  CA  . LEU B 1 495 ? 121.261 125.015 159.687 1.00 23.07  ? 470  LEU B CA  1 
ATOM   7236  C  C   . LEU B 1 495 ? 122.185 124.251 160.629 1.00 27.23  ? 470  LEU B C   1 
ATOM   7237  O  O   . LEU B 1 495 ? 122.389 124.681 161.770 1.00 34.06  ? 470  LEU B O   1 
ATOM   7238  C  CB  . LEU B 1 495 ? 119.809 124.558 159.857 1.00 22.28  ? 470  LEU B CB  1 
ATOM   7239  C  CG  . LEU B 1 495 ? 118.651 125.502 159.485 1.00 28.13  ? 470  LEU B CG  1 
ATOM   7240  C  CD1 . LEU B 1 495 ? 118.903 126.358 158.251 1.00 27.76  ? 470  LEU B CD1 1 
ATOM   7241  C  CD2 . LEU B 1 495 ? 117.362 124.712 159.313 1.00 27.20  ? 470  LEU B CD2 1 
ATOM   7242  N  N   . HIS B 1 496 ? 122.755 123.130 160.183 1.00 27.81  ? 471  HIS B N   1 
ATOM   7243  C  CA  . HIS B 1 496 ? 123.711 122.418 161.025 1.00 26.19  ? 471  HIS B CA  1 
ATOM   7244  C  C   . HIS B 1 496 ? 125.044 123.154 161.092 1.00 28.47  ? 471  HIS B C   1 
ATOM   7245  O  O   . HIS B 1 496 ? 125.657 123.241 162.163 1.00 38.67  ? 471  HIS B O   1 
ATOM   7246  C  CB  . HIS B 1 496 ? 123.907 120.994 160.508 1.00 23.27  ? 471  HIS B CB  1 
ATOM   7247  C  CG  . HIS B 1 496 ? 122.867 120.031 160.989 1.00 25.37  ? 471  HIS B CG  1 
ATOM   7248  N  ND1 . HIS B 1 496 ? 121.551 120.098 160.588 1.00 33.49  ? 471  HIS B ND1 1 
ATOM   7249  C  CD2 . HIS B 1 496 ? 122.950 118.976 161.832 1.00 32.06  ? 471  HIS B CD2 1 
ATOM   7250  C  CE1 . HIS B 1 496 ? 120.866 119.128 161.167 1.00 33.16  ? 471  HIS B CE1 1 
ATOM   7251  N  NE2 . HIS B 1 496 ? 121.693 118.432 161.927 1.00 37.28  ? 471  HIS B NE2 1 
ATOM   7252  N  N   . ALA B 1 497 ? 125.509 123.694 159.964 1.00 29.15  ? 472  ALA B N   1 
ATOM   7253  C  CA  . ALA B 1 497 ? 126.782 124.404 159.947 1.00 29.16  ? 472  ALA B CA  1 
ATOM   7254  C  C   . ALA B 1 497 ? 126.712 125.748 160.657 1.00 34.36  ? 472  ALA B C   1 
ATOM   7255  O  O   . ALA B 1 497 ? 127.757 126.290 161.031 1.00 40.76  ? 472  ALA B O   1 
ATOM   7256  C  CB  . ALA B 1 497 ? 127.253 124.602 158.507 1.00 25.54  ? 472  ALA B CB  1 
ATOM   7257  N  N   . ASP B 1 498 ? 125.512 126.300 160.850 1.00 40.03  ? 473  ASP B N   1 
ATOM   7258  C  CA  . ASP B 1 498 ? 125.385 127.584 161.529 1.00 40.56  ? 473  ASP B CA  1 
ATOM   7259  C  C   . ASP B 1 498 ? 125.692 127.487 163.016 1.00 45.90  ? 473  ASP B C   1 
ATOM   7260  O  O   . ASP B 1 498 ? 125.895 128.521 163.661 1.00 50.90  ? 473  ASP B O   1 
ATOM   7261  C  CB  . ASP B 1 498 ? 123.980 128.152 161.328 1.00 37.55  ? 473  ASP B CB  1 
ATOM   7262  C  CG  . ASP B 1 498 ? 123.908 129.134 160.178 1.00 45.52  ? 473  ASP B CG  1 
ATOM   7263  O  OD1 . ASP B 1 498 ? 124.948 129.367 159.527 1.00 46.55  ? 473  ASP B OD1 1 
ATOM   7264  O  OD2 . ASP B 1 498 ? 122.811 129.674 159.924 1.00 47.05  ? 473  ASP B OD2 1 
ATOM   7265  N  N   . TYR B 1 499 ? 125.728 126.278 163.574 1.00 47.31  ? 474  TYR B N   1 
ATOM   7266  C  CA  . TYR B 1 499 ? 126.025 126.070 164.985 1.00 48.98  ? 474  TYR B CA  1 
ATOM   7267  C  C   . TYR B 1 499 ? 127.362 125.362 165.184 1.00 50.18  ? 474  TYR B C   1 
ATOM   7268  O  O   . TYR B 1 499 ? 127.550 124.639 166.166 1.00 48.93  ? 474  TYR B O   1 
ATOM   7269  C  CB  . TYR B 1 499 ? 124.894 125.299 165.660 1.00 43.43  ? 474  TYR B CB  1 
ATOM   7270  C  CG  . TYR B 1 499 ? 123.602 126.080 165.723 1.00 44.86  ? 474  TYR B CG  1 
ATOM   7271  C  CD1 . TYR B 1 499 ? 122.716 126.082 164.655 1.00 46.38  ? 474  TYR B CD1 1 
ATOM   7272  C  CD2 . TYR B 1 499 ? 123.277 126.831 166.843 1.00 50.18  ? 474  TYR B CD2 1 
ATOM   7273  C  CE1 . TYR B 1 499 ? 121.538 126.800 164.706 1.00 48.04  ? 474  TYR B CE1 1 
ATOM   7274  C  CE2 . TYR B 1 499 ? 122.102 127.553 166.903 1.00 52.23  ? 474  TYR B CE2 1 
ATOM   7275  C  CZ  . TYR B 1 499 ? 121.237 127.534 165.831 1.00 51.21  ? 474  TYR B CZ  1 
ATOM   7276  O  OH  . TYR B 1 499 ? 120.065 128.251 165.886 1.00 55.03  ? 474  TYR B OH  1 
ATOM   7277  N  N   . GLN B 1 500 ? 128.292 125.564 164.250 1.00 47.50  ? 475  GLN B N   1 
ATOM   7278  C  CA  . GLN B 1 500 ? 129.675 125.101 164.365 1.00 48.90  ? 475  GLN B CA  1 
ATOM   7279  C  C   . GLN B 1 500 ? 129.748 123.584 164.549 1.00 53.41  ? 475  GLN B C   1 
ATOM   7280  O  O   . GLN B 1 500 ? 130.314 123.070 165.515 1.00 60.25  ? 475  GLN B O   1 
ATOM   7281  C  CB  . GLN B 1 500 ? 130.400 125.834 165.499 1.00 51.72  ? 475  GLN B CB  1 
ATOM   7282  C  CG  . GLN B 1 500 ? 130.104 127.324 165.564 1.00 52.15  ? 475  GLN B CG  1 
ATOM   7283  C  CD  . GLN B 1 500 ? 130.595 128.068 164.339 1.00 56.84  ? 475  GLN B CD  1 
ATOM   7284  O  OE1 . GLN B 1 500 ? 131.628 127.727 163.764 1.00 58.73  ? 475  GLN B OE1 1 
ATOM   7285  N  NE2 . GLN B 1 500 ? 129.852 129.090 163.930 1.00 54.02  ? 475  GLN B NE2 1 
ATOM   7286  N  N   . SER B 1 501 ? 129.164 122.870 163.591 1.00 40.66  ? 476  SER B N   1 
ATOM   7287  C  CA  . SER B 1 501 ? 129.243 121.423 163.539 1.00 39.39  ? 476  SER B CA  1 
ATOM   7288  C  C   . SER B 1 501 ? 129.795 120.999 162.185 1.00 39.37  ? 476  SER B C   1 
ATOM   7289  O  O   . SER B 1 501 ? 129.321 121.490 161.151 1.00 45.87  ? 476  SER B O   1 
ATOM   7290  C  CB  . SER B 1 501 ? 127.866 120.783 163.768 1.00 36.45  ? 476  SER B CB  1 
ATOM   7291  O  OG  . SER B 1 501 ? 127.184 120.595 162.542 1.00 44.28  ? 476  SER B OG  1 
ATOM   7292  N  N   . PRO B 1 502 ? 130.793 120.117 162.143 1.00 34.40  ? 477  PRO B N   1 
ATOM   7293  C  CA  . PRO B 1 502 ? 131.388 119.726 160.855 1.00 38.12  ? 477  PRO B CA  1 
ATOM   7294  C  C   . PRO B 1 502 ? 130.354 119.111 159.926 1.00 40.92  ? 477  PRO B C   1 
ATOM   7295  O  O   . PRO B 1 502 ? 129.742 118.087 160.237 1.00 53.74  ? 477  PRO B O   1 
ATOM   7296  C  CB  . PRO B 1 502 ? 132.464 118.712 161.259 1.00 40.92  ? 477  PRO B CB  1 
ATOM   7297  C  CG  . PRO B 1 502 ? 132.780 119.038 162.679 1.00 37.77  ? 477  PRO B CG  1 
ATOM   7298  C  CD  . PRO B 1 502 ? 131.494 119.509 163.286 1.00 34.75  ? 477  PRO B CD  1 
ATOM   7299  N  N   . VAL B 1 503 ? 130.165 119.747 158.774 1.00 34.52  ? 478  VAL B N   1 
ATOM   7300  C  CA  . VAL B 1 503 ? 129.200 119.317 157.771 1.00 31.28  ? 478  VAL B CA  1 
ATOM   7301  C  C   . VAL B 1 503 ? 129.932 119.128 156.452 1.00 35.52  ? 478  VAL B C   1 
ATOM   7302  O  O   . VAL B 1 503 ? 130.614 120.045 155.981 1.00 52.67  ? 478  VAL B O   1 
ATOM   7303  C  CB  . VAL B 1 503 ? 128.056 120.333 157.619 1.00 28.73  ? 478  VAL B CB  1 
ATOM   7304  C  CG1 . VAL B 1 503 ? 127.281 120.063 156.351 1.00 30.90  ? 478  VAL B CG1 1 
ATOM   7305  C  CG2 . VAL B 1 503 ? 127.140 120.280 158.827 1.00 38.34  ? 478  VAL B CG2 1 
ATOM   7306  N  N   . TYR B 1 504 ? 129.790 117.946 155.857 1.00 39.69  ? 479  TYR B N   1 
ATOM   7307  C  CA  . TYR B 1 504 ? 130.414 117.634 154.576 1.00 39.44  ? 479  TYR B CA  1 
ATOM   7308  C  C   . TYR B 1 504 ? 129.325 117.312 153.563 1.00 44.84  ? 479  TYR B C   1 
ATOM   7309  O  O   . TYR B 1 504 ? 128.520 116.404 153.785 1.00 60.49  ? 479  TYR B O   1 
ATOM   7310  C  CB  . TYR B 1 504 ? 131.387 116.462 154.709 1.00 42.50  ? 479  TYR B CB  1 
ATOM   7311  C  CG  . TYR B 1 504 ? 132.671 116.805 155.428 1.00 39.32  ? 479  TYR B CG  1 
ATOM   7312  C  CD1 . TYR B 1 504 ? 132.690 117.001 156.800 1.00 41.85  ? 479  TYR B CD1 1 
ATOM   7313  C  CD2 . TYR B 1 504 ? 133.864 116.932 154.734 1.00 44.49  ? 479  TYR B CD2 1 
ATOM   7314  C  CE1 . TYR B 1 504 ? 133.858 117.314 157.461 1.00 42.76  ? 479  TYR B CE1 1 
ATOM   7315  C  CE2 . TYR B 1 504 ? 135.039 117.246 155.386 1.00 43.40  ? 479  TYR B CE2 1 
ATOM   7316  C  CZ  . TYR B 1 504 ? 135.030 117.436 156.749 1.00 45.67  ? 479  TYR B CZ  1 
ATOM   7317  O  OH  . TYR B 1 504 ? 136.197 117.749 157.405 1.00 51.20  ? 479  TYR B OH  1 
ATOM   7318  N  N   . PHE B 1 505 ? 129.317 118.030 152.445 1.00 40.65  ? 480  PHE B N   1 
ATOM   7319  C  CA  . PHE B 1 505 ? 128.289 117.890 151.421 1.00 42.07  ? 480  PHE B CA  1 
ATOM   7320  C  C   . PHE B 1 505 ? 128.868 117.169 150.212 1.00 48.58  ? 480  PHE B C   1 
ATOM   7321  O  O   . PHE B 1 505 ? 129.950 117.525 149.737 1.00 60.71  ? 480  PHE B O   1 
ATOM   7322  C  CB  . PHE B 1 505 ? 127.747 119.261 151.012 1.00 48.36  ? 480  PHE B CB  1 
ATOM   7323  C  CG  . PHE B 1 505 ? 126.423 119.211 150.304 1.00 46.51  ? 480  PHE B CG  1 
ATOM   7324  C  CD1 . PHE B 1 505 ? 126.349 118.886 148.961 1.00 51.01  ? 480  PHE B CD1 1 
ATOM   7325  C  CD2 . PHE B 1 505 ? 125.253 119.501 150.981 1.00 46.24  ? 480  PHE B CD2 1 
ATOM   7326  C  CE1 . PHE B 1 505 ? 125.134 118.845 148.310 1.00 49.34  ? 480  PHE B CE1 1 
ATOM   7327  C  CE2 . PHE B 1 505 ? 124.036 119.461 150.335 1.00 50.29  ? 480  PHE B CE2 1 
ATOM   7328  C  CZ  . PHE B 1 505 ? 123.978 119.133 148.998 1.00 49.53  ? 480  PHE B CZ  1 
ATOM   7329  N  N   . TYR B 1 506 ? 128.151 116.161 149.717 1.00 46.61  ? 481  TYR B N   1 
ATOM   7330  C  CA  . TYR B 1 506 ? 128.572 115.445 148.520 1.00 38.70  ? 481  TYR B CA  1 
ATOM   7331  C  C   . TYR B 1 506 ? 127.436 115.388 147.508 1.00 41.11  ? 481  TYR B C   1 
ATOM   7332  O  O   . TYR B 1 506 ? 126.253 115.403 147.864 1.00 55.86  ? 481  TYR B O   1 
ATOM   7333  C  CB  . TYR B 1 506 ? 129.077 114.019 148.840 1.00 41.85  ? 481  TYR B CB  1 
ATOM   7334  C  CG  . TYR B 1 506 ? 128.034 112.916 148.830 1.00 46.02  ? 481  TYR B CG  1 
ATOM   7335  C  CD1 . TYR B 1 506 ? 127.653 112.297 147.644 1.00 48.77  ? 481  TYR B CD1 1 
ATOM   7336  C  CD2 . TYR B 1 506 ? 127.469 112.459 150.011 1.00 44.63  ? 481  TYR B CD2 1 
ATOM   7337  C  CE1 . TYR B 1 506 ? 126.713 111.288 147.634 1.00 48.77  ? 481  TYR B CE1 1 
ATOM   7338  C  CE2 . TYR B 1 506 ? 126.531 111.446 150.009 1.00 42.57  ? 481  TYR B CE2 1 
ATOM   7339  C  CZ  . TYR B 1 506 ? 126.158 110.866 148.818 1.00 47.68  ? 481  TYR B CZ  1 
ATOM   7340  O  OH  . TYR B 1 506 ? 125.224 109.857 148.810 1.00 54.35  ? 481  TYR B OH  1 
ATOM   7341  N  N   . THR B 1 507 ? 127.814 115.304 146.235 1.00 36.15  ? 482  THR B N   1 
ATOM   7342  C  CA  . THR B 1 507 ? 126.864 115.267 145.126 1.00 32.86  ? 482  THR B CA  1 
ATOM   7343  C  C   . THR B 1 507 ? 127.279 114.155 144.168 1.00 38.91  ? 482  THR B C   1 
ATOM   7344  O  O   . THR B 1 507 ? 128.135 114.357 143.303 1.00 51.85  ? 482  THR B O   1 
ATOM   7345  C  CB  . THR B 1 507 ? 126.800 116.612 144.416 1.00 35.50  ? 482  THR B CB  1 
ATOM   7346  O  OG1 . THR B 1 507 ? 126.415 117.623 145.353 1.00 46.10  ? 482  THR B OG1 1 
ATOM   7347  C  CG2 . THR B 1 507 ? 125.782 116.565 143.297 1.00 41.79  ? 482  THR B CG2 1 
ATOM   7348  N  N   . PHE B 1 508 ? 126.670 112.985 144.331 1.00 37.50  ? 483  PHE B N   1 
ATOM   7349  C  CA  . PHE B 1 508 ? 126.934 111.860 143.446 1.00 35.50  ? 483  PHE B CA  1 
ATOM   7350  C  C   . PHE B 1 508 ? 126.456 112.174 142.035 1.00 39.98  ? 483  PHE B C   1 
ATOM   7351  O  O   . PHE B 1 508 ? 125.401 112.784 141.840 1.00 47.50  ? 483  PHE B O   1 
ATOM   7352  C  CB  . PHE B 1 508 ? 126.237 110.606 143.969 1.00 33.92  ? 483  PHE B CB  1 
ATOM   7353  C  CG  . PHE B 1 508 ? 126.979 109.335 143.687 1.00 32.12  ? 483  PHE B CG  1 
ATOM   7354  C  CD1 . PHE B 1 508 ? 128.198 109.083 144.287 1.00 39.40  ? 483  PHE B CD1 1 
ATOM   7355  C  CD2 . PHE B 1 508 ? 126.455 108.389 142.826 1.00 37.54  ? 483  PHE B CD2 1 
ATOM   7356  C  CE1 . PHE B 1 508 ? 128.881 107.915 144.033 1.00 42.29  ? 483  PHE B CE1 1 
ATOM   7357  C  CE2 . PHE B 1 508 ? 127.135 107.219 142.569 1.00 43.61  ? 483  PHE B CE2 1 
ATOM   7358  C  CZ  . PHE B 1 508 ? 128.350 106.983 143.172 1.00 42.94  ? 483  PHE B CZ  1 
ATOM   7359  N  N   . TYR B 1 509 ? 127.241 111.754 141.045 1.00 37.50  ? 484  TYR B N   1 
ATOM   7360  C  CA  . TYR B 1 509 ? 126.930 112.058 139.653 1.00 34.51  ? 484  TYR B CA  1 
ATOM   7361  C  C   . TYR B 1 509 ? 127.082 110.882 138.702 1.00 42.70  ? 484  TYR B C   1 
ATOM   7362  O  O   . TYR B 1 509 ? 126.702 111.016 137.536 1.00 48.24  ? 484  TYR B O   1 
ATOM   7363  C  CB  . TYR B 1 509 ? 127.809 113.216 139.165 1.00 34.20  ? 484  TYR B CB  1 
ATOM   7364  C  CG  . TYR B 1 509 ? 127.064 114.516 138.968 1.00 40.70  ? 484  TYR B CG  1 
ATOM   7365  C  CD1 . TYR B 1 509 ? 126.904 115.413 140.015 1.00 42.54  ? 484  TYR B CD1 1 
ATOM   7366  C  CD2 . TYR B 1 509 ? 126.493 114.833 137.745 1.00 41.23  ? 484  TYR B CD2 1 
ATOM   7367  C  CE1 . TYR B 1 509 ? 126.223 116.601 139.841 1.00 42.46  ? 484  TYR B CE1 1 
ATOM   7368  C  CE2 . TYR B 1 509 ? 125.814 116.021 137.562 1.00 43.03  ? 484  TYR B CE2 1 
ATOM   7369  C  CZ  . TYR B 1 509 ? 125.676 116.897 138.614 1.00 46.19  ? 484  TYR B CZ  1 
ATOM   7370  O  OH  . TYR B 1 509 ? 124.993 118.077 138.437 1.00 48.34  ? 484  TYR B OH  1 
ATOM   7371  N  N   . HIS B 1 510 ? 127.617 109.749 139.141 1.00 55.45  ? 485  HIS B N   1 
ATOM   7372  C  CA  . HIS B 1 510 ? 127.790 108.575 138.299 1.00 55.18  ? 485  HIS B CA  1 
ATOM   7373  C  C   . HIS B 1 510 ? 126.692 107.557 138.578 1.00 55.23  ? 485  HIS B C   1 
ATOM   7374  O  O   . HIS B 1 510 ? 126.131 107.506 139.674 1.00 59.50  ? 485  HIS B O   1 
ATOM   7375  C  CB  . HIS B 1 510 ? 129.161 107.941 138.534 1.00 57.12  ? 485  HIS B CB  1 
ATOM   7376  C  CG  . HIS B 1 510 ? 129.507 106.865 137.553 1.00 57.15  ? 485  HIS B CG  1 
ATOM   7377  N  ND1 . HIS B 1 510 ? 129.328 107.009 136.195 1.00 59.63  ? 485  HIS B ND1 1 
ATOM   7378  C  CD2 . HIS B 1 510 ? 130.024 105.627 137.735 1.00 55.15  ? 485  HIS B CD2 1 
ATOM   7379  C  CE1 . HIS B 1 510 ? 129.719 105.907 135.582 1.00 60.36  ? 485  HIS B CE1 1 
ATOM   7380  N  NE2 . HIS B 1 510 ? 130.145 105.052 136.494 1.00 59.42  ? 485  HIS B NE2 1 
ATOM   7381  N  N   . HIS B 1 511 ? 126.388 106.744 137.569 1.00 67.87  ? 486  HIS B N   1 
ATOM   7382  C  CA  . HIS B 1 511 ? 125.355 105.725 137.683 1.00 67.62  ? 486  HIS B CA  1 
ATOM   7383  C  C   . HIS B 1 511 ? 125.766 104.489 136.900 1.00 74.75  ? 486  HIS B C   1 
ATOM   7384  O  O   . HIS B 1 511 ? 126.278 104.595 135.782 1.00 76.05  ? 486  HIS B O   1 
ATOM   7385  C  CB  . HIS B 1 511 ? 124.001 106.234 137.173 1.00 68.57  ? 486  HIS B CB  1 
ATOM   7386  C  CG  . HIS B 1 511 ? 124.009 106.639 135.732 1.00 74.02  ? 486  HIS B CG  1 
ATOM   7387  N  ND1 . HIS B 1 511 ? 124.849 107.613 135.236 1.00 73.51  ? 486  HIS B ND1 1 
ATOM   7388  C  CD2 . HIS B 1 511 ? 123.281 106.199 134.679 1.00 72.26  ? 486  HIS B CD2 1 
ATOM   7389  C  CE1 . HIS B 1 511 ? 124.637 107.757 133.940 1.00 72.85  ? 486  HIS B CE1 1 
ATOM   7390  N  NE2 . HIS B 1 511 ? 123.690 106.911 133.577 1.00 74.23  ? 486  HIS B NE2 1 
ATOM   7391  N  N   . CYS B 1 512 ? 125.543 103.321 137.494 1.00 98.74  ? 487  CYS B N   1 
ATOM   7392  C  CA  . CYS B 1 512 ? 125.799 102.070 136.797 1.00 98.02  ? 487  CYS B CA  1 
ATOM   7393  C  C   . CYS B 1 512 ? 124.782 101.872 135.680 1.00 98.59  ? 487  CYS B C   1 
ATOM   7394  O  O   . CYS B 1 512 ? 123.592 102.156 135.844 1.00 99.42  ? 487  CYS B O   1 
ATOM   7395  C  CB  . CYS B 1 512 ? 125.751 100.897 137.775 1.00 96.49  ? 487  CYS B CB  1 
ATOM   7396  S  SG  . CYS B 1 512 ? 124.524 101.072 139.090 1.00 100.30 ? 487  CYS B SG  1 
ATOM   7397  N  N   . GLN B 1 513 ? 125.256 101.382 134.537 1.00 107.88 ? 488  GLN B N   1 
ATOM   7398  C  CA  . GLN B 1 513 ? 124.409 101.234 133.358 1.00 109.83 ? 488  GLN B CA  1 
ATOM   7399  C  C   . GLN B 1 513 ? 123.451 100.066 133.559 1.00 110.89 ? 488  GLN B C   1 
ATOM   7400  O  O   . GLN B 1 513 ? 123.850 98.901  133.460 1.00 112.19 ? 488  GLN B O   1 
ATOM   7401  C  CB  . GLN B 1 513 ? 125.271 101.025 132.117 1.00 110.08 ? 488  GLN B CB  1 
ATOM   7402  C  CG  . GLN B 1 513 ? 124.505 101.111 130.808 1.00 110.21 ? 488  GLN B CG  1 
ATOM   7403  C  CD  . GLN B 1 513 ? 123.573 102.307 130.755 1.00 111.05 ? 488  GLN B CD  1 
ATOM   7404  O  OE1 . GLN B 1 513 ? 122.372 102.164 130.532 1.00 110.41 ? 488  GLN B OE1 1 
ATOM   7405  N  NE2 . GLN B 1 513 ? 124.128 103.498 130.952 1.00 110.28 ? 488  GLN B NE2 1 
ATOM   7406  N  N   . ALA B 1 514 ? 122.186 100.372 133.829 1.00 104.37 ? 489  ALA B N   1 
ATOM   7407  C  CA  . ALA B 1 514 ? 121.182 99.351  134.081 1.00 103.59 ? 489  ALA B CA  1 
ATOM   7408  C  C   . ALA B 1 514 ? 120.575 98.851  132.775 1.00 104.06 ? 489  ALA B C   1 
ATOM   7409  O  O   . ALA B 1 514 ? 120.537 99.557  131.765 1.00 103.05 ? 489  ALA B O   1 
ATOM   7410  C  CB  . ALA B 1 514 ? 120.083 99.888  134.999 1.00 101.02 ? 489  ALA B CB  1 
ATOM   7411  N  N   . GLU B 1 515 ? 120.104 97.602  132.809 1.00 95.91  ? 490  GLU B N   1 
ATOM   7412  C  CA  . GLU B 1 515 ? 119.515 96.999  131.618 1.00 93.84  ? 490  GLU B CA  1 
ATOM   7413  C  C   . GLU B 1 515 ? 118.226 97.704  131.212 1.00 97.34  ? 490  GLU B C   1 
ATOM   7414  O  O   . GLU B 1 515 ? 117.999 97.957  130.023 1.00 98.36  ? 490  GLU B O   1 
ATOM   7415  C  CB  . GLU B 1 515 ? 119.259 95.511  131.858 1.00 92.01  ? 490  GLU B CB  1 
ATOM   7416  N  N   . GLY B 1 516 ? 117.372 98.027  132.179 1.00 92.21  ? 491  GLY B N   1 
ATOM   7417  C  CA  . GLY B 1 516 ? 116.088 98.638  131.913 1.00 90.61  ? 491  GLY B CA  1 
ATOM   7418  C  C   . GLY B 1 516 ? 115.987 100.122 132.191 1.00 89.13  ? 491  GLY B C   1 
ATOM   7419  O  O   . GLY B 1 516 ? 114.870 100.655 132.201 1.00 88.90  ? 491  GLY B O   1 
ATOM   7420  N  N   . ARG B 1 517 ? 117.107 100.813 132.416 1.00 77.98  ? 492  ARG B N   1 
ATOM   7421  C  CA  . ARG B 1 517 ? 116.952 102.229 132.706 1.00 79.18  ? 492  ARG B CA  1 
ATOM   7422  C  C   . ARG B 1 517 ? 117.139 103.065 131.445 1.00 79.12  ? 492  ARG B C   1 
ATOM   7423  O  O   . ARG B 1 517 ? 117.909 102.694 130.554 1.00 79.84  ? 492  ARG B O   1 
ATOM   7424  C  CB  . ARG B 1 517 ? 117.958 102.680 133.769 1.00 78.39  ? 492  ARG B CB  1 
ATOM   7425  C  CG  . ARG B 1 517 ? 117.484 102.464 135.198 1.00 77.14  ? 492  ARG B CG  1 
ATOM   7426  C  CD  . ARG B 1 517 ? 117.360 103.781 135.942 1.00 72.40  ? 492  ARG B CD  1 
ATOM   7427  N  NE  . ARG B 1 517 ? 118.466 104.682 135.644 1.00 75.41  ? 492  ARG B NE  1 
ATOM   7428  C  CZ  . ARG B 1 517 ? 119.541 104.825 136.406 1.00 76.46  ? 492  ARG B CZ  1 
ATOM   7429  N  NH1 . ARG B 1 517 ? 119.690 104.137 137.526 1.00 77.97  ? 492  ARG B NH1 1 
ATOM   7430  N  NH2 . ARG B 1 517 ? 120.490 105.680 136.036 1.00 71.28  ? 492  ARG B NH2 1 
ATOM   7431  N  N   . PRO B 1 518 ? 116.434 104.192 131.345 1.00 80.65  ? 493  PRO B N   1 
ATOM   7432  C  CA  . PRO B 1 518 ? 116.588 105.056 130.170 1.00 79.50  ? 493  PRO B CA  1 
ATOM   7433  C  C   . PRO B 1 518 ? 118.003 105.602 130.053 1.00 80.25  ? 493  PRO B C   1 
ATOM   7434  O  O   . PRO B 1 518 ? 118.685 105.850 131.050 1.00 79.92  ? 493  PRO B O   1 
ATOM   7435  C  CB  . PRO B 1 518 ? 115.576 106.179 130.420 1.00 78.19  ? 493  PRO B CB  1 
ATOM   7436  C  CG  . PRO B 1 518 ? 114.568 105.578 131.342 1.00 79.48  ? 493  PRO B CG  1 
ATOM   7437  C  CD  . PRO B 1 518 ? 115.342 104.644 132.223 1.00 79.21  ? 493  PRO B CD  1 
ATOM   7438  N  N   . GLU B 1 519 ? 118.443 105.783 128.805 1.00 88.47  ? 494  GLU B N   1 
ATOM   7439  C  CA  . GLU B 1 519 ? 119.779 106.315 128.557 1.00 89.16  ? 494  GLU B CA  1 
ATOM   7440  C  C   . GLU B 1 519 ? 119.899 107.760 129.026 1.00 88.72  ? 494  GLU B C   1 
ATOM   7441  O  O   . GLU B 1 519 ? 120.933 108.155 129.577 1.00 90.28  ? 494  GLU B O   1 
ATOM   7442  C  CB  . GLU B 1 519 ? 120.122 106.202 127.072 1.00 89.00  ? 494  GLU B CB  1 
ATOM   7443  N  N   . TRP B 1 520 ? 118.856 108.566 128.812 1.00 73.53  ? 495  TRP B N   1 
ATOM   7444  C  CA  . TRP B 1 520 ? 118.891 109.959 129.239 1.00 72.78  ? 495  TRP B CA  1 
ATOM   7445  C  C   . TRP B 1 520 ? 118.917 110.099 130.755 1.00 72.07  ? 495  TRP B C   1 
ATOM   7446  O  O   . TRP B 1 520 ? 119.292 111.162 131.260 1.00 69.43  ? 495  TRP B O   1 
ATOM   7447  C  CB  . TRP B 1 520 ? 117.686 110.717 128.676 1.00 73.06  ? 495  TRP B CB  1 
ATOM   7448  C  CG  . TRP B 1 520 ? 116.367 110.234 129.204 1.00 73.63  ? 495  TRP B CG  1 
ATOM   7449  C  CD1 . TRP B 1 520 ? 115.553 109.295 128.641 1.00 71.03  ? 495  TRP B CD1 1 
ATOM   7450  C  CD2 . TRP B 1 520 ? 115.704 110.676 130.396 1.00 73.96  ? 495  TRP B CD2 1 
ATOM   7451  N  NE1 . TRP B 1 520 ? 114.428 109.120 129.410 1.00 69.39  ? 495  TRP B NE1 1 
ATOM   7452  C  CE2 . TRP B 1 520 ? 114.497 109.956 130.493 1.00 69.67  ? 495  TRP B CE2 1 
ATOM   7453  C  CE3 . TRP B 1 520 ? 116.015 111.608 131.390 1.00 73.19  ? 495  TRP B CE3 1 
ATOM   7454  C  CZ2 . TRP B 1 520 ? 113.602 110.139 131.544 1.00 68.31  ? 495  TRP B CZ2 1 
ATOM   7455  C  CZ3 . TRP B 1 520 ? 115.126 111.787 132.433 1.00 70.80  ? 495  TRP B CZ3 1 
ATOM   7456  C  CH2 . TRP B 1 520 ? 113.934 111.057 132.502 1.00 69.82  ? 495  TRP B CH2 1 
ATOM   7457  N  N   . ALA B 1 521 ? 118.525 109.057 131.483 1.00 74.66  ? 496  ALA B N   1 
ATOM   7458  C  CA  . ALA B 1 521 ? 118.467 109.132 132.935 1.00 73.11  ? 496  ALA B CA  1 
ATOM   7459  C  C   . ALA B 1 521 ? 119.865 109.209 133.532 1.00 72.81  ? 496  ALA B C   1 
ATOM   7460  O  O   . ALA B 1 521 ? 120.805 108.575 133.046 1.00 74.94  ? 496  ALA B O   1 
ATOM   7461  C  CB  . ALA B 1 521 ? 117.725 107.922 133.499 1.00 73.38  ? 496  ALA B CB  1 
ATOM   7462  N  N   . ASP B 1 522 ? 119.995 109.995 134.592 1.00 60.11  ? 497  ASP B N   1 
ATOM   7463  C  CA  . ASP B 1 522 ? 121.233 110.154 135.333 1.00 58.58  ? 497  ASP B CA  1 
ATOM   7464  C  C   . ASP B 1 522 ? 121.095 109.456 136.684 1.00 63.32  ? 497  ASP B C   1 
ATOM   7465  O  O   . ASP B 1 522 ? 120.111 108.751 136.939 1.00 69.85  ? 497  ASP B O   1 
ATOM   7466  C  CB  . ASP B 1 522 ? 121.569 111.639 135.464 1.00 55.60  ? 497  ASP B CB  1 
ATOM   7467  C  CG  . ASP B 1 522 ? 121.652 112.332 134.116 1.00 66.42  ? 497  ASP B CG  1 
ATOM   7468  O  OD1 . ASP B 1 522 ? 121.608 111.629 133.086 1.00 69.78  ? 497  ASP B OD1 1 
ATOM   7469  O  OD2 . ASP B 1 522 ? 121.749 113.576 134.079 1.00 67.03  ? 497  ASP B OD2 1 
ATOM   7470  N  N   . ALA B 1 523 ? 122.096 109.636 137.548 1.00 45.27  ? 498  ALA B N   1 
ATOM   7471  C  CA  . ALA B 1 523 ? 122.118 108.959 138.840 1.00 43.49  ? 498  ALA B CA  1 
ATOM   7472  C  C   . ALA B 1 523 ? 120.834 109.223 139.612 1.00 41.84  ? 498  ALA B C   1 
ATOM   7473  O  O   . ALA B 1 523 ? 120.579 110.353 140.039 1.00 51.76  ? 498  ALA B O   1 
ATOM   7474  C  CB  . ALA B 1 523 ? 123.331 109.404 139.659 1.00 41.16  ? 498  ALA B CB  1 
ATOM   7475  N  N   . ALA B 1 524 ? 120.027 108.183 139.802 1.00 30.88  ? 499  ALA B N   1 
ATOM   7476  C  CA  . ALA B 1 524 ? 118.702 108.328 140.378 1.00 29.22  ? 499  ALA B CA  1 
ATOM   7477  C  C   . ALA B 1 524 ? 118.739 108.092 141.885 1.00 36.38  ? 499  ALA B C   1 
ATOM   7478  O  O   . ALA B 1 524 ? 119.799 107.924 142.492 1.00 51.34  ? 499  ALA B O   1 
ATOM   7479  C  CB  . ALA B 1 524 ? 117.723 107.375 139.696 1.00 29.64  ? 499  ALA B CB  1 
ATOM   7480  N  N   . HIS B 1 525 ? 117.559 108.084 142.498 1.00 30.54  ? 500  HIS B N   1 
ATOM   7481  C  CA  . HIS B 1 525 ? 117.460 107.904 143.939 1.00 29.28  ? 500  HIS B CA  1 
ATOM   7482  C  C   . HIS B 1 525 ? 117.878 106.491 144.321 1.00 35.98  ? 500  HIS B C   1 
ATOM   7483  O  O   . HIS B 1 525 ? 117.369 105.510 143.771 1.00 44.40  ? 500  HIS B O   1 
ATOM   7484  C  CB  . HIS B 1 525 ? 116.033 108.184 144.405 1.00 27.70  ? 500  HIS B CB  1 
ATOM   7485  C  CG  . HIS B 1 525 ? 115.855 108.128 145.890 1.00 30.68  ? 500  HIS B CG  1 
ATOM   7486  N  ND1 . HIS B 1 525 ? 114.614 108.076 146.487 1.00 34.56  ? 500  HIS B ND1 1 
ATOM   7487  C  CD2 . HIS B 1 525 ? 116.758 108.125 146.898 1.00 32.59  ? 500  HIS B CD2 1 
ATOM   7488  C  CE1 . HIS B 1 525 ? 114.761 108.038 147.799 1.00 33.08  ? 500  HIS B CE1 1 
ATOM   7489  N  NE2 . HIS B 1 525 ? 116.052 108.066 148.075 1.00 34.10  ? 500  HIS B NE2 1 
ATOM   7490  N  N   . GLY B 1 526 ? 118.804 106.388 145.271 1.00 31.49  ? 501  GLY B N   1 
ATOM   7491  C  CA  . GLY B 1 526 ? 119.285 105.107 145.735 1.00 31.19  ? 501  GLY B CA  1 
ATOM   7492  C  C   . GLY B 1 526 ? 120.349 104.461 144.877 1.00 31.55  ? 501  GLY B C   1 
ATOM   7493  O  O   . GLY B 1 526 ? 120.749 103.328 145.171 1.00 39.87  ? 501  GLY B O   1 
ATOM   7494  N  N   . ASP B 1 527 ? 120.830 105.137 143.837 1.00 29.72  ? 502  ASP B N   1 
ATOM   7495  C  CA  . ASP B 1 527 ? 121.875 104.576 142.992 1.00 29.59  ? 502  ASP B CA  1 
ATOM   7496  C  C   . ASP B 1 527 ? 123.265 104.753 143.585 1.00 34.44  ? 502  ASP B C   1 
ATOM   7497  O  O   . ASP B 1 527 ? 124.238 104.266 143.000 1.00 45.84  ? 502  ASP B O   1 
ATOM   7498  C  CB  . ASP B 1 527 ? 121.820 105.204 141.598 1.00 34.35  ? 502  ASP B CB  1 
ATOM   7499  C  CG  . ASP B 1 527 ? 120.972 104.400 140.632 1.00 44.06  ? 502  ASP B CG  1 
ATOM   7500  O  OD1 . ASP B 1 527 ? 120.182 103.553 141.098 1.00 47.30  ? 502  ASP B OD1 1 
ATOM   7501  O  OD2 . ASP B 1 527 ? 121.092 104.616 139.409 1.00 47.09  ? 502  ASP B OD2 1 
ATOM   7502  N  N   . GLU B 1 528 ? 123.376 105.438 144.720 1.00 32.40  ? 503  GLU B N   1 
ATOM   7503  C  CA  . GLU B 1 528 ? 124.624 105.563 145.456 1.00 31.29  ? 503  GLU B CA  1 
ATOM   7504  C  C   . GLU B 1 528 ? 124.836 104.439 146.460 1.00 28.13  ? 503  GLU B C   1 
ATOM   7505  O  O   . GLU B 1 528 ? 125.948 104.292 146.979 1.00 38.69  ? 503  GLU B O   1 
ATOM   7506  C  CB  . GLU B 1 528 ? 124.663 106.919 146.173 1.00 31.58  ? 503  GLU B CB  1 
ATOM   7507  C  CG  . GLU B 1 528 ? 124.400 106.843 147.666 1.00 34.69  ? 503  GLU B CG  1 
ATOM   7508  C  CD  . GLU B 1 528 ? 122.919 106.885 147.991 1.00 50.14  ? 503  GLU B CD  1 
ATOM   7509  O  OE1 . GLU B 1 528 ? 122.106 106.993 147.050 1.00 49.99  ? 503  GLU B OE1 1 
ATOM   7510  O  OE2 . GLU B 1 528 ? 122.565 106.788 149.184 1.00 48.46  ? 503  GLU B OE2 1 
ATOM   7511  N  N   . LEU B 1 529 ? 123.814 103.628 146.719 1.00 31.16  ? 504  LEU B N   1 
ATOM   7512  C  CA  . LEU B 1 529 ? 123.885 102.538 147.685 1.00 31.28  ? 504  LEU B CA  1 
ATOM   7513  C  C   . LEU B 1 529 ? 124.738 101.370 147.194 1.00 34.97  ? 504  LEU B C   1 
ATOM   7514  O  O   . LEU B 1 529 ? 125.464 100.777 148.002 1.00 44.20  ? 504  LEU B O   1 
ATOM   7515  C  CB  . LEU B 1 529 ? 122.477 102.053 148.041 1.00 29.05  ? 504  LEU B CB  1 
ATOM   7516  C  CG  . LEU B 1 529 ? 121.919 102.574 149.365 1.00 33.58  ? 504  LEU B CG  1 
ATOM   7517  C  CD1 . LEU B 1 529 ? 120.619 101.875 149.719 1.00 36.84  ? 504  LEU B CD1 1 
ATOM   7518  C  CD2 . LEU B 1 529 ? 122.940 102.404 150.474 1.00 36.88  ? 504  LEU B CD2 1 
ATOM   7519  N  N   . PRO B 1 530 ? 124.678 100.981 145.911 1.00 38.24  ? 505  PRO B N   1 
ATOM   7520  C  CA  . PRO B 1 530 ? 125.592 99.921  145.451 1.00 36.34  ? 505  PRO B CA  1 
ATOM   7521  C  C   . PRO B 1 530 ? 127.057 100.246 145.675 1.00 41.98  ? 505  PRO B C   1 
ATOM   7522  O  O   . PRO B 1 530 ? 127.842 99.352  146.014 1.00 50.23  ? 505  PRO B O   1 
ATOM   7523  C  CB  . PRO B 1 530 ? 125.263 99.804  143.958 1.00 36.27  ? 505  PRO B CB  1 
ATOM   7524  C  CG  . PRO B 1 530 ? 123.858 100.216 143.859 1.00 35.56  ? 505  PRO B CG  1 
ATOM   7525  C  CD  . PRO B 1 530 ? 123.669 101.296 144.881 1.00 42.30  ? 505  PRO B CD  1 
ATOM   7526  N  N   . TYR B 1 531 ? 127.450 101.507 145.499 1.00 39.97  ? 506  TYR B N   1 
ATOM   7527  C  CA  . TYR B 1 531 ? 128.857 101.871 145.618 1.00 36.40  ? 506  TYR B CA  1 
ATOM   7528  C  C   . TYR B 1 531 ? 129.316 101.901 147.071 1.00 39.58  ? 506  TYR B C   1 
ATOM   7529  O  O   . TYR B 1 531 ? 130.444 101.500 147.374 1.00 47.32  ? 506  TYR B O   1 
ATOM   7530  C  CB  . TYR B 1 531 ? 129.111 103.222 144.947 1.00 33.40  ? 506  TYR B CB  1 
ATOM   7531  C  CG  . TYR B 1 531 ? 128.944 103.205 143.443 1.00 31.55  ? 506  TYR B CG  1 
ATOM   7532  C  CD1 . TYR B 1 531 ? 127.707 102.965 142.861 1.00 38.41  ? 506  TYR B CD1 1 
ATOM   7533  C  CD2 . TYR B 1 531 ? 130.026 103.421 142.605 1.00 39.30  ? 506  TYR B CD2 1 
ATOM   7534  C  CE1 . TYR B 1 531 ? 127.554 102.945 141.492 1.00 40.57  ? 506  TYR B CE1 1 
ATOM   7535  C  CE2 . TYR B 1 531 ? 129.882 103.403 141.234 1.00 44.45  ? 506  TYR B CE2 1 
ATOM   7536  C  CZ  . TYR B 1 531 ? 128.643 103.164 140.684 1.00 45.82  ? 506  TYR B CZ  1 
ATOM   7537  O  OH  . TYR B 1 531 ? 128.493 103.144 139.318 1.00 51.87  ? 506  TYR B OH  1 
ATOM   7538  N  N   . VAL B 1 532 ? 128.460 102.373 147.980 1.00 29.54  ? 507  VAL B N   1 
ATOM   7539  C  CA  . VAL B 1 532 ? 128.844 102.469 149.386 1.00 22.82  ? 507  VAL B CA  1 
ATOM   7540  C  C   . VAL B 1 532 ? 129.076 101.084 149.976 1.00 40.89  ? 507  VAL B C   1 
ATOM   7541  O  O   . VAL B 1 532 ? 129.980 100.885 150.796 1.00 45.74  ? 507  VAL B O   1 
ATOM   7542  C  CB  . VAL B 1 532 ? 127.779 103.251 150.177 1.00 27.60  ? 507  VAL B CB  1 
ATOM   7543  C  CG1 . VAL B 1 532 ? 128.112 103.261 151.656 1.00 33.48  ? 507  VAL B CG1 1 
ATOM   7544  C  CG2 . VAL B 1 532 ? 127.667 104.668 149.650 1.00 37.75  ? 507  VAL B CG2 1 
ATOM   7545  N  N   . PHE B 1 533 ? 128.277 100.104 149.561 1.00 47.62  ? 508  PHE B N   1 
ATOM   7546  C  CA  . PHE B 1 533 ? 128.353 98.755  150.105 1.00 41.70  ? 508  PHE B CA  1 
ATOM   7547  C  C   . PHE B 1 533 ? 129.281 97.844  149.311 1.00 41.84  ? 508  PHE B C   1 
ATOM   7548  O  O   . PHE B 1 533 ? 129.361 96.649  149.613 1.00 50.76  ? 508  PHE B O   1 
ATOM   7549  C  CB  . PHE B 1 533 ? 126.954 98.142  150.182 1.00 40.39  ? 508  PHE B CB  1 
ATOM   7550  C  CG  . PHE B 1 533 ? 126.235 98.445  151.463 1.00 40.39  ? 508  PHE B CG  1 
ATOM   7551  C  CD1 . PHE B 1 533 ? 126.602 97.821  152.642 1.00 49.86  ? 508  PHE B CD1 1 
ATOM   7552  C  CD2 . PHE B 1 533 ? 125.200 99.359  151.491 1.00 35.12  ? 508  PHE B CD2 1 
ATOM   7553  C  CE1 . PHE B 1 533 ? 125.947 98.099  153.821 1.00 44.64  ? 508  PHE B CE1 1 
ATOM   7554  C  CE2 . PHE B 1 533 ? 124.541 99.641  152.668 1.00 45.80  ? 508  PHE B CE2 1 
ATOM   7555  C  CZ  . PHE B 1 533 ? 124.915 99.010  153.834 1.00 50.72  ? 508  PHE B CZ  1 
ATOM   7556  N  N   . GLY B 1 534 ? 129.979 98.375  148.311 1.00 32.92  ? 509  GLY B N   1 
ATOM   7557  C  CA  . GLY B 1 534 ? 130.960 97.595  147.580 1.00 36.54  ? 509  GLY B CA  1 
ATOM   7558  C  C   . GLY B 1 534 ? 130.401 96.455  146.763 1.00 43.71  ? 509  GLY B C   1 
ATOM   7559  O  O   . GLY B 1 534 ? 131.038 95.402  146.666 1.00 54.28  ? 509  GLY B O   1 
ATOM   7560  N  N   . VAL B 1 535 ? 129.216 96.633  146.178 1.00 46.31  ? 510  VAL B N   1 
ATOM   7561  C  CA  . VAL B 1 535 ? 128.689 95.626  145.255 1.00 42.78  ? 510  VAL B CA  1 
ATOM   7562  C  C   . VAL B 1 535 ? 129.588 95.435  144.040 1.00 52.37  ? 510  VAL B C   1 
ATOM   7563  O  O   . VAL B 1 535 ? 129.830 94.280  143.659 1.00 56.12  ? 510  VAL B O   1 
ATOM   7564  C  CB  . VAL B 1 535 ? 127.235 95.955  144.888 1.00 42.14  ? 510  VAL B CB  1 
ATOM   7565  C  CG1 . VAL B 1 535 ? 126.846 95.291  143.581 1.00 49.04  ? 510  VAL B CG1 1 
ATOM   7566  C  CG2 . VAL B 1 535 ? 126.302 95.517  146.004 1.00 45.45  ? 510  VAL B CG2 1 
ATOM   7567  N  N   . PRO B 1 536 ? 130.109 96.484  143.382 1.00 55.04  ? 511  PRO B N   1 
ATOM   7568  C  CA  . PRO B 1 536 ? 130.908 96.244  142.165 1.00 55.75  ? 511  PRO B CA  1 
ATOM   7569  C  C   . PRO B 1 536 ? 132.110 95.333  142.361 1.00 54.22  ? 511  PRO B C   1 
ATOM   7570  O  O   . PRO B 1 536 ? 132.419 94.539  141.464 1.00 58.95  ? 511  PRO B O   1 
ATOM   7571  C  CB  . PRO B 1 536 ? 131.333 97.658  141.752 1.00 55.68  ? 511  PRO B CB  1 
ATOM   7572  C  CG  . PRO B 1 536 ? 130.249 98.519  142.250 1.00 55.42  ? 511  PRO B CG  1 
ATOM   7573  C  CD  . PRO B 1 536 ? 129.844 97.924  143.565 1.00 55.54  ? 511  PRO B CD  1 
ATOM   7574  N  N   . MET B 1 537 ? 132.802 95.413  143.498 1.00 49.02  ? 512  MET B N   1 
ATOM   7575  C  CA  . MET B 1 537 ? 133.978 94.572  143.686 1.00 52.52  ? 512  MET B CA  1 
ATOM   7576  C  C   . MET B 1 537 ? 133.631 93.112  143.939 1.00 55.89  ? 512  MET B C   1 
ATOM   7577  O  O   . MET B 1 537 ? 134.536 92.271  143.953 1.00 61.05  ? 512  MET B O   1 
ATOM   7578  C  CB  . MET B 1 537 ? 134.844 95.095  144.834 1.00 50.91  ? 512  MET B CB  1 
ATOM   7579  C  CG  . MET B 1 537 ? 135.335 96.518  144.645 1.00 54.33  ? 512  MET B CG  1 
ATOM   7580  S  SD  . MET B 1 537 ? 136.239 97.123  146.080 1.00 63.78  ? 512  MET B SD  1 
ATOM   7581  C  CE  . MET B 1 537 ? 135.392 96.254  147.392 1.00 54.30  ? 512  MET B CE  1 
ATOM   7582  N  N   . VAL B 1 538 ? 132.356 92.791  144.141 1.00 54.99  ? 513  VAL B N   1 
ATOM   7583  C  CA  . VAL B 1 538 ? 131.920 91.407  144.259 1.00 58.31  ? 513  VAL B CA  1 
ATOM   7584  C  C   . VAL B 1 538 ? 131.248 90.904  142.987 1.00 60.39  ? 513  VAL B C   1 
ATOM   7585  O  O   . VAL B 1 538 ? 131.463 89.740  142.612 1.00 67.06  ? 513  VAL B O   1 
ATOM   7586  C  CB  . VAL B 1 538 ? 130.985 91.223  145.473 1.00 57.32  ? 513  VAL B CB  1 
ATOM   7587  C  CG1 . VAL B 1 538 ? 130.227 89.907  145.392 1.00 55.41  ? 513  VAL B CG1 1 
ATOM   7588  C  CG2 . VAL B 1 538 ? 131.782 91.295  146.762 1.00 58.27  ? 513  VAL B CG2 1 
ATOM   7589  N  N   . GLY B 1 539 ? 130.492 91.740  142.292 1.00 60.10  ? 514  GLY B N   1 
ATOM   7590  C  CA  . GLY B 1 539 ? 129.814 91.356  141.072 1.00 62.09  ? 514  GLY B CA  1 
ATOM   7591  C  C   . GLY B 1 539 ? 128.324 91.649  141.134 1.00 63.23  ? 514  GLY B C   1 
ATOM   7592  O  O   . GLY B 1 539 ? 127.766 92.014  142.169 1.00 64.51  ? 514  GLY B O   1 
ATOM   7593  N  N   . ALA B 1 540 ? 127.686 91.486  139.979 1.00 74.88  ? 515  ALA B N   1 
ATOM   7594  C  CA  . ALA B 1 540 ? 126.256 91.733  139.875 1.00 73.85  ? 515  ALA B CA  1 
ATOM   7595  C  C   . ALA B 1 540 ? 125.475 90.729  140.712 1.00 73.50  ? 515  ALA B C   1 
ATOM   7596  O  O   . ALA B 1 540 ? 125.819 89.545  140.774 1.00 77.79  ? 515  ALA B O   1 
ATOM   7597  C  CB  . ALA B 1 540 ? 125.809 91.662  138.416 1.00 72.93  ? 515  ALA B CB  1 
ATOM   7598  N  N   . THR B 1 541 ? 124.419 91.208  141.357 1.00 74.20  ? 516  THR B N   1 
ATOM   7599  C  CA  . THR B 1 541 ? 123.545 90.387  142.182 1.00 76.80  ? 516  THR B CA  1 
ATOM   7600  C  C   . THR B 1 541 ? 122.126 90.441  141.624 1.00 77.66  ? 516  THR B C   1 
ATOM   7601  O  O   . THR B 1 541 ? 121.864 91.052  140.585 1.00 76.25  ? 516  THR B O   1 
ATOM   7602  C  CB  . THR B 1 541 ? 123.575 90.850  143.642 1.00 75.36  ? 516  THR B CB  1 
ATOM   7603  O  OG1 . THR B 1 541 ? 122.917 92.118  143.758 1.00 74.36  ? 516  THR B OG1 1 
ATOM   7604  C  CG2 . THR B 1 541 ? 125.008 90.984  144.134 1.00 73.60  ? 516  THR B CG2 1 
ATOM   7605  N  N   . ASP B 1 542 ? 121.203 89.784  142.329 1.00 78.84  ? 517  ASP B N   1 
ATOM   7606  C  CA  . ASP B 1 542 ? 119.803 89.826  141.923 1.00 76.91  ? 517  ASP B CA  1 
ATOM   7607  C  C   . ASP B 1 542 ? 119.234 91.232  142.060 1.00 76.64  ? 517  ASP B C   1 
ATOM   7608  O  O   . ASP B 1 542 ? 118.402 91.653  141.248 1.00 78.74  ? 517  ASP B O   1 
ATOM   7609  C  CB  . ASP B 1 542 ? 118.986 88.831  142.748 1.00 76.80  ? 517  ASP B CB  1 
ATOM   7610  C  CG  . ASP B 1 542 ? 119.413 88.792  144.202 1.00 78.85  ? 517  ASP B CG  1 
ATOM   7611  O  OD1 . ASP B 1 542 ? 120.633 88.808  144.465 1.00 79.61  ? 517  ASP B OD1 1 
ATOM   7612  O  OD2 . ASP B 1 542 ? 118.528 88.743  145.083 1.00 80.75  ? 517  ASP B OD2 1 
ATOM   7613  N  N   . LEU B 1 543 ? 119.667 91.969  143.083 1.00 70.43  ? 518  LEU B N   1 
ATOM   7614  C  CA  . LEU B 1 543 ? 119.200 93.337  143.275 1.00 69.61  ? 518  LEU B CA  1 
ATOM   7615  C  C   . LEU B 1 543 ? 119.861 94.313  142.311 1.00 71.59  ? 518  LEU B C   1 
ATOM   7616  O  O   . LEU B 1 543 ? 119.248 95.319  141.941 1.00 69.81  ? 518  LEU B O   1 
ATOM   7617  C  CB  . LEU B 1 543 ? 119.455 93.780  144.715 1.00 70.91  ? 518  LEU B CB  1 
ATOM   7618  C  CG  . LEU B 1 543 ? 118.336 93.493  145.713 1.00 69.23  ? 518  LEU B CG  1 
ATOM   7619  C  CD1 . LEU B 1 543 ? 118.875 93.536  147.130 1.00 67.56  ? 518  LEU B CD1 1 
ATOM   7620  C  CD2 . LEU B 1 543 ? 117.197 94.481  145.537 1.00 68.71  ? 518  LEU B CD2 1 
ATOM   7621  N  N   . PHE B 1 544 ? 121.102 94.045  141.906 1.00 73.09  ? 519  PHE B N   1 
ATOM   7622  C  CA  . PHE B 1 544 ? 121.841 94.910  140.988 1.00 70.36  ? 519  PHE B CA  1 
ATOM   7623  C  C   . PHE B 1 544 ? 122.324 94.064  139.818 1.00 74.53  ? 519  PHE B C   1 
ATOM   7624  O  O   . PHE B 1 544 ? 123.414 93.476  139.868 1.00 77.48  ? 519  PHE B O   1 
ATOM   7625  C  CB  . PHE B 1 544 ? 123.001 95.602  141.701 1.00 67.91  ? 519  PHE B CB  1 
ATOM   7626  C  CG  . PHE B 1 544 ? 122.622 96.195  143.027 1.00 69.45  ? 519  PHE B CG  1 
ATOM   7627  C  CD1 . PHE B 1 544 ? 121.729 97.248  143.098 1.00 71.50  ? 519  PHE B CD1 1 
ATOM   7628  C  CD2 . PHE B 1 544 ? 123.160 95.700  144.202 1.00 71.17  ? 519  PHE B CD2 1 
ATOM   7629  C  CE1 . PHE B 1 544 ? 121.376 97.793  144.316 1.00 69.60  ? 519  PHE B CE1 1 
ATOM   7630  C  CE2 . PHE B 1 544 ? 122.812 96.243  145.423 1.00 69.30  ? 519  PHE B CE2 1 
ATOM   7631  C  CZ  . PHE B 1 544 ? 121.920 97.291  145.479 1.00 66.63  ? 519  PHE B CZ  1 
ATOM   7632  N  N   . PRO B 1 545 ? 121.537 93.984  138.736 1.00 90.28  ? 520  PRO B N   1 
ATOM   7633  C  CA  . PRO B 1 545 ? 121.909 93.131  137.599 1.00 91.42  ? 520  PRO B CA  1 
ATOM   7634  C  C   . PRO B 1 545 ? 122.849 93.833  136.630 1.00 94.02  ? 520  PRO B C   1 
ATOM   7635  O  O   . PRO B 1 545 ? 123.012 93.414  135.481 1.00 94.57  ? 520  PRO B O   1 
ATOM   7636  C  CB  . PRO B 1 545 ? 120.556 92.826  136.949 1.00 89.30  ? 520  PRO B CB  1 
ATOM   7637  C  CG  . PRO B 1 545 ? 119.742 94.048  137.226 1.00 89.94  ? 520  PRO B CG  1 
ATOM   7638  C  CD  . PRO B 1 545 ? 120.219 94.614  138.547 1.00 89.46  ? 520  PRO B CD  1 
ATOM   7639  N  N   . CYS B 1 546 ? 123.471 94.909  137.095 1.00 106.37 ? 521  CYS B N   1 
ATOM   7640  C  CA  . CYS B 1 546 ? 124.236 95.788  136.220 1.00 105.46 ? 521  CYS B CA  1 
ATOM   7641  C  C   . CYS B 1 546 ? 125.523 95.133  135.720 1.00 106.63 ? 521  CYS B C   1 
ATOM   7642  O  O   . CYS B 1 546 ? 126.082 94.239  136.365 1.00 106.22 ? 521  CYS B O   1 
ATOM   7643  C  CB  . CYS B 1 546 ? 124.579 97.087  136.957 1.00 107.18 ? 521  CYS B CB  1 
ATOM   7644  S  SG  . CYS B 1 546 ? 123.516 98.492  136.582 1.00 113.59 ? 521  CYS B SG  1 
ATOM   7645  N  N   . ASN B 1 547 ? 125.978 95.578  134.543 1.00 119.04 ? 522  ASN B N   1 
ATOM   7646  C  CA  . ASN B 1 547 ? 127.382 95.478  134.175 1.00 119.49 ? 522  ASN B CA  1 
ATOM   7647  C  C   . ASN B 1 547 ? 128.186 96.333  135.147 1.00 118.46 ? 522  ASN B C   1 
ATOM   7648  O  O   . ASN B 1 547 ? 127.788 97.459  135.472 1.00 120.43 ? 522  ASN B O   1 
ATOM   7649  C  CB  . ASN B 1 547 ? 127.614 96.014  132.758 1.00 119.98 ? 522  ASN B CB  1 
ATOM   7650  C  CG  . ASN B 1 547 ? 129.101 96.084  132.403 1.00 121.54 ? 522  ASN B CG  1 
ATOM   7651  O  OD1 . ASN B 1 547 ? 129.787 96.947  132.956 1.00 119.46 ? 522  ASN B OD1 1 
ATOM   7652  N  ND2 . ASN B 1 547 ? 129.602 95.293  131.453 1.00 124.97 ? 522  ASN B ND2 1 
ATOM   7653  N  N   . PHE B 1 548 ? 129.343 95.830  135.563 1.00 88.48  ? 523  PHE B N   1 
ATOM   7654  C  CA  . PHE B 1 548 ? 130.321 96.620  136.300 1.00 87.65  ? 523  PHE B CA  1 
ATOM   7655  C  C   . PHE B 1 548 ? 131.685 96.569  135.623 1.00 88.28  ? 523  PHE B C   1 
ATOM   7656  O  O   . PHE B 1 548 ? 132.283 95.496  135.490 1.00 90.29  ? 523  PHE B O   1 
ATOM   7657  C  CB  . PHE B 1 548 ? 130.413 96.151  137.753 1.00 87.29  ? 523  PHE B CB  1 
ATOM   7658  C  CG  . PHE B 1 548 ? 129.188 96.470  138.561 1.00 88.60  ? 523  PHE B CG  1 
ATOM   7659  C  CD1 . PHE B 1 548 ? 128.636 97.741  138.508 1.00 89.00  ? 523  PHE B CD1 1 
ATOM   7660  C  CD2 . PHE B 1 548 ? 128.570 95.510  139.340 1.00 87.38  ? 523  PHE B CD2 1 
ATOM   7661  C  CE1 . PHE B 1 548 ? 127.508 98.059  139.239 1.00 87.27  ? 523  PHE B CE1 1 
ATOM   7662  C  CE2 . PHE B 1 548 ? 127.436 95.821  140.071 1.00 87.43  ? 523  PHE B CE2 1 
ATOM   7663  C  CZ  . PHE B 1 548 ? 126.905 97.097  140.020 1.00 87.68  ? 523  PHE B CZ  1 
ATOM   7664  N  N   . SER B 1 549 ? 132.177 97.736  135.210 1.00 77.27  ? 524  SER B N   1 
ATOM   7665  C  CA  . SER B 1 549 ? 133.485 97.864  134.584 1.00 76.86  ? 524  SER B CA  1 
ATOM   7666  C  C   . SER B 1 549 ? 134.540 98.215  135.636 1.00 76.51  ? 524  SER B C   1 
ATOM   7667  O  O   . SER B 1 549 ? 134.292 98.161  136.843 1.00 79.09  ? 524  SER B O   1 
ATOM   7668  C  CB  . SER B 1 549 ? 133.428 98.902  133.466 1.00 76.30  ? 524  SER B CB  1 
ATOM   7669  O  OG  . SER B 1 549 ? 132.997 100.153 133.976 1.00 72.00  ? 524  SER B OG  1 
ATOM   7670  N  N   . LYS B 1 550 ? 135.745 98.567  135.178 1.00 69.13  ? 525  LYS B N   1 
ATOM   7671  C  CA  . LYS B 1 550 ? 136.811 98.953  136.098 1.00 66.27  ? 525  LYS B CA  1 
ATOM   7672  C  C   . LYS B 1 550 ? 136.554 100.318 136.723 1.00 69.54  ? 525  LYS B C   1 
ATOM   7673  O  O   . LYS B 1 550 ? 136.925 100.547 137.882 1.00 70.62  ? 525  LYS B O   1 
ATOM   7674  C  CB  . LYS B 1 550 ? 138.154 98.949  135.370 1.00 65.01  ? 525  LYS B CB  1 
ATOM   7675  N  N   . ASN B 1 551 ? 135.937 101.236 135.974 1.00 70.13  ? 526  ASN B N   1 
ATOM   7676  C  CA  . ASN B 1 551 ? 135.620 102.550 136.524 1.00 68.68  ? 526  ASN B CA  1 
ATOM   7677  C  C   . ASN B 1 551 ? 134.665 102.434 137.703 1.00 67.09  ? 526  ASN B C   1 
ATOM   7678  O  O   . ASN B 1 551 ? 134.819 103.137 138.709 1.00 64.84  ? 526  ASN B O   1 
ATOM   7679  C  CB  . ASN B 1 551 ? 135.020 103.444 135.439 1.00 67.25  ? 526  ASN B CB  1 
ATOM   7680  C  CG  . ASN B 1 551 ? 135.938 103.611 134.247 1.00 68.69  ? 526  ASN B CG  1 
ATOM   7681  O  OD1 . ASN B 1 551 ? 137.159 103.633 134.390 1.00 70.70  ? 526  ASN B OD1 1 
ATOM   7682  N  ND2 . ASN B 1 551 ? 135.353 103.733 133.060 1.00 68.51  ? 526  ASN B ND2 1 
ATOM   7683  N  N   . ASP B 1 552 ? 133.669 101.552 137.596 1.00 64.06  ? 527  ASP B N   1 
ATOM   7684  C  CA  . ASP B 1 552 ? 132.736 101.352 138.699 1.00 59.39  ? 527  ASP B CA  1 
ATOM   7685  C  C   . ASP B 1 552 ? 133.446 100.796 139.925 1.00 60.62  ? 527  ASP B C   1 
ATOM   7686  O  O   . ASP B 1 552 ? 133.156 101.203 141.055 1.00 64.41  ? 527  ASP B O   1 
ATOM   7687  C  CB  . ASP B 1 552 ? 131.602 100.425 138.265 1.00 61.93  ? 527  ASP B CB  1 
ATOM   7688  C  CG  . ASP B 1 552 ? 130.800 100.988 137.108 1.00 69.06  ? 527  ASP B CG  1 
ATOM   7689  O  OD1 . ASP B 1 552 ? 130.588 102.218 137.075 1.00 67.52  ? 527  ASP B OD1 1 
ATOM   7690  O  OD2 . ASP B 1 552 ? 130.382 100.203 136.231 1.00 71.55  ? 527  ASP B OD2 1 
ATOM   7691  N  N   . VAL B 1 553 ? 134.383 99.866  139.724 1.00 58.28  ? 528  VAL B N   1 
ATOM   7692  C  CA  . VAL B 1 553 ? 135.130 99.306  140.848 1.00 56.26  ? 528  VAL B CA  1 
ATOM   7693  C  C   . VAL B 1 553 ? 135.975 100.382 141.518 1.00 54.34  ? 528  VAL B C   1 
ATOM   7694  O  O   . VAL B 1 553 ? 136.024 100.477 142.752 1.00 57.83  ? 528  VAL B O   1 
ATOM   7695  C  CB  . VAL B 1 553 ? 135.991 98.120  140.377 1.00 54.09  ? 528  VAL B CB  1 
ATOM   7696  C  CG1 . VAL B 1 553 ? 136.914 97.655  141.490 1.00 51.40  ? 528  VAL B CG1 1 
ATOM   7697  C  CG2 . VAL B 1 553 ? 135.106 96.980  139.902 1.00 52.84  ? 528  VAL B CG2 1 
ATOM   7698  N  N   . MET B 1 554 ? 136.652 101.210 140.718 1.00 53.88  ? 529  MET B N   1 
ATOM   7699  C  CA  . MET B 1 554 ? 137.453 102.293 141.282 1.00 59.07  ? 529  MET B CA  1 
ATOM   7700  C  C   . MET B 1 554 ? 136.586 103.274 142.063 1.00 64.09  ? 529  MET B C   1 
ATOM   7701  O  O   . MET B 1 554 ? 136.946 103.689 143.173 1.00 63.98  ? 529  MET B O   1 
ATOM   7702  C  CB  . MET B 1 554 ? 138.213 103.013 140.168 1.00 58.76  ? 529  MET B CB  1 
ATOM   7703  C  CG  . MET B 1 554 ? 138.444 104.495 140.417 1.00 60.22  ? 529  MET B CG  1 
ATOM   7704  S  SD  . MET B 1 554 ? 139.066 105.350 138.956 1.00 76.96  ? 529  MET B SD  1 
ATOM   7705  C  CE  . MET B 1 554 ? 138.537 107.029 139.291 1.00 60.70  ? 529  MET B CE  1 
ATOM   7706  N  N   . LEU B 1 555 ? 135.435 103.651 141.500 1.00 56.26  ? 530  LEU B N   1 
ATOM   7707  C  CA  . LEU B 1 555 ? 134.551 104.587 142.184 1.00 48.17  ? 530  LEU B CA  1 
ATOM   7708  C  C   . LEU B 1 555 ? 134.006 103.993 143.474 1.00 42.07  ? 530  LEU B C   1 
ATOM   7709  O  O   . LEU B 1 555 ? 133.886 104.697 144.482 1.00 48.18  ? 530  LEU B O   1 
ATOM   7710  C  CB  . LEU B 1 555 ? 133.409 105.006 141.264 1.00 45.65  ? 530  LEU B CB  1 
ATOM   7711  C  CG  . LEU B 1 555 ? 132.613 106.207 141.770 1.00 44.57  ? 530  LEU B CG  1 
ATOM   7712  C  CD1 . LEU B 1 555 ? 133.537 107.378 142.050 1.00 45.12  ? 530  LEU B CD1 1 
ATOM   7713  C  CD2 . LEU B 1 555 ? 131.551 106.596 140.768 1.00 46.66  ? 530  LEU B CD2 1 
ATOM   7714  N  N   . SER B 1 556 ? 133.662 102.704 143.463 1.00 35.07  ? 531  SER B N   1 
ATOM   7715  C  CA  . SER B 1 556 ? 133.186 102.055 144.679 1.00 36.72  ? 531  SER B CA  1 
ATOM   7716  C  C   . SER B 1 556 ? 134.267 102.046 145.750 1.00 36.76  ? 531  SER B C   1 
ATOM   7717  O  O   . SER B 1 556 ? 134.003 102.357 146.918 1.00 40.20  ? 531  SER B O   1 
ATOM   7718  C  CB  . SER B 1 556 ? 132.726 100.633 144.365 1.00 41.38  ? 531  SER B CB  1 
ATOM   7719  O  OG  . SER B 1 556 ? 132.673 99.847  145.541 1.00 40.38  ? 531  SER B OG  1 
ATOM   7720  N  N   . ALA B 1 557 ? 135.498 101.700 145.365 1.00 43.79  ? 532  ALA B N   1 
ATOM   7721  C  CA  . ALA B 1 557 ? 136.590 101.694 146.331 1.00 46.37  ? 532  ALA B CA  1 
ATOM   7722  C  C   . ALA B 1 557 ? 136.798 103.079 146.923 1.00 49.10  ? 532  ALA B C   1 
ATOM   7723  O  O   . ALA B 1 557 ? 136.974 103.224 148.138 1.00 51.25  ? 532  ALA B O   1 
ATOM   7724  C  CB  . ALA B 1 557 ? 137.874 101.191 145.673 1.00 42.40  ? 532  ALA B CB  1 
ATOM   7725  N  N   . VAL B 1 558 ? 136.748 104.113 146.083 1.00 44.75  ? 533  VAL B N   1 
ATOM   7726  C  CA  . VAL B 1 558 ? 136.923 105.480 146.566 1.00 41.19  ? 533  VAL B CA  1 
ATOM   7727  C  C   . VAL B 1 558 ? 135.791 105.876 147.509 1.00 43.36  ? 533  VAL B C   1 
ATOM   7728  O  O   . VAL B 1 558 ? 136.021 106.506 148.551 1.00 47.41  ? 533  VAL B O   1 
ATOM   7729  C  CB  . VAL B 1 558 ? 137.036 106.444 145.373 1.00 41.40  ? 533  VAL B CB  1 
ATOM   7730  C  CG1 . VAL B 1 558 ? 136.707 107.865 145.798 1.00 45.02  ? 533  VAL B CG1 1 
ATOM   7731  C  CG2 . VAL B 1 558 ? 138.426 106.351 144.778 1.00 48.36  ? 533  VAL B CG2 1 
ATOM   7732  N  N   . VAL B 1 559 ? 134.552 105.530 147.154 1.00 41.70  ? 534  VAL B N   1 
ATOM   7733  C  CA  . VAL B 1 559 ? 133.405 105.934 147.962 1.00 34.15  ? 534  VAL B CA  1 
ATOM   7734  C  C   . VAL B 1 559 ? 133.474 105.292 149.342 1.00 33.99  ? 534  VAL B C   1 
ATOM   7735  O  O   . VAL B 1 559 ? 133.292 105.962 150.367 1.00 38.38  ? 534  VAL B O   1 
ATOM   7736  C  CB  . VAL B 1 559 ? 132.091 105.591 147.238 1.00 31.58  ? 534  VAL B CB  1 
ATOM   7737  C  CG1 . VAL B 1 559 ? 130.970 105.394 148.235 1.00 39.86  ? 534  VAL B CG1 1 
ATOM   7738  C  CG2 . VAL B 1 559 ? 131.735 106.685 146.251 1.00 28.56  ? 534  VAL B CG2 1 
ATOM   7739  N  N   . MET B 1 560 ? 133.751 103.985 149.396 1.00 34.44  ? 535  MET B N   1 
ATOM   7740  C  CA  . MET B 1 560 ? 133.875 103.362 150.711 1.00 38.11  ? 535  MET B CA  1 
ATOM   7741  C  C   . MET B 1 560 ? 135.121 103.826 151.450 1.00 41.24  ? 535  MET B C   1 
ATOM   7742  O  O   . MET B 1 560 ? 135.117 103.853 152.683 1.00 43.52  ? 535  MET B O   1 
ATOM   7743  C  CB  . MET B 1 560 ? 133.845 101.837 150.623 1.00 30.58  ? 535  MET B CB  1 
ATOM   7744  C  CG  . MET B 1 560 ? 133.055 101.275 149.479 1.00 37.50  ? 535  MET B CG  1 
ATOM   7745  S  SD  . MET B 1 560 ? 132.974 99.487  149.583 1.00 56.13  ? 535  MET B SD  1 
ATOM   7746  C  CE  . MET B 1 560 ? 134.706 99.087  149.437 1.00 43.99  ? 535  MET B CE  1 
ATOM   7747  N  N   . THR B 1 561 ? 136.184 104.214 150.741 1.00 39.42  ? 536  THR B N   1 
ATOM   7748  C  CA  . THR B 1 561 ? 137.325 104.807 151.429 1.00 38.02  ? 536  THR B CA  1 
ATOM   7749  C  C   . THR B 1 561 ? 136.923 106.097 152.131 1.00 40.50  ? 536  THR B C   1 
ATOM   7750  O  O   . THR B 1 561 ? 137.262 106.309 153.301 1.00 43.32  ? 536  THR B O   1 
ATOM   7751  C  CB  . THR B 1 561 ? 138.464 105.065 150.442 1.00 37.30  ? 536  THR B CB  1 
ATOM   7752  O  OG1 . THR B 1 561 ? 139.058 103.819 150.059 1.00 44.72  ? 536  THR B OG1 1 
ATOM   7753  C  CG2 . THR B 1 561 ? 139.525 105.952 151.071 1.00 36.04  ? 536  THR B CG2 1 
ATOM   7754  N  N   . TYR B 1 562 ? 136.170 106.955 151.439 1.00 38.97  ? 537  TYR B N   1 
ATOM   7755  C  CA  . TYR B 1 562 ? 135.691 108.194 152.049 1.00 36.72  ? 537  TYR B CA  1 
ATOM   7756  C  C   . TYR B 1 562 ? 134.793 107.904 153.247 1.00 37.67  ? 537  TYR B C   1 
ATOM   7757  O  O   . TYR B 1 562 ? 134.948 108.503 154.321 1.00 43.03  ? 537  TYR B O   1 
ATOM   7758  C  CB  . TYR B 1 562 ? 134.935 109.026 151.013 1.00 38.11  ? 537  TYR B CB  1 
ATOM   7759  C  CG  . TYR B 1 562 ? 135.802 109.935 150.175 1.00 40.88  ? 537  TYR B CG  1 
ATOM   7760  C  CD1 . TYR B 1 562 ? 136.736 110.774 150.763 1.00 38.55  ? 537  TYR B CD1 1 
ATOM   7761  C  CD2 . TYR B 1 562 ? 135.679 109.960 148.793 1.00 41.22  ? 537  TYR B CD2 1 
ATOM   7762  C  CE1 . TYR B 1 562 ? 137.527 111.607 149.998 1.00 36.04  ? 537  TYR B CE1 1 
ATOM   7763  C  CE2 . TYR B 1 562 ? 136.464 110.789 148.021 1.00 40.44  ? 537  TYR B CE2 1 
ATOM   7764  C  CZ  . TYR B 1 562 ? 137.386 111.610 148.629 1.00 39.51  ? 537  TYR B CZ  1 
ATOM   7765  O  OH  . TYR B 1 562 ? 138.171 112.438 147.864 1.00 47.47  ? 537  TYR B OH  1 
ATOM   7766  N  N   . TRP B 1 563 ? 133.844 106.980 153.076 1.00 38.87  ? 538  TRP B N   1 
ATOM   7767  C  CA  . TRP B 1 563 ? 132.903 106.674 154.150 1.00 40.32  ? 538  TRP B CA  1 
ATOM   7768  C  C   . TRP B 1 563 ? 133.617 106.105 155.371 1.00 44.75  ? 538  TRP B C   1 
ATOM   7769  O  O   . TRP B 1 563 ? 133.329 106.498 156.508 1.00 47.58  ? 538  TRP B O   1 
ATOM   7770  C  CB  . TRP B 1 563 ? 131.835 105.701 153.651 1.00 35.58  ? 538  TRP B CB  1 
ATOM   7771  C  CG  . TRP B 1 563 ? 130.579 106.351 153.133 1.00 33.40  ? 538  TRP B CG  1 
ATOM   7772  C  CD1 . TRP B 1 563 ? 129.301 106.048 153.495 1.00 36.72  ? 538  TRP B CD1 1 
ATOM   7773  C  CD2 . TRP B 1 563 ? 130.478 107.395 152.151 1.00 36.14  ? 538  TRP B CD2 1 
ATOM   7774  N  NE1 . TRP B 1 563 ? 128.412 106.839 152.811 1.00 39.38  ? 538  TRP B NE1 1 
ATOM   7775  C  CE2 . TRP B 1 563 ? 129.109 107.673 151.979 1.00 32.49  ? 538  TRP B CE2 1 
ATOM   7776  C  CE3 . TRP B 1 563 ? 131.410 108.122 151.406 1.00 38.16  ? 538  TRP B CE3 1 
ATOM   7777  C  CZ2 . TRP B 1 563 ? 128.651 108.644 151.095 1.00 35.62  ? 538  TRP B CZ2 1 
ATOM   7778  C  CZ3 . TRP B 1 563 ? 130.952 109.084 150.529 1.00 35.84  ? 538  TRP B CZ3 1 
ATOM   7779  C  CH2 . TRP B 1 563 ? 129.586 109.337 150.381 1.00 38.12  ? 538  TRP B CH2 1 
ATOM   7780  N  N   . THR B 1 564 ? 134.560 105.185 155.157 1.00 39.43  ? 539  THR B N   1 
ATOM   7781  C  CA  . THR B 1 564 ? 135.275 104.589 156.277 1.00 31.28  ? 539  THR B CA  1 
ATOM   7782  C  C   . THR B 1 564 ? 136.219 105.582 156.937 1.00 41.97  ? 539  THR B C   1 
ATOM   7783  O  O   . THR B 1 564 ? 136.414 105.523 158.153 1.00 47.81  ? 539  THR B O   1 
ATOM   7784  C  CB  . THR B 1 564 ? 136.039 103.353 155.814 1.00 33.31  ? 539  THR B CB  1 
ATOM   7785  O  OG1 . THR B 1 564 ? 136.834 103.683 154.671 1.00 43.09  ? 539  THR B OG1 1 
ATOM   7786  C  CG2 . THR B 1 564 ? 135.065 102.248 155.445 1.00 34.35  ? 539  THR B CG2 1 
ATOM   7787  N  N   . ASN B 1 565 ? 136.812 106.500 156.168 1.00 40.95  ? 540  ASN B N   1 
ATOM   7788  C  CA  . ASN B 1 565 ? 137.605 107.558 156.784 1.00 36.93  ? 540  ASN B CA  1 
ATOM   7789  C  C   . ASN B 1 565 ? 136.740 108.428 157.686 1.00 38.19  ? 540  ASN B C   1 
ATOM   7790  O  O   . ASN B 1 565 ? 137.143 108.773 158.807 1.00 40.61  ? 540  ASN B O   1 
ATOM   7791  C  CB  . ASN B 1 565 ? 138.277 108.407 155.707 1.00 39.73  ? 540  ASN B CB  1 
ATOM   7792  C  CG  . ASN B 1 565 ? 139.402 107.675 155.011 1.00 48.80  ? 540  ASN B CG  1 
ATOM   7793  O  OD1 . ASN B 1 565 ? 139.816 106.600 155.440 1.00 49.78  ? 540  ASN B OD1 1 
ATOM   7794  N  ND2 . ASN B 1 565 ? 139.906 108.254 153.928 1.00 48.29  ? 540  ASN B ND2 1 
ATOM   7795  N  N   . PHE B 1 566 ? 135.541 108.784 157.217 1.00 36.10  ? 541  PHE B N   1 
ATOM   7796  C  CA  . PHE B 1 566 ? 134.629 109.558 158.053 1.00 37.85  ? 541  PHE B CA  1 
ATOM   7797  C  C   . PHE B 1 566 ? 134.248 108.787 159.309 1.00 38.35  ? 541  PHE B C   1 
ATOM   7798  O  O   . PHE B 1 566 ? 134.185 109.359 160.403 1.00 43.87  ? 541  PHE B O   1 
ATOM   7799  C  CB  . PHE B 1 566 ? 133.375 109.941 157.268 1.00 39.54  ? 541  PHE B CB  1 
ATOM   7800  C  CG  . PHE B 1 566 ? 132.424 110.806 158.043 1.00 37.96  ? 541  PHE B CG  1 
ATOM   7801  C  CD1 . PHE B 1 566 ? 132.682 112.152 158.224 1.00 36.70  ? 541  PHE B CD1 1 
ATOM   7802  C  CD2 . PHE B 1 566 ? 131.281 110.269 158.605 1.00 36.77  ? 541  PHE B CD2 1 
ATOM   7803  C  CE1 . PHE B 1 566 ? 131.813 112.948 158.941 1.00 35.65  ? 541  PHE B CE1 1 
ATOM   7804  C  CE2 . PHE B 1 566 ? 130.409 111.060 159.323 1.00 37.23  ? 541  PHE B CE2 1 
ATOM   7805  C  CZ  . PHE B 1 566 ? 130.676 112.400 159.491 1.00 38.69  ? 541  PHE B CZ  1 
ATOM   7806  N  N   . ALA B 1 567 ? 133.982 107.488 159.171 1.00 32.30  ? 542  ALA B N   1 
ATOM   7807  C  CA  . ALA B 1 567 ? 133.638 106.680 160.337 1.00 28.54  ? 542  ALA B CA  1 
ATOM   7808  C  C   . ALA B 1 567 ? 134.795 106.613 161.325 1.00 34.75  ? 542  ALA B C   1 
ATOM   7809  O  O   . ALA B 1 567 ? 134.585 106.665 162.543 1.00 31.06  ? 542  ALA B O   1 
ATOM   7810  C  CB  . ALA B 1 567 ? 133.224 105.277 159.900 1.00 32.38  ? 542  ALA B CB  1 
ATOM   7811  N  N   . LYS B 1 568 ? 136.025 106.489 160.821 1.00 43.63  ? 543  LYS B N   1 
ATOM   7812  C  CA  . LYS B 1 568 ? 137.182 106.350 161.698 1.00 35.85  ? 543  LYS B CA  1 
ATOM   7813  C  C   . LYS B 1 568 ? 137.474 107.640 162.452 1.00 37.75  ? 543  LYS B C   1 
ATOM   7814  O  O   . LYS B 1 568 ? 137.653 107.626 163.675 1.00 39.74  ? 543  LYS B O   1 
ATOM   7815  C  CB  . LYS B 1 568 ? 138.408 105.925 160.890 1.00 32.73  ? 543  LYS B CB  1 
ATOM   7816  C  CG  . LYS B 1 568 ? 138.409 104.476 160.446 1.00 33.36  ? 543  LYS B CG  1 
ATOM   7817  C  CD  . LYS B 1 568 ? 139.571 104.211 159.506 1.00 36.50  ? 543  LYS B CD  1 
ATOM   7818  C  CE  . LYS B 1 568 ? 139.369 102.935 158.714 1.00 36.82  ? 543  LYS B CE  1 
ATOM   7819  N  NZ  . LYS B 1 568 ? 140.199 102.917 157.479 1.00 36.46  ? 543  LYS B NZ  1 
ATOM   7820  N  N   . THR B 1 569 ? 137.527 108.772 161.745 1.00 38.48  ? 544  THR B N   1 
ATOM   7821  C  CA  . THR B 1 569 ? 138.018 109.998 162.359 1.00 39.79  ? 544  THR B CA  1 
ATOM   7822  C  C   . THR B 1 569 ? 137.107 111.207 162.202 1.00 34.65  ? 544  THR B C   1 
ATOM   7823  O  O   . THR B 1 569 ? 137.443 112.277 162.720 1.00 37.57  ? 544  THR B O   1 
ATOM   7824  C  CB  . THR B 1 569 ? 139.402 110.358 161.799 1.00 37.87  ? 544  THR B CB  1 
ATOM   7825  O  OG1 . THR B 1 569 ? 139.944 111.459 162.538 1.00 43.94  ? 544  THR B OG1 1 
ATOM   7826  C  CG2 . THR B 1 569 ? 139.290 110.751 160.342 1.00 32.65  ? 544  THR B CG2 1 
ATOM   7827  N  N   . GLY B 1 570 ? 135.978 111.081 161.514 1.00 30.23  ? 545  GLY B N   1 
ATOM   7828  C  CA  . GLY B 1 570 ? 135.120 112.228 161.301 1.00 35.54  ? 545  GLY B CA  1 
ATOM   7829  C  C   . GLY B 1 570 ? 135.597 113.188 160.238 1.00 39.64  ? 545  GLY B C   1 
ATOM   7830  O  O   . GLY B 1 570 ? 134.998 114.256 160.076 1.00 41.22  ? 545  GLY B O   1 
ATOM   7831  N  N   . ASP B 1 571 ? 136.656 112.843 159.512 1.00 44.22  ? 546  ASP B N   1 
ATOM   7832  C  CA  . ASP B 1 571 ? 137.191 113.662 158.434 1.00 41.16  ? 546  ASP B CA  1 
ATOM   7833  C  C   . ASP B 1 571 ? 137.525 112.751 157.261 1.00 47.38  ? 546  ASP B C   1 
ATOM   7834  O  O   . ASP B 1 571 ? 138.399 111.884 157.378 1.00 60.16  ? 546  ASP B O   1 
ATOM   7835  C  CB  . ASP B 1 571 ? 138.426 114.433 158.903 1.00 43.35  ? 546  ASP B CB  1 
ATOM   7836  C  CG  . ASP B 1 571 ? 138.862 115.497 157.916 1.00 51.90  ? 546  ASP B CG  1 
ATOM   7837  O  OD1 . ASP B 1 571 ? 138.183 115.676 156.885 1.00 58.29  ? 546  ASP B OD1 1 
ATOM   7838  O  OD2 . ASP B 1 571 ? 139.889 116.158 158.173 1.00 53.63  ? 546  ASP B OD2 1 
ATOM   7839  N  N   . PRO B 1 572 ? 136.859 112.912 156.118 1.00 37.45  ? 547  PRO B N   1 
ATOM   7840  C  CA  . PRO B 1 572 ? 137.009 111.939 155.026 1.00 42.88  ? 547  PRO B CA  1 
ATOM   7841  C  C   . PRO B 1 572 ? 138.368 111.952 154.339 1.00 50.45  ? 547  PRO B C   1 
ATOM   7842  O  O   . PRO B 1 572 ? 138.545 111.274 153.323 1.00 52.55  ? 547  PRO B O   1 
ATOM   7843  C  CB  . PRO B 1 572 ? 135.900 112.346 154.048 1.00 33.84  ? 547  PRO B CB  1 
ATOM   7844  C  CG  . PRO B 1 572 ? 134.910 113.083 154.880 1.00 35.58  ? 547  PRO B CG  1 
ATOM   7845  C  CD  . PRO B 1 572 ? 135.725 113.821 155.891 1.00 37.70  ? 547  PRO B CD  1 
ATOM   7846  N  N   . ASN B 1 573 ? 139.334 112.707 154.864 1.00 53.50  ? 548  ASN B N   1 
ATOM   7847  C  CA  . ASN B 1 573 ? 140.650 112.797 154.248 1.00 55.06  ? 548  ASN B CA  1 
ATOM   7848  C  C   . ASN B 1 573 ? 141.798 112.338 155.134 1.00 55.62  ? 548  ASN B C   1 
ATOM   7849  O  O   . ASN B 1 573 ? 142.864 112.012 154.602 1.00 61.35  ? 548  ASN B O   1 
ATOM   7850  C  CB  . ASN B 1 573 ? 140.938 114.241 153.804 1.00 50.69  ? 548  ASN B CB  1 
ATOM   7851  C  CG  . ASN B 1 573 ? 139.680 115.008 153.462 1.00 49.76  ? 548  ASN B CG  1 
ATOM   7852  O  OD1 . ASN B 1 573 ? 138.974 114.671 152.513 1.00 53.93  ? 548  ASN B OD1 1 
ATOM   7853  N  ND2 . ASN B 1 573 ? 139.393 116.049 154.234 1.00 47.06  ? 548  ASN B ND2 1 
ATOM   7854  N  N   . GLN B 1 574 ? 141.620 112.301 156.450 1.00 61.70  ? 549  GLN B N   1 
ATOM   7855  C  CA  . GLN B 1 574 ? 142.740 112.141 157.372 1.00 64.98  ? 549  GLN B CA  1 
ATOM   7856  C  C   . GLN B 1 574 ? 143.389 110.756 157.334 1.00 70.76  ? 549  GLN B C   1 
ATOM   7857  O  O   . GLN B 1 574 ? 144.559 110.647 156.945 1.00 74.37  ? 549  GLN B O   1 
ATOM   7858  C  CB  . GLN B 1 574 ? 142.292 112.469 158.800 1.00 62.16  ? 549  GLN B CB  1 
ATOM   7859  N  N   . PRO B 1 575 ? 142.686 109.673 157.726 1.00 67.00  ? 550  PRO B N   1 
ATOM   7860  C  CA  . PRO B 1 575 ? 143.404 108.438 158.077 1.00 63.78  ? 550  PRO B CA  1 
ATOM   7861  C  C   . PRO B 1 575 ? 144.054 107.710 156.908 1.00 64.36  ? 550  PRO B C   1 
ATOM   7862  O  O   . PRO B 1 575 ? 145.251 107.414 156.955 1.00 66.03  ? 550  PRO B O   1 
ATOM   7863  C  CB  . PRO B 1 575 ? 142.314 107.579 158.727 1.00 60.41  ? 550  PRO B CB  1 
ATOM   7864  C  CG  . PRO B 1 575 ? 141.059 108.019 158.085 1.00 63.76  ? 550  PRO B CG  1 
ATOM   7865  C  CD  . PRO B 1 575 ? 141.230 109.452 157.652 1.00 61.30  ? 550  PRO B CD  1 
ATOM   7866  N  N   . VAL B 1 576 ? 143.295 107.420 155.860 1.00 70.09  ? 551  VAL B N   1 
ATOM   7867  C  CA  . VAL B 1 576 ? 143.743 106.547 154.779 1.00 71.79  ? 551  VAL B CA  1 
ATOM   7868  C  C   . VAL B 1 576 ? 144.005 107.408 153.547 1.00 72.28  ? 551  VAL B C   1 
ATOM   7869  O  O   . VAL B 1 576 ? 143.104 108.128 153.099 1.00 73.28  ? 551  VAL B O   1 
ATOM   7870  C  CB  . VAL B 1 576 ? 142.714 105.445 154.478 1.00 70.46  ? 551  VAL B CB  1 
ATOM   7871  C  CG1 . VAL B 1 576 ? 142.805 104.998 153.027 1.00 67.68  ? 551  VAL B CG1 1 
ATOM   7872  C  CG2 . VAL B 1 576 ? 142.916 104.265 155.415 1.00 70.55  ? 551  VAL B CG2 1 
ATOM   7873  N  N   . PRO B 1 577 ? 145.212 107.383 152.985 1.00 83.49  ? 552  PRO B N   1 
ATOM   7874  C  CA  . PRO B 1 577 ? 145.457 108.115 151.739 1.00 83.84  ? 552  PRO B CA  1 
ATOM   7875  C  C   . PRO B 1 577 ? 144.660 107.523 150.590 1.00 80.96  ? 552  PRO B C   1 
ATOM   7876  O  O   . PRO B 1 577 ? 144.370 106.325 150.552 1.00 79.14  ? 552  PRO B O   1 
ATOM   7877  C  CB  . PRO B 1 577 ? 146.964 107.945 151.518 1.00 83.45  ? 552  PRO B CB  1 
ATOM   7878  C  CG  . PRO B 1 577 ? 147.301 106.676 152.226 1.00 82.11  ? 552  PRO B CG  1 
ATOM   7879  C  CD  . PRO B 1 577 ? 146.395 106.625 153.426 1.00 82.87  ? 552  PRO B CD  1 
ATOM   7880  N  N   . GLN B 1 578 ? 144.308 108.382 149.640 1.00 71.66  ? 553  GLN B N   1 
ATOM   7881  C  CA  . GLN B 1 578 ? 143.467 107.961 148.530 1.00 72.61  ? 553  GLN B CA  1 
ATOM   7882  C  C   . GLN B 1 578 ? 144.302 107.371 147.399 1.00 72.65  ? 553  GLN B C   1 
ATOM   7883  O  O   . GLN B 1 578 ? 144.591 108.045 146.412 1.00 78.24  ? 553  GLN B O   1 
ATOM   7884  C  CB  . GLN B 1 578 ? 142.636 109.134 148.014 1.00 72.25  ? 553  GLN B CB  1 
ATOM   7885  C  CG  . GLN B 1 578 ? 141.405 108.697 147.257 1.00 69.82  ? 553  GLN B CG  1 
ATOM   7886  C  CD  . GLN B 1 578 ? 140.270 108.350 148.195 1.00 70.34  ? 553  GLN B CD  1 
ATOM   7887  O  OE1 . GLN B 1 578 ? 140.303 108.690 149.376 1.00 70.51  ? 553  GLN B OE1 1 
ATOM   7888  N  NE2 . GLN B 1 578 ? 139.272 107.649 147.681 1.00 70.40  ? 553  GLN B NE2 1 
ATOM   7889  N  N   . ARG B 1 589 ? 141.712 110.687 139.488 1.00 93.36  ? 564  ARG B N   1 
ATOM   7890  C  CA  . ARG B 1 589 ? 141.825 112.113 139.766 1.00 94.69  ? 564  ARG B CA  1 
ATOM   7891  C  C   . ARG B 1 589 ? 141.460 112.378 141.221 1.00 95.70  ? 564  ARG B C   1 
ATOM   7892  O  O   . ARG B 1 589 ? 141.340 113.525 141.651 1.00 98.24  ? 564  ARG B O   1 
ATOM   7893  C  CB  . ARG B 1 589 ? 140.924 112.915 138.828 1.00 94.42  ? 564  ARG B CB  1 
ATOM   7894  C  CG  . ARG B 1 589 ? 141.228 112.695 137.355 1.00 95.14  ? 564  ARG B CG  1 
ATOM   7895  C  CD  . ARG B 1 589 ? 140.022 113.019 136.490 1.00 95.19  ? 564  ARG B CD  1 
ATOM   7896  N  NE  . ARG B 1 589 ? 140.045 112.294 135.225 1.00 96.77  ? 564  ARG B NE  1 
ATOM   7897  C  CZ  . ARG B 1 589 ? 139.683 111.026 135.087 1.00 96.38  ? 564  ARG B CZ  1 
ATOM   7898  N  NH1 . ARG B 1 589 ? 139.262 110.312 136.117 1.00 95.54  ? 564  ARG B NH1 1 
ATOM   7899  N  NH2 . ARG B 1 589 ? 139.741 110.461 133.884 1.00 94.54  ? 564  ARG B NH2 1 
ATOM   7900  N  N   . PHE B 1 590 ? 141.288 111.293 141.970 1.00 84.73  ? 565  PHE B N   1 
ATOM   7901  C  CA  . PHE B 1 590 ? 140.886 111.323 143.370 1.00 86.63  ? 565  PHE B CA  1 
ATOM   7902  C  C   . PHE B 1 590 ? 142.056 111.513 144.326 1.00 86.78  ? 565  PHE B C   1 
ATOM   7903  O  O   . PHE B 1 590 ? 141.835 111.638 145.535 1.00 84.69  ? 565  PHE B O   1 
ATOM   7904  C  CB  . PHE B 1 590 ? 140.147 110.024 143.706 1.00 86.19  ? 565  PHE B CB  1 
ATOM   7905  C  CG  . PHE B 1 590 ? 138.673 110.064 143.411 1.00 85.90  ? 565  PHE B CG  1 
ATOM   7906  C  CD1 . PHE B 1 590 ? 137.920 111.190 143.686 1.00 81.03  ? 565  PHE B CD1 1 
ATOM   7907  C  CD2 . PHE B 1 590 ? 138.058 108.995 142.785 1.00 85.89  ? 565  PHE B CD2 1 
ATOM   7908  C  CE1 . PHE B 1 590 ? 136.566 111.214 143.411 1.00 78.13  ? 565  PHE B CE1 1 
ATOM   7909  C  CE2 . PHE B 1 590 ? 136.710 109.021 142.495 1.00 83.20  ? 565  PHE B CE2 1 
ATOM   7910  C  CZ  . PHE B 1 590 ? 135.965 110.134 142.803 1.00 79.42  ? 565  PHE B CZ  1 
ATOM   7911  N  N   . GLU B 1 591 ? 143.290 111.527 143.820 1.00 106.41 ? 566  GLU B N   1 
ATOM   7912  C  CA  . GLU B 1 591 ? 144.452 111.684 144.687 1.00 106.63 ? 566  GLU B CA  1 
ATOM   7913  C  C   . GLU B 1 591 ? 144.622 113.123 145.160 1.00 107.06 ? 566  GLU B C   1 
ATOM   7914  O  O   . GLU B 1 591 ? 144.943 113.358 146.331 1.00 105.59 ? 566  GLU B O   1 
ATOM   7915  C  CB  . GLU B 1 591 ? 145.712 111.212 143.959 1.00 108.17 ? 566  GLU B CB  1 
ATOM   7916  C  CG  . GLU B 1 591 ? 145.830 109.701 143.839 1.00 107.22 ? 566  GLU B CG  1 
ATOM   7917  C  CD  . GLU B 1 591 ? 145.457 109.191 142.461 1.00 107.64 ? 566  GLU B CD  1 
ATOM   7918  O  OE1 . GLU B 1 591 ? 145.998 109.714 141.464 1.00 107.33 ? 566  GLU B OE1 1 
ATOM   7919  O  OE2 . GLU B 1 591 ? 144.622 108.267 142.375 1.00 108.33 ? 566  GLU B OE2 1 
ATOM   7920  N  N   . GLU B 1 592 ? 144.408 114.094 144.275 1.00 114.35 ? 567  GLU B N   1 
ATOM   7921  C  CA  . GLU B 1 592 ? 144.716 115.495 144.540 1.00 114.45 ? 567  GLU B CA  1 
ATOM   7922  C  C   . GLU B 1 592 ? 143.460 116.333 144.762 1.00 114.07 ? 567  GLU B C   1 
ATOM   7923  O  O   . GLU B 1 592 ? 143.384 117.488 144.340 1.00 113.73 ? 567  GLU B O   1 
ATOM   7924  C  CB  . GLU B 1 592 ? 145.550 116.086 143.406 1.00 115.45 ? 567  GLU B CB  1 
ATOM   7925  C  CG  . GLU B 1 592 ? 145.009 115.797 142.014 1.00 116.24 ? 567  GLU B CG  1 
ATOM   7926  C  CD  . GLU B 1 592 ? 145.726 114.645 141.337 1.00 116.87 ? 567  GLU B CD  1 
ATOM   7927  O  OE1 . GLU B 1 592 ? 146.586 114.014 141.986 1.00 115.91 ? 567  GLU B OE1 1 
ATOM   7928  O  OE2 . GLU B 1 592 ? 145.432 114.374 140.153 1.00 117.15 ? 567  GLU B OE2 1 
ATOM   7929  N  N   . VAL B 1 593 ? 142.458 115.765 145.427 1.00 92.25  ? 568  VAL B N   1 
ATOM   7930  C  CA  . VAL B 1 593 ? 141.245 116.485 145.793 1.00 87.55  ? 568  VAL B CA  1 
ATOM   7931  C  C   . VAL B 1 593 ? 141.124 116.477 147.311 1.00 84.34  ? 568  VAL B C   1 
ATOM   7932  O  O   . VAL B 1 593 ? 141.195 115.415 147.941 1.00 85.60  ? 568  VAL B O   1 
ATOM   7933  C  CB  . VAL B 1 593 ? 139.993 115.878 145.133 1.00 83.91  ? 568  VAL B CB  1 
ATOM   7934  C  CG1 . VAL B 1 593 ? 139.934 116.266 143.667 1.00 85.73  ? 568  VAL B CG1 1 
ATOM   7935  C  CG2 . VAL B 1 593 ? 139.991 114.367 145.275 1.00 83.92  ? 568  VAL B CG2 1 
ATOM   7936  N  N   . VAL B 1 594 ? 140.959 117.660 147.895 1.00 54.30  ? 569  VAL B N   1 
ATOM   7937  C  CA  . VAL B 1 594 ? 140.808 117.817 149.336 1.00 52.66  ? 569  VAL B CA  1 
ATOM   7938  C  C   . VAL B 1 594 ? 139.359 118.190 149.612 1.00 58.66  ? 569  VAL B C   1 
ATOM   7939  O  O   . VAL B 1 594 ? 138.882 119.238 149.160 1.00 63.44  ? 569  VAL B O   1 
ATOM   7940  C  CB  . VAL B 1 594 ? 141.770 118.875 149.897 1.00 57.29  ? 569  VAL B CB  1 
ATOM   7941  C  CG1 . VAL B 1 594 ? 141.319 119.328 151.277 1.00 53.30  ? 569  VAL B CG1 1 
ATOM   7942  C  CG2 . VAL B 1 594 ? 143.185 118.325 149.949 1.00 59.51  ? 569  VAL B CG2 1 
ATOM   7943  N  N   . TRP B 1 595 ? 138.660 117.331 150.348 1.00 52.73  ? 570  TRP B N   1 
ATOM   7944  C  CA  . TRP B 1 595 ? 137.263 117.573 150.682 1.00 48.48  ? 570  TRP B CA  1 
ATOM   7945  C  C   . TRP B 1 595 ? 137.185 118.578 151.825 1.00 54.31  ? 570  TRP B C   1 
ATOM   7946  O  O   . TRP B 1 595 ? 137.656 118.304 152.934 1.00 54.05  ? 570  TRP B O   1 
ATOM   7947  C  CB  . TRP B 1 595 ? 136.576 116.264 151.059 1.00 47.09  ? 570  TRP B CB  1 
ATOM   7948  C  CG  . TRP B 1 595 ? 135.085 116.308 150.956 1.00 48.98  ? 570  TRP B CG  1 
ATOM   7949  C  CD1 . TRP B 1 595 ? 134.306 117.416 150.801 1.00 46.12  ? 570  TRP B CD1 1 
ATOM   7950  C  CD2 . TRP B 1 595 ? 134.190 115.192 151.002 1.00 49.81  ? 570  TRP B CD2 1 
ATOM   7951  N  NE1 . TRP B 1 595 ? 132.982 117.059 150.749 1.00 50.50  ? 570  TRP B NE1 1 
ATOM   7952  C  CE2 . TRP B 1 595 ? 132.885 115.698 150.870 1.00 49.04  ? 570  TRP B CE2 1 
ATOM   7953  C  CE3 . TRP B 1 595 ? 134.368 113.814 151.143 1.00 49.74  ? 570  TRP B CE3 1 
ATOM   7954  C  CZ2 . TRP B 1 595 ? 131.765 114.876 150.874 1.00 48.23  ? 570  TRP B CZ2 1 
ATOM   7955  C  CZ3 . TRP B 1 595 ? 133.254 113.000 151.146 1.00 47.83  ? 570  TRP B CZ3 1 
ATOM   7956  C  CH2 . TRP B 1 595 ? 131.969 113.532 151.012 1.00 44.44  ? 570  TRP B CH2 1 
ATOM   7957  N  N   . SER B 1 596 ? 136.593 119.736 151.555 1.00 40.52  ? 571  SER B N   1 
ATOM   7958  C  CA  . SER B 1 596 ? 136.479 120.807 152.532 1.00 37.59  ? 571  SER B CA  1 
ATOM   7959  C  C   . SER B 1 596 ? 135.092 120.810 153.163 1.00 38.58  ? 571  SER B C   1 
ATOM   7960  O  O   . SER B 1 596 ? 134.144 120.218 152.642 1.00 43.90  ? 571  SER B O   1 
ATOM   7961  C  CB  . SER B 1 596 ? 136.765 122.163 151.884 1.00 37.54  ? 571  SER B CB  1 
ATOM   7962  O  OG  . SER B 1 596 ? 136.978 123.162 152.864 1.00 45.29  ? 571  SER B OG  1 
ATOM   7963  N  N   . LYS B 1 597 ? 134.986 121.492 154.300 1.00 33.29  ? 572  LYS B N   1 
ATOM   7964  C  CA  . LYS B 1 597 ? 133.732 121.549 155.035 1.00 34.64  ? 572  LYS B CA  1 
ATOM   7965  C  C   . LYS B 1 597 ? 132.698 122.368 154.264 1.00 36.73  ? 572  LYS B C   1 
ATOM   7966  O  O   . LYS B 1 597 ? 132.966 122.924 153.195 1.00 45.20  ? 572  LYS B O   1 
ATOM   7967  C  CB  . LYS B 1 597 ? 133.958 122.134 156.427 1.00 33.79  ? 572  LYS B CB  1 
ATOM   7968  C  CG  . LYS B 1 597 ? 134.988 121.391 157.255 1.00 40.34  ? 572  LYS B CG  1 
ATOM   7969  C  CD  . LYS B 1 597 ? 134.843 121.721 158.730 1.00 41.13  ? 572  LYS B CD  1 
ATOM   7970  C  CE  . LYS B 1 597 ? 136.150 121.508 159.474 1.00 45.88  ? 572  LYS B CE  1 
ATOM   7971  N  NZ  . LYS B 1 597 ? 136.692 120.137 159.267 1.00 46.06  ? 572  LYS B NZ  1 
ATOM   7972  N  N   . PHE B 1 598 ? 131.496 122.444 154.823 1.00 30.16  ? 573  PHE B N   1 
ATOM   7973  C  CA  . PHE B 1 598 ? 130.375 123.160 154.222 1.00 30.64  ? 573  PHE B CA  1 
ATOM   7974  C  C   . PHE B 1 598 ? 130.088 124.383 155.088 1.00 37.43  ? 573  PHE B C   1 
ATOM   7975  O  O   . PHE B 1 598 ? 129.293 124.326 156.027 1.00 37.78  ? 573  PHE B O   1 
ATOM   7976  C  CB  . PHE B 1 598 ? 129.153 122.251 154.103 1.00 33.83  ? 573  PHE B CB  1 
ATOM   7977  C  CG  . PHE B 1 598 ? 127.993 122.874 153.378 1.00 25.31  ? 573  PHE B CG  1 
ATOM   7978  C  CD1 . PHE B 1 598 ? 127.059 123.636 154.058 1.00 23.20  ? 573  PHE B CD1 1 
ATOM   7979  C  CD2 . PHE B 1 598 ? 127.828 122.685 152.020 1.00 34.33  ? 573  PHE B CD2 1 
ATOM   7980  C  CE1 . PHE B 1 598 ? 125.993 124.204 153.397 1.00 28.87  ? 573  PHE B CE1 1 
ATOM   7981  C  CE2 . PHE B 1 598 ? 126.762 123.250 151.354 1.00 33.22  ? 573  PHE B CE2 1 
ATOM   7982  C  CZ  . PHE B 1 598 ? 125.844 124.010 152.043 1.00 32.22  ? 573  PHE B CZ  1 
ATOM   7983  N  N   . ASN B 1 599 ? 130.750 125.491 154.772 1.00 42.73  ? 574  ASN B N   1 
ATOM   7984  C  CA  . ASN B 1 599 ? 130.474 126.750 155.445 1.00 38.55  ? 574  ASN B CA  1 
ATOM   7985  C  C   . ASN B 1 599 ? 129.215 127.381 154.868 1.00 38.05  ? 574  ASN B C   1 
ATOM   7986  O  O   . ASN B 1 599 ? 128.947 127.280 153.668 1.00 36.49  ? 574  ASN B O   1 
ATOM   7987  C  CB  . ASN B 1 599 ? 131.658 127.707 155.304 1.00 28.75  ? 574  ASN B CB  1 
ATOM   7988  N  N   . SER B 1 600 ? 128.429 128.023 155.734 1.00 38.26  ? 575  SER B N   1 
ATOM   7989  C  CA  . SER B 1 600 ? 127.205 128.670 155.274 1.00 32.37  ? 575  SER B CA  1 
ATOM   7990  C  C   . SER B 1 600 ? 127.510 129.802 154.300 1.00 39.44  ? 575  SER B C   1 
ATOM   7991  O  O   . SER B 1 600 ? 126.818 129.964 153.289 1.00 41.27  ? 575  SER B O   1 
ATOM   7992  C  CB  . SER B 1 600 ? 126.404 129.189 156.467 1.00 35.03  ? 575  SER B CB  1 
ATOM   7993  O  OG  . SER B 1 600 ? 125.327 130.003 156.039 1.00 34.78  ? 575  SER B OG  1 
ATOM   7994  N  N   . LYS B 1 601 ? 128.541 130.599 154.591 1.00 40.73  ? 576  LYS B N   1 
ATOM   7995  C  CA  . LYS B 1 601 ? 128.906 131.696 153.699 1.00 34.63  ? 576  LYS B CA  1 
ATOM   7996  C  C   . LYS B 1 601 ? 129.473 131.178 152.383 1.00 40.06  ? 576  LYS B C   1 
ATOM   7997  O  O   . LYS B 1 601 ? 129.160 131.712 151.313 1.00 44.00  ? 576  LYS B O   1 
ATOM   7998  C  CB  . LYS B 1 601 ? 129.910 132.617 154.390 1.00 35.71  ? 576  LYS B CB  1 
ATOM   7999  C  CG  . LYS B 1 601 ? 129.342 133.369 155.581 1.00 42.02  ? 576  LYS B CG  1 
ATOM   8000  C  CD  . LYS B 1 601 ? 130.272 133.286 156.780 1.00 43.65  ? 576  LYS B CD  1 
ATOM   8001  C  CE  . LYS B 1 601 ? 130.068 131.990 157.548 1.00 44.24  ? 576  LYS B CE  1 
ATOM   8002  N  NZ  . LYS B 1 601 ? 128.849 132.036 158.403 1.00 40.23  ? 576  LYS B NZ  1 
ATOM   8003  N  N   . GLU B 1 602 ? 130.308 130.143 152.442 1.00 43.00  ? 577  GLU B N   1 
ATOM   8004  C  CA  . GLU B 1 602 ? 130.947 129.561 151.263 1.00 43.10  ? 577  GLU B CA  1 
ATOM   8005  C  C   . GLU B 1 602 ? 130.598 128.076 151.240 1.00 42.19  ? 577  GLU B C   1 
ATOM   8006  O  O   . GLU B 1 602 ? 131.225 127.275 151.940 1.00 50.27  ? 577  GLU B O   1 
ATOM   8007  C  CB  . GLU B 1 602 ? 132.455 129.787 151.294 1.00 41.33  ? 577  GLU B CB  1 
ATOM   8008  C  CG  . GLU B 1 602 ? 133.193 129.277 150.074 1.00 39.47  ? 577  GLU B CG  1 
ATOM   8009  C  CD  . GLU B 1 602 ? 134.693 129.239 150.281 1.00 48.26  ? 577  GLU B CD  1 
ATOM   8010  O  OE1 . GLU B 1 602 ? 135.136 129.376 151.440 1.00 49.48  ? 577  GLU B OE1 1 
ATOM   8011  O  OE2 . GLU B 1 602 ? 135.430 129.077 149.285 1.00 48.39  ? 577  GLU B OE2 1 
ATOM   8012  N  N   . LYS B 1 603 ? 129.605 127.710 150.433 1.00 26.44  ? 578  LYS B N   1 
ATOM   8013  C  CA  . LYS B 1 603 ? 129.022 126.369 150.474 1.00 34.52  ? 578  LYS B CA  1 
ATOM   8014  C  C   . LYS B 1 603 ? 129.814 125.395 149.599 1.00 34.97  ? 578  LYS B C   1 
ATOM   8015  O  O   . LYS B 1 603 ? 129.318 124.844 148.619 1.00 37.49  ? 578  LYS B O   1 
ATOM   8016  C  CB  . LYS B 1 603 ? 127.560 126.424 150.049 1.00 39.92  ? 578  LYS B CB  1 
ATOM   8017  C  CG  . LYS B 1 603 ? 126.800 127.624 150.586 1.00 38.23  ? 578  LYS B CG  1 
ATOM   8018  C  CD  . LYS B 1 603 ? 125.303 127.447 150.412 1.00 35.20  ? 578  LYS B CD  1 
ATOM   8019  C  CE  . LYS B 1 603 ? 124.569 128.761 150.604 1.00 29.14  ? 578  LYS B CE  1 
ATOM   8020  N  NZ  . LYS B 1 603 ? 125.058 129.500 151.797 1.00 33.21  ? 578  LYS B NZ  1 
ATOM   8021  N  N   . GLN B 1 604 ? 131.066 125.171 149.988 1.00 41.24  ? 579  GLN B N   1 
ATOM   8022  C  CA  . GLN B 1 604 ? 131.922 124.253 149.249 1.00 41.31  ? 579  GLN B CA  1 
ATOM   8023  C  C   . GLN B 1 604 ? 131.435 122.817 149.398 1.00 42.60  ? 579  GLN B C   1 
ATOM   8024  O  O   . GLN B 1 604 ? 131.099 122.367 150.497 1.00 39.83  ? 579  GLN B O   1 
ATOM   8025  C  CB  . GLN B 1 604 ? 133.365 124.364 149.736 1.00 35.15  ? 579  GLN B CB  1 
ATOM   8026  C  CG  . GLN B 1 604 ? 134.224 125.316 148.927 1.00 41.98  ? 579  GLN B CG  1 
ATOM   8027  C  CD  . GLN B 1 604 ? 135.651 125.370 149.426 1.00 46.13  ? 579  GLN B CD  1 
ATOM   8028  O  OE1 . GLN B 1 604 ? 135.897 125.480 150.627 1.00 45.68  ? 579  GLN B OE1 1 
ATOM   8029  N  NE2 . GLN B 1 604 ? 136.604 125.291 148.505 1.00 45.03  ? 579  GLN B NE2 1 
ATOM   8030  N  N   . TYR B 1 605 ? 131.403 122.093 148.281 1.00 38.47  ? 580  TYR B N   1 
ATOM   8031  C  CA  . TYR B 1 605 ? 131.052 120.680 148.279 1.00 30.62  ? 580  TYR B CA  1 
ATOM   8032  C  C   . TYR B 1 605 ? 131.991 119.955 147.328 1.00 40.96  ? 580  TYR B C   1 
ATOM   8033  O  O   . TYR B 1 605 ? 132.785 120.574 146.618 1.00 56.12  ? 580  TYR B O   1 
ATOM   8034  C  CB  . TYR B 1 605 ? 129.584 120.461 147.887 1.00 33.10  ? 580  TYR B CB  1 
ATOM   8035  C  CG  . TYR B 1 605 ? 129.288 120.624 146.413 1.00 29.99  ? 580  TYR B CG  1 
ATOM   8036  C  CD1 . TYR B 1 605 ? 129.372 119.546 145.542 1.00 44.01  ? 580  TYR B CD1 1 
ATOM   8037  C  CD2 . TYR B 1 605 ? 128.915 121.852 145.893 1.00 37.02  ? 580  TYR B CD2 1 
ATOM   8038  C  CE1 . TYR B 1 605 ? 129.101 119.689 144.199 1.00 40.15  ? 580  TYR B CE1 1 
ATOM   8039  C  CE2 . TYR B 1 605 ? 128.642 122.004 144.550 1.00 41.66  ? 580  TYR B CE2 1 
ATOM   8040  C  CZ  . TYR B 1 605 ? 128.736 120.919 143.708 1.00 36.46  ? 580  TYR B CZ  1 
ATOM   8041  O  OH  . TYR B 1 605 ? 128.465 121.063 142.368 1.00 41.41  ? 580  TYR B OH  1 
ATOM   8042  N  N   . LEU B 1 606 ? 131.905 118.628 147.318 1.00 34.98  ? 581  LEU B N   1 
ATOM   8043  C  CA  . LEU B 1 606 ? 132.763 117.806 146.478 1.00 35.45  ? 581  LEU B CA  1 
ATOM   8044  C  C   . LEU B 1 606 ? 131.900 116.973 145.541 1.00 31.91  ? 581  LEU B C   1 
ATOM   8045  O  O   . LEU B 1 606 ? 130.873 116.427 145.952 1.00 45.99  ? 581  LEU B O   1 
ATOM   8046  C  CB  . LEU B 1 606 ? 133.672 116.914 147.332 1.00 44.26  ? 581  LEU B CB  1 
ATOM   8047  C  CG  . LEU B 1 606 ? 134.396 115.735 146.683 1.00 42.60  ? 581  LEU B CG  1 
ATOM   8048  C  CD1 . LEU B 1 606 ? 135.802 115.644 147.248 1.00 46.42  ? 581  LEU B CD1 1 
ATOM   8049  C  CD2 . LEU B 1 606 ? 133.663 114.433 146.903 1.00 40.23  ? 581  LEU B CD2 1 
ATOM   8050  N  N   . HIS B 1 607 ? 132.327 116.866 144.284 1.00 31.41  ? 582  HIS B N   1 
ATOM   8051  C  CA  . HIS B 1 607 ? 131.507 116.318 143.205 1.00 35.91  ? 582  HIS B CA  1 
ATOM   8052  C  C   . HIS B 1 607 ? 131.996 114.910 142.883 1.00 39.45  ? 582  HIS B C   1 
ATOM   8053  O  O   . HIS B 1 607 ? 132.900 114.718 142.071 1.00 50.49  ? 582  HIS B O   1 
ATOM   8054  C  CB  . HIS B 1 607 ? 131.579 117.243 141.995 1.00 39.12  ? 582  HIS B CB  1 
ATOM   8055  C  CG  . HIS B 1 607 ? 130.932 116.698 140.762 1.00 36.49  ? 582  HIS B CG  1 
ATOM   8056  N  ND1 . HIS B 1 607 ? 131.489 115.686 140.010 1.00 39.22  ? 582  HIS B ND1 1 
ATOM   8057  C  CD2 . HIS B 1 607 ? 129.787 117.048 140.130 1.00 37.63  ? 582  HIS B CD2 1 
ATOM   8058  C  CE1 . HIS B 1 607 ? 130.707 115.424 138.979 1.00 42.58  ? 582  HIS B CE1 1 
ATOM   8059  N  NE2 . HIS B 1 607 ? 129.669 116.239 139.026 1.00 40.95  ? 582  HIS B NE2 1 
ATOM   8060  N  N   . ILE B 1 608 ? 131.385 113.913 143.524 1.00 24.86  ? 583  ILE B N   1 
ATOM   8061  C  CA  . ILE B 1 608 ? 131.775 112.526 143.295 1.00 22.63  ? 583  ILE B CA  1 
ATOM   8062  C  C   . ILE B 1 608 ? 131.426 112.129 141.868 1.00 29.39  ? 583  ILE B C   1 
ATOM   8063  O  O   . ILE B 1 608 ? 130.335 112.431 141.369 1.00 37.07  ? 583  ILE B O   1 
ATOM   8064  C  CB  . ILE B 1 608 ? 131.097 111.597 144.311 1.00 26.97  ? 583  ILE B CB  1 
ATOM   8065  C  CG1 . ILE B 1 608 ? 131.395 112.057 145.735 1.00 29.97  ? 583  ILE B CG1 1 
ATOM   8066  C  CG2 . ILE B 1 608 ? 131.581 110.171 144.127 1.00 30.62  ? 583  ILE B CG2 1 
ATOM   8067  C  CD1 . ILE B 1 608 ? 130.949 111.090 146.799 1.00 30.77  ? 583  ILE B CD1 1 
ATOM   8068  N  N   . GLY B 1 609 ? 132.352 111.454 141.204 1.00 45.53  ? 584  GLY B N   1 
ATOM   8069  C  CA  . GLY B 1 609 ? 132.139 111.024 139.839 1.00 46.51  ? 584  GLY B CA  1 
ATOM   8070  C  C   . GLY B 1 609 ? 133.463 110.695 139.179 1.00 51.94  ? 584  GLY B C   1 
ATOM   8071  O  O   . GLY B 1 609 ? 134.513 110.676 139.821 1.00 52.69  ? 584  GLY B O   1 
ATOM   8072  N  N   . LEU B 1 610 ? 133.385 110.437 137.872 1.00 63.22  ? 585  LEU B N   1 
ATOM   8073  C  CA  . LEU B 1 610 ? 134.584 110.144 137.098 1.00 63.27  ? 585  LEU B CA  1 
ATOM   8074  C  C   . LEU B 1 610 ? 135.453 111.374 136.875 1.00 64.56  ? 585  LEU B C   1 
ATOM   8075  O  O   . LEU B 1 610 ? 136.605 111.229 136.453 1.00 64.57  ? 585  LEU B O   1 
ATOM   8076  C  CB  . LEU B 1 610 ? 134.206 109.528 135.751 1.00 60.21  ? 585  LEU B CB  1 
ATOM   8077  C  CG  . LEU B 1 610 ? 134.067 108.004 135.722 1.00 60.23  ? 585  LEU B CG  1 
ATOM   8078  C  CD1 . LEU B 1 610 ? 135.282 107.342 136.352 1.00 59.59  ? 585  LEU B CD1 1 
ATOM   8079  C  CD2 . LEU B 1 610 ? 132.789 107.557 136.414 1.00 60.07  ? 585  LEU B CD2 1 
ATOM   8080  N  N   . LYS B 1 611 ? 134.932 112.570 137.140 1.00 59.45  ? 586  LYS B N   1 
ATOM   8081  C  CA  . LYS B 1 611 ? 135.689 113.817 137.039 1.00 55.29  ? 586  LYS B CA  1 
ATOM   8082  C  C   . LYS B 1 611 ? 135.492 114.606 138.327 1.00 59.22  ? 586  LYS B C   1 
ATOM   8083  O  O   . LYS B 1 611 ? 134.749 115.595 138.362 1.00 61.30  ? 586  LYS B O   1 
ATOM   8084  C  CB  . LYS B 1 611 ? 135.255 114.629 135.818 1.00 54.60  ? 586  LYS B CB  1 
ATOM   8085  N  N   . PRO B 1 612 ? 136.142 114.188 139.411 1.00 61.83  ? 587  PRO B N   1 
ATOM   8086  C  CA  . PRO B 1 612 ? 135.933 114.851 140.703 1.00 60.19  ? 587  PRO B CA  1 
ATOM   8087  C  C   . PRO B 1 612 ? 136.434 116.284 140.705 1.00 55.13  ? 587  PRO B C   1 
ATOM   8088  O  O   . PRO B 1 612 ? 137.365 116.646 139.981 1.00 58.02  ? 587  PRO B O   1 
ATOM   8089  C  CB  . PRO B 1 612 ? 136.743 113.992 141.676 1.00 54.38  ? 587  PRO B CB  1 
ATOM   8090  C  CG  . PRO B 1 612 ? 137.778 113.342 140.827 1.00 59.40  ? 587  PRO B CG  1 
ATOM   8091  C  CD  . PRO B 1 612 ? 137.120 113.092 139.504 1.00 57.79  ? 587  PRO B CD  1 
ATOM   8092  N  N   . ARG B 1 613 ? 135.807 117.099 141.549 1.00 38.92  ? 588  ARG B N   1 
ATOM   8093  C  CA  . ARG B 1 613 ? 136.177 118.499 141.688 1.00 45.24  ? 588  ARG B CA  1 
ATOM   8094  C  C   . ARG B 1 613 ? 135.470 119.068 142.908 1.00 47.66  ? 588  ARG B C   1 
ATOM   8095  O  O   . ARG B 1 613 ? 134.362 118.647 143.249 1.00 52.20  ? 588  ARG B O   1 
ATOM   8096  C  CB  . ARG B 1 613 ? 135.812 119.295 140.427 1.00 47.31  ? 588  ARG B CB  1 
ATOM   8097  C  CG  . ARG B 1 613 ? 136.417 120.684 140.351 1.00 50.95  ? 588  ARG B CG  1 
ATOM   8098  C  CD  . ARG B 1 613 ? 136.369 121.205 138.922 1.00 47.96  ? 588  ARG B CD  1 
ATOM   8099  N  NE  . ARG B 1 613 ? 135.578 122.423 138.793 1.00 46.35  ? 588  ARG B NE  1 
ATOM   8100  C  CZ  . ARG B 1 613 ? 135.961 123.618 139.219 1.00 49.63  ? 588  ARG B CZ  1 
ATOM   8101  N  NH1 . ARG B 1 613 ? 137.129 123.800 139.814 1.00 50.39  ? 588  ARG B NH1 1 
ATOM   8102  N  NH2 . ARG B 1 613 ? 135.153 124.660 139.040 1.00 48.19  ? 588  ARG B NH2 1 
ATOM   8103  N  N   . VAL B 1 614 ? 136.122 120.021 143.563 1.00 37.58  ? 589  VAL B N   1 
ATOM   8104  C  CA  . VAL B 1 614 ? 135.540 120.707 144.710 1.00 33.48  ? 589  VAL B CA  1 
ATOM   8105  C  C   . VAL B 1 614 ? 134.915 122.000 144.202 1.00 35.91  ? 589  VAL B C   1 
ATOM   8106  O  O   . VAL B 1 614 ? 135.616 122.894 143.722 1.00 48.06  ? 589  VAL B O   1 
ATOM   8107  C  CB  . VAL B 1 614 ? 136.586 120.977 145.797 1.00 38.01  ? 589  VAL B CB  1 
ATOM   8108  C  CG1 . VAL B 1 614 ? 135.911 121.423 147.083 1.00 35.49  ? 589  VAL B CG1 1 
ATOM   8109  C  CG2 . VAL B 1 614 ? 137.422 119.733 146.040 1.00 42.56  ? 589  VAL B CG2 1 
ATOM   8110  N  N   . ARG B 1 615 ? 133.595 122.099 144.307 1.00 37.33  ? 590  ARG B N   1 
ATOM   8111  C  CA  . ARG B 1 615 ? 132.843 123.224 143.776 1.00 39.01  ? 590  ARG B CA  1 
ATOM   8112  C  C   . ARG B 1 615 ? 132.333 124.106 144.909 1.00 43.52  ? 590  ARG B C   1 
ATOM   8113  O  O   . ARG B 1 615 ? 132.411 123.759 146.091 1.00 48.44  ? 590  ARG B O   1 
ATOM   8114  C  CB  . ARG B 1 615 ? 131.683 122.732 142.905 1.00 41.36  ? 590  ARG B CB  1 
ATOM   8115  C  CG  . ARG B 1 615 ? 132.076 121.612 141.956 1.00 41.36  ? 590  ARG B CG  1 
ATOM   8116  C  CD  . ARG B 1 615 ? 132.517 122.153 140.609 1.00 45.24  ? 590  ARG B CD  1 
ATOM   8117  N  NE  . ARG B 1 615 ? 131.457 122.065 139.612 1.00 48.59  ? 590  ARG B NE  1 
ATOM   8118  C  CZ  . ARG B 1 615 ? 131.373 121.112 138.694 1.00 51.28  ? 590  ARG B CZ  1 
ATOM   8119  N  NH1 . ARG B 1 615 ? 132.273 120.146 138.616 1.00 49.75  ? 590  ARG B NH1 1 
ATOM   8120  N  NH2 . ARG B 1 615 ? 130.360 121.130 137.832 1.00 49.52  ? 590  ARG B NH2 1 
ATOM   8121  N  N   . ASP B 1 616 ? 131.785 125.258 144.522 1.00 38.03  ? 591  ASP B N   1 
ATOM   8122  C  CA  . ASP B 1 616 ? 131.486 126.333 145.458 1.00 39.21  ? 591  ASP B CA  1 
ATOM   8123  C  C   . ASP B 1 616 ? 130.011 126.488 145.789 1.00 45.61  ? 591  ASP B C   1 
ATOM   8124  O  O   . ASP B 1 616 ? 129.689 126.920 146.897 1.00 53.50  ? 591  ASP B O   1 
ATOM   8125  C  CB  . ASP B 1 616 ? 132.007 127.667 144.908 1.00 44.68  ? 591  ASP B CB  1 
ATOM   8126  C  CG  . ASP B 1 616 ? 132.742 128.479 145.952 1.00 49.53  ? 591  ASP B CG  1 
ATOM   8127  O  OD1 . ASP B 1 616 ? 132.306 128.478 147.120 1.00 49.37  ? 591  ASP B OD1 1 
ATOM   8128  O  OD2 . ASP B 1 616 ? 133.758 129.117 145.604 1.00 50.32  ? 591  ASP B OD2 1 
ATOM   8129  N  N   . ASN B 1 617 ? 129.108 126.167 144.866 1.00 42.10  ? 592  ASN B N   1 
ATOM   8130  C  CA  . ASN B 1 617 ? 127.677 126.321 145.125 1.00 39.84  ? 592  ASN B CA  1 
ATOM   8131  C  C   . ASN B 1 617 ? 126.914 125.372 144.217 1.00 42.73  ? 592  ASN B C   1 
ATOM   8132  O  O   . ASN B 1 617 ? 127.040 125.457 142.992 1.00 46.64  ? 592  ASN B O   1 
ATOM   8133  C  CB  . ASN B 1 617 ? 127.229 127.764 144.894 1.00 38.80  ? 592  ASN B CB  1 
ATOM   8134  C  CG  . ASN B 1 617 ? 127.208 128.580 146.170 1.00 42.87  ? 592  ASN B CG  1 
ATOM   8135  O  OD1 . ASN B 1 617 ? 128.166 129.283 146.488 1.00 47.66  ? 592  ASN B OD1 1 
ATOM   8136  N  ND2 . ASN B 1 617 ? 126.110 128.491 146.910 1.00 42.69  ? 592  ASN B ND2 1 
ATOM   8137  N  N   . TYR B 1 618 ? 126.125 124.479 144.809 1.00 37.74  ? 593  TYR B N   1 
ATOM   8138  C  CA  . TYR B 1 618 ? 125.329 123.521 144.049 1.00 40.56  ? 593  TYR B CA  1 
ATOM   8139  C  C   . TYR B 1 618 ? 123.965 124.130 143.752 1.00 43.78  ? 593  TYR B C   1 
ATOM   8140  O  O   . TYR B 1 618 ? 123.125 124.249 144.649 1.00 48.59  ? 593  TYR B O   1 
ATOM   8141  C  CB  . TYR B 1 618 ? 125.177 122.208 144.810 1.00 40.32  ? 593  TYR B CB  1 
ATOM   8142  C  CG  . TYR B 1 618 ? 124.572 121.106 143.973 1.00 38.91  ? 593  TYR B CG  1 
ATOM   8143  C  CD1 . TYR B 1 618 ? 125.018 120.869 142.682 1.00 44.20  ? 593  TYR B CD1 1 
ATOM   8144  C  CD2 . TYR B 1 618 ? 123.552 120.310 144.469 1.00 36.13  ? 593  TYR B CD2 1 
ATOM   8145  C  CE1 . TYR B 1 618 ? 124.470 119.868 141.910 1.00 40.12  ? 593  TYR B CE1 1 
ATOM   8146  C  CE2 . TYR B 1 618 ? 122.997 119.305 143.703 1.00 41.73  ? 593  TYR B CE2 1 
ATOM   8147  C  CZ  . TYR B 1 618 ? 123.460 119.090 142.425 1.00 43.16  ? 593  TYR B CZ  1 
ATOM   8148  O  OH  . TYR B 1 618 ? 122.912 118.091 141.657 1.00 49.11  ? 593  TYR B OH  1 
ATOM   8149  N  N   . ARG B 1 619 ? 123.745 124.498 142.491 1.00 38.03  ? 594  ARG B N   1 
ATOM   8150  C  CA  . ARG B 1 619 ? 122.464 125.022 142.023 1.00 30.35  ? 594  ARG B CA  1 
ATOM   8151  C  C   . ARG B 1 619 ? 121.991 126.174 142.907 1.00 32.98  ? 594  ARG B C   1 
ATOM   8152  O  O   . ARG B 1 619 ? 120.893 126.159 143.463 1.00 42.30  ? 594  ARG B O   1 
ATOM   8153  C  CB  . ARG B 1 619 ? 121.415 123.910 141.962 1.00 33.78  ? 594  ARG B CB  1 
ATOM   8154  C  CG  . ARG B 1 619 ? 121.583 122.956 140.794 1.00 30.53  ? 594  ARG B CG  1 
ATOM   8155  C  CD  . ARG B 1 619 ? 120.462 121.934 140.762 1.00 29.24  ? 594  ARG B CD  1 
ATOM   8156  N  NE  . ARG B 1 619 ? 120.254 121.388 139.427 1.00 35.19  ? 594  ARG B NE  1 
ATOM   8157  C  CZ  . ARG B 1 619 ? 119.555 121.987 138.473 1.00 38.75  ? 594  ARG B CZ  1 
ATOM   8158  N  NH1 . ARG B 1 619 ? 118.977 123.159 138.672 1.00 39.29  ? 594  ARG B NH1 1 
ATOM   8159  N  NH2 . ARG B 1 619 ? 119.433 121.394 137.289 1.00 43.17  ? 594  ARG B NH2 1 
ATOM   8160  N  N   . ALA B 1 620 ? 122.857 127.181 143.034 1.00 26.64  ? 595  ALA B N   1 
ATOM   8161  C  CA  . ALA B 1 620 ? 122.564 128.297 143.927 1.00 25.54  ? 595  ALA B CA  1 
ATOM   8162  C  C   . ALA B 1 620 ? 121.295 129.023 143.507 1.00 30.50  ? 595  ALA B C   1 
ATOM   8163  O  O   . ALA B 1 620 ? 120.502 129.443 144.357 1.00 39.26  ? 595  ALA B O   1 
ATOM   8164  C  CB  . ALA B 1 620 ? 123.747 129.262 143.969 1.00 27.13  ? 595  ALA B CB  1 
ATOM   8165  N  N   . ASN B 1 621 ? 121.078 129.168 142.199 1.00 32.76  ? 596  ASN B N   1 
ATOM   8166  C  CA  . ASN B 1 621 ? 119.901 129.883 141.714 1.00 32.12  ? 596  ASN B CA  1 
ATOM   8167  C  C   . ASN B 1 621 ? 118.614 129.181 142.133 1.00 41.45  ? 596  ASN B C   1 
ATOM   8168  O  O   . ASN B 1 621 ? 117.728 129.795 142.736 1.00 48.89  ? 596  ASN B O   1 
ATOM   8169  C  CB  . ASN B 1 621 ? 119.972 130.025 140.194 1.00 33.23  ? 596  ASN B CB  1 
ATOM   8170  C  CG  . ASN B 1 621 ? 119.030 131.085 139.664 1.00 40.94  ? 596  ASN B CG  1 
ATOM   8171  O  OD1 . ASN B 1 621 ? 118.398 131.809 140.431 1.00 46.53  ? 596  ASN B OD1 1 
ATOM   8172  N  ND2 . ASN B 1 621 ? 118.933 131.183 138.343 1.00 38.43  ? 596  ASN B ND2 1 
ATOM   8173  N  N   . LYS B 1 622 ? 118.502 127.881 141.848 1.00 37.28  ? 597  LYS B N   1 
ATOM   8174  C  CA  . LYS B 1 622 ? 117.257 127.171 142.132 1.00 33.57  ? 597  LYS B CA  1 
ATOM   8175  C  C   . LYS B 1 622 ? 117.071 126.934 143.627 1.00 34.48  ? 597  LYS B C   1 
ATOM   8176  O  O   . LYS B 1 622 ? 115.946 127.002 144.137 1.00 46.48  ? 597  LYS B O   1 
ATOM   8177  C  CB  . LYS B 1 622 ? 117.224 125.852 141.366 1.00 32.70  ? 597  LYS B CB  1 
ATOM   8178  C  CG  . LYS B 1 622 ? 117.791 125.951 139.963 1.00 35.39  ? 597  LYS B CG  1 
ATOM   8179  C  CD  . LYS B 1 622 ? 116.877 126.744 139.048 1.00 31.79  ? 597  LYS B CD  1 
ATOM   8180  C  CE  . LYS B 1 622 ? 117.311 126.618 137.598 1.00 34.60  ? 597  LYS B CE  1 
ATOM   8181  N  NZ  . LYS B 1 622 ? 116.545 127.527 136.705 1.00 43.72  ? 597  LYS B NZ  1 
ATOM   8182  N  N   . VAL B 1 623 ? 118.158 126.647 144.346 1.00 29.77  ? 598  VAL B N   1 
ATOM   8183  C  CA  . VAL B 1 623 ? 118.059 126.476 145.793 1.00 31.07  ? 598  VAL B CA  1 
ATOM   8184  C  C   . VAL B 1 623 ? 117.617 127.776 146.452 1.00 39.90  ? 598  VAL B C   1 
ATOM   8185  O  O   . VAL B 1 623 ? 116.754 127.777 147.340 1.00 48.00  ? 598  VAL B O   1 
ATOM   8186  C  CB  . VAL B 1 623 ? 119.394 125.972 146.367 1.00 26.27  ? 598  VAL B CB  1 
ATOM   8187  C  CG1 . VAL B 1 623 ? 119.384 126.056 147.879 1.00 27.67  ? 598  VAL B CG1 1 
ATOM   8188  C  CG2 . VAL B 1 623 ? 119.651 124.548 145.922 1.00 29.69  ? 598  VAL B CG2 1 
ATOM   8189  N  N   . ALA B 1 624 ? 118.195 128.903 146.029 1.00 36.73  ? 599  ALA B N   1 
ATOM   8190  C  CA  . ALA B 1 624 ? 117.758 130.192 146.551 1.00 36.12  ? 599  ALA B CA  1 
ATOM   8191  C  C   . ALA B 1 624 ? 116.323 130.499 146.147 1.00 40.35  ? 599  ALA B C   1 
ATOM   8192  O  O   . ALA B 1 624 ? 115.590 131.130 146.915 1.00 48.31  ? 599  ALA B O   1 
ATOM   8193  C  CB  . ALA B 1 624 ? 118.694 131.299 146.073 1.00 42.56  ? 599  ALA B CB  1 
ATOM   8194  N  N   . PHE B 1 625 ? 115.906 130.064 144.957 1.00 41.31  ? 600  PHE B N   1 
ATOM   8195  C  CA  . PHE B 1 625 ? 114.515 130.225 144.548 1.00 46.36  ? 600  PHE B CA  1 
ATOM   8196  C  C   . PHE B 1 625 ? 113.582 129.493 145.504 1.00 51.01  ? 600  PHE B C   1 
ATOM   8197  O  O   . PHE B 1 625 ? 112.574 130.048 145.957 1.00 55.63  ? 600  PHE B O   1 
ATOM   8198  C  CB  . PHE B 1 625 ? 114.344 129.711 143.116 1.00 50.52  ? 600  PHE B CB  1 
ATOM   8199  C  CG  . PHE B 1 625 ? 112.915 129.618 142.656 1.00 46.74  ? 600  PHE B CG  1 
ATOM   8200  C  CD1 . PHE B 1 625 ? 111.989 130.585 142.998 1.00 51.40  ? 600  PHE B CD1 1 
ATOM   8201  C  CD2 . PHE B 1 625 ? 112.504 128.562 141.867 1.00 46.57  ? 600  PHE B CD2 1 
ATOM   8202  C  CE1 . PHE B 1 625 ? 110.683 130.494 142.571 1.00 44.95  ? 600  PHE B CE1 1 
ATOM   8203  C  CE2 . PHE B 1 625 ? 111.200 128.469 141.438 1.00 48.95  ? 600  PHE B CE2 1 
ATOM   8204  C  CZ  . PHE B 1 625 ? 110.290 129.436 141.791 1.00 45.26  ? 600  PHE B CZ  1 
ATOM   8205  N  N   . TRP B 1 626 ? 113.912 128.246 145.834 1.00 54.10  ? 601  TRP B N   1 
ATOM   8206  C  CA  . TRP B 1 626 ? 113.025 127.451 146.677 1.00 48.83  ? 601  TRP B CA  1 
ATOM   8207  C  C   . TRP B 1 626 ? 113.076 127.867 148.140 1.00 49.45  ? 601  TRP B C   1 
ATOM   8208  O  O   . TRP B 1 626 ? 112.087 127.693 148.859 1.00 53.88  ? 601  TRP B O   1 
ATOM   8209  C  CB  . TRP B 1 626 ? 113.358 125.967 146.546 1.00 46.22  ? 601  TRP B CB  1 
ATOM   8210  C  CG  . TRP B 1 626 ? 112.877 125.382 145.268 1.00 40.90  ? 601  TRP B CG  1 
ATOM   8211  C  CD1 . TRP B 1 626 ? 113.639 124.870 144.266 1.00 48.70  ? 601  TRP B CD1 1 
ATOM   8212  C  CD2 . TRP B 1 626 ? 111.517 125.263 144.842 1.00 37.72  ? 601  TRP B CD2 1 
ATOM   8213  N  NE1 . TRP B 1 626 ? 112.839 124.430 143.241 1.00 47.24  ? 601  TRP B NE1 1 
ATOM   8214  C  CE2 . TRP B 1 626 ? 111.531 124.661 143.572 1.00 41.34  ? 601  TRP B CE2 1 
ATOM   8215  C  CE3 . TRP B 1 626 ? 110.288 125.602 145.413 1.00 42.44  ? 601  TRP B CE3 1 
ATOM   8216  C  CZ2 . TRP B 1 626 ? 110.367 124.393 142.863 1.00 50.61  ? 601  TRP B CZ2 1 
ATOM   8217  C  CZ3 . TRP B 1 626 ? 109.135 125.335 144.707 1.00 51.10  ? 601  TRP B CZ3 1 
ATOM   8218  C  CH2 . TRP B 1 626 ? 109.181 124.736 143.447 1.00 54.65  ? 601  TRP B CH2 1 
ATOM   8219  N  N   . LEU B 1 627 ? 114.201 128.409 148.603 1.00 47.67  ? 602  LEU B N   1 
ATOM   8220  C  CA  . LEU B 1 627 ? 114.329 128.737 150.017 1.00 46.82  ? 602  LEU B CA  1 
ATOM   8221  C  C   . LEU B 1 627 ? 113.961 130.177 150.347 1.00 50.34  ? 602  LEU B C   1 
ATOM   8222  O  O   . LEU B 1 627 ? 113.437 130.434 151.437 1.00 53.15  ? 602  LEU B O   1 
ATOM   8223  C  CB  . LEU B 1 627 ? 115.757 128.462 150.496 1.00 49.09  ? 602  LEU B CB  1 
ATOM   8224  C  CG  . LEU B 1 627 ? 116.239 127.013 150.442 1.00 48.85  ? 602  LEU B CG  1 
ATOM   8225  C  CD1 . LEU B 1 627 ? 117.636 126.899 151.025 1.00 45.32  ? 602  LEU B CD1 1 
ATOM   8226  C  CD2 . LEU B 1 627 ? 115.273 126.099 151.174 1.00 50.68  ? 602  LEU B CD2 1 
ATOM   8227  N  N   . GLU B 1 628 ? 114.218 131.127 149.445 1.00 43.04  ? 603  GLU B N   1 
ATOM   8228  C  CA  . GLU B 1 628 ? 114.117 132.538 149.780 1.00 39.33  ? 603  GLU B CA  1 
ATOM   8229  C  C   . GLU B 1 628 ? 113.128 133.328 148.935 1.00 41.20  ? 603  GLU B C   1 
ATOM   8230  O  O   . GLU B 1 628 ? 112.849 134.484 149.274 1.00 46.85  ? 603  GLU B O   1 
ATOM   8231  C  CB  . GLU B 1 628 ? 115.498 133.204 149.677 1.00 42.46  ? 603  GLU B CB  1 
ATOM   8232  C  CG  . GLU B 1 628 ? 116.639 132.308 150.129 1.00 42.67  ? 603  GLU B CG  1 
ATOM   8233  C  CD  . GLU B 1 628 ? 117.693 133.055 150.916 1.00 48.85  ? 603  GLU B CD  1 
ATOM   8234  O  OE1 . GLU B 1 628 ? 117.396 134.166 151.403 1.00 48.83  ? 603  GLU B OE1 1 
ATOM   8235  O  OE2 . GLU B 1 628 ? 118.817 132.530 151.053 1.00 48.76  ? 603  GLU B OE2 1 
ATOM   8236  N  N   . LEU B 1 629 ? 112.591 132.762 147.856 1.00 33.35  ? 604  LEU B N   1 
ATOM   8237  C  CA  . LEU B 1 629 ? 111.591 133.453 147.050 1.00 25.52  ? 604  LEU B CA  1 
ATOM   8238  C  C   . LEU B 1 629 ? 110.201 132.853 147.189 1.00 38.63  ? 604  LEU B C   1 
ATOM   8239  O  O   . LEU B 1 629 ? 109.236 133.586 147.421 1.00 48.96  ? 604  LEU B O   1 
ATOM   8240  C  CB  . LEU B 1 629 ? 111.993 133.462 145.570 1.00 27.40  ? 604  LEU B CB  1 
ATOM   8241  C  CG  . LEU B 1 629 ? 110.919 134.098 144.683 1.00 29.11  ? 604  LEU B CG  1 
ATOM   8242  C  CD1 . LEU B 1 629 ? 110.698 135.549 145.075 1.00 32.34  ? 604  LEU B CD1 1 
ATOM   8243  C  CD2 . LEU B 1 629 ? 111.256 133.988 143.212 1.00 33.12  ? 604  LEU B CD2 1 
ATOM   8244  N  N   . VAL B 1 630 ? 110.072 131.532 147.035 1.00 37.42  ? 605  VAL B N   1 
ATOM   8245  C  CA  . VAL B 1 630 ? 108.755 130.898 147.154 1.00 25.14  ? 605  VAL B CA  1 
ATOM   8246  C  C   . VAL B 1 630 ? 108.093 131.203 148.490 1.00 36.27  ? 605  VAL B C   1 
ATOM   8247  O  O   . VAL B 1 630 ? 106.882 131.471 148.505 1.00 46.88  ? 605  VAL B O   1 
ATOM   8248  C  CB  . VAL B 1 630 ? 108.861 129.396 146.856 1.00 25.90  ? 605  VAL B CB  1 
ATOM   8249  C  CG1 . VAL B 1 630 ? 107.742 128.635 147.537 1.00 37.62  ? 605  VAL B CG1 1 
ATOM   8250  C  CG2 . VAL B 1 630 ? 108.821 129.158 145.358 1.00 33.03  ? 605  VAL B CG2 1 
ATOM   8251  N  N   . PRO B 1 631 ? 108.790 131.189 149.634 1.00 34.88  ? 606  PRO B N   1 
ATOM   8252  C  CA  . PRO B 1 631 ? 108.128 131.616 150.878 1.00 35.30  ? 606  PRO B CA  1 
ATOM   8253  C  C   . PRO B 1 631 ? 107.586 133.034 150.827 1.00 38.99  ? 606  PRO B C   1 
ATOM   8254  O  O   . PRO B 1 631 ? 106.619 133.340 151.536 1.00 48.09  ? 606  PRO B O   1 
ATOM   8255  C  CB  . PRO B 1 631 ? 109.240 131.476 151.924 1.00 34.12  ? 606  PRO B CB  1 
ATOM   8256  C  CG  . PRO B 1 631 ? 110.072 130.372 151.410 1.00 37.02  ? 606  PRO B CG  1 
ATOM   8257  C  CD  . PRO B 1 631 ? 110.088 130.548 149.917 1.00 39.01  ? 606  PRO B CD  1 
ATOM   8258  N  N   . HIS B 1 632 ? 108.173 133.913 150.013 1.00 29.92  ? 607  HIS B N   1 
ATOM   8259  C  CA  . HIS B 1 632 ? 107.643 135.263 149.869 1.00 38.14  ? 607  HIS B CA  1 
ATOM   8260  C  C   . HIS B 1 632 ? 106.359 135.306 149.053 1.00 35.78  ? 607  HIS B C   1 
ATOM   8261  O  O   . HIS B 1 632 ? 105.591 136.265 149.184 1.00 40.94  ? 607  HIS B O   1 
ATOM   8262  C  CB  . HIS B 1 632 ? 108.683 136.178 149.220 1.00 35.65  ? 607  HIS B CB  1 
ATOM   8263  C  CG  . HIS B 1 632 ? 109.831 136.524 150.116 1.00 38.16  ? 607  HIS B CG  1 
ATOM   8264  N  ND1 . HIS B 1 632 ? 110.982 137.123 149.652 1.00 37.10  ? 607  HIS B ND1 1 
ATOM   8265  C  CD2 . HIS B 1 632 ? 110.004 136.356 151.448 1.00 39.42  ? 607  HIS B CD2 1 
ATOM   8266  C  CE1 . HIS B 1 632 ? 111.816 137.309 150.659 1.00 38.02  ? 607  HIS B CE1 1 
ATOM   8267  N  NE2 . HIS B 1 632 ? 111.247 136.852 151.760 1.00 45.72  ? 607  HIS B NE2 1 
ATOM   8268  N  N   . LEU B 1 633 ? 106.107 134.300 148.223 1.00 25.25  ? 608  LEU B N   1 
ATOM   8269  C  CA  . LEU B 1 633 ? 104.911 134.276 147.392 1.00 27.27  ? 608  LEU B CA  1 
ATOM   8270  C  C   . LEU B 1 633 ? 103.811 133.438 148.035 1.00 36.74  ? 608  LEU B C   1 
ATOM   8271  O  O   . LEU B 1 633 ? 104.071 132.639 148.935 1.00 38.66  ? 608  LEU B O   1 
ATOM   8272  C  CB  . LEU B 1 633 ? 105.236 133.737 145.997 1.00 21.62  ? 608  LEU B CB  1 
ATOM   8273  C  CG  . LEU B 1 633 ? 106.383 134.411 145.243 1.00 15.81  ? 608  LEU B CG  1 
ATOM   8274  C  CD1 . LEU B 1 633 ? 106.382 133.990 143.785 1.00 16.79  ? 608  LEU B CD1 1 
ATOM   8275  C  CD2 . LEU B 1 633 ? 106.291 135.921 145.361 1.00 31.55  ? 608  LEU B CD2 1 
ATOM   8276  N  N   . ALA C 2 106 ? 94.466  141.347 74.125  1.00 118.37 ? 83   ALA C N   1 
ATOM   8277  C  CA  . ALA C 2 106 ? 95.167  142.171 73.147  1.00 118.36 ? 83   ALA C CA  1 
ATOM   8278  C  C   . ALA C 2 106 ? 96.641  141.790 73.068  1.00 119.07 ? 83   ALA C C   1 
ATOM   8279  O  O   . ALA C 2 106 ? 97.151  141.462 71.996  1.00 119.22 ? 83   ALA C O   1 
ATOM   8280  C  CB  . ALA C 2 106 ? 95.017  143.644 73.491  1.00 115.73 ? 83   ALA C CB  1 
ATOM   8281  N  N   . GLY C 2 107 ? 97.322  141.833 74.210  1.00 115.15 ? 84   GLY C N   1 
ATOM   8282  C  CA  . GLY C 2 107 ? 98.731  141.499 74.267  1.00 112.84 ? 84   GLY C CA  1 
ATOM   8283  C  C   . GLY C 2 107 ? 98.986  140.007 74.308  1.00 113.80 ? 84   GLY C C   1 
ATOM   8284  O  O   . GLY C 2 107 ? 98.327  139.239 73.600  1.00 114.05 ? 84   GLY C O   1 
ATOM   8285  N  N   . THR C 2 108 ? 99.942  139.584 75.133  1.00 121.78 ? 85   THR C N   1 
ATOM   8286  C  CA  . THR C 2 108 ? 100.266 138.167 75.264  1.00 122.54 ? 85   THR C CA  1 
ATOM   8287  C  C   . THR C 2 108 ? 99.119  137.452 75.966  1.00 122.62 ? 85   THR C C   1 
ATOM   8288  O  O   . THR C 2 108 ? 98.794  137.763 77.117  1.00 121.91 ? 85   THR C O   1 
ATOM   8289  C  CB  . THR C 2 108 ? 101.572 137.991 76.032  1.00 121.27 ? 85   THR C CB  1 
ATOM   8290  O  OG1 . THR C 2 108 ? 102.595 138.795 75.430  1.00 119.97 ? 85   THR C OG1 1 
ATOM   8291  C  CG2 . THR C 2 108 ? 102.006 136.533 76.014  1.00 120.71 ? 85   THR C CG2 1 
ATOM   8292  N  N   . THR C 2 109 ? 98.504  136.496 75.277  1.00 130.55 ? 86   THR C N   1 
ATOM   8293  C  CA  . THR C 2 109 ? 97.332  135.788 75.774  1.00 130.15 ? 86   THR C CA  1 
ATOM   8294  C  C   . THR C 2 109 ? 97.671  134.320 75.989  1.00 130.07 ? 86   THR C C   1 
ATOM   8295  O  O   . THR C 2 109 ? 98.274  133.684 75.118  1.00 130.15 ? 86   THR C O   1 
ATOM   8296  C  CB  . THR C 2 109 ? 96.160  135.920 74.799  1.00 129.43 ? 86   THR C CB  1 
ATOM   8297  O  OG1 . THR C 2 109 ? 95.864  137.307 74.589  1.00 127.82 ? 86   THR C OG1 1 
ATOM   8298  C  CG2 . THR C 2 109 ? 94.924  135.223 75.349  1.00 128.69 ? 86   THR C CG2 1 
ATOM   8299  N  N   . TYR C 2 110 ? 97.284  133.790 77.146  1.00 135.35 ? 87   TYR C N   1 
ATOM   8300  C  CA  . TYR C 2 110 ? 97.480  132.387 77.480  1.00 136.35 ? 87   TYR C CA  1 
ATOM   8301  C  C   . TYR C 2 110 ? 96.126  131.696 77.559  1.00 136.31 ? 87   TYR C C   1 
ATOM   8302  O  O   . TYR C 2 110 ? 95.221  132.173 78.253  1.00 135.65 ? 87   TYR C O   1 
ATOM   8303  C  CB  . TYR C 2 110 ? 98.237  132.237 78.802  1.00 135.23 ? 87   TYR C CB  1 
ATOM   8304  C  CG  . TYR C 2 110 ? 99.737  132.339 78.653  1.00 135.42 ? 87   TYR C CG  1 
ATOM   8305  C  CD1 . TYR C 2 110 ? 100.371 133.574 78.642  1.00 135.10 ? 87   TYR C CD1 1 
ATOM   8306  C  CD2 . TYR C 2 110 ? 100.518 131.200 78.516  1.00 135.25 ? 87   TYR C CD2 1 
ATOM   8307  C  CE1 . TYR C 2 110 ? 101.742 133.670 78.503  1.00 135.71 ? 87   TYR C CE1 1 
ATOM   8308  C  CE2 . TYR C 2 110 ? 101.889 131.287 78.376  1.00 135.67 ? 87   TYR C CE2 1 
ATOM   8309  C  CZ  . TYR C 2 110 ? 102.496 132.524 78.371  1.00 135.93 ? 87   TYR C CZ  1 
ATOM   8310  O  OH  . TYR C 2 110 ? 103.861 132.613 78.231  1.00 134.98 ? 87   TYR C OH  1 
ATOM   8311  N  N   . ILE C 2 111 ? 95.993  130.580 76.851  1.00 144.20 ? 88   ILE C N   1 
ATOM   8312  C  CA  . ILE C 2 111 ? 94.739  129.851 76.776  1.00 144.59 ? 88   ILE C CA  1 
ATOM   8313  C  C   . ILE C 2 111 ? 94.791  128.668 77.733  1.00 144.49 ? 88   ILE C C   1 
ATOM   8314  O  O   . ILE C 2 111 ? 95.860  128.185 78.119  1.00 144.05 ? 88   ILE C O   1 
ATOM   8315  C  CB  . ILE C 2 111 ? 94.433  129.390 75.331  1.00 144.63 ? 88   ILE C CB  1 
ATOM   8316  C  CG1 . ILE C 2 111 ? 92.930  129.180 75.134  1.00 144.01 ? 88   ILE C CG1 1 
ATOM   8317  C  CG2 . ILE C 2 111 ? 95.192  128.118 74.998  1.00 144.74 ? 88   ILE C CG2 1 
ATOM   8318  C  CD1 . ILE C 2 111 ? 92.098  130.383 75.484  1.00 143.14 ? 88   ILE C CD1 1 
ATOM   8319  N  N   . PHE C 2 112 ? 93.613  128.201 78.133  1.00 139.39 ? 89   PHE C N   1 
ATOM   8320  C  CA  . PHE C 2 112 ? 93.469  127.058 79.023  1.00 139.02 ? 89   PHE C CA  1 
ATOM   8321  C  C   . PHE C 2 112 ? 92.791  125.922 78.270  1.00 139.19 ? 89   PHE C C   1 
ATOM   8322  O  O   . PHE C 2 112 ? 91.704  126.104 77.712  1.00 138.78 ? 89   PHE C O   1 
ATOM   8323  C  CB  . PHE C 2 112 ? 92.655  127.429 80.265  1.00 139.95 ? 89   PHE C CB  1 
ATOM   8324  C  CG  . PHE C 2 112 ? 93.363  128.373 81.197  1.00 140.54 ? 89   PHE C CG  1 
ATOM   8325  C  CD1 . PHE C 2 112 ? 93.375  129.735 80.948  1.00 139.14 ? 89   PHE C CD1 1 
ATOM   8326  C  CD2 . PHE C 2 112 ? 94.008  127.898 82.326  1.00 139.79 ? 89   PHE C CD2 1 
ATOM   8327  C  CE1 . PHE C 2 112 ? 94.022  130.605 81.804  1.00 138.15 ? 89   PHE C CE1 1 
ATOM   8328  C  CE2 . PHE C 2 112 ? 94.655  128.764 83.187  1.00 138.83 ? 89   PHE C CE2 1 
ATOM   8329  C  CZ  . PHE C 2 112 ? 94.663  130.119 82.925  1.00 138.04 ? 89   PHE C CZ  1 
ATOM   8330  N  N   . SER C 2 113 ? 93.428  124.757 78.261  1.00 144.00 ? 90   SER C N   1 
ATOM   8331  C  CA  . SER C 2 113 ? 92.919  123.592 77.558  1.00 144.74 ? 90   SER C CA  1 
ATOM   8332  C  C   . SER C 2 113 ? 92.106  122.723 78.516  1.00 144.09 ? 90   SER C C   1 
ATOM   8333  O  O   . SER C 2 113 ? 91.784  123.127 79.638  1.00 143.20 ? 90   SER C O   1 
ATOM   8334  C  CB  . SER C 2 113 ? 94.074  122.816 76.922  1.00 143.65 ? 90   SER C CB  1 
ATOM   8335  O  OG  . SER C 2 113 ? 93.633  121.567 76.419  1.00 142.77 ? 90   SER C OG  1 
ATOM   8336  N  N   . LYS C 2 114 ? 91.760  121.518 78.066  1.00 145.18 ? 91   LYS C N   1 
ATOM   8337  C  CA  . LYS C 2 114 ? 90.974  120.609 78.888  1.00 145.51 ? 91   LYS C CA  1 
ATOM   8338  C  C   . LYS C 2 114 ? 91.742  120.227 80.148  1.00 145.04 ? 91   LYS C C   1 
ATOM   8339  O  O   . LYS C 2 114 ? 92.969  120.096 80.135  1.00 145.14 ? 91   LYS C O   1 
ATOM   8340  C  CB  . LYS C 2 114 ? 90.609  119.355 78.093  1.00 144.72 ? 91   LYS C CB  1 
ATOM   8341  C  CG  . LYS C 2 114 ? 91.771  118.735 77.336  1.00 144.20 ? 91   LYS C CG  1 
ATOM   8342  C  CD  . LYS C 2 114 ? 91.320  117.527 76.529  1.00 143.68 ? 91   LYS C CD  1 
ATOM   8343  C  CE  . LYS C 2 114 ? 92.447  116.986 75.665  1.00 144.12 ? 91   LYS C CE  1 
ATOM   8344  N  NZ  . LYS C 2 114 ? 93.574  116.462 76.485  1.00 143.80 ? 91   LYS C NZ  1 
ATOM   8345  N  N   . GLY C 2 115 ? 91.008  120.050 81.243  1.00 136.43 ? 92   GLY C N   1 
ATOM   8346  C  CA  . GLY C 2 115 ? 91.620  119.776 82.526  1.00 135.91 ? 92   GLY C CA  1 
ATOM   8347  C  C   . GLY C 2 115 ? 91.901  121.042 83.307  1.00 136.43 ? 92   GLY C C   1 
ATOM   8348  O  O   . GLY C 2 115 ? 91.294  121.280 84.355  1.00 136.37 ? 92   GLY C O   1 
ATOM   8349  N  N   . GLY C 2 116 ? 92.816  121.861 82.807  1.00 139.80 ? 93   GLY C N   1 
ATOM   8350  C  CA  . GLY C 2 116 ? 93.142  123.128 83.418  1.00 140.04 ? 93   GLY C CA  1 
ATOM   8351  C  C   . GLY C 2 116 ? 94.635  123.362 83.400  1.00 140.56 ? 93   GLY C C   1 
ATOM   8352  O  O   . GLY C 2 116 ? 95.398  122.618 82.785  1.00 139.67 ? 93   GLY C O   1 
ATOM   8353  N  N   . GLY C 2 117 ? 95.051  124.418 84.090  1.00 144.64 ? 94   GLY C N   1 
ATOM   8354  C  CA  . GLY C 2 117 ? 96.457  124.768 84.171  1.00 143.55 ? 94   GLY C CA  1 
ATOM   8355  C  C   . GLY C 2 117 ? 96.650  125.931 85.116  1.00 144.05 ? 94   GLY C C   1 
ATOM   8356  O  O   . GLY C 2 117 ? 95.688  126.544 85.588  1.00 143.89 ? 94   GLY C O   1 
ATOM   8357  N  N   . GLN C 2 118 ? 97.919  126.231 85.384  1.00 138.36 ? 95   GLN C N   1 
ATOM   8358  C  CA  . GLN C 2 118 ? 98.268  127.276 86.333  1.00 137.06 ? 95   GLN C CA  1 
ATOM   8359  C  C   . GLN C 2 118 ? 99.579  127.931 85.930  1.00 136.90 ? 95   GLN C C   1 
ATOM   8360  O  O   . GLN C 2 118 ? 100.489 127.271 85.414  1.00 136.03 ? 95   GLN C O   1 
ATOM   8361  C  CB  . GLN C 2 118 ? 98.385  126.722 87.758  1.00 136.36 ? 95   GLN C CB  1 
ATOM   8362  C  CG  . GLN C 2 118 ? 97.076  126.692 88.522  1.00 135.89 ? 95   GLN C CG  1 
ATOM   8363  C  CD  . GLN C 2 118 ? 97.274  126.417 89.998  1.00 137.50 ? 95   GLN C CD  1 
ATOM   8364  O  OE1 . GLN C 2 118 ? 96.633  127.035 90.848  1.00 138.04 ? 95   GLN C OE1 1 
ATOM   8365  N  NE2 . GLN C 2 118 ? 98.168  125.487 90.311  1.00 137.23 ? 95   GLN C NE2 1 
ATOM   8366  N  N   . ILE C 2 119 ? 99.658  129.237 86.172  1.00 134.76 ? 96   ILE C N   1 
ATOM   8367  C  CA  . ILE C 2 119 ? 100.880 130.015 86.014  1.00 135.04 ? 96   ILE C CA  1 
ATOM   8368  C  C   . ILE C 2 119 ? 101.232 130.594 87.377  1.00 134.36 ? 96   ILE C C   1 
ATOM   8369  O  O   . ILE C 2 119 ? 100.427 131.316 87.978  1.00 133.55 ? 96   ILE C O   1 
ATOM   8370  C  CB  . ILE C 2 119 ? 100.724 131.129 84.967  1.00 133.25 ? 96   ILE C CB  1 
ATOM   8371  C  CG1 . ILE C 2 119 ? 100.379 130.533 83.601  1.00 133.11 ? 96   ILE C CG1 1 
ATOM   8372  C  CG2 . ILE C 2 119 ? 101.993 131.961 84.883  1.00 132.82 ? 96   ILE C CG2 1 
ATOM   8373  C  CD1 . ILE C 2 119 ? 98.934  130.725 83.200  1.00 133.26 ? 96   ILE C CD1 1 
ATOM   8374  N  N   . THR C 2 120 ? 102.428 130.283 87.862  1.00 124.43 ? 97   THR C N   1 
ATOM   8375  C  CA  . THR C 2 120 ? 102.865 130.678 89.192  1.00 123.22 ? 97   THR C CA  1 
ATOM   8376  C  C   . THR C 2 120 ? 104.084 131.579 89.081  1.00 122.54 ? 97   THR C C   1 
ATOM   8377  O  O   . THR C 2 120 ? 105.069 131.219 88.427  1.00 122.14 ? 97   THR C O   1 
ATOM   8378  C  CB  . THR C 2 120 ? 103.198 129.453 90.050  1.00 123.64 ? 97   THR C CB  1 
ATOM   8379  O  OG1 . THR C 2 120 ? 102.029 128.638 90.199  1.00 122.81 ? 97   THR C OG1 1 
ATOM   8380  C  CG2 . THR C 2 120 ? 103.694 129.880 91.423  1.00 122.96 ? 97   THR C CG2 1 
ATOM   8381  N  N   . TYR C 2 121 ? 104.016 132.744 89.717  1.00 111.75 ? 98   TYR C N   1 
ATOM   8382  C  CA  . TYR C 2 121 ? 105.165 133.630 89.843  1.00 110.21 ? 98   TYR C CA  1 
ATOM   8383  C  C   . TYR C 2 121 ? 105.627 133.604 91.292  1.00 109.26 ? 98   TYR C C   1 
ATOM   8384  O  O   . TYR C 2 121 ? 104.838 133.883 92.205  1.00 109.02 ? 98   TYR C O   1 
ATOM   8385  C  CB  . TYR C 2 121 ? 104.831 135.056 89.407  1.00 108.55 ? 98   TYR C CB  1 
ATOM   8386  C  CG  . TYR C 2 121 ? 105.985 136.033 89.509  1.00 108.78 ? 98   TYR C CG  1 
ATOM   8387  C  CD1 . TYR C 2 121 ? 107.301 135.605 89.403  1.00 109.50 ? 98   TYR C CD1 1 
ATOM   8388  C  CD2 . TYR C 2 121 ? 105.757 137.383 89.725  1.00 108.89 ? 98   TYR C CD2 1 
ATOM   8389  C  CE1 . TYR C 2 121 ? 108.351 136.496 89.499  1.00 109.84 ? 98   TYR C CE1 1 
ATOM   8390  C  CE2 . TYR C 2 121 ? 106.804 138.276 89.824  1.00 108.67 ? 98   TYR C CE2 1 
ATOM   8391  C  CZ  . TYR C 2 121 ? 108.097 137.829 89.709  1.00 108.67 ? 98   TYR C CZ  1 
ATOM   8392  O  OH  . TYR C 2 121 ? 109.140 138.719 89.806  1.00 108.69 ? 98   TYR C OH  1 
ATOM   8393  N  N   . LYS C 2 122 ? 106.898 133.265 91.488  1.00 104.42 ? 99   LYS C N   1 
ATOM   8394  C  CA  . LYS C 2 122 ? 107.536 133.206 92.794  1.00 103.72 ? 99   LYS C CA  1 
ATOM   8395  C  C   . LYS C 2 122 ? 108.503 134.376 92.904  1.00 103.57 ? 99   LYS C C   1 
ATOM   8396  O  O   . LYS C 2 122 ? 109.401 134.522 92.067  1.00 103.55 ? 99   LYS C O   1 
ATOM   8397  C  CB  . LYS C 2 122 ? 108.281 131.883 92.975  1.00 103.76 ? 99   LYS C CB  1 
ATOM   8398  C  CG  . LYS C 2 122 ? 107.392 130.660 93.127  1.00 104.81 ? 99   LYS C CG  1 
ATOM   8399  C  CD  . LYS C 2 122 ? 106.794 130.582 94.517  1.00 103.87 ? 99   LYS C CD  1 
ATOM   8400  C  CE  . LYS C 2 122 ? 106.925 129.184 95.100  1.00 104.06 ? 99   LYS C CE  1 
ATOM   8401  N  NZ  . LYS C 2 122 ? 106.025 128.989 96.269  1.00 103.23 ? 99   LYS C NZ  1 
ATOM   8402  N  N   . TRP C 2 123 ? 108.321 135.204 93.927  1.00 97.70  ? 100  TRP C N   1 
ATOM   8403  C  CA  . TRP C 2 123 ? 109.220 136.325 94.134  1.00 96.79  ? 100  TRP C CA  1 
ATOM   8404  C  C   . TRP C 2 123 ? 110.571 135.834 94.656  1.00 97.51  ? 100  TRP C C   1 
ATOM   8405  O  O   . TRP C 2 123 ? 110.659 134.760 95.258  1.00 95.30  ? 100  TRP C O   1 
ATOM   8406  C  CB  . TRP C 2 123 ? 108.615 137.326 95.113  1.00 95.46  ? 100  TRP C CB  1 
ATOM   8407  C  CG  . TRP C 2 123 ? 107.934 138.477 94.445  1.00 93.44  ? 100  TRP C CG  1 
ATOM   8408  C  CD1 . TRP C 2 123 ? 108.531 139.564 93.878  1.00 93.65  ? 100  TRP C CD1 1 
ATOM   8409  C  CD2 . TRP C 2 123 ? 106.524 138.660 94.276  1.00 93.59  ? 100  TRP C CD2 1 
ATOM   8410  N  NE1 . TRP C 2 123 ? 107.581 140.413 93.365  1.00 95.52  ? 100  TRP C NE1 1 
ATOM   8411  C  CE2 . TRP C 2 123 ? 106.340 139.880 93.597  1.00 93.87  ? 100  TRP C CE2 1 
ATOM   8412  C  CE3 . TRP C 2 123 ? 105.399 137.912 94.631  1.00 94.15  ? 100  TRP C CE3 1 
ATOM   8413  C  CZ2 . TRP C 2 123 ? 105.079 140.368 93.266  1.00 93.48  ? 100  TRP C CZ2 1 
ATOM   8414  C  CZ3 . TRP C 2 123 ? 104.149 138.397 94.302  1.00 94.08  ? 100  TRP C CZ3 1 
ATOM   8415  C  CH2 . TRP C 2 123 ? 103.999 139.613 93.627  1.00 94.58  ? 100  TRP C CH2 1 
ATOM   8416  N  N   . PRO C 2 124 ? 111.639 136.594 94.420  1.00 106.60 ? 101  PRO C N   1 
ATOM   8417  C  CA  . PRO C 2 124 ? 112.934 136.218 94.978  1.00 105.17 ? 101  PRO C CA  1 
ATOM   8418  C  C   . PRO C 2 124 ? 112.864 136.148 96.487  1.00 105.27 ? 101  PRO C C   1 
ATOM   8419  O  O   . PRO C 2 124 ? 112.085 136.880 97.128  1.00 105.79 ? 101  PRO C O   1 
ATOM   8420  C  CB  . PRO C 2 124 ? 113.866 137.345 94.509  1.00 104.59 ? 101  PRO C CB  1 
ATOM   8421  C  CG  . PRO C 2 124 ? 113.149 138.079 93.440  1.00 105.65 ? 101  PRO C CG  1 
ATOM   8422  C  CD  . PRO C 2 124 ? 111.740 137.605 93.354  1.00 105.59 ? 101  PRO C CD  1 
ATOM   8423  N  N   . PRO C 2 125 ? 113.653 135.265 97.107  1.00 108.43 ? 102  PRO C N   1 
ATOM   8424  C  CA  . PRO C 2 125 ? 113.547 135.078 98.564  1.00 107.80 ? 102  PRO C CA  1 
ATOM   8425  C  C   . PRO C 2 125 ? 113.803 136.339 99.370  1.00 104.91 ? 102  PRO C C   1 
ATOM   8426  O  O   . PRO C 2 125 ? 113.207 136.506 100.441 1.00 104.20 ? 102  PRO C O   1 
ATOM   8427  C  CB  . PRO C 2 125 ? 114.604 134.002 98.853  1.00 108.29 ? 102  PRO C CB  1 
ATOM   8428  C  CG  . PRO C 2 125 ? 114.787 133.289 97.551  1.00 108.66 ? 102  PRO C CG  1 
ATOM   8429  C  CD  . PRO C 2 125 ? 114.622 134.339 96.497  1.00 108.27 ? 102  PRO C CD  1 
ATOM   8430  N  N   . ASN C 2 126 ? 114.670 137.232 98.894  1.00 108.28 ? 103  ASN C N   1 
ATOM   8431  C  CA  . ASN C 2 126 ? 115.001 138.456 99.611  1.00 110.13 ? 103  ASN C CA  1 
ATOM   8432  C  C   . ASN C 2 126 ? 114.439 139.700 98.932  1.00 109.60 ? 103  ASN C C   1 
ATOM   8433  O  O   . ASN C 2 126 ? 114.885 140.814 99.222  1.00 107.80 ? 103  ASN C O   1 
ATOM   8434  C  CB  . ASN C 2 126 ? 116.516 138.582 99.772  1.00 109.59 ? 103  ASN C CB  1 
ATOM   8435  C  CG  . ASN C 2 126 ? 117.163 137.289 100.226 1.00 110.28 ? 103  ASN C CG  1 
ATOM   8436  O  OD1 . ASN C 2 126 ? 117.233 137.003 101.421 1.00 109.75 ? 103  ASN C OD1 1 
ATOM   8437  N  ND2 . ASN C 2 126 ? 117.643 136.499 99.271  1.00 109.82 ? 103  ASN C ND2 1 
ATOM   8438  N  N   . ASP C 2 127 ? 113.469 139.536 98.035  1.00 106.60 ? 104  ASP C N   1 
ATOM   8439  C  CA  . ASP C 2 127 ? 112.907 140.659 97.293  1.00 106.88 ? 104  ASP C CA  1 
ATOM   8440  C  C   . ASP C 2 127 ? 111.389 140.557 97.230  1.00 105.78 ? 104  ASP C C   1 
ATOM   8441  O  O   . ASP C 2 127 ? 110.774 140.817 96.191  1.00 105.59 ? 104  ASP C O   1 
ATOM   8442  C  CB  . ASP C 2 127 ? 113.499 140.741 95.887  1.00 107.81 ? 104  ASP C CB  1 
ATOM   8443  C  CG  . ASP C 2 127 ? 113.415 142.134 95.300  1.00 108.59 ? 104  ASP C CG  1 
ATOM   8444  O  OD1 . ASP C 2 127 ? 113.327 143.105 96.080  1.00 110.43 ? 104  ASP C OD1 1 
ATOM   8445  O  OD2 . ASP C 2 127 ? 113.435 142.259 94.057  1.00 106.73 ? 104  ASP C OD2 1 
ATOM   8446  N  N   . ARG C 2 128 ? 110.762 140.174 98.340  1.00 90.03  ? 105  ARG C N   1 
ATOM   8447  C  CA  . ARG C 2 128 ? 109.308 140.142 98.414  1.00 87.69  ? 105  ARG C CA  1 
ATOM   8448  C  C   . ARG C 2 128 ? 108.798 141.485 98.915  1.00 89.00  ? 105  ARG C C   1 
ATOM   8449  O  O   . ARG C 2 128 ? 109.149 141.889 100.031 1.00 92.50  ? 105  ARG C O   1 
ATOM   8450  C  CB  . ARG C 2 128 ? 108.836 139.030 99.335  1.00 87.63  ? 105  ARG C CB  1 
ATOM   8451  C  CG  . ARG C 2 128 ? 109.334 137.648 98.954  1.00 91.53  ? 105  ARG C CG  1 
ATOM   8452  C  CD  . ARG C 2 128 ? 108.744 136.589 99.870  1.00 90.92  ? 105  ARG C CD  1 
ATOM   8453  N  NE  . ARG C 2 128 ? 109.429 135.308 99.748  1.00 93.75  ? 105  ARG C NE  1 
ATOM   8454  C  CZ  . ARG C 2 128 ? 110.455 134.933 100.499 1.00 93.18  ? 105  ARG C CZ  1 
ATOM   8455  N  NH1 . ARG C 2 128 ? 110.947 135.721 101.440 1.00 91.27  ? 105  ARG C NH1 1 
ATOM   8456  N  NH2 . ARG C 2 128 ? 110.999 133.736 100.302 1.00 92.17  ? 105  ARG C NH2 1 
ATOM   8457  N  N   . PRO C 2 129 ? 107.986 142.201 98.144  1.00 73.44  ? 106  PRO C N   1 
ATOM   8458  C  CA  . PRO C 2 129 ? 107.537 143.530 98.563  1.00 72.89  ? 106  PRO C CA  1 
ATOM   8459  C  C   . PRO C 2 129 ? 106.233 143.504 99.343  1.00 73.15  ? 106  PRO C C   1 
ATOM   8460  O  O   . PRO C 2 129 ? 105.343 142.684 99.110  1.00 73.01  ? 106  PRO C O   1 
ATOM   8461  C  CB  . PRO C 2 129 ? 107.352 144.254 97.223  1.00 71.34  ? 106  PRO C CB  1 
ATOM   8462  C  CG  . PRO C 2 129 ? 106.915 143.170 96.291  1.00 72.74  ? 106  PRO C CG  1 
ATOM   8463  C  CD  . PRO C 2 129 ? 107.536 141.875 96.779  1.00 76.77  ? 106  PRO C CD  1 
ATOM   8464  N  N   . SER C 2 130 ? 106.137 144.434 100.288 1.00 60.35  ? 107  SER C N   1 
ATOM   8465  C  CA  . SER C 2 130 ? 104.915 144.686 101.040 1.00 51.97  ? 107  SER C CA  1 
ATOM   8466  C  C   . SER C 2 130 ? 104.406 146.068 100.658 1.00 57.02  ? 107  SER C C   1 
ATOM   8467  O  O   . SER C 2 130 ? 105.142 147.054 100.770 1.00 65.42  ? 107  SER C O   1 
ATOM   8468  C  CB  . SER C 2 130 ? 105.165 144.594 102.544 1.00 52.90  ? 107  SER C CB  1 
ATOM   8469  O  OG  . SER C 2 130 ? 106.044 143.526 102.846 1.00 63.22  ? 107  SER C OG  1 
ATOM   8470  N  N   . THR C 2 131 ? 103.158 146.139 100.208 1.00 60.09  ? 108  THR C N   1 
ATOM   8471  C  CA  . THR C 2 131 ? 102.602 147.356 99.636  1.00 60.44  ? 108  THR C CA  1 
ATOM   8472  C  C   . THR C 2 131 ? 101.352 147.782 100.391 1.00 60.82  ? 108  THR C C   1 
ATOM   8473  O  O   . THR C 2 131 ? 100.492 146.954 100.708 1.00 64.58  ? 108  THR C O   1 
ATOM   8474  C  CB  . THR C 2 131 ? 102.263 147.159 98.155  1.00 67.67  ? 108  THR C CB  1 
ATOM   8475  O  OG1 . THR C 2 131 ? 101.286 146.120 98.023  1.00 68.97  ? 108  THR C OG1 1 
ATOM   8476  C  CG2 . THR C 2 131 ? 103.508 146.780 97.368  1.00 68.58  ? 108  THR C CG2 1 
ATOM   8477  N  N   . ARG C 2 132 ? 101.257 149.082 100.673 1.00 61.70  ? 109  ARG C N   1 
ATOM   8478  C  CA  . ARG C 2 132 ? 100.051 149.629 101.284 1.00 61.35  ? 109  ARG C CA  1 
ATOM   8479  C  C   . ARG C 2 132 ? 98.924  149.754 100.267 1.00 68.05  ? 109  ARG C C   1 
ATOM   8480  O  O   . ARG C 2 132 ? 97.753  149.550 100.605 1.00 71.64  ? 109  ARG C O   1 
ATOM   8481  C  CB  . ARG C 2 132 ? 100.353 150.989 101.916 1.00 62.57  ? 109  ARG C CB  1 
ATOM   8482  C  CG  . ARG C 2 132 ? 99.143  151.678 102.527 1.00 62.91  ? 109  ARG C CG  1 
ATOM   8483  C  CD  . ARG C 2 132 ? 99.542  152.915 103.318 1.00 64.05  ? 109  ARG C CD  1 
ATOM   8484  N  NE  . ARG C 2 132 ? 100.771 152.714 104.077 1.00 67.25  ? 109  ARG C NE  1 
ATOM   8485  C  CZ  . ARG C 2 132 ? 100.831 152.637 105.400 1.00 68.05  ? 109  ARG C CZ  1 
ATOM   8486  N  NH1 . ARG C 2 132 ? 99.744  152.736 106.148 1.00 67.29  ? 109  ARG C NH1 1 
ATOM   8487  N  NH2 . ARG C 2 132 ? 102.011 152.456 105.986 1.00 66.73  ? 109  ARG C NH2 1 
ATOM   8488  N  N   . ALA C 2 133 ? 99.259  150.078 99.020  1.00 81.80  ? 110  ALA C N   1 
ATOM   8489  C  CA  . ALA C 2 133 ? 98.288  150.219 97.945  1.00 79.48  ? 110  ALA C CA  1 
ATOM   8490  C  C   . ALA C 2 133 ? 98.639  149.265 96.812  1.00 80.02  ? 110  ALA C C   1 
ATOM   8491  O  O   . ALA C 2 133 ? 99.818  149.033 96.526  1.00 80.73  ? 110  ALA C O   1 
ATOM   8492  C  CB  . ALA C 2 133 ? 98.242  151.658 97.425  1.00 79.59  ? 110  ALA C CB  1 
ATOM   8493  N  N   . ASP C 2 134 ? 97.611  148.718 96.168  1.00 93.02  ? 111  ASP C N   1 
ATOM   8494  C  CA  . ASP C 2 134 ? 97.784  147.704 95.138  1.00 93.73  ? 111  ASP C CA  1 
ATOM   8495  C  C   . ASP C 2 134 ? 96.950  148.032 93.909  1.00 96.26  ? 111  ASP C C   1 
ATOM   8496  O  O   . ASP C 2 134 ? 95.891  148.660 94.001  1.00 96.84  ? 111  ASP C O   1 
ATOM   8497  C  CB  . ASP C 2 134 ? 97.397  146.307 95.648  1.00 94.51  ? 111  ASP C CB  1 
ATOM   8498  C  CG  . ASP C 2 134 ? 98.062  145.959 96.963  1.00 96.91  ? 111  ASP C CG  1 
ATOM   8499  O  OD1 . ASP C 2 134 ? 99.252  146.293 97.136  1.00 98.85  ? 111  ASP C OD1 1 
ATOM   8500  O  OD2 . ASP C 2 134 ? 97.395  145.347 97.822  1.00 95.03  ? 111  ASP C OD2 1 
ATOM   8501  N  N   . ARG C 2 135 ? 97.441  147.585 92.754  1.00 112.68 ? 112  ARG C N   1 
ATOM   8502  C  CA  . ARG C 2 135 ? 96.744  147.705 91.481  1.00 112.75 ? 112  ARG C CA  1 
ATOM   8503  C  C   . ARG C 2 135 ? 96.678  146.335 90.823  1.00 114.36 ? 112  ARG C C   1 
ATOM   8504  O  O   . ARG C 2 135 ? 97.636  145.560 90.895  1.00 116.04 ? 112  ARG C O   1 
ATOM   8505  C  CB  . ARG C 2 135 ? 97.447  148.696 90.550  1.00 113.39 ? 112  ARG C CB  1 
ATOM   8506  C  CG  . ARG C 2 135 ? 97.073  150.146 90.786  1.00 114.29 ? 112  ARG C CG  1 
ATOM   8507  C  CD  . ARG C 2 135 ? 97.931  151.075 89.943  1.00 115.17 ? 112  ARG C CD  1 
ATOM   8508  N  NE  . ARG C 2 135 ? 97.265  152.343 89.672  1.00 115.07 ? 112  ARG C NE  1 
ATOM   8509  C  CZ  . ARG C 2 135 ? 97.126  153.322 90.556  1.00 115.75 ? 112  ARG C CZ  1 
ATOM   8510  N  NH1 . ARG C 2 135 ? 97.604  153.216 91.786  1.00 115.54 ? 112  ARG C NH1 1 
ATOM   8511  N  NH2 . ARG C 2 135 ? 96.494  154.435 90.198  1.00 115.35 ? 112  ARG C NH2 1 
ATOM   8512  N  N   . LEU C 2 136 ? 95.550  146.039 90.180  1.00 117.90 ? 113  LEU C N   1 
ATOM   8513  C  CA  . LEU C 2 136 ? 95.359  144.737 89.546  1.00 117.55 ? 113  LEU C CA  1 
ATOM   8514  C  C   . LEU C 2 136 ? 94.461  144.922 88.332  1.00 118.56 ? 113  LEU C C   1 
ATOM   8515  O  O   . LEU C 2 136 ? 93.253  145.112 88.484  1.00 118.58 ? 113  LEU C O   1 
ATOM   8516  C  CB  . LEU C 2 136 ? 94.753  143.739 90.529  1.00 116.95 ? 113  LEU C CB  1 
ATOM   8517  C  CG  . LEU C 2 136 ? 94.522  142.316 90.022  1.00 117.67 ? 113  LEU C CG  1 
ATOM   8518  C  CD1 . LEU C 2 136 ? 95.841  141.656 89.656  1.00 118.14 ? 113  LEU C CD1 1 
ATOM   8519  C  CD2 . LEU C 2 136 ? 93.775  141.498 91.061  1.00 118.26 ? 113  LEU C CD2 1 
ATOM   8520  N  N   . ALA C 2 137 ? 95.042  144.867 87.137  1.00 126.88 ? 114  ALA C N   1 
ATOM   8521  C  CA  . ALA C 2 137 ? 94.291  145.013 85.899  1.00 127.23 ? 114  ALA C CA  1 
ATOM   8522  C  C   . ALA C 2 137 ? 94.575  143.826 84.992  1.00 128.56 ? 114  ALA C C   1 
ATOM   8523  O  O   . ALA C 2 137 ? 95.726  143.399 84.860  1.00 129.36 ? 114  ALA C O   1 
ATOM   8524  C  CB  . ALA C 2 137 ? 94.645  146.320 85.180  1.00 127.11 ? 114  ALA C CB  1 
ATOM   8525  N  N   . ILE C 2 138 ? 93.525  143.297 84.368  1.00 128.94 ? 115  ILE C N   1 
ATOM   8526  C  CA  . ILE C 2 138 ? 93.670  142.125 83.508  1.00 129.35 ? 115  ILE C CA  1 
ATOM   8527  C  C   . ILE C 2 138 ? 92.459  142.044 82.589  1.00 130.39 ? 115  ILE C C   1 
ATOM   8528  O  O   . ILE C 2 138 ? 91.336  142.362 82.990  1.00 130.40 ? 115  ILE C O   1 
ATOM   8529  C  CB  . ILE C 2 138 ? 93.848  140.836 84.348  1.00 127.02 ? 115  ILE C CB  1 
ATOM   8530  C  CG1 . ILE C 2 138 ? 94.048  139.617 83.447  1.00 127.73 ? 115  ILE C CG1 1 
ATOM   8531  C  CG2 . ILE C 2 138 ? 92.667  140.631 85.286  1.00 126.05 ? 115  ILE C CG2 1 
ATOM   8532  C  CD1 . ILE C 2 138 ? 94.320  138.339 84.207  1.00 127.85 ? 115  ILE C CD1 1 
ATOM   8533  N  N   . GLY C 2 139 ? 92.695  141.629 81.349  1.00 134.67 ? 116  GLY C N   1 
ATOM   8534  C  CA  . GLY C 2 139 ? 91.625  141.359 80.404  1.00 133.83 ? 116  GLY C CA  1 
ATOM   8535  C  C   . GLY C 2 139 ? 91.335  139.869 80.359  1.00 132.63 ? 116  GLY C C   1 
ATOM   8536  O  O   . GLY C 2 139 ? 92.250  139.048 80.328  1.00 131.73 ? 116  GLY C O   1 
ATOM   8537  N  N   . PHE C 2 140 ? 90.051  139.532 80.361  1.00 139.59 ? 117  PHE C N   1 
ATOM   8538  C  CA  . PHE C 2 140 ? 89.626  138.143 80.407  1.00 140.57 ? 117  PHE C CA  1 
ATOM   8539  C  C   . PHE C 2 140 ? 88.448  137.930 79.468  1.00 143.06 ? 117  PHE C C   1 
ATOM   8540  O  O   . PHE C 2 140 ? 87.712  138.862 79.128  1.00 142.42 ? 117  PHE C O   1 
ATOM   8541  C  CB  . PHE C 2 140 ? 89.250  137.717 81.833  1.00 139.98 ? 117  PHE C CB  1 
ATOM   8542  C  CG  . PHE C 2 140 ? 87.984  138.342 82.339  1.00 140.60 ? 117  PHE C CG  1 
ATOM   8543  C  CD1 . PHE C 2 140 ? 87.946  139.684 82.681  1.00 140.54 ? 117  PHE C CD1 1 
ATOM   8544  C  CD2 . PHE C 2 140 ? 86.831  137.590 82.474  1.00 140.69 ? 117  PHE C CD2 1 
ATOM   8545  C  CE1 . PHE C 2 140 ? 86.784  140.262 83.146  1.00 140.73 ? 117  PHE C CE1 1 
ATOM   8546  C  CE2 . PHE C 2 140 ? 85.665  138.163 82.939  1.00 141.18 ? 117  PHE C CE2 1 
ATOM   8547  C  CZ  . PHE C 2 140 ? 85.642  139.500 83.276  1.00 141.06 ? 117  PHE C CZ  1 
ATOM   8548  N  N   . SER C 2 141 ? 88.293  136.678 79.043  1.00 146.85 ? 118  SER C N   1 
ATOM   8549  C  CA  . SER C 2 141 ? 87.147  136.274 78.232  1.00 145.71 ? 118  SER C CA  1 
ATOM   8550  C  C   . SER C 2 141 ? 86.901  134.792 78.478  1.00 145.24 ? 118  SER C C   1 
ATOM   8551  O  O   . SER C 2 141 ? 87.742  133.957 78.131  1.00 144.51 ? 118  SER C O   1 
ATOM   8552  C  CB  . SER C 2 141 ? 87.388  136.557 76.752  1.00 145.22 ? 118  SER C CB  1 
ATOM   8553  O  OG  . SER C 2 141 ? 88.490  135.816 76.263  1.00 144.54 ? 118  SER C OG  1 
ATOM   8554  N  N   . THR C 2 142 ? 85.758  134.474 79.080  1.00 144.23 ? 119  THR C N   1 
ATOM   8555  C  CA  . THR C 2 142 ? 85.395  133.097 79.389  1.00 144.54 ? 119  THR C CA  1 
ATOM   8556  C  C   . THR C 2 142 ? 83.894  133.042 79.638  1.00 144.38 ? 119  THR C C   1 
ATOM   8557  O  O   . THR C 2 142 ? 83.222  134.072 79.731  1.00 143.51 ? 119  THR C O   1 
ATOM   8558  C  CB  . THR C 2 142 ? 86.170  132.565 80.598  1.00 144.21 ? 119  THR C CB  1 
ATOM   8559  O  OG1 . THR C 2 142 ? 86.086  131.135 80.631  1.00 143.09 ? 119  THR C OG1 1 
ATOM   8560  C  CG2 . THR C 2 142 ? 85.596  133.132 81.887  1.00 144.11 ? 119  THR C CG2 1 
ATOM   8561  N  N   . VAL C 2 143 ? 83.374  131.819 79.744  1.00 147.09 ? 120  VAL C N   1 
ATOM   8562  C  CA  . VAL C 2 143 ? 81.941  131.609 79.923  1.00 147.12 ? 120  VAL C CA  1 
ATOM   8563  C  C   . VAL C 2 143 ? 81.682  130.727 81.137  1.00 146.57 ? 120  VAL C C   1 
ATOM   8564  O  O   . VAL C 2 143 ? 80.548  130.293 81.370  1.00 145.71 ? 120  VAL C O   1 
ATOM   8565  C  CB  . VAL C 2 143 ? 81.310  130.991 78.661  1.00 146.70 ? 120  VAL C CB  1 
ATOM   8566  C  CG1 . VAL C 2 143 ? 81.384  131.964 77.497  1.00 145.32 ? 120  VAL C CG1 1 
ATOM   8567  C  CG2 . VAL C 2 143 ? 82.000  129.681 78.313  1.00 145.58 ? 120  VAL C CG2 1 
ATOM   8568  N  N   . GLN C 2 144 ? 82.724  130.455 81.919  1.00 144.58 ? 121  GLN C N   1 
ATOM   8569  C  CA  . GLN C 2 144 ? 82.574  129.583 83.077  1.00 144.38 ? 121  GLN C CA  1 
ATOM   8570  C  C   . GLN C 2 144 ? 81.813  130.298 84.188  1.00 144.76 ? 121  GLN C C   1 
ATOM   8571  O  O   . GLN C 2 144 ? 82.126  131.440 84.538  1.00 145.63 ? 121  GLN C O   1 
ATOM   8572  C  CB  . GLN C 2 144 ? 83.942  129.119 83.573  1.00 143.29 ? 121  GLN C CB  1 
ATOM   8573  C  CG  . GLN C 2 144 ? 84.732  128.347 82.530  1.00 143.63 ? 121  GLN C CG  1 
ATOM   8574  C  CD  . GLN C 2 144 ? 85.728  127.386 83.145  1.00 144.08 ? 121  GLN C CD  1 
ATOM   8575  O  OE1 . GLN C 2 144 ? 86.854  127.763 83.465  1.00 144.26 ? 121  GLN C OE1 1 
ATOM   8576  N  NE2 . GLN C 2 144 ? 85.317  126.135 83.313  1.00 143.94 ? 121  GLN C NE2 1 
ATOM   8577  N  N   . LYS C 2 145 ? 80.806  129.616 84.739  1.00 146.15 ? 122  LYS C N   1 
ATOM   8578  C  CA  . LYS C 2 145 ? 79.953  130.230 85.753  1.00 146.50 ? 122  LYS C CA  1 
ATOM   8579  C  C   . LYS C 2 145 ? 80.717  130.493 87.045  1.00 146.96 ? 122  LYS C C   1 
ATOM   8580  O  O   . LYS C 2 145 ? 80.581  131.565 87.646  1.00 146.02 ? 122  LYS C O   1 
ATOM   8581  C  CB  . LYS C 2 145 ? 78.739  129.339 86.016  1.00 146.46 ? 122  LYS C CB  1 
ATOM   8582  C  CG  . LYS C 2 145 ? 77.464  130.098 86.345  1.00 147.11 ? 122  LYS C CG  1 
ATOM   8583  C  CD  . LYS C 2 145 ? 76.233  129.274 85.998  1.00 146.40 ? 122  LYS C CD  1 
ATOM   8584  C  CE  . LYS C 2 145 ? 74.957  129.965 86.451  1.00 145.96 ? 122  LYS C CE  1 
ATOM   8585  N  NZ  . LYS C 2 145 ? 74.825  129.969 87.934  1.00 145.78 ? 122  LYS C NZ  1 
ATOM   8586  N  N   . GLU C 2 146 ? 81.521  129.530 87.491  1.00 147.22 ? 123  GLU C N   1 
ATOM   8587  C  CA  . GLU C 2 146 ? 82.287  129.643 88.726  1.00 146.80 ? 123  GLU C CA  1 
ATOM   8588  C  C   . GLU C 2 146 ? 83.755  129.407 88.409  1.00 146.26 ? 123  GLU C C   1 
ATOM   8589  O  O   . GLU C 2 146 ? 84.112  128.353 87.873  1.00 146.76 ? 123  GLU C O   1 
ATOM   8590  C  CB  . GLU C 2 146 ? 81.799  128.637 89.771  1.00 146.57 ? 123  GLU C CB  1 
ATOM   8591  C  CG  . GLU C 2 146 ? 80.288  128.511 89.861  1.00 146.61 ? 123  GLU C CG  1 
ATOM   8592  C  CD  . GLU C 2 146 ? 79.625  129.790 90.325  1.00 146.01 ? 123  GLU C CD  1 
ATOM   8593  O  OE1 . GLU C 2 146 ? 80.125  130.398 91.293  1.00 146.37 ? 123  GLU C OE1 1 
ATOM   8594  O  OE2 . GLU C 2 146 ? 78.606  130.187 89.723  1.00 145.33 ? 123  GLU C OE2 1 
ATOM   8595  N  N   . ALA C 2 147 ? 84.602  130.378 88.745  1.00 137.22 ? 124  ALA C N   1 
ATOM   8596  C  CA  . ALA C 2 147 ? 86.028  130.250 88.472  1.00 137.07 ? 124  ALA C CA  1 
ATOM   8597  C  C   . ALA C 2 147 ? 86.788  131.283 89.289  1.00 136.97 ? 124  ALA C C   1 
ATOM   8598  O  O   . ALA C 2 147 ? 86.205  132.191 89.883  1.00 136.33 ? 124  ALA C O   1 
ATOM   8599  C  CB  . ALA C 2 147 ? 86.330  130.412 86.978  1.00 135.71 ? 124  ALA C CB  1 
ATOM   8600  N  N   . VAL C 2 148 ? 88.109  131.127 89.309  1.00 126.53 ? 125  VAL C N   1 
ATOM   8601  C  CA  . VAL C 2 148 ? 89.017  132.086 89.925  1.00 124.22 ? 125  VAL C CA  1 
ATOM   8602  C  C   . VAL C 2 148 ? 90.098  132.423 88.904  1.00 124.28 ? 125  VAL C C   1 
ATOM   8603  O  O   . VAL C 2 148 ? 90.605  131.533 88.211  1.00 125.03 ? 125  VAL C O   1 
ATOM   8604  C  CB  . VAL C 2 148 ? 89.613  131.545 91.245  1.00 124.13 ? 125  VAL C CB  1 
ATOM   8605  C  CG1 . VAL C 2 148 ? 90.757  130.575 91.002  1.00 122.99 ? 125  VAL C CG1 1 
ATOM   8606  C  CG2 . VAL C 2 148 ? 90.064  132.687 92.140  1.00 123.63 ? 125  VAL C CG2 1 
ATOM   8607  N  N   . LEU C 2 149 ? 90.399  133.713 88.759  1.00 118.68 ? 126  LEU C N   1 
ATOM   8608  C  CA  . LEU C 2 149 ? 91.340  134.177 87.744  1.00 118.67 ? 126  LEU C CA  1 
ATOM   8609  C  C   . LEU C 2 149 ? 92.745  134.342 88.310  1.00 120.12 ? 126  LEU C C   1 
ATOM   8610  O  O   . LEU C 2 149 ? 93.693  133.716 87.826  1.00 118.84 ? 126  LEU C O   1 
ATOM   8611  C  CB  . LEU C 2 149 ? 90.861  135.501 87.124  1.00 118.68 ? 126  LEU C CB  1 
ATOM   8612  C  CG  . LEU C 2 149 ? 89.569  135.579 86.296  1.00 119.69 ? 126  LEU C CG  1 
ATOM   8613  C  CD1 . LEU C 2 149 ? 88.312  135.289 87.109  1.00 120.04 ? 126  LEU C CD1 1 
ATOM   8614  C  CD2 . LEU C 2 149 ? 89.460  136.934 85.609  1.00 120.28 ? 126  LEU C CD2 1 
ATOM   8615  N  N   . VAL C 2 150 ? 92.896  135.178 89.337  1.00 113.73 ? 127  VAL C N   1 
ATOM   8616  C  CA  . VAL C 2 150 ? 94.190  135.448 89.943  1.00 111.39 ? 127  VAL C CA  1 
ATOM   8617  C  C   . VAL C 2 150 ? 94.057  135.332 91.456  1.00 109.58 ? 127  VAL C C   1 
ATOM   8618  O  O   . VAL C 2 150 ? 92.969  135.452 92.022  1.00 108.32 ? 127  VAL C O   1 
ATOM   8619  C  CB  . VAL C 2 150 ? 94.742  136.837 89.546  1.00 109.98 ? 127  VAL C CB  1 
ATOM   8620  C  CG1 . VAL C 2 150 ? 94.181  137.920 90.453  1.00 109.90 ? 127  VAL C CG1 1 
ATOM   8621  C  CG2 . VAL C 2 150 ? 96.263  136.838 89.569  1.00 109.38 ? 127  VAL C CG2 1 
ATOM   8622  N  N   . ARG C 2 151 ? 95.190  135.078 92.107  1.00 106.43 ? 128  ARG C N   1 
ATOM   8623  C  CA  . ARG C 2 151 ? 95.226  134.940 93.560  1.00 107.02 ? 128  ARG C CA  1 
ATOM   8624  C  C   . ARG C 2 151 ? 96.630  135.273 94.033  1.00 108.55 ? 128  ARG C C   1 
ATOM   8625  O  O   . ARG C 2 151 ? 97.590  134.602 93.641  1.00 109.14 ? 128  ARG C O   1 
ATOM   8626  C  CB  . ARG C 2 151 ? 94.827  133.527 93.986  1.00 107.66 ? 128  ARG C CB  1 
ATOM   8627  C  CG  . ARG C 2 151 ? 95.298  133.134 95.377  1.00 107.46 ? 128  ARG C CG  1 
ATOM   8628  C  CD  . ARG C 2 151 ? 94.138  133.060 96.356  1.00 107.71 ? 128  ARG C CD  1 
ATOM   8629  N  NE  . ARG C 2 151 ? 94.573  132.635 97.681  1.00 107.85 ? 128  ARG C NE  1 
ATOM   8630  C  CZ  . ARG C 2 151 ? 93.904  132.873 98.801  1.00 108.22 ? 128  ARG C CZ  1 
ATOM   8631  N  NH1 . ARG C 2 151 ? 92.761  133.537 98.796  1.00 107.57 ? 128  ARG C NH1 1 
ATOM   8632  N  NH2 . ARG C 2 151 ? 94.396  132.433 99.955  1.00 107.93 ? 128  ARG C NH2 1 
ATOM   8633  N  N   . VAL C 2 152 ? 96.752  136.303 94.866  1.00 100.92 ? 129  VAL C N   1 
ATOM   8634  C  CA  . VAL C 2 152 ? 98.031  136.740 95.413  1.00 98.53  ? 129  VAL C CA  1 
ATOM   8635  C  C   . VAL C 2 152 ? 98.086  136.328 96.875  1.00 97.61  ? 129  VAL C C   1 
ATOM   8636  O  O   . VAL C 2 152 ? 97.172  136.639 97.649  1.00 96.30  ? 129  VAL C O   1 
ATOM   8637  C  CB  . VAL C 2 152 ? 98.226  138.257 95.260  1.00 97.85  ? 129  VAL C CB  1 
ATOM   8638  C  CG1 . VAL C 2 152 ? 99.702  138.609 95.330  1.00 98.66  ? 129  VAL C CG1 1 
ATOM   8639  C  CG2 . VAL C 2 152 ? 97.623  138.738 93.951  1.00 97.51  ? 129  VAL C CG2 1 
ATOM   8640  N  N   . ASP C 2 153 ? 99.153  135.630 97.251  1.00 95.33  ? 130  ASP C N   1 
ATOM   8641  C  CA  . ASP C 2 153 ? 99.305  135.091 98.593  1.00 94.18  ? 130  ASP C CA  1 
ATOM   8642  C  C   . ASP C 2 153 ? 100.535 135.685 99.265  1.00 93.54  ? 130  ASP C C   1 
ATOM   8643  O  O   . ASP C 2 153 ? 101.530 136.012 98.610  1.00 95.22  ? 130  ASP C O   1 
ATOM   8644  C  CB  . ASP C 2 153 ? 99.419  133.560 98.569  1.00 96.88  ? 130  ASP C CB  1 
ATOM   8645  C  CG  . ASP C 2 153 ? 98.074  132.870 98.707  1.00 99.94  ? 130  ASP C CG  1 
ATOM   8646  O  OD1 . ASP C 2 153 ? 97.365  133.139 99.699  1.00 100.49 ? 130  ASP C OD1 1 
ATOM   8647  O  OD2 . ASP C 2 153 ? 97.728  132.055 97.825  1.00 98.65  ? 130  ASP C OD2 1 
ATOM   8648  N  N   . SER C 2 154 ? 100.451 135.830 100.583 1.00 87.33  ? 131  SER C N   1 
ATOM   8649  C  CA  . SER C 2 154 ? 101.599 136.234 101.374 1.00 86.76  ? 131  SER C CA  1 
ATOM   8650  C  C   . SER C 2 154 ? 102.524 135.038 101.586 1.00 85.81  ? 131  SER C C   1 
ATOM   8651  O  O   . SER C 2 154 ? 102.286 133.936 101.084 1.00 88.79  ? 131  SER C O   1 
ATOM   8652  C  CB  . SER C 2 154 ? 101.144 136.829 102.704 1.00 85.84  ? 131  SER C CB  1 
ATOM   8653  O  OG  . SER C 2 154 ? 100.050 136.104 103.236 1.00 85.84  ? 131  SER C OG  1 
ATOM   8654  N  N   . SER C 2 155 ? 103.596 135.253 102.342 1.00 81.05  ? 132  SER C N   1 
ATOM   8655  C  CA  . SER C 2 155 ? 104.526 134.175 102.637 1.00 83.44  ? 132  SER C CA  1 
ATOM   8656  C  C   . SER C 2 155 ? 103.888 133.188 103.614 1.00 86.23  ? 132  SER C C   1 
ATOM   8657  O  O   . SER C 2 155 ? 102.730 133.324 104.019 1.00 86.87  ? 132  SER C O   1 
ATOM   8658  C  CB  . SER C 2 155 ? 105.831 134.737 103.192 1.00 82.91  ? 132  SER C CB  1 
ATOM   8659  O  OG  . SER C 2 155 ? 106.663 135.215 102.150 1.00 82.35  ? 132  SER C OG  1 
ATOM   8660  N  N   . SER C 2 156 ? 104.661 132.172 103.990 1.00 87.15  ? 133  SER C N   1 
ATOM   8661  C  CA  . SER C 2 156 ? 104.157 131.149 104.895 1.00 86.81  ? 133  SER C CA  1 
ATOM   8662  C  C   . SER C 2 156 ? 103.825 131.750 106.255 1.00 87.00  ? 133  SER C C   1 
ATOM   8663  O  O   . SER C 2 156 ? 104.542 132.614 106.765 1.00 87.33  ? 133  SER C O   1 
ATOM   8664  C  CB  . SER C 2 156 ? 105.186 130.029 105.050 1.00 87.40  ? 133  SER C CB  1 
ATOM   8665  O  OG  . SER C 2 156 ? 106.473 130.556 105.323 1.00 87.20  ? 133  SER C OG  1 
ATOM   8666  N  N   . GLY C 2 157 ? 102.726 131.284 106.843 1.00 90.53  ? 134  GLY C N   1 
ATOM   8667  C  CA  . GLY C 2 157 ? 102.306 131.760 108.146 1.00 91.13  ? 134  GLY C CA  1 
ATOM   8668  C  C   . GLY C 2 157 ? 101.310 132.900 108.100 1.00 92.04  ? 134  GLY C C   1 
ATOM   8669  O  O   . GLY C 2 157 ? 100.191 132.770 108.604 1.00 94.93  ? 134  GLY C O   1 
ATOM   8670  N  N   . LEU C 2 158 ? 101.705 134.024 107.505 1.00 83.12  ? 135  LEU C N   1 
ATOM   8671  C  CA  . LEU C 2 158 ? 100.833 135.191 107.458 1.00 81.81  ? 135  LEU C CA  1 
ATOM   8672  C  C   . LEU C 2 158 ? 99.586  134.898 106.632 1.00 79.33  ? 135  LEU C C   1 
ATOM   8673  O  O   . LEU C 2 158 ? 99.649  134.245 105.587 1.00 80.44  ? 135  LEU C O   1 
ATOM   8674  C  CB  . LEU C 2 158 ? 101.584 136.390 106.880 1.00 80.86  ? 135  LEU C CB  1 
ATOM   8675  C  CG  . LEU C 2 158 ? 103.063 136.498 107.259 1.00 77.41  ? 135  LEU C CG  1 
ATOM   8676  C  CD1 . LEU C 2 158 ? 103.755 137.562 106.427 1.00 76.15  ? 135  LEU C CD1 1 
ATOM   8677  C  CD2 . LEU C 2 158 ? 103.213 136.792 108.741 1.00 77.02  ? 135  LEU C CD2 1 
ATOM   8678  N  N   . GLY C 2 159 ? 98.446  135.389 107.109 1.00 87.65  ? 136  GLY C N   1 
ATOM   8679  C  CA  . GLY C 2 159 ? 97.159  135.133 106.500 1.00 91.43  ? 136  GLY C CA  1 
ATOM   8680  C  C   . GLY C 2 159 ? 96.705  136.134 105.461 1.00 94.42  ? 136  GLY C C   1 
ATOM   8681  O  O   . GLY C 2 159 ? 95.569  136.035 104.987 1.00 94.00  ? 136  GLY C O   1 
ATOM   8682  N  N   . ASP C 2 160 ? 97.546  137.098 105.094 1.00 89.87  ? 137  ASP C N   1 
ATOM   8683  C  CA  . ASP C 2 160 ? 97.161  138.088 104.097 1.00 87.52  ? 137  ASP C CA  1 
ATOM   8684  C  C   . ASP C 2 160 ? 97.043  137.435 102.726 1.00 86.03  ? 137  ASP C C   1 
ATOM   8685  O  O   . ASP C 2 160 ? 97.920  136.668 102.317 1.00 85.01  ? 137  ASP C O   1 
ATOM   8686  C  CB  . ASP C 2 160 ? 98.185  139.222 104.055 1.00 83.87  ? 137  ASP C CB  1 
ATOM   8687  C  CG  . ASP C 2 160 ? 98.268  139.980 105.364 1.00 83.79  ? 137  ASP C CG  1 
ATOM   8688  O  OD1 . ASP C 2 160 ? 97.206  140.300 105.934 1.00 84.50  ? 137  ASP C OD1 1 
ATOM   8689  O  OD2 . ASP C 2 160 ? 99.394  140.258 105.824 1.00 82.50  ? 137  ASP C OD2 1 
ATOM   8690  N  N   . TYR C 2 161 ? 95.958  137.737 102.013 1.00 95.13  ? 138  TYR C N   1 
ATOM   8691  C  CA  . TYR C 2 161 ? 95.782  137.199 100.671 1.00 95.84  ? 138  TYR C CA  1 
ATOM   8692  C  C   . TYR C 2 161 ? 94.891  138.126 99.857  1.00 97.71  ? 138  TYR C C   1 
ATOM   8693  O  O   . TYR C 2 161 ? 94.184  138.978 100.399 1.00 97.87  ? 138  TYR C O   1 
ATOM   8694  C  CB  . TYR C 2 161 ? 95.236  135.755 100.707 1.00 95.85  ? 138  TYR C CB  1 
ATOM   8695  C  CG  . TYR C 2 161 ? 93.848  135.535 101.300 1.00 96.53  ? 138  TYR C CG  1 
ATOM   8696  C  CD1 . TYR C 2 161 ? 92.742  136.265 100.877 1.00 97.01  ? 138  TYR C CD1 1 
ATOM   8697  C  CD2 . TYR C 2 161 ? 93.650  134.575 102.285 1.00 97.20  ? 138  TYR C CD2 1 
ATOM   8698  C  CE1 . TYR C 2 161 ? 91.490  136.052 101.417 1.00 96.82  ? 138  TYR C CE1 1 
ATOM   8699  C  CE2 . TYR C 2 161 ? 92.400  134.355 102.831 1.00 98.84  ? 138  TYR C CE2 1 
ATOM   8700  C  CZ  . TYR C 2 161 ? 91.325  135.096 102.394 1.00 98.90  ? 138  TYR C CZ  1 
ATOM   8701  O  OH  . TYR C 2 161 ? 90.080  134.880 102.936 1.00 99.69  ? 138  TYR C OH  1 
ATOM   8702  N  N   . LEU C 2 162 ? 94.941  137.948 98.538  1.00 101.51 ? 139  LEU C N   1 
ATOM   8703  C  CA  . LEU C 2 162 ? 94.127  138.713 97.603  1.00 101.10 ? 139  LEU C CA  1 
ATOM   8704  C  C   . LEU C 2 162 ? 93.756  137.807 96.440  1.00 102.39 ? 139  LEU C C   1 
ATOM   8705  O  O   . LEU C 2 162 ? 94.616  137.093 95.919  1.00 103.14 ? 139  LEU C O   1 
ATOM   8706  C  CB  . LEU C 2 162 ? 94.880  139.948 97.097  1.00 100.70 ? 139  LEU C CB  1 
ATOM   8707  C  CG  . LEU C 2 162 ? 94.342  140.638 95.845  1.00 99.85  ? 139  LEU C CG  1 
ATOM   8708  C  CD1 . LEU C 2 162 ? 93.179  141.530 96.212  1.00 101.03 ? 139  LEU C CD1 1 
ATOM   8709  C  CD2 . LEU C 2 162 ? 95.435  141.441 95.161  1.00 101.20 ? 139  LEU C CD2 1 
ATOM   8710  N  N   . GLU C 2 163 ? 92.487  137.833 96.033  1.00 113.34 ? 140  GLU C N   1 
ATOM   8711  C  CA  . GLU C 2 163 ? 92.041  136.955 94.963  1.00 114.07 ? 140  GLU C CA  1 
ATOM   8712  C  C   . GLU C 2 163 ? 90.961  137.641 94.139  1.00 114.97 ? 140  GLU C C   1 
ATOM   8713  O  O   . GLU C 2 163 ? 90.227  138.503 94.633  1.00 114.60 ? 140  GLU C O   1 
ATOM   8714  C  CB  . GLU C 2 163 ? 91.520  135.623 95.514  1.00 113.90 ? 140  GLU C CB  1 
ATOM   8715  C  CG  . GLU C 2 163 ? 90.213  135.731 96.279  1.00 114.64 ? 140  GLU C CG  1 
ATOM   8716  C  CD  . GLU C 2 163 ? 89.976  134.543 97.190  1.00 114.75 ? 140  GLU C CD  1 
ATOM   8717  O  OE1 . GLU C 2 163 ? 90.883  133.693 97.307  1.00 114.58 ? 140  GLU C OE1 1 
ATOM   8718  O  OE2 . GLU C 2 163 ? 88.883  134.460 97.788  1.00 113.77 ? 140  GLU C OE2 1 
ATOM   8719  N  N   . LEU C 2 164 ? 90.883  137.245 92.871  1.00 124.16 ? 141  LEU C N   1 
ATOM   8720  C  CA  . LEU C 2 164 ? 89.871  137.710 91.934  1.00 124.67 ? 141  LEU C CA  1 
ATOM   8721  C  C   . LEU C 2 164 ? 89.124  136.498 91.398  1.00 127.09 ? 141  LEU C C   1 
ATOM   8722  O  O   . LEU C 2 164 ? 89.748  135.559 90.894  1.00 127.12 ? 141  LEU C O   1 
ATOM   8723  C  CB  . LEU C 2 164 ? 90.511  138.498 90.789  1.00 122.43 ? 141  LEU C CB  1 
ATOM   8724  C  CG  . LEU C 2 164 ? 89.646  138.791 89.564  1.00 124.92 ? 141  LEU C CG  1 
ATOM   8725  C  CD1 . LEU C 2 164 ? 88.619  139.859 89.880  1.00 124.21 ? 141  LEU C CD1 1 
ATOM   8726  C  CD2 . LEU C 2 164 ? 90.515  139.207 88.389  1.00 125.51 ? 141  LEU C CD2 1 
ATOM   8727  N  N   . HIS C 2 165 ? 87.797  136.513 91.500  1.00 132.68 ? 142  HIS C N   1 
ATOM   8728  C  CA  . HIS C 2 165 ? 87.023  135.325 91.174  1.00 131.68 ? 142  HIS C CA  1 
ATOM   8729  C  C   . HIS C 2 165 ? 85.666  135.718 90.608  1.00 133.10 ? 142  HIS C C   1 
ATOM   8730  O  O   . HIS C 2 165 ? 85.114  136.768 90.946  1.00 132.06 ? 142  HIS C O   1 
ATOM   8731  C  CB  . HIS C 2 165 ? 86.842  134.429 92.405  1.00 131.03 ? 142  HIS C CB  1 
ATOM   8732  C  CG  . HIS C 2 165 ? 85.901  134.986 93.427  1.00 131.81 ? 142  HIS C CG  1 
ATOM   8733  N  ND1 . HIS C 2 165 ? 85.769  136.338 93.660  1.00 131.02 ? 142  HIS C ND1 1 
ATOM   8734  C  CD2 . HIS C 2 165 ? 85.049  134.373 94.282  1.00 132.23 ? 142  HIS C CD2 1 
ATOM   8735  C  CE1 . HIS C 2 165 ? 84.874  136.534 94.611  1.00 131.35 ? 142  HIS C CE1 1 
ATOM   8736  N  NE2 . HIS C 2 165 ? 84.422  135.358 95.006  1.00 132.25 ? 142  HIS C NE2 1 
ATOM   8737  N  N   . ILE C 2 166 ? 85.131  134.851 89.753  1.00 139.19 ? 143  ILE C N   1 
ATOM   8738  C  CA  . ILE C 2 166 ? 83.807  135.017 89.167  1.00 138.52 ? 143  ILE C CA  1 
ATOM   8739  C  C   . ILE C 2 166 ? 82.892  133.963 89.772  1.00 137.64 ? 143  ILE C C   1 
ATOM   8740  O  O   . ILE C 2 166 ? 83.147  132.757 89.645  1.00 137.27 ? 143  ILE C O   1 
ATOM   8741  C  CB  . ILE C 2 166 ? 83.841  134.902 87.636  1.00 138.18 ? 143  ILE C CB  1 
ATOM   8742  C  CG1 . ILE C 2 166 ? 84.751  135.975 87.040  1.00 137.69 ? 143  ILE C CG1 1 
ATOM   8743  C  CG2 . ILE C 2 166 ? 82.437  135.016 87.064  1.00 138.11 ? 143  ILE C CG2 1 
ATOM   8744  C  CD1 . ILE C 2 166 ? 84.899  135.876 85.540  1.00 137.53 ? 143  ILE C CD1 1 
ATOM   8745  N  N   . HIS C 2 167 ? 81.829  134.421 90.427  1.00 141.36 ? 144  HIS C N   1 
ATOM   8746  C  CA  . HIS C 2 167 ? 80.809  133.563 91.012  1.00 143.17 ? 144  HIS C CA  1 
ATOM   8747  C  C   . HIS C 2 167 ? 79.451  133.968 90.458  1.00 143.63 ? 144  HIS C C   1 
ATOM   8748  O  O   . HIS C 2 167 ? 79.098  135.152 90.479  1.00 142.15 ? 144  HIS C O   1 
ATOM   8749  C  CB  . HIS C 2 167 ? 80.815  133.663 92.540  1.00 142.61 ? 144  HIS C CB  1 
ATOM   8750  C  CG  . HIS C 2 167 ? 79.661  132.971 93.197  1.00 144.25 ? 144  HIS C CG  1 
ATOM   8751  N  ND1 . HIS C 2 167 ? 79.443  131.615 93.084  1.00 144.32 ? 144  HIS C ND1 1 
ATOM   8752  C  CD2 . HIS C 2 167 ? 78.660  133.450 93.974  1.00 143.29 ? 144  HIS C CD2 1 
ATOM   8753  C  CE1 . HIS C 2 167 ? 78.358  131.288 93.763  1.00 142.61 ? 144  HIS C CE1 1 
ATOM   8754  N  NE2 . HIS C 2 167 ? 77.864  132.383 94.313  1.00 142.95 ? 144  HIS C NE2 1 
ATOM   8755  N  N   . GLN C 2 168 ? 78.700  132.984 89.958  1.00 143.06 ? 145  GLN C N   1 
ATOM   8756  C  CA  . GLN C 2 168 ? 77.370  133.205 89.387  1.00 142.10 ? 145  GLN C CA  1 
ATOM   8757  C  C   . GLN C 2 168 ? 77.401  134.225 88.252  1.00 142.75 ? 145  GLN C C   1 
ATOM   8758  O  O   . GLN C 2 168 ? 76.447  134.982 88.056  1.00 143.44 ? 145  GLN C O   1 
ATOM   8759  C  CB  . GLN C 2 168 ? 76.367  133.636 90.462  1.00 141.90 ? 145  GLN C CB  1 
ATOM   8760  C  CG  . GLN C 2 168 ? 75.722  132.482 91.210  1.00 142.01 ? 145  GLN C CG  1 
ATOM   8761  C  CD  . GLN C 2 168 ? 74.900  132.946 92.396  1.00 142.20 ? 145  GLN C CD  1 
ATOM   8762  O  OE1 . GLN C 2 168 ? 74.610  134.134 92.538  1.00 142.20 ? 145  GLN C OE1 1 
ATOM   8763  N  NE2 . GLN C 2 168 ? 74.522  132.009 93.257  1.00 142.02 ? 145  GLN C NE2 1 
ATOM   8764  N  N   . GLY C 2 169 ? 78.496  134.254 87.496  1.00 139.49 ? 146  GLY C N   1 
ATOM   8765  C  CA  . GLY C 2 169 ? 78.649  135.199 86.411  1.00 138.91 ? 146  GLY C CA  1 
ATOM   8766  C  C   . GLY C 2 169 ? 79.061  136.594 86.826  1.00 139.65 ? 146  GLY C C   1 
ATOM   8767  O  O   . GLY C 2 169 ? 79.186  137.467 85.957  1.00 139.16 ? 146  GLY C O   1 
ATOM   8768  N  N   . LYS C 2 170 ? 79.276  136.837 88.115  1.00 141.42 ? 147  LYS C N   1 
ATOM   8769  C  CA  . LYS C 2 170 ? 79.672  138.143 88.623  1.00 141.02 ? 147  LYS C CA  1 
ATOM   8770  C  C   . LYS C 2 170 ? 81.132  138.094 89.049  1.00 141.44 ? 147  LYS C C   1 
ATOM   8771  O  O   . LYS C 2 170 ? 81.525  137.216 89.823  1.00 141.95 ? 147  LYS C O   1 
ATOM   8772  C  CB  . LYS C 2 170 ? 78.792  138.562 89.803  1.00 140.11 ? 147  LYS C CB  1 
ATOM   8773  C  CG  . LYS C 2 170 ? 77.361  138.055 89.731  1.00 140.31 ? 147  LYS C CG  1 
ATOM   8774  C  CD  . LYS C 2 170 ? 76.552  138.817 88.695  1.00 140.73 ? 147  LYS C CD  1 
ATOM   8775  C  CE  . LYS C 2 170 ? 75.064  138.550 88.855  1.00 140.29 ? 147  LYS C CE  1 
ATOM   8776  N  NZ  . LYS C 2 170 ? 74.750  137.096 88.801  1.00 139.69 ? 147  LYS C NZ  1 
ATOM   8777  N  N   . ILE C 2 171 ? 81.928  139.029 88.546  1.00 140.17 ? 148  ILE C N   1 
ATOM   8778  C  CA  . ILE C 2 171 ? 83.349  139.098 88.868  1.00 139.75 ? 148  ILE C CA  1 
ATOM   8779  C  C   . ILE C 2 171 ? 83.534  139.968 90.104  1.00 139.06 ? 148  ILE C C   1 
ATOM   8780  O  O   . ILE C 2 171 ? 82.824  140.964 90.294  1.00 139.36 ? 148  ILE C O   1 
ATOM   8781  C  CB  . ILE C 2 171 ? 84.156  139.629 87.666  1.00 139.17 ? 148  ILE C CB  1 
ATOM   8782  C  CG1 . ILE C 2 171 ? 85.656  139.453 87.903  1.00 137.76 ? 148  ILE C CG1 1 
ATOM   8783  C  CG2 . ILE C 2 171 ? 83.812  141.085 87.371  1.00 138.53 ? 148  ILE C CG2 1 
ATOM   8784  C  CD1 . ILE C 2 171 ? 86.512  139.900 86.742  1.00 138.13 ? 148  ILE C CD1 1 
ATOM   8785  N  N   . GLY C 2 172 ? 84.477  139.585 90.963  1.00 131.36 ? 149  GLY C N   1 
ATOM   8786  C  CA  . GLY C 2 172 ? 84.691  140.314 92.198  1.00 131.71 ? 149  GLY C CA  1 
ATOM   8787  C  C   . GLY C 2 172 ? 86.036  140.006 92.813  1.00 132.52 ? 149  GLY C C   1 
ATOM   8788  O  O   . GLY C 2 172 ? 86.641  138.959 92.557  1.00 132.34 ? 149  GLY C O   1 
ATOM   8789  N  N   . VAL C 2 173 ? 86.491  140.932 93.652  1.00 125.60 ? 150  VAL C N   1 
ATOM   8790  C  CA  . VAL C 2 173 ? 87.795  140.857 94.298  1.00 124.48 ? 150  VAL C CA  1 
ATOM   8791  C  C   . VAL C 2 173 ? 87.584  140.707 95.797  1.00 123.28 ? 150  VAL C C   1 
ATOM   8792  O  O   . VAL C 2 173 ? 86.850  141.494 96.408  1.00 123.02 ? 150  VAL C O   1 
ATOM   8793  C  CB  . VAL C 2 173 ? 88.645  142.102 93.990  1.00 126.05 ? 150  VAL C CB  1 
ATOM   8794  C  CG1 . VAL C 2 173 ? 90.037  141.947 94.569  1.00 125.53 ? 150  VAL C CG1 1 
ATOM   8795  C  CG2 . VAL C 2 173 ? 88.701  142.356 92.493  1.00 126.15 ? 150  VAL C CG2 1 
ATOM   8796  N  N   . LYS C 2 174 ? 88.234  139.708 96.391  1.00 114.42 ? 151  LYS C N   1 
ATOM   8797  C  CA  . LYS C 2 174 ? 88.154  139.467 97.826  1.00 115.36 ? 151  LYS C CA  1 
ATOM   8798  C  C   . LYS C 2 174 ? 89.559  139.402 98.404  1.00 115.89 ? 151  LYS C C   1 
ATOM   8799  O  O   . LYS C 2 174 ? 90.416  138.682 97.882  1.00 115.39 ? 151  LYS C O   1 
ATOM   8800  C  CB  . LYS C 2 174 ? 87.394  138.171 98.129  1.00 116.01 ? 151  LYS C CB  1 
ATOM   8801  C  CG  . LYS C 2 174 ? 87.390  137.783 99.600  1.00 116.42 ? 151  LYS C CG  1 
ATOM   8802  C  CD  . LYS C 2 174 ? 86.234  136.852 99.932  1.00 114.70 ? 151  LYS C CD  1 
ATOM   8803  C  CE  . LYS C 2 174 ? 86.111  135.726 98.919  1.00 114.16 ? 151  LYS C CE  1 
ATOM   8804  N  NZ  . LYS C 2 174 ? 84.824  134.994 99.065  1.00 114.50 ? 151  LYS C NZ  1 
ATOM   8805  N  N   . PHE C 2 175 ? 89.794  140.146 99.485  1.00 107.84 ? 152  PHE C N   1 
ATOM   8806  C  CA  . PHE C 2 175 ? 91.114  140.181 100.098 1.00 106.01 ? 152  PHE C CA  1 
ATOM   8807  C  C   . PHE C 2 175 ? 91.006  140.142 101.616 1.00 105.94 ? 152  PHE C C   1 
ATOM   8808  O  O   . PHE C 2 175 ? 89.993  140.534 102.204 1.00 105.11 ? 152  PHE C O   1 
ATOM   8809  C  CB  . PHE C 2 175 ? 91.923  141.405 99.600  1.00 106.36 ? 152  PHE C CB  1 
ATOM   8810  C  CG  . PHE C 2 175 ? 91.315  142.754 99.930  1.00 104.92 ? 152  PHE C CG  1 
ATOM   8811  C  CD1 . PHE C 2 175 ? 91.065  143.149 101.235 1.00 105.15 ? 152  PHE C CD1 1 
ATOM   8812  C  CD2 . PHE C 2 175 ? 90.981  143.625 98.907  1.00 105.08 ? 152  PHE C CD2 1 
ATOM   8813  C  CE1 . PHE C 2 175 ? 90.513  144.382 101.511 1.00 107.50 ? 152  PHE C CE1 1 
ATOM   8814  C  CE2 . PHE C 2 175 ? 90.421  144.857 99.178  1.00 105.14 ? 152  PHE C CE2 1 
ATOM   8815  C  CZ  . PHE C 2 175 ? 90.188  145.237 100.481 1.00 106.57 ? 152  PHE C CZ  1 
ATOM   8816  N  N   . ASN C 2 176 ? 92.070  139.641 102.240 1.00 100.47 ? 153  ASN C N   1 
ATOM   8817  C  CA  . ASN C 2 176 ? 92.229  139.619 103.691 1.00 98.43  ? 153  ASN C CA  1 
ATOM   8818  C  C   . ASN C 2 176 ? 93.559  140.283 104.018 1.00 97.27  ? 153  ASN C C   1 
ATOM   8819  O  O   . ASN C 2 176 ? 94.623  139.768 103.653 1.00 96.66  ? 153  ASN C O   1 
ATOM   8820  C  CB  . ASN C 2 176 ? 92.180  138.191 104.233 1.00 99.32  ? 153  ASN C CB  1 
ATOM   8821  C  CG  . ASN C 2 176 ? 91.544  138.111 105.606 1.00 99.33  ? 153  ASN C CG  1 
ATOM   8822  O  OD1 . ASN C 2 176 ? 91.023  139.100 106.119 1.00 98.18  ? 153  ASN C OD1 1 
ATOM   8823  N  ND2 . ASN C 2 176 ? 91.582  136.929 106.208 1.00 98.89  ? 153  ASN C ND2 1 
ATOM   8824  N  N   . VAL C 2 177 ? 93.495  141.426 104.700 1.00 88.60  ? 154  VAL C N   1 
ATOM   8825  C  CA  . VAL C 2 177 ? 94.676  142.197 105.063 1.00 86.73  ? 154  VAL C CA  1 
ATOM   8826  C  C   . VAL C 2 177 ? 94.960  142.161 106.553 1.00 87.10  ? 154  VAL C C   1 
ATOM   8827  O  O   . VAL C 2 177 ? 95.894  142.836 107.009 1.00 89.54  ? 154  VAL C O   1 
ATOM   8828  C  CB  . VAL C 2 177 ? 94.564  143.654 104.576 1.00 83.44  ? 154  VAL C CB  1 
ATOM   8829  C  CG1 . VAL C 2 177 ? 94.771  143.723 103.073 1.00 84.89  ? 154  VAL C CG1 1 
ATOM   8830  C  CG2 . VAL C 2 177 ? 93.216  144.235 104.959 1.00 85.12  ? 154  VAL C CG2 1 
ATOM   8831  N  N   . GLY C 2 178 ? 94.193  141.398 107.328 1.00 92.16  ? 155  GLY C N   1 
ATOM   8832  C  CA  . GLY C 2 178 ? 94.484  141.242 108.739 1.00 90.99  ? 155  GLY C CA  1 
ATOM   8833  C  C   . GLY C 2 178 ? 93.285  141.306 109.663 1.00 94.17  ? 155  GLY C C   1 
ATOM   8834  O  O   . GLY C 2 178 ? 93.267  140.632 110.697 1.00 94.33  ? 155  GLY C O   1 
ATOM   8835  N  N   . THR C 2 179 ? 92.277  142.105 109.314 1.00 106.71 ? 156  THR C N   1 
ATOM   8836  C  CA  . THR C 2 179 ? 91.098  142.234 110.166 1.00 107.64 ? 156  THR C CA  1 
ATOM   8837  C  C   . THR C 2 179 ? 89.981  141.284 109.743 1.00 107.45 ? 156  THR C C   1 
ATOM   8838  O  O   . THR C 2 179 ? 89.598  140.387 110.500 1.00 106.31 ? 156  THR C O   1 
ATOM   8839  C  CB  . THR C 2 179 ? 90.587  143.679 110.153 1.00 104.89 ? 156  THR C CB  1 
ATOM   8840  O  OG1 . THR C 2 179 ? 90.491  144.143 108.801 1.00 105.62 ? 156  THR C OG1 1 
ATOM   8841  C  CG2 . THR C 2 179 ? 91.520  144.582 110.930 1.00 103.37 ? 156  THR C CG2 1 
ATOM   8842  N  N   . ASP C 2 180 ? 89.465  141.460 108.529 1.00 114.18 ? 157  ASP C N   1 
ATOM   8843  C  CA  . ASP C 2 180 ? 88.332  140.681 108.057 1.00 115.47 ? 157  ASP C CA  1 
ATOM   8844  C  C   . ASP C 2 180 ? 88.405  140.572 106.543 1.00 114.61 ? 157  ASP C C   1 
ATOM   8845  O  O   . ASP C 2 180 ? 89.079  141.360 105.875 1.00 113.57 ? 157  ASP C O   1 
ATOM   8846  C  CB  . ASP C 2 180 ? 86.997  141.308 108.482 1.00 117.25 ? 157  ASP C CB  1 
ATOM   8847  C  CG  . ASP C 2 180 ? 86.696  141.105 109.956 1.00 115.94 ? 157  ASP C CG  1 
ATOM   8848  O  OD1 . ASP C 2 180 ? 86.794  139.955 110.432 1.00 114.61 ? 157  ASP C OD1 1 
ATOM   8849  O  OD2 . ASP C 2 180 ? 86.362  142.097 110.638 1.00 114.62 ? 157  ASP C OD2 1 
ATOM   8850  N  N   . ASP C 2 181 ? 87.699  139.581 106.007 1.00 110.83 ? 158  ASP C N   1 
ATOM   8851  C  CA  . ASP C 2 181 ? 87.646  139.392 104.564 1.00 109.80 ? 158  ASP C CA  1 
ATOM   8852  C  C   . ASP C 2 181 ? 86.741  140.447 103.944 1.00 109.60 ? 158  ASP C C   1 
ATOM   8853  O  O   . ASP C 2 181 ? 85.553  140.528 104.275 1.00 110.20 ? 158  ASP C O   1 
ATOM   8854  C  CB  . ASP C 2 181 ? 87.139  137.991 104.234 1.00 109.51 ? 158  ASP C CB  1 
ATOM   8855  C  CG  . ASP C 2 181 ? 88.250  136.966 104.190 1.00 109.55 ? 158  ASP C CG  1 
ATOM   8856  O  OD1 . ASP C 2 181 ? 89.155  137.106 103.342 1.00 109.47 ? 158  ASP C OD1 1 
ATOM   8857  O  OD2 . ASP C 2 181 ? 88.219  136.020 105.004 1.00 109.26 ? 158  ASP C OD2 1 
ATOM   8858  N  N   . ILE C 2 182 ? 87.297  141.257 103.048 1.00 112.84 ? 159  ILE C N   1 
ATOM   8859  C  CA  . ILE C 2 182 ? 86.542  142.284 102.341 1.00 113.78 ? 159  ILE C CA  1 
ATOM   8860  C  C   . ILE C 2 182 ? 86.410  141.839 100.893 1.00 114.86 ? 159  ILE C C   1 
ATOM   8861  O  O   . ILE C 2 182 ? 87.417  141.656 100.198 1.00 115.25 ? 159  ILE C O   1 
ATOM   8862  C  CB  . ILE C 2 182 ? 87.216  143.660 102.441 1.00 113.10 ? 159  ILE C CB  1 
ATOM   8863  C  CG1 . ILE C 2 182 ? 87.596  143.965 103.891 1.00 113.53 ? 159  ILE C CG1 1 
ATOM   8864  C  CG2 . ILE C 2 182 ? 86.298  144.741 101.893 1.00 113.23 ? 159  ILE C CG2 1 
ATOM   8865  C  CD1 . ILE C 2 182 ? 86.416  144.004 104.835 1.00 114.15 ? 159  ILE C CD1 1 
ATOM   8866  N  N   . ALA C 2 183 ? 85.172  141.652 100.445 1.00 120.51 ? 160  ALA C N   1 
ATOM   8867  C  CA  . ALA C 2 183 ? 84.878  141.206 99.090  1.00 119.76 ? 160  ALA C CA  1 
ATOM   8868  C  C   . ALA C 2 183 ? 83.964  142.224 98.427  1.00 120.64 ? 160  ALA C C   1 
ATOM   8869  O  O   . ALA C 2 183 ? 82.863  142.489 98.921  1.00 120.66 ? 160  ALA C O   1 
ATOM   8870  C  CB  . ALA C 2 183 ? 84.229  139.821 99.094  1.00 119.25 ? 160  ALA C CB  1 
ATOM   8871  N  N   . ILE C 2 184 ? 84.420  142.788 97.313  1.00 131.67 ? 161  ILE C N   1 
ATOM   8872  C  CA  . ILE C 2 184 ? 83.640  143.731 96.523  1.00 132.81 ? 161  ILE C CA  1 
ATOM   8873  C  C   . ILE C 2 184 ? 83.438  143.126 95.141  1.00 133.63 ? 161  ILE C C   1 
ATOM   8874  O  O   . ILE C 2 184 ? 84.408  142.755 94.470  1.00 132.60 ? 161  ILE C O   1 
ATOM   8875  C  CB  . ILE C 2 184 ? 84.321  145.112 96.449  1.00 132.49 ? 161  ILE C CB  1 
ATOM   8876  C  CG1 . ILE C 2 184 ? 83.537  146.055 95.535  1.00 132.09 ? 161  ILE C CG1 1 
ATOM   8877  C  CG2 . ILE C 2 184 ? 85.783  144.989 96.026  1.00 132.64 ? 161  ILE C CG2 1 
ATOM   8878  C  CD1 . ILE C 2 184 ? 84.159  147.424 95.408  1.00 130.72 ? 161  ILE C CD1 1 
ATOM   8879  N  N   . GLU C 2 185 ? 82.180  143.011 94.725  1.00 142.91 ? 162  GLU C N   1 
ATOM   8880  C  CA  . GLU C 2 185 ? 81.825  142.266 93.526  1.00 142.67 ? 162  GLU C CA  1 
ATOM   8881  C  C   . GLU C 2 185 ? 80.927  143.105 92.631  1.00 144.00 ? 162  GLU C C   1 
ATOM   8882  O  O   . GLU C 2 185 ? 80.034  143.808 93.114  1.00 143.12 ? 162  GLU C O   1 
ATOM   8883  C  CB  . GLU C 2 185 ? 81.124  140.951 93.892  1.00 141.90 ? 162  GLU C CB  1 
ATOM   8884  C  CG  . GLU C 2 185 ? 81.035  139.943 92.760  1.00 142.94 ? 162  GLU C CG  1 
ATOM   8885  C  CD  . GLU C 2 185 ? 80.472  138.611 93.217  1.00 144.53 ? 162  GLU C CD  1 
ATOM   8886  O  OE1 . GLU C 2 185 ? 79.891  138.558 94.321  1.00 144.66 ? 162  GLU C OE1 1 
ATOM   8887  O  OE2 . GLU C 2 185 ? 80.611  137.616 92.475  1.00 145.19 ? 162  GLU C OE2 1 
ATOM   8888  N  N   . GLU C 2 186 ? 81.172  143.027 91.325  1.00 150.95 ? 163  GLU C N   1 
ATOM   8889  C  CA  . GLU C 2 186 ? 80.325  143.684 90.336  1.00 150.45 ? 163  GLU C CA  1 
ATOM   8890  C  C   . GLU C 2 186 ? 79.039  142.878 90.196  1.00 150.43 ? 163  GLU C C   1 
ATOM   8891  O  O   . GLU C 2 186 ? 79.062  141.737 89.724  1.00 149.67 ? 163  GLU C O   1 
ATOM   8892  C  CB  . GLU C 2 186 ? 81.056  143.802 89.002  1.00 149.92 ? 163  GLU C CB  1 
ATOM   8893  C  CG  . GLU C 2 186 ? 80.151  144.081 87.813  1.00 150.66 ? 163  GLU C CG  1 
ATOM   8894  C  CD  . GLU C 2 186 ? 79.575  145.482 87.836  1.00 151.26 ? 163  GLU C CD  1 
ATOM   8895  O  OE1 . GLU C 2 186 ? 80.304  146.418 88.225  1.00 151.44 ? 163  GLU C OE1 1 
ATOM   8896  O  OE2 . GLU C 2 186 ? 78.394  145.647 87.466  1.00 151.24 ? 163  GLU C OE2 1 
ATOM   8897  N  N   . SER C 2 187 ? 77.917  143.464 90.608  1.00 151.89 ? 164  SER C N   1 
ATOM   8898  C  CA  . SER C 2 187 ? 76.645  142.754 90.661  1.00 152.12 ? 164  SER C CA  1 
ATOM   8899  C  C   . SER C 2 187 ? 75.733  143.054 89.479  1.00 152.45 ? 164  SER C C   1 
ATOM   8900  O  O   . SER C 2 187 ? 75.059  142.147 88.981  1.00 151.83 ? 164  SER C O   1 
ATOM   8901  C  CB  . SER C 2 187 ? 75.910  143.088 91.963  1.00 152.45 ? 164  SER C CB  1 
ATOM   8902  O  OG  . SER C 2 187 ? 74.675  142.399 92.043  1.00 152.32 ? 164  SER C OG  1 
ATOM   8903  N  N   . ASN C 2 188 ? 75.694  144.299 89.017  1.00 151.74 ? 165  ASN C N   1 
ATOM   8904  C  CA  . ASN C 2 188 ? 74.770  144.699 87.955  1.00 151.37 ? 165  ASN C CA  1 
ATOM   8905  C  C   . ASN C 2 188 ? 75.388  144.530 86.570  1.00 151.56 ? 165  ASN C C   1 
ATOM   8906  O  O   . ASN C 2 188 ? 75.400  145.455 85.759  1.00 151.27 ? 165  ASN C O   1 
ATOM   8907  C  CB  . ASN C 2 188 ? 74.319  146.138 88.178  1.00 150.54 ? 165  ASN C CB  1 
ATOM   8908  C  CG  . ASN C 2 188 ? 73.469  146.294 89.422  1.00 151.29 ? 165  ASN C CG  1 
ATOM   8909  O  OD1 . ASN C 2 188 ? 72.255  146.094 89.388  1.00 151.29 ? 165  ASN C OD1 1 
ATOM   8910  N  ND2 . ASN C 2 188 ? 74.104  146.656 90.531  1.00 151.67 ? 165  ASN C ND2 1 
ATOM   8911  N  N   . ALA C 2 189 ? 75.897  143.331 86.289  1.00 149.32 ? 166  ALA C N   1 
ATOM   8912  C  CA  . ALA C 2 189 ? 76.489  143.029 84.993  1.00 148.37 ? 166  ALA C CA  1 
ATOM   8913  C  C   . ALA C 2 189 ? 76.702  141.529 84.879  1.00 148.43 ? 166  ALA C C   1 
ATOM   8914  O  O   . ALA C 2 189 ? 77.034  140.868 85.866  1.00 147.64 ? 166  ALA C O   1 
ATOM   8915  C  CB  . ALA C 2 189 ? 77.823  143.764 84.799  1.00 147.78 ? 166  ALA C CB  1 
ATOM   8916  N  N   . ILE C 2 190 ? 76.509  141.002 83.673  1.00 148.11 ? 167  ILE C N   1 
ATOM   8917  C  CA  . ILE C 2 190 ? 76.820  139.616 83.345  1.00 148.23 ? 167  ILE C CA  1 
ATOM   8918  C  C   . ILE C 2 190 ? 77.996  139.634 82.382  1.00 148.43 ? 167  ILE C C   1 
ATOM   8919  O  O   . ILE C 2 190 ? 77.930  140.271 81.323  1.00 148.43 ? 167  ILE C O   1 
ATOM   8920  C  CB  . ILE C 2 190 ? 75.612  138.887 82.738  1.00 147.47 ? 167  ILE C CB  1 
ATOM   8921  C  CG1 . ILE C 2 190 ? 74.512  138.710 83.788  1.00 146.99 ? 167  ILE C CG1 1 
ATOM   8922  C  CG2 . ILE C 2 190 ? 76.032  137.541 82.167  1.00 146.36 ? 167  ILE C CG2 1 
ATOM   8923  C  CD1 . ILE C 2 190 ? 75.001  138.126 85.097  1.00 146.41 ? 167  ILE C CD1 1 
ATOM   8924  N  N   . ILE C 2 191 ? 79.071  138.940 82.744  1.00 146.33 ? 168  ILE C N   1 
ATOM   8925  C  CA  . ILE C 2 191 ? 80.328  139.049 82.017  1.00 145.65 ? 168  ILE C CA  1 
ATOM   8926  C  C   . ILE C 2 191 ? 80.722  137.763 81.297  1.00 145.38 ? 168  ILE C C   1 
ATOM   8927  O  O   . ILE C 2 191 ? 81.587  137.815 80.409  1.00 145.01 ? 168  ILE C O   1 
ATOM   8928  C  CB  . ILE C 2 191 ? 81.467  139.508 82.953  1.00 144.63 ? 168  ILE C CB  1 
ATOM   8929  C  CG1 . ILE C 2 191 ? 82.449  140.402 82.196  1.00 145.01 ? 168  ILE C CG1 1 
ATOM   8930  C  CG2 . ILE C 2 191 ? 82.174  138.311 83.576  1.00 143.94 ? 168  ILE C CG2 1 
ATOM   8931  C  CD1 . ILE C 2 191 ? 81.912  141.788 81.913  1.00 145.15 ? 168  ILE C CD1 1 
ATOM   8932  N  N   . ASN C 2 192 ? 80.122  136.625 81.632  1.00 145.40 ? 169  ASN C N   1 
ATOM   8933  C  CA  . ASN C 2 192 ? 80.489  135.352 81.010  1.00 145.42 ? 169  ASN C CA  1 
ATOM   8934  C  C   . ASN C 2 192 ? 79.642  135.062 79.774  1.00 145.40 ? 169  ASN C C   1 
ATOM   8935  O  O   . ASN C 2 192 ? 79.039  133.997 79.641  1.00 144.51 ? 169  ASN C O   1 
ATOM   8936  C  CB  . ASN C 2 192 ? 80.377  134.226 82.031  1.00 144.79 ? 169  ASN C CB  1 
ATOM   8937  C  CG  . ASN C 2 192 ? 79.023  134.185 82.708  1.00 145.44 ? 169  ASN C CG  1 
ATOM   8938  O  OD1 . ASN C 2 192 ? 78.293  135.177 82.724  1.00 145.55 ? 169  ASN C OD1 1 
ATOM   8939  N  ND2 . ASN C 2 192 ? 78.679  133.035 83.275  1.00 144.59 ? 169  ASN C ND2 1 
ATOM   8940  N  N   . ASP C 2 193 ? 79.599  136.019 78.849  1.00 148.19 ? 170  ASP C N   1 
ATOM   8941  C  CA  . ASP C 2 193 ? 78.846  135.881 77.610  1.00 147.67 ? 170  ASP C CA  1 
ATOM   8942  C  C   . ASP C 2 193 ? 79.736  135.589 76.408  1.00 147.74 ? 170  ASP C C   1 
ATOM   8943  O  O   . ASP C 2 193 ? 79.255  135.627 75.271  1.00 147.36 ? 170  ASP C O   1 
ATOM   8944  C  CB  . ASP C 2 193 ? 78.016  137.141 77.354  1.00 147.46 ? 170  ASP C CB  1 
ATOM   8945  C  CG  . ASP C 2 193 ? 78.841  138.411 77.437  1.00 147.67 ? 170  ASP C CG  1 
ATOM   8946  O  OD1 . ASP C 2 193 ? 80.043  138.323 77.764  1.00 147.85 ? 170  ASP C OD1 1 
ATOM   8947  O  OD2 . ASP C 2 193 ? 78.285  139.498 77.175  1.00 147.14 ? 170  ASP C OD2 1 
ATOM   8948  N  N   . GLY C 2 194 ? 81.017  135.299 76.631  1.00 142.64 ? 171  GLY C N   1 
ATOM   8949  C  CA  . GLY C 2 194 ? 81.936  134.993 75.557  1.00 141.73 ? 171  GLY C CA  1 
ATOM   8950  C  C   . GLY C 2 194 ? 82.669  136.182 74.976  1.00 141.99 ? 171  GLY C C   1 
ATOM   8951  O  O   . GLY C 2 194 ? 83.561  135.989 74.139  1.00 141.24 ? 171  GLY C O   1 
ATOM   8952  N  N   . LYS C 2 195 ? 82.329  137.400 75.386  1.00 148.01 ? 172  LYS C N   1 
ATOM   8953  C  CA  . LYS C 2 195 ? 82.997  138.583 74.872  1.00 147.78 ? 172  LYS C CA  1 
ATOM   8954  C  C   . LYS C 2 195 ? 84.325  138.807 75.595  1.00 148.63 ? 172  LYS C C   1 
ATOM   8955  O  O   . LYS C 2 195 ? 84.628  138.181 76.614  1.00 148.08 ? 172  LYS C O   1 
ATOM   8956  C  CB  . LYS C 2 195 ? 82.098  139.810 75.012  1.00 147.02 ? 172  LYS C CB  1 
ATOM   8957  C  CG  . LYS C 2 195 ? 80.789  139.710 74.246  1.00 147.71 ? 172  LYS C CG  1 
ATOM   8958  C  CD  . LYS C 2 195 ? 81.035  139.516 72.759  1.00 147.69 ? 172  LYS C CD  1 
ATOM   8959  C  CE  . LYS C 2 195 ? 79.741  139.216 72.020  1.00 147.61 ? 172  LYS C CE  1 
ATOM   8960  N  NZ  . LYS C 2 195 ? 79.095  137.970 72.515  1.00 147.42 ? 172  LYS C NZ  1 
ATOM   8961  N  N   . TYR C 2 196 ? 85.124  139.718 75.046  1.00 150.14 ? 173  TYR C N   1 
ATOM   8962  C  CA  . TYR C 2 196 ? 86.449  140.036 75.567  1.00 149.87 ? 173  TYR C CA  1 
ATOM   8963  C  C   . TYR C 2 196 ? 86.339  141.285 76.436  1.00 149.70 ? 173  TYR C C   1 
ATOM   8964  O  O   . TYR C 2 196 ? 86.181  142.395 75.918  1.00 149.24 ? 173  TYR C O   1 
ATOM   8965  C  CB  . TYR C 2 196 ? 87.433  140.239 74.417  1.00 149.64 ? 173  TYR C CB  1 
ATOM   8966  C  CG  . TYR C 2 196 ? 88.873  140.426 74.834  1.00 149.56 ? 173  TYR C CG  1 
ATOM   8967  C  CD1 . TYR C 2 196 ? 89.681  139.334 75.119  1.00 148.56 ? 173  TYR C CD1 1 
ATOM   8968  C  CD2 . TYR C 2 196 ? 89.430  141.695 74.925  1.00 149.00 ? 173  TYR C CD2 1 
ATOM   8969  C  CE1 . TYR C 2 196 ? 91.001  139.500 75.493  1.00 148.31 ? 173  TYR C CE1 1 
ATOM   8970  C  CE2 . TYR C 2 196 ? 90.748  141.871 75.299  1.00 148.86 ? 173  TYR C CE2 1 
ATOM   8971  C  CZ  . TYR C 2 196 ? 91.528  140.770 75.581  1.00 148.96 ? 173  TYR C CZ  1 
ATOM   8972  O  OH  . TYR C 2 196 ? 92.841  140.943 75.954  1.00 148.61 ? 173  TYR C OH  1 
ATOM   8973  N  N   . HIS C 2 197 ? 86.426  141.106 77.751  1.00 146.89 ? 174  HIS C N   1 
ATOM   8974  C  CA  . HIS C 2 197 ? 86.275  142.202 78.699  1.00 146.76 ? 174  HIS C CA  1 
ATOM   8975  C  C   . HIS C 2 197 ? 87.591  142.467 79.418  1.00 146.91 ? 174  HIS C C   1 
ATOM   8976  O  O   . HIS C 2 197 ? 88.565  141.728 79.279  1.00 146.73 ? 174  HIS C O   1 
ATOM   8977  C  CB  . HIS C 2 197 ? 85.172  141.898 79.720  1.00 146.82 ? 174  HIS C CB  1 
ATOM   8978  C  CG  . HIS C 2 197 ? 83.992  141.181 79.143  1.00 147.80 ? 174  HIS C CG  1 
ATOM   8979  N  ND1 . HIS C 2 197 ? 82.872  141.841 78.686  1.00 148.05 ? 174  HIS C ND1 1 
ATOM   8980  C  CD2 . HIS C 2 197 ? 83.751  139.861 78.963  1.00 147.01 ? 174  HIS C CD2 1 
ATOM   8981  C  CE1 . HIS C 2 197 ? 81.994  140.959 78.243  1.00 147.71 ? 174  HIS C CE1 1 
ATOM   8982  N  NE2 . HIS C 2 197 ? 82.504  139.750 78.398  1.00 147.24 ? 174  HIS C NE2 1 
ATOM   8983  N  N   . VAL C 2 198 ? 87.603  143.545 80.204  1.00 141.57 ? 175  VAL C N   1 
ATOM   8984  C  CA  . VAL C 2 198 ? 88.739  143.900 81.043  1.00 140.61 ? 175  VAL C CA  1 
ATOM   8985  C  C   . VAL C 2 198 ? 88.219  144.274 82.425  1.00 139.81 ? 175  VAL C C   1 
ATOM   8986  O  O   . VAL C 2 198 ? 87.063  144.670 82.594  1.00 139.77 ? 175  VAL C O   1 
ATOM   8987  C  CB  . VAL C 2 198 ? 89.577  145.051 80.438  1.00 139.71 ? 175  VAL C CB  1 
ATOM   8988  C  CG1 . VAL C 2 198 ? 88.992  146.405 80.816  1.00 139.54 ? 175  VAL C CG1 1 
ATOM   8989  C  CG2 . VAL C 2 198 ? 91.030  144.945 80.879  1.00 138.41 ? 175  VAL C CG2 1 
ATOM   8990  N  N   . VAL C 2 199 ? 89.086  144.127 83.425  1.00 134.08 ? 176  VAL C N   1 
ATOM   8991  C  CA  . VAL C 2 199 ? 88.738  144.432 84.808  1.00 134.05 ? 176  VAL C CA  1 
ATOM   8992  C  C   . VAL C 2 199 ? 89.939  145.075 85.490  1.00 134.35 ? 176  VAL C C   1 
ATOM   8993  O  O   . VAL C 2 199 ? 91.082  144.637 85.313  1.00 133.85 ? 176  VAL C O   1 
ATOM   8994  C  CB  . VAL C 2 199 ? 88.270  143.169 85.565  1.00 133.40 ? 176  VAL C CB  1 
ATOM   8995  C  CG1 . VAL C 2 199 ? 89.307  142.062 85.469  1.00 132.15 ? 176  VAL C CG1 1 
ATOM   8996  C  CG2 . VAL C 2 199 ? 87.962  143.496 87.017  1.00 133.41 ? 176  VAL C CG2 1 
ATOM   8997  N  N   . ARG C 2 200 ? 89.674  146.127 86.266  1.00 129.38 ? 177  ARG C N   1 
ATOM   8998  C  CA  . ARG C 2 200 ? 90.689  146.833 87.029  1.00 127.80 ? 177  ARG C CA  1 
ATOM   8999  C  C   . ARG C 2 200 ? 90.233  146.954 88.476  1.00 128.29 ? 177  ARG C C   1 
ATOM   9000  O  O   . ARG C 2 200 ? 89.040  147.097 88.763  1.00 128.79 ? 177  ARG C O   1 
ATOM   9001  C  CB  . ARG C 2 200 ? 90.970  148.228 86.448  1.00 126.96 ? 177  ARG C CB  1 
ATOM   9002  C  CG  . ARG C 2 200 ? 90.898  148.298 84.930  1.00 128.25 ? 177  ARG C CG  1 
ATOM   9003  C  CD  . ARG C 2 200 ? 91.712  149.461 84.385  1.00 127.77 ? 177  ARG C CD  1 
ATOM   9004  N  NE  . ARG C 2 200 ? 91.607  149.571 82.935  1.00 128.50 ? 177  ARG C NE  1 
ATOM   9005  C  CZ  . ARG C 2 200 ? 92.230  148.777 82.074  1.00 128.43 ? 177  ARG C CZ  1 
ATOM   9006  N  NH1 . ARG C 2 200 ? 93.024  147.801 82.482  1.00 128.27 ? 177  ARG C NH1 1 
ATOM   9007  N  NH2 . ARG C 2 200 ? 92.054  148.970 80.770  1.00 129.50 ? 177  ARG C NH2 1 
ATOM   9008  N  N   . PHE C 2 201 ? 91.200  146.890 89.388  1.00 118.43 ? 178  PHE C N   1 
ATOM   9009  C  CA  . PHE C 2 201 ? 90.915  146.908 90.817  1.00 117.67 ? 178  PHE C CA  1 
ATOM   9010  C  C   . PHE C 2 201 ? 92.049  147.629 91.527  1.00 116.43 ? 178  PHE C C   1 
ATOM   9011  O  O   . PHE C 2 201 ? 93.209  147.218 91.425  1.00 115.34 ? 178  PHE C O   1 
ATOM   9012  C  CB  . PHE C 2 201 ? 90.753  145.486 91.356  1.00 116.67 ? 178  PHE C CB  1 
ATOM   9013  C  CG  . PHE C 2 201 ? 91.077  145.346 92.813  1.00 115.73 ? 178  PHE C CG  1 
ATOM   9014  C  CD1 . PHE C 2 201 ? 90.246  145.891 93.776  1.00 116.35 ? 178  PHE C CD1 1 
ATOM   9015  C  CD2 . PHE C 2 201 ? 92.214  144.671 93.219  1.00 115.94 ? 178  PHE C CD2 1 
ATOM   9016  C  CE1 . PHE C 2 201 ? 90.542  145.761 95.118  1.00 116.83 ? 178  PHE C CE1 1 
ATOM   9017  C  CE2 . PHE C 2 201 ? 92.516  144.541 94.558  1.00 116.01 ? 178  PHE C CE2 1 
ATOM   9018  C  CZ  . PHE C 2 201 ? 91.678  145.085 95.509  1.00 116.47 ? 178  PHE C CZ  1 
ATOM   9019  N  N   . THR C 2 202 ? 91.712  148.698 92.241  1.00 117.19 ? 179  THR C N   1 
ATOM   9020  C  CA  . THR C 2 202 ? 92.683  149.492 92.982  1.00 115.83 ? 179  THR C CA  1 
ATOM   9021  C  C   . THR C 2 202 ? 92.342  149.446 94.463  1.00 115.18 ? 179  THR C C   1 
ATOM   9022  O  O   . THR C 2 202 ? 91.204  149.728 94.852  1.00 115.98 ? 179  THR C O   1 
ATOM   9023  C  CB  . THR C 2 202 ? 92.706  150.942 92.491  1.00 117.31 ? 179  THR C CB  1 
ATOM   9024  O  OG1 . THR C 2 202 ? 91.486  151.594 92.865  1.00 116.59 ? 179  THR C OG1 1 
ATOM   9025  C  CG2 . THR C 2 202 ? 92.860  150.991 90.979  1.00 116.90 ? 179  THR C CG2 1 
ATOM   9026  N  N   . ARG C 2 203 ? 93.328  149.103 95.285  1.00 95.77  ? 180  ARG C N   1 
ATOM   9027  C  CA  . ARG C 2 203 ? 93.149  148.984 96.724  1.00 94.53  ? 180  ARG C CA  1 
ATOM   9028  C  C   . ARG C 2 203 ? 94.046  149.992 97.424  1.00 94.88  ? 180  ARG C C   1 
ATOM   9029  O  O   . ARG C 2 203 ? 95.234  150.093 97.102  1.00 96.38  ? 180  ARG C O   1 
ATOM   9030  C  CB  . ARG C 2 203 ? 93.477  147.570 97.204  1.00 94.10  ? 180  ARG C CB  1 
ATOM   9031  C  CG  . ARG C 2 203 ? 92.862  147.215 98.541  1.00 96.02  ? 180  ARG C CG  1 
ATOM   9032  C  CD  . ARG C 2 203 ? 93.864  147.376 99.665  1.00 94.22  ? 180  ARG C CD  1 
ATOM   9033  N  NE  . ARG C 2 203 ? 95.042  146.539 99.481  1.00 91.58  ? 180  ARG C NE  1 
ATOM   9034  C  CZ  . ARG C 2 203 ? 96.049  146.471 100.340 1.00 91.75  ? 180  ARG C CZ  1 
ATOM   9035  N  NH1 . ARG C 2 203 ? 96.054  147.182 101.455 1.00 91.98  ? 180  ARG C NH1 1 
ATOM   9036  N  NH2 . ARG C 2 203 ? 97.076  145.672 100.073 1.00 91.83  ? 180  ARG C NH2 1 
ATOM   9037  N  N   . SER C 2 204 ? 93.481  150.726 98.381  1.00 97.41  ? 181  SER C N   1 
ATOM   9038  C  CA  . SER C 2 204 ? 94.240  151.678 99.183  1.00 96.83  ? 181  SER C CA  1 
ATOM   9039  C  C   . SER C 2 204 ? 93.745  151.591 100.617 1.00 99.60  ? 181  SER C C   1 
ATOM   9040  O  O   . SER C 2 204 ? 92.568  151.853 100.882 1.00 102.99 ? 181  SER C O   1 
ATOM   9041  C  CB  . SER C 2 204 ? 94.092  153.104 98.645  1.00 97.61  ? 181  SER C CB  1 
ATOM   9042  O  OG  . SER C 2 204 ? 92.760  153.566 98.786  1.00 100.76 ? 181  SER C OG  1 
ATOM   9043  N  N   . GLY C 2 205 ? 94.638  151.240 101.534 1.00 89.15  ? 182  GLY C N   1 
ATOM   9044  C  CA  . GLY C 2 205 ? 94.219  151.006 102.905 1.00 87.18  ? 182  GLY C CA  1 
ATOM   9045  C  C   . GLY C 2 205 ? 93.265  149.830 102.958 1.00 87.01  ? 182  GLY C C   1 
ATOM   9046  O  O   . GLY C 2 205 ? 93.586  148.719 102.520 1.00 85.85  ? 182  GLY C O   1 
ATOM   9047  N  N   . GLY C 2 206 ? 92.078  150.057 103.511 1.00 99.75  ? 183  GLY C N   1 
ATOM   9048  C  CA  . GLY C 2 206 ? 91.029  149.059 103.459 1.00 101.68 ? 183  GLY C CA  1 
ATOM   9049  C  C   . GLY C 2 206 ? 90.052  149.337 102.335 1.00 104.11 ? 183  GLY C C   1 
ATOM   9050  O  O   . GLY C 2 206 ? 89.231  148.484 101.985 1.00 104.95 ? 183  GLY C O   1 
ATOM   9051  N  N   . ASN C 2 207 ? 90.144  150.531 101.757 1.00 116.54 ? 184  ASN C N   1 
ATOM   9052  C  CA  . ASN C 2 207 ? 89.246  150.923 100.680 1.00 116.14 ? 184  ASN C CA  1 
ATOM   9053  C  C   . ASN C 2 207 ? 89.579  150.182 99.391  1.00 115.87 ? 184  ASN C C   1 
ATOM   9054  O  O   . ASN C 2 207 ? 90.749  149.948 99.071  1.00 114.44 ? 184  ASN C O   1 
ATOM   9055  C  CB  . ASN C 2 207 ? 89.321  152.430 100.450 1.00 115.88 ? 184  ASN C CB  1 
ATOM   9056  C  CG  . ASN C 2 207 ? 89.053  153.228 101.710 1.00 116.80 ? 184  ASN C CG  1 
ATOM   9057  O  OD1 . ASN C 2 207 ? 88.348  152.773 102.610 1.00 116.46 ? 184  ASN C OD1 1 
ATOM   9058  N  ND2 . ASN C 2 207 ? 89.613  154.430 101.777 1.00 118.34 ? 184  ASN C ND2 1 
ATOM   9059  N  N   . ALA C 2 208 ? 88.537  149.828 98.641  1.00 125.88 ? 185  ALA C N   1 
ATOM   9060  C  CA  . ALA C 2 208 ? 88.687  149.103 97.388  1.00 125.95 ? 185  ALA C CA  1 
ATOM   9061  C  C   . ALA C 2 208 ? 87.870  149.774 96.293  1.00 127.38 ? 185  ALA C C   1 
ATOM   9062  O  O   . ALA C 2 208 ? 86.853  150.419 96.561  1.00 128.48 ? 185  ALA C O   1 
ATOM   9063  C  CB  . ALA C 2 208 ? 88.257  147.637 97.532  1.00 125.19 ? 185  ALA C CB  1 
ATOM   9064  N  N   . THR C 2 209 ? 88.327  149.615 95.052  1.00 130.09 ? 186  THR C N   1 
ATOM   9065  C  CA  . THR C 2 209 ? 87.633  150.152 93.889  1.00 131.04 ? 186  THR C CA  1 
ATOM   9066  C  C   . THR C 2 209 ? 87.719  149.138 92.760  1.00 130.64 ? 186  THR C C   1 
ATOM   9067  O  O   . THR C 2 209 ? 88.816  148.702 92.400  1.00 130.12 ? 186  THR C O   1 
ATOM   9068  C  CB  . THR C 2 209 ? 88.237  151.492 93.449  1.00 129.54 ? 186  THR C CB  1 
ATOM   9069  O  OG1 . THR C 2 209 ? 87.748  152.540 94.295  1.00 129.38 ? 186  THR C OG1 1 
ATOM   9070  C  CG2 . THR C 2 209 ? 87.870  151.801 92.005  1.00 129.90 ? 186  THR C CG2 1 
ATOM   9071  N  N   . LEU C 2 210 ? 86.566  148.769 92.209  1.00 137.77 ? 187  LEU C N   1 
ATOM   9072  C  CA  . LEU C 2 210 ? 86.469  147.764 91.159  1.00 137.54 ? 187  LEU C CA  1 
ATOM   9073  C  C   . LEU C 2 210 ? 85.756  148.364 89.956  1.00 137.53 ? 187  LEU C C   1 
ATOM   9074  O  O   . LEU C 2 210 ? 84.697  148.982 90.105  1.00 138.45 ? 187  LEU C O   1 
ATOM   9075  C  CB  . LEU C 2 210 ? 85.719  146.527 91.661  1.00 137.39 ? 187  LEU C CB  1 
ATOM   9076  C  CG  . LEU C 2 210 ? 85.535  145.366 90.683  1.00 137.44 ? 187  LEU C CG  1 
ATOM   9077  C  CD1 . LEU C 2 210 ? 86.883  144.855 90.209  1.00 136.75 ? 187  LEU C CD1 1 
ATOM   9078  C  CD2 . LEU C 2 210 ? 84.730  144.249 91.328  1.00 137.69 ? 187  LEU C CD2 1 
ATOM   9079  N  N   . GLN C 2 211 ? 86.332  148.184 88.767  1.00 140.50 ? 188  GLN C N   1 
ATOM   9080  C  CA  . GLN C 2 211 ? 85.753  148.736 87.550  1.00 141.08 ? 188  GLN C CA  1 
ATOM   9081  C  C   . GLN C 2 211 ? 85.917  147.750 86.405  1.00 142.02 ? 188  GLN C C   1 
ATOM   9082  O  O   . GLN C 2 211 ? 87.025  147.274 86.142  1.00 141.78 ? 188  GLN C O   1 
ATOM   9083  C  CB  . GLN C 2 211 ? 86.406  150.075 87.188  1.00 141.53 ? 188  GLN C CB  1 
ATOM   9084  C  CG  . GLN C 2 211 ? 85.831  150.729 85.943  1.00 141.06 ? 188  GLN C CG  1 
ATOM   9085  C  CD  . GLN C 2 211 ? 86.546  152.015 85.579  1.00 141.06 ? 188  GLN C CD  1 
ATOM   9086  O  OE1 . GLN C 2 211 ? 87.626  152.305 86.093  1.00 141.36 ? 188  GLN C OE1 1 
ATOM   9087  N  NE2 . GLN C 2 211 ? 85.944  152.794 84.688  1.00 141.40 ? 188  GLN C NE2 1 
ATOM   9088  N  N   . VAL C 2 212 ? 84.819  147.462 85.712  1.00 149.87 ? 189  VAL C N   1 
ATOM   9089  C  CA  . VAL C 2 212 ? 84.822  146.559 84.566  1.00 149.50 ? 189  VAL C CA  1 
ATOM   9090  C  C   . VAL C 2 212 ? 84.465  147.368 83.326  1.00 149.63 ? 189  VAL C C   1 
ATOM   9091  O  O   . VAL C 2 212 ? 83.403  148.001 83.272  1.00 148.70 ? 189  VAL C O   1 
ATOM   9092  C  CB  . VAL C 2 212 ? 83.853  145.384 84.767  1.00 149.20 ? 189  VAL C CB  1 
ATOM   9093  C  CG1 . VAL C 2 212 ? 84.507  144.304 85.612  1.00 148.96 ? 189  VAL C CG1 1 
ATOM   9094  C  CG2 . VAL C 2 212 ? 82.565  145.858 85.424  1.00 148.89 ? 189  VAL C CG2 1 
ATOM   9095  N  N   . ASP C 2 213 ? 85.358  147.347 82.335  1.00 152.34 ? 190  ASP C N   1 
ATOM   9096  C  CA  . ASP C 2 213 ? 85.169  148.048 81.069  1.00 152.27 ? 190  ASP C CA  1 
ATOM   9097  C  C   . ASP C 2 213 ? 84.798  149.512 81.278  1.00 152.64 ? 190  ASP C C   1 
ATOM   9098  O  O   . ASP C 2 213 ? 85.545  150.265 81.909  1.00 152.50 ? 190  ASP C O   1 
ATOM   9099  C  CB  . ASP C 2 213 ? 84.101  147.347 80.227  1.00 152.73 ? 190  ASP C CB  1 
ATOM   9100  C  CG  . ASP C 2 213 ? 84.608  146.066 79.594  1.00 152.51 ? 190  ASP C CG  1 
ATOM   9101  O  OD1 . ASP C 2 213 ? 85.825  145.972 79.334  1.00 152.12 ? 190  ASP C OD1 1 
ATOM   9102  O  OD2 . ASP C 2 213 ? 83.789  145.153 79.357  1.00 152.50 ? 190  ASP C OD2 1 
ATOM   9103  N  N   . SER C 2 214 ? 83.643  149.920 80.753  1.00 164.60 ? 191  SER C N   1 
ATOM   9104  C  CA  . SER C 2 214 ? 83.172  151.295 80.863  1.00 165.15 ? 191  SER C CA  1 
ATOM   9105  C  C   . SER C 2 214 ? 82.091  151.462 81.923  1.00 165.29 ? 191  SER C C   1 
ATOM   9106  O  O   . SER C 2 214 ? 81.507  152.546 82.033  1.00 165.43 ? 191  SER C O   1 
ATOM   9107  C  CB  . SER C 2 214 ? 82.656  151.785 79.508  1.00 164.70 ? 191  SER C CB  1 
ATOM   9108  O  OG  . SER C 2 214 ? 81.504  151.064 79.109  1.00 164.88 ? 191  SER C OG  1 
ATOM   9109  N  N   . TRP C 2 215 ? 81.809  150.421 82.701  1.00 159.72 ? 192  TRP C N   1 
ATOM   9110  C  CA  . TRP C 2 215 ? 80.793  150.517 83.735  1.00 159.33 ? 192  TRP C CA  1 
ATOM   9111  C  C   . TRP C 2 215 ? 81.249  151.465 84.845  1.00 159.91 ? 192  TRP C C   1 
ATOM   9112  O  O   . TRP C 2 215 ? 82.450  151.655 85.054  1.00 160.10 ? 192  TRP C O   1 
ATOM   9113  C  CB  . TRP C 2 215 ? 80.492  149.138 84.316  1.00 158.46 ? 192  TRP C CB  1 
ATOM   9114  C  CG  . TRP C 2 215 ? 79.455  148.378 83.548  1.00 159.42 ? 192  TRP C CG  1 
ATOM   9115  C  CD1 . TRP C 2 215 ? 78.106  148.582 83.573  1.00 159.43 ? 192  TRP C CD1 1 
ATOM   9116  C  CD2 . TRP C 2 215 ? 79.680  147.292 82.641  1.00 160.25 ? 192  TRP C CD2 1 
ATOM   9117  N  NE1 . TRP C 2 215 ? 77.477  147.691 82.738  1.00 159.07 ? 192  TRP C NE1 1 
ATOM   9118  C  CE2 . TRP C 2 215 ? 78.421  146.888 82.154  1.00 160.01 ? 192  TRP C CE2 1 
ATOM   9119  C  CE3 . TRP C 2 215 ? 80.823  146.622 82.194  1.00 159.78 ? 192  TRP C CE3 1 
ATOM   9120  C  CZ2 . TRP C 2 215 ? 78.273  145.845 81.242  1.00 159.59 ? 192  TRP C CZ2 1 
ATOM   9121  C  CZ3 . TRP C 2 215 ? 80.674  145.587 81.288  1.00 159.47 ? 192  TRP C CZ3 1 
ATOM   9122  C  CH2 . TRP C 2 215 ? 79.409  145.209 80.822  1.00 159.16 ? 192  TRP C CH2 1 
ATOM   9123  N  N   . PRO C 2 216 ? 80.307  152.085 85.558  1.00 161.33 ? 193  PRO C N   1 
ATOM   9124  C  CA  . PRO C 2 216 ? 80.689  152.964 86.669  1.00 161.48 ? 193  PRO C CA  1 
ATOM   9125  C  C   . PRO C 2 216 ? 81.435  152.201 87.752  1.00 161.78 ? 193  PRO C C   1 
ATOM   9126  O  O   . PRO C 2 216 ? 81.180  151.021 88.004  1.00 161.27 ? 193  PRO C O   1 
ATOM   9127  C  CB  . PRO C 2 216 ? 79.345  153.497 87.182  1.00 160.73 ? 193  PRO C CB  1 
ATOM   9128  C  CG  . PRO C 2 216 ? 78.323  152.532 86.671  1.00 160.79 ? 193  PRO C CG  1 
ATOM   9129  C  CD  . PRO C 2 216 ? 78.849  152.053 85.356  1.00 160.76 ? 193  PRO C CD  1 
ATOM   9130  N  N   . VAL C 2 217 ? 82.376  152.897 88.394  1.00 149.70 ? 194  VAL C N   1 
ATOM   9131  C  CA  . VAL C 2 217 ? 83.213  152.269 89.406  1.00 148.11 ? 194  VAL C CA  1 
ATOM   9132  C  C   . VAL C 2 217 ? 82.376  151.897 90.624  1.00 148.23 ? 194  VAL C C   1 
ATOM   9133  O  O   . VAL C 2 217 ? 81.414  152.588 90.987  1.00 147.51 ? 194  VAL C O   1 
ATOM   9134  C  CB  . VAL C 2 217 ? 84.376  153.197 89.802  1.00 146.88 ? 194  VAL C CB  1 
ATOM   9135  C  CG1 . VAL C 2 217 ? 85.416  153.249 88.696  1.00 147.06 ? 194  VAL C CG1 1 
ATOM   9136  C  CG2 . VAL C 2 217 ? 83.858  154.592 90.118  1.00 147.54 ? 194  VAL C CG2 1 
ATOM   9137  N  N   . ILE C 2 218 ? 82.744  150.789 91.260  1.00 148.61 ? 195  ILE C N   1 
ATOM   9138  C  CA  . ILE C 2 218 ? 82.166  150.370 92.530  1.00 148.09 ? 195  ILE C CA  1 
ATOM   9139  C  C   . ILE C 2 218 ? 83.217  150.602 93.604  1.00 147.52 ? 195  ILE C C   1 
ATOM   9140  O  O   . ILE C 2 218 ? 84.318  150.041 93.536  1.00 146.68 ? 195  ILE C O   1 
ATOM   9141  C  CB  . ILE C 2 218 ? 81.719  148.901 92.501  1.00 147.60 ? 195  ILE C CB  1 
ATOM   9142  C  CG1 . ILE C 2 218 ? 80.806  148.642 91.302  1.00 147.21 ? 195  ILE C CG1 1 
ATOM   9143  C  CG2 . ILE C 2 218 ? 81.015  148.535 93.799  1.00 147.04 ? 195  ILE C CG2 1 
ATOM   9144  C  CD1 . ILE C 2 218 ? 80.106  147.300 91.349  1.00 146.75 ? 195  ILE C CD1 1 
ATOM   9145  N  N   . GLU C 2 219 ? 82.883  151.430 94.588  1.00 149.13 ? 196  GLU C N   1 
ATOM   9146  C  CA  . GLU C 2 219 ? 83.801  151.793 95.657  1.00 148.67 ? 196  GLU C CA  1 
ATOM   9147  C  C   . GLU C 2 219 ? 83.306  151.227 96.980  1.00 148.50 ? 196  GLU C C   1 
ATOM   9148  O  O   . GLU C 2 219 ? 82.118  151.323 97.304  1.00 148.49 ? 196  GLU C O   1 
ATOM   9149  C  CB  . GLU C 2 219 ? 83.953  153.315 95.758  1.00 148.52 ? 196  GLU C CB  1 
ATOM   9150  C  CG  . GLU C 2 219 ? 82.640  154.081 95.739  1.00 148.81 ? 196  GLU C CG  1 
ATOM   9151  C  CD  . GLU C 2 219 ? 82.224  154.488 94.339  1.00 149.26 ? 196  GLU C CD  1 
ATOM   9152  O  OE1 . GLU C 2 219 ? 82.974  154.189 93.385  1.00 149.05 ? 196  GLU C OE1 1 
ATOM   9153  O  OE2 . GLU C 2 219 ? 81.148  155.105 94.191  1.00 149.14 ? 196  GLU C OE2 1 
ATOM   9154  N  N   . ARG C 2 220 ? 84.223  150.633 97.739  1.00 139.52 ? 197  ARG C N   1 
ATOM   9155  C  CA  . ARG C 2 220 ? 83.915  150.023 99.025  1.00 138.53 ? 197  ARG C CA  1 
ATOM   9156  C  C   . ARG C 2 220 ? 84.808  150.640 100.090 1.00 137.86 ? 197  ARG C C   1 
ATOM   9157  O  O   . ARG C 2 220 ? 86.038  150.624 99.959  1.00 138.27 ? 197  ARG C O   1 
ATOM   9158  C  CB  . ARG C 2 220 ? 84.109  148.507 98.978  1.00 138.11 ? 197  ARG C CB  1 
ATOM   9159  C  CG  . ARG C 2 220 ? 83.864  147.813 100.305 1.00 137.37 ? 197  ARG C CG  1 
ATOM   9160  C  CD  . ARG C 2 220 ? 82.394  147.480 100.494 1.00 137.92 ? 197  ARG C CD  1 
ATOM   9161  N  NE  . ARG C 2 220 ? 82.208  146.332 101.372 1.00 139.37 ? 197  ARG C NE  1 
ATOM   9162  C  CZ  . ARG C 2 220 ? 82.345  145.069 100.992 1.00 138.71 ? 197  ARG C CZ  1 
ATOM   9163  N  NH1 . ARG C 2 220 ? 82.662  144.752 99.748  1.00 137.30 ? 197  ARG C NH1 1 
ATOM   9164  N  NH2 . ARG C 2 220 ? 82.158  144.100 101.884 1.00 138.19 ? 197  ARG C NH2 1 
ATOM   9165  N  N   . TYR C 2 221 ? 84.184  151.179 101.139 1.00 139.99 ? 198  TYR C N   1 
ATOM   9166  C  CA  . TYR C 2 221 ? 84.875  151.724 102.307 1.00 139.82 ? 198  TYR C CA  1 
ATOM   9167  C  C   . TYR C 2 221 ? 84.413  150.925 103.518 1.00 139.95 ? 198  TYR C C   1 
ATOM   9168  O  O   . TYR C 2 221 ? 83.369  151.236 104.114 1.00 140.01 ? 198  TYR C O   1 
ATOM   9169  C  CB  . TYR C 2 221 ? 84.579  153.211 102.490 1.00 138.84 ? 198  TYR C CB  1 
ATOM   9170  C  CG  . TYR C 2 221 ? 84.800  154.057 101.256 1.00 139.96 ? 198  TYR C CG  1 
ATOM   9171  C  CD1 . TYR C 2 221 ? 86.050  154.585 100.966 1.00 140.66 ? 198  TYR C CD1 1 
ATOM   9172  C  CD2 . TYR C 2 221 ? 83.753  154.340 100.389 1.00 140.11 ? 198  TYR C CD2 1 
ATOM   9173  C  CE1 . TYR C 2 221 ? 86.254  155.364 99.842  1.00 140.54 ? 198  TYR C CE1 1 
ATOM   9174  C  CE2 . TYR C 2 221 ? 83.947  155.118 99.263  1.00 139.76 ? 198  TYR C CE2 1 
ATOM   9175  C  CZ  . TYR C 2 221 ? 85.199  155.627 98.995  1.00 140.29 ? 198  TYR C CZ  1 
ATOM   9176  O  OH  . TYR C 2 221 ? 85.397  156.401 97.876  1.00 139.85 ? 198  TYR C OH  1 
ATOM   9177  N  N   . PRO C 2 222 ? 85.144  149.880 103.907 1.00 132.11 ? 199  PRO C N   1 
ATOM   9178  C  CA  . PRO C 2 222 ? 84.723  149.077 105.061 1.00 131.65 ? 199  PRO C CA  1 
ATOM   9179  C  C   . PRO C 2 222 ? 84.665  149.914 106.332 1.00 131.65 ? 199  PRO C C   1 
ATOM   9180  O  O   . PRO C 2 222 ? 85.492  150.800 106.555 1.00 131.01 ? 199  PRO C O   1 
ATOM   9181  C  CB  . PRO C 2 222 ? 85.798  147.987 105.150 1.00 131.40 ? 199  PRO C CB  1 
ATOM   9182  C  CG  . PRO C 2 222 ? 86.951  148.503 104.350 1.00 131.05 ? 199  PRO C CG  1 
ATOM   9183  C  CD  . PRO C 2 222 ? 86.360  149.350 103.273 1.00 131.29 ? 199  PRO C CD  1 
ATOM   9184  N  N   . ALA C 2 223 ? 83.670  149.621 107.164 1.00 130.90 ? 200  ALA C N   1 
ATOM   9185  C  CA  . ALA C 2 223 ? 83.451  150.392 108.378 1.00 130.64 ? 200  ALA C CA  1 
ATOM   9186  C  C   . ALA C 2 223 ? 84.495  150.055 109.437 1.00 130.90 ? 200  ALA C C   1 
ATOM   9187  O  O   . ALA C 2 223 ? 85.007  148.935 109.506 1.00 130.47 ? 200  ALA C O   1 
ATOM   9188  C  CB  . ALA C 2 223 ? 82.048  150.136 108.926 1.00 129.62 ? 200  ALA C CB  1 
ATOM   9189  N  N   . GLY C 2 224 ? 84.807  151.047 110.269 1.00 141.68 ? 201  GLY C N   1 
ATOM   9190  C  CA  . GLY C 2 224 ? 85.760  150.864 111.344 1.00 141.24 ? 201  GLY C CA  1 
ATOM   9191  C  C   . GLY C 2 224 ? 87.197  151.011 110.885 1.00 142.18 ? 201  GLY C C   1 
ATOM   9192  O  O   . GLY C 2 224 ? 87.503  151.206 109.707 1.00 141.95 ? 201  GLY C O   1 
ATOM   9193  N  N   . ARG C 2 225 ? 88.127  151.006 111.830 1.00 142.55 ? 232  ARG C N   1 
ATOM   9194  C  CA  . ARG C 2 225 ? 89.538  151.197 111.426 1.00 141.50 ? 232  ARG C CA  1 
ATOM   9195  C  C   . ARG C 2 225 ? 90.109  149.813 111.081 1.00 140.57 ? 232  ARG C C   1 
ATOM   9196  O  O   . ARG C 2 225 ? 90.000  148.893 111.910 1.00 139.81 ? 232  ARG C O   1 
ATOM   9197  C  CB  . ARG C 2 225 ? 90.234  152.124 112.426 1.00 141.65 ? 232  ARG C CB  1 
ATOM   9198  C  CG  . ARG C 2 225 ? 89.696  152.112 113.854 1.00 140.65 ? 232  ARG C CG  1 
ATOM   9199  C  CD  . ARG C 2 225 ? 90.717  152.612 114.866 1.00 141.18 ? 232  ARG C CD  1 
ATOM   9200  N  NE  . ARG C 2 225 ? 91.924  153.074 114.185 1.00 142.45 ? 232  ARG C NE  1 
ATOM   9201  C  CZ  . ARG C 2 225 ? 92.781  154.005 114.574 1.00 141.84 ? 232  ARG C CZ  1 
ATOM   9202  N  NH1 . ARG C 2 225 ? 92.636  154.608 115.737 1.00 140.88 ? 232  ARG C NH1 1 
ATOM   9203  N  NH2 . ARG C 2 225 ? 93.785  154.326 113.780 1.00 141.74 ? 232  ARG C NH2 1 
ATOM   9204  N  N   . GLN C 2 226 ? 90.511  149.645 109.821 1.00 122.35 ? 233  GLN C N   1 
ATOM   9205  C  CA  . GLN C 2 226 ? 90.930  148.427 109.146 1.00 121.72 ? 233  GLN C CA  1 
ATOM   9206  C  C   . GLN C 2 226 ? 92.441  148.412 108.954 1.00 120.63 ? 233  GLN C C   1 
ATOM   9207  O  O   . GLN C 2 226 ? 93.070  149.453 108.749 1.00 120.13 ? 233  GLN C O   1 
ATOM   9208  C  CB  . GLN C 2 226 ? 90.242  148.289 107.782 1.00 120.27 ? 233  GLN C CB  1 
ATOM   9209  C  CG  . GLN C 2 226 ? 88.729  148.532 107.755 1.00 121.97 ? 233  GLN C CG  1 
ATOM   9210  C  CD  . GLN C 2 226 ? 87.943  147.640 108.707 1.00 123.62 ? 233  GLN C CD  1 
ATOM   9211  O  OE1 . GLN C 2 226 ? 88.012  147.783 109.927 1.00 123.55 ? 233  GLN C OE1 1 
ATOM   9212  N  NE2 . GLN C 2 226 ? 87.188  146.706 108.140 1.00 123.06 ? 233  GLN C NE2 1 
ATOM   9213  N  N   . LEU C 2 227 ? 93.017  147.215 109.031 1.00 89.33  ? 234  LEU C N   1 
ATOM   9214  C  CA  . LEU C 2 227 ? 94.419  147.033 108.689 1.00 85.54  ? 234  LEU C CA  1 
ATOM   9215  C  C   . LEU C 2 227 ? 94.641  147.315 107.207 1.00 86.10  ? 234  LEU C C   1 
ATOM   9216  O  O   . LEU C 2 227 ? 93.749  147.129 106.375 1.00 89.39  ? 234  LEU C O   1 
ATOM   9217  C  CB  . LEU C 2 227 ? 94.878  145.616 109.038 1.00 86.33  ? 234  LEU C CB  1 
ATOM   9218  C  CG  . LEU C 2 227 ? 95.519  145.387 110.409 1.00 83.72  ? 234  LEU C CG  1 
ATOM   9219  C  CD1 . LEU C 2 227 ? 96.920  145.955 110.411 1.00 82.41  ? 234  LEU C CD1 1 
ATOM   9220  C  CD2 . LEU C 2 227 ? 94.708  146.011 111.530 1.00 85.67  ? 234  LEU C CD2 1 
ATOM   9221  N  N   . THR C 2 228 ? 95.844  147.777 106.881 1.00 70.46  ? 235  THR C N   1 
ATOM   9222  C  CA  . THR C 2 228 ? 96.138  148.283 105.546 1.00 69.52  ? 235  THR C CA  1 
ATOM   9223  C  C   . THR C 2 228 ? 97.248  147.533 104.828 1.00 70.22  ? 235  THR C C   1 
ATOM   9224  O  O   . THR C 2 228 ? 97.128  147.271 103.629 1.00 75.06  ? 235  THR C O   1 
ATOM   9225  C  CB  . THR C 2 228 ? 96.515  149.770 105.622 1.00 67.28  ? 235  THR C CB  1 
ATOM   9226  O  OG1 . THR C 2 228 ? 97.760  149.911 106.317 1.00 66.52  ? 235  THR C OG1 1 
ATOM   9227  C  CG2 . THR C 2 228 ? 95.442  150.557 106.357 1.00 67.49  ? 235  THR C CG2 1 
ATOM   9228  N  N   . ILE C 2 229 ? 98.323  147.177 105.523 1.00 57.70  ? 236  ILE C N   1 
ATOM   9229  C  CA  . ILE C 2 229 ? 99.536  146.706 104.863 1.00 56.65  ? 236  ILE C CA  1 
ATOM   9230  C  C   . ILE C 2 229 ? 99.362  145.259 104.421 1.00 59.48  ? 236  ILE C C   1 
ATOM   9231  O  O   . ILE C 2 229 ? 98.938  144.401 105.204 1.00 60.70  ? 236  ILE C O   1 
ATOM   9232  C  CB  . ILE C 2 229 ? 100.750 146.858 105.790 1.00 52.75  ? 236  ILE C CB  1 
ATOM   9233  C  CG1 . ILE C 2 229 ? 100.900 148.315 106.224 1.00 54.13  ? 236  ILE C CG1 1 
ATOM   9234  C  CG2 . ILE C 2 229 ? 102.013 146.385 105.094 1.00 56.90  ? 236  ILE C CG2 1 
ATOM   9235  C  CD1 . ILE C 2 229 ? 101.332 149.233 105.111 1.00 58.29  ? 236  ILE C CD1 1 
ATOM   9236  N  N   . PHE C 2 230 ? 99.691  144.990 103.158 1.00 66.76  ? 237  PHE C N   1 
ATOM   9237  C  CA  . PHE C 2 230 ? 99.757  143.635 102.621 1.00 64.64  ? 237  PHE C CA  1 
ATOM   9238  C  C   . PHE C 2 230 ? 101.162 143.105 102.879 1.00 64.87  ? 237  PHE C C   1 
ATOM   9239  O  O   . PHE C 2 230 ? 102.117 143.510 102.209 1.00 70.82  ? 237  PHE C O   1 
ATOM   9240  C  CB  . PHE C 2 230 ? 99.431  143.639 101.131 1.00 67.41  ? 237  PHE C CB  1 
ATOM   9241  C  CG  . PHE C 2 230 ? 98.911  142.330 100.612 1.00 67.99  ? 237  PHE C CG  1 
ATOM   9242  C  CD1 . PHE C 2 230 ? 99.635  141.162 100.774 1.00 68.27  ? 237  PHE C CD1 1 
ATOM   9243  C  CD2 . PHE C 2 230 ? 97.700  142.272 99.946  1.00 69.08  ? 237  PHE C CD2 1 
ATOM   9244  C  CE1 . PHE C 2 230 ? 99.156  139.962 100.291 1.00 71.24  ? 237  PHE C CE1 1 
ATOM   9245  C  CE2 . PHE C 2 230 ? 97.218  141.077 99.461  1.00 71.72  ? 237  PHE C CE2 1 
ATOM   9246  C  CZ  . PHE C 2 230 ? 97.947  139.920 99.633  1.00 72.97  ? 237  PHE C CZ  1 
ATOM   9247  N  N   . ASN C 2 231 ? 101.292 142.195 103.840 1.00 62.70  ? 238  ASN C N   1 
ATOM   9248  C  CA  . ASN C 2 231 ? 102.594 141.821 104.383 1.00 64.17  ? 238  ASN C CA  1 
ATOM   9249  C  C   . ASN C 2 231 ? 103.218 140.708 103.548 1.00 66.02  ? 238  ASN C C   1 
ATOM   9250  O  O   . ASN C 2 231 ? 102.700 139.588 103.504 1.00 67.49  ? 238  ASN C O   1 
ATOM   9251  C  CB  . ASN C 2 231 ? 102.459 141.390 105.840 1.00 62.67  ? 238  ASN C CB  1 
ATOM   9252  C  CG  . ASN C 2 231 ? 101.922 142.493 106.723 1.00 65.30  ? 238  ASN C CG  1 
ATOM   9253  O  OD1 . ASN C 2 231 ? 100.738 142.513 107.061 1.00 66.56  ? 238  ASN C OD1 1 
ATOM   9254  N  ND2 . ASN C 2 231 ? 102.790 143.424 107.101 1.00 64.58  ? 238  ASN C ND2 1 
ATOM   9255  N  N   . SER C 2 232 ? 104.337 141.023 102.892 1.00 74.28  ? 239  SER C N   1 
ATOM   9256  C  CA  . SER C 2 232 ? 105.258 140.038 102.326 1.00 70.97  ? 239  SER C CA  1 
ATOM   9257  C  C   . SER C 2 232 ? 104.558 139.118 101.320 1.00 76.41  ? 239  SER C C   1 
ATOM   9258  O  O   . SER C 2 232 ? 104.398 137.915 101.535 1.00 80.92  ? 239  SER C O   1 
ATOM   9259  C  CB  . SER C 2 232 ? 105.924 139.225 103.442 1.00 68.81  ? 239  SER C CB  1 
ATOM   9260  O  OG  . SER C 2 232 ? 106.724 138.187 102.907 1.00 74.54  ? 239  SER C OG  1 
ATOM   9261  N  N   . GLN C 2 233 ? 104.134 139.723 100.212 1.00 80.41  ? 240  GLN C N   1 
ATOM   9262  C  CA  . GLN C 2 233 ? 103.637 138.938 99.090  1.00 78.66  ? 240  GLN C CA  1 
ATOM   9263  C  C   . GLN C 2 233 ? 104.720 137.987 98.601  1.00 83.74  ? 240  GLN C C   1 
ATOM   9264  O  O   . GLN C 2 233 ? 105.875 138.380 98.420  1.00 85.52  ? 240  GLN C O   1 
ATOM   9265  C  CB  . GLN C 2 233 ? 103.201 139.854 97.948  1.00 79.38  ? 240  GLN C CB  1 
ATOM   9266  C  CG  . GLN C 2 233 ? 101.842 140.484 98.136  1.00 81.55  ? 240  GLN C CG  1 
ATOM   9267  C  CD  . GLN C 2 233 ? 101.840 141.961 97.813  1.00 82.98  ? 240  GLN C CD  1 
ATOM   9268  O  OE1 . GLN C 2 233 ? 102.874 142.537 97.477  1.00 82.52  ? 240  GLN C OE1 1 
ATOM   9269  N  NE2 . GLN C 2 233 ? 100.673 142.585 97.910  1.00 83.10  ? 240  GLN C NE2 1 
ATOM   9270  N  N   . ALA C 2 234 ? 104.349 136.729 98.383  1.00 91.78  ? 241  ALA C N   1 
ATOM   9271  C  CA  . ALA C 2 234 ? 105.317 135.723 97.965  1.00 89.55  ? 241  ALA C CA  1 
ATOM   9272  C  C   . ALA C 2 234 ? 104.986 135.078 96.632  1.00 90.25  ? 241  ALA C C   1 
ATOM   9273  O  O   . ALA C 2 234 ? 105.891 134.837 95.829  1.00 90.17  ? 241  ALA C O   1 
ATOM   9274  C  CB  . ALA C 2 234 ? 105.445 134.632 99.038  1.00 88.89  ? 241  ALA C CB  1 
ATOM   9275  N  N   . THR C 2 235 ? 103.714 134.791 96.368  1.00 99.93  ? 242  THR C N   1 
ATOM   9276  C  CA  . THR C 2 235 ? 103.311 134.071 95.171  1.00 99.57  ? 242  THR C CA  1 
ATOM   9277  C  C   . THR C 2 235 ? 102.196 134.826 94.465  1.00 99.26  ? 242  THR C C   1 
ATOM   9278  O  O   . THR C 2 235 ? 101.401 135.524 95.100  1.00 98.34  ? 242  THR C O   1 
ATOM   9279  C  CB  . THR C 2 235 ? 102.811 132.656 95.500  1.00 100.45 ? 242  THR C CB  1 
ATOM   9280  O  OG1 . THR C 2 235 ? 101.687 132.742 96.384  1.00 101.59 ? 242  THR C OG1 1 
ATOM   9281  C  CG2 . THR C 2 235 ? 103.897 131.859 96.190  1.00 99.17  ? 242  THR C CG2 1 
ATOM   9282  N  N   . ILE C 2 236 ? 102.146 134.685 93.143  1.00 106.22 ? 243  ILE C N   1 
ATOM   9283  C  CA  . ILE C 2 236 ? 100.958 135.047 92.378  1.00 105.77 ? 243  ILE C CA  1 
ATOM   9284  C  C   . ILE C 2 236 ? 100.543 133.835 91.554  1.00 107.13 ? 243  ILE C C   1 
ATOM   9285  O  O   . ILE C 2 236 ? 101.388 133.136 90.979  1.00 108.80 ? 243  ILE C O   1 
ATOM   9286  C  CB  . ILE C 2 236 ? 101.161 136.303 91.497  1.00 103.74 ? 243  ILE C CB  1 
ATOM   9287  C  CG1 . ILE C 2 236 ? 99.838  137.050 91.338  1.00 105.65 ? 243  ILE C CG1 1 
ATOM   9288  C  CG2 . ILE C 2 236 ? 101.653 135.960 90.119  1.00 105.10 ? 243  ILE C CG2 1 
ATOM   9289  C  CD1 . ILE C 2 236 ? 99.986  138.432 90.746  1.00 106.25 ? 243  ILE C CD1 1 
ATOM   9290  N  N   . ILE C 2 237 ? 99.241  133.561 91.550  1.00 113.20 ? 244  ILE C N   1 
ATOM   9291  C  CA  . ILE C 2 237 ? 98.672  132.360 90.952  1.00 113.86 ? 244  ILE C CA  1 
ATOM   9292  C  C   . ILE C 2 237 ? 97.656  132.783 89.902  1.00 114.78 ? 244  ILE C C   1 
ATOM   9293  O  O   . ILE C 2 237 ? 96.756  133.579 90.191  1.00 113.89 ? 244  ILE C O   1 
ATOM   9294  C  CB  . ILE C 2 237 ? 98.009  131.462 92.014  1.00 113.53 ? 244  ILE C CB  1 
ATOM   9295  C  CG1 . ILE C 2 237 ? 99.053  130.933 92.999  1.00 114.00 ? 244  ILE C CG1 1 
ATOM   9296  C  CG2 . ILE C 2 237 ? 97.257  130.317 91.356  1.00 113.58 ? 244  ILE C CG2 1 
ATOM   9297  C  CD1 . ILE C 2 237 ? 100.163 130.152 92.348  1.00 112.64 ? 244  ILE C CD1 1 
ATOM   9298  N  N   . ILE C 2 238 ? 97.798  132.251 88.691  1.00 124.64 ? 245  ILE C N   1 
ATOM   9299  C  CA  . ILE C 2 238 ? 96.867  132.505 87.598  1.00 124.53 ? 245  ILE C CA  1 
ATOM   9300  C  C   . ILE C 2 238 ? 96.267  131.169 87.187  1.00 125.41 ? 245  ILE C C   1 
ATOM   9301  O  O   . ILE C 2 238 ? 96.996  130.256 86.777  1.00 125.25 ? 245  ILE C O   1 
ATOM   9302  C  CB  . ILE C 2 238 ? 97.555  133.186 86.406  1.00 124.92 ? 245  ILE C CB  1 
ATOM   9303  C  CG1 . ILE C 2 238 ? 98.663  134.121 86.891  1.00 123.90 ? 245  ILE C CG1 1 
ATOM   9304  C  CG2 . ILE C 2 238 ? 96.541  133.962 85.585  1.00 125.21 ? 245  ILE C CG2 1 
ATOM   9305  C  CD1 . ILE C 2 238 ? 99.567  134.613 85.787  1.00 123.92 ? 245  ILE C CD1 1 
ATOM   9306  N  N   . GLY C 2 239 ? 94.946  131.057 87.295  1.00 125.90 ? 246  GLY C N   1 
ATOM   9307  C  CA  . GLY C 2 239 ? 94.247  129.828 86.973  1.00 126.56 ? 246  GLY C CA  1 
ATOM   9308  C  C   . GLY C 2 239 ? 93.589  129.203 88.186  1.00 126.35 ? 246  GLY C C   1 
ATOM   9309  O  O   . GLY C 2 239 ? 92.442  128.749 88.115  1.00 126.82 ? 246  GLY C O   1 
ATOM   9310  N  N   . GLY C 2 240 ? 94.305  129.183 89.305  1.00 134.05 ? 247  GLY C N   1 
ATOM   9311  C  CA  . GLY C 2 240 ? 93.739  128.709 90.560  1.00 134.74 ? 247  GLY C CA  1 
ATOM   9312  C  C   . GLY C 2 240 ? 93.279  127.268 90.553  1.00 134.61 ? 247  GLY C C   1 
ATOM   9313  O  O   . GLY C 2 240 ? 92.197  126.963 91.071  1.00 133.31 ? 247  GLY C O   1 
ATOM   9314  N  N   . LYS C 2 241 ? 94.076  126.368 89.974  1.00 140.69 ? 248  LYS C N   1 
ATOM   9315  C  CA  . LYS C 2 241 ? 93.732  124.951 90.024  1.00 140.97 ? 248  LYS C CA  1 
ATOM   9316  C  C   . LYS C 2 241 ? 93.895  124.387 91.430  1.00 141.58 ? 248  LYS C C   1 
ATOM   9317  O  O   . LYS C 2 241 ? 93.219  123.416 91.789  1.00 141.42 ? 248  LYS C O   1 
ATOM   9318  C  CB  . LYS C 2 241 ? 94.589  124.164 89.033  1.00 140.84 ? 248  LYS C CB  1 
ATOM   9319  C  CG  . LYS C 2 241 ? 93.966  122.857 88.572  1.00 140.58 ? 248  LYS C CG  1 
ATOM   9320  C  CD  . LYS C 2 241 ? 94.826  122.180 87.518  1.00 140.64 ? 248  LYS C CD  1 
ATOM   9321  C  CE  . LYS C 2 241 ? 94.158  120.923 86.988  1.00 140.74 ? 248  LYS C CE  1 
ATOM   9322  N  NZ  . LYS C 2 241 ? 92.873  121.227 86.303  1.00 140.40 ? 248  LYS C NZ  1 
ATOM   9323  N  N   . GLU C 2 242 ? 94.784  124.976 92.233  1.00 141.55 ? 249  GLU C N   1 
ATOM   9324  C  CA  . GLU C 2 242 ? 94.967  124.514 93.605  1.00 140.92 ? 249  GLU C CA  1 
ATOM   9325  C  C   . GLU C 2 242 ? 93.767  124.852 94.479  1.00 140.72 ? 249  GLU C C   1 
ATOM   9326  O  O   . GLU C 2 242 ? 93.426  124.083 95.384  1.00 140.83 ? 249  GLU C O   1 
ATOM   9327  C  CB  . GLU C 2 242 ? 96.238  125.119 94.198  1.00 140.34 ? 249  GLU C CB  1 
ATOM   9328  C  CG  . GLU C 2 242 ? 97.513  124.723 93.476  1.00 140.77 ? 249  GLU C CG  1 
ATOM   9329  C  CD  . GLU C 2 242 ? 98.743  125.379 94.068  1.00 141.37 ? 249  GLU C CD  1 
ATOM   9330  O  OE1 . GLU C 2 242 ? 98.613  126.060 95.107  1.00 141.40 ? 249  GLU C OE1 1 
ATOM   9331  O  OE2 . GLU C 2 242 ? 99.841  125.216 93.494  1.00 141.24 ? 249  GLU C OE2 1 
ATOM   9332  N  N   . GLN C 2 243 ? 93.125  125.997 94.233  1.00 135.24 ? 250  GLN C N   1 
ATOM   9333  C  CA  . GLN C 2 243 ? 91.980  126.395 95.046  1.00 135.44 ? 250  GLN C CA  1 
ATOM   9334  C  C   . GLN C 2 243 ? 90.820  125.422 94.883  1.00 136.00 ? 250  GLN C C   1 
ATOM   9335  O  O   . GLN C 2 243 ? 90.137  125.088 95.859  1.00 136.33 ? 250  GLN C O   1 
ATOM   9336  C  CB  . GLN C 2 243 ? 91.545  127.815 94.681  1.00 135.12 ? 250  GLN C CB  1 
ATOM   9337  C  CG  . GLN C 2 243 ? 92.282  128.906 95.441  1.00 134.76 ? 250  GLN C CG  1 
ATOM   9338  C  CD  . GLN C 2 243 ? 93.753  128.974 95.081  1.00 135.74 ? 250  GLN C CD  1 
ATOM   9339  O  OE1 . GLN C 2 243 ? 94.140  128.698 93.946  1.00 136.14 ? 250  GLN C OE1 1 
ATOM   9340  N  NE2 . GLN C 2 243 ? 94.583  129.344 96.050  1.00 135.03 ? 250  GLN C NE2 1 
ATOM   9341  N  N   . GLY C 2 244 ? 90.579  124.957 93.660  1.00 131.82 ? 251  GLY C N   1 
ATOM   9342  C  CA  . GLY C 2 244 ? 89.508  124.013 93.413  1.00 131.53 ? 251  GLY C CA  1 
ATOM   9343  C  C   . GLY C 2 244 ? 88.618  124.405 92.253  1.00 131.74 ? 251  GLY C C   1 
ATOM   9344  O  O   . GLY C 2 244 ? 87.816  123.597 91.777  1.00 131.41 ? 251  GLY C O   1 
ATOM   9345  N  N   . GLN C 2 245 ? 88.749  125.647 91.789  1.00 129.89 ? 252  GLN C N   1 
ATOM   9346  C  CA  . GLN C 2 245 ? 87.963  126.144 90.664  1.00 130.15 ? 252  GLN C CA  1 
ATOM   9347  C  C   . GLN C 2 245 ? 88.882  126.412 89.482  1.00 129.89 ? 252  GLN C C   1 
ATOM   9348  O  O   . GLN C 2 245 ? 89.570  127.444 89.452  1.00 129.85 ? 252  GLN C O   1 
ATOM   9349  C  CB  . GLN C 2 245 ? 87.202  127.415 91.052  1.00 129.01 ? 252  GLN C CB  1 
ATOM   9350  C  CG  . GLN C 2 245 ? 85.967  127.164 91.901  1.00 128.89 ? 252  GLN C CG  1 
ATOM   9351  C  CD  . GLN C 2 245 ? 86.297  126.973 93.368  1.00 129.90 ? 252  GLN C CD  1 
ATOM   9352  O  OE1 . GLN C 2 245 ? 87.387  127.324 93.821  1.00 129.77 ? 252  GLN C OE1 1 
ATOM   9353  N  NE2 . GLN C 2 245 ? 85.356  126.414 94.118  1.00 129.89 ? 252  GLN C NE2 1 
ATOM   9354  N  N   . PRO C 2 246 ? 88.938  125.525 88.492  1.00 132.68 ? 253  PRO C N   1 
ATOM   9355  C  CA  . PRO C 2 246 ? 89.806  125.763 87.336  1.00 132.49 ? 253  PRO C CA  1 
ATOM   9356  C  C   . PRO C 2 246 ? 89.268  126.879 86.456  1.00 132.78 ? 253  PRO C C   1 
ATOM   9357  O  O   . PRO C 2 246 ? 88.115  127.303 86.567  1.00 131.65 ? 253  PRO C O   1 
ATOM   9358  C  CB  . PRO C 2 246 ? 89.798  124.420 86.593  1.00 132.03 ? 253  PRO C CB  1 
ATOM   9359  C  CG  . PRO C 2 246 ? 89.202  123.430 87.556  1.00 132.29 ? 253  PRO C CG  1 
ATOM   9360  C  CD  . PRO C 2 246 ? 88.275  124.214 88.423  1.00 132.65 ? 253  PRO C CD  1 
ATOM   9361  N  N   . PHE C 2 247 ? 90.133  127.357 85.568  1.00 132.48 ? 254  PHE C N   1 
ATOM   9362  C  CA  . PHE C 2 247 ? 89.790  128.404 84.618  1.00 132.74 ? 254  PHE C CA  1 
ATOM   9363  C  C   . PHE C 2 247 ? 89.946  127.876 83.199  1.00 133.31 ? 254  PHE C C   1 
ATOM   9364  O  O   . PHE C 2 247 ? 90.893  127.141 82.902  1.00 132.54 ? 254  PHE C O   1 
ATOM   9365  C  CB  . PHE C 2 247 ? 90.666  129.644 84.812  1.00 131.65 ? 254  PHE C CB  1 
ATOM   9366  C  CG  . PHE C 2 247 ? 90.141  130.866 84.118  1.00 131.76 ? 254  PHE C CG  1 
ATOM   9367  C  CD1 . PHE C 2 247 ? 88.951  131.448 84.520  1.00 131.66 ? 254  PHE C CD1 1 
ATOM   9368  C  CD2 . PHE C 2 247 ? 90.831  131.427 83.058  1.00 131.36 ? 254  PHE C CD2 1 
ATOM   9369  C  CE1 . PHE C 2 247 ? 88.463  132.571 83.884  1.00 131.01 ? 254  PHE C CE1 1 
ATOM   9370  C  CE2 . PHE C 2 247 ? 90.346  132.550 82.416  1.00 132.09 ? 254  PHE C CE2 1 
ATOM   9371  C  CZ  . PHE C 2 247 ? 89.160  133.122 82.830  1.00 131.39 ? 254  PHE C CZ  1 
ATOM   9372  N  N   . GLN C 2 248 ? 89.007  128.246 82.329  1.00 137.83 ? 255  GLN C N   1 
ATOM   9373  C  CA  . GLN C 2 248 ? 89.054  127.865 80.916  1.00 137.04 ? 255  GLN C CA  1 
ATOM   9374  C  C   . GLN C 2 248 ? 88.629  129.080 80.096  1.00 136.85 ? 255  GLN C C   1 
ATOM   9375  O  O   . GLN C 2 248 ? 87.433  129.343 79.937  1.00 135.80 ? 255  GLN C O   1 
ATOM   9376  C  CB  . GLN C 2 248 ? 88.166  126.659 80.634  1.00 136.93 ? 255  GLN C CB  1 
ATOM   9377  C  CG  . GLN C 2 248 ? 88.726  125.717 79.579  1.00 136.75 ? 255  GLN C CG  1 
ATOM   9378  C  CD  . GLN C 2 248 ? 87.983  124.397 79.519  1.00 137.00 ? 255  GLN C CD  1 
ATOM   9379  O  OE1 . GLN C 2 248 ? 86.757  124.356 79.619  1.00 137.29 ? 255  GLN C OE1 1 
ATOM   9380  N  NE2 . GLN C 2 248 ? 88.724  123.308 79.353  1.00 136.46 ? 255  GLN C NE2 1 
ATOM   9381  N  N   . GLY C 2 249 ? 89.609  129.810 79.579  1.00 136.15 ? 256  GLY C N   1 
ATOM   9382  C  CA  . GLY C 2 249 ? 89.321  131.007 78.815  1.00 135.58 ? 256  GLY C CA  1 
ATOM   9383  C  C   . GLY C 2 249 ? 90.603  131.711 78.433  1.00 135.85 ? 256  GLY C C   1 
ATOM   9384  O  O   . GLY C 2 249 ? 91.701  131.177 78.606  1.00 134.71 ? 256  GLY C O   1 
ATOM   9385  N  N   . GLN C 2 250 ? 90.452  132.925 77.912  1.00 140.48 ? 257  GLN C N   1 
ATOM   9386  C  CA  . GLN C 2 250 ? 91.583  133.728 77.465  1.00 140.85 ? 257  GLN C CA  1 
ATOM   9387  C  C   . GLN C 2 250 ? 91.884  134.815 78.488  1.00 141.24 ? 257  GLN C C   1 
ATOM   9388  O  O   . GLN C 2 250 ? 90.976  135.529 78.931  1.00 140.64 ? 257  GLN C O   1 
ATOM   9389  C  CB  . GLN C 2 250 ? 91.306  134.353 76.096  1.00 140.15 ? 257  GLN C CB  1 
ATOM   9390  C  CG  . GLN C 2 250 ? 90.415  133.515 75.194  1.00 140.66 ? 257  GLN C CG  1 
ATOM   9391  C  CD  . GLN C 2 250 ? 90.678  133.762 73.721  1.00 140.08 ? 257  GLN C CD  1 
ATOM   9392  O  OE1 . GLN C 2 250 ? 91.790  134.114 73.328  1.00 140.02 ? 257  GLN C OE1 1 
ATOM   9393  N  NE2 . GLN C 2 250 ? 89.653  133.578 72.898  1.00 139.78 ? 257  GLN C NE2 1 
ATOM   9394  N  N   . LEU C 2 251 ? 93.158  134.931 78.861  1.00 135.29 ? 258  LEU C N   1 
ATOM   9395  C  CA  . LEU C 2 251 ? 93.641  135.937 79.797  1.00 133.54 ? 258  LEU C CA  1 
ATOM   9396  C  C   . LEU C 2 251 ? 94.769  136.728 79.152  1.00 133.90 ? 258  LEU C C   1 
ATOM   9397  O  O   . LEU C 2 251 ? 95.632  136.156 78.479  1.00 134.00 ? 258  LEU C O   1 
ATOM   9398  C  CB  . LEU C 2 251 ? 94.140  135.294 81.095  1.00 132.77 ? 258  LEU C CB  1 
ATOM   9399  C  CG  . LEU C 2 251 ? 93.091  134.688 82.026  1.00 134.06 ? 258  LEU C CG  1 
ATOM   9400  C  CD1 . LEU C 2 251 ? 93.760  133.937 83.164  1.00 133.40 ? 258  LEU C CD1 1 
ATOM   9401  C  CD2 . LEU C 2 251 ? 92.172  135.766 82.565  1.00 134.19 ? 258  LEU C CD2 1 
ATOM   9402  N  N   . SER C 2 252 ? 94.766  138.043 79.364  1.00 132.44 ? 259  SER C N   1 
ATOM   9403  C  CA  . SER C 2 252 ? 95.771  138.910 78.766  1.00 132.41 ? 259  SER C CA  1 
ATOM   9404  C  C   . SER C 2 252 ? 96.045  140.091 79.686  1.00 131.86 ? 259  SER C C   1 
ATOM   9405  O  O   . SER C 2 252 ? 95.221  140.454 80.531  1.00 131.86 ? 259  SER C O   1 
ATOM   9406  C  CB  . SER C 2 252 ? 95.333  139.412 77.385  1.00 131.52 ? 259  SER C CB  1 
ATOM   9407  O  OG  . SER C 2 252 ? 94.912  138.343 76.557  1.00 132.25 ? 259  SER C OG  1 
ATOM   9408  N  N   . GLY C 2 253 ? 97.225  140.682 79.507  1.00 131.68 ? 260  GLY C N   1 
ATOM   9409  C  CA  . GLY C 2 253 ? 97.598  141.921 80.164  1.00 131.95 ? 260  GLY C CA  1 
ATOM   9410  C  C   . GLY C 2 253 ? 97.412  141.955 81.666  1.00 131.63 ? 260  GLY C C   1 
ATOM   9411  O  O   . GLY C 2 253 ? 96.650  142.779 82.179  1.00 131.28 ? 260  GLY C O   1 
ATOM   9412  N  N   . LEU C 2 254 ? 98.100  141.073 82.385  1.00 125.64 ? 261  LEU C N   1 
ATOM   9413  C  CA  . LEU C 2 254 ? 98.034  141.063 83.842  1.00 125.16 ? 261  LEU C CA  1 
ATOM   9414  C  C   . LEU C 2 254 ? 98.973  142.141 84.370  1.00 125.70 ? 261  LEU C C   1 
ATOM   9415  O  O   . LEU C 2 254 ? 100.198 142.006 84.284  1.00 124.34 ? 261  LEU C O   1 
ATOM   9416  C  CB  . LEU C 2 254 ? 98.403  139.687 84.389  1.00 125.12 ? 261  LEU C CB  1 
ATOM   9417  C  CG  . LEU C 2 254 ? 98.749  139.573 85.878  1.00 124.54 ? 261  LEU C CG  1 
ATOM   9418  C  CD1 . LEU C 2 254 ? 97.672  140.208 86.749  1.00 123.45 ? 261  LEU C CD1 1 
ATOM   9419  C  CD2 . LEU C 2 254 ? 98.964  138.124 86.269  1.00 124.46 ? 261  LEU C CD2 1 
ATOM   9420  N  N   . TYR C 2 255 ? 98.402  143.213 84.911  1.00 122.91 ? 262  TYR C N   1 
ATOM   9421  C  CA  . TYR C 2 255 ? 99.164  144.331 85.453  1.00 120.59 ? 262  TYR C CA  1 
ATOM   9422  C  C   . TYR C 2 255 ? 99.000  144.340 86.967  1.00 121.03 ? 262  TYR C C   1 
ATOM   9423  O  O   . TYR C 2 255 ? 97.873  144.379 87.471  1.00 121.98 ? 262  TYR C O   1 
ATOM   9424  C  CB  . TYR C 2 255 ? 98.694  145.654 84.849  1.00 120.67 ? 262  TYR C CB  1 
ATOM   9425  C  CG  . TYR C 2 255 ? 99.256  146.879 85.532  1.00 122.24 ? 262  TYR C CG  1 
ATOM   9426  C  CD1 . TYR C 2 255 ? 100.561 147.289 85.298  1.00 122.10 ? 262  TYR C CD1 1 
ATOM   9427  C  CD2 . TYR C 2 255 ? 98.480  147.630 86.405  1.00 122.77 ? 262  TYR C CD2 1 
ATOM   9428  C  CE1 . TYR C 2 255 ? 101.079 148.409 85.916  1.00 121.16 ? 262  TYR C CE1 1 
ATOM   9429  C  CE2 . TYR C 2 255 ? 98.991  148.752 87.029  1.00 122.08 ? 262  TYR C CE2 1 
ATOM   9430  C  CZ  . TYR C 2 255 ? 100.291 149.136 86.781  1.00 121.37 ? 262  TYR C CZ  1 
ATOM   9431  O  OH  . TYR C 2 255 ? 100.806 150.252 87.399  1.00 121.76 ? 262  TYR C OH  1 
ATOM   9432  N  N   . TYR C 2 256 ? 100.121 144.301 87.686  1.00 110.11 ? 263  TYR C N   1 
ATOM   9433  C  CA  . TYR C 2 256 ? 100.106 144.251 89.148  1.00 109.68 ? 263  TYR C CA  1 
ATOM   9434  C  C   . TYR C 2 256 ? 101.285 145.067 89.669  1.00 109.53 ? 263  TYR C C   1 
ATOM   9435  O  O   . TYR C 2 256 ? 102.394 144.542 89.802  1.00 108.98 ? 263  TYR C O   1 
ATOM   9436  C  CB  . TYR C 2 256 ? 100.163 142.812 89.646  1.00 108.47 ? 263  TYR C CB  1 
ATOM   9437  C  CG  . TYR C 2 256 ? 100.081 142.680 91.149  1.00 108.60 ? 263  TYR C CG  1 
ATOM   9438  C  CD1 . TYR C 2 256 ? 98.866  142.794 91.810  1.00 109.20 ? 263  TYR C CD1 1 
ATOM   9439  C  CD2 . TYR C 2 256 ? 101.219 142.443 91.907  1.00 109.08 ? 263  TYR C CD2 1 
ATOM   9440  C  CE1 . TYR C 2 256 ? 98.786  142.677 93.184  1.00 109.43 ? 263  TYR C CE1 1 
ATOM   9441  C  CE2 . TYR C 2 256 ? 101.149 142.324 93.281  1.00 109.25 ? 263  TYR C CE2 1 
ATOM   9442  C  CZ  . TYR C 2 256 ? 99.930  142.441 93.913  1.00 109.14 ? 263  TYR C CZ  1 
ATOM   9443  O  OH  . TYR C 2 256 ? 99.856  142.323 95.281  1.00 108.03 ? 263  TYR C OH  1 
ATOM   9444  N  N   . ASN C 2 257 ? 101.036 146.340 89.975  1.00 113.82 ? 264  ASN C N   1 
ATOM   9445  C  CA  . ASN C 2 257 ? 102.039 147.230 90.559  1.00 114.12 ? 264  ASN C CA  1 
ATOM   9446  C  C   . ASN C 2 257 ? 103.279 147.329 89.672  1.00 116.90 ? 264  ASN C C   1 
ATOM   9447  O  O   . ASN C 2 257 ? 104.415 147.164 90.122  1.00 117.17 ? 264  ASN C O   1 
ATOM   9448  C  CB  . ASN C 2 257 ? 102.412 146.776 91.971  1.00 113.06 ? 264  ASN C CB  1 
ATOM   9449  C  CG  . ASN C 2 257 ? 101.257 146.893 92.942  1.00 112.60 ? 264  ASN C CG  1 
ATOM   9450  O  OD1 . ASN C 2 257 ? 100.104 147.045 92.539  1.00 113.47 ? 264  ASN C OD1 1 
ATOM   9451  N  ND2 . ASN C 2 257 ? 101.559 146.818 94.232  1.00 111.41 ? 264  ASN C ND2 1 
ATOM   9452  N  N   . GLY C 2 258 ? 103.052 147.604 88.389  1.00 127.40 ? 265  GLY C N   1 
ATOM   9453  C  CA  . GLY C 2 258 ? 104.133 147.697 87.431  1.00 126.39 ? 265  GLY C CA  1 
ATOM   9454  C  C   . GLY C 2 258 ? 104.645 146.372 86.915  1.00 126.25 ? 265  GLY C C   1 
ATOM   9455  O  O   . GLY C 2 258 ? 105.635 146.355 86.173  1.00 127.18 ? 265  GLY C O   1 
ATOM   9456  N  N   . LEU C 2 259 ? 104.008 145.266 87.283  1.00 123.21 ? 266  LEU C N   1 
ATOM   9457  C  CA  . LEU C 2 259 ? 104.456 143.931 86.916  1.00 123.04 ? 266  LEU C CA  1 
ATOM   9458  C  C   . LEU C 2 259 ? 103.526 143.341 85.864  1.00 125.61 ? 266  LEU C C   1 
ATOM   9459  O  O   . LEU C 2 259 ? 102.301 143.391 86.012  1.00 125.95 ? 266  LEU C O   1 
ATOM   9460  C  CB  . LEU C 2 259 ? 104.499 143.032 88.150  1.00 121.68 ? 266  LEU C CB  1 
ATOM   9461  C  CG  . LEU C 2 259 ? 105.386 141.796 88.144  1.00 121.43 ? 266  LEU C CG  1 
ATOM   9462  C  CD1 . LEU C 2 259 ? 106.767 142.120 88.681  1.00 122.45 ? 266  LEU C CD1 1 
ATOM   9463  C  CD2 . LEU C 2 259 ? 104.712 140.749 88.996  1.00 122.71 ? 266  LEU C CD2 1 
ATOM   9464  N  N   . LYS C 2 260 ? 104.111 142.788 84.806  1.00 126.40 ? 267  LYS C N   1 
ATOM   9465  C  CA  . LYS C 2 260 ? 103.368 142.158 83.717  1.00 124.31 ? 267  LYS C CA  1 
ATOM   9466  C  C   . LYS C 2 260 ? 103.785 140.689 83.665  1.00 124.22 ? 267  LYS C C   1 
ATOM   9467  O  O   . LYS C 2 260 ? 104.706 140.316 82.938  1.00 124.00 ? 267  LYS C O   1 
ATOM   9468  C  CB  . LYS C 2 260 ? 103.631 142.873 82.395  1.00 124.02 ? 267  LYS C CB  1 
ATOM   9469  C  CG  . LYS C 2 260 ? 103.307 144.358 82.435  1.00 123.85 ? 267  LYS C CG  1 
ATOM   9470  C  CD  . LYS C 2 260 ? 103.336 144.980 81.050  1.00 123.76 ? 267  LYS C CD  1 
ATOM   9471  C  CE  . LYS C 2 260 ? 102.742 146.378 81.069  1.00 123.61 ? 267  LYS C CE  1 
ATOM   9472  N  NZ  . LYS C 2 260 ? 102.611 146.949 79.701  1.00 124.47 ? 267  LYS C NZ  1 
ATOM   9473  N  N   . VAL C 2 261 ? 103.087 139.856 84.441  1.00 124.36 ? 268  VAL C N   1 
ATOM   9474  C  CA  . VAL C 2 261 ? 103.465 138.449 84.564  1.00 125.11 ? 268  VAL C CA  1 
ATOM   9475  C  C   . VAL C 2 261 ? 103.325 137.732 83.228  1.00 126.34 ? 268  VAL C C   1 
ATOM   9476  O  O   . VAL C 2 261 ? 104.192 136.941 82.837  1.00 125.29 ? 268  VAL C O   1 
ATOM   9477  C  CB  . VAL C 2 261 ? 102.627 137.766 85.660  1.00 124.30 ? 268  VAL C CB  1 
ATOM   9478  C  CG1 . VAL C 2 261 ? 102.973 136.288 85.752  1.00 123.91 ? 268  VAL C CG1 1 
ATOM   9479  C  CG2 . VAL C 2 261 ? 102.839 138.451 86.995  1.00 124.68 ? 268  VAL C CG2 1 
ATOM   9480  N  N   . LEU C 2 262 ? 102.229 137.991 82.510  1.00 127.99 ? 269  LEU C N   1 
ATOM   9481  C  CA  . LEU C 2 262 ? 101.987 137.290 81.252  1.00 126.27 ? 269  LEU C CA  1 
ATOM   9482  C  C   . LEU C 2 262 ? 103.051 137.626 80.215  1.00 126.26 ? 269  LEU C C   1 
ATOM   9483  O  O   . LEU C 2 262 ? 103.471 136.756 79.443  1.00 126.20 ? 269  LEU C O   1 
ATOM   9484  C  CB  . LEU C 2 262 ? 100.591 137.626 80.727  1.00 126.38 ? 269  LEU C CB  1 
ATOM   9485  C  CG  . LEU C 2 262 ? 99.418  137.075 81.542  1.00 126.78 ? 269  LEU C CG  1 
ATOM   9486  C  CD1 . LEU C 2 262 ? 98.169  136.965 80.685  1.00 126.85 ? 269  LEU C CD1 1 
ATOM   9487  C  CD2 . LEU C 2 262 ? 99.763  135.727 82.159  1.00 126.16 ? 269  LEU C CD2 1 
ATOM   9488  N  N   . ASN C 2 263 ? 103.492 138.885 80.174  1.00 125.55 ? 270  ASN C N   1 
ATOM   9489  C  CA  . ASN C 2 263 ? 104.534 139.273 79.229  1.00 124.94 ? 270  ASN C CA  1 
ATOM   9490  C  C   . ASN C 2 263 ? 105.845 138.559 79.539  1.00 126.09 ? 270  ASN C C   1 
ATOM   9491  O  O   . ASN C 2 263 ? 106.509 138.043 78.632  1.00 126.60 ? 270  ASN C O   1 
ATOM   9492  C  CB  . ASN C 2 263 ? 104.710 140.795 79.253  1.00 123.90 ? 270  ASN C CB  1 
ATOM   9493  C  CG  . ASN C 2 263 ? 105.713 141.303 78.220  1.00 123.96 ? 270  ASN C CG  1 
ATOM   9494  O  OD1 . ASN C 2 263 ? 106.789 140.736 78.030  1.00 124.48 ? 270  ASN C OD1 1 
ATOM   9495  N  ND2 . ASN C 2 263 ? 105.351 142.386 77.544  1.00 123.95 ? 270  ASN C ND2 1 
ATOM   9496  N  N   . MET C 2 264 ? 106.230 138.508 80.818  1.00 129.98 ? 271  MET C N   1 
ATOM   9497  C  CA  . MET C 2 264 ? 107.474 137.835 81.183  1.00 129.84 ? 271  MET C CA  1 
ATOM   9498  C  C   . MET C 2 264 ? 107.378 136.327 80.993  1.00 129.87 ? 271  MET C C   1 
ATOM   9499  O  O   . MET C 2 264 ? 108.401 135.666 80.780  1.00 128.76 ? 271  MET C O   1 
ATOM   9500  C  CB  . MET C 2 264 ? 107.854 138.162 82.627  1.00 130.19 ? 271  MET C CB  1 
ATOM   9501  C  CG  . MET C 2 264 ? 107.810 139.641 82.970  1.00 129.34 ? 271  MET C CG  1 
ATOM   9502  S  SD  . MET C 2 264 ? 107.276 139.945 84.665  1.00 132.03 ? 271  MET C SD  1 
ATOM   9503  C  CE  . MET C 2 264 ? 108.775 139.560 85.565  1.00 129.45 ? 271  MET C CE  1 
ATOM   9504  N  N   . ALA C 2 265 ? 106.169 135.767 81.072  1.00 131.88 ? 272  ALA C N   1 
ATOM   9505  C  CA  . ALA C 2 265 ? 106.003 134.334 80.856  1.00 131.97 ? 272  ALA C CA  1 
ATOM   9506  C  C   . ALA C 2 265 ? 106.386 133.942 79.434  1.00 132.64 ? 272  ALA C C   1 
ATOM   9507  O  O   . ALA C 2 265 ? 107.006 132.894 79.216  1.00 131.44 ? 272  ALA C O   1 
ATOM   9508  C  CB  . ALA C 2 265 ? 104.563 133.920 81.159  1.00 130.34 ? 272  ALA C CB  1 
ATOM   9509  N  N   . ALA C 2 266 ? 106.020 134.770 78.453  1.00 137.70 ? 273  ALA C N   1 
ATOM   9510  C  CA  . ALA C 2 266 ? 106.380 134.486 77.068  1.00 136.74 ? 273  ALA C CA  1 
ATOM   9511  C  C   . ALA C 2 266 ? 107.890 134.535 76.868  1.00 137.14 ? 273  ALA C C   1 
ATOM   9512  O  O   . ALA C 2 266 ? 108.451 133.725 76.120  1.00 137.53 ? 273  ALA C O   1 
ATOM   9513  C  CB  . ALA C 2 266 ? 105.680 135.469 76.131  1.00 135.27 ? 273  ALA C CB  1 
ATOM   9514  N  N   . GLU C 2 267 ? 108.564 135.474 77.528  1.00 138.25 ? 274  GLU C N   1 
ATOM   9515  C  CA  . GLU C 2 267 ? 110.008 135.633 77.403  1.00 138.31 ? 274  GLU C CA  1 
ATOM   9516  C  C   . GLU C 2 267 ? 110.795 134.576 78.171  1.00 138.44 ? 274  GLU C C   1 
ATOM   9517  O  O   . GLU C 2 267 ? 112.018 134.712 78.295  1.00 137.33 ? 274  GLU C O   1 
ATOM   9518  C  CB  . GLU C 2 267 ? 110.424 137.031 77.870  1.00 137.51 ? 274  GLU C CB  1 
ATOM   9519  C  CG  . GLU C 2 267 ? 109.667 138.163 77.193  1.00 137.53 ? 274  GLU C CG  1 
ATOM   9520  C  CD  . GLU C 2 267 ? 109.880 138.193 75.691  1.00 138.42 ? 274  GLU C CD  1 
ATOM   9521  O  OE1 . GLU C 2 267 ? 110.996 137.859 75.238  1.00 138.81 ? 274  GLU C OE1 1 
ATOM   9522  O  OE2 . GLU C 2 267 ? 108.931 138.550 74.962  1.00 138.32 ? 274  GLU C OE2 1 
ATOM   9523  N  N   . ASN C 2 268 ? 110.125 133.544 78.687  1.00 145.67 ? 275  ASN C N   1 
ATOM   9524  C  CA  . ASN C 2 268 ? 110.769 132.426 79.379  1.00 145.81 ? 275  ASN C CA  1 
ATOM   9525  C  C   . ASN C 2 268 ? 111.542 132.907 80.609  1.00 145.43 ? 275  ASN C C   1 
ATOM   9526  O  O   . ASN C 2 268 ? 112.740 132.660 80.765  1.00 145.11 ? 275  ASN C O   1 
ATOM   9527  C  CB  . ASN C 2 268 ? 111.676 131.640 78.425  1.00 146.19 ? 275  ASN C CB  1 
ATOM   9528  C  CG  . ASN C 2 268 ? 111.768 130.171 78.786  1.00 146.18 ? 275  ASN C CG  1 
ATOM   9529  O  OD1 . ASN C 2 268 ? 111.742 129.806 79.961  1.00 145.57 ? 275  ASN C OD1 1 
ATOM   9530  N  ND2 . ASN C 2 268 ? 111.876 129.319 77.774  1.00 146.19 ? 275  ASN C ND2 1 
ATOM   9531  N  N   . ASP C 2 269 ? 110.829 133.606 81.486  1.00 133.41 ? 276  ASP C N   1 
ATOM   9532  C  CA  . ASP C 2 269 ? 111.419 134.041 82.743  1.00 133.32 ? 276  ASP C CA  1 
ATOM   9533  C  C   . ASP C 2 269 ? 111.570 132.856 83.689  1.00 132.27 ? 276  ASP C C   1 
ATOM   9534  O  O   . ASP C 2 269 ? 110.705 131.979 83.756  1.00 131.77 ? 276  ASP C O   1 
ATOM   9535  C  CB  . ASP C 2 269 ? 110.563 135.131 83.388  1.00 132.74 ? 276  ASP C CB  1 
ATOM   9536  C  CG  . ASP C 2 269 ? 111.390 136.141 84.159  1.00 131.99 ? 276  ASP C CG  1 
ATOM   9537  O  OD1 . ASP C 2 269 ? 112.615 135.936 84.286  1.00 131.05 ? 276  ASP C OD1 1 
ATOM   9538  O  OD2 . ASP C 2 269 ? 110.815 137.141 84.637  1.00 131.02 ? 276  ASP C OD2 1 
ATOM   9539  N  N   . ALA C 2 270 ? 112.686 132.833 84.422  1.00 124.67 ? 277  ALA C N   1 
ATOM   9540  C  CA  . ALA C 2 270 ? 112.982 131.695 85.287  1.00 124.10 ? 277  ALA C CA  1 
ATOM   9541  C  C   . ALA C 2 270 ? 111.956 131.558 86.404  1.00 124.39 ? 277  ALA C C   1 
ATOM   9542  O  O   . ALA C 2 270 ? 111.532 130.444 86.734  1.00 123.66 ? 277  ALA C O   1 
ATOM   9543  C  CB  . ALA C 2 270 ? 114.390 131.831 85.867  1.00 123.49 ? 277  ALA C CB  1 
ATOM   9544  N  N   . ASN C 2 271 ? 111.550 132.679 87.004  1.00 120.22 ? 278  ASN C N   1 
ATOM   9545  C  CA  . ASN C 2 271 ? 110.621 132.624 88.128  1.00 118.99 ? 278  ASN C CA  1 
ATOM   9546  C  C   . ASN C 2 271 ? 109.251 132.110 87.700  1.00 117.94 ? 278  ASN C C   1 
ATOM   9547  O  O   . ASN C 2 271 ? 108.611 131.350 88.436  1.00 115.96 ? 278  ASN C O   1 
ATOM   9548  C  CB  . ASN C 2 271 ? 110.501 134.003 88.772  1.00 118.21 ? 278  ASN C CB  1 
ATOM   9549  C  CG  . ASN C 2 271 ? 111.842 134.694 88.927  1.00 118.81 ? 278  ASN C CG  1 
ATOM   9550  O  OD1 . ASN C 2 271 ? 112.599 134.404 89.853  1.00 119.04 ? 278  ASN C OD1 1 
ATOM   9551  N  ND2 . ASN C 2 271 ? 112.141 135.615 88.020  1.00 117.99 ? 278  ASN C ND2 1 
ATOM   9552  N  N   . ILE C 2 272 ? 108.783 132.516 86.519  1.00 124.48 ? 279  ILE C N   1 
ATOM   9553  C  CA  . ILE C 2 272 ? 107.474 132.090 86.040  1.00 125.60 ? 279  ILE C CA  1 
ATOM   9554  C  C   . ILE C 2 272 ? 107.495 130.594 85.759  1.00 125.75 ? 279  ILE C C   1 
ATOM   9555  O  O   . ILE C 2 272 ? 108.406 130.082 85.096  1.00 125.85 ? 279  ILE C O   1 
ATOM   9556  C  CB  . ILE C 2 272 ? 107.073 132.881 84.787  1.00 124.71 ? 279  ILE C CB  1 
ATOM   9557  C  CG1 . ILE C 2 272 ? 107.403 134.365 84.954  1.00 122.91 ? 279  ILE C CG1 1 
ATOM   9558  C  CG2 . ILE C 2 272 ? 105.594 132.690 84.491  1.00 124.62 ? 279  ILE C CG2 1 
ATOM   9559  C  CD1 . ILE C 2 272 ? 106.576 135.060 86.008  1.00 123.19 ? 279  ILE C CD1 1 
ATOM   9560  N  N   . ALA C 2 273 ? 106.487 129.885 86.263  1.00 128.00 ? 280  ALA C N   1 
ATOM   9561  C  CA  . ALA C 2 273 ? 106.340 128.457 86.026  1.00 127.64 ? 280  ALA C CA  1 
ATOM   9562  C  C   . ALA C 2 273 ? 104.945 128.176 85.490  1.00 128.05 ? 280  ALA C C   1 
ATOM   9563  O  O   . ALA C 2 273 ? 103.959 128.736 85.976  1.00 128.17 ? 280  ALA C O   1 
ATOM   9564  C  CB  . ALA C 2 273 ? 106.584 127.648 87.306  1.00 127.38 ? 280  ALA C CB  1 
ATOM   9565  N  N   . ILE C 2 274 ? 104.866 127.310 84.484  1.00 131.33 ? 281  ILE C N   1 
ATOM   9566  C  CA  . ILE C 2 274 ? 103.600 126.917 83.875  1.00 132.12 ? 281  ILE C CA  1 
ATOM   9567  C  C   . ILE C 2 274 ? 103.419 125.424 84.107  1.00 131.39 ? 281  ILE C C   1 
ATOM   9568  O  O   . ILE C 2 274 ? 104.276 124.623 83.713  1.00 129.76 ? 281  ILE C O   1 
ATOM   9569  C  CB  . ILE C 2 274 ? 103.560 127.248 82.375  1.00 132.08 ? 281  ILE C CB  1 
ATOM   9570  C  CG1 . ILE C 2 274 ? 104.163 128.629 82.116  1.00 130.78 ? 281  ILE C CG1 1 
ATOM   9571  C  CG2 . ILE C 2 274 ? 102.135 127.181 81.856  1.00 131.54 ? 281  ILE C CG2 1 
ATOM   9572  C  CD1 . ILE C 2 274 ? 104.509 128.881 80.666  1.00 130.22 ? 281  ILE C CD1 1 
ATOM   9573  N  N   . VAL C 2 275 ? 102.311 125.048 84.743  1.00 132.75 ? 282  VAL C N   1 
ATOM   9574  C  CA  . VAL C 2 275 ? 102.039 123.650 85.059  1.00 133.14 ? 282  VAL C CA  1 
ATOM   9575  C  C   . VAL C 2 275 ? 100.615 123.331 84.631  1.00 134.37 ? 282  VAL C C   1 
ATOM   9576  O  O   . VAL C 2 275 ? 99.667  123.981 85.087  1.00 134.35 ? 282  VAL C O   1 
ATOM   9577  C  CB  . VAL C 2 275 ? 102.242 123.347 86.554  1.00 132.30 ? 282  VAL C CB  1 
ATOM   9578  C  CG1 . VAL C 2 275 ? 101.388 122.161 86.988  1.00 131.26 ? 282  VAL C CG1 1 
ATOM   9579  C  CG2 . VAL C 2 275 ? 103.712 123.088 86.847  1.00 131.65 ? 282  VAL C CG2 1 
ATOM   9580  N  N   . GLY C 2 276 ? 100.461 122.331 83.762  1.00 135.37 ? 283  GLY C N   1 
ATOM   9581  C  CA  . GLY C 2 276 ? 99.157  121.897 83.309  1.00 133.81 ? 283  GLY C CA  1 
ATOM   9582  C  C   . GLY C 2 276 ? 99.013  122.026 81.802  1.00 133.52 ? 283  GLY C C   1 
ATOM   9583  O  O   . GLY C 2 276 ? 99.988  121.892 81.053  1.00 133.52 ? 283  GLY C O   1 
ATOM   9584  N  N   . ASN C 2 277 ? 97.780  122.292 81.369  1.00 144.09 ? 284  ASN C N   1 
ATOM   9585  C  CA  . ASN C 2 277 ? 97.436  122.383 79.956  1.00 145.28 ? 284  ASN C CA  1 
ATOM   9586  C  C   . ASN C 2 277 ? 97.322  123.826 79.475  1.00 145.44 ? 284  ASN C C   1 
ATOM   9587  O  O   . ASN C 2 277 ? 96.480  124.132 78.624  1.00 144.62 ? 284  ASN C O   1 
ATOM   9588  C  CB  . ASN C 2 277 ? 96.135  121.628 79.682  1.00 145.09 ? 284  ASN C CB  1 
ATOM   9589  C  CG  . ASN C 2 277 ? 96.311  120.124 79.737  1.00 144.93 ? 284  ASN C CG  1 
ATOM   9590  O  OD1 . ASN C 2 277 ? 97.320  119.588 79.276  1.00 144.24 ? 284  ASN C OD1 1 
ATOM   9591  N  ND2 . ASN C 2 277 ? 95.328  119.433 80.302  1.00 144.85 ? 284  ASN C ND2 1 
ATOM   9592  N  N   . VAL C 2 278 ? 98.150  124.721 80.003  1.00 149.75 ? 285  VAL C N   1 
ATOM   9593  C  CA  . VAL C 2 278 ? 98.117  126.121 79.598  1.00 149.93 ? 285  VAL C CA  1 
ATOM   9594  C  C   . VAL C 2 278 ? 98.959  126.296 78.342  1.00 149.95 ? 285  VAL C C   1 
ATOM   9595  O  O   . VAL C 2 278 ? 100.123 125.879 78.295  1.00 148.94 ? 285  VAL C O   1 
ATOM   9596  C  CB  . VAL C 2 278 ? 98.614  127.030 80.733  1.00 150.37 ? 285  VAL C CB  1 
ATOM   9597  C  CG1 . VAL C 2 278 ? 99.090  128.366 80.180  1.00 149.68 ? 285  VAL C CG1 1 
ATOM   9598  C  CG2 . VAL C 2 278 ? 97.518  127.240 81.760  1.00 149.08 ? 285  VAL C CG2 1 
ATOM   9599  N  N   . ARG C 2 279 ? 98.371  126.909 77.319  1.00 149.67 ? 286  ARG C N   1 
ATOM   9600  C  CA  . ARG C 2 279 ? 99.051  127.184 76.065  1.00 148.61 ? 286  ARG C CA  1 
ATOM   9601  C  C   . ARG C 2 279 ? 99.081  128.684 75.809  1.00 148.03 ? 286  ARG C C   1 
ATOM   9602  O  O   . ARG C 2 279 ? 98.215  129.433 76.269  1.00 147.93 ? 286  ARG C O   1 
ATOM   9603  C  CB  . ARG C 2 279 ? 98.369  126.475 74.888  1.00 149.15 ? 286  ARG C CB  1 
ATOM   9604  C  CG  . ARG C 2 279 ? 98.508  124.964 74.883  1.00 149.32 ? 286  ARG C CG  1 
ATOM   9605  C  CD  . ARG C 2 279 ? 97.760  124.348 73.707  1.00 149.48 ? 286  ARG C CD  1 
ATOM   9606  N  NE  . ARG C 2 279 ? 98.150  124.937 72.430  1.00 149.81 ? 286  ARG C NE  1 
ATOM   9607  C  CZ  . ARG C 2 279 ? 97.419  125.812 71.752  1.00 149.60 ? 286  ARG C CZ  1 
ATOM   9608  N  NH1 . ARG C 2 279 ? 96.247  126.230 72.202  1.00 149.73 ? 286  ARG C NH1 1 
ATOM   9609  N  NH2 . ARG C 2 279 ? 97.877  126.282 70.595  1.00 148.44 ? 286  ARG C NH2 1 
ATOM   9610  N  N   . LEU C 2 280 ? 100.093 129.116 75.062  1.00 141.50 ? 287  LEU C N   1 
ATOM   9611  C  CA  . LEU C 2 280 ? 100.240 130.510 74.669  1.00 141.71 ? 287  LEU C CA  1 
ATOM   9612  C  C   . LEU C 2 280 ? 99.644  130.706 73.281  1.00 141.99 ? 287  LEU C C   1 
ATOM   9613  O  O   . LEU C 2 280 ? 99.828  129.864 72.395  1.00 142.16 ? 287  LEU C O   1 
ATOM   9614  C  CB  . LEU C 2 280 ? 101.712 130.934 74.706  1.00 141.25 ? 287  LEU C CB  1 
ATOM   9615  C  CG  . LEU C 2 280 ? 102.762 130.230 73.837  1.00 140.94 ? 287  LEU C CG  1 
ATOM   9616  C  CD1 . LEU C 2 280 ? 102.857 130.826 72.435  1.00 141.00 ? 287  LEU C CD1 1 
ATOM   9617  C  CD2 . LEU C 2 280 ? 104.121 130.255 74.524  1.00 140.11 ? 287  LEU C CD2 1 
ATOM   9618  N  N   . VAL C 2 281 ? 98.916  131.805 73.102  1.00 134.89 ? 288  VAL C N   1 
ATOM   9619  C  CA  . VAL C 2 281 ? 98.215  132.097 71.857  1.00 134.70 ? 288  VAL C CA  1 
ATOM   9620  C  C   . VAL C 2 281 ? 99.035  133.096 71.055  1.00 134.25 ? 288  VAL C C   1 
ATOM   9621  O  O   . VAL C 2 281 ? 99.381  134.173 71.557  1.00 132.99 ? 288  VAL C O   1 
ATOM   9622  C  CB  . VAL C 2 281 ? 96.800  132.636 72.128  1.00 133.02 ? 288  VAL C CB  1 
ATOM   9623  C  CG1 . VAL C 2 281 ? 96.238  133.310 70.886  1.00 132.37 ? 288  VAL C CG1 1 
ATOM   9624  C  CG2 . VAL C 2 281 ? 95.886  131.513 72.593  1.00 132.47 ? 288  VAL C CG2 1 
ATOM   9625  N  N   . GLY C 2 282 ? 99.347  132.743 69.812  1.00 125.41 ? 289  GLY C N   1 
ATOM   9626  C  CA  . GLY C 2 282 ? 100.105 133.617 68.937  1.00 124.45 ? 289  GLY C CA  1 
ATOM   9627  C  C   . GLY C 2 282 ? 101.599 133.587 69.195  1.00 123.91 ? 289  GLY C C   1 
ATOM   9628  O  O   . GLY C 2 282 ? 102.043 133.281 70.301  1.00 123.75 ? 289  GLY C O   1 
ATOM   9629  N  N   . ALA D 2 106 ? 139.197 121.923 199.541 1.00 136.30 ? 83   ALA D N   1 
ATOM   9630  C  CA  . ALA D 2 106 ? 139.710 122.786 198.484 1.00 137.33 ? 83   ALA D CA  1 
ATOM   9631  C  C   . ALA D 2 106 ? 140.797 122.080 197.680 1.00 138.55 ? 83   ALA D C   1 
ATOM   9632  O  O   . ALA D 2 106 ? 141.751 121.545 198.244 1.00 138.46 ? 83   ALA D O   1 
ATOM   9633  C  CB  . ALA D 2 106 ? 140.243 124.084 199.072 1.00 136.28 ? 83   ALA D CB  1 
ATOM   9634  N  N   . GLY D 2 107 ? 140.645 122.083 196.358 1.00 134.32 ? 84   GLY D N   1 
ATOM   9635  C  CA  . GLY D 2 107 ? 141.613 121.453 195.482 1.00 131.89 ? 84   GLY D CA  1 
ATOM   9636  C  C   . GLY D 2 107 ? 142.801 122.345 195.188 1.00 132.72 ? 84   GLY D C   1 
ATOM   9637  O  O   . GLY D 2 107 ? 143.421 122.887 196.109 1.00 133.19 ? 84   GLY D O   1 
ATOM   9638  N  N   . THR D 2 108 ? 143.132 122.503 193.910 1.00 141.26 ? 85   THR D N   1 
ATOM   9639  C  CA  . THR D 2 108 ? 144.232 123.373 193.499 1.00 141.77 ? 85   THR D CA  1 
ATOM   9640  C  C   . THR D 2 108 ? 143.805 124.821 193.702 1.00 142.03 ? 85   THR D C   1 
ATOM   9641  O  O   . THR D 2 108 ? 143.088 125.394 192.880 1.00 141.49 ? 85   THR D O   1 
ATOM   9642  C  CB  . THR D 2 108 ? 144.610 123.106 192.046 1.00 140.70 ? 85   THR D CB  1 
ATOM   9643  O  OG1 . THR D 2 108 ? 144.868 121.708 191.867 1.00 139.53 ? 85   THR D OG1 1 
ATOM   9644  C  CG2 . THR D 2 108 ? 145.851 123.896 191.667 1.00 140.11 ? 85   THR D CG2 1 
ATOM   9645  N  N   . THR D 2 109 ? 144.249 125.419 194.805 1.00 148.81 ? 86   THR D N   1 
ATOM   9646  C  CA  . THR D 2 109 ? 143.808 126.756 195.177 1.00 148.70 ? 86   THR D CA  1 
ATOM   9647  C  C   . THR D 2 109 ? 144.553 127.812 194.370 1.00 148.90 ? 86   THR D C   1 
ATOM   9648  O  O   . THR D 2 109 ? 145.781 127.764 194.246 1.00 148.30 ? 86   THR D O   1 
ATOM   9649  C  CB  . THR D 2 109 ? 144.020 126.989 196.673 1.00 147.78 ? 86   THR D CB  1 
ATOM   9650  O  OG1 . THR D 2 109 ? 143.421 125.919 197.415 1.00 146.25 ? 86   THR D OG1 1 
ATOM   9651  C  CG2 . THR D 2 109 ? 143.390 128.306 197.103 1.00 147.62 ? 86   THR D CG2 1 
ATOM   9652  N  N   . TYR D 2 110 ? 143.803 128.764 193.822 1.00 151.21 ? 87   TYR D N   1 
ATOM   9653  C  CA  . TYR D 2 110 ? 144.357 129.897 193.095 1.00 151.57 ? 87   TYR D CA  1 
ATOM   9654  C  C   . TYR D 2 110 ? 143.949 131.183 193.798 1.00 151.08 ? 87   TYR D C   1 
ATOM   9655  O  O   . TYR D 2 110 ? 142.770 131.376 194.117 1.00 149.96 ? 87   TYR D O   1 
ATOM   9656  C  CB  . TYR D 2 110 ? 143.886 129.905 191.639 1.00 150.91 ? 87   TYR D CB  1 
ATOM   9657  C  CG  . TYR D 2 110 ? 144.796 129.138 190.706 1.00 150.79 ? 87   TYR D CG  1 
ATOM   9658  C  CD1 . TYR D 2 110 ? 144.842 127.750 190.735 1.00 150.33 ? 87   TYR D CD1 1 
ATOM   9659  C  CD2 . TYR D 2 110 ? 145.612 129.801 189.799 1.00 150.58 ? 87   TYR D CD2 1 
ATOM   9660  C  CE1 . TYR D 2 110 ? 145.673 127.045 189.885 1.00 151.10 ? 87   TYR D CE1 1 
ATOM   9661  C  CE2 . TYR D 2 110 ? 146.447 129.104 188.946 1.00 150.93 ? 87   TYR D CE2 1 
ATOM   9662  C  CZ  . TYR D 2 110 ? 146.473 127.726 188.993 1.00 151.38 ? 87   TYR D CZ  1 
ATOM   9663  O  OH  . TYR D 2 110 ? 147.302 127.028 188.146 1.00 149.91 ? 87   TYR D OH  1 
ATOM   9664  N  N   . ILE D 2 111 ? 144.923 132.060 194.032 1.00 153.22 ? 88   ILE D N   1 
ATOM   9665  C  CA  . ILE D 2 111 ? 144.723 133.290 194.791 1.00 152.66 ? 88   ILE D CA  1 
ATOM   9666  C  C   . ILE D 2 111 ? 144.638 134.460 193.822 1.00 152.20 ? 88   ILE D C   1 
ATOM   9667  O  O   . ILE D 2 111 ? 145.484 134.604 192.929 1.00 151.93 ? 88   ILE D O   1 
ATOM   9668  C  CB  . ILE D 2 111 ? 145.853 133.498 195.816 1.00 152.15 ? 88   ILE D CB  1 
ATOM   9669  C  CG1 . ILE D 2 111 ? 145.829 134.923 196.377 1.00 151.94 ? 88   ILE D CG1 1 
ATOM   9670  C  CG2 . ILE D 2 111 ? 147.207 133.184 195.197 1.00 152.14 ? 88   ILE D CG2 1 
ATOM   9671  C  CD1 . ILE D 2 111 ? 144.590 135.252 197.180 1.00 151.45 ? 88   ILE D CD1 1 
ATOM   9672  N  N   . PHE D 2 112 ? 143.613 135.291 193.990 1.00 145.91 ? 89   PHE D N   1 
ATOM   9673  C  CA  . PHE D 2 112 ? 143.439 136.509 193.213 1.00 145.79 ? 89   PHE D CA  1 
ATOM   9674  C  C   . PHE D 2 112 ? 143.755 137.706 194.098 1.00 145.42 ? 89   PHE D C   1 
ATOM   9675  O  O   . PHE D 2 112 ? 143.278 137.785 195.235 1.00 145.31 ? 89   PHE D O   1 
ATOM   9676  C  CB  . PHE D 2 112 ? 142.016 136.612 192.660 1.00 146.60 ? 89   PHE D CB  1 
ATOM   9677  C  CG  . PHE D 2 112 ? 141.791 135.810 191.409 1.00 146.40 ? 89   PHE D CG  1 
ATOM   9678  C  CD1 . PHE D 2 112 ? 141.871 134.427 191.432 1.00 145.81 ? 89   PHE D CD1 1 
ATOM   9679  C  CD2 . PHE D 2 112 ? 141.499 136.438 190.211 1.00 145.35 ? 89   PHE D CD2 1 
ATOM   9680  C  CE1 . PHE D 2 112 ? 141.664 133.687 190.284 1.00 145.45 ? 89   PHE D CE1 1 
ATOM   9681  C  CE2 . PHE D 2 112 ? 141.291 135.704 189.059 1.00 145.40 ? 89   PHE D CE2 1 
ATOM   9682  C  CZ  . PHE D 2 112 ? 141.374 134.327 189.096 1.00 145.77 ? 89   PHE D CZ  1 
ATOM   9683  N  N   . SER D 2 113 ? 144.552 138.630 193.576 1.00 139.65 ? 90   SER D N   1 
ATOM   9684  C  CA  . SER D 2 113 ? 145.045 139.775 194.328 1.00 139.06 ? 90   SER D CA  1 
ATOM   9685  C  C   . SER D 2 113 ? 144.526 141.068 193.699 1.00 138.87 ? 90   SER D C   1 
ATOM   9686  O  O   . SER D 2 113 ? 143.651 141.053 192.828 1.00 138.52 ? 90   SER D O   1 
ATOM   9687  C  CB  . SER D 2 113 ? 146.574 139.753 194.394 1.00 138.63 ? 90   SER D CB  1 
ATOM   9688  O  OG  . SER D 2 113 ? 147.070 140.872 195.107 1.00 137.69 ? 90   SER D OG  1 
ATOM   9689  N  N   . LYS D 2 114 ? 145.062 142.193 194.172 1.00 135.69 ? 91   LYS D N   1 
ATOM   9690  C  CA  . LYS D 2 114 ? 144.671 143.499 193.656 1.00 135.48 ? 91   LYS D CA  1 
ATOM   9691  C  C   . LYS D 2 114 ? 144.878 143.563 192.148 1.00 135.33 ? 91   LYS D C   1 
ATOM   9692  O  O   . LYS D 2 114 ? 145.921 143.152 191.632 1.00 135.51 ? 91   LYS D O   1 
ATOM   9693  C  CB  . LYS D 2 114 ? 145.477 144.598 194.347 1.00 134.83 ? 91   LYS D CB  1 
ATOM   9694  C  CG  . LYS D 2 114 ? 146.958 144.278 194.487 1.00 134.88 ? 91   LYS D CG  1 
ATOM   9695  C  CD  . LYS D 2 114 ? 147.763 145.509 194.864 1.00 133.93 ? 91   LYS D CD  1 
ATOM   9696  C  CE  . LYS D 2 114 ? 149.213 145.151 195.143 1.00 133.66 ? 91   LYS D CE  1 
ATOM   9697  N  NZ  . LYS D 2 114 ? 149.806 144.341 194.043 1.00 133.23 ? 91   LYS D NZ  1 
ATOM   9698  N  N   . GLY D 2 115 ? 143.878 144.078 191.444 1.00 135.03 ? 92   GLY D N   1 
ATOM   9699  C  CA  . GLY D 2 115 ? 143.872 144.111 189.991 1.00 134.52 ? 92   GLY D CA  1 
ATOM   9700  C  C   . GLY D 2 115 ? 143.268 142.868 189.371 1.00 135.48 ? 92   GLY D C   1 
ATOM   9701  O  O   . GLY D 2 115 ? 142.530 142.958 188.388 1.00 135.44 ? 92   GLY D O   1 
ATOM   9702  N  N   . GLY D 2 116 ? 143.569 141.702 189.938 1.00 142.10 ? 93   GLY D N   1 
ATOM   9703  C  CA  . GLY D 2 116 ? 142.996 140.466 189.451 1.00 142.36 ? 93   GLY D CA  1 
ATOM   9704  C  C   . GLY D 2 116 ? 143.616 140.007 188.139 1.00 142.62 ? 93   GLY D C   1 
ATOM   9705  O  O   . GLY D 2 116 ? 144.696 140.441 187.729 1.00 142.03 ? 93   GLY D O   1 
ATOM   9706  N  N   . GLY D 2 117 ? 142.900 139.104 187.481 1.00 151.39 ? 94   GLY D N   1 
ATOM   9707  C  CA  . GLY D 2 117 ? 143.359 138.551 186.221 1.00 151.32 ? 94   GLY D CA  1 
ATOM   9708  C  C   . GLY D 2 117 ? 142.339 137.571 185.687 1.00 152.43 ? 94   GLY D C   1 
ATOM   9709  O  O   . GLY D 2 117 ? 141.281 137.348 186.285 1.00 151.88 ? 94   GLY D O   1 
ATOM   9710  N  N   . GLN D 2 118 ? 142.673 136.983 184.540 1.00 148.60 ? 95   GLN D N   1 
ATOM   9711  C  CA  . GLN D 2 118 ? 141.784 136.039 183.880 1.00 146.83 ? 95   GLN D CA  1 
ATOM   9712  C  C   . GLN D 2 118 ? 142.559 134.826 183.392 1.00 146.25 ? 95   GLN D C   1 
ATOM   9713  O  O   . GLN D 2 118 ? 143.665 134.949 182.856 1.00 145.71 ? 95   GLN D O   1 
ATOM   9714  C  CB  . GLN D 2 118 ? 141.048 136.692 182.702 1.00 145.58 ? 95   GLN D CB  1 
ATOM   9715  C  CG  . GLN D 2 118 ? 140.002 137.713 183.117 1.00 145.04 ? 95   GLN D CG  1 
ATOM   9716  C  CD  . GLN D 2 118 ? 139.025 138.031 182.003 1.00 146.20 ? 95   GLN D CD  1 
ATOM   9717  O  OE1 . GLN D 2 118 ? 138.057 138.764 182.203 1.00 147.33 ? 95   GLN D OE1 1 
ATOM   9718  N  NE2 . GLN D 2 118 ? 139.273 137.477 180.822 1.00 146.41 ? 95   GLN D NE2 1 
ATOM   9719  N  N   . ILE D 2 119 ? 141.959 133.653 183.574 1.00 146.92 ? 96   ILE D N   1 
ATOM   9720  C  CA  . ILE D 2 119 ? 142.480 132.400 183.043 1.00 147.12 ? 96   ILE D CA  1 
ATOM   9721  C  C   . ILE D 2 119 ? 141.429 131.805 182.116 1.00 147.31 ? 96   ILE D C   1 
ATOM   9722  O  O   . ILE D 2 119 ? 140.261 131.659 182.498 1.00 146.37 ? 96   ILE D O   1 
ATOM   9723  C  CB  . ILE D 2 119 ? 142.868 131.416 184.165 1.00 146.64 ? 96   ILE D CB  1 
ATOM   9724  C  CG1 . ILE D 2 119 ? 143.023 129.995 183.617 1.00 146.48 ? 96   ILE D CG1 1 
ATOM   9725  C  CG2 . ILE D 2 119 ? 141.882 131.478 185.310 1.00 146.01 ? 96   ILE D CG2 1 
ATOM   9726  C  CD1 . ILE D 2 119 ? 143.836 129.088 184.513 1.00 146.60 ? 96   ILE D CD1 1 
ATOM   9727  N  N   . THR D 2 120 ? 141.846 131.479 180.894 1.00 146.78 ? 97   THR D N   1 
ATOM   9728  C  CA  . THR D 2 120 ? 140.953 131.045 179.831 1.00 146.14 ? 97   THR D CA  1 
ATOM   9729  C  C   . THR D 2 120 ? 141.326 129.641 179.384 1.00 146.00 ? 97   THR D C   1 
ATOM   9730  O  O   . THR D 2 120 ? 142.496 129.366 179.089 1.00 145.37 ? 97   THR D O   1 
ATOM   9731  C  CB  . THR D 2 120 ? 141.020 131.997 178.634 1.00 146.03 ? 97   THR D CB  1 
ATOM   9732  O  OG1 . THR D 2 120 ? 141.064 133.352 179.097 1.00 146.24 ? 97   THR D OG1 1 
ATOM   9733  C  CG2 . THR D 2 120 ? 139.809 131.808 177.734 1.00 145.98 ? 97   THR D CG2 1 
ATOM   9734  N  N   . TYR D 2 121 ? 140.331 128.762 179.333 1.00 140.25 ? 98   TYR D N   1 
ATOM   9735  C  CA  . TYR D 2 121 ? 140.463 127.441 178.728 1.00 139.23 ? 98   TYR D CA  1 
ATOM   9736  C  C   . TYR D 2 121 ? 139.700 127.457 177.411 1.00 138.55 ? 98   TYR D C   1 
ATOM   9737  O  O   . TYR D 2 121 ? 138.469 127.551 177.406 1.00 138.25 ? 98   TYR D O   1 
ATOM   9738  C  CB  . TYR D 2 121 ? 139.934 126.348 179.653 1.00 139.40 ? 98   TYR D CB  1 
ATOM   9739  C  CG  . TYR D 2 121 ? 140.005 124.961 179.052 1.00 139.77 ? 98   TYR D CG  1 
ATOM   9740  C  CD1 . TYR D 2 121 ? 141.147 124.525 178.396 1.00 140.37 ? 98   TYR D CD1 1 
ATOM   9741  C  CD2 . TYR D 2 121 ? 138.929 124.089 179.140 1.00 139.25 ? 98   TYR D CD2 1 
ATOM   9742  C  CE1 . TYR D 2 121 ? 141.216 123.260 177.845 1.00 139.56 ? 98   TYR D CE1 1 
ATOM   9743  C  CE2 . TYR D 2 121 ? 138.988 122.822 178.592 1.00 139.46 ? 98   TYR D CE2 1 
ATOM   9744  C  CZ  . TYR D 2 121 ? 140.134 122.413 177.946 1.00 139.01 ? 98   TYR D CZ  1 
ATOM   9745  O  OH  . TYR D 2 121 ? 140.199 121.153 177.399 1.00 138.86 ? 98   TYR D OH  1 
ATOM   9746  N  N   . LYS D 2 122 ? 140.426 127.370 176.301 1.00 140.16 ? 99   LYS D N   1 
ATOM   9747  C  CA  . LYS D 2 122 ? 139.836 127.408 174.969 1.00 140.15 ? 99   LYS D CA  1 
ATOM   9748  C  C   . LYS D 2 122 ? 139.852 126.004 174.381 1.00 139.40 ? 99   LYS D C   1 
ATOM   9749  O  O   . LYS D 2 122 ? 140.918 125.393 174.249 1.00 139.49 ? 99   LYS D O   1 
ATOM   9750  C  CB  . LYS D 2 122 ? 140.587 128.382 174.061 1.00 140.60 ? 99   LYS D CB  1 
ATOM   9751  C  CG  . LYS D 2 122 ? 139.934 128.589 172.704 1.00 140.85 ? 99   LYS D CG  1 
ATOM   9752  C  CD  . LYS D 2 122 ? 140.530 129.784 171.979 1.00 140.19 ? 99   LYS D CD  1 
ATOM   9753  C  CE  . LYS D 2 122 ? 139.829 130.031 170.653 1.00 140.22 ? 99   LYS D CE  1 
ATOM   9754  N  NZ  . LYS D 2 122 ? 140.295 131.286 170.000 1.00 139.98 ? 99   LYS D NZ  1 
ATOM   9755  N  N   . TRP D 2 123 ? 138.673 125.500 174.030 1.00 124.12 ? 100  TRP D N   1 
ATOM   9756  C  CA  . TRP D 2 123 ? 138.569 124.177 173.442 1.00 124.27 ? 100  TRP D CA  1 
ATOM   9757  C  C   . TRP D 2 123 ? 139.131 124.179 172.021 1.00 124.86 ? 100  TRP D C   1 
ATOM   9758  O  O   . TRP D 2 123 ? 139.167 125.220 171.360 1.00 123.00 ? 100  TRP D O   1 
ATOM   9759  C  CB  . TRP D 2 123 ? 137.114 123.719 173.418 1.00 123.61 ? 100  TRP D CB  1 
ATOM   9760  C  CG  . TRP D 2 123 ? 136.665 123.052 174.678 1.00 122.45 ? 100  TRP D CG  1 
ATOM   9761  C  CD1 . TRP D 2 123 ? 137.014 121.810 175.116 1.00 122.56 ? 100  TRP D CD1 1 
ATOM   9762  C  CD2 . TRP D 2 123 ? 135.782 123.593 175.666 1.00 122.31 ? 100  TRP D CD2 1 
ATOM   9763  N  NE1 . TRP D 2 123 ? 136.400 121.541 176.315 1.00 122.49 ? 100  TRP D NE1 1 
ATOM   9764  C  CE2 . TRP D 2 123 ? 135.639 122.622 176.675 1.00 122.35 ? 100  TRP D CE2 1 
ATOM   9765  C  CE3 . TRP D 2 123 ? 135.099 124.806 175.795 1.00 122.29 ? 100  TRP D CE3 1 
ATOM   9766  C  CZ2 . TRP D 2 123 ? 134.841 122.824 177.797 1.00 122.99 ? 100  TRP D CZ2 1 
ATOM   9767  C  CZ3 . TRP D 2 123 ? 134.308 125.005 176.911 1.00 121.95 ? 100  TRP D CZ3 1 
ATOM   9768  C  CH2 . TRP D 2 123 ? 134.184 124.019 177.895 1.00 123.38 ? 100  TRP D CH2 1 
ATOM   9769  N  N   . PRO D 2 124 ? 139.590 123.027 171.536 1.00 127.72 ? 101  PRO D N   1 
ATOM   9770  C  CA  . PRO D 2 124 ? 139.979 122.937 170.133 1.00 127.06 ? 101  PRO D CA  1 
ATOM   9771  C  C   . PRO D 2 124 ? 138.787 123.187 169.235 1.00 126.09 ? 101  PRO D C   1 
ATOM   9772  O  O   . PRO D 2 124 ? 137.633 122.900 169.608 1.00 126.75 ? 101  PRO D O   1 
ATOM   9773  C  CB  . PRO D 2 124 ? 140.499 121.497 170.000 1.00 125.57 ? 101  PRO D CB  1 
ATOM   9774  C  CG  . PRO D 2 124 ? 140.010 120.778 171.213 1.00 125.19 ? 101  PRO D CG  1 
ATOM   9775  C  CD  . PRO D 2 124 ? 139.914 121.803 172.285 1.00 125.52 ? 101  PRO D CD  1 
ATOM   9776  N  N   . PRO D 2 125 ? 139.012 123.738 168.038 1.00 120.55 ? 102  PRO D N   1 
ATOM   9777  C  CA  . PRO D 2 125 ? 137.874 124.142 167.192 1.00 120.12 ? 102  PRO D CA  1 
ATOM   9778  C  C   . PRO D 2 125 ? 136.934 123.005 166.825 1.00 119.62 ? 102  PRO D C   1 
ATOM   9779  O  O   . PRO D 2 125 ? 135.720 123.224 166.730 1.00 120.51 ? 102  PRO D O   1 
ATOM   9780  C  CB  . PRO D 2 125 ? 138.559 124.734 165.950 1.00 120.41 ? 102  PRO D CB  1 
ATOM   9781  C  CG  . PRO D 2 125 ? 139.936 125.102 166.406 1.00 121.49 ? 102  PRO D CG  1 
ATOM   9782  C  CD  . PRO D 2 125 ? 140.308 124.071 167.424 1.00 120.55 ? 102  PRO D CD  1 
ATOM   9783  N  N   . ASN D 2 126 ? 137.453 121.798 166.614 1.00 115.26 ? 103  ASN D N   1 
ATOM   9784  C  CA  . ASN D 2 126 ? 136.642 120.680 166.152 1.00 115.69 ? 103  ASN D CA  1 
ATOM   9785  C  C   . ASN D 2 126 ? 136.143 119.785 167.278 1.00 116.18 ? 103  ASN D C   1 
ATOM   9786  O  O   . ASN D 2 126 ? 135.464 118.791 167.003 1.00 114.50 ? 103  ASN D O   1 
ATOM   9787  C  CB  . ASN D 2 126 ? 137.433 119.842 165.142 1.00 114.73 ? 103  ASN D CB  1 
ATOM   9788  C  CG  . ASN D 2 126 ? 137.803 120.627 163.900 1.00 115.04 ? 103  ASN D CG  1 
ATOM   9789  O  OD1 . ASN D 2 126 ? 137.115 121.574 163.521 1.00 115.48 ? 103  ASN D OD1 1 
ATOM   9790  N  ND2 . ASN D 2 126 ? 138.897 120.236 163.258 1.00 115.58 ? 103  ASN D ND2 1 
ATOM   9791  N  N   . ASP D 2 127 ? 136.454 120.108 168.535 1.00 120.80 ? 104  ASP D N   1 
ATOM   9792  C  CA  . ASP D 2 127 ? 136.019 119.307 169.674 1.00 120.19 ? 104  ASP D CA  1 
ATOM   9793  C  C   . ASP D 2 127 ? 135.161 120.110 170.645 1.00 119.32 ? 104  ASP D C   1 
ATOM   9794  O  O   . ASP D 2 127 ? 135.043 119.737 171.816 1.00 119.40 ? 104  ASP D O   1 
ATOM   9795  C  CB  . ASP D 2 127 ? 137.224 118.709 170.403 1.00 121.54 ? 104  ASP D CB  1 
ATOM   9796  C  CG  . ASP D 2 127 ? 138.011 117.742 169.538 1.00 122.56 ? 104  ASP D CG  1 
ATOM   9797  O  OD1 . ASP D 2 127 ? 137.509 117.354 168.463 1.00 122.78 ? 104  ASP D OD1 1 
ATOM   9798  O  OD2 . ASP D 2 127 ? 139.136 117.371 169.934 1.00 121.84 ? 104  ASP D OD2 1 
ATOM   9799  N  N   . ARG D 2 128 ? 134.569 121.204 170.186 1.00 111.96 ? 105  ARG D N   1 
ATOM   9800  C  CA  . ARG D 2 128 ? 133.730 122.016 171.057 1.00 110.49 ? 105  ARG D CA  1 
ATOM   9801  C  C   . ARG D 2 128 ? 132.464 121.248 171.423 1.00 112.02 ? 105  ARG D C   1 
ATOM   9802  O  O   . ARG D 2 128 ? 131.796 120.704 170.535 1.00 113.06 ? 105  ARG D O   1 
ATOM   9803  C  CB  . ARG D 2 128 ? 133.377 123.335 170.377 1.00 109.27 ? 105  ARG D CB  1 
ATOM   9804  C  CG  . ARG D 2 128 ? 134.525 124.334 170.340 1.00 111.91 ? 105  ARG D CG  1 
ATOM   9805  C  CD  . ARG D 2 128 ? 134.299 125.407 169.289 1.00 112.79 ? 105  ARG D CD  1 
ATOM   9806  N  NE  . ARG D 2 128 ? 135.552 125.879 168.713 1.00 114.56 ? 105  ARG D NE  1 
ATOM   9807  C  CZ  . ARG D 2 128 ? 136.270 126.882 169.200 1.00 113.26 ? 105  ARG D CZ  1 
ATOM   9808  N  NH1 . ARG D 2 128 ? 135.886 127.548 170.277 1.00 113.12 ? 105  ARG D NH1 1 
ATOM   9809  N  NH2 . ARG D 2 128 ? 137.402 127.225 168.593 1.00 111.68 ? 105  ARG D NH2 1 
ATOM   9810  N  N   . PRO D 2 129 ? 132.103 121.178 172.700 1.00 104.07 ? 106  PRO D N   1 
ATOM   9811  C  CA  . PRO D 2 129 ? 130.940 120.388 173.109 1.00 103.55 ? 106  PRO D CA  1 
ATOM   9812  C  C   . PRO D 2 129 ? 129.644 121.182 173.099 1.00 102.06 ? 106  PRO D C   1 
ATOM   9813  O  O   . PRO D 2 129 ? 129.621 122.404 173.241 1.00 104.12 ? 106  PRO D O   1 
ATOM   9814  C  CB  . PRO D 2 129 ? 131.310 119.967 174.537 1.00 100.65 ? 106  PRO D CB  1 
ATOM   9815  C  CG  . PRO D 2 129 ? 132.115 121.118 175.049 1.00 101.64 ? 106  PRO D CG  1 
ATOM   9816  C  CD  . PRO D 2 129 ? 132.832 121.725 173.858 1.00 103.96 ? 106  PRO D CD  1 
ATOM   9817  N  N   . SER D 2 130 ? 128.548 120.454 172.900 1.00 82.37  ? 107  SER D N   1 
ATOM   9818  C  CA  . SER D 2 130 ? 127.200 120.986 173.056 1.00 78.27  ? 107  SER D CA  1 
ATOM   9819  C  C   . SER D 2 130 ? 126.402 119.976 173.862 1.00 82.14  ? 107  SER D C   1 
ATOM   9820  O  O   . SER D 2 130 ? 126.224 118.836 173.422 1.00 86.65  ? 107  SER D O   1 
ATOM   9821  C  CB  . SER D 2 130 ? 126.539 121.249 171.701 1.00 79.28  ? 107  SER D CB  1 
ATOM   9822  O  OG  . SER D 2 130 ? 127.406 121.971 170.844 1.00 85.29  ? 107  SER D OG  1 
ATOM   9823  N  N   . THR D 2 131 ? 125.927 120.385 175.035 1.00 86.04  ? 108  THR D N   1 
ATOM   9824  C  CA  . THR D 2 131 ? 125.328 119.458 175.981 1.00 85.58  ? 108  THR D CA  1 
ATOM   9825  C  C   . THR D 2 131 ? 123.993 119.989 176.480 1.00 86.04  ? 108  THR D C   1 
ATOM   9826  O  O   . THR D 2 131 ? 123.794 121.199 176.614 1.00 88.41  ? 108  THR D O   1 
ATOM   9827  C  CB  . THR D 2 131 ? 126.256 119.203 177.175 1.00 89.13  ? 108  THR D CB  1 
ATOM   9828  O  OG1 . THR D 2 131 ? 125.521 118.565 178.227 1.00 92.69  ? 108  THR D OG1 1 
ATOM   9829  C  CG2 . THR D 2 131 ? 126.837 120.512 177.688 1.00 88.53  ? 108  THR D CG2 1 
ATOM   9830  N  N   . ARG D 2 132 ? 123.075 119.059 176.750 1.00 84.90  ? 109  ARG D N   1 
ATOM   9831  C  CA  . ARG D 2 132 ? 121.776 119.431 177.300 1.00 85.46  ? 109  ARG D CA  1 
ATOM   9832  C  C   . ARG D 2 132 ? 121.893 119.849 178.760 1.00 90.35  ? 109  ARG D C   1 
ATOM   9833  O  O   . ARG D 2 132 ? 121.226 120.795 179.196 1.00 92.75  ? 109  ARG D O   1 
ATOM   9834  C  CB  . ARG D 2 132 ? 120.794 118.268 177.162 1.00 84.57  ? 109  ARG D CB  1 
ATOM   9835  C  CG  . ARG D 2 132 ? 120.492 117.855 175.733 1.00 84.97  ? 109  ARG D CG  1 
ATOM   9836  C  CD  . ARG D 2 132 ? 119.312 116.896 175.683 1.00 84.66  ? 109  ARG D CD  1 
ATOM   9837  N  NE  . ARG D 2 132 ? 118.251 117.367 174.800 1.00 86.51  ? 109  ARG D NE  1 
ATOM   9838  C  CZ  . ARG D 2 132 ? 118.270 117.262 173.479 1.00 87.27  ? 109  ARG D CZ  1 
ATOM   9839  N  NH1 . ARG D 2 132 ? 119.286 116.700 172.844 1.00 88.23  ? 109  ARG D NH1 1 
ATOM   9840  N  NH2 . ARG D 2 132 ? 117.244 117.733 172.775 1.00 84.86  ? 109  ARG D NH2 1 
ATOM   9841  N  N   . ALA D 2 133 ? 122.731 119.160 179.529 1.00 107.18 ? 110  ALA D N   1 
ATOM   9842  C  CA  . ALA D 2 133 ? 122.837 119.362 180.966 1.00 106.56 ? 110  ALA D CA  1 
ATOM   9843  C  C   . ALA D 2 133 ? 124.211 119.908 181.330 1.00 107.65 ? 110  ALA D C   1 
ATOM   9844  O  O   . ALA D 2 133 ? 125.220 119.537 180.722 1.00 107.81 ? 110  ALA D O   1 
ATOM   9845  C  CB  . ALA D 2 133 ? 122.581 118.056 181.722 1.00 106.77 ? 110  ALA D CB  1 
ATOM   9846  N  N   . ASP D 2 134 ? 124.240 120.788 182.328 1.00 125.58 ? 111  ASP D N   1 
ATOM   9847  C  CA  . ASP D 2 134 ? 125.467 121.394 182.820 1.00 127.16 ? 111  ASP D CA  1 
ATOM   9848  C  C   . ASP D 2 134 ? 125.648 121.068 184.296 1.00 127.93 ? 111  ASP D C   1 
ATOM   9849  O  O   . ASP D 2 134 ? 124.675 120.952 185.047 1.00 126.72 ? 111  ASP D O   1 
ATOM   9850  C  CB  . ASP D 2 134 ? 125.458 122.915 182.621 1.00 126.99 ? 111  ASP D CB  1 
ATOM   9851  C  CG  . ASP D 2 134 ? 125.466 123.312 181.158 1.00 127.46 ? 111  ASP D CG  1 
ATOM   9852  O  OD1 . ASP D 2 134 ? 126.029 122.556 180.338 1.00 127.35 ? 111  ASP D OD1 1 
ATOM   9853  O  OD2 . ASP D 2 134 ? 124.908 124.379 180.827 1.00 127.52 ? 111  ASP D OD2 1 
ATOM   9854  N  N   . ARG D 2 135 ? 126.907 120.921 184.705 1.00 140.03 ? 112  ARG D N   1 
ATOM   9855  C  CA  . ARG D 2 135 ? 127.247 120.580 186.085 1.00 139.23 ? 112  ARG D CA  1 
ATOM   9856  C  C   . ARG D 2 135 ? 128.456 121.406 186.498 1.00 139.99 ? 112  ARG D C   1 
ATOM   9857  O  O   . ARG D 2 135 ? 129.577 121.132 186.058 1.00 139.39 ? 112  ARG D O   1 
ATOM   9858  C  CB  . ARG D 2 135 ? 127.530 119.085 186.229 1.00 139.34 ? 112  ARG D CB  1 
ATOM   9859  C  CG  . ARG D 2 135 ? 127.950 118.659 187.626 1.00 140.08 ? 112  ARG D CG  1 
ATOM   9860  C  CD  . ARG D 2 135 ? 127.854 117.150 187.796 1.00 139.37 ? 112  ARG D CD  1 
ATOM   9861  N  NE  . ARG D 2 135 ? 126.535 116.641 187.439 1.00 139.61 ? 112  ARG D NE  1 
ATOM   9862  C  CZ  . ARG D 2 135 ? 126.278 115.919 186.357 1.00 140.13 ? 112  ARG D CZ  1 
ATOM   9863  N  NH1 . ARG D 2 135 ? 127.232 115.597 185.498 1.00 140.28 ? 112  ARG D NH1 1 
ATOM   9864  N  NH2 . ARG D 2 135 ? 125.032 115.512 186.129 1.00 139.56 ? 112  ARG D NH2 1 
ATOM   9865  N  N   . LEU D 2 136 ? 128.232 122.410 187.339 1.00 145.91 ? 113  LEU D N   1 
ATOM   9866  C  CA  . LEU D 2 136 ? 129.286 123.291 187.820 1.00 146.22 ? 113  LEU D CA  1 
ATOM   9867  C  C   . LEU D 2 136 ? 129.482 123.088 189.317 1.00 146.64 ? 113  LEU D C   1 
ATOM   9868  O  O   . LEU D 2 136 ? 128.520 122.853 190.050 1.00 146.36 ? 113  LEU D O   1 
ATOM   9869  C  CB  . LEU D 2 136 ? 128.949 124.757 187.529 1.00 145.61 ? 113  LEU D CB  1 
ATOM   9870  C  CG  . LEU D 2 136 ? 130.096 125.769 187.585 1.00 145.33 ? 113  LEU D CG  1 
ATOM   9871  C  CD1 . LEU D 2 136 ? 131.402 125.142 187.122 1.00 144.72 ? 113  LEU D CD1 1 
ATOM   9872  C  CD2 . LEU D 2 136 ? 129.765 126.999 186.754 1.00 145.24 ? 113  LEU D CD2 1 
ATOM   9873  N  N   . ALA D 2 137 ? 130.733 123.170 189.766 1.00 146.92 ? 114  ALA D N   1 
ATOM   9874  C  CA  . ALA D 2 137 ? 131.039 123.028 191.184 1.00 147.00 ? 114  ALA D CA  1 
ATOM   9875  C  C   . ALA D 2 137 ? 132.370 123.705 191.465 1.00 147.54 ? 114  ALA D C   1 
ATOM   9876  O  O   . ALA D 2 137 ? 133.347 123.465 190.749 1.00 147.54 ? 114  ALA D O   1 
ATOM   9877  C  CB  . ALA D 2 137 ? 131.089 121.553 191.597 1.00 145.94 ? 114  ALA D CB  1 
ATOM   9878  N  N   . ILE D 2 138 ? 132.408 124.542 192.499 1.00 144.69 ? 115  ILE D N   1 
ATOM   9879  C  CA  . ILE D 2 138 ? 133.629 125.274 192.829 1.00 144.39 ? 115  ILE D CA  1 
ATOM   9880  C  C   . ILE D 2 138 ? 133.531 125.779 194.262 1.00 145.49 ? 115  ILE D C   1 
ATOM   9881  O  O   . ILE D 2 138 ? 132.466 126.208 194.711 1.00 145.31 ? 115  ILE D O   1 
ATOM   9882  C  CB  . ILE D 2 138 ? 133.873 126.431 191.829 1.00 143.73 ? 115  ILE D CB  1 
ATOM   9883  C  CG1 . ILE D 2 138 ? 135.096 127.257 192.235 1.00 144.26 ? 115  ILE D CG1 1 
ATOM   9884  C  CG2 . ILE D 2 138 ? 132.638 127.309 191.706 1.00 142.95 ? 115  ILE D CG2 1 
ATOM   9885  C  CD1 . ILE D 2 138 ? 135.350 128.451 191.345 1.00 143.83 ? 115  ILE D CD1 1 
ATOM   9886  N  N   . GLY D 2 139 ? 134.648 125.714 194.983 1.00 147.19 ? 116  GLY D N   1 
ATOM   9887  C  CA  . GLY D 2 139 ? 134.759 126.320 196.294 1.00 146.44 ? 116  GLY D CA  1 
ATOM   9888  C  C   . GLY D 2 139 ? 135.496 127.643 196.199 1.00 145.75 ? 116  GLY D C   1 
ATOM   9889  O  O   . GLY D 2 139 ? 136.323 127.846 195.314 1.00 144.79 ? 116  GLY D O   1 
ATOM   9890  N  N   . PHE D 2 140 ? 135.193 128.546 197.127 1.00 150.89 ? 117  PHE D N   1 
ATOM   9891  C  CA  . PHE D 2 140 ? 135.728 129.895 197.050 1.00 151.75 ? 117  PHE D CA  1 
ATOM   9892  C  C   . PHE D 2 140 ? 135.811 130.500 198.443 1.00 152.31 ? 117  PHE D C   1 
ATOM   9893  O  O   . PHE D 2 140 ? 135.184 130.023 199.392 1.00 151.58 ? 117  PHE D O   1 
ATOM   9894  C  CB  . PHE D 2 140 ? 134.872 130.779 196.136 1.00 150.82 ? 117  PHE D CB  1 
ATOM   9895  C  CG  . PHE D 2 140 ? 133.441 130.885 196.570 1.00 150.74 ? 117  PHE D CG  1 
ATOM   9896  C  CD1 . PHE D 2 140 ? 132.517 129.927 196.191 1.00 150.43 ? 117  PHE D CD1 1 
ATOM   9897  C  CD2 . PHE D 2 140 ? 133.019 131.941 197.358 1.00 150.66 ? 117  PHE D CD2 1 
ATOM   9898  C  CE1 . PHE D 2 140 ? 131.201 130.017 196.593 1.00 151.38 ? 117  PHE D CE1 1 
ATOM   9899  C  CE2 . PHE D 2 140 ? 131.705 132.038 197.761 1.00 150.36 ? 117  PHE D CE2 1 
ATOM   9900  C  CZ  . PHE D 2 140 ? 130.794 131.075 197.379 1.00 150.89 ? 117  PHE D CZ  1 
ATOM   9901  N  N   . SER D 2 141 ? 136.602 131.566 198.546 1.00 149.44 ? 118  SER D N   1 
ATOM   9902  C  CA  . SER D 2 141 ? 136.732 132.312 199.795 1.00 148.40 ? 118  SER D CA  1 
ATOM   9903  C  C   . SER D 2 141 ? 137.143 133.735 199.441 1.00 148.77 ? 118  SER D C   1 
ATOM   9904  O  O   . SER D 2 141 ? 138.244 133.949 198.923 1.00 148.53 ? 118  SER D O   1 
ATOM   9905  C  CB  . SER D 2 141 ? 137.748 131.654 200.722 1.00 147.80 ? 118  SER D CB  1 
ATOM   9906  O  OG  . SER D 2 141 ? 138.939 131.331 200.027 1.00 147.59 ? 118  SER D OG  1 
ATOM   9907  N  N   . THR D 2 142 ? 136.260 134.693 199.711 1.00 146.40 ? 119  THR D N   1 
ATOM   9908  C  CA  . THR D 2 142 ? 136.517 136.092 199.394 1.00 146.23 ? 119  THR D CA  1 
ATOM   9909  C  C   . THR D 2 142 ? 135.572 136.959 200.212 1.00 146.64 ? 119  THR D C   1 
ATOM   9910  O  O   . THR D 2 142 ? 134.629 136.470 200.839 1.00 145.59 ? 119  THR D O   1 
ATOM   9911  C  CB  . THR D 2 142 ? 136.344 136.372 197.898 1.00 145.76 ? 119  THR D CB  1 
ATOM   9912  O  OG1 . THR D 2 142 ? 136.890 137.659 197.586 1.00 145.13 ? 119  THR D OG1 1 
ATOM   9913  C  CG2 . THR D 2 142 ? 134.869 136.353 197.526 1.00 145.60 ? 119  THR D CG2 1 
ATOM   9914  N  N   . VAL D 2 143 ? 135.842 138.265 200.197 1.00 153.27 ? 120  VAL D N   1 
ATOM   9915  C  CA  . VAL D 2 143 ? 135.008 139.257 200.859 1.00 152.88 ? 120  VAL D CA  1 
ATOM   9916  C  C   . VAL D 2 143 ? 134.433 140.267 199.875 1.00 152.30 ? 120  VAL D C   1 
ATOM   9917  O  O   . VAL D 2 143 ? 133.793 141.234 200.289 1.00 152.00 ? 120  VAL D O   1 
ATOM   9918  C  CB  . VAL D 2 143 ? 135.779 139.973 201.986 1.00 151.72 ? 120  VAL D CB  1 
ATOM   9919  C  CG1 . VAL D 2 143 ? 136.255 138.971 203.025 1.00 150.76 ? 120  VAL D CG1 1 
ATOM   9920  C  CG2 . VAL D 2 143 ? 136.951 140.754 201.412 1.00 150.99 ? 120  VAL D CG2 1 
ATOM   9921  N  N   . GLN D 2 144 ? 134.653 140.066 198.578 1.00 148.25 ? 121  GLN D N   1 
ATOM   9922  C  CA  . GLN D 2 144 ? 134.157 141.000 197.577 1.00 147.45 ? 121  GLN D CA  1 
ATOM   9923  C  C   . GLN D 2 144 ? 132.635 140.977 197.519 1.00 148.53 ? 121  GLN D C   1 
ATOM   9924  O  O   . GLN D 2 144 ? 132.007 139.918 197.611 1.00 148.72 ? 121  GLN D O   1 
ATOM   9925  C  CB  . GLN D 2 144 ? 134.737 140.666 196.203 1.00 146.83 ? 121  GLN D CB  1 
ATOM   9926  C  CG  . GLN D 2 144 ? 136.154 141.163 195.987 1.00 146.46 ? 121  GLN D CG  1 
ATOM   9927  C  CD  . GLN D 2 144 ? 136.296 141.965 194.709 1.00 146.89 ? 121  GLN D CD  1 
ATOM   9928  O  OE1 . GLN D 2 144 ? 135.369 142.038 193.904 1.00 147.44 ? 121  GLN D OE1 1 
ATOM   9929  N  NE2 . GLN D 2 144 ? 137.460 142.574 194.518 1.00 147.12 ? 121  GLN D NE2 1 
ATOM   9930  N  N   . LYS D 2 145 ? 132.043 142.160 197.363 1.00 149.03 ? 122  LYS D N   1 
ATOM   9931  C  CA  . LYS D 2 145 ? 130.595 142.284 197.259 1.00 149.03 ? 122  LYS D CA  1 
ATOM   9932  C  C   . LYS D 2 145 ? 130.095 142.148 195.827 1.00 148.83 ? 122  LYS D C   1 
ATOM   9933  O  O   . LYS D 2 145 ? 128.968 141.685 195.615 1.00 148.13 ? 122  LYS D O   1 
ATOM   9934  C  CB  . LYS D 2 145 ? 130.143 143.629 197.836 1.00 148.32 ? 122  LYS D CB  1 
ATOM   9935  C  CG  . LYS D 2 145 ? 128.710 143.645 198.340 1.00 148.57 ? 122  LYS D CG  1 
ATOM   9936  C  CD  . LYS D 2 145 ? 128.447 144.872 199.199 1.00 148.13 ? 122  LYS D CD  1 
ATOM   9937  C  CE  . LYS D 2 145 ? 126.981 144.980 199.583 1.00 147.49 ? 122  LYS D CE  1 
ATOM   9938  N  NZ  . LYS D 2 145 ? 126.122 145.306 198.411 1.00 147.06 ? 122  LYS D NZ  1 
ATOM   9939  N  N   . GLU D 2 146 ? 130.904 142.539 194.843 1.00 150.63 ? 123  GLU D N   1 
ATOM   9940  C  CA  . GLU D 2 146 ? 130.533 142.469 193.432 1.00 150.77 ? 123  GLU D CA  1 
ATOM   9941  C  C   . GLU D 2 146 ? 131.685 141.836 192.665 1.00 150.65 ? 123  GLU D C   1 
ATOM   9942  O  O   . GLU D 2 146 ? 132.750 142.446 192.529 1.00 150.95 ? 123  GLU D O   1 
ATOM   9943  C  CB  . GLU D 2 146 ? 130.210 143.856 192.874 1.00 150.41 ? 123  GLU D CB  1 
ATOM   9944  C  CG  . GLU D 2 146 ? 129.203 144.648 193.690 1.00 149.91 ? 123  GLU D CG  1 
ATOM   9945  C  CD  . GLU D 2 146 ? 127.831 144.008 193.701 1.00 150.04 ? 123  GLU D CD  1 
ATOM   9946  O  OE1 . GLU D 2 146 ? 127.476 143.347 192.702 1.00 150.42 ? 123  GLU D OE1 1 
ATOM   9947  O  OE2 . GLU D 2 146 ? 127.108 144.166 194.706 1.00 149.25 ? 123  GLU D OE2 1 
ATOM   9948  N  N   . ALA D 2 147 ? 131.475 140.623 192.159 1.00 147.39 ? 124  ALA D N   1 
ATOM   9949  C  CA  . ALA D 2 147 ? 132.516 139.942 191.402 1.00 147.03 ? 124  ALA D CA  1 
ATOM   9950  C  C   . ALA D 2 147 ? 131.881 138.873 190.527 1.00 147.43 ? 124  ALA D C   1 
ATOM   9951  O  O   . ALA D 2 147 ? 130.728 138.488 190.726 1.00 146.59 ? 124  ALA D O   1 
ATOM   9952  C  CB  . ALA D 2 147 ? 133.571 139.325 192.326 1.00 145.75 ? 124  ALA D CB  1 
ATOM   9953  N  N   . VAL D 2 148 ? 132.653 138.400 189.551 1.00 139.65 ? 125  VAL D N   1 
ATOM   9954  C  CA  . VAL D 2 148 ? 132.245 137.314 188.667 1.00 138.13 ? 125  VAL D CA  1 
ATOM   9955  C  C   . VAL D 2 148 ? 133.301 136.222 188.747 1.00 137.23 ? 125  VAL D C   1 
ATOM   9956  O  O   . VAL D 2 148 ? 134.488 136.484 188.520 1.00 136.30 ? 125  VAL D O   1 
ATOM   9957  C  CB  . VAL D 2 148 ? 132.068 137.793 187.213 1.00 137.67 ? 125  VAL D CB  1 
ATOM   9958  C  CG1 . VAL D 2 148 ? 131.768 136.615 186.298 1.00 137.15 ? 125  VAL D CG1 1 
ATOM   9959  C  CG2 . VAL D 2 148 ? 130.967 138.839 187.127 1.00 137.39 ? 125  VAL D CG2 1 
ATOM   9960  N  N   . LEU D 2 149 ? 132.874 134.999 189.064 1.00 133.61 ? 126  LEU D N   1 
ATOM   9961  C  CA  . LEU D 2 149 ? 133.811 133.903 189.287 1.00 134.15 ? 126  LEU D CA  1 
ATOM   9962  C  C   . LEU D 2 149 ? 134.183 133.203 187.981 1.00 134.96 ? 126  LEU D C   1 
ATOM   9963  O  O   . LEU D 2 149 ? 135.356 133.175 187.597 1.00 133.62 ? 126  LEU D O   1 
ATOM   9964  C  CB  . LEU D 2 149 ? 133.219 132.899 190.284 1.00 133.78 ? 126  LEU D CB  1 
ATOM   9965  C  CG  . LEU D 2 149 ? 132.934 133.392 191.705 1.00 133.92 ? 126  LEU D CG  1 
ATOM   9966  C  CD1 . LEU D 2 149 ? 131.517 133.930 191.821 1.00 134.56 ? 126  LEU D CD1 1 
ATOM   9967  C  CD2 . LEU D 2 149 ? 133.171 132.279 192.714 1.00 133.34 ? 126  LEU D CD2 1 
ATOM   9968  N  N   . VAL D 2 150 ? 133.193 132.643 187.289 1.00 130.22 ? 127  VAL D N   1 
ATOM   9969  C  CA  . VAL D 2 150 ? 133.423 131.902 186.054 1.00 128.85 ? 127  VAL D CA  1 
ATOM   9970  C  C   . VAL D 2 150 ? 132.380 132.317 185.024 1.00 127.24 ? 127  VAL D C   1 
ATOM   9971  O  O   . VAL D 2 150 ? 131.195 132.463 185.343 1.00 126.35 ? 127  VAL D O   1 
ATOM   9972  C  CB  . VAL D 2 150 ? 133.400 130.375 186.296 1.00 128.66 ? 127  VAL D CB  1 
ATOM   9973  C  CG1 . VAL D 2 150 ? 132.084 129.941 186.927 1.00 128.17 ? 127  VAL D CG1 1 
ATOM   9974  C  CG2 . VAL D 2 150 ? 133.656 129.619 185.000 1.00 128.07 ? 127  VAL D CG2 1 
ATOM   9975  N  N   . ARG D 2 151 ? 132.830 132.524 183.788 1.00 126.63 ? 128  ARG D N   1 
ATOM   9976  C  CA  . ARG D 2 151 ? 131.962 132.854 182.666 1.00 126.78 ? 128  ARG D CA  1 
ATOM   9977  C  C   . ARG D 2 151 ? 132.231 131.870 181.541 1.00 128.62 ? 128  ARG D C   1 
ATOM   9978  O  O   . ARG D 2 151 ? 133.388 131.646 181.170 1.00 129.07 ? 128  ARG D O   1 
ATOM   9979  C  CB  . ARG D 2 151 ? 132.190 134.290 182.179 1.00 127.63 ? 128  ARG D CB  1 
ATOM   9980  C  CG  . ARG D 2 151 ? 131.392 134.645 180.933 1.00 126.44 ? 128  ARG D CG  1 
ATOM   9981  C  CD  . ARG D 2 151 ? 129.940 134.934 181.270 1.00 127.21 ? 128  ARG D CD  1 
ATOM   9982  N  NE  . ARG D 2 151 ? 129.132 135.123 180.072 1.00 126.81 ? 128  ARG D NE  1 
ATOM   9983  C  CZ  . ARG D 2 151 ? 128.784 136.303 179.578 1.00 126.22 ? 128  ARG D CZ  1 
ATOM   9984  N  NH1 . ARG D 2 151 ? 129.162 137.431 180.156 1.00 126.34 ? 128  ARG D NH1 1 
ATOM   9985  N  NH2 . ARG D 2 151 ? 128.041 136.352 178.477 1.00 127.08 ? 128  ARG D NH2 1 
ATOM   9986  N  N   . VAL D 2 152 ? 131.166 131.284 181.003 1.00 125.34 ? 129  VAL D N   1 
ATOM   9987  C  CA  . VAL D 2 152 ? 131.259 130.278 179.952 1.00 123.65 ? 129  VAL D CA  1 
ATOM   9988  C  C   . VAL D 2 152 ? 130.577 130.837 178.711 1.00 121.74 ? 129  VAL D C   1 
ATOM   9989  O  O   . VAL D 2 152 ? 129.404 131.226 178.760 1.00 120.72 ? 129  VAL D O   1 
ATOM   9990  C  CB  . VAL D 2 152 ? 130.626 128.950 180.389 1.00 122.46 ? 129  VAL D CB  1 
ATOM   9991  C  CG1 . VAL D 2 152 ? 130.845 127.890 179.331 1.00 123.09 ? 129  VAL D CG1 1 
ATOM   9992  C  CG2 . VAL D 2 152 ? 131.195 128.509 181.735 1.00 123.13 ? 129  VAL D CG2 1 
ATOM   9993  N  N   . ASP D 2 153 ? 131.307 130.874 177.602 1.00 120.99 ? 130  ASP D N   1 
ATOM   9994  C  CA  . ASP D 2 153 ? 130.844 131.509 176.379 1.00 121.49 ? 130  ASP D CA  1 
ATOM   9995  C  C   . ASP D 2 153 ? 130.667 130.488 175.262 1.00 121.56 ? 130  ASP D C   1 
ATOM   9996  O  O   . ASP D 2 153 ? 131.255 129.404 175.273 1.00 122.65 ? 130  ASP D O   1 
ATOM   9997  C  CB  . ASP D 2 153 ? 131.817 132.606 175.934 1.00 123.34 ? 130  ASP D CB  1 
ATOM   9998  C  CG  . ASP D 2 153 ? 131.391 133.977 176.405 1.00 124.55 ? 130  ASP D CG  1 
ATOM   9999  O  OD1 . ASP D 2 153 ? 130.169 134.201 176.530 1.00 124.44 ? 130  ASP D OD1 1 
ATOM   10000 O  OD2 . ASP D 2 153 ? 132.272 134.825 176.657 1.00 123.82 ? 130  ASP D OD2 1 
ATOM   10001 N  N   . SER D 2 154 ? 129.827 130.851 174.297 1.00 115.31 ? 131  SER D N   1 
ATOM   10002 C  CA  . SER D 2 154 ? 129.629 130.060 173.093 1.00 113.31 ? 131  SER D CA  1 
ATOM   10003 C  C   . SER D 2 154 ? 130.592 130.542 172.011 1.00 113.05 ? 131  SER D C   1 
ATOM   10004 O  O   . SER D 2 154 ? 131.469 131.374 172.256 1.00 115.98 ? 131  SER D O   1 
ATOM   10005 C  CB  . SER D 2 154 ? 128.176 130.149 172.638 1.00 113.10 ? 131  SER D CB  1 
ATOM   10006 O  OG  . SER D 2 154 ? 127.297 129.958 173.729 1.00 115.14 ? 131  SER D OG  1 
ATOM   10007 N  N   . SER D 2 155 ? 130.428 130.037 170.792 1.00 109.49 ? 132  SER D N   1 
ATOM   10008 C  CA  . SER D 2 155 ? 131.266 130.456 169.677 1.00 112.51 ? 132  SER D CA  1 
ATOM   10009 C  C   . SER D 2 155 ? 130.741 131.775 169.111 1.00 113.29 ? 132  SER D C   1 
ATOM   10010 O  O   . SER D 2 155 ? 129.879 132.435 169.698 1.00 112.49 ? 132  SER D O   1 
ATOM   10011 C  CB  . SER D 2 155 ? 131.330 129.358 168.619 1.00 112.01 ? 132  SER D CB  1 
ATOM   10012 O  OG  . SER D 2 155 ? 132.177 128.302 169.034 1.00 111.17 ? 132  SER D OG  1 
ATOM   10013 N  N   . SER D 2 156 ? 131.268 132.179 167.957 1.00 114.36 ? 133  SER D N   1 
ATOM   10014 C  CA  . SER D 2 156 ? 130.870 133.440 167.347 1.00 114.20 ? 133  SER D CA  1 
ATOM   10015 C  C   . SER D 2 156 ? 129.405 133.397 166.927 1.00 114.32 ? 133  SER D C   1 
ATOM   10016 O  O   . SER D 2 156 ? 128.947 132.418 166.330 1.00 115.40 ? 133  SER D O   1 
ATOM   10017 C  CB  . SER D 2 156 ? 131.756 133.746 166.142 1.00 115.19 ? 133  SER D CB  1 
ATOM   10018 O  OG  . SER D 2 156 ? 131.979 132.583 165.365 1.00 114.41 ? 133  SER D OG  1 
ATOM   10019 N  N   . GLY D 2 157 ? 128.679 134.455 167.237 1.00 111.81 ? 134  GLY D N   1 
ATOM   10020 C  CA  . GLY D 2 157 ? 127.278 134.581 166.844 1.00 112.43 ? 134  GLY D CA  1 
ATOM   10021 C  C   . GLY D 2 157 ? 126.245 134.086 167.834 1.00 113.51 ? 134  GLY D C   1 
ATOM   10022 O  O   . GLY D 2 157 ? 125.278 134.788 168.126 1.00 114.72 ? 134  GLY D O   1 
ATOM   10023 N  N   . LEU D 2 158 ? 126.434 132.876 168.354 1.00 107.20 ? 135  LEU D N   1 
ATOM   10024 C  CA  . LEU D 2 158 ? 125.459 132.291 169.263 1.00 105.82 ? 135  LEU D CA  1 
ATOM   10025 C  C   . LEU D 2 158 ? 125.409 133.069 170.573 1.00 106.50 ? 135  LEU D C   1 
ATOM   10026 O  O   . LEU D 2 158 ? 126.442 133.453 171.128 1.00 106.58 ? 135  LEU D O   1 
ATOM   10027 C  CB  . LEU D 2 158 ? 125.798 130.824 169.526 1.00 105.58 ? 135  LEU D CB  1 
ATOM   10028 C  CG  . LEU D 2 158 ? 126.407 130.064 168.344 1.00 104.41 ? 135  LEU D CG  1 
ATOM   10029 C  CD1 . LEU D 2 158 ? 126.935 128.711 168.787 1.00 103.98 ? 135  LEU D CD1 1 
ATOM   10030 C  CD2 . LEU D 2 158 ? 125.394 129.902 167.219 1.00 102.87 ? 135  LEU D CD2 1 
ATOM   10031 N  N   . GLY D 2 159 ? 124.195 133.298 171.067 1.00 114.52 ? 136  GLY D N   1 
ATOM   10032 C  CA  . GLY D 2 159 ? 124.000 134.094 172.263 1.00 115.42 ? 136  GLY D CA  1 
ATOM   10033 C  C   . GLY D 2 159 ? 123.846 133.270 173.523 1.00 115.94 ? 136  GLY D C   1 
ATOM   10034 O  O   . GLY D 2 159 ? 123.362 133.766 174.545 1.00 115.42 ? 136  GLY D O   1 
ATOM   10035 N  N   . ASP D 2 160 ? 124.249 132.004 173.460 1.00 108.75 ? 137  ASP D N   1 
ATOM   10036 C  CA  . ASP D 2 160 ? 124.148 131.113 174.607 1.00 108.00 ? 137  ASP D CA  1 
ATOM   10037 C  C   . ASP D 2 160 ? 125.269 131.430 175.590 1.00 107.42 ? 137  ASP D C   1 
ATOM   10038 O  O   . ASP D 2 160 ? 126.431 131.551 175.191 1.00 107.51 ? 137  ASP D O   1 
ATOM   10039 C  CB  . ASP D 2 160 ? 124.240 129.658 174.145 1.00 106.83 ? 137  ASP D CB  1 
ATOM   10040 C  CG  . ASP D 2 160 ? 122.954 129.162 173.518 1.00 106.97 ? 137  ASP D CG  1 
ATOM   10041 O  OD1 . ASP D 2 160 ? 121.924 129.131 174.217 1.00 106.84 ? 137  ASP D OD1 1 
ATOM   10042 O  OD2 . ASP D 2 160 ? 122.976 128.796 172.323 1.00 106.20 ? 137  ASP D OD2 1 
ATOM   10043 N  N   . TYR D 2 161 ? 124.932 131.572 176.872 1.00 117.51 ? 138  TYR D N   1 
ATOM   10044 C  CA  . TYR D 2 161 ? 125.967 131.923 177.838 1.00 118.21 ? 138  TYR D CA  1 
ATOM   10045 C  C   . TYR D 2 161 ? 125.618 131.358 179.208 1.00 120.05 ? 138  TYR D C   1 
ATOM   10046 O  O   . TYR D 2 161 ? 124.466 131.030 179.494 1.00 120.52 ? 138  TYR D O   1 
ATOM   10047 C  CB  . TYR D 2 161 ? 126.199 133.451 177.884 1.00 118.30 ? 138  TYR D CB  1 
ATOM   10048 C  CG  . TYR D 2 161 ? 125.214 134.306 178.677 1.00 119.32 ? 138  TYR D CG  1 
ATOM   10049 C  CD1 . TYR D 2 161 ? 125.086 134.184 180.059 1.00 119.45 ? 138  TYR D CD1 1 
ATOM   10050 C  CD2 . TYR D 2 161 ? 124.427 135.255 178.036 1.00 119.71 ? 138  TYR D CD2 1 
ATOM   10051 C  CE1 . TYR D 2 161 ? 124.199 134.967 180.771 1.00 119.65 ? 138  TYR D CE1 1 
ATOM   10052 C  CE2 . TYR D 2 161 ? 123.536 136.044 178.743 1.00 120.54 ? 138  TYR D CE2 1 
ATOM   10053 C  CZ  . TYR D 2 161 ? 123.427 135.895 180.108 1.00 120.60 ? 138  TYR D CZ  1 
ATOM   10054 O  OH  . TYR D 2 161 ? 122.542 136.678 180.812 1.00 120.67 ? 138  TYR D OH  1 
ATOM   10055 N  N   . LEU D 2 162 ? 126.644 131.251 180.051 1.00 124.73 ? 139  LEU D N   1 
ATOM   10056 C  CA  . LEU D 2 162 ? 126.495 130.852 181.445 1.00 124.05 ? 139  LEU D CA  1 
ATOM   10057 C  C   . LEU D 2 162 ? 127.431 131.703 182.287 1.00 124.97 ? 139  LEU D C   1 
ATOM   10058 O  O   . LEU D 2 162 ? 128.599 131.877 181.927 1.00 125.35 ? 139  LEU D O   1 
ATOM   10059 C  CB  . LEU D 2 162 ? 126.809 129.365 181.638 1.00 123.93 ? 139  LEU D CB  1 
ATOM   10060 C  CG  . LEU D 2 162 ? 126.843 128.859 183.080 1.00 124.43 ? 139  LEU D CG  1 
ATOM   10061 C  CD1 . LEU D 2 162 ? 125.435 128.668 183.604 1.00 124.98 ? 139  LEU D CD1 1 
ATOM   10062 C  CD2 . LEU D 2 162 ? 127.634 127.565 183.180 1.00 124.66 ? 139  LEU D CD2 1 
ATOM   10063 N  N   . GLU D 2 163 ? 126.927 132.231 183.402 1.00 132.43 ? 140  GLU D N   1 
ATOM   10064 C  CA  . GLU D 2 163 ? 127.712 133.122 184.241 1.00 132.85 ? 140  GLU D CA  1 
ATOM   10065 C  C   . GLU D 2 163 ? 127.424 132.844 185.708 1.00 132.99 ? 140  GLU D C   1 
ATOM   10066 O  O   . GLU D 2 163 ? 126.272 132.627 186.094 1.00 132.37 ? 140  GLU D O   1 
ATOM   10067 C  CB  . GLU D 2 163 ? 127.410 134.589 183.913 1.00 133.24 ? 140  GLU D CB  1 
ATOM   10068 C  CG  . GLU D 2 163 ? 128.373 135.583 184.533 1.00 133.82 ? 140  GLU D CG  1 
ATOM   10069 C  CD  . GLU D 2 163 ? 128.029 137.017 184.180 1.00 134.16 ? 140  GLU D CD  1 
ATOM   10070 O  OE1 . GLU D 2 163 ? 126.893 137.261 183.721 1.00 133.09 ? 140  GLU D OE1 1 
ATOM   10071 O  OE2 . GLU D 2 163 ? 128.896 137.898 184.356 1.00 134.57 ? 140  GLU D OE2 1 
ATOM   10072 N  N   . LEU D 2 164 ? 128.480 132.845 186.518 1.00 136.87 ? 141  LEU D N   1 
ATOM   10073 C  CA  . LEU D 2 164 ? 128.381 132.711 187.965 1.00 136.51 ? 141  LEU D CA  1 
ATOM   10074 C  C   . LEU D 2 164 ? 129.012 133.938 188.606 1.00 138.30 ? 141  LEU D C   1 
ATOM   10075 O  O   . LEU D 2 164 ? 130.162 134.276 188.305 1.00 138.01 ? 141  LEU D O   1 
ATOM   10076 C  CB  . LEU D 2 164 ? 129.076 131.433 188.446 1.00 135.40 ? 141  LEU D CB  1 
ATOM   10077 C  CG  . LEU D 2 164 ? 129.480 131.359 189.919 1.00 136.41 ? 141  LEU D CG  1 
ATOM   10078 C  CD1 . LEU D 2 164 ? 128.255 131.373 190.814 1.00 136.62 ? 141  LEU D CD1 1 
ATOM   10079 C  CD2 . LEU D 2 164 ? 130.324 130.122 190.185 1.00 137.17 ? 141  LEU D CD2 1 
ATOM   10080 N  N   . HIS D 2 165 ? 128.268 134.604 189.487 1.00 143.48 ? 142  HIS D N   1 
ATOM   10081 C  CA  . HIS D 2 165 ? 128.749 135.861 190.038 1.00 142.86 ? 142  HIS D CA  1 
ATOM   10082 C  C   . HIS D 2 165 ? 128.153 136.101 191.417 1.00 142.98 ? 142  HIS D C   1 
ATOM   10083 O  O   . HIS D 2 165 ? 127.070 135.609 191.740 1.00 143.04 ? 142  HIS D O   1 
ATOM   10084 C  CB  . HIS D 2 165 ? 128.415 137.033 189.107 1.00 141.64 ? 142  HIS D CB  1 
ATOM   10085 C  CG  . HIS D 2 165 ? 127.037 136.969 188.526 1.00 141.73 ? 142  HIS D CG  1 
ATOM   10086 N  ND1 . HIS D 2 165 ? 125.915 136.744 189.293 1.00 141.23 ? 142  HIS D ND1 1 
ATOM   10087 C  CD2 . HIS D 2 165 ? 126.601 137.103 187.251 1.00 141.15 ? 142  HIS D CD2 1 
ATOM   10088 C  CE1 . HIS D 2 165 ? 124.846 136.740 188.517 1.00 140.47 ? 142  HIS D CE1 1 
ATOM   10089 N  NE2 . HIS D 2 165 ? 125.235 136.956 187.273 1.00 141.53 ? 142  HIS D NE2 1 
ATOM   10090 N  N   . ILE D 2 166 ? 128.871 136.885 192.217 1.00 145.01 ? 143  ILE D N   1 
ATOM   10091 C  CA  . ILE D 2 166 ? 128.421 137.313 193.536 1.00 145.18 ? 143  ILE D CA  1 
ATOM   10092 C  C   . ILE D 2 166 ? 128.044 138.784 193.437 1.00 145.05 ? 143  ILE D C   1 
ATOM   10093 O  O   . ILE D 2 166 ? 128.890 139.631 193.120 1.00 144.97 ? 143  ILE D O   1 
ATOM   10094 C  CB  . ILE D 2 166 ? 129.499 137.090 194.607 1.00 146.02 ? 143  ILE D CB  1 
ATOM   10095 C  CG1 . ILE D 2 166 ? 129.949 135.627 194.616 1.00 146.03 ? 143  ILE D CG1 1 
ATOM   10096 C  CG2 . ILE D 2 166 ? 128.983 137.512 195.976 1.00 145.73 ? 143  ILE D CG2 1 
ATOM   10097 C  CD1 . ILE D 2 166 ? 130.682 135.213 195.875 1.00 145.10 ? 143  ILE D CD1 1 
ATOM   10098 N  N   . HIS D 2 167 ? 126.774 139.083 193.703 1.00 146.28 ? 144  HIS D N   1 
ATOM   10099 C  CA  . HIS D 2 167 ? 126.243 140.437 193.650 1.00 147.37 ? 144  HIS D CA  1 
ATOM   10100 C  C   . HIS D 2 167 ? 125.585 140.761 194.983 1.00 147.38 ? 144  HIS D C   1 
ATOM   10101 O  O   . HIS D 2 167 ? 124.754 139.987 195.471 1.00 146.22 ? 144  HIS D O   1 
ATOM   10102 C  CB  . HIS D 2 167 ? 125.236 140.586 192.504 1.00 146.91 ? 144  HIS D CB  1 
ATOM   10103 C  CG  . HIS D 2 167 ? 124.667 141.964 192.370 1.00 147.44 ? 144  HIS D CG  1 
ATOM   10104 N  ND1 . HIS D 2 167 ? 125.372 143.011 191.817 1.00 147.14 ? 144  HIS D ND1 1 
ATOM   10105 C  CD2 . HIS D 2 167 ? 123.455 142.465 192.710 1.00 146.72 ? 144  HIS D CD2 1 
ATOM   10106 C  CE1 . HIS D 2 167 ? 124.621 144.098 191.827 1.00 146.54 ? 144  HIS D CE1 1 
ATOM   10107 N  NE2 . HIS D 2 167 ? 123.454 143.794 192.363 1.00 146.47 ? 144  HIS D NE2 1 
ATOM   10108 N  N   . GLN D 2 168 ? 125.967 141.899 195.567 1.00 147.74 ? 145  GLN D N   1 
ATOM   10109 C  CA  . GLN D 2 168 ? 125.396 142.381 196.826 1.00 147.18 ? 145  GLN D CA  1 
ATOM   10110 C  C   . GLN D 2 168 ? 125.474 141.320 197.921 1.00 147.19 ? 145  GLN D C   1 
ATOM   10111 O  O   . GLN D 2 168 ? 124.558 141.160 198.730 1.00 147.27 ? 145  GLN D O   1 
ATOM   10112 C  CB  . GLN D 2 168 ? 123.955 142.856 196.629 1.00 147.39 ? 145  GLN D CB  1 
ATOM   10113 C  CG  . GLN D 2 168 ? 123.823 144.077 195.735 1.00 147.59 ? 145  GLN D CG  1 
ATOM   10114 C  CD  . GLN D 2 168 ? 122.446 144.706 195.807 1.00 147.47 ? 145  GLN D CD  1 
ATOM   10115 O  OE1 . GLN D 2 168 ? 121.851 144.800 196.880 1.00 147.35 ? 145  GLN D OE1 1 
ATOM   10116 N  NE2 . GLN D 2 168 ? 121.933 145.140 194.662 1.00 146.89 ? 145  GLN D NE2 1 
ATOM   10117 N  N   . GLY D 2 169 ? 126.583 140.585 197.945 1.00 143.68 ? 146  GLY D N   1 
ATOM   10118 C  CA  . GLY D 2 169 ? 126.801 139.571 198.953 1.00 143.30 ? 146  GLY D CA  1 
ATOM   10119 C  C   . GLY D 2 169 ? 126.058 138.271 198.742 1.00 143.68 ? 146  GLY D C   1 
ATOM   10120 O  O   . GLY D 2 169 ? 126.124 137.394 199.613 1.00 142.27 ? 146  GLY D O   1 
ATOM   10121 N  N   . LYS D 2 170 ? 125.354 138.111 197.623 1.00 147.34 ? 147  LYS D N   1 
ATOM   10122 C  CA  . LYS D 2 170 ? 124.629 136.885 197.318 1.00 146.91 ? 147  LYS D CA  1 
ATOM   10123 C  C   . LYS D 2 170 ? 125.198 136.272 196.048 1.00 146.37 ? 147  LYS D C   1 
ATOM   10124 O  O   . LYS D 2 170 ? 125.350 136.963 195.037 1.00 145.69 ? 147  LYS D O   1 
ATOM   10125 C  CB  . LYS D 2 170 ? 123.129 137.150 197.150 1.00 146.76 ? 147  LYS D CB  1 
ATOM   10126 C  CG  . LYS D 2 170 ? 122.631 138.426 197.811 1.00 146.20 ? 147  LYS D CG  1 
ATOM   10127 C  CD  . LYS D 2 170 ? 122.505 138.260 199.317 1.00 145.67 ? 147  LYS D CD  1 
ATOM   10128 C  CE  . LYS D 2 170 ? 121.808 139.456 199.947 1.00 145.85 ? 147  LYS D CE  1 
ATOM   10129 N  NZ  . LYS D 2 170 ? 122.384 140.749 199.484 1.00 145.39 ? 147  LYS D NZ  1 
ATOM   10130 N  N   . ILE D 2 171 ? 125.517 134.984 196.104 1.00 146.18 ? 148  ILE D N   1 
ATOM   10131 C  CA  . ILE D 2 171 ? 126.036 134.284 194.936 1.00 146.40 ? 148  ILE D CA  1 
ATOM   10132 C  C   . ILE D 2 171 ? 124.872 133.810 194.076 1.00 146.18 ? 148  ILE D C   1 
ATOM   10133 O  O   . ILE D 2 171 ? 123.787 133.490 194.576 1.00 145.40 ? 148  ILE D O   1 
ATOM   10134 C  CB  . ILE D 2 171 ? 126.950 133.115 195.360 1.00 146.12 ? 148  ILE D CB  1 
ATOM   10135 C  CG1 . ILE D 2 171 ? 127.789 132.637 194.174 1.00 144.70 ? 148  ILE D CG1 1 
ATOM   10136 C  CG2 . ILE D 2 171 ? 126.137 131.969 195.949 1.00 145.26 ? 148  ILE D CG2 1 
ATOM   10137 C  CD1 . ILE D 2 171 ? 128.775 131.551 194.522 1.00 144.60 ? 148  ILE D CD1 1 
ATOM   10138 N  N   . GLY D 2 172 ? 125.088 133.779 192.763 1.00 141.28 ? 149  GLY D N   1 
ATOM   10139 C  CA  . GLY D 2 172 ? 124.035 133.395 191.845 1.00 140.41 ? 149  GLY D CA  1 
ATOM   10140 C  C   . GLY D 2 172 ? 124.591 132.988 190.502 1.00 140.65 ? 149  GLY D C   1 
ATOM   10141 O  O   . GLY D 2 172 ? 125.738 133.292 190.156 1.00 140.26 ? 149  GLY D O   1 
ATOM   10142 N  N   . VAL D 2 173 ? 123.757 132.276 189.748 1.00 139.04 ? 150  VAL D N   1 
ATOM   10143 C  CA  . VAL D 2 173 ? 124.100 131.783 188.420 1.00 138.78 ? 150  VAL D CA  1 
ATOM   10144 C  C   . VAL D 2 173 ? 122.999 132.197 187.455 1.00 136.69 ? 150  VAL D C   1 
ATOM   10145 O  O   . VAL D 2 173 ? 121.815 131.959 187.720 1.00 135.40 ? 150  VAL D O   1 
ATOM   10146 C  CB  . VAL D 2 173 ? 124.281 130.252 188.401 1.00 138.38 ? 150  VAL D CB  1 
ATOM   10147 C  CG1 . VAL D 2 173 ? 124.783 129.798 187.043 1.00 137.95 ? 150  VAL D CG1 1 
ATOM   10148 C  CG2 . VAL D 2 173 ? 125.233 129.808 189.499 1.00 137.83 ? 150  VAL D CG2 1 
ATOM   10149 N  N   . LYS D 2 174 ? 123.388 132.808 186.339 1.00 131.49 ? 151  LYS D N   1 
ATOM   10150 C  CA  . LYS D 2 174 ? 122.452 133.211 185.298 1.00 131.94 ? 151  LYS D CA  1 
ATOM   10151 C  C   . LYS D 2 174 ? 122.913 132.641 183.966 1.00 132.58 ? 151  LYS D C   1 
ATOM   10152 O  O   . LYS D 2 174 ? 124.086 132.775 183.601 1.00 132.37 ? 151  LYS D O   1 
ATOM   10153 C  CB  . LYS D 2 174 ? 122.334 134.736 185.211 1.00 132.53 ? 151  LYS D CB  1 
ATOM   10154 C  CG  . LYS D 2 174 ? 121.259 135.216 184.248 1.00 132.13 ? 151  LYS D CG  1 
ATOM   10155 C  CD  . LYS D 2 174 ? 121.096 136.727 184.299 1.00 131.48 ? 151  LYS D CD  1 
ATOM   10156 C  CE  . LYS D 2 174 ? 122.405 137.438 184.001 1.00 131.81 ? 151  LYS D CE  1 
ATOM   10157 N  NZ  . LYS D 2 174 ? 122.247 138.918 184.010 1.00 131.68 ? 151  LYS D NZ  1 
ATOM   10158 N  N   . PHE D 2 175 ? 121.993 132.012 183.240 1.00 126.11 ? 152  PHE D N   1 
ATOM   10159 C  CA  . PHE D 2 175 ? 122.316 131.421 181.951 1.00 124.76 ? 152  PHE D CA  1 
ATOM   10160 C  C   . PHE D 2 175 ? 121.280 131.809 180.907 1.00 124.69 ? 152  PHE D C   1 
ATOM   10161 O  O   . PHE D 2 175 ? 120.096 131.982 181.206 1.00 124.90 ? 152  PHE D O   1 
ATOM   10162 C  CB  . PHE D 2 175 ? 122.424 129.886 182.037 1.00 124.54 ? 152  PHE D CB  1 
ATOM   10163 C  CG  . PHE D 2 175 ? 121.205 129.212 182.603 1.00 124.93 ? 152  PHE D CG  1 
ATOM   10164 C  CD1 . PHE D 2 175 ? 120.129 128.894 181.790 1.00 123.97 ? 152  PHE D CD1 1 
ATOM   10165 C  CD2 . PHE D 2 175 ? 121.143 128.883 183.946 1.00 125.34 ? 152  PHE D CD2 1 
ATOM   10166 C  CE1 . PHE D 2 175 ? 119.012 128.270 182.309 1.00 124.59 ? 152  PHE D CE1 1 
ATOM   10167 C  CE2 . PHE D 2 175 ? 120.028 128.258 184.470 1.00 125.32 ? 152  PHE D CE2 1 
ATOM   10168 C  CZ  . PHE D 2 175 ? 118.962 127.950 183.650 1.00 125.23 ? 152  PHE D CZ  1 
ATOM   10169 N  N   . ASN D 2 176 ? 121.754 131.941 179.671 1.00 117.74 ? 153  ASN D N   1 
ATOM   10170 C  CA  . ASN D 2 176 ? 120.917 132.172 178.499 1.00 116.22 ? 153  ASN D CA  1 
ATOM   10171 C  C   . ASN D 2 176 ? 121.040 130.950 177.601 1.00 115.64 ? 153  ASN D C   1 
ATOM   10172 O  O   . ASN D 2 176 ? 122.116 130.687 177.046 1.00 115.23 ? 153  ASN D O   1 
ATOM   10173 C  CB  . ASN D 2 176 ? 121.335 133.442 177.761 1.00 117.28 ? 153  ASN D CB  1 
ATOM   10174 C  CG  . ASN D 2 176 ? 120.302 133.892 176.749 1.00 116.80 ? 153  ASN D CG  1 
ATOM   10175 O  OD1 . ASN D 2 176 ? 119.098 133.771 176.977 1.00 115.81 ? 153  ASN D OD1 1 
ATOM   10176 N  ND2 . ASN D 2 176 ? 120.767 134.425 175.626 1.00 116.28 ? 153  ASN D ND2 1 
ATOM   10177 N  N   . VAL D 2 177 ? 119.942 130.208 177.468 1.00 112.21 ? 154  VAL D N   1 
ATOM   10178 C  CA  . VAL D 2 177 ? 119.887 128.994 176.667 1.00 110.88 ? 154  VAL D CA  1 
ATOM   10179 C  C   . VAL D 2 177 ? 119.154 129.219 175.352 1.00 109.94 ? 154  VAL D C   1 
ATOM   10180 O  O   . VAL D 2 177 ? 118.919 128.263 174.606 1.00 110.71 ? 154  VAL D O   1 
ATOM   10181 C  CB  . VAL D 2 177 ? 119.255 127.834 177.453 1.00 110.78 ? 154  VAL D CB  1 
ATOM   10182 C  CG1 . VAL D 2 177 ? 120.233 127.300 178.486 1.00 111.57 ? 154  VAL D CG1 1 
ATOM   10183 C  CG2 . VAL D 2 177 ? 117.966 128.287 178.121 1.00 111.77 ? 154  VAL D CG2 1 
ATOM   10184 N  N   . GLY D 2 178 ? 118.780 130.459 175.051 1.00 111.59 ? 155  GLY D N   1 
ATOM   10185 C  CA  . GLY D 2 178 ? 118.160 130.774 173.780 1.00 110.45 ? 155  GLY D CA  1 
ATOM   10186 C  C   . GLY D 2 178 ? 116.865 131.550 173.895 1.00 113.20 ? 155  GLY D C   1 
ATOM   10187 O  O   . GLY D 2 178 ? 116.624 132.477 173.116 1.00 114.00 ? 155  GLY D O   1 
ATOM   10188 N  N   . THR D 2 179 ? 116.023 131.194 174.867 1.00 127.79 ? 156  THR D N   1 
ATOM   10189 C  CA  . THR D 2 179 ? 114.742 131.877 175.020 1.00 128.90 ? 156  THR D CA  1 
ATOM   10190 C  C   . THR D 2 179 ? 114.901 133.182 175.792 1.00 128.93 ? 156  THR D C   1 
ATOM   10191 O  O   . THR D 2 179 ? 114.618 134.265 175.269 1.00 128.00 ? 156  THR D O   1 
ATOM   10192 C  CB  . THR D 2 179 ? 113.733 130.959 175.716 1.00 127.53 ? 156  THR D CB  1 
ATOM   10193 O  OG1 . THR D 2 179 ? 114.397 130.190 176.726 1.00 126.33 ? 156  THR D OG1 1 
ATOM   10194 C  CG2 . THR D 2 179 ? 113.086 130.019 174.710 1.00 126.97 ? 156  THR D CG2 1 
ATOM   10195 N  N   . ASP D 2 180 ? 115.353 133.094 177.040 1.00 135.40 ? 157  ASP D N   1 
ATOM   10196 C  CA  . ASP D 2 180 ? 115.568 134.272 177.867 1.00 135.31 ? 157  ASP D CA  1 
ATOM   10197 C  C   . ASP D 2 180 ? 116.532 133.909 178.985 1.00 135.33 ? 157  ASP D C   1 
ATOM   10198 O  O   . ASP D 2 180 ? 116.776 132.732 179.261 1.00 134.99 ? 157  ASP D O   1 
ATOM   10199 C  CB  . ASP D 2 180 ? 114.252 134.810 178.441 1.00 135.30 ? 157  ASP D CB  1 
ATOM   10200 C  CG  . ASP D 2 180 ? 113.756 136.040 177.706 1.00 135.21 ? 157  ASP D CG  1 
ATOM   10201 O  OD1 . ASP D 2 180 ? 114.597 136.822 177.216 1.00 134.93 ? 157  ASP D OD1 1 
ATOM   10202 O  OD2 . ASP D 2 180 ? 112.524 136.225 177.618 1.00 135.62 ? 157  ASP D OD2 1 
ATOM   10203 N  N   . ASP D 2 181 ? 117.079 134.940 179.623 1.00 132.56 ? 158  ASP D N   1 
ATOM   10204 C  CA  . ASP D 2 181 ? 118.008 134.728 180.723 1.00 132.13 ? 158  ASP D CA  1 
ATOM   10205 C  C   . ASP D 2 181 ? 117.264 134.200 181.944 1.00 131.57 ? 158  ASP D C   1 
ATOM   10206 O  O   . ASP D 2 181 ? 116.215 134.730 182.323 1.00 130.63 ? 158  ASP D O   1 
ATOM   10207 C  CB  . ASP D 2 181 ? 118.730 136.030 181.064 1.00 131.47 ? 158  ASP D CB  1 
ATOM   10208 C  CG  . ASP D 2 181 ? 119.251 136.744 179.834 1.00 130.89 ? 158  ASP D CG  1 
ATOM   10209 O  OD1 . ASP D 2 181 ? 120.021 136.127 179.069 1.00 131.09 ? 158  ASP D OD1 1 
ATOM   10210 O  OD2 . ASP D 2 181 ? 118.889 137.921 179.630 1.00 130.73 ? 158  ASP D OD2 1 
ATOM   10211 N  N   . ILE D 2 182 ? 117.807 133.152 182.558 1.00 132.68 ? 159  ILE D N   1 
ATOM   10212 C  CA  . ILE D 2 182 ? 117.261 132.577 183.780 1.00 132.38 ? 159  ILE D CA  1 
ATOM   10213 C  C   . ILE D 2 182 ? 118.336 132.658 184.852 1.00 133.40 ? 159  ILE D C   1 
ATOM   10214 O  O   . ILE D 2 182 ? 119.456 132.174 184.651 1.00 133.98 ? 159  ILE D O   1 
ATOM   10215 C  CB  . ILE D 2 182 ? 116.797 131.123 183.571 1.00 132.60 ? 159  ILE D CB  1 
ATOM   10216 C  CG1 . ILE D 2 182 ? 115.437 131.094 182.873 1.00 133.25 ? 159  ILE D CG1 1 
ATOM   10217 C  CG2 . ILE D 2 182 ? 116.722 130.390 184.902 1.00 133.02 ? 159  ILE D CG2 1 
ATOM   10218 C  CD1 . ILE D 2 182 ? 114.299 131.603 183.730 1.00 133.68 ? 159  ILE D CD1 1 
ATOM   10219 N  N   . ALA D 2 183 ? 117.997 133.274 185.982 1.00 136.70 ? 160  ALA D N   1 
ATOM   10220 C  CA  . ALA D 2 183 ? 118.935 133.497 187.071 1.00 136.95 ? 160  ALA D CA  1 
ATOM   10221 C  C   . ALA D 2 183 ? 118.397 132.888 188.358 1.00 136.42 ? 160  ALA D C   1 
ATOM   10222 O  O   . ALA D 2 183 ? 117.209 133.016 188.670 1.00 135.14 ? 160  ALA D O   1 
ATOM   10223 C  CB  . ALA D 2 183 ? 119.200 134.992 187.276 1.00 136.09 ? 160  ALA D CB  1 
ATOM   10224 N  N   . ILE D 2 184 ? 119.281 132.225 189.099 1.00 143.95 ? 161  ILE D N   1 
ATOM   10225 C  CA  . ILE D 2 184 ? 118.963 131.665 190.406 1.00 145.14 ? 161  ILE D CA  1 
ATOM   10226 C  C   . ILE D 2 184 ? 120.029 132.129 191.391 1.00 145.71 ? 161  ILE D C   1 
ATOM   10227 O  O   . ILE D 2 184 ? 121.229 131.987 191.130 1.00 145.37 ? 161  ILE D O   1 
ATOM   10228 C  CB  . ILE D 2 184 ? 118.858 130.126 190.360 1.00 144.60 ? 161  ILE D CB  1 
ATOM   10229 C  CG1 . ILE D 2 184 ? 118.449 129.568 191.725 1.00 144.34 ? 161  ILE D CG1 1 
ATOM   10230 C  CG2 . ILE D 2 184 ? 120.145 129.486 189.837 1.00 144.06 ? 161  ILE D CG2 1 
ATOM   10231 C  CD1 . ILE D 2 184 ? 118.013 128.121 191.676 1.00 143.55 ? 161  ILE D CD1 1 
ATOM   10232 N  N   . GLU D 2 185 ? 119.592 132.704 192.510 1.00 152.14 ? 162  GLU D N   1 
ATOM   10233 C  CA  . GLU D 2 185 ? 120.491 133.356 193.450 1.00 152.20 ? 162  GLU D CA  1 
ATOM   10234 C  C   . GLU D 2 185 ? 120.184 132.914 194.873 1.00 153.01 ? 162  GLU D C   1 
ATOM   10235 O  O   . GLU D 2 185 ? 119.031 132.653 195.227 1.00 151.74 ? 162  GLU D O   1 
ATOM   10236 C  CB  . GLU D 2 185 ? 120.383 134.887 193.344 1.00 151.65 ? 162  GLU D CB  1 
ATOM   10237 C  CG  . GLU D 2 185 ? 121.458 135.653 194.097 1.00 151.66 ? 162  GLU D CG  1 
ATOM   10238 C  CD  . GLU D 2 185 ? 121.286 137.155 193.991 1.00 151.75 ? 162  GLU D CD  1 
ATOM   10239 O  OE1 . GLU D 2 185 ? 120.133 137.615 193.854 1.00 151.79 ? 162  GLU D OE1 1 
ATOM   10240 O  OE2 . GLU D 2 185 ? 122.304 137.877 194.045 1.00 151.54 ? 162  GLU D OE2 1 
ATOM   10241 N  N   . GLU D 2 186 ? 121.237 132.835 195.689 1.00 157.77 ? 163  GLU D N   1 
ATOM   10242 C  CA  . GLU D 2 186 ? 121.114 132.510 197.110 1.00 157.38 ? 163  GLU D CA  1 
ATOM   10243 C  C   . GLU D 2 186 ? 120.790 133.797 197.864 1.00 156.63 ? 163  GLU D C   1 
ATOM   10244 O  O   . GLU D 2 186 ? 121.647 134.437 198.479 1.00 156.28 ? 163  GLU D O   1 
ATOM   10245 C  CB  . GLU D 2 186 ? 122.390 131.856 197.624 1.00 156.64 ? 163  GLU D CB  1 
ATOM   10246 C  CG  . GLU D 2 186 ? 122.270 131.269 199.020 1.00 157.07 ? 163  GLU D CG  1 
ATOM   10247 C  CD  . GLU D 2 186 ? 121.292 130.114 199.084 1.00 157.62 ? 163  GLU D CD  1 
ATOM   10248 O  OE1 . GLU D 2 186 ? 121.340 129.243 198.190 1.00 157.63 ? 163  GLU D OE1 1 
ATOM   10249 O  OE2 . GLU D 2 186 ? 120.474 130.078 200.028 1.00 157.15 ? 163  GLU D OE2 1 
ATOM   10250 N  N   . SER D 2 187 ? 119.514 134.182 197.806 1.00 156.00 ? 164  SER D N   1 
ATOM   10251 C  CA  . SER D 2 187 ? 119.094 135.461 198.372 1.00 156.21 ? 164  SER D CA  1 
ATOM   10252 C  C   . SER D 2 187 ? 119.148 135.444 199.895 1.00 156.83 ? 164  SER D C   1 
ATOM   10253 O  O   . SER D 2 187 ? 119.651 136.386 200.518 1.00 156.49 ? 164  SER D O   1 
ATOM   10254 C  CB  . SER D 2 187 ? 117.685 135.807 197.888 1.00 156.14 ? 164  SER D CB  1 
ATOM   10255 O  OG  . SER D 2 187 ? 117.233 137.020 198.463 1.00 156.23 ? 164  SER D OG  1 
ATOM   10256 N  N   . ASN D 2 188 ? 118.635 134.382 200.514 1.00 150.11 ? 165  ASN D N   1 
ATOM   10257 C  CA  . ASN D 2 188 ? 118.502 134.325 201.971 1.00 149.00 ? 165  ASN D CA  1 
ATOM   10258 C  C   . ASN D 2 188 ? 119.787 133.806 202.619 1.00 148.91 ? 165  ASN D C   1 
ATOM   10259 O  O   . ASN D 2 188 ? 119.793 132.825 203.364 1.00 148.62 ? 165  ASN D O   1 
ATOM   10260 C  CB  . ASN D 2 188 ? 117.303 133.464 202.354 1.00 148.37 ? 165  ASN D CB  1 
ATOM   10261 C  CG  . ASN D 2 188 ? 115.997 134.005 201.809 1.00 148.85 ? 165  ASN D CG  1 
ATOM   10262 O  OD1 . ASN D 2 188 ? 115.271 134.719 202.501 1.00 149.18 ? 165  ASN D OD1 1 
ATOM   10263 N  ND2 . ASN D 2 188 ? 115.689 133.665 200.563 1.00 148.33 ? 165  ASN D ND2 1 
ATOM   10264 N  N   . ALA D 2 189 ? 120.888 134.495 202.330 1.00 146.92 ? 166  ALA D N   1 
ATOM   10265 C  CA  . ALA D 2 189 ? 122.186 134.133 202.886 1.00 146.30 ? 166  ALA D CA  1 
ATOM   10266 C  C   . ALA D 2 189 ? 123.162 135.277 202.648 1.00 145.68 ? 166  ALA D C   1 
ATOM   10267 O  O   . ALA D 2 189 ? 122.903 136.190 201.859 1.00 144.69 ? 166  ALA D O   1 
ATOM   10268 C  CB  . ALA D 2 189 ? 122.719 132.835 202.276 1.00 145.31 ? 166  ALA D CB  1 
ATOM   10269 N  N   . ILE D 2 190 ? 124.292 135.211 203.348 1.00 149.09 ? 167  ILE D N   1 
ATOM   10270 C  CA  . ILE D 2 190 ? 125.413 136.122 203.158 1.00 149.89 ? 167  ILE D CA  1 
ATOM   10271 C  C   . ILE D 2 190 ? 126.655 135.277 202.919 1.00 149.82 ? 167  ILE D C   1 
ATOM   10272 O  O   . ILE D 2 190 ? 126.945 134.361 203.697 1.00 149.41 ? 167  ILE D O   1 
ATOM   10273 C  CB  . ILE D 2 190 ? 125.608 137.057 204.368 1.00 149.68 ? 167  ILE D CB  1 
ATOM   10274 C  CG1 . ILE D 2 190 ? 124.577 138.187 204.338 1.00 148.28 ? 167  ILE D CG1 1 
ATOM   10275 C  CG2 . ILE D 2 190 ? 127.023 137.623 204.393 1.00 148.64 ? 167  ILE D CG2 1 
ATOM   10276 C  CD1 . ILE D 2 190 ? 124.776 139.224 205.421 1.00 148.11 ? 167  ILE D CD1 1 
ATOM   10277 N  N   . ILE D 2 191 ? 127.384 135.575 201.846 1.00 150.79 ? 168  ILE D N   1 
ATOM   10278 C  CA  . ILE D 2 191 ? 128.490 134.728 201.423 1.00 150.47 ? 168  ILE D CA  1 
ATOM   10279 C  C   . ILE D 2 191 ? 129.844 135.425 201.477 1.00 150.50 ? 168  ILE D C   1 
ATOM   10280 O  O   . ILE D 2 191 ? 130.873 134.733 201.550 1.00 150.14 ? 168  ILE D O   1 
ATOM   10281 C  CB  . ILE D 2 191 ? 128.238 134.162 200.008 1.00 150.19 ? 168  ILE D CB  1 
ATOM   10282 C  CG1 . ILE D 2 191 ? 129.022 132.866 199.804 1.00 149.67 ? 168  ILE D CG1 1 
ATOM   10283 C  CG2 . ILE D 2 191 ? 128.593 135.186 198.941 1.00 149.34 ? 168  ILE D CG2 1 
ATOM   10284 C  CD1 . ILE D 2 191 ? 128.237 131.621 200.137 1.00 149.96 ? 168  ILE D CD1 1 
ATOM   10285 N  N   . ASN D 2 192 ? 129.903 136.753 201.456 1.00 150.83 ? 169  ASN D N   1 
ATOM   10286 C  CA  . ASN D 2 192 ? 131.184 137.460 201.479 1.00 150.18 ? 169  ASN D CA  1 
ATOM   10287 C  C   . ASN D 2 192 ? 131.647 137.737 202.907 1.00 150.52 ? 169  ASN D C   1 
ATOM   10288 O  O   . ASN D 2 192 ? 131.968 138.867 203.273 1.00 150.30 ? 169  ASN D O   1 
ATOM   10289 C  CB  . ASN D 2 192 ? 131.078 138.750 200.675 1.00 149.90 ? 169  ASN D CB  1 
ATOM   10290 C  CG  . ASN D 2 192 ? 129.946 139.640 201.146 1.00 150.19 ? 169  ASN D CG  1 
ATOM   10291 O  OD1 . ASN D 2 192 ? 128.835 139.172 201.393 1.00 150.18 ? 169  ASN D OD1 1 
ATOM   10292 N  ND2 . ASN D 2 192 ? 130.223 140.932 201.274 1.00 149.46 ? 169  ASN D ND2 1 
ATOM   10293 N  N   . ASP D 2 193 ? 131.690 136.690 203.728 1.00 152.33 ? 170  ASP D N   1 
ATOM   10294 C  CA  . ASP D 2 193 ? 132.118 136.799 205.116 1.00 152.29 ? 170  ASP D CA  1 
ATOM   10295 C  C   . ASP D 2 193 ? 133.539 136.292 205.335 1.00 152.09 ? 170  ASP D C   1 
ATOM   10296 O  O   . ASP D 2 193 ? 133.964 136.152 206.486 1.00 151.37 ? 170  ASP D O   1 
ATOM   10297 C  CB  . ASP D 2 193 ? 131.146 136.050 206.029 1.00 152.05 ? 170  ASP D CB  1 
ATOM   10298 C  CG  . ASP D 2 193 ? 130.955 134.605 205.618 1.00 152.53 ? 170  ASP D CG  1 
ATOM   10299 O  OD1 . ASP D 2 193 ? 131.133 134.297 204.421 1.00 152.57 ? 170  ASP D OD1 1 
ATOM   10300 O  OD2 . ASP D 2 193 ? 130.624 133.776 206.493 1.00 152.05 ? 170  ASP D OD2 1 
ATOM   10301 N  N   . GLY D 2 194 ? 134.278 136.013 204.263 1.00 145.47 ? 171  GLY D N   1 
ATOM   10302 C  CA  . GLY D 2 194 ? 135.657 135.587 204.371 1.00 144.53 ? 171  GLY D CA  1 
ATOM   10303 C  C   . GLY D 2 194 ? 135.870 134.107 204.595 1.00 144.59 ? 171  GLY D C   1 
ATOM   10304 O  O   . GLY D 2 194 ? 137.026 133.670 204.658 1.00 143.74 ? 171  GLY D O   1 
ATOM   10305 N  N   . LYS D 2 195 ? 134.806 133.320 204.715 1.00 151.50 ? 172  LYS D N   1 
ATOM   10306 C  CA  . LYS D 2 195 ? 134.918 131.888 204.943 1.00 151.62 ? 172  LYS D CA  1 
ATOM   10307 C  C   . LYS D 2 195 ? 134.793 131.123 203.631 1.00 152.21 ? 172  LYS D C   1 
ATOM   10308 O  O   . LYS D 2 195 ? 134.186 131.597 202.667 1.00 151.05 ? 172  LYS D O   1 
ATOM   10309 C  CB  . LYS D 2 195 ? 133.854 131.407 205.931 1.00 150.53 ? 172  LYS D CB  1 
ATOM   10310 C  CG  . LYS D 2 195 ? 134.218 131.634 207.388 1.00 150.31 ? 172  LYS D CG  1 
ATOM   10311 C  CD  . LYS D 2 195 ? 135.554 130.990 207.724 1.00 150.62 ? 172  LYS D CD  1 
ATOM   10312 C  CE  . LYS D 2 195 ? 135.952 131.255 209.166 1.00 150.34 ? 172  LYS D CE  1 
ATOM   10313 N  NZ  . LYS D 2 195 ? 136.097 132.710 209.443 1.00 150.81 ? 172  LYS D NZ  1 
ATOM   10314 N  N   . TYR D 2 196 ? 135.381 129.930 203.606 1.00 155.42 ? 173  TYR D N   1 
ATOM   10315 C  CA  . TYR D 2 196 ? 135.324 129.086 202.421 1.00 155.14 ? 173  TYR D CA  1 
ATOM   10316 C  C   . TYR D 2 196 ? 133.946 128.450 202.293 1.00 154.84 ? 173  TYR D C   1 
ATOM   10317 O  O   . TYR D 2 196 ? 133.436 127.847 203.243 1.00 154.63 ? 173  TYR D O   1 
ATOM   10318 C  CB  . TYR D 2 196 ? 136.409 128.010 202.489 1.00 154.94 ? 173  TYR D CB  1 
ATOM   10319 C  CG  . TYR D 2 196 ? 136.390 127.010 201.350 1.00 154.55 ? 173  TYR D CG  1 
ATOM   10320 C  CD1 . TYR D 2 196 ? 135.610 125.861 201.418 1.00 154.08 ? 173  TYR D CD1 1 
ATOM   10321 C  CD2 . TYR D 2 196 ? 137.159 127.211 200.212 1.00 153.93 ? 173  TYR D CD2 1 
ATOM   10322 C  CE1 . TYR D 2 196 ? 135.591 124.946 200.383 1.00 153.52 ? 173  TYR D CE1 1 
ATOM   10323 C  CE2 . TYR D 2 196 ? 137.147 126.300 199.171 1.00 153.99 ? 173  TYR D CE2 1 
ATOM   10324 C  CZ  . TYR D 2 196 ? 136.362 125.170 199.263 1.00 154.12 ? 173  TYR D CZ  1 
ATOM   10325 O  OH  . TYR D 2 196 ? 136.345 124.259 198.232 1.00 154.15 ? 173  TYR D OH  1 
ATOM   10326 N  N   . HIS D 2 197 ? 133.344 128.585 201.115 1.00 153.54 ? 174  HIS D N   1 
ATOM   10327 C  CA  . HIS D 2 197 ? 132.057 127.974 200.819 1.00 153.90 ? 174  HIS D CA  1 
ATOM   10328 C  C   . HIS D 2 197 ? 132.115 127.354 199.433 1.00 154.02 ? 174  HIS D C   1 
ATOM   10329 O  O   . HIS D 2 197 ? 132.752 127.901 198.529 1.00 153.11 ? 174  HIS D O   1 
ATOM   10330 C  CB  . HIS D 2 197 ? 130.914 128.996 200.889 1.00 154.09 ? 174  HIS D CB  1 
ATOM   10331 C  CG  . HIS D 2 197 ? 130.951 129.863 202.109 1.00 154.37 ? 174  HIS D CG  1 
ATOM   10332 N  ND1 . HIS D 2 197 ? 130.756 129.368 203.380 1.00 153.99 ? 174  HIS D ND1 1 
ATOM   10333 C  CD2 . HIS D 2 197 ? 131.156 131.194 202.251 1.00 153.76 ? 174  HIS D CD2 1 
ATOM   10334 C  CE1 . HIS D 2 197 ? 130.841 130.356 204.253 1.00 153.67 ? 174  HIS D CE1 1 
ATOM   10335 N  NE2 . HIS D 2 197 ? 131.084 131.474 203.593 1.00 153.57 ? 174  HIS D NE2 1 
ATOM   10336 N  N   . VAL D 2 198 ? 131.455 126.213 199.269 1.00 151.85 ? 175  VAL D N   1 
ATOM   10337 C  CA  . VAL D 2 198 ? 131.394 125.530 197.984 1.00 150.90 ? 175  VAL D CA  1 
ATOM   10338 C  C   . VAL D 2 198 ? 130.012 125.749 197.386 1.00 150.31 ? 175  VAL D C   1 
ATOM   10339 O  O   . VAL D 2 198 ? 129.017 125.907 198.104 1.00 149.22 ? 175  VAL D O   1 
ATOM   10340 C  CB  . VAL D 2 198 ? 131.721 124.025 198.109 1.00 150.05 ? 175  VAL D CB  1 
ATOM   10341 C  CG1 . VAL D 2 198 ? 130.498 123.232 198.551 1.00 150.47 ? 175  VAL D CG1 1 
ATOM   10342 C  CG2 . VAL D 2 198 ? 132.267 123.489 196.793 1.00 149.51 ? 175  VAL D CG2 1 
ATOM   10343 N  N   . VAL D 2 199 ? 129.959 125.790 196.058 1.00 149.70 ? 176  VAL D N   1 
ATOM   10344 C  CA  . VAL D 2 199 ? 128.716 125.977 195.324 1.00 149.99 ? 176  VAL D CA  1 
ATOM   10345 C  C   . VAL D 2 199 ? 128.643 124.940 194.211 1.00 150.57 ? 176  VAL D C   1 
ATOM   10346 O  O   . VAL D 2 199 ? 129.642 124.660 193.534 1.00 149.63 ? 176  VAL D O   1 
ATOM   10347 C  CB  . VAL D 2 199 ? 128.587 127.413 194.766 1.00 149.68 ? 176  VAL D CB  1 
ATOM   10348 C  CG1 . VAL D 2 199 ? 129.691 127.719 193.767 1.00 149.05 ? 176  VAL D CG1 1 
ATOM   10349 C  CG2 . VAL D 2 199 ? 127.217 127.622 194.138 1.00 149.35 ? 176  VAL D CG2 1 
ATOM   10350 N  N   . ARG D 2 200 ? 127.460 124.349 194.051 1.00 154.56 ? 177  ARG D N   1 
ATOM   10351 C  CA  . ARG D 2 200 ? 127.178 123.361 193.023 1.00 153.43 ? 177  ARG D CA  1 
ATOM   10352 C  C   . ARG D 2 200 ? 125.922 123.773 192.270 1.00 153.25 ? 177  ARG D C   1 
ATOM   10353 O  O   . ARG D 2 200 ? 125.012 124.390 192.834 1.00 152.90 ? 177  ARG D O   1 
ATOM   10354 C  CB  . ARG D 2 200 ? 126.994 121.960 193.622 1.00 153.08 ? 177  ARG D CB  1 
ATOM   10355 C  CG  . ARG D 2 200 ? 128.020 121.595 194.682 1.00 153.60 ? 177  ARG D CG  1 
ATOM   10356 C  CD  . ARG D 2 200 ? 127.869 120.148 195.118 1.00 154.03 ? 177  ARG D CD  1 
ATOM   10357 N  NE  . ARG D 2 200 ? 128.714 119.834 196.263 1.00 154.27 ? 177  ARG D NE  1 
ATOM   10358 C  CZ  . ARG D 2 200 ? 129.999 119.516 196.182 1.00 154.32 ? 177  ARG D CZ  1 
ATOM   10359 N  NH1 . ARG D 2 200 ? 130.624 119.456 195.017 1.00 154.15 ? 177  ARG D NH1 1 
ATOM   10360 N  NH2 . ARG D 2 200 ? 130.674 119.252 197.297 1.00 154.34 ? 177  ARG D NH2 1 
ATOM   10361 N  N   . PHE D 2 201 ? 125.878 123.419 190.989 1.00 142.27 ? 178  PHE D N   1 
ATOM   10362 C  CA  . PHE D 2 201 ? 124.808 123.864 190.104 1.00 142.01 ? 178  PHE D CA  1 
ATOM   10363 C  C   . PHE D 2 201 ? 124.570 122.784 189.061 1.00 141.30 ? 178  PHE D C   1 
ATOM   10364 O  O   . PHE D 2 201 ? 125.497 122.402 188.339 1.00 139.63 ? 178  PHE D O   1 
ATOM   10365 C  CB  . PHE D 2 201 ? 125.179 125.193 189.435 1.00 141.24 ? 178  PHE D CB  1 
ATOM   10366 C  CG  . PHE D 2 201 ? 124.335 125.538 188.237 1.00 141.12 ? 178  PHE D CG  1 
ATOM   10367 C  CD1 . PHE D 2 201 ? 122.959 125.369 188.258 1.00 141.35 ? 178  PHE D CD1 1 
ATOM   10368 C  CD2 . PHE D 2 201 ? 124.916 126.094 187.110 1.00 140.73 ? 178  PHE D CD2 1 
ATOM   10369 C  CE1 . PHE D 2 201 ? 122.189 125.702 187.161 1.00 141.01 ? 178  PHE D CE1 1 
ATOM   10370 C  CE2 . PHE D 2 201 ? 124.151 126.426 186.012 1.00 140.55 ? 178  PHE D CE2 1 
ATOM   10371 C  CZ  . PHE D 2 201 ? 122.786 126.234 186.038 1.00 140.50 ? 178  PHE D CZ  1 
ATOM   10372 N  N   . THR D 2 202 ? 123.334 122.300 188.987 1.00 139.20 ? 179  THR D N   1 
ATOM   10373 C  CA  . THR D 2 202 ? 122.904 121.361 187.963 1.00 138.82 ? 179  THR D CA  1 
ATOM   10374 C  C   . THR D 2 202 ? 121.862 122.028 187.077 1.00 138.49 ? 179  THR D C   1 
ATOM   10375 O  O   . THR D 2 202 ? 121.000 122.767 187.564 1.00 138.50 ? 179  THR D O   1 
ATOM   10376 C  CB  . THR D 2 202 ? 122.322 120.086 188.580 1.00 140.21 ? 179  THR D CB  1 
ATOM   10377 O  OG1 . THR D 2 202 ? 120.936 120.290 188.879 1.00 140.01 ? 179  THR D OG1 1 
ATOM   10378 C  CG2 . THR D 2 202 ? 123.065 119.722 189.857 1.00 139.53 ? 179  THR D CG2 1 
ATOM   10379 N  N   . ARG D 2 203 ? 121.944 121.770 185.775 1.00 120.42 ? 180  ARG D N   1 
ATOM   10380 C  CA  . ARG D 2 203 ? 121.063 122.400 184.805 1.00 119.38 ? 180  ARG D CA  1 
ATOM   10381 C  C   . ARG D 2 203 ? 120.437 121.340 183.912 1.00 119.10 ? 180  ARG D C   1 
ATOM   10382 O  O   . ARG D 2 203 ? 121.110 120.396 183.489 1.00 119.08 ? 180  ARG D O   1 
ATOM   10383 C  CB  . ARG D 2 203 ? 121.822 123.421 183.953 1.00 118.71 ? 180  ARG D CB  1 
ATOM   10384 C  CG  . ARG D 2 203 ? 120.945 124.497 183.343 1.00 119.98 ? 180  ARG D CG  1 
ATOM   10385 C  CD  . ARG D 2 203 ? 120.639 124.188 181.892 1.00 118.16 ? 180  ARG D CD  1 
ATOM   10386 N  NE  . ARG D 2 203 ? 121.830 124.261 181.058 1.00 117.96 ? 180  ARG D NE  1 
ATOM   10387 C  CZ  . ARG D 2 203 ? 121.917 123.758 179.836 1.00 117.06 ? 180  ARG D CZ  1 
ATOM   10388 N  NH1 . ARG D 2 203 ? 120.889 123.152 179.264 1.00 115.97 ? 180  ARG D NH1 1 
ATOM   10389 N  NH2 . ARG D 2 203 ? 123.063 123.862 179.171 1.00 117.61 ? 180  ARG D NH2 1 
ATOM   10390 N  N   . SER D 2 204 ? 119.142 121.498 183.634 1.00 126.48 ? 181  SER D N   1 
ATOM   10391 C  CA  . SER D 2 204 ? 118.408 120.625 182.713 1.00 127.35 ? 181  SER D CA  1 
ATOM   10392 C  C   . SER D 2 204 ? 117.426 121.518 181.957 1.00 128.00 ? 181  SER D C   1 
ATOM   10393 O  O   . SER D 2 204 ? 116.317 121.783 182.431 1.00 128.48 ? 181  SER D O   1 
ATOM   10394 C  CB  . SER D 2 204 ? 117.702 119.495 183.450 1.00 127.74 ? 181  SER D CB  1 
ATOM   10395 O  OG  . SER D 2 204 ? 118.617 118.482 183.827 1.00 127.78 ? 181  SER D OG  1 
ATOM   10396 N  N   . GLY D 2 205 ? 117.846 121.986 180.785 1.00 115.31 ? 182  GLY D N   1 
ATOM   10397 C  CA  . GLY D 2 205 ? 117.033 122.895 180.003 1.00 114.21 ? 182  GLY D CA  1 
ATOM   10398 C  C   . GLY D 2 205 ? 116.791 124.211 180.710 1.00 113.86 ? 182  GLY D C   1 
ATOM   10399 O  O   . GLY D 2 205 ? 117.711 125.017 180.873 1.00 112.88 ? 182  GLY D O   1 
ATOM   10400 N  N   . GLY D 2 206 ? 115.550 124.442 181.128 1.00 126.64 ? 183  GLY D N   1 
ATOM   10401 C  CA  . GLY D 2 206 ? 115.237 125.612 181.922 1.00 128.24 ? 183  GLY D CA  1 
ATOM   10402 C  C   . GLY D 2 206 ? 115.406 125.359 183.405 1.00 129.07 ? 183  GLY D C   1 
ATOM   10403 O  O   . GLY D 2 206 ? 115.704 126.280 184.171 1.00 128.43 ? 183  GLY D O   1 
ATOM   10404 N  N   . ASN D 2 207 ? 115.226 124.106 183.818 1.00 138.76 ? 184  ASN D N   1 
ATOM   10405 C  CA  . ASN D 2 207 ? 115.321 123.758 185.229 1.00 138.63 ? 184  ASN D CA  1 
ATOM   10406 C  C   . ASN D 2 207 ? 116.746 123.948 185.735 1.00 138.55 ? 184  ASN D C   1 
ATOM   10407 O  O   . ASN D 2 207 ? 117.714 123.555 185.080 1.00 137.43 ? 184  ASN D O   1 
ATOM   10408 C  CB  . ASN D 2 207 ? 114.869 122.314 185.445 1.00 137.85 ? 184  ASN D CB  1 
ATOM   10409 C  CG  . ASN D 2 207 ? 113.506 122.035 184.840 1.00 138.97 ? 184  ASN D CG  1 
ATOM   10410 O  OD1 . ASN D 2 207 ? 112.796 122.955 184.435 1.00 138.43 ? 184  ASN D OD1 1 
ATOM   10411 N  ND2 . ASN D 2 207 ? 113.134 120.762 184.775 1.00 140.65 ? 184  ASN D ND2 1 
ATOM   10412 N  N   . ALA D 2 208 ? 116.872 124.557 186.913 1.00 141.56 ? 185  ALA D N   1 
ATOM   10413 C  CA  . ALA D 2 208 ? 118.185 124.847 187.483 1.00 140.83 ? 185  ALA D CA  1 
ATOM   10414 C  C   . ALA D 2 208 ? 118.157 124.610 188.984 1.00 142.05 ? 185  ALA D C   1 
ATOM   10415 O  O   . ALA D 2 208 ? 117.336 125.200 189.690 1.00 142.84 ? 185  ALA D O   1 
ATOM   10416 C  CB  . ALA D 2 208 ? 118.610 126.287 187.177 1.00 140.15 ? 185  ALA D CB  1 
ATOM   10417 N  N   . THR D 2 209 ? 119.060 123.766 189.475 1.00 143.89 ? 186  THR D N   1 
ATOM   10418 C  CA  . THR D 2 209 ? 119.198 123.506 190.902 1.00 144.14 ? 186  THR D CA  1 
ATOM   10419 C  C   . THR D 2 209 ? 120.537 124.050 191.379 1.00 144.15 ? 186  THR D C   1 
ATOM   10420 O  O   . THR D 2 209 ? 121.585 123.699 190.829 1.00 143.18 ? 186  THR D O   1 
ATOM   10421 C  CB  . THR D 2 209 ? 119.099 122.010 191.206 1.00 143.55 ? 186  THR D CB  1 
ATOM   10422 O  OG1 . THR D 2 209 ? 120.352 121.378 190.915 1.00 144.31 ? 186  THR D OG1 1 
ATOM   10423 C  CG2 . THR D 2 209 ? 118.006 121.366 190.366 1.00 142.44 ? 186  THR D CG2 1 
ATOM   10424 N  N   . LEU D 2 210 ? 120.499 124.903 192.401 1.00 151.13 ? 187  LEU D N   1 
ATOM   10425 C  CA  . LEU D 2 210 ? 121.692 125.547 192.933 1.00 151.11 ? 187  LEU D CA  1 
ATOM   10426 C  C   . LEU D 2 210 ? 121.796 125.265 194.424 1.00 150.95 ? 187  LEU D C   1 
ATOM   10427 O  O   . LEU D 2 210 ? 120.812 125.409 195.155 1.00 150.66 ? 187  LEU D O   1 
ATOM   10428 C  CB  . LEU D 2 210 ? 121.659 127.057 192.678 1.00 151.00 ? 187  LEU D CB  1 
ATOM   10429 C  CG  . LEU D 2 210 ? 122.906 127.845 193.081 1.00 151.19 ? 187  LEU D CG  1 
ATOM   10430 C  CD1 . LEU D 2 210 ? 124.066 127.510 192.160 1.00 150.45 ? 187  LEU D CD1 1 
ATOM   10431 C  CD2 . LEU D 2 210 ? 122.622 129.338 193.070 1.00 150.59 ? 187  LEU D CD2 1 
ATOM   10432 N  N   . GLN D 2 211 ? 122.983 124.863 194.871 1.00 152.61 ? 188  GLN D N   1 
ATOM   10433 C  CA  . GLN D 2 211 ? 123.231 124.602 196.279 1.00 152.62 ? 188  GLN D CA  1 
ATOM   10434 C  C   . GLN D 2 211 ? 124.552 125.233 196.691 1.00 153.43 ? 188  GLN D C   1 
ATOM   10435 O  O   . GLN D 2 211 ? 125.482 125.343 195.889 1.00 153.41 ? 188  GLN D O   1 
ATOM   10436 C  CB  . GLN D 2 211 ? 123.257 123.095 196.580 1.00 152.41 ? 188  GLN D CB  1 
ATOM   10437 C  CG  . GLN D 2 211 ? 123.245 122.763 198.064 1.00 152.07 ? 188  GLN D CG  1 
ATOM   10438 C  CD  . GLN D 2 211 ? 123.619 121.322 198.347 1.00 153.08 ? 188  GLN D CD  1 
ATOM   10439 O  OE1 . GLN D 2 211 ? 124.031 120.588 197.450 1.00 153.78 ? 188  GLN D OE1 1 
ATOM   10440 N  NE2 . GLN D 2 211 ? 123.476 120.911 199.601 1.00 153.05 ? 188  GLN D NE2 1 
ATOM   10441 N  N   . VAL D 2 212 ? 124.620 125.660 197.948 1.00 157.32 ? 189  VAL D N   1 
ATOM   10442 C  CA  . VAL D 2 212 ? 125.843 126.200 198.530 1.00 157.15 ? 189  VAL D CA  1 
ATOM   10443 C  C   . VAL D 2 212 ? 125.985 125.645 199.941 1.00 157.66 ? 189  VAL D C   1 
ATOM   10444 O  O   . VAL D 2 212 ? 125.016 125.631 200.707 1.00 156.74 ? 189  VAL D O   1 
ATOM   10445 C  CB  . VAL D 2 212 ? 125.847 127.743 198.530 1.00 156.70 ? 189  VAL D CB  1 
ATOM   10446 C  CG1 . VAL D 2 212 ? 124.518 128.284 199.030 1.00 156.31 ? 189  VAL D CG1 1 
ATOM   10447 C  CG2 . VAL D 2 212 ? 126.999 128.278 199.365 1.00 156.17 ? 189  VAL D CG2 1 
ATOM   10448 N  N   . ASP D 2 213 ? 127.187 125.176 200.274 1.00 157.51 ? 190  ASP D N   1 
ATOM   10449 C  CA  . ASP D 2 213 ? 127.494 124.541 201.565 1.00 156.34 ? 190  ASP D CA  1 
ATOM   10450 C  C   . ASP D 2 213 ? 126.595 123.312 201.688 1.00 156.47 ? 190  ASP D C   1 
ATOM   10451 O  O   . ASP D 2 213 ? 126.468 122.555 200.712 1.00 156.44 ? 190  ASP D O   1 
ATOM   10452 C  CB  . ASP D 2 213 ? 127.368 125.568 202.686 1.00 156.01 ? 190  ASP D CB  1 
ATOM   10453 C  CG  . ASP D 2 213 ? 128.457 126.620 202.638 1.00 156.16 ? 190  ASP D CG  1 
ATOM   10454 O  OD1 . ASP D 2 213 ? 129.611 126.269 202.316 1.00 155.31 ? 190  ASP D OD1 1 
ATOM   10455 O  OD2 . ASP D 2 213 ? 128.159 127.799 202.923 1.00 156.37 ? 190  ASP D OD2 1 
ATOM   10456 N  N   . SER D 2 214 ? 125.964 123.070 202.836 1.00 160.73 ? 191  SER D N   1 
ATOM   10457 C  CA  . SER D 2 214 ? 125.028 121.966 203.003 1.00 160.79 ? 191  SER D CA  1 
ATOM   10458 C  C   . SER D 2 214 ? 123.587 122.446 203.110 1.00 161.22 ? 191  SER D C   1 
ATOM   10459 O  O   . SER D 2 214 ? 122.712 121.674 203.516 1.00 160.83 ? 191  SER D O   1 
ATOM   10460 C  CB  . SER D 2 214 ? 125.400 121.136 204.234 1.00 160.90 ? 191  SER D CB  1 
ATOM   10461 O  OG  . SER D 2 214 ? 125.309 121.910 205.418 1.00 161.00 ? 191  SER D OG  1 
ATOM   10462 N  N   . TRP D 2 215 ? 123.324 123.701 202.757 1.00 158.50 ? 192  TRP D N   1 
ATOM   10463 C  CA  . TRP D 2 215 ? 121.989 124.261 202.851 1.00 157.97 ? 192  TRP D CA  1 
ATOM   10464 C  C   . TRP D 2 215 ? 121.081 123.645 201.787 1.00 158.12 ? 192  TRP D C   1 
ATOM   10465 O  O   . TRP D 2 215 ? 121.562 123.110 200.785 1.00 158.38 ? 192  TRP D O   1 
ATOM   10466 C  CB  . TRP D 2 215 ? 122.050 125.781 202.701 1.00 157.03 ? 192  TRP D CB  1 
ATOM   10467 C  CG  . TRP D 2 215 ? 123.106 126.429 203.558 1.00 157.19 ? 192  TRP D CG  1 
ATOM   10468 C  CD1 . TRP D 2 215 ? 123.651 125.932 204.707 1.00 157.52 ? 192  TRP D CD1 1 
ATOM   10469 C  CD2 . TRP D 2 215 ? 123.745 127.690 203.326 1.00 158.02 ? 192  TRP D CD2 1 
ATOM   10470 N  NE1 . TRP D 2 215 ? 124.587 126.805 205.205 1.00 157.54 ? 192  TRP D NE1 1 
ATOM   10471 C  CE2 . TRP D 2 215 ? 124.664 127.892 204.375 1.00 158.22 ? 192  TRP D CE2 1 
ATOM   10472 C  CE3 . TRP D 2 215 ? 123.627 128.669 202.336 1.00 158.16 ? 192  TRP D CE3 1 
ATOM   10473 C  CZ2 . TRP D 2 215 ? 125.461 129.032 204.460 1.00 158.19 ? 192  TRP D CZ2 1 
ATOM   10474 C  CZ3 . TRP D 2 215 ? 124.421 129.798 202.421 1.00 157.68 ? 192  TRP D CZ3 1 
ATOM   10475 C  CH2 . TRP D 2 215 ? 125.324 129.971 203.476 1.00 157.58 ? 192  TRP D CH2 1 
ATOM   10476 N  N   . PRO D 2 216 ? 119.763 123.687 201.994 1.00 158.25 ? 193  PRO D N   1 
ATOM   10477 C  CA  . PRO D 2 216 ? 118.847 123.075 201.023 1.00 158.16 ? 193  PRO D CA  1 
ATOM   10478 C  C   . PRO D 2 216 ? 118.996 123.683 199.636 1.00 158.96 ? 193  PRO D C   1 
ATOM   10479 O  O   . PRO D 2 216 ? 119.253 124.879 199.481 1.00 158.43 ? 193  PRO D O   1 
ATOM   10480 C  CB  . PRO D 2 216 ? 117.459 123.355 201.616 1.00 157.88 ? 193  PRO D CB  1 
ATOM   10481 C  CG  . PRO D 2 216 ? 117.672 124.421 202.648 1.00 157.96 ? 193  PRO D CG  1 
ATOM   10482 C  CD  . PRO D 2 216 ? 119.045 124.186 203.178 1.00 158.10 ? 193  PRO D CD  1 
ATOM   10483 N  N   . VAL D 2 217 ? 118.831 122.837 198.624 1.00 156.09 ? 194  VAL D N   1 
ATOM   10484 C  CA  . VAL D 2 217 ? 119.044 123.232 197.236 1.00 155.26 ? 194  VAL D CA  1 
ATOM   10485 C  C   . VAL D 2 217 ? 117.854 124.050 196.755 1.00 154.96 ? 194  VAL D C   1 
ATOM   10486 O  O   . VAL D 2 217 ? 116.702 123.608 196.844 1.00 154.71 ? 194  VAL D O   1 
ATOM   10487 C  CB  . VAL D 2 217 ? 119.257 121.993 196.351 1.00 154.57 ? 194  VAL D CB  1 
ATOM   10488 C  CG1 . VAL D 2 217 ? 119.821 122.391 194.998 1.00 154.27 ? 194  VAL D CG1 1 
ATOM   10489 C  CG2 . VAL D 2 217 ? 120.169 120.994 197.046 1.00 154.31 ? 194  VAL D CG2 1 
ATOM   10490 N  N   . ILE D 2 218 ? 118.128 125.247 196.242 1.00 155.66 ? 195  ILE D N   1 
ATOM   10491 C  CA  . ILE D 2 218 ? 117.087 126.083 195.656 1.00 156.29 ? 195  ILE D CA  1 
ATOM   10492 C  C   . ILE D 2 218 ? 116.875 125.668 194.207 1.00 156.43 ? 195  ILE D C   1 
ATOM   10493 O  O   . ILE D 2 218 ? 117.831 125.383 193.473 1.00 156.25 ? 195  ILE D O   1 
ATOM   10494 C  CB  . ILE D 2 218 ? 117.450 127.575 195.780 1.00 156.88 ? 195  ILE D CB  1 
ATOM   10495 C  CG1 . ILE D 2 218 ? 116.402 128.449 195.084 1.00 155.94 ? 195  ILE D CG1 1 
ATOM   10496 C  CG2 . ILE D 2 218 ? 118.838 127.850 195.225 1.00 156.06 ? 195  ILE D CG2 1 
ATOM   10497 C  CD1 . ILE D 2 218 ? 116.088 129.732 195.823 1.00 154.99 ? 195  ILE D CD1 1 
ATOM   10498 N  N   . GLU D 2 219 ? 115.612 125.616 193.790 1.00 156.88 ? 196  GLU D N   1 
ATOM   10499 C  CA  . GLU D 2 219 ? 115.241 125.142 192.465 1.00 156.15 ? 196  GLU D CA  1 
ATOM   10500 C  C   . GLU D 2 219 ? 114.510 126.235 191.699 1.00 155.83 ? 196  GLU D C   1 
ATOM   10501 O  O   . GLU D 2 219 ? 113.701 126.975 192.267 1.00 155.45 ? 196  GLU D O   1 
ATOM   10502 C  CB  . GLU D 2 219 ? 114.359 123.893 192.556 1.00 156.19 ? 196  GLU D CB  1 
ATOM   10503 C  CG  . GLU D 2 219 ? 114.836 122.871 193.574 1.00 156.57 ? 196  GLU D CG  1 
ATOM   10504 C  CD  . GLU D 2 219 ? 113.737 121.918 194.000 1.00 156.63 ? 196  GLU D CD  1 
ATOM   10505 O  OE1 . GLU D 2 219 ? 112.689 121.874 193.320 1.00 156.56 ? 196  GLU D OE1 1 
ATOM   10506 O  OE2 . GLU D 2 219 ? 113.919 121.216 195.017 1.00 155.79 ? 196  GLU D OE2 1 
ATOM   10507 N  N   . ARG D 2 220 ? 114.804 126.326 190.404 1.00 149.23 ? 197  ARG D N   1 
ATOM   10508 C  CA  . ARG D 2 220 ? 114.136 127.238 189.487 1.00 148.55 ? 197  ARG D CA  1 
ATOM   10509 C  C   . ARG D 2 220 ? 113.533 126.410 188.363 1.00 147.31 ? 197  ARG D C   1 
ATOM   10510 O  O   . ARG D 2 220 ? 114.254 125.675 187.675 1.00 147.71 ? 197  ARG D O   1 
ATOM   10511 C  CB  . ARG D 2 220 ? 115.111 128.280 188.933 1.00 148.12 ? 197  ARG D CB  1 
ATOM   10512 C  CG  . ARG D 2 220 ? 114.524 129.171 187.852 1.00 148.18 ? 197  ARG D CG  1 
ATOM   10513 C  CD  . ARG D 2 220 ? 113.326 129.951 188.367 1.00 147.97 ? 197  ARG D CD  1 
ATOM   10514 N  NE  . ARG D 2 220 ? 112.896 130.977 187.425 1.00 147.97 ? 197  ARG D NE  1 
ATOM   10515 C  CZ  . ARG D 2 220 ? 113.377 132.213 187.393 1.00 147.91 ? 197  ARG D CZ  1 
ATOM   10516 N  NH1 . ARG D 2 220 ? 114.312 132.613 188.239 1.00 147.30 ? 197  ARG D NH1 1 
ATOM   10517 N  NH2 . ARG D 2 220 ? 112.908 133.068 186.490 1.00 147.58 ? 197  ARG D NH2 1 
ATOM   10518 N  N   . TYR D 2 221 ? 112.218 126.530 188.184 1.00 144.51 ? 198  TYR D N   1 
ATOM   10519 C  CA  . TYR D 2 221 ? 111.457 125.749 187.210 1.00 145.20 ? 198  TYR D CA  1 
ATOM   10520 C  C   . TYR D 2 221 ? 110.678 126.724 186.339 1.00 145.92 ? 198  TYR D C   1 
ATOM   10521 O  O   . TYR D 2 221 ? 109.509 127.026 186.618 1.00 145.82 ? 198  TYR D O   1 
ATOM   10522 C  CB  . TYR D 2 221 ? 110.520 124.760 187.903 1.00 145.19 ? 198  TYR D CB  1 
ATOM   10523 C  CG  . TYR D 2 221 ? 111.159 123.438 188.269 1.00 145.92 ? 198  TYR D CG  1 
ATOM   10524 C  CD1 . TYR D 2 221 ? 112.351 123.391 188.979 1.00 145.44 ? 198  TYR D CD1 1 
ATOM   10525 C  CD2 . TYR D 2 221 ? 110.562 122.235 187.914 1.00 145.55 ? 198  TYR D CD2 1 
ATOM   10526 C  CE1 . TYR D 2 221 ? 112.936 122.186 189.317 1.00 145.30 ? 198  TYR D CE1 1 
ATOM   10527 C  CE2 . TYR D 2 221 ? 111.138 121.025 188.250 1.00 145.27 ? 198  TYR D CE2 1 
ATOM   10528 C  CZ  . TYR D 2 221 ? 112.325 121.006 188.951 1.00 145.43 ? 198  TYR D CZ  1 
ATOM   10529 O  OH  . TYR D 2 221 ? 112.902 119.803 189.286 1.00 145.43 ? 198  TYR D OH  1 
ATOM   10530 N  N   . PRO D 2 222 ? 111.296 127.245 185.279 1.00 144.84 ? 199  PRO D N   1 
ATOM   10531 C  CA  . PRO D 2 222 ? 110.629 128.266 184.462 1.00 144.42 ? 199  PRO D CA  1 
ATOM   10532 C  C   . PRO D 2 222 ? 109.383 127.726 183.777 1.00 143.75 ? 199  PRO D C   1 
ATOM   10533 O  O   . PRO D 2 222 ? 109.302 126.551 183.412 1.00 143.05 ? 199  PRO D O   1 
ATOM   10534 C  CB  . PRO D 2 222 ? 111.701 128.658 183.436 1.00 142.90 ? 199  PRO D CB  1 
ATOM   10535 C  CG  . PRO D 2 222 ? 112.997 128.172 184.014 1.00 142.83 ? 199  PRO D CG  1 
ATOM   10536 C  CD  . PRO D 2 222 ? 112.652 126.947 184.795 1.00 143.79 ? 199  PRO D CD  1 
ATOM   10537 N  N   . ALA D 2 223 ? 108.403 128.608 183.608 1.00 137.27 ? 200  ALA D N   1 
ATOM   10538 C  CA  . ALA D 2 223 ? 107.164 128.275 182.924 1.00 136.52 ? 200  ALA D CA  1 
ATOM   10539 C  C   . ALA D 2 223 ? 107.266 128.621 181.444 1.00 136.61 ? 200  ALA D C   1 
ATOM   10540 O  O   . ALA D 2 223 ? 108.025 129.508 181.043 1.00 136.67 ? 200  ALA D O   1 
ATOM   10541 C  CB  . ALA D 2 223 ? 105.981 129.012 183.552 1.00 135.01 ? 200  ALA D CB  1 
ATOM   10542 N  N   . GLY D 2 224 ? 106.488 127.910 180.633 1.00 139.90 ? 201  GLY D N   1 
ATOM   10543 C  CA  . GLY D 2 224 ? 106.515 128.106 179.198 1.00 140.11 ? 201  GLY D CA  1 
ATOM   10544 C  C   . GLY D 2 224 ? 107.580 127.272 178.517 1.00 141.04 ? 201  GLY D C   1 
ATOM   10545 O  O   . GLY D 2 224 ? 108.291 126.469 179.128 1.00 140.24 ? 201  GLY D O   1 
ATOM   10546 N  N   . ARG D 2 225 ? 107.684 127.439 177.190 1.00 147.71 ? 232  ARG D N   1 
ATOM   10547 C  CA  . ARG D 2 225 ? 108.631 126.631 176.380 1.00 147.67 ? 232  ARG D CA  1 
ATOM   10548 C  C   . ARG D 2 225 ? 110.033 127.257 176.407 1.00 147.22 ? 232  ARG D C   1 
ATOM   10549 O  O   . ARG D 2 225 ? 110.196 128.401 175.999 1.00 146.39 ? 232  ARG D O   1 
ATOM   10550 C  CB  . ARG D 2 225 ? 108.037 126.334 175.002 1.00 147.07 ? 232  ARG D CB  1 
ATOM   10551 C  CG  . ARG D 2 225 ? 107.734 124.858 174.776 1.00 146.19 ? 232  ARG D CG  1 
ATOM   10552 C  CD  . ARG D 2 225 ? 108.217 124.293 173.439 1.00 146.87 ? 232  ARG D CD  1 
ATOM   10553 N  NE  . ARG D 2 225 ? 108.397 122.846 173.391 1.00 147.71 ? 232  ARG D NE  1 
ATOM   10554 C  CZ  . ARG D 2 225 ? 109.560 122.207 173.339 1.00 147.63 ? 232  ARG D CZ  1 
ATOM   10555 N  NH1 . ARG D 2 225 ? 110.696 122.873 173.336 1.00 147.42 ? 232  ARG D NH1 1 
ATOM   10556 N  NH2 . ARG D 2 225 ? 109.587 120.894 173.304 1.00 147.00 ? 232  ARG D NH2 1 
ATOM   10557 N  N   . GLN D 2 226 ? 111.005 126.478 176.871 1.00 133.37 ? 233  GLN D N   1 
ATOM   10558 C  CA  . GLN D 2 226 ? 112.390 126.890 177.042 1.00 132.60 ? 233  GLN D CA  1 
ATOM   10559 C  C   . GLN D 2 226 ? 113.292 125.985 176.219 1.00 131.79 ? 233  GLN D C   1 
ATOM   10560 O  O   . GLN D 2 226 ? 113.100 124.766 176.189 1.00 131.45 ? 233  GLN D O   1 
ATOM   10561 C  CB  . GLN D 2 226 ? 112.811 126.838 178.516 1.00 131.86 ? 233  GLN D CB  1 
ATOM   10562 C  CG  . GLN D 2 226 ? 111.953 127.679 179.443 1.00 132.55 ? 233  GLN D CG  1 
ATOM   10563 C  CD  . GLN D 2 226 ? 112.492 129.085 179.613 1.00 133.97 ? 233  GLN D CD  1 
ATOM   10564 O  OE1 . GLN D 2 226 ? 113.684 129.332 179.430 1.00 133.56 ? 233  GLN D OE1 1 
ATOM   10565 N  NE2 . GLN D 2 226 ? 111.613 130.016 179.965 1.00 133.53 ? 233  GLN D NE2 1 
ATOM   10566 N  N   . LEU D 2 227 ? 114.274 126.584 175.551 1.00 105.75 ? 234  LEU D N   1 
ATOM   10567 C  CA  . LEU D 2 227 ? 115.272 125.793 174.850 1.00 103.22 ? 234  LEU D CA  1 
ATOM   10568 C  C   . LEU D 2 227 ? 116.189 125.103 175.851 1.00 101.60 ? 234  LEU D C   1 
ATOM   10569 O  O   . LEU D 2 227 ? 116.418 125.593 176.961 1.00 103.26 ? 234  LEU D O   1 
ATOM   10570 C  CB  . LEU D 2 227 ? 116.087 126.669 173.900 1.00 102.26 ? 234  LEU D CB  1 
ATOM   10571 C  CG  . LEU D 2 227 ? 115.270 127.440 172.864 1.00 100.65 ? 234  LEU D CG  1 
ATOM   10572 C  CD1 . LEU D 2 227 ? 116.177 128.266 171.971 1.00 100.40 ? 234  LEU D CD1 1 
ATOM   10573 C  CD2 . LEU D 2 227 ? 114.422 126.485 172.041 1.00 97.89  ? 234  LEU D CD2 1 
ATOM   10574 N  N   . THR D 2 228 ? 116.726 123.954 175.446 1.00 90.91  ? 235  THR D N   1 
ATOM   10575 C  CA  . THR D 2 228 ? 117.476 123.102 176.355 1.00 92.13  ? 235  THR D CA  1 
ATOM   10576 C  C   . THR D 2 228 ? 118.924 122.873 175.946 1.00 93.62  ? 235  THR D C   1 
ATOM   10577 O  O   . THR D 2 228 ? 119.631 122.132 176.640 1.00 94.89  ? 235  THR D O   1 
ATOM   10578 C  CB  . THR D 2 228 ? 116.783 121.740 176.503 1.00 91.12  ? 235  THR D CB  1 
ATOM   10579 O  OG1 . THR D 2 228 ? 116.754 121.074 175.235 1.00 90.03  ? 235  THR D OG1 1 
ATOM   10580 C  CG2 . THR D 2 228 ? 115.356 121.913 177.001 1.00 91.74  ? 235  THR D CG2 1 
ATOM   10581 N  N   . ILE D 2 229 ? 119.396 123.474 174.858 1.00 83.68  ? 236  ILE D N   1 
ATOM   10582 C  CA  . ILE D 2 229 ? 120.715 123.165 174.312 1.00 81.22  ? 236  ILE D CA  1 
ATOM   10583 C  C   . ILE D 2 229 ? 121.637 124.366 174.444 1.00 82.37  ? 236  ILE D C   1 
ATOM   10584 O  O   . ILE D 2 229 ? 121.351 125.447 173.916 1.00 84.61  ? 236  ILE D O   1 
ATOM   10585 C  CB  . ILE D 2 229 ? 120.626 122.687 172.853 1.00 78.09  ? 236  ILE D CB  1 
ATOM   10586 C  CG1 . ILE D 2 229 ? 119.401 121.797 172.669 1.00 77.22  ? 236  ILE D CG1 1 
ATOM   10587 C  CG2 . ILE D 2 229 ? 121.893 121.961 172.456 1.00 77.77  ? 236  ILE D CG2 1 
ATOM   10588 C  CD1 . ILE D 2 229 ? 119.525 120.453 173.374 1.00 81.06  ? 236  ILE D CD1 1 
ATOM   10589 N  N   . PHE D 2 230 ? 122.751 124.159 175.139 1.00 92.53  ? 237  PHE D N   1 
ATOM   10590 C  CA  . PHE D 2 230 ? 123.843 125.115 175.205 1.00 93.00  ? 237  PHE D CA  1 
ATOM   10591 C  C   . PHE D 2 230 ? 124.786 124.812 174.048 1.00 93.00  ? 237  PHE D C   1 
ATOM   10592 O  O   . PHE D 2 230 ? 125.515 123.818 174.077 1.00 96.30  ? 237  PHE D O   1 
ATOM   10593 C  CB  . PHE D 2 230 ? 124.536 125.000 176.554 1.00 94.32  ? 237  PHE D CB  1 
ATOM   10594 C  CG  . PHE D 2 230 ? 125.240 126.245 176.976 1.00 94.11  ? 237  PHE D CG  1 
ATOM   10595 C  CD1 . PHE D 2 230 ? 125.843 127.075 176.047 1.00 94.71  ? 237  PHE D CD1 1 
ATOM   10596 C  CD2 . PHE D 2 230 ? 125.301 126.585 178.308 1.00 95.92  ? 237  PHE D CD2 1 
ATOM   10597 C  CE1 . PHE D 2 230 ? 126.497 128.206 176.454 1.00 95.09  ? 237  PHE D CE1 1 
ATOM   10598 C  CE2 . PHE D 2 230 ? 125.944 127.713 178.716 1.00 97.25  ? 237  PHE D CE2 1 
ATOM   10599 C  CZ  . PHE D 2 230 ? 126.548 128.529 177.791 1.00 96.88  ? 237  PHE D CZ  1 
ATOM   10600 N  N   . ASN D 2 231 ? 124.781 125.681 173.039 1.00 86.92  ? 238  ASN D N   1 
ATOM   10601 C  CA  . ASN D 2 231 ? 125.332 125.367 171.723 1.00 88.17  ? 238  ASN D CA  1 
ATOM   10602 C  C   . ASN D 2 231 ? 126.804 125.759 171.649 1.00 88.06  ? 238  ASN D C   1 
ATOM   10603 O  O   . ASN D 2 231 ? 127.148 126.936 171.794 1.00 88.56  ? 238  ASN D O   1 
ATOM   10604 C  CB  . ASN D 2 231 ? 124.546 126.094 170.634 1.00 88.38  ? 238  ASN D CB  1 
ATOM   10605 C  CG  . ASN D 2 231 ? 123.120 125.586 170.488 1.00 88.35  ? 238  ASN D CG  1 
ATOM   10606 O  OD1 . ASN D 2 231 ? 122.187 126.156 171.056 1.00 88.80  ? 238  ASN D OD1 1 
ATOM   10607 N  ND2 . ASN D 2 231 ? 122.942 124.535 169.697 1.00 85.68  ? 238  ASN D ND2 1 
ATOM   10608 N  N   . SER D 2 232 ? 127.668 124.772 171.408 1.00 98.70  ? 239  SER D N   1 
ATOM   10609 C  CA  . SER D 2 232 ? 129.035 124.983 170.929 1.00 97.94  ? 239  SER D CA  1 
ATOM   10610 C  C   . SER D 2 232 ? 129.841 125.854 171.901 1.00 101.14 ? 239  SER D C   1 
ATOM   10611 O  O   . SER D 2 232 ? 130.192 127.003 171.622 1.00 104.72 ? 239  SER D O   1 
ATOM   10612 C  CB  . SER D 2 232 ? 129.015 125.580 169.515 1.00 97.85  ? 239  SER D CB  1 
ATOM   10613 O  OG  . SER D 2 232 ? 130.316 125.633 168.969 1.00 99.54  ? 239  SER D OG  1 
ATOM   10614 N  N   . GLN D 2 233 ? 130.101 125.267 173.068 1.00 106.77 ? 240  GLN D N   1 
ATOM   10615 C  CA  . GLN D 2 233 ? 130.963 125.879 174.072 1.00 107.32 ? 240  GLN D CA  1 
ATOM   10616 C  C   . GLN D 2 233 ? 132.292 126.284 173.442 1.00 111.04 ? 240  GLN D C   1 
ATOM   10617 O  O   . GLN D 2 233 ? 132.848 125.546 172.627 1.00 110.68 ? 240  GLN D O   1 
ATOM   10618 C  CB  . GLN D 2 233 ? 131.227 124.867 175.184 1.00 107.74 ? 240  GLN D CB  1 
ATOM   10619 C  CG  . GLN D 2 233 ? 129.994 124.103 175.685 1.00 107.57 ? 240  GLN D CG  1 
ATOM   10620 C  CD  . GLN D 2 233 ? 129.030 124.959 176.473 1.00 107.61 ? 240  GLN D CD  1 
ATOM   10621 O  OE1 . GLN D 2 233 ? 129.428 125.917 177.134 1.00 109.33 ? 240  GLN D OE1 1 
ATOM   10622 N  NE2 . GLN D 2 233 ? 127.765 124.596 176.425 1.00 107.58 ? 240  GLN D NE2 1 
ATOM   10623 N  N   . ALA D 2 234 ? 132.810 127.463 173.801 1.00 124.58 ? 241  ALA D N   1 
ATOM   10624 C  CA  . ALA D 2 234 ? 134.062 127.944 173.223 1.00 123.37 ? 241  ALA D CA  1 
ATOM   10625 C  C   . ALA D 2 234 ? 135.171 128.120 174.253 1.00 123.84 ? 241  ALA D C   1 
ATOM   10626 O  O   . ALA D 2 234 ? 136.230 127.502 174.122 1.00 122.80 ? 241  ALA D O   1 
ATOM   10627 C  CB  . ALA D 2 234 ? 133.831 129.260 172.473 1.00 122.93 ? 241  ALA D CB  1 
ATOM   10628 N  N   . THR D 2 235 ? 134.971 128.957 175.272 1.00 135.18 ? 242  THR D N   1 
ATOM   10629 C  CA  . THR D 2 235 ? 135.996 129.217 176.276 1.00 136.30 ? 242  THR D CA  1 
ATOM   10630 C  C   . THR D 2 235 ? 135.385 129.222 177.668 1.00 136.31 ? 242  THR D C   1 
ATOM   10631 O  O   . THR D 2 235 ? 134.242 129.651 177.855 1.00 135.35 ? 242  THR D O   1 
ATOM   10632 C  CB  . THR D 2 235 ? 136.701 130.563 176.041 1.00 135.63 ? 242  THR D CB  1 
ATOM   10633 O  OG1 . THR D 2 235 ? 135.724 131.609 175.966 1.00 136.24 ? 242  THR D OG1 1 
ATOM   10634 C  CG2 . THR D 2 235 ? 137.516 130.534 174.759 1.00 134.64 ? 242  THR D CG2 1 
ATOM   10635 N  N   . ILE D 2 236 ? 136.155 128.746 178.641 1.00 139.82 ? 243  ILE D N   1 
ATOM   10636 C  CA  . ILE D 2 236 ? 135.842 128.919 180.054 1.00 139.03 ? 243  ILE D CA  1 
ATOM   10637 C  C   . ILE D 2 236 ? 136.716 130.046 180.583 1.00 139.85 ? 243  ILE D C   1 
ATOM   10638 O  O   . ILE D 2 236 ? 137.950 129.967 180.522 1.00 140.45 ? 243  ILE D O   1 
ATOM   10639 C  CB  . ILE D 2 236 ? 136.064 127.627 180.856 1.00 138.28 ? 243  ILE D CB  1 
ATOM   10640 C  CG1 . ILE D 2 236 ? 135.803 126.396 179.991 1.00 139.04 ? 243  ILE D CG1 1 
ATOM   10641 C  CG2 . ILE D 2 236 ? 135.167 127.608 182.086 1.00 137.89 ? 243  ILE D CG2 1 
ATOM   10642 C  CD1 . ILE D 2 236 ? 135.965 125.088 180.743 1.00 139.46 ? 243  ILE D CD1 1 
ATOM   10643 N  N   . ILE D 2 237 ? 136.076 131.092 181.099 1.00 138.14 ? 244  ILE D N   1 
ATOM   10644 C  CA  . ILE D 2 237 ? 136.751 132.275 181.618 1.00 138.20 ? 244  ILE D CA  1 
ATOM   10645 C  C   . ILE D 2 237 ? 136.629 132.260 183.134 1.00 138.77 ? 244  ILE D C   1 
ATOM   10646 O  O   . ILE D 2 237 ? 135.524 132.109 183.669 1.00 138.95 ? 244  ILE D O   1 
ATOM   10647 C  CB  . ILE D 2 237 ? 136.146 133.565 181.035 1.00 137.71 ? 244  ILE D CB  1 
ATOM   10648 C  CG1 . ILE D 2 237 ? 136.722 133.854 179.649 1.00 138.08 ? 244  ILE D CG1 1 
ATOM   10649 C  CG2 . ILE D 2 237 ? 136.387 134.746 181.968 1.00 136.47 ? 244  ILE D CG2 1 
ATOM   10650 C  CD1 . ILE D 2 237 ? 138.132 134.386 179.679 1.00 137.31 ? 244  ILE D CD1 1 
ATOM   10651 N  N   . ILE D 2 238 ? 137.756 132.406 183.825 1.00 140.48 ? 245  ILE D N   1 
ATOM   10652 C  CA  . ILE D 2 238 ? 137.769 132.525 185.278 1.00 139.91 ? 245  ILE D CA  1 
ATOM   10653 C  C   . ILE D 2 238 ? 138.438 133.846 185.628 1.00 140.29 ? 245  ILE D C   1 
ATOM   10654 O  O   . ILE D 2 238 ? 139.580 134.097 185.220 1.00 140.41 ? 245  ILE D O   1 
ATOM   10655 C  CB  . ILE D 2 238 ? 138.495 131.350 185.947 1.00 140.06 ? 245  ILE D CB  1 
ATOM   10656 C  CG1 . ILE D 2 238 ? 137.908 130.017 185.486 1.00 139.63 ? 245  ILE D CG1 1 
ATOM   10657 C  CG2 . ILE D 2 238 ? 138.419 131.471 187.458 1.00 139.44 ? 245  ILE D CG2 1 
ATOM   10658 C  CD1 . ILE D 2 238 ? 138.930 128.904 185.436 1.00 139.06 ? 245  ILE D CD1 1 
ATOM   10659 N  N   . GLY D 2 239 ? 137.730 134.682 186.384 1.00 134.16 ? 246  GLY D N   1 
ATOM   10660 C  CA  . GLY D 2 239 ? 138.239 135.974 186.800 1.00 134.15 ? 246  GLY D CA  1 
ATOM   10661 C  C   . GLY D 2 239 ? 137.268 137.107 186.537 1.00 133.64 ? 246  GLY D C   1 
ATOM   10662 O  O   . GLY D 2 239 ? 137.130 138.016 187.360 1.00 133.95 ? 246  GLY D O   1 
ATOM   10663 N  N   . GLY D 2 240 ? 136.582 137.056 185.397 1.00 137.90 ? 247  GLY D N   1 
ATOM   10664 C  CA  . GLY D 2 240 ? 135.575 138.052 185.074 1.00 138.06 ? 247  GLY D CA  1 
ATOM   10665 C  C   . GLY D 2 240 ? 136.084 139.471 184.978 1.00 138.21 ? 247  GLY D C   1 
ATOM   10666 O  O   . GLY D 2 240 ? 135.301 140.411 185.139 1.00 136.74 ? 247  GLY D O   1 
ATOM   10667 N  N   . LYS D 2 241 ? 137.381 139.659 184.722 1.00 143.81 ? 248  LYS D N   1 
ATOM   10668 C  CA  . LYS D 2 241 ? 137.932 141.010 184.670 1.00 143.64 ? 248  LYS D CA  1 
ATOM   10669 C  C   . LYS D 2 241 ? 137.471 141.753 183.421 1.00 143.39 ? 248  LYS D C   1 
ATOM   10670 O  O   . LYS D 2 241 ? 137.111 142.934 183.493 1.00 142.36 ? 248  LYS D O   1 
ATOM   10671 C  CB  . LYS D 2 241 ? 139.458 140.955 184.733 1.00 143.45 ? 248  LYS D CB  1 
ATOM   10672 C  CG  . LYS D 2 241 ? 140.139 142.306 184.590 1.00 143.59 ? 248  LYS D CG  1 
ATOM   10673 C  CD  . LYS D 2 241 ? 141.601 142.233 185.002 1.00 143.02 ? 248  LYS D CD  1 
ATOM   10674 C  CE  . LYS D 2 241 ? 142.389 143.413 184.459 1.00 142.86 ? 248  LYS D CE  1 
ATOM   10675 N  NZ  . LYS D 2 241 ? 141.798 144.715 184.873 1.00 142.17 ? 248  LYS D NZ  1 
ATOM   10676 N  N   . GLU D 2 242 ? 137.472 141.079 182.268 1.00 144.99 ? 249  GLU D N   1 
ATOM   10677 C  CA  . GLU D 2 242 ? 137.069 141.737 181.029 1.00 144.13 ? 249  GLU D CA  1 
ATOM   10678 C  C   . GLU D 2 242 ? 135.571 142.010 180.994 1.00 144.06 ? 249  GLU D C   1 
ATOM   10679 O  O   . GLU D 2 242 ? 135.128 142.930 180.296 1.00 143.84 ? 249  GLU D O   1 
ATOM   10680 C  CB  . GLU D 2 242 ? 137.480 140.890 179.825 1.00 143.64 ? 249  GLU D CB  1 
ATOM   10681 C  CG  . GLU D 2 242 ? 138.981 140.801 179.610 1.00 143.60 ? 249  GLU D CG  1 
ATOM   10682 C  CD  . GLU D 2 242 ? 139.362 139.740 178.597 1.00 143.46 ? 249  GLU D CD  1 
ATOM   10683 O  OE1 . GLU D 2 242 ? 138.508 138.886 178.280 1.00 143.29 ? 249  GLU D OE1 1 
ATOM   10684 O  OE2 . GLU D 2 242 ? 140.516 139.758 178.118 1.00 143.50 ? 249  GLU D OE2 1 
ATOM   10685 N  N   . GLN D 2 243 ? 134.779 141.224 181.727 1.00 142.24 ? 250  GLN D N   1 
ATOM   10686 C  CA  . GLN D 2 243 ? 133.334 141.433 181.737 1.00 142.37 ? 250  GLN D CA  1 
ATOM   10687 C  C   . GLN D 2 243 ? 132.971 142.776 182.360 1.00 142.55 ? 250  GLN D C   1 
ATOM   10688 O  O   . GLN D 2 243 ? 132.064 143.465 181.879 1.00 141.91 ? 250  GLN D O   1 
ATOM   10689 C  CB  . GLN D 2 243 ? 132.643 140.290 182.480 1.00 141.95 ? 250  GLN D CB  1 
ATOM   10690 C  CG  . GLN D 2 243 ? 132.327 139.084 181.610 1.00 142.27 ? 250  GLN D CG  1 
ATOM   10691 C  CD  . GLN D 2 243 ? 133.573 138.414 181.065 1.00 142.32 ? 250  GLN D CD  1 
ATOM   10692 O  OE1 . GLN D 2 243 ? 134.585 138.304 181.756 1.00 141.41 ? 250  GLN D OE1 1 
ATOM   10693 N  NE2 . GLN D 2 243 ? 133.505 137.964 179.818 1.00 142.50 ? 250  GLN D NE2 1 
ATOM   10694 N  N   . GLY D 2 244 ? 133.665 143.164 183.427 1.00 136.10 ? 251  GLY D N   1 
ATOM   10695 C  CA  . GLY D 2 244 ? 133.401 144.434 184.073 1.00 135.19 ? 251  GLY D CA  1 
ATOM   10696 C  C   . GLY D 2 244 ? 133.493 144.374 185.583 1.00 135.10 ? 251  GLY D C   1 
ATOM   10697 O  O   . GLY D 2 244 ? 133.572 145.412 186.248 1.00 134.27 ? 251  GLY D O   1 
ATOM   10698 N  N   . GLN D 2 245 ? 133.484 143.164 186.138 1.00 139.71 ? 252  GLN D N   1 
ATOM   10699 C  CA  . GLN D 2 245 ? 133.559 142.947 187.583 1.00 139.50 ? 252  GLN D CA  1 
ATOM   10700 C  C   . GLN D 2 245 ? 134.670 141.947 187.873 1.00 140.02 ? 252  GLN D C   1 
ATOM   10701 O  O   . GLN D 2 245 ? 134.418 140.741 188.004 1.00 139.30 ? 252  GLN D O   1 
ATOM   10702 C  CB  . GLN D 2 245 ? 132.220 142.465 188.143 1.00 137.80 ? 252  GLN D CB  1 
ATOM   10703 C  CG  . GLN D 2 245 ? 131.121 143.514 188.112 1.00 138.24 ? 252  GLN D CG  1 
ATOM   10704 C  CD  . GLN D 2 245 ? 129.901 143.104 188.914 1.00 138.77 ? 252  GLN D CD  1 
ATOM   10705 O  OE1 . GLN D 2 245 ? 129.957 142.175 189.720 1.00 137.99 ? 252  GLN D OE1 1 
ATOM   10706 N  NE2 . GLN D 2 245 ? 128.790 143.797 188.695 1.00 139.33 ? 252  GLN D NE2 1 
ATOM   10707 N  N   . PRO D 2 246 ? 135.916 142.411 187.965 1.00 142.57 ? 253  PRO D N   1 
ATOM   10708 C  CA  . PRO D 2 246 ? 137.011 141.505 188.328 1.00 141.43 ? 253  PRO D CA  1 
ATOM   10709 C  C   . PRO D 2 246 ? 136.817 140.939 189.727 1.00 141.18 ? 253  PRO D C   1 
ATOM   10710 O  O   . PRO D 2 246 ? 136.247 141.583 190.610 1.00 140.52 ? 253  PRO D O   1 
ATOM   10711 C  CB  . PRO D 2 246 ? 138.256 142.398 188.252 1.00 140.49 ? 253  PRO D CB  1 
ATOM   10712 C  CG  . PRO D 2 246 ? 137.850 143.562 187.402 1.00 140.46 ? 253  PRO D CG  1 
ATOM   10713 C  CD  . PRO D 2 246 ? 136.393 143.772 187.672 1.00 140.93 ? 253  PRO D CD  1 
ATOM   10714 N  N   . PHE D 2 247 ? 137.300 139.716 189.920 1.00 139.73 ? 254  PHE D N   1 
ATOM   10715 C  CA  . PHE D 2 247 ? 137.137 138.989 191.171 1.00 139.42 ? 254  PHE D CA  1 
ATOM   10716 C  C   . PHE D 2 247 ? 138.471 138.921 191.902 1.00 140.34 ? 254  PHE D C   1 
ATOM   10717 O  O   . PHE D 2 247 ? 139.502 138.618 191.293 1.00 139.08 ? 254  PHE D O   1 
ATOM   10718 C  CB  . PHE D 2 247 ? 136.601 137.578 190.917 1.00 138.32 ? 254  PHE D CB  1 
ATOM   10719 C  CG  . PHE D 2 247 ? 136.730 136.658 192.097 1.00 139.04 ? 254  PHE D CG  1 
ATOM   10720 C  CD1 . PHE D 2 247 ? 135.805 136.698 193.126 1.00 139.33 ? 254  PHE D CD1 1 
ATOM   10721 C  CD2 . PHE D 2 247 ? 137.774 135.750 192.178 1.00 138.29 ? 254  PHE D CD2 1 
ATOM   10722 C  CE1 . PHE D 2 247 ? 135.918 135.854 194.212 1.00 139.54 ? 254  PHE D CE1 1 
ATOM   10723 C  CE2 . PHE D 2 247 ? 137.894 134.907 193.264 1.00 138.22 ? 254  PHE D CE2 1 
ATOM   10724 C  CZ  . PHE D 2 247 ? 136.964 134.957 194.281 1.00 139.14 ? 254  PHE D CZ  1 
ATOM   10725 N  N   . GLN D 2 248 ? 138.445 139.202 193.202 1.00 141.55 ? 255  GLN D N   1 
ATOM   10726 C  CA  . GLN D 2 248 ? 139.618 139.106 194.060 1.00 139.88 ? 255  GLN D CA  1 
ATOM   10727 C  C   . GLN D 2 248 ? 139.301 138.188 195.231 1.00 140.11 ? 255  GLN D C   1 
ATOM   10728 O  O   . GLN D 2 248 ? 138.304 138.392 195.932 1.00 140.03 ? 255  GLN D O   1 
ATOM   10729 C  CB  . GLN D 2 248 ? 140.048 140.487 194.562 1.00 139.82 ? 255  GLN D CB  1 
ATOM   10730 C  CG  . GLN D 2 248 ? 141.318 140.479 195.395 1.00 140.18 ? 255  GLN D CG  1 
ATOM   10731 C  CD  . GLN D 2 248 ? 141.703 141.862 195.881 1.00 140.27 ? 255  GLN D CD  1 
ATOM   10732 O  OE1 . GLN D 2 248 ? 140.919 142.806 195.789 1.00 140.07 ? 255  GLN D OE1 1 
ATOM   10733 N  NE2 . GLN D 2 248 ? 142.918 141.989 196.402 1.00 139.84 ? 255  GLN D NE2 1 
ATOM   10734 N  N   . GLY D 2 249 ? 140.145 137.187 195.439 1.00 142.58 ? 256  GLY D N   1 
ATOM   10735 C  CA  . GLY D 2 249 ? 139.918 136.208 196.492 1.00 143.07 ? 256  GLY D CA  1 
ATOM   10736 C  C   . GLY D 2 249 ? 140.657 134.915 196.184 1.00 143.83 ? 256  GLY D C   1 
ATOM   10737 O  O   . GLY D 2 249 ? 141.698 134.924 195.527 1.00 144.37 ? 256  GLY D O   1 
ATOM   10738 N  N   . GLN D 2 250 ? 140.095 133.812 196.676 1.00 145.45 ? 257  GLN D N   1 
ATOM   10739 C  CA  . GLN D 2 250 ? 140.667 132.489 196.470 1.00 145.94 ? 257  GLN D CA  1 
ATOM   10740 C  C   . GLN D 2 250 ? 139.618 131.555 195.885 1.00 146.26 ? 257  GLN D C   1 
ATOM   10741 O  O   . GLN D 2 250 ? 138.465 131.551 196.326 1.00 145.41 ? 257  GLN D O   1 
ATOM   10742 C  CB  . GLN D 2 250 ? 141.209 131.904 197.779 1.00 145.38 ? 257  GLN D CB  1 
ATOM   10743 C  CG  . GLN D 2 250 ? 142.308 132.731 198.420 1.00 145.59 ? 257  GLN D CG  1 
ATOM   10744 C  CD  . GLN D 2 250 ? 143.134 131.933 199.408 1.00 145.84 ? 257  GLN D CD  1 
ATOM   10745 O  OE1 . GLN D 2 250 ? 142.759 130.827 199.796 1.00 145.33 ? 257  GLN D OE1 1 
ATOM   10746 N  NE2 . GLN D 2 250 ? 144.267 132.490 199.818 1.00 145.38 ? 257  GLN D NE2 1 
ATOM   10747 N  N   . LEU D 2 251 ? 140.029 130.759 194.899 1.00 148.74 ? 258  LEU D N   1 
ATOM   10748 C  CA  . LEU D 2 251 ? 139.157 129.796 194.242 1.00 147.74 ? 258  LEU D CA  1 
ATOM   10749 C  C   . LEU D 2 251 ? 139.795 128.415 194.295 1.00 147.98 ? 258  LEU D C   1 
ATOM   10750 O  O   . LEU D 2 251 ? 141.016 128.279 194.403 1.00 147.97 ? 258  LEU D O   1 
ATOM   10751 C  CB  . LEU D 2 251 ? 138.881 130.185 192.784 1.00 147.39 ? 258  LEU D CB  1 
ATOM   10752 C  CG  . LEU D 2 251 ? 138.159 131.513 192.562 1.00 148.07 ? 258  LEU D CG  1 
ATOM   10753 C  CD1 . LEU D 2 251 ? 138.115 131.859 191.083 1.00 147.51 ? 258  LEU D CD1 1 
ATOM   10754 C  CD2 . LEU D 2 251 ? 136.758 131.461 193.142 1.00 147.64 ? 258  LEU D CD2 1 
ATOM   10755 N  N   . SER D 2 252 ? 138.956 127.383 194.221 1.00 144.29 ? 259  SER D N   1 
ATOM   10756 C  CA  . SER D 2 252 ? 139.452 126.016 194.285 1.00 144.15 ? 259  SER D CA  1 
ATOM   10757 C  C   . SER D 2 252 ? 138.445 125.071 193.645 1.00 144.45 ? 259  SER D C   1 
ATOM   10758 O  O   . SER D 2 252 ? 137.233 125.300 193.696 1.00 144.20 ? 259  SER D O   1 
ATOM   10759 C  CB  . SER D 2 252 ? 139.729 125.587 195.731 1.00 143.40 ? 259  SER D CB  1 
ATOM   10760 O  OG  . SER D 2 252 ? 140.727 126.395 196.328 1.00 143.24 ? 259  SER D OG  1 
ATOM   10761 N  N   . GLY D 2 253 ? 138.973 124.006 193.041 1.00 140.71 ? 260  GLY D N   1 
ATOM   10762 C  CA  . GLY D 2 253 ? 138.175 122.902 192.542 1.00 140.06 ? 260  GLY D CA  1 
ATOM   10763 C  C   . GLY D 2 253 ? 137.039 123.267 191.609 1.00 140.86 ? 260  GLY D C   1 
ATOM   10764 O  O   . GLY D 2 253 ? 135.869 123.095 191.961 1.00 140.15 ? 260  GLY D O   1 
ATOM   10765 N  N   . LEU D 2 254 ? 137.362 123.765 190.419 1.00 139.08 ? 261  LEU D N   1 
ATOM   10766 C  CA  . LEU D 2 254 ? 136.354 124.075 189.411 1.00 138.25 ? 261  LEU D CA  1 
ATOM   10767 C  C   . LEU D 2 254 ? 136.077 122.814 188.600 1.00 138.55 ? 261  LEU D C   1 
ATOM   10768 O  O   . LEU D 2 254 ? 136.928 122.363 187.827 1.00 137.23 ? 261  LEU D O   1 
ATOM   10769 C  CB  . LEU D 2 254 ? 136.811 125.219 188.511 1.00 137.76 ? 261  LEU D CB  1 
ATOM   10770 C  CG  . LEU D 2 254 ? 135.745 125.749 187.549 1.00 137.62 ? 261  LEU D CG  1 
ATOM   10771 C  CD1 . LEU D 2 254 ? 134.653 126.485 188.303 1.00 137.32 ? 261  LEU D CD1 1 
ATOM   10772 C  CD2 . LEU D 2 254 ? 136.361 126.650 186.497 1.00 137.86 ? 261  LEU D CD2 1 
ATOM   10773 N  N   . TYR D 2 255 ? 134.887 122.247 188.777 1.00 140.64 ? 262  TYR D N   1 
ATOM   10774 C  CA  . TYR D 2 255 ? 134.468 121.037 188.083 1.00 139.96 ? 262  TYR D CA  1 
ATOM   10775 C  C   . TYR D 2 255 ? 133.358 121.401 187.108 1.00 140.77 ? 262  TYR D C   1 
ATOM   10776 O  O   . TYR D 2 255 ? 132.344 121.984 187.508 1.00 140.27 ? 262  TYR D O   1 
ATOM   10777 C  CB  . TYR D 2 255 ? 133.995 119.978 189.078 1.00 139.49 ? 262  TYR D CB  1 
ATOM   10778 C  CG  . TYR D 2 255 ? 133.368 118.759 188.442 1.00 139.86 ? 262  TYR D CG  1 
ATOM   10779 C  CD1 . TYR D 2 255 ? 134.156 117.770 187.869 1.00 139.44 ? 262  TYR D CD1 1 
ATOM   10780 C  CD2 . TYR D 2 255 ? 131.990 118.593 188.420 1.00 139.54 ? 262  TYR D CD2 1 
ATOM   10781 C  CE1 . TYR D 2 255 ? 133.589 116.652 187.291 1.00 139.92 ? 262  TYR D CE1 1 
ATOM   10782 C  CE2 . TYR D 2 255 ? 131.414 117.479 187.843 1.00 139.40 ? 262  TYR D CE2 1 
ATOM   10783 C  CZ  . TYR D 2 255 ? 132.218 116.511 187.279 1.00 140.01 ? 262  TYR D CZ  1 
ATOM   10784 O  OH  . TYR D 2 255 ? 131.649 115.399 186.703 1.00 139.59 ? 262  TYR D OH  1 
ATOM   10785 N  N   . TYR D 2 256 ? 133.547 121.058 185.834 1.00 137.90 ? 263  TYR D N   1 
ATOM   10786 C  CA  . TYR D 2 256 ? 132.598 121.426 184.782 1.00 136.93 ? 263  TYR D CA  1 
ATOM   10787 C  C   . TYR D 2 256 ? 132.397 120.227 183.860 1.00 136.37 ? 263  TYR D C   1 
ATOM   10788 O  O   . TYR D 2 256 ? 133.177 120.022 182.925 1.00 136.28 ? 263  TYR D O   1 
ATOM   10789 C  CB  . TYR D 2 256 ? 133.086 122.643 184.006 1.00 135.75 ? 263  TYR D CB  1 
ATOM   10790 C  CG  . TYR D 2 256 ? 132.051 123.222 183.070 1.00 135.56 ? 263  TYR D CG  1 
ATOM   10791 C  CD1 . TYR D 2 256 ? 130.896 123.812 183.562 1.00 135.87 ? 263  TYR D CD1 1 
ATOM   10792 C  CD2 . TYR D 2 256 ? 132.229 123.176 181.693 1.00 135.69 ? 263  TYR D CD2 1 
ATOM   10793 C  CE1 . TYR D 2 256 ? 129.946 124.342 182.710 1.00 136.18 ? 263  TYR D CE1 1 
ATOM   10794 C  CE2 . TYR D 2 256 ? 131.285 123.702 180.834 1.00 136.06 ? 263  TYR D CE2 1 
ATOM   10795 C  CZ  . TYR D 2 256 ? 130.146 124.284 181.348 1.00 136.13 ? 263  TYR D CZ  1 
ATOM   10796 O  OH  . TYR D 2 256 ? 129.202 124.811 180.497 1.00 135.17 ? 263  TYR D OH  1 
ATOM   10797 N  N   . ASN D 2 257 ? 131.345 119.452 184.125 1.00 133.51 ? 264  ASN D N   1 
ATOM   10798 C  CA  . ASN D 2 257 ? 130.916 118.355 183.255 1.00 133.15 ? 264  ASN D CA  1 
ATOM   10799 C  C   . ASN D 2 257 ? 132.063 117.389 182.962 1.00 133.87 ? 264  ASN D C   1 
ATOM   10800 O  O   . ASN D 2 257 ? 132.329 117.025 181.814 1.00 133.88 ? 264  ASN D O   1 
ATOM   10801 C  CB  . ASN D 2 257 ? 130.312 118.896 181.959 1.00 132.61 ? 264  ASN D CB  1 
ATOM   10802 C  CG  . ASN D 2 257 ? 129.175 119.866 182.209 1.00 132.66 ? 264  ASN D CG  1 
ATOM   10803 O  OD1 . ASN D 2 257 ? 128.163 119.511 182.812 1.00 132.48 ? 264  ASN D OD1 1 
ATOM   10804 N  ND2 . ASN D 2 257 ? 129.338 121.100 181.747 1.00 133.00 ? 264  ASN D ND2 1 
ATOM   10805 N  N   . GLY D 2 258 ? 132.749 116.969 184.021 1.00 141.18 ? 265  GLY D N   1 
ATOM   10806 C  CA  . GLY D 2 258 ? 133.865 116.060 183.875 1.00 140.92 ? 265  GLY D CA  1 
ATOM   10807 C  C   . GLY D 2 258 ? 135.171 116.704 183.472 1.00 141.23 ? 265  GLY D C   1 
ATOM   10808 O  O   . GLY D 2 258 ? 136.094 115.991 183.064 1.00 141.06 ? 265  GLY D O   1 
ATOM   10809 N  N   . LEU D 2 259 ? 135.280 118.026 183.569 1.00 140.37 ? 266  LEU D N   1 
ATOM   10810 C  CA  . LEU D 2 259 ? 136.500 118.752 183.223 1.00 140.45 ? 266  LEU D CA  1 
ATOM   10811 C  C   . LEU D 2 259 ? 136.920 119.575 184.436 1.00 141.28 ? 266  LEU D C   1 
ATOM   10812 O  O   . LEU D 2 259 ? 136.320 120.615 184.728 1.00 140.97 ? 266  LEU D O   1 
ATOM   10813 C  CB  . LEU D 2 259 ? 136.284 119.636 181.998 1.00 139.26 ? 266  LEU D CB  1 
ATOM   10814 C  CG  . LEU D 2 259 ? 136.449 118.966 180.634 1.00 139.76 ? 266  LEU D CG  1 
ATOM   10815 C  CD1 . LEU D 2 259 ? 136.089 119.930 179.516 1.00 139.92 ? 266  LEU D CD1 1 
ATOM   10816 C  CD2 . LEU D 2 259 ? 137.865 118.441 180.458 1.00 139.21 ? 266  LEU D CD2 1 
ATOM   10817 N  N   . LYS D 2 260 ? 137.948 119.110 185.142 1.00 140.04 ? 267  LYS D N   1 
ATOM   10818 C  CA  . LYS D 2 260 ? 138.507 119.845 186.273 1.00 138.60 ? 267  LYS D CA  1 
ATOM   10819 C  C   . LYS D 2 260 ? 139.442 120.911 185.719 1.00 138.98 ? 267  LYS D C   1 
ATOM   10820 O  O   . LYS D 2 260 ? 140.590 120.627 185.369 1.00 137.58 ? 267  LYS D O   1 
ATOM   10821 C  CB  . LYS D 2 260 ? 139.231 118.900 187.225 1.00 137.89 ? 267  LYS D CB  1 
ATOM   10822 C  CG  . LYS D 2 260 ? 138.306 117.992 188.018 1.00 138.32 ? 267  LYS D CG  1 
ATOM   10823 C  CD  . LYS D 2 260 ? 139.092 117.006 188.866 1.00 138.11 ? 267  LYS D CD  1 
ATOM   10824 C  CE  . LYS D 2 260 ? 138.174 115.990 189.524 1.00 138.01 ? 267  LYS D CE  1 
ATOM   10825 N  NZ  . LYS D 2 260 ? 138.939 114.869 190.133 1.00 138.86 ? 267  LYS D NZ  1 
ATOM   10826 N  N   . VAL D 2 261 ? 138.945 122.146 185.634 1.00 141.28 ? 268  VAL D N   1 
ATOM   10827 C  CA  . VAL D 2 261 ? 139.685 123.208 184.955 1.00 141.09 ? 268  VAL D CA  1 
ATOM   10828 C  C   . VAL D 2 261 ? 140.977 123.524 185.698 1.00 141.81 ? 268  VAL D C   1 
ATOM   10829 O  O   . VAL D 2 261 ? 142.057 123.586 185.100 1.00 141.44 ? 268  VAL D O   1 
ATOM   10830 C  CB  . VAL D 2 261 ? 138.804 124.459 184.798 1.00 140.30 ? 268  VAL D CB  1 
ATOM   10831 C  CG1 . VAL D 2 261 ? 139.544 125.532 184.015 1.00 140.18 ? 268  VAL D CG1 1 
ATOM   10832 C  CG2 . VAL D 2 261 ? 137.496 124.098 184.112 1.00 140.72 ? 268  VAL D CG2 1 
ATOM   10833 N  N   . LEU D 2 262 ? 140.888 123.727 187.014 1.00 140.99 ? 269  LEU D N   1 
ATOM   10834 C  CA  . LEU D 2 262 ? 142.074 124.091 187.783 1.00 139.66 ? 269  LEU D CA  1 
ATOM   10835 C  C   . LEU D 2 262 ? 143.063 122.934 187.866 1.00 139.31 ? 269  LEU D C   1 
ATOM   10836 O  O   . LEU D 2 262 ? 144.281 123.148 187.832 1.00 139.03 ? 269  LEU D O   1 
ATOM   10837 C  CB  . LEU D 2 262 ? 141.670 124.557 189.181 1.00 138.89 ? 269  LEU D CB  1 
ATOM   10838 C  CG  . LEU D 2 262 ? 140.729 125.762 189.225 1.00 138.86 ? 269  LEU D CG  1 
ATOM   10839 C  CD1 . LEU D 2 262 ? 140.272 126.040 190.647 1.00 138.66 ? 269  LEU D CD1 1 
ATOM   10840 C  CD2 . LEU D 2 262 ? 141.403 126.986 188.625 1.00 138.91 ? 269  LEU D CD2 1 
ATOM   10841 N  N   . ASN D 2 263 ? 142.559 121.702 187.973 1.00 142.35 ? 270  ASN D N   1 
ATOM   10842 C  CA  . ASN D 2 263 ? 143.446 120.547 188.081 1.00 142.39 ? 270  ASN D CA  1 
ATOM   10843 C  C   . ASN D 2 263 ? 144.300 120.384 186.830 1.00 142.44 ? 270  ASN D C   1 
ATOM   10844 O  O   . ASN D 2 263 ? 145.506 120.128 186.923 1.00 141.99 ? 270  ASN D O   1 
ATOM   10845 C  CB  . ASN D 2 263 ? 142.629 119.283 188.345 1.00 141.86 ? 270  ASN D CB  1 
ATOM   10846 C  CG  . ASN D 2 263 ? 143.496 118.089 188.690 1.00 142.09 ? 270  ASN D CG  1 
ATOM   10847 O  OD1 . ASN D 2 263 ? 144.084 117.459 187.811 1.00 141.93 ? 270  ASN D OD1 1 
ATOM   10848 N  ND2 . ASN D 2 263 ? 143.580 117.771 189.977 1.00 141.93 ? 270  ASN D ND2 1 
ATOM   10849 N  N   . MET D 2 264 ? 143.695 120.527 185.649 1.00 143.25 ? 271  MET D N   1 
ATOM   10850 C  CA  . MET D 2 264 ? 144.467 120.437 184.414 1.00 143.46 ? 271  MET D CA  1 
ATOM   10851 C  C   . MET D 2 264 ? 145.270 121.705 184.148 1.00 143.55 ? 271  MET D C   1 
ATOM   10852 O  O   . MET D 2 264 ? 146.312 121.643 183.485 1.00 143.07 ? 271  MET D O   1 
ATOM   10853 C  CB  . MET D 2 264 ? 143.546 120.127 183.231 1.00 143.04 ? 271  MET D CB  1 
ATOM   10854 C  CG  . MET D 2 264 ? 142.774 121.317 182.688 1.00 142.90 ? 271  MET D CG  1 
ATOM   10855 S  SD  . MET D 2 264 ? 141.678 120.851 181.334 1.00 144.59 ? 271  MET D SD  1 
ATOM   10856 C  CE  . MET D 2 264 ? 140.089 120.867 182.156 1.00 142.91 ? 271  MET D CE  1 
ATOM   10857 N  N   . ALA D 2 265 ? 144.808 122.854 184.647 1.00 141.53 ? 272  ALA D N   1 
ATOM   10858 C  CA  . ALA D 2 265 ? 145.582 124.084 184.513 1.00 140.86 ? 272  ALA D CA  1 
ATOM   10859 C  C   . ALA D 2 265 ? 146.888 123.991 185.289 1.00 140.91 ? 272  ALA D C   1 
ATOM   10860 O  O   . ALA D 2 265 ? 147.933 124.459 184.821 1.00 140.46 ? 272  ALA D O   1 
ATOM   10861 C  CB  . ALA D 2 265 ? 144.756 125.280 184.986 1.00 139.61 ? 272  ALA D CB  1 
ATOM   10862 N  N   . ALA D 2 266 ? 146.845 123.393 186.481 1.00 140.24 ? 273  ALA D N   1 
ATOM   10863 C  CA  . ALA D 2 266 ? 148.064 123.158 187.244 1.00 139.61 ? 273  ALA D CA  1 
ATOM   10864 C  C   . ALA D 2 266 ? 149.016 122.213 186.523 1.00 139.54 ? 273  ALA D C   1 
ATOM   10865 O  O   . ALA D 2 266 ? 150.212 122.200 186.831 1.00 138.71 ? 273  ALA D O   1 
ATOM   10866 C  CB  . ALA D 2 266 ? 147.723 122.602 188.627 1.00 138.92 ? 273  ALA D CB  1 
ATOM   10867 N  N   . GLU D 2 267 ? 148.513 121.425 185.573 1.00 146.54 ? 274  GLU D N   1 
ATOM   10868 C  CA  . GLU D 2 267 ? 149.350 120.560 184.753 1.00 146.93 ? 274  GLU D CA  1 
ATOM   10869 C  C   . GLU D 2 267 ? 149.943 121.283 183.551 1.00 147.36 ? 274  GLU D C   1 
ATOM   10870 O  O   . GLU D 2 267 ? 150.701 120.667 182.793 1.00 147.53 ? 274  GLU D O   1 
ATOM   10871 C  CB  . GLU D 2 267 ? 148.547 119.345 184.279 1.00 145.95 ? 274  GLU D CB  1 
ATOM   10872 C  CG  . GLU D 2 267 ? 148.056 118.446 185.402 1.00 145.70 ? 274  GLU D CG  1 
ATOM   10873 C  CD  . GLU D 2 267 ? 149.154 117.567 185.968 1.00 146.13 ? 274  GLU D CD  1 
ATOM   10874 O  OE1 . GLU D 2 267 ? 150.176 117.369 185.278 1.00 146.07 ? 274  GLU D OE1 1 
ATOM   10875 O  OE2 . GLU D 2 267 ? 148.994 117.072 187.104 1.00 146.84 ? 274  GLU D OE2 1 
ATOM   10876 N  N   . ASN D 2 268 ? 149.614 122.564 183.364 1.00 150.37 ? 275  ASN D N   1 
ATOM   10877 C  CA  . ASN D 2 268 ? 150.154 123.383 182.277 1.00 150.62 ? 275  ASN D CA  1 
ATOM   10878 C  C   . ASN D 2 268 ? 149.858 122.767 180.909 1.00 150.91 ? 275  ASN D C   1 
ATOM   10879 O  O   . ASN D 2 268 ? 150.738 122.632 180.057 1.00 150.33 ? 275  ASN D O   1 
ATOM   10880 C  CB  . ASN D 2 268 ? 151.656 123.618 182.461 1.00 150.83 ? 275  ASN D CB  1 
ATOM   10881 C  CG  . ASN D 2 268 ? 152.140 124.877 181.765 1.00 150.40 ? 275  ASN D CG  1 
ATOM   10882 O  OD1 . ASN D 2 268 ? 151.560 125.314 180.771 1.00 149.87 ? 275  ASN D OD1 1 
ATOM   10883 N  ND2 . ASN D 2 268 ? 153.211 125.466 182.286 1.00 150.09 ? 275  ASN D ND2 1 
ATOM   10884 N  N   . ASP D 2 269 ? 148.600 122.385 180.705 1.00 149.93 ? 276  ASP D N   1 
ATOM   10885 C  CA  . ASP D 2 269 ? 148.179 121.886 179.405 1.00 149.87 ? 276  ASP D CA  1 
ATOM   10886 C  C   . ASP D 2 269 ? 148.182 123.017 178.381 1.00 150.45 ? 276  ASP D C   1 
ATOM   10887 O  O   . ASP D 2 269 ? 148.041 124.195 178.720 1.00 150.03 ? 276  ASP D O   1 
ATOM   10888 C  CB  . ASP D 2 269 ? 146.792 121.249 179.495 1.00 149.33 ? 276  ASP D CB  1 
ATOM   10889 C  CG  . ASP D 2 269 ? 146.509 120.302 178.345 1.00 149.67 ? 276  ASP D CG  1 
ATOM   10890 O  OD1 . ASP D 2 269 ? 147.434 120.039 177.548 1.00 148.89 ? 276  ASP D OD1 1 
ATOM   10891 O  OD2 . ASP D 2 269 ? 145.362 119.819 178.239 1.00 150.02 ? 276  ASP D OD2 1 
ATOM   10892 N  N   . ALA D 2 270 ? 148.343 122.643 177.110 1.00 150.27 ? 277  ALA D N   1 
ATOM   10893 C  CA  . ALA D 2 270 ? 148.581 123.616 176.050 1.00 149.45 ? 277  ALA D CA  1 
ATOM   10894 C  C   . ALA D 2 270 ? 147.362 124.464 175.711 1.00 149.68 ? 277  ALA D C   1 
ATOM   10895 O  O   . ALA D 2 270 ? 147.499 125.429 174.952 1.00 149.58 ? 277  ALA D O   1 
ATOM   10896 C  CB  . ALA D 2 270 ? 149.071 122.900 174.790 1.00 148.55 ? 277  ALA D CB  1 
ATOM   10897 N  N   . ASN D 2 271 ? 146.183 124.141 176.242 1.00 148.11 ? 278  ASN D N   1 
ATOM   10898 C  CA  . ASN D 2 271 ? 144.954 124.836 175.881 1.00 147.56 ? 278  ASN D CA  1 
ATOM   10899 C  C   . ASN D 2 271 ? 144.485 125.814 176.956 1.00 146.98 ? 278  ASN D C   1 
ATOM   10900 O  O   . ASN D 2 271 ? 143.327 126.244 176.927 1.00 146.08 ? 278  ASN D O   1 
ATOM   10901 C  CB  . ASN D 2 271 ? 143.851 123.824 175.570 1.00 147.08 ? 278  ASN D CB  1 
ATOM   10902 C  CG  . ASN D 2 271 ? 144.252 122.842 174.488 1.00 147.41 ? 278  ASN D CG  1 
ATOM   10903 O  OD1 . ASN D 2 271 ? 144.354 123.201 173.315 1.00 147.59 ? 278  ASN D OD1 1 
ATOM   10904 N  ND2 . ASN D 2 271 ? 144.482 121.593 174.877 1.00 146.78 ? 278  ASN D ND2 1 
ATOM   10905 N  N   . ILE D 2 272 ? 145.353 126.177 177.896 1.00 145.68 ? 279  ILE D N   1 
ATOM   10906 C  CA  . ILE D 2 272 ? 145.015 127.103 178.970 1.00 146.14 ? 279  ILE D CA  1 
ATOM   10907 C  C   . ILE D 2 272 ? 145.972 128.285 178.922 1.00 146.03 ? 279  ILE D C   1 
ATOM   10908 O  O   . ILE D 2 272 ? 147.187 128.106 178.780 1.00 145.06 ? 279  ILE D O   1 
ATOM   10909 C  CB  . ILE D 2 272 ? 145.059 126.419 180.352 1.00 145.33 ? 279  ILE D CB  1 
ATOM   10910 C  CG1 . ILE D 2 272 ? 144.086 125.239 180.396 1.00 144.38 ? 279  ILE D CG1 1 
ATOM   10911 C  CG2 . ILE D 2 272 ? 144.737 127.412 181.452 1.00 144.97 ? 279  ILE D CG2 1 
ATOM   10912 C  CD1 . ILE D 2 272 ? 144.749 123.912 180.655 1.00 143.56 ? 279  ILE D CD1 1 
ATOM   10913 N  N   . ALA D 2 273 ? 145.422 129.494 179.036 1.00 145.24 ? 280  ALA D N   1 
ATOM   10914 C  CA  . ALA D 2 273 ? 146.214 130.717 179.037 1.00 145.05 ? 280  ALA D CA  1 
ATOM   10915 C  C   . ALA D 2 273 ? 145.847 131.559 180.249 1.00 145.85 ? 280  ALA D C   1 
ATOM   10916 O  O   . ALA D 2 273 ? 144.667 131.837 180.479 1.00 145.37 ? 280  ALA D O   1 
ATOM   10917 C  CB  . ALA D 2 273 ? 145.998 131.519 177.749 1.00 144.27 ? 280  ALA D CB  1 
ATOM   10918 N  N   . ILE D 2 274 ? 146.855 131.982 181.008 1.00 143.90 ? 281  ILE D N   1 
ATOM   10919 C  CA  . ILE D 2 274 ? 146.659 132.771 182.219 1.00 143.29 ? 281  ILE D CA  1 
ATOM   10920 C  C   . ILE D 2 274 ? 147.258 134.155 182.004 1.00 142.97 ? 281  ILE D C   1 
ATOM   10921 O  O   . ILE D 2 274 ? 148.309 134.297 181.364 1.00 142.60 ? 281  ILE D O   1 
ATOM   10922 C  CB  . ILE D 2 274 ? 147.265 132.070 183.455 1.00 142.81 ? 281  ILE D CB  1 
ATOM   10923 C  CG1 . ILE D 2 274 ? 146.402 132.316 184.693 1.00 142.99 ? 281  ILE D CG1 1 
ATOM   10924 C  CG2 . ILE D 2 274 ? 148.705 132.502 183.713 1.00 142.60 ? 281  ILE D CG2 1 
ATOM   10925 C  CD1 . ILE D 2 274 ? 146.532 131.237 185.744 1.00 142.21 ? 281  ILE D CD1 1 
ATOM   10926 N  N   . VAL D 2 275 ? 146.559 135.182 182.490 1.00 141.43 ? 282  VAL D N   1 
ATOM   10927 C  CA  . VAL D 2 275 ? 147.017 136.565 182.400 1.00 141.99 ? 282  VAL D CA  1 
ATOM   10928 C  C   . VAL D 2 275 ? 146.638 137.275 183.692 1.00 142.05 ? 282  VAL D C   1 
ATOM   10929 O  O   . VAL D 2 275 ? 145.541 137.074 184.222 1.00 141.91 ? 282  VAL D O   1 
ATOM   10930 C  CB  . VAL D 2 275 ? 146.411 137.292 181.177 1.00 141.38 ? 282  VAL D CB  1 
ATOM   10931 C  CG1 . VAL D 2 275 ? 146.651 138.792 181.262 1.00 140.41 ? 282  VAL D CG1 1 
ATOM   10932 C  CG2 . VAL D 2 275 ? 146.984 136.743 179.877 1.00 140.69 ? 282  VAL D CG2 1 
ATOM   10933 N  N   . GLY D 2 276 ? 147.552 138.093 184.210 1.00 145.85 ? 283  GLY D N   1 
ATOM   10934 C  CA  . GLY D 2 276 ? 147.238 138.940 185.344 1.00 145.29 ? 283  GLY D CA  1 
ATOM   10935 C  C   . GLY D 2 276 ? 147.769 138.453 186.676 1.00 145.67 ? 283  GLY D C   1 
ATOM   10936 O  O   . GLY D 2 276 ? 148.820 137.808 186.740 1.00 145.26 ? 283  GLY D O   1 
ATOM   10937 N  N   . ASN D 2 277 ? 147.040 138.759 187.752 1.00 150.76 ? 284  ASN D N   1 
ATOM   10938 C  CA  . ASN D 2 277 ? 147.454 138.433 189.112 1.00 150.69 ? 284  ASN D CA  1 
ATOM   10939 C  C   . ASN D 2 277 ? 146.932 137.080 189.580 1.00 150.48 ? 284  ASN D C   1 
ATOM   10940 O  O   . ASN D 2 277 ? 146.767 136.869 190.789 1.00 149.62 ? 284  ASN D O   1 
ATOM   10941 C  CB  . ASN D 2 277 ? 147.005 139.535 190.073 1.00 149.40 ? 284  ASN D CB  1 
ATOM   10942 C  CG  . ASN D 2 277 ? 148.099 140.548 190.351 1.00 149.24 ? 284  ASN D CG  1 
ATOM   10943 O  OD1 . ASN D 2 277 ? 147.933 141.741 190.102 1.00 148.90 ? 284  ASN D OD1 1 
ATOM   10944 N  ND2 . ASN D 2 277 ? 149.225 140.075 190.872 1.00 149.44 ? 284  ASN D ND2 1 
ATOM   10945 N  N   . VAL D 2 278 ? 146.668 136.157 188.660 1.00 159.06 ? 285  VAL D N   1 
ATOM   10946 C  CA  . VAL D 2 278 ? 146.198 134.824 189.023 1.00 159.97 ? 285  VAL D CA  1 
ATOM   10947 C  C   . VAL D 2 278 ? 147.411 133.997 189.437 1.00 159.61 ? 285  VAL D C   1 
ATOM   10948 O  O   . VAL D 2 278 ? 148.202 133.571 188.593 1.00 159.36 ? 285  VAL D O   1 
ATOM   10949 C  CB  . VAL D 2 278 ? 145.438 134.159 187.870 1.00 159.80 ? 285  VAL D CB  1 
ATOM   10950 C  CG1 . VAL D 2 278 ? 144.656 132.958 188.376 1.00 159.15 ? 285  VAL D CG1 1 
ATOM   10951 C  CG2 . VAL D 2 278 ? 144.511 135.160 187.199 1.00 157.57 ? 285  VAL D CG2 1 
ATOM   10952 N  N   . ARG D 2 279 ? 147.558 133.771 190.739 1.00 157.93 ? 286  ARG D N   1 
ATOM   10953 C  CA  . ARG D 2 279 ? 148.692 133.050 191.293 1.00 157.40 ? 286  ARG D CA  1 
ATOM   10954 C  C   . ARG D 2 279 ? 148.240 131.723 191.888 1.00 157.35 ? 286  ARG D C   1 
ATOM   10955 O  O   . ARG D 2 279 ? 147.082 131.551 192.279 1.00 157.75 ? 286  ARG D O   1 
ATOM   10956 C  CB  . ARG D 2 279 ? 149.405 133.885 192.362 1.00 157.50 ? 286  ARG D CB  1 
ATOM   10957 C  CG  . ARG D 2 279 ? 150.197 135.059 191.813 1.00 157.35 ? 286  ARG D CG  1 
ATOM   10958 C  CD  . ARG D 2 279 ? 150.786 135.903 192.934 1.00 157.93 ? 286  ARG D CD  1 
ATOM   10959 N  NE  . ARG D 2 279 ? 151.558 135.105 193.879 1.00 158.88 ? 286  ARG D NE  1 
ATOM   10960 C  CZ  . ARG D 2 279 ? 151.177 134.837 195.121 1.00 158.32 ? 286  ARG D CZ  1 
ATOM   10961 N  NH1 . ARG D 2 279 ? 150.033 135.290 195.606 1.00 157.35 ? 286  ARG D NH1 1 
ATOM   10962 N  NH2 . ARG D 2 279 ? 151.964 134.095 195.895 1.00 157.96 ? 286  ARG D NH2 1 
ATOM   10963 N  N   . LEU D 2 280 ? 149.178 130.782 191.953 1.00 152.18 ? 287  LEU D N   1 
ATOM   10964 C  CA  . LEU D 2 280 ? 148.914 129.456 192.491 1.00 152.51 ? 287  LEU D CA  1 
ATOM   10965 C  C   . LEU D 2 280 ? 149.315 129.407 193.960 1.00 153.05 ? 287  LEU D C   1 
ATOM   10966 O  O   . LEU D 2 280 ? 150.422 129.818 194.322 1.00 152.76 ? 287  LEU D O   1 
ATOM   10967 C  CB  . LEU D 2 280 ? 149.673 128.393 191.696 1.00 152.41 ? 287  LEU D CB  1 
ATOM   10968 C  CG  . LEU D 2 280 ? 149.774 126.997 192.315 1.00 152.46 ? 287  LEU D CG  1 
ATOM   10969 C  CD1 . LEU D 2 280 ? 148.394 126.392 192.511 1.00 152.23 ? 287  LEU D CD1 1 
ATOM   10970 C  CD2 . LEU D 2 280 ? 150.644 126.091 191.457 1.00 151.46 ? 287  LEU D CD2 1 
ATOM   10971 N  N   . VAL D 2 281 ? 148.415 128.904 194.799 1.00 147.05 ? 288  VAL D N   1 
ATOM   10972 C  CA  . VAL D 2 281 ? 148.672 128.801 196.231 1.00 146.69 ? 288  VAL D CA  1 
ATOM   10973 C  C   . VAL D 2 281 ? 149.557 127.586 196.482 1.00 145.88 ? 288  VAL D C   1 
ATOM   10974 O  O   . VAL D 2 281 ? 149.215 126.464 196.094 1.00 145.08 ? 288  VAL D O   1 
ATOM   10975 C  CB  . VAL D 2 281 ? 147.361 128.704 197.025 1.00 145.73 ? 288  VAL D CB  1 
ATOM   10976 C  CG1 . VAL D 2 281 ? 147.626 128.193 198.434 1.00 144.59 ? 288  VAL D CG1 1 
ATOM   10977 C  CG2 . VAL D 2 281 ? 146.668 130.056 197.067 1.00 144.99 ? 288  VAL D CG2 1 
ATOM   10978 N  N   . GLY D 2 282 ? 150.696 127.809 197.130 1.00 128.30 ? 289  GLY D N   1 
ATOM   10979 C  CA  . GLY D 2 282 ? 151.623 126.735 197.436 1.00 127.69 ? 289  GLY D CA  1 
ATOM   10980 C  C   . GLY D 2 282 ? 152.339 126.921 198.759 1.00 127.13 ? 289  GLY D C   1 
ATOM   10981 O  O   . GLY D 2 282 ? 153.439 127.471 198.808 1.00 127.07 ? 289  GLY D O   1 
HETATM 10982 C  C1  . NAG E 3 .   ? 131.148 181.923 99.839  1.00 105.27 ? 1017 NAG A C1  1 
HETATM 10983 C  C2  . NAG E 3 .   ? 130.797 183.219 99.095  1.00 106.12 ? 1017 NAG A C2  1 
HETATM 10984 C  C3  . NAG E 3 .   ? 132.036 183.785 98.394  1.00 105.00 ? 1017 NAG A C3  1 
HETATM 10985 C  C4  . NAG E 3 .   ? 133.185 183.953 99.377  1.00 106.50 ? 1017 NAG A C4  1 
HETATM 10986 C  C5  . NAG E 3 .   ? 133.483 182.618 100.042 1.00 105.39 ? 1017 NAG A C5  1 
HETATM 10987 C  C6  . NAG E 3 .   ? 134.555 182.714 101.103 1.00 104.75 ? 1017 NAG A C6  1 
HETATM 10988 C  C7  . NAG E 3 .   ? 128.932 183.952 97.676  1.00 105.18 ? 1017 NAG A C7  1 
HETATM 10989 C  C8  . NAG E 3 .   ? 127.901 183.530 96.673  1.00 103.11 ? 1017 NAG A C8  1 
HETATM 10990 N  N2  . NAG E 3 .   ? 129.736 182.985 98.129  1.00 105.77 ? 1017 NAG A N2  1 
HETATM 10991 O  O3  . NAG E 3 .   ? 131.727 185.038 97.794  1.00 104.16 ? 1017 NAG A O3  1 
HETATM 10992 O  O4  . NAG E 3 .   ? 134.352 184.411 98.704  1.00 106.52 ? 1017 NAG A O4  1 
HETATM 10993 O  O5  . NAG E 3 .   ? 132.299 182.144 100.695 1.00 106.79 ? 1017 NAG A O5  1 
HETATM 10994 O  O6  . NAG E 3 .   ? 134.068 183.344 102.280 1.00 104.28 ? 1017 NAG A O6  1 
HETATM 10995 O  O7  . NAG E 3 .   ? 129.031 185.114 98.059  1.00 104.30 ? 1017 NAG A O7  1 
HETATM 10996 C  C1  . NAG F 3 .   ? 147.667 158.372 125.682 1.00 30.00  ? 1018 NAG A C1  1 
HETATM 10997 C  C2  . NAG F 3 .   ? 148.652 157.791 126.690 1.00 30.00  ? 1018 NAG A C2  1 
HETATM 10998 C  C3  . NAG F 3 .   ? 149.862 158.708 126.806 1.00 30.00  ? 1018 NAG A C3  1 
HETATM 10999 C  C4  . NAG F 3 .   ? 150.474 158.886 125.425 1.00 30.00  ? 1018 NAG A C4  1 
HETATM 11000 C  C5  . NAG F 3 .   ? 149.427 159.429 124.462 1.00 30.00  ? 1018 NAG A C5  1 
HETATM 11001 C  C6  . NAG F 3 .   ? 150.006 159.582 123.060 1.00 30.00  ? 1018 NAG A C6  1 
HETATM 11002 C  C7  . NAG F 3 .   ? 148.656 157.428 129.104 1.00 30.00  ? 1018 NAG A C7  1 
HETATM 11003 C  C8  . NAG F 3 .   ? 147.915 157.767 130.363 1.00 30.00  ? 1018 NAG A C8  1 
HETATM 11004 N  N2  . NAG F 3 .   ? 147.989 157.630 127.971 1.00 30.00  ? 1018 NAG A N2  1 
HETATM 11005 O  O3  . NAG F 3 .   ? 150.841 158.132 127.677 1.00 30.00  ? 1018 NAG A O3  1 
HETATM 11006 O  O4  . NAG F 3 .   ? 151.576 159.797 125.500 1.00 30.00  ? 1018 NAG A O4  1 
HETATM 11007 O  O5  . NAG F 3 .   ? 148.306 158.546 124.417 1.00 30.00  ? 1018 NAG A O5  1 
HETATM 11008 O  O6  . NAG F 3 .   ? 150.311 158.289 122.527 1.00 30.00  ? 1018 NAG A O6  1 
HETATM 11009 O  O7  . NAG F 3 .   ? 149.797 156.995 129.118 1.00 30.00  ? 1018 NAG A O7  1 
HETATM 11010 C  C1  . NAG G 3 .   ? 123.399 74.934  167.576 1.00 146.36 ? 1017 NAG B C1  1 
HETATM 11011 C  C2  . NAG G 3 .   ? 122.438 74.290  168.570 1.00 147.09 ? 1017 NAG B C2  1 
HETATM 11012 C  C3  . NAG G 3 .   ? 123.082 73.060  169.200 1.00 148.52 ? 1017 NAG B C3  1 
HETATM 11013 C  C4  . NAG G 3 .   ? 123.564 72.101  168.118 1.00 149.29 ? 1017 NAG B C4  1 
HETATM 11014 C  C5  . NAG G 3 .   ? 124.462 72.830  167.121 1.00 147.80 ? 1017 NAG B C5  1 
HETATM 11015 C  C6  . NAG G 3 .   ? 124.857 71.968  165.944 1.00 147.87 ? 1017 NAG B C6  1 
HETATM 11016 C  C7  . NAG G 3 .   ? 120.861 75.884  169.565 1.00 147.04 ? 1017 NAG B C7  1 
HETATM 11017 C  C8  . NAG G 3 .   ? 120.599 76.823  170.703 1.00 145.67 ? 1017 NAG B C8  1 
HETATM 11018 N  N2  . NAG G 3 .   ? 122.030 75.237  169.595 1.00 146.22 ? 1017 NAG B N2  1 
HETATM 11019 O  O3  . NAG G 3 .   ? 122.140 72.409  170.045 1.00 148.59 ? 1017 NAG B O3  1 
HETATM 11020 O  O4  . NAG G 3 .   ? 124.291 71.030  168.707 1.00 148.82 ? 1017 NAG B O4  1 
HETATM 11021 O  O5  . NAG G 3 .   ? 123.779 73.973  166.584 1.00 147.07 ? 1017 NAG B O5  1 
HETATM 11022 O  O6  . NAG G 3 .   ? 123.861 71.985  164.930 1.00 147.24 ? 1017 NAG B O6  1 
HETATM 11023 O  O7  . NAG G 3 .   ? 120.051 75.719  168.658 1.00 148.38 ? 1017 NAG B O7  1 
HETATM 11024 C  C1  . NAG H 3 .   ? 129.272 94.303  130.460 1.00 161.11 ? 1018 NAG B C1  1 
HETATM 11025 C  C2  . NAG H 3 .   ? 127.903 93.557  130.363 1.00 161.06 ? 1018 NAG B C2  1 
HETATM 11026 C  C3  . NAG H 3 .   ? 127.743 92.928  128.973 1.00 160.59 ? 1018 NAG B C3  1 
HETATM 11027 C  C4  . NAG H 3 .   ? 128.004 93.949  127.876 1.00 160.79 ? 1018 NAG B C4  1 
HETATM 11028 C  C5  . NAG H 3 .   ? 129.399 94.513  128.056 1.00 160.36 ? 1018 NAG B C5  1 
HETATM 11029 C  C6  . NAG H 3 .   ? 129.783 95.562  127.029 1.00 160.06 ? 1018 NAG B C6  1 
HETATM 11030 C  C7  . NAG H 3 .   ? 126.781 91.704  131.573 1.00 160.37 ? 1018 NAG B C7  1 
HETATM 11031 C  C8  . NAG H 3 .   ? 126.909 90.717  132.690 1.00 160.33 ? 1018 NAG B C8  1 
HETATM 11032 N  N2  . NAG H 3 .   ? 127.825 92.527  131.394 1.00 160.30 ? 1018 NAG B N2  1 
HETATM 11033 O  O3  . NAG H 3 .   ? 126.435 92.398  128.821 1.00 160.16 ? 1018 NAG B O3  1 
HETATM 11034 O  O4  . NAG H 3 .   ? 127.880 93.388  126.575 1.00 161.48 ? 1018 NAG B O4  1 
HETATM 11035 O  O5  . NAG H 3 .   ? 129.445 95.163  129.325 1.00 160.90 ? 1018 NAG B O5  1 
HETATM 11036 O  O6  . NAG H 3 .   ? 131.146 95.950  127.177 1.00 160.29 ? 1018 NAG B O6  1 
HETATM 11037 O  O7  . NAG H 3 .   ? 125.776 91.756  130.866 1.00 161.19 ? 1018 NAG B O7  1 
HETATM 11038 CA CA  . CA  I 4 .   ? 98.406  142.647 107.190 1.00 59.46  ? 1007 CA  C CA  1 
HETATM 11039 C  C1  . NAG J 3 .   ? 89.429  155.295 102.912 1.00 141.41 ? 1008 NAG C C1  1 
HETATM 11040 C  C2  . NAG J 3 .   ? 90.668  156.162 103.145 1.00 142.03 ? 1008 NAG C C2  1 
HETATM 11041 C  C3  . NAG J 3 .   ? 90.423  157.147 104.286 1.00 142.53 ? 1008 NAG C C3  1 
HETATM 11042 C  C4  . NAG J 3 .   ? 89.156  157.952 104.034 1.00 142.86 ? 1008 NAG C C4  1 
HETATM 11043 C  C5  . NAG J 3 .   ? 87.982  157.010 103.793 1.00 141.86 ? 1008 NAG C C5  1 
HETATM 11044 C  C6  . NAG J 3 .   ? 86.706  157.735 103.433 1.00 141.08 ? 1008 NAG C C6  1 
HETATM 11045 C  C7  . NAG J 3 .   ? 93.071  155.671 103.044 1.00 141.11 ? 1008 NAG C C7  1 
HETATM 11046 C  C8  . NAG J 3 .   ? 94.155  154.706 103.418 1.00 140.75 ? 1008 NAG C C8  1 
HETATM 11047 N  N2  . NAG J 3 .   ? 91.833  155.338 103.424 1.00 140.54 ? 1008 NAG C N2  1 
HETATM 11048 O  O3  . NAG J 3 .   ? 91.538  158.024 104.403 1.00 141.62 ? 1008 NAG C O3  1 
HETATM 11049 O  O4  . NAG J 3 .   ? 88.874  158.784 105.153 1.00 142.27 ? 1008 NAG C O4  1 
HETATM 11050 O  O5  . NAG J 3 .   ? 88.284  156.134 102.698 1.00 142.71 ? 1008 NAG C O5  1 
HETATM 11051 O  O6  . NAG J 3 .   ? 86.806  158.364 102.162 1.00 140.18 ? 1008 NAG C O6  1 
HETATM 11052 O  O7  . NAG J 3 .   ? 93.305  156.704 102.425 1.00 142.33 ? 1008 NAG C O7  1 
HETATM 11053 CA CA  . CA  K 4 .   ? 120.512 127.320 172.258 1.00 80.36  ? 1007 CA  D CA  1 
HETATM 11054 C  C1  . NAG L 3 .   ? 111.856 120.393 184.218 1.00 157.87 ? 1008 NAG D C1  1 
HETATM 11055 C  C2  . NAG L 3 .   ? 111.989 119.258 183.202 1.00 157.45 ? 1008 NAG D C2  1 
HETATM 11056 C  C3  . NAG L 3 .   ? 110.618 118.886 182.645 1.00 156.71 ? 1008 NAG D C3  1 
HETATM 11057 C  C4  . NAG L 3 .   ? 109.649 118.575 183.778 1.00 157.65 ? 1008 NAG D C4  1 
HETATM 11058 C  C5  . NAG L 3 .   ? 109.609 119.735 184.769 1.00 157.63 ? 1008 NAG D C5  1 
HETATM 11059 C  C6  . NAG L 3 .   ? 108.758 119.445 185.983 1.00 156.78 ? 1008 NAG D C6  1 
HETATM 11060 C  C7  . NAG L 3 .   ? 113.944 118.877 181.768 1.00 157.58 ? 1008 NAG D C7  1 
HETATM 11061 C  C8  . NAG L 3 .   ? 114.772 119.407 180.637 1.00 156.57 ? 1008 NAG D C8  1 
HETATM 11062 N  N2  . NAG L 3 .   ? 112.895 119.625 182.126 1.00 157.29 ? 1008 NAG D N2  1 
HETATM 11063 O  O3  . NAG L 3 .   ? 110.746 117.756 181.789 1.00 155.76 ? 1008 NAG D O3  1 
HETATM 11064 O  O4  . NAG L 3 .   ? 108.343 118.357 183.257 1.00 157.20 ? 1008 NAG D O4  1 
HETATM 11065 O  O5  . NAG L 3 .   ? 110.933 120.013 185.248 1.00 157.80 ? 1008 NAG D O5  1 
HETATM 11066 O  O6  . NAG L 3 .   ? 109.444 118.614 186.910 1.00 156.48 ? 1008 NAG D O6  1 
HETATM 11067 O  O7  . NAG L 3 .   ? 114.213 117.822 182.333 1.00 157.81 ? 1008 NAG D O7  1 
# 
