data_9BGG
# 
_entry.id   9BGG 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9BGG         pdb_00009bgg 10.2210/pdb9bgg/pdb 
WWPDB D_1000283252 ?            ?                   
EMDB  EMD-44512    ?            ?                   
# 
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 2025-02-26 ? 
2 'EM metadata'     1 0 2025-02-26 ? 
3 FSC               1 0 2025-02-26 ? 
4 'Half map'        1 0 2025-02-26 1 
5 'Half map'        1 0 2025-02-26 2 
6 Image             1 0 2025-02-26 ? 
7 Mask              1 0 2025-02-26 1 
8 'Primary map'     1 0 2025-02-26 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 FSC               repository 'Initial release' ? ? 
4 4 'Half map'        repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 Image             repository 'Initial release' ? ? 
7 7 Mask              repository 'Initial release' ? ? 
8 8 'Primary map'     repository 'Initial release' ? ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BGG 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-18 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB  .                                                                                            9bgf      unspecified            
EMDB 'Cryo-EM structure of a highly active truncation of human GlcNAc-1-phosphotransferase, S1S3' EMD-44512 'associated EM volume' 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              huilin.li@vai.org 
_pdbx_contact_author.name_first         Huilin 
_pdbx_contact_author.name_last          Li 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8085-8928 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, H.' 1 0000-0003-0493-0566 
'Li, H.' 2 0000-0001-8085-8928 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_id_ASTM           JBCHA3 
_citation.journal_id_CSD            0071 
_citation.journal_id_ISSN           1083-351X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            300 
_citation.language                  ? 
_citation.page_first                107706 
_citation.page_last                 107706 
_citation.title                     
'Structure of a truncated human GlcNAc-1-phosphotransferase variant reveals the basis for its hyperactivity.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jbc.2024.107706 
_citation.pdbx_database_id_PubMed   39178950 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Li, H.'         1 ? 
primary 'Doray, B.'      2 ? 
primary 'Jennings, B.C.' 3 ? 
primary 'Lee, W.S.'      4 ? 
primary 'Liu, L.'        5 ? 
primary 'Kornfeld, S.'   6 ? 
primary 'Li, H.'         7 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 
'highly active truncation of GlcNAc-1-phosphotransferase, S1S3,N-acetylglucosamine-1-phosphotransferase subunit beta' 58669.336 2 
? ? ? ? 
2 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   4 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;DEDQVDPRLIDGKWSRDQYHVLFDSYRDNIAGKSFQNRLCLPMPIDVVYTWVNGTDLELLKELTELKRSKRDPLIPECQG
KQTPEKDKCYRDDISASRFEDNEELRYSLRSIERHAPWVRNIFIVTNGQIPSWLNLDNPRVTIVTHQDVFRNLSHLPTFS
SPAIESHIHRIEGLSQKFIYLNDDVMFGKDVWPDDFYSHSKGQKVYLTWPVPNGGSGGDTFADSLRYVNKILNSKFGFTS
RKVPAHMPHMIDRIVMQELQDMFPEEFDKTSFHKVRHSEDMQFAFSYFYYLMSAVQPLNISQVFDEVDTDQSGVLSDREI
RTLATRIHELPLSLQDLTGLEHMLINCSKMLPADITQLNNIPPTQESYYDPNLPPVTKSLVTNCKPVTDKIHKAYKDKNK
YRFEIMGEEEIAFKMIRTNVSHVVGQLDDIRKNPRKFVCLNDNIDHNHKDAQTVKAVLRDFYESMFPIPSQFELPREYRN
RFLHMHELQEWRAYRDKLK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;DEDQVDPRLIDGKWSRDQYHVLFDSYRDNIAGKSFQNRLCLPMPIDVVYTWVNGTDLELLKELTELKRSKRDPLIPECQG
KQTPEKDKCYRDDISASRFEDNEELRYSLRSIERHAPWVRNIFIVTNGQIPSWLNLDNPRVTIVTHQDVFRNLSHLPTFS
SPAIESHIHRIEGLSQKFIYLNDDVMFGKDVWPDDFYSHSKGQKVYLTWPVPNGGSGGDTFADSLRYVNKILNSKFGFTS
RKVPAHMPHMIDRIVMQELQDMFPEEFDKTSFHKVRHSEDMQFAFSYFYYLMSAVQPLNISQVFDEVDTDQSGVLSDREI
RTLATRIHELPLSLQDLTGLEHMLINCSKMLPADITQLNNIPPTQESYYDPNLPPVTKSLVTNCKPVTDKIHKAYKDKNK
YRFEIMGEEEIAFKMIRTNVSHVVGQLDDIRKNPRKFVCLNDNIDHNHKDAQTVKAVLRDFYESMFPIPSQFELPREYRN
RFLHMHELQEWRAYRDKLK
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        2-acetamido-2-deoxy-beta-D-glucopyranose 
_pdbx_entity_nonpoly.comp_id     NAG 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ASP n 
1 2   GLU n 
1 3   ASP n 
1 4   GLN n 
1 5   VAL n 
1 6   ASP n 
1 7   PRO n 
1 8   ARG n 
1 9   LEU n 
1 10  ILE n 
1 11  ASP n 
1 12  GLY n 
1 13  LYS n 
1 14  TRP n 
1 15  SER n 
1 16  ARG n 
1 17  ASP n 
1 18  GLN n 
1 19  TYR n 
1 20  HIS n 
1 21  VAL n 
1 22  LEU n 
1 23  PHE n 
1 24  ASP n 
1 25  SER n 
1 26  TYR n 
1 27  ARG n 
1 28  ASP n 
1 29  ASN n 
1 30  ILE n 
1 31  ALA n 
1 32  GLY n 
1 33  LYS n 
1 34  SER n 
1 35  PHE n 
1 36  GLN n 
1 37  ASN n 
1 38  ARG n 
1 39  LEU n 
1 40  CYS n 
1 41  LEU n 
1 42  PRO n 
1 43  MET n 
1 44  PRO n 
1 45  ILE n 
1 46  ASP n 
1 47  VAL n 
1 48  VAL n 
1 49  TYR n 
1 50  THR n 
1 51  TRP n 
1 52  VAL n 
1 53  ASN n 
1 54  GLY n 
1 55  THR n 
1 56  ASP n 
1 57  LEU n 
1 58  GLU n 
1 59  LEU n 
1 60  LEU n 
1 61  LYS n 
1 62  GLU n 
1 63  LEU n 
1 64  THR n 
1 65  GLU n 
1 66  LEU n 
1 67  LYS n 
1 68  ARG n 
1 69  SER n 
1 70  LYS n 
1 71  ARG n 
1 72  ASP n 
1 73  PRO n 
1 74  LEU n 
1 75  ILE n 
1 76  PRO n 
1 77  GLU n 
1 78  CYS n 
1 79  GLN n 
1 80  GLY n 
1 81  LYS n 
1 82  GLN n 
1 83  THR n 
1 84  PRO n 
1 85  GLU n 
1 86  LYS n 
1 87  ASP n 
1 88  LYS n 
1 89  CYS n 
1 90  TYR n 
1 91  ARG n 
1 92  ASP n 
1 93  ASP n 
1 94  ILE n 
1 95  SER n 
1 96  ALA n 
1 97  SER n 
1 98  ARG n 
1 99  PHE n 
1 100 GLU n 
1 101 ASP n 
1 102 ASN n 
1 103 GLU n 
1 104 GLU n 
1 105 LEU n 
1 106 ARG n 
1 107 TYR n 
1 108 SER n 
1 109 LEU n 
1 110 ARG n 
1 111 SER n 
1 112 ILE n 
1 113 GLU n 
1 114 ARG n 
1 115 HIS n 
1 116 ALA n 
1 117 PRO n 
1 118 TRP n 
1 119 VAL n 
1 120 ARG n 
1 121 ASN n 
1 122 ILE n 
1 123 PHE n 
1 124 ILE n 
1 125 VAL n 
1 126 THR n 
1 127 ASN n 
1 128 GLY n 
1 129 GLN n 
1 130 ILE n 
1 131 PRO n 
1 132 SER n 
1 133 TRP n 
1 134 LEU n 
1 135 ASN n 
1 136 LEU n 
1 137 ASP n 
1 138 ASN n 
1 139 PRO n 
1 140 ARG n 
1 141 VAL n 
1 142 THR n 
1 143 ILE n 
1 144 VAL n 
1 145 THR n 
1 146 HIS n 
1 147 GLN n 
1 148 ASP n 
1 149 VAL n 
1 150 PHE n 
1 151 ARG n 
1 152 ASN n 
1 153 LEU n 
1 154 SER n 
1 155 HIS n 
1 156 LEU n 
1 157 PRO n 
1 158 THR n 
1 159 PHE n 
1 160 SER n 
1 161 SER n 
1 162 PRO n 
1 163 ALA n 
1 164 ILE n 
1 165 GLU n 
1 166 SER n 
1 167 HIS n 
1 168 ILE n 
1 169 HIS n 
1 170 ARG n 
1 171 ILE n 
1 172 GLU n 
1 173 GLY n 
1 174 LEU n 
1 175 SER n 
1 176 GLN n 
1 177 LYS n 
1 178 PHE n 
1 179 ILE n 
1 180 TYR n 
1 181 LEU n 
1 182 ASN n 
1 183 ASP n 
1 184 ASP n 
1 185 VAL n 
1 186 MET n 
1 187 PHE n 
1 188 GLY n 
1 189 LYS n 
1 190 ASP n 
1 191 VAL n 
1 192 TRP n 
1 193 PRO n 
1 194 ASP n 
1 195 ASP n 
1 196 PHE n 
1 197 TYR n 
1 198 SER n 
1 199 HIS n 
1 200 SER n 
1 201 LYS n 
1 202 GLY n 
1 203 GLN n 
1 204 LYS n 
1 205 VAL n 
1 206 TYR n 
1 207 LEU n 
1 208 THR n 
1 209 TRP n 
1 210 PRO n 
1 211 VAL n 
1 212 PRO n 
1 213 ASN n 
1 214 GLY n 
1 215 GLY n 
1 216 SER n 
1 217 GLY n 
1 218 GLY n 
1 219 ASP n 
1 220 THR n 
1 221 PHE n 
1 222 ALA n 
1 223 ASP n 
1 224 SER n 
1 225 LEU n 
1 226 ARG n 
1 227 TYR n 
1 228 VAL n 
1 229 ASN n 
1 230 LYS n 
1 231 ILE n 
1 232 LEU n 
1 233 ASN n 
1 234 SER n 
1 235 LYS n 
1 236 PHE n 
1 237 GLY n 
1 238 PHE n 
1 239 THR n 
1 240 SER n 
1 241 ARG n 
1 242 LYS n 
1 243 VAL n 
1 244 PRO n 
1 245 ALA n 
1 246 HIS n 
1 247 MET n 
1 248 PRO n 
1 249 HIS n 
1 250 MET n 
1 251 ILE n 
1 252 ASP n 
1 253 ARG n 
1 254 ILE n 
1 255 VAL n 
1 256 MET n 
1 257 GLN n 
1 258 GLU n 
1 259 LEU n 
1 260 GLN n 
1 261 ASP n 
1 262 MET n 
1 263 PHE n 
1 264 PRO n 
1 265 GLU n 
1 266 GLU n 
1 267 PHE n 
1 268 ASP n 
1 269 LYS n 
1 270 THR n 
1 271 SER n 
1 272 PHE n 
1 273 HIS n 
1 274 LYS n 
1 275 VAL n 
1 276 ARG n 
1 277 HIS n 
1 278 SER n 
1 279 GLU n 
1 280 ASP n 
1 281 MET n 
1 282 GLN n 
1 283 PHE n 
1 284 ALA n 
1 285 PHE n 
1 286 SER n 
1 287 TYR n 
1 288 PHE n 
1 289 TYR n 
1 290 TYR n 
1 291 LEU n 
1 292 MET n 
1 293 SER n 
1 294 ALA n 
1 295 VAL n 
1 296 GLN n 
1 297 PRO n 
1 298 LEU n 
1 299 ASN n 
1 300 ILE n 
1 301 SER n 
1 302 GLN n 
1 303 VAL n 
1 304 PHE n 
1 305 ASP n 
1 306 GLU n 
1 307 VAL n 
1 308 ASP n 
1 309 THR n 
1 310 ASP n 
1 311 GLN n 
1 312 SER n 
1 313 GLY n 
1 314 VAL n 
1 315 LEU n 
1 316 SER n 
1 317 ASP n 
1 318 ARG n 
1 319 GLU n 
1 320 ILE n 
1 321 ARG n 
1 322 THR n 
1 323 LEU n 
1 324 ALA n 
1 325 THR n 
1 326 ARG n 
1 327 ILE n 
1 328 HIS n 
1 329 GLU n 
1 330 LEU n 
1 331 PRO n 
1 332 LEU n 
1 333 SER n 
1 334 LEU n 
1 335 GLN n 
1 336 ASP n 
1 337 LEU n 
1 338 THR n 
1 339 GLY n 
1 340 LEU n 
1 341 GLU n 
1 342 HIS n 
1 343 MET n 
1 344 LEU n 
1 345 ILE n 
1 346 ASN n 
1 347 CYS n 
1 348 SER n 
1 349 LYS n 
1 350 MET n 
1 351 LEU n 
1 352 PRO n 
1 353 ALA n 
1 354 ASP n 
1 355 ILE n 
1 356 THR n 
1 357 GLN n 
1 358 LEU n 
1 359 ASN n 
1 360 ASN n 
1 361 ILE n 
1 362 PRO n 
1 363 PRO n 
1 364 THR n 
1 365 GLN n 
1 366 GLU n 
1 367 SER n 
1 368 TYR n 
1 369 TYR n 
1 370 ASP n 
1 371 PRO n 
1 372 ASN n 
1 373 LEU n 
1 374 PRO n 
1 375 PRO n 
1 376 VAL n 
1 377 THR n 
1 378 LYS n 
1 379 SER n 
1 380 LEU n 
1 381 VAL n 
1 382 THR n 
1 383 ASN n 
1 384 CYS n 
1 385 LYS n 
1 386 PRO n 
1 387 VAL n 
1 388 THR n 
1 389 ASP n 
1 390 LYS n 
1 391 ILE n 
1 392 HIS n 
1 393 LYS n 
1 394 ALA n 
1 395 TYR n 
1 396 LYS n 
1 397 ASP n 
1 398 LYS n 
1 399 ASN n 
1 400 LYS n 
1 401 TYR n 
1 402 ARG n 
1 403 PHE n 
1 404 GLU n 
1 405 ILE n 
1 406 MET n 
1 407 GLY n 
1 408 GLU n 
1 409 GLU n 
1 410 GLU n 
1 411 ILE n 
1 412 ALA n 
1 413 PHE n 
1 414 LYS n 
1 415 MET n 
1 416 ILE n 
1 417 ARG n 
1 418 THR n 
1 419 ASN n 
1 420 VAL n 
1 421 SER n 
1 422 HIS n 
1 423 VAL n 
1 424 VAL n 
1 425 GLY n 
1 426 GLN n 
1 427 LEU n 
1 428 ASP n 
1 429 ASP n 
1 430 ILE n 
1 431 ARG n 
1 432 LYS n 
1 433 ASN n 
1 434 PRO n 
1 435 ARG n 
1 436 LYS n 
1 437 PHE n 
1 438 VAL n 
1 439 CYS n 
1 440 LEU n 
1 441 ASN n 
1 442 ASP n 
1 443 ASN n 
1 444 ILE n 
1 445 ASP n 
1 446 HIS n 
1 447 ASN n 
1 448 HIS n 
1 449 LYS n 
1 450 ASP n 
1 451 ALA n 
1 452 GLN n 
1 453 THR n 
1 454 VAL n 
1 455 LYS n 
1 456 ALA n 
1 457 VAL n 
1 458 LEU n 
1 459 ARG n 
1 460 ASP n 
1 461 PHE n 
1 462 TYR n 
1 463 GLU n 
1 464 SER n 
1 465 MET n 
1 466 PHE n 
1 467 PRO n 
1 468 ILE n 
1 469 PRO n 
1 470 SER n 
1 471 GLN n 
1 472 PHE n 
1 473 GLU n 
1 474 LEU n 
1 475 PRO n 
1 476 ARG n 
1 477 GLU n 
1 478 TYR n 
1 479 ARG n 
1 480 ASN n 
1 481 ARG n 
1 482 PHE n 
1 483 LEU n 
1 484 HIS n 
1 485 MET n 
1 486 HIS n 
1 487 GLU n 
1 488 LEU n 
1 489 GLN n 
1 490 GLU n 
1 491 TRP n 
1 492 ARG n 
1 493 ALA n 
1 494 TYR n 
1 495 ARG n 
1 496 ASP n 
1 497 LYS n 
1 498 LEU n 
1 499 LYS 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   218 ?     ? ?                         ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Insect BA phytoplasma' 1286942 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 219 499 human ? 'GNPTAB, GNPTA, KIAA1208' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Insect BA phytoplasma' 1286942 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'          y ALANINE                                  ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking'          y ARGININE                                 ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking'          y ASPARAGINE                               ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking'          y 'ASPARTIC ACID'                          ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking'          y CYSTEINE                                 ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking'          y GLUTAMINE                                ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID'                          ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'            y GLYCINE                                  ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking'          y HISTIDINE                                ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking'          y ISOLEUCINE                               ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'          y LEUCINE                                  ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'          y LYSINE                                   ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'          y METHIONINE                               ? 'C5 H11 N O2 S'  149.211 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PHE 'L-peptide linking'          y PHENYLALANINE                            ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'          y PROLINE                                  ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking'          y SERINE                                   ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking'          y THREONINE                                ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'          y TRYPTOPHAN                               ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'          y TYROSINE                                 ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'          y VALINE                                   ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ASP 1   -12 ?   ?   ?   A . n 
A 1 2   GLU 2   -11 ?   ?   ?   A . n 
A 1 3   ASP 3   -10 ?   ?   ?   A . n 
A 1 4   GLN 4   -9  ?   ?   ?   A . n 
A 1 5   VAL 5   -8  ?   ?   ?   A . n 
A 1 6   ASP 6   -7  ?   ?   ?   A . n 
A 1 7   PRO 7   -6  ?   ?   ?   A . n 
A 1 8   ARG 8   -5  ?   ?   ?   A . n 
A 1 9   LEU 9   -4  ?   ?   ?   A . n 
A 1 10  ILE 10  -3  ?   ?   ?   A . n 
A 1 11  ASP 11  -2  ?   ?   ?   A . n 
A 1 12  GLY 12  -1  ?   ?   ?   A . n 
A 1 13  LYS 13  0   ?   ?   ?   A . n 
A 1 14  TRP 14  1   ?   ?   ?   A . n 
A 1 15  SER 15  2   ?   ?   ?   A . n 
A 1 16  ARG 16  3   ?   ?   ?   A . n 
A 1 17  ASP 17  4   ?   ?   ?   A . n 
A 1 18  GLN 18  5   ?   ?   ?   A . n 
A 1 19  TYR 19  6   6   TYR TYR A . n 
A 1 20  HIS 20  7   7   HIS HIS A . n 
A 1 21  VAL 21  8   8   VAL VAL A . n 
A 1 22  LEU 22  9   9   LEU LEU A . n 
A 1 23  PHE 23  10  10  PHE PHE A . n 
A 1 24  ASP 24  11  11  ASP ASP A . n 
A 1 25  SER 25  12  12  SER SER A . n 
A 1 26  TYR 26  13  13  TYR TYR A . n 
A 1 27  ARG 27  14  14  ARG ARG A . n 
A 1 28  ASP 28  15  15  ASP ASP A . n 
A 1 29  ASN 29  16  16  ASN ASN A . n 
A 1 30  ILE 30  17  17  ILE ILE A . n 
A 1 31  ALA 31  18  18  ALA ALA A . n 
A 1 32  GLY 32  19  19  GLY GLY A . n 
A 1 33  LYS 33  20  20  LYS LYS A . n 
A 1 34  SER 34  21  21  SER SER A . n 
A 1 35  PHE 35  22  22  PHE PHE A . n 
A 1 36  GLN 36  23  23  GLN GLN A . n 
A 1 37  ASN 37  24  24  ASN ASN A . n 
A 1 38  ARG 38  25  25  ARG ARG A . n 
A 1 39  LEU 39  26  26  LEU LEU A . n 
A 1 40  CYS 40  27  27  CYS CYS A . n 
A 1 41  LEU 41  28  28  LEU LEU A . n 
A 1 42  PRO 42  29  29  PRO PRO A . n 
A 1 43  MET 43  30  30  MET MET A . n 
A 1 44  PRO 44  31  31  PRO PRO A . n 
A 1 45  ILE 45  32  32  ILE ILE A . n 
A 1 46  ASP 46  33  33  ASP ASP A . n 
A 1 47  VAL 47  34  34  VAL VAL A . n 
A 1 48  VAL 48  35  35  VAL VAL A . n 
A 1 49  TYR 49  36  36  TYR TYR A . n 
A 1 50  THR 50  37  37  THR THR A . n 
A 1 51  TRP 51  38  38  TRP TRP A . n 
A 1 52  VAL 52  39  39  VAL VAL A . n 
A 1 53  ASN 53  40  40  ASN ASN A . n 
A 1 54  GLY 54  41  41  GLY GLY A . n 
A 1 55  THR 55  42  42  THR THR A . n 
A 1 56  ASP 56  43  43  ASP ASP A . n 
A 1 57  LEU 57  44  44  LEU LEU A . n 
A 1 58  GLU 58  45  45  GLU GLU A . n 
A 1 59  LEU 59  46  46  LEU LEU A . n 
A 1 60  LEU 60  47  47  LEU LEU A . n 
A 1 61  LYS 61  48  48  LYS LYS A . n 
A 1 62  GLU 62  49  49  GLU GLU A . n 
A 1 63  LEU 63  50  50  LEU LEU A . n 
A 1 64  THR 64  51  51  THR THR A . n 
A 1 65  GLU 65  52  52  GLU GLU A . n 
A 1 66  LEU 66  53  53  LEU LEU A . n 
A 1 67  LYS 67  54  54  LYS LYS A . n 
A 1 68  ARG 68  55  55  ARG ARG A . n 
A 1 69  SER 69  56  56  SER SER A . n 
A 1 70  LYS 70  57  ?   ?   ?   A . n 
A 1 71  ARG 71  58  ?   ?   ?   A . n 
A 1 72  ASP 72  59  ?   ?   ?   A . n 
A 1 73  PRO 73  60  ?   ?   ?   A . n 
A 1 74  LEU 74  61  ?   ?   ?   A . n 
A 1 75  ILE 75  62  ?   ?   ?   A . n 
A 1 76  PRO 76  63  ?   ?   ?   A . n 
A 1 77  GLU 77  64  ?   ?   ?   A . n 
A 1 78  CYS 78  65  ?   ?   ?   A . n 
A 1 79  GLN 79  66  ?   ?   ?   A . n 
A 1 80  GLY 80  67  ?   ?   ?   A . n 
A 1 81  LYS 81  68  ?   ?   ?   A . n 
A 1 82  GLN 82  69  ?   ?   ?   A . n 
A 1 83  THR 83  70  ?   ?   ?   A . n 
A 1 84  PRO 84  71  ?   ?   ?   A . n 
A 1 85  GLU 85  72  ?   ?   ?   A . n 
A 1 86  LYS 86  73  ?   ?   ?   A . n 
A 1 87  ASP 87  74  ?   ?   ?   A . n 
A 1 88  LYS 88  75  ?   ?   ?   A . n 
A 1 89  CYS 89  76  ?   ?   ?   A . n 
A 1 90  TYR 90  77  ?   ?   ?   A . n 
A 1 91  ARG 91  78  ?   ?   ?   A . n 
A 1 92  ASP 92  79  ?   ?   ?   A . n 
A 1 93  ASP 93  80  ?   ?   ?   A . n 
A 1 94  ILE 94  81  ?   ?   ?   A . n 
A 1 95  SER 95  82  ?   ?   ?   A . n 
A 1 96  ALA 96  83  ?   ?   ?   A . n 
A 1 97  SER 97  84  ?   ?   ?   A . n 
A 1 98  ARG 98  85  ?   ?   ?   A . n 
A 1 99  PHE 99  86  ?   ?   ?   A . n 
A 1 100 GLU 100 87  ?   ?   ?   A . n 
A 1 101 ASP 101 88  ?   ?   ?   A . n 
A 1 102 ASN 102 89  89  ASN ASN A . n 
A 1 103 GLU 103 90  90  GLU GLU A . n 
A 1 104 GLU 104 91  91  GLU GLU A . n 
A 1 105 LEU 105 92  92  LEU LEU A . n 
A 1 106 ARG 106 93  93  ARG ARG A . n 
A 1 107 TYR 107 94  94  TYR TYR A . n 
A 1 108 SER 108 95  95  SER SER A . n 
A 1 109 LEU 109 96  96  LEU LEU A . n 
A 1 110 ARG 110 97  97  ARG ARG A . n 
A 1 111 SER 111 98  98  SER SER A . n 
A 1 112 ILE 112 99  99  ILE ILE A . n 
A 1 113 GLU 113 100 100 GLU GLU A . n 
A 1 114 ARG 114 101 101 ARG ARG A . n 
A 1 115 HIS 115 102 102 HIS HIS A . n 
A 1 116 ALA 116 103 103 ALA ALA A . n 
A 1 117 PRO 117 104 104 PRO PRO A . n 
A 1 118 TRP 118 105 105 TRP TRP A . n 
A 1 119 VAL 119 106 106 VAL VAL A . n 
A 1 120 ARG 120 107 107 ARG ARG A . n 
A 1 121 ASN 121 108 108 ASN ASN A . n 
A 1 122 ILE 122 109 109 ILE ILE A . n 
A 1 123 PHE 123 110 110 PHE PHE A . n 
A 1 124 ILE 124 111 111 ILE ILE A . n 
A 1 125 VAL 125 112 112 VAL VAL A . n 
A 1 126 THR 126 113 113 THR THR A . n 
A 1 127 ASN 127 114 114 ASN ASN A . n 
A 1 128 GLY 128 115 115 GLY GLY A . n 
A 1 129 GLN 129 116 116 GLN GLN A . n 
A 1 130 ILE 130 117 117 ILE ILE A . n 
A 1 131 PRO 131 118 118 PRO PRO A . n 
A 1 132 SER 132 119 119 SER SER A . n 
A 1 133 TRP 133 120 120 TRP TRP A . n 
A 1 134 LEU 134 121 121 LEU LEU A . n 
A 1 135 ASN 135 122 122 ASN ASN A . n 
A 1 136 LEU 136 123 123 LEU LEU A . n 
A 1 137 ASP 137 124 124 ASP ASP A . n 
A 1 138 ASN 138 125 125 ASN ASN A . n 
A 1 139 PRO 139 126 126 PRO PRO A . n 
A 1 140 ARG 140 127 127 ARG ARG A . n 
A 1 141 VAL 141 128 128 VAL VAL A . n 
A 1 142 THR 142 129 129 THR THR A . n 
A 1 143 ILE 143 130 130 ILE ILE A . n 
A 1 144 VAL 144 131 131 VAL VAL A . n 
A 1 145 THR 145 132 132 THR THR A . n 
A 1 146 HIS 146 133 133 HIS HIS A . n 
A 1 147 GLN 147 134 134 GLN GLN A . n 
A 1 148 ASP 148 135 135 ASP ASP A . n 
A 1 149 VAL 149 136 136 VAL VAL A . n 
A 1 150 PHE 150 137 137 PHE PHE A . n 
A 1 151 ARG 151 138 138 ARG ARG A . n 
A 1 152 ASN 152 139 139 ASN ASN A . n 
A 1 153 LEU 153 140 140 LEU LEU A . n 
A 1 154 SER 154 141 141 SER SER A . n 
A 1 155 HIS 155 142 142 HIS HIS A . n 
A 1 156 LEU 156 143 143 LEU LEU A . n 
A 1 157 PRO 157 144 144 PRO PRO A . n 
A 1 158 THR 158 145 145 THR THR A . n 
A 1 159 PHE 159 146 146 PHE PHE A . n 
A 1 160 SER 160 147 147 SER SER A . n 
A 1 161 SER 161 148 148 SER SER A . n 
A 1 162 PRO 162 149 149 PRO PRO A . n 
A 1 163 ALA 163 150 150 ALA ALA A . n 
A 1 164 ILE 164 151 151 ILE ILE A . n 
A 1 165 GLU 165 152 152 GLU GLU A . n 
A 1 166 SER 166 153 153 SER SER A . n 
A 1 167 HIS 167 154 154 HIS HIS A . n 
A 1 168 ILE 168 155 155 ILE ILE A . n 
A 1 169 HIS 169 156 156 HIS HIS A . n 
A 1 170 ARG 170 157 157 ARG ARG A . n 
A 1 171 ILE 171 158 158 ILE ILE A . n 
A 1 172 GLU 172 159 159 GLU GLU A . n 
A 1 173 GLY 173 160 160 GLY GLY A . n 
A 1 174 LEU 174 161 161 LEU LEU A . n 
A 1 175 SER 175 162 162 SER SER A . n 
A 1 176 GLN 176 163 163 GLN GLN A . n 
A 1 177 LYS 177 164 164 LYS LYS A . n 
A 1 178 PHE 178 165 165 PHE PHE A . n 
A 1 179 ILE 179 166 166 ILE ILE A . n 
A 1 180 TYR 180 167 167 TYR TYR A . n 
A 1 181 LEU 181 168 168 LEU LEU A . n 
A 1 182 ASN 182 169 169 ASN ASN A . n 
A 1 183 ASP 183 170 170 ASP ASP A . n 
A 1 184 ASP 184 171 171 ASP ASP A . n 
A 1 185 VAL 185 172 172 VAL VAL A . n 
A 1 186 MET 186 173 173 MET MET A . n 
A 1 187 PHE 187 174 174 PHE PHE A . n 
A 1 188 GLY 188 175 175 GLY GLY A . n 
A 1 189 LYS 189 176 176 LYS LYS A . n 
A 1 190 ASP 190 177 177 ASP ASP A . n 
A 1 191 VAL 191 178 178 VAL VAL A . n 
A 1 192 TRP 192 179 179 TRP TRP A . n 
A 1 193 PRO 193 180 180 PRO PRO A . n 
A 1 194 ASP 194 181 181 ASP ASP A . n 
A 1 195 ASP 195 182 182 ASP ASP A . n 
A 1 196 PHE 196 183 183 PHE PHE A . n 
A 1 197 TYR 197 184 184 TYR TYR A . n 
A 1 198 SER 198 185 185 SER SER A . n 
A 1 199 HIS 199 186 186 HIS HIS A . n 
A 1 200 SER 200 187 187 SER SER A . n 
A 1 201 LYS 201 188 188 LYS LYS A . n 
A 1 202 GLY 202 189 189 GLY GLY A . n 
A 1 203 GLN 203 190 190 GLN GLN A . n 
A 1 204 LYS 204 191 191 LYS LYS A . n 
A 1 205 VAL 205 192 192 VAL VAL A . n 
A 1 206 TYR 206 193 193 TYR TYR A . n 
A 1 207 LEU 207 194 194 LEU LEU A . n 
A 1 208 THR 208 195 195 THR THR A . n 
A 1 209 TRP 209 196 196 TRP TRP A . n 
A 1 210 PRO 210 197 197 PRO PRO A . n 
A 1 211 VAL 211 198 198 VAL VAL A . n 
A 1 212 PRO 212 199 199 PRO PRO A . n 
A 1 213 ASN 213 200 200 ASN ASN A . n 
A 1 214 GLY 214 201 201 GLY GLY A . n 
A 1 215 GLY 215 202 202 GLY GLY A . n 
A 1 216 SER 216 203 203 SER SER A . n 
A 1 217 GLY 217 204 204 GLY GLY A . n 
A 1 218 GLY 218 205 205 GLY GLY A . n 
A 1 219 ASP 219 206 206 ASP ASP A . n 
A 1 220 THR 220 207 207 THR THR A . n 
A 1 221 PHE 221 208 208 PHE PHE A . n 
A 1 222 ALA 222 209 209 ALA ALA A . n 
A 1 223 ASP 223 210 210 ASP ASP A . n 
A 1 224 SER 224 211 211 SER SER A . n 
A 1 225 LEU 225 212 212 LEU LEU A . n 
A 1 226 ARG 226 213 213 ARG ARG A . n 
A 1 227 TYR 227 214 214 TYR TYR A . n 
A 1 228 VAL 228 215 215 VAL VAL A . n 
A 1 229 ASN 229 216 216 ASN ASN A . n 
A 1 230 LYS 230 217 217 LYS LYS A . n 
A 1 231 ILE 231 218 218 ILE ILE A . n 
A 1 232 LEU 232 219 219 LEU LEU A . n 
A 1 233 ASN 233 220 220 ASN ASN A . n 
A 1 234 SER 234 221 221 SER SER A . n 
A 1 235 LYS 235 222 222 LYS LYS A . n 
A 1 236 PHE 236 223 223 PHE PHE A . n 
A 1 237 GLY 237 224 224 GLY GLY A . n 
A 1 238 PHE 238 225 225 PHE PHE A . n 
A 1 239 THR 239 226 226 THR THR A . n 
A 1 240 SER 240 227 227 SER SER A . n 
A 1 241 ARG 241 228 228 ARG ARG A . n 
A 1 242 LYS 242 229 229 LYS LYS A . n 
A 1 243 VAL 243 230 230 VAL VAL A . n 
A 1 244 PRO 244 231 231 PRO PRO A . n 
A 1 245 ALA 245 232 232 ALA ALA A . n 
A 1 246 HIS 246 233 233 HIS HIS A . n 
A 1 247 MET 247 234 234 MET MET A . n 
A 1 248 PRO 248 235 235 PRO PRO A . n 
A 1 249 HIS 249 236 236 HIS HIS A . n 
A 1 250 MET 250 237 237 MET MET A . n 
A 1 251 ILE 251 238 238 ILE ILE A . n 
A 1 252 ASP 252 239 239 ASP ASP A . n 
A 1 253 ARG 253 240 240 ARG ARG A . n 
A 1 254 ILE 254 241 241 ILE ILE A . n 
A 1 255 VAL 255 242 242 VAL VAL A . n 
A 1 256 MET 256 243 243 MET MET A . n 
A 1 257 GLN 257 244 244 GLN GLN A . n 
A 1 258 GLU 258 245 245 GLU GLU A . n 
A 1 259 LEU 259 246 246 LEU LEU A . n 
A 1 260 GLN 260 247 247 GLN GLN A . n 
A 1 261 ASP 261 248 248 ASP ASP A . n 
A 1 262 MET 262 249 249 MET MET A . n 
A 1 263 PHE 263 250 250 PHE PHE A . n 
A 1 264 PRO 264 251 251 PRO PRO A . n 
A 1 265 GLU 265 252 252 GLU GLU A . n 
A 1 266 GLU 266 253 253 GLU GLU A . n 
A 1 267 PHE 267 254 254 PHE PHE A . n 
A 1 268 ASP 268 255 255 ASP ASP A . n 
A 1 269 LYS 269 256 256 LYS LYS A . n 
A 1 270 THR 270 257 257 THR THR A . n 
A 1 271 SER 271 258 258 SER SER A . n 
A 1 272 PHE 272 259 259 PHE PHE A . n 
A 1 273 HIS 273 260 260 HIS HIS A . n 
A 1 274 LYS 274 261 261 LYS LYS A . n 
A 1 275 VAL 275 262 262 VAL VAL A . n 
A 1 276 ARG 276 263 263 ARG ARG A . n 
A 1 277 HIS 277 264 264 HIS HIS A . n 
A 1 278 SER 278 265 265 SER SER A . n 
A 1 279 GLU 279 266 266 GLU GLU A . n 
A 1 280 ASP 280 267 267 ASP ASP A . n 
A 1 281 MET 281 268 268 MET MET A . n 
A 1 282 GLN 282 269 269 GLN GLN A . n 
A 1 283 PHE 283 270 270 PHE PHE A . n 
A 1 284 ALA 284 271 271 ALA ALA A . n 
A 1 285 PHE 285 272 272 PHE PHE A . n 
A 1 286 SER 286 273 273 SER SER A . n 
A 1 287 TYR 287 274 274 TYR TYR A . n 
A 1 288 PHE 288 275 275 PHE PHE A . n 
A 1 289 TYR 289 276 276 TYR TYR A . n 
A 1 290 TYR 290 277 277 TYR TYR A . n 
A 1 291 LEU 291 278 278 LEU LEU A . n 
A 1 292 MET 292 279 279 MET MET A . n 
A 1 293 SER 293 280 280 SER SER A . n 
A 1 294 ALA 294 281 281 ALA ALA A . n 
A 1 295 VAL 295 282 282 VAL VAL A . n 
A 1 296 GLN 296 283 283 GLN GLN A . n 
A 1 297 PRO 297 284 284 PRO PRO A . n 
A 1 298 LEU 298 285 285 LEU LEU A . n 
A 1 299 ASN 299 286 286 ASN ASN A . n 
A 1 300 ILE 300 287 287 ILE ILE A . n 
A 1 301 SER 301 288 288 SER SER A . n 
A 1 302 GLN 302 289 289 GLN GLN A . n 
A 1 303 VAL 303 290 290 VAL VAL A . n 
A 1 304 PHE 304 291 291 PHE PHE A . n 
A 1 305 ASP 305 292 292 ASP ASP A . n 
A 1 306 GLU 306 293 293 GLU GLU A . n 
A 1 307 VAL 307 294 294 VAL VAL A . n 
A 1 308 ASP 308 295 295 ASP ASP A . n 
A 1 309 THR 309 296 296 THR THR A . n 
A 1 310 ASP 310 297 297 ASP ASP A . n 
A 1 311 GLN 311 298 298 GLN GLN A . n 
A 1 312 SER 312 299 299 SER SER A . n 
A 1 313 GLY 313 300 300 GLY GLY A . n 
A 1 314 VAL 314 301 301 VAL VAL A . n 
A 1 315 LEU 315 302 302 LEU LEU A . n 
A 1 316 SER 316 303 303 SER SER A . n 
A 1 317 ASP 317 304 304 ASP ASP A . n 
A 1 318 ARG 318 305 305 ARG ARG A . n 
A 1 319 GLU 319 306 306 GLU GLU A . n 
A 1 320 ILE 320 307 307 ILE ILE A . n 
A 1 321 ARG 321 308 308 ARG ARG A . n 
A 1 322 THR 322 309 309 THR THR A . n 
A 1 323 LEU 323 310 310 LEU LEU A . n 
A 1 324 ALA 324 311 311 ALA ALA A . n 
A 1 325 THR 325 312 312 THR THR A . n 
A 1 326 ARG 326 313 313 ARG ARG A . n 
A 1 327 ILE 327 314 314 ILE ILE A . n 
A 1 328 HIS 328 315 315 HIS HIS A . n 
A 1 329 GLU 329 316 316 GLU GLU A . n 
A 1 330 LEU 330 317 317 LEU LEU A . n 
A 1 331 PRO 331 318 318 PRO PRO A . n 
A 1 332 LEU 332 319 319 LEU LEU A . n 
A 1 333 SER 333 320 320 SER SER A . n 
A 1 334 LEU 334 321 321 LEU LEU A . n 
A 1 335 GLN 335 322 322 GLN GLN A . n 
A 1 336 ASP 336 323 323 ASP ASP A . n 
A 1 337 LEU 337 324 324 LEU LEU A . n 
A 1 338 THR 338 325 325 THR THR A . n 
A 1 339 GLY 339 326 326 GLY GLY A . n 
A 1 340 LEU 340 327 327 LEU LEU A . n 
A 1 341 GLU 341 328 328 GLU GLU A . n 
A 1 342 HIS 342 329 329 HIS HIS A . n 
A 1 343 MET 343 330 330 MET MET A . n 
A 1 344 LEU 344 331 331 LEU LEU A . n 
A 1 345 ILE 345 332 332 ILE ILE A . n 
A 1 346 ASN 346 333 333 ASN ASN A . n 
A 1 347 CYS 347 334 334 CYS CYS A . n 
A 1 348 SER 348 335 335 SER SER A . n 
A 1 349 LYS 349 336 336 LYS LYS A . n 
A 1 350 MET 350 337 337 MET MET A . n 
A 1 351 LEU 351 338 338 LEU LEU A . n 
A 1 352 PRO 352 339 339 PRO PRO A . n 
A 1 353 ALA 353 340 340 ALA ALA A . n 
A 1 354 ASP 354 341 ?   ?   ?   A . n 
A 1 355 ILE 355 342 ?   ?   ?   A . n 
A 1 356 THR 356 343 ?   ?   ?   A . n 
A 1 357 GLN 357 344 ?   ?   ?   A . n 
A 1 358 LEU 358 345 ?   ?   ?   A . n 
A 1 359 ASN 359 346 ?   ?   ?   A . n 
A 1 360 ASN 360 347 ?   ?   ?   A . n 
A 1 361 ILE 361 348 ?   ?   ?   A . n 
A 1 362 PRO 362 349 ?   ?   ?   A . n 
A 1 363 PRO 363 350 ?   ?   ?   A . n 
A 1 364 THR 364 351 351 THR THR A . n 
A 1 365 GLN 365 352 352 GLN GLN A . n 
A 1 366 GLU 366 353 353 GLU GLU A . n 
A 1 367 SER 367 354 354 SER SER A . n 
A 1 368 TYR 368 355 355 TYR TYR A . n 
A 1 369 TYR 369 356 356 TYR TYR A . n 
A 1 370 ASP 370 357 357 ASP ASP A . n 
A 1 371 PRO 371 358 358 PRO PRO A . n 
A 1 372 ASN 372 359 359 ASN ASN A . n 
A 1 373 LEU 373 360 360 LEU LEU A . n 
A 1 374 PRO 374 361 361 PRO PRO A . n 
A 1 375 PRO 375 362 362 PRO PRO A . n 
A 1 376 VAL 376 363 363 VAL VAL A . n 
A 1 377 THR 377 364 364 THR THR A . n 
A 1 378 LYS 378 365 365 LYS LYS A . n 
A 1 379 SER 379 366 366 SER SER A . n 
A 1 380 LEU 380 367 367 LEU LEU A . n 
A 1 381 VAL 381 368 368 VAL VAL A . n 
A 1 382 THR 382 369 369 THR THR A . n 
A 1 383 ASN 383 370 370 ASN ASN A . n 
A 1 384 CYS 384 371 371 CYS CYS A . n 
A 1 385 LYS 385 372 372 LYS LYS A . n 
A 1 386 PRO 386 373 373 PRO PRO A . n 
A 1 387 VAL 387 374 374 VAL VAL A . n 
A 1 388 THR 388 375 375 THR THR A . n 
A 1 389 ASP 389 376 376 ASP ASP A . n 
A 1 390 LYS 390 377 377 LYS LYS A . n 
A 1 391 ILE 391 378 378 ILE ILE A . n 
A 1 392 HIS 392 379 379 HIS HIS A . n 
A 1 393 LYS 393 380 380 LYS LYS A . n 
A 1 394 ALA 394 381 381 ALA ALA A . n 
A 1 395 TYR 395 382 382 TYR TYR A . n 
A 1 396 LYS 396 383 383 LYS LYS A . n 
A 1 397 ASP 397 384 384 ASP ASP A . n 
A 1 398 LYS 398 385 385 LYS LYS A . n 
A 1 399 ASN 399 386 386 ASN ASN A . n 
A 1 400 LYS 400 387 387 LYS LYS A . n 
A 1 401 TYR 401 388 388 TYR TYR A . n 
A 1 402 ARG 402 389 389 ARG ARG A . n 
A 1 403 PHE 403 390 390 PHE PHE A . n 
A 1 404 GLU 404 391 391 GLU GLU A . n 
A 1 405 ILE 405 392 392 ILE ILE A . n 
A 1 406 MET 406 393 393 MET MET A . n 
A 1 407 GLY 407 394 394 GLY GLY A . n 
A 1 408 GLU 408 395 395 GLU GLU A . n 
A 1 409 GLU 409 396 396 GLU GLU A . n 
A 1 410 GLU 410 397 397 GLU GLU A . n 
A 1 411 ILE 411 398 398 ILE ILE A . n 
A 1 412 ALA 412 399 399 ALA ALA A . n 
A 1 413 PHE 413 400 400 PHE PHE A . n 
A 1 414 LYS 414 401 401 LYS LYS A . n 
A 1 415 MET 415 402 402 MET MET A . n 
A 1 416 ILE 416 403 403 ILE ILE A . n 
A 1 417 ARG 417 404 404 ARG ARG A . n 
A 1 418 THR 418 405 405 THR THR A . n 
A 1 419 ASN 419 406 406 ASN ASN A . n 
A 1 420 VAL 420 407 407 VAL VAL A . n 
A 1 421 SER 421 408 408 SER SER A . n 
A 1 422 HIS 422 409 409 HIS HIS A . n 
A 1 423 VAL 423 410 410 VAL VAL A . n 
A 1 424 VAL 424 411 411 VAL VAL A . n 
A 1 425 GLY 425 412 412 GLY GLY A . n 
A 1 426 GLN 426 413 413 GLN GLN A . n 
A 1 427 LEU 427 414 414 LEU LEU A . n 
A 1 428 ASP 428 415 415 ASP ASP A . n 
A 1 429 ASP 429 416 416 ASP ASP A . n 
A 1 430 ILE 430 417 417 ILE ILE A . n 
A 1 431 ARG 431 418 418 ARG ARG A . n 
A 1 432 LYS 432 419 419 LYS LYS A . n 
A 1 433 ASN 433 420 420 ASN ASN A . n 
A 1 434 PRO 434 421 421 PRO PRO A . n 
A 1 435 ARG 435 422 422 ARG ARG A . n 
A 1 436 LYS 436 423 423 LYS LYS A . n 
A 1 437 PHE 437 424 424 PHE PHE A . n 
A 1 438 VAL 438 425 425 VAL VAL A . n 
A 1 439 CYS 439 426 426 CYS CYS A . n 
A 1 440 LEU 440 427 427 LEU LEU A . n 
A 1 441 ASN 441 428 428 ASN ASN A . n 
A 1 442 ASP 442 429 429 ASP ASP A . n 
A 1 443 ASN 443 430 430 ASN ASN A . n 
A 1 444 ILE 444 431 431 ILE ILE A . n 
A 1 445 ASP 445 432 432 ASP ASP A . n 
A 1 446 HIS 446 433 433 HIS HIS A . n 
A 1 447 ASN 447 434 434 ASN ASN A . n 
A 1 448 HIS 448 435 435 HIS HIS A . n 
A 1 449 LYS 449 436 436 LYS LYS A . n 
A 1 450 ASP 450 437 437 ASP ASP A . n 
A 1 451 ALA 451 438 438 ALA ALA A . n 
A 1 452 GLN 452 439 439 GLN GLN A . n 
A 1 453 THR 453 440 440 THR THR A . n 
A 1 454 VAL 454 441 441 VAL VAL A . n 
A 1 455 LYS 455 442 442 LYS LYS A . n 
A 1 456 ALA 456 443 443 ALA ALA A . n 
A 1 457 VAL 457 444 444 VAL VAL A . n 
A 1 458 LEU 458 445 445 LEU LEU A . n 
A 1 459 ARG 459 446 446 ARG ARG A . n 
A 1 460 ASP 460 447 447 ASP ASP A . n 
A 1 461 PHE 461 448 448 PHE PHE A . n 
A 1 462 TYR 462 449 449 TYR TYR A . n 
A 1 463 GLU 463 450 450 GLU GLU A . n 
A 1 464 SER 464 451 451 SER SER A . n 
A 1 465 MET 465 452 452 MET MET A . n 
A 1 466 PHE 466 453 453 PHE PHE A . n 
A 1 467 PRO 467 454 454 PRO PRO A . n 
A 1 468 ILE 468 455 455 ILE ILE A . n 
A 1 469 PRO 469 456 456 PRO PRO A . n 
A 1 470 SER 470 457 457 SER SER A . n 
A 1 471 GLN 471 458 458 GLN GLN A . n 
A 1 472 PHE 472 459 459 PHE PHE A . n 
A 1 473 GLU 473 460 460 GLU GLU A . n 
A 1 474 LEU 474 461 461 LEU LEU A . n 
A 1 475 PRO 475 462 462 PRO PRO A . n 
A 1 476 ARG 476 463 463 ARG ARG A . n 
A 1 477 GLU 477 464 ?   ?   ?   A . n 
A 1 478 TYR 478 465 ?   ?   ?   A . n 
A 1 479 ARG 479 466 ?   ?   ?   A . n 
A 1 480 ASN 480 467 ?   ?   ?   A . n 
A 1 481 ARG 481 468 ?   ?   ?   A . n 
A 1 482 PHE 482 469 ?   ?   ?   A . n 
A 1 483 LEU 483 470 ?   ?   ?   A . n 
A 1 484 HIS 484 471 ?   ?   ?   A . n 
A 1 485 MET 485 472 ?   ?   ?   A . n 
A 1 486 HIS 486 473 ?   ?   ?   A . n 
A 1 487 GLU 487 474 ?   ?   ?   A . n 
A 1 488 LEU 488 475 ?   ?   ?   A . n 
A 1 489 GLN 489 476 ?   ?   ?   A . n 
A 1 490 GLU 490 477 ?   ?   ?   A . n 
A 1 491 TRP 491 478 ?   ?   ?   A . n 
A 1 492 ARG 492 479 ?   ?   ?   A . n 
A 1 493 ALA 493 480 ?   ?   ?   A . n 
A 1 494 TYR 494 481 ?   ?   ?   A . n 
A 1 495 ARG 495 482 ?   ?   ?   A . n 
A 1 496 ASP 496 483 ?   ?   ?   A . n 
A 1 497 LYS 497 484 ?   ?   ?   A . n 
A 1 498 LEU 498 485 ?   ?   ?   A . n 
A 1 499 LYS 499 486 ?   ?   ?   A . n 
B 1 1   ASP 1   -12 ?   ?   ?   B . n 
B 1 2   GLU 2   -11 ?   ?   ?   B . n 
B 1 3   ASP 3   -10 ?   ?   ?   B . n 
B 1 4   GLN 4   -9  ?   ?   ?   B . n 
B 1 5   VAL 5   -8  ?   ?   ?   B . n 
B 1 6   ASP 6   -7  ?   ?   ?   B . n 
B 1 7   PRO 7   -6  ?   ?   ?   B . n 
B 1 8   ARG 8   -5  ?   ?   ?   B . n 
B 1 9   LEU 9   -4  ?   ?   ?   B . n 
B 1 10  ILE 10  -3  ?   ?   ?   B . n 
B 1 11  ASP 11  -2  ?   ?   ?   B . n 
B 1 12  GLY 12  -1  ?   ?   ?   B . n 
B 1 13  LYS 13  0   ?   ?   ?   B . n 
B 1 14  TRP 14  1   ?   ?   ?   B . n 
B 1 15  SER 15  2   ?   ?   ?   B . n 
B 1 16  ARG 16  3   ?   ?   ?   B . n 
B 1 17  ASP 17  4   ?   ?   ?   B . n 
B 1 18  GLN 18  5   ?   ?   ?   B . n 
B 1 19  TYR 19  6   6   TYR TYR B . n 
B 1 20  HIS 20  7   7   HIS HIS B . n 
B 1 21  VAL 21  8   8   VAL VAL B . n 
B 1 22  LEU 22  9   9   LEU LEU B . n 
B 1 23  PHE 23  10  10  PHE PHE B . n 
B 1 24  ASP 24  11  11  ASP ASP B . n 
B 1 25  SER 25  12  12  SER SER B . n 
B 1 26  TYR 26  13  13  TYR TYR B . n 
B 1 27  ARG 27  14  14  ARG ARG B . n 
B 1 28  ASP 28  15  15  ASP ASP B . n 
B 1 29  ASN 29  16  16  ASN ASN B . n 
B 1 30  ILE 30  17  17  ILE ILE B . n 
B 1 31  ALA 31  18  18  ALA ALA B . n 
B 1 32  GLY 32  19  19  GLY GLY B . n 
B 1 33  LYS 33  20  20  LYS LYS B . n 
B 1 34  SER 34  21  21  SER SER B . n 
B 1 35  PHE 35  22  22  PHE PHE B . n 
B 1 36  GLN 36  23  23  GLN GLN B . n 
B 1 37  ASN 37  24  24  ASN ASN B . n 
B 1 38  ARG 38  25  25  ARG ARG B . n 
B 1 39  LEU 39  26  26  LEU LEU B . n 
B 1 40  CYS 40  27  27  CYS CYS B . n 
B 1 41  LEU 41  28  28  LEU LEU B . n 
B 1 42  PRO 42  29  29  PRO PRO B . n 
B 1 43  MET 43  30  30  MET MET B . n 
B 1 44  PRO 44  31  31  PRO PRO B . n 
B 1 45  ILE 45  32  32  ILE ILE B . n 
B 1 46  ASP 46  33  33  ASP ASP B . n 
B 1 47  VAL 47  34  34  VAL VAL B . n 
B 1 48  VAL 48  35  35  VAL VAL B . n 
B 1 49  TYR 49  36  36  TYR TYR B . n 
B 1 50  THR 50  37  37  THR THR B . n 
B 1 51  TRP 51  38  38  TRP TRP B . n 
B 1 52  VAL 52  39  39  VAL VAL B . n 
B 1 53  ASN 53  40  40  ASN ASN B . n 
B 1 54  GLY 54  41  41  GLY GLY B . n 
B 1 55  THR 55  42  42  THR THR B . n 
B 1 56  ASP 56  43  43  ASP ASP B . n 
B 1 57  LEU 57  44  44  LEU LEU B . n 
B 1 58  GLU 58  45  45  GLU GLU B . n 
B 1 59  LEU 59  46  46  LEU LEU B . n 
B 1 60  LEU 60  47  47  LEU LEU B . n 
B 1 61  LYS 61  48  48  LYS LYS B . n 
B 1 62  GLU 62  49  49  GLU GLU B . n 
B 1 63  LEU 63  50  50  LEU LEU B . n 
B 1 64  THR 64  51  51  THR THR B . n 
B 1 65  GLU 65  52  52  GLU GLU B . n 
B 1 66  LEU 66  53  53  LEU LEU B . n 
B 1 67  LYS 67  54  54  LYS LYS B . n 
B 1 68  ARG 68  55  55  ARG ARG B . n 
B 1 69  SER 69  56  56  SER SER B . n 
B 1 70  LYS 70  57  ?   ?   ?   B . n 
B 1 71  ARG 71  58  ?   ?   ?   B . n 
B 1 72  ASP 72  59  ?   ?   ?   B . n 
B 1 73  PRO 73  60  ?   ?   ?   B . n 
B 1 74  LEU 74  61  ?   ?   ?   B . n 
B 1 75  ILE 75  62  ?   ?   ?   B . n 
B 1 76  PRO 76  63  ?   ?   ?   B . n 
B 1 77  GLU 77  64  ?   ?   ?   B . n 
B 1 78  CYS 78  65  ?   ?   ?   B . n 
B 1 79  GLN 79  66  ?   ?   ?   B . n 
B 1 80  GLY 80  67  ?   ?   ?   B . n 
B 1 81  LYS 81  68  ?   ?   ?   B . n 
B 1 82  GLN 82  69  ?   ?   ?   B . n 
B 1 83  THR 83  70  ?   ?   ?   B . n 
B 1 84  PRO 84  71  ?   ?   ?   B . n 
B 1 85  GLU 85  72  ?   ?   ?   B . n 
B 1 86  LYS 86  73  ?   ?   ?   B . n 
B 1 87  ASP 87  74  ?   ?   ?   B . n 
B 1 88  LYS 88  75  ?   ?   ?   B . n 
B 1 89  CYS 89  76  ?   ?   ?   B . n 
B 1 90  TYR 90  77  ?   ?   ?   B . n 
B 1 91  ARG 91  78  ?   ?   ?   B . n 
B 1 92  ASP 92  79  ?   ?   ?   B . n 
B 1 93  ASP 93  80  ?   ?   ?   B . n 
B 1 94  ILE 94  81  ?   ?   ?   B . n 
B 1 95  SER 95  82  ?   ?   ?   B . n 
B 1 96  ALA 96  83  ?   ?   ?   B . n 
B 1 97  SER 97  84  ?   ?   ?   B . n 
B 1 98  ARG 98  85  ?   ?   ?   B . n 
B 1 99  PHE 99  86  ?   ?   ?   B . n 
B 1 100 GLU 100 87  ?   ?   ?   B . n 
B 1 101 ASP 101 88  88  ASP ASP B . n 
B 1 102 ASN 102 89  89  ASN ASN B . n 
B 1 103 GLU 103 90  90  GLU GLU B . n 
B 1 104 GLU 104 91  91  GLU GLU B . n 
B 1 105 LEU 105 92  92  LEU LEU B . n 
B 1 106 ARG 106 93  93  ARG ARG B . n 
B 1 107 TYR 107 94  94  TYR TYR B . n 
B 1 108 SER 108 95  95  SER SER B . n 
B 1 109 LEU 109 96  96  LEU LEU B . n 
B 1 110 ARG 110 97  97  ARG ARG B . n 
B 1 111 SER 111 98  98  SER SER B . n 
B 1 112 ILE 112 99  99  ILE ILE B . n 
B 1 113 GLU 113 100 100 GLU GLU B . n 
B 1 114 ARG 114 101 101 ARG ARG B . n 
B 1 115 HIS 115 102 102 HIS HIS B . n 
B 1 116 ALA 116 103 103 ALA ALA B . n 
B 1 117 PRO 117 104 104 PRO PRO B . n 
B 1 118 TRP 118 105 105 TRP TRP B . n 
B 1 119 VAL 119 106 106 VAL VAL B . n 
B 1 120 ARG 120 107 107 ARG ARG B . n 
B 1 121 ASN 121 108 108 ASN ASN B . n 
B 1 122 ILE 122 109 109 ILE ILE B . n 
B 1 123 PHE 123 110 110 PHE PHE B . n 
B 1 124 ILE 124 111 111 ILE ILE B . n 
B 1 125 VAL 125 112 112 VAL VAL B . n 
B 1 126 THR 126 113 113 THR THR B . n 
B 1 127 ASN 127 114 114 ASN ASN B . n 
B 1 128 GLY 128 115 115 GLY GLY B . n 
B 1 129 GLN 129 116 116 GLN GLN B . n 
B 1 130 ILE 130 117 117 ILE ILE B . n 
B 1 131 PRO 131 118 118 PRO PRO B . n 
B 1 132 SER 132 119 119 SER SER B . n 
B 1 133 TRP 133 120 120 TRP TRP B . n 
B 1 134 LEU 134 121 121 LEU LEU B . n 
B 1 135 ASN 135 122 122 ASN ASN B . n 
B 1 136 LEU 136 123 123 LEU LEU B . n 
B 1 137 ASP 137 124 124 ASP ASP B . n 
B 1 138 ASN 138 125 125 ASN ASN B . n 
B 1 139 PRO 139 126 126 PRO PRO B . n 
B 1 140 ARG 140 127 127 ARG ARG B . n 
B 1 141 VAL 141 128 128 VAL VAL B . n 
B 1 142 THR 142 129 129 THR THR B . n 
B 1 143 ILE 143 130 130 ILE ILE B . n 
B 1 144 VAL 144 131 131 VAL VAL B . n 
B 1 145 THR 145 132 132 THR THR B . n 
B 1 146 HIS 146 133 133 HIS HIS B . n 
B 1 147 GLN 147 134 134 GLN GLN B . n 
B 1 148 ASP 148 135 135 ASP ASP B . n 
B 1 149 VAL 149 136 136 VAL VAL B . n 
B 1 150 PHE 150 137 137 PHE PHE B . n 
B 1 151 ARG 151 138 138 ARG ARG B . n 
B 1 152 ASN 152 139 139 ASN ASN B . n 
B 1 153 LEU 153 140 140 LEU LEU B . n 
B 1 154 SER 154 141 141 SER SER B . n 
B 1 155 HIS 155 142 142 HIS HIS B . n 
B 1 156 LEU 156 143 143 LEU LEU B . n 
B 1 157 PRO 157 144 144 PRO PRO B . n 
B 1 158 THR 158 145 145 THR THR B . n 
B 1 159 PHE 159 146 146 PHE PHE B . n 
B 1 160 SER 160 147 147 SER SER B . n 
B 1 161 SER 161 148 148 SER SER B . n 
B 1 162 PRO 162 149 149 PRO PRO B . n 
B 1 163 ALA 163 150 150 ALA ALA B . n 
B 1 164 ILE 164 151 151 ILE ILE B . n 
B 1 165 GLU 165 152 152 GLU GLU B . n 
B 1 166 SER 166 153 153 SER SER B . n 
B 1 167 HIS 167 154 154 HIS HIS B . n 
B 1 168 ILE 168 155 155 ILE ILE B . n 
B 1 169 HIS 169 156 156 HIS HIS B . n 
B 1 170 ARG 170 157 157 ARG ARG B . n 
B 1 171 ILE 171 158 158 ILE ILE B . n 
B 1 172 GLU 172 159 159 GLU GLU B . n 
B 1 173 GLY 173 160 160 GLY GLY B . n 
B 1 174 LEU 174 161 161 LEU LEU B . n 
B 1 175 SER 175 162 162 SER SER B . n 
B 1 176 GLN 176 163 163 GLN GLN B . n 
B 1 177 LYS 177 164 164 LYS LYS B . n 
B 1 178 PHE 178 165 165 PHE PHE B . n 
B 1 179 ILE 179 166 166 ILE ILE B . n 
B 1 180 TYR 180 167 167 TYR TYR B . n 
B 1 181 LEU 181 168 168 LEU LEU B . n 
B 1 182 ASN 182 169 169 ASN ASN B . n 
B 1 183 ASP 183 170 170 ASP ASP B . n 
B 1 184 ASP 184 171 171 ASP ASP B . n 
B 1 185 VAL 185 172 172 VAL VAL B . n 
B 1 186 MET 186 173 173 MET MET B . n 
B 1 187 PHE 187 174 174 PHE PHE B . n 
B 1 188 GLY 188 175 175 GLY GLY B . n 
B 1 189 LYS 189 176 176 LYS LYS B . n 
B 1 190 ASP 190 177 177 ASP ASP B . n 
B 1 191 VAL 191 178 178 VAL VAL B . n 
B 1 192 TRP 192 179 179 TRP TRP B . n 
B 1 193 PRO 193 180 180 PRO PRO B . n 
B 1 194 ASP 194 181 181 ASP ASP B . n 
B 1 195 ASP 195 182 182 ASP ASP B . n 
B 1 196 PHE 196 183 183 PHE PHE B . n 
B 1 197 TYR 197 184 184 TYR TYR B . n 
B 1 198 SER 198 185 185 SER SER B . n 
B 1 199 HIS 199 186 186 HIS HIS B . n 
B 1 200 SER 200 187 187 SER SER B . n 
B 1 201 LYS 201 188 188 LYS LYS B . n 
B 1 202 GLY 202 189 189 GLY GLY B . n 
B 1 203 GLN 203 190 190 GLN GLN B . n 
B 1 204 LYS 204 191 191 LYS LYS B . n 
B 1 205 VAL 205 192 192 VAL VAL B . n 
B 1 206 TYR 206 193 193 TYR TYR B . n 
B 1 207 LEU 207 194 194 LEU LEU B . n 
B 1 208 THR 208 195 195 THR THR B . n 
B 1 209 TRP 209 196 196 TRP TRP B . n 
B 1 210 PRO 210 197 197 PRO PRO B . n 
B 1 211 VAL 211 198 198 VAL VAL B . n 
B 1 212 PRO 212 199 199 PRO PRO B . n 
B 1 213 ASN 213 200 200 ASN ASN B . n 
B 1 214 GLY 214 201 201 GLY GLY B . n 
B 1 215 GLY 215 202 202 GLY GLY B . n 
B 1 216 SER 216 203 203 SER SER B . n 
B 1 217 GLY 217 204 204 GLY GLY B . n 
B 1 218 GLY 218 205 205 GLY GLY B . n 
B 1 219 ASP 219 206 206 ASP ASP B . n 
B 1 220 THR 220 207 207 THR THR B . n 
B 1 221 PHE 221 208 208 PHE PHE B . n 
B 1 222 ALA 222 209 209 ALA ALA B . n 
B 1 223 ASP 223 210 210 ASP ASP B . n 
B 1 224 SER 224 211 211 SER SER B . n 
B 1 225 LEU 225 212 212 LEU LEU B . n 
B 1 226 ARG 226 213 213 ARG ARG B . n 
B 1 227 TYR 227 214 214 TYR TYR B . n 
B 1 228 VAL 228 215 215 VAL VAL B . n 
B 1 229 ASN 229 216 216 ASN ASN B . n 
B 1 230 LYS 230 217 217 LYS LYS B . n 
B 1 231 ILE 231 218 218 ILE ILE B . n 
B 1 232 LEU 232 219 219 LEU LEU B . n 
B 1 233 ASN 233 220 220 ASN ASN B . n 
B 1 234 SER 234 221 221 SER SER B . n 
B 1 235 LYS 235 222 222 LYS LYS B . n 
B 1 236 PHE 236 223 223 PHE PHE B . n 
B 1 237 GLY 237 224 224 GLY GLY B . n 
B 1 238 PHE 238 225 225 PHE PHE B . n 
B 1 239 THR 239 226 226 THR THR B . n 
B 1 240 SER 240 227 227 SER SER B . n 
B 1 241 ARG 241 228 228 ARG ARG B . n 
B 1 242 LYS 242 229 229 LYS LYS B . n 
B 1 243 VAL 243 230 230 VAL VAL B . n 
B 1 244 PRO 244 231 231 PRO PRO B . n 
B 1 245 ALA 245 232 232 ALA ALA B . n 
B 1 246 HIS 246 233 233 HIS HIS B . n 
B 1 247 MET 247 234 234 MET MET B . n 
B 1 248 PRO 248 235 235 PRO PRO B . n 
B 1 249 HIS 249 236 236 HIS HIS B . n 
B 1 250 MET 250 237 237 MET MET B . n 
B 1 251 ILE 251 238 238 ILE ILE B . n 
B 1 252 ASP 252 239 239 ASP ASP B . n 
B 1 253 ARG 253 240 240 ARG ARG B . n 
B 1 254 ILE 254 241 241 ILE ILE B . n 
B 1 255 VAL 255 242 242 VAL VAL B . n 
B 1 256 MET 256 243 243 MET MET B . n 
B 1 257 GLN 257 244 244 GLN GLN B . n 
B 1 258 GLU 258 245 245 GLU GLU B . n 
B 1 259 LEU 259 246 246 LEU LEU B . n 
B 1 260 GLN 260 247 247 GLN GLN B . n 
B 1 261 ASP 261 248 248 ASP ASP B . n 
B 1 262 MET 262 249 249 MET MET B . n 
B 1 263 PHE 263 250 250 PHE PHE B . n 
B 1 264 PRO 264 251 251 PRO PRO B . n 
B 1 265 GLU 265 252 252 GLU GLU B . n 
B 1 266 GLU 266 253 253 GLU GLU B . n 
B 1 267 PHE 267 254 254 PHE PHE B . n 
B 1 268 ASP 268 255 255 ASP ASP B . n 
B 1 269 LYS 269 256 256 LYS LYS B . n 
B 1 270 THR 270 257 257 THR THR B . n 
B 1 271 SER 271 258 258 SER SER B . n 
B 1 272 PHE 272 259 259 PHE PHE B . n 
B 1 273 HIS 273 260 260 HIS HIS B . n 
B 1 274 LYS 274 261 261 LYS LYS B . n 
B 1 275 VAL 275 262 262 VAL VAL B . n 
B 1 276 ARG 276 263 263 ARG ARG B . n 
B 1 277 HIS 277 264 264 HIS HIS B . n 
B 1 278 SER 278 265 265 SER SER B . n 
B 1 279 GLU 279 266 266 GLU GLU B . n 
B 1 280 ASP 280 267 267 ASP ASP B . n 
B 1 281 MET 281 268 268 MET MET B . n 
B 1 282 GLN 282 269 269 GLN GLN B . n 
B 1 283 PHE 283 270 270 PHE PHE B . n 
B 1 284 ALA 284 271 271 ALA ALA B . n 
B 1 285 PHE 285 272 272 PHE PHE B . n 
B 1 286 SER 286 273 273 SER SER B . n 
B 1 287 TYR 287 274 274 TYR TYR B . n 
B 1 288 PHE 288 275 275 PHE PHE B . n 
B 1 289 TYR 289 276 276 TYR TYR B . n 
B 1 290 TYR 290 277 277 TYR TYR B . n 
B 1 291 LEU 291 278 278 LEU LEU B . n 
B 1 292 MET 292 279 279 MET MET B . n 
B 1 293 SER 293 280 280 SER SER B . n 
B 1 294 ALA 294 281 281 ALA ALA B . n 
B 1 295 VAL 295 282 282 VAL VAL B . n 
B 1 296 GLN 296 283 283 GLN GLN B . n 
B 1 297 PRO 297 284 284 PRO PRO B . n 
B 1 298 LEU 298 285 285 LEU LEU B . n 
B 1 299 ASN 299 286 286 ASN ASN B . n 
B 1 300 ILE 300 287 287 ILE ILE B . n 
B 1 301 SER 301 288 288 SER SER B . n 
B 1 302 GLN 302 289 289 GLN GLN B . n 
B 1 303 VAL 303 290 290 VAL VAL B . n 
B 1 304 PHE 304 291 291 PHE PHE B . n 
B 1 305 ASP 305 292 292 ASP ASP B . n 
B 1 306 GLU 306 293 293 GLU GLU B . n 
B 1 307 VAL 307 294 294 VAL VAL B . n 
B 1 308 ASP 308 295 295 ASP ASP B . n 
B 1 309 THR 309 296 296 THR THR B . n 
B 1 310 ASP 310 297 297 ASP ASP B . n 
B 1 311 GLN 311 298 298 GLN GLN B . n 
B 1 312 SER 312 299 299 SER SER B . n 
B 1 313 GLY 313 300 300 GLY GLY B . n 
B 1 314 VAL 314 301 301 VAL VAL B . n 
B 1 315 LEU 315 302 302 LEU LEU B . n 
B 1 316 SER 316 303 303 SER SER B . n 
B 1 317 ASP 317 304 304 ASP ASP B . n 
B 1 318 ARG 318 305 305 ARG ARG B . n 
B 1 319 GLU 319 306 306 GLU GLU B . n 
B 1 320 ILE 320 307 307 ILE ILE B . n 
B 1 321 ARG 321 308 308 ARG ARG B . n 
B 1 322 THR 322 309 309 THR THR B . n 
B 1 323 LEU 323 310 310 LEU LEU B . n 
B 1 324 ALA 324 311 311 ALA ALA B . n 
B 1 325 THR 325 312 312 THR THR B . n 
B 1 326 ARG 326 313 313 ARG ARG B . n 
B 1 327 ILE 327 314 314 ILE ILE B . n 
B 1 328 HIS 328 315 315 HIS HIS B . n 
B 1 329 GLU 329 316 316 GLU GLU B . n 
B 1 330 LEU 330 317 317 LEU LEU B . n 
B 1 331 PRO 331 318 318 PRO PRO B . n 
B 1 332 LEU 332 319 319 LEU LEU B . n 
B 1 333 SER 333 320 320 SER SER B . n 
B 1 334 LEU 334 321 321 LEU LEU B . n 
B 1 335 GLN 335 322 322 GLN GLN B . n 
B 1 336 ASP 336 323 323 ASP ASP B . n 
B 1 337 LEU 337 324 324 LEU LEU B . n 
B 1 338 THR 338 325 325 THR THR B . n 
B 1 339 GLY 339 326 326 GLY GLY B . n 
B 1 340 LEU 340 327 327 LEU LEU B . n 
B 1 341 GLU 341 328 328 GLU GLU B . n 
B 1 342 HIS 342 329 329 HIS HIS B . n 
B 1 343 MET 343 330 330 MET MET B . n 
B 1 344 LEU 344 331 331 LEU LEU B . n 
B 1 345 ILE 345 332 332 ILE ILE B . n 
B 1 346 ASN 346 333 333 ASN ASN B . n 
B 1 347 CYS 347 334 334 CYS CYS B . n 
B 1 348 SER 348 335 335 SER SER B . n 
B 1 349 LYS 349 336 336 LYS LYS B . n 
B 1 350 MET 350 337 337 MET MET B . n 
B 1 351 LEU 351 338 338 LEU LEU B . n 
B 1 352 PRO 352 339 ?   ?   ?   B . n 
B 1 353 ALA 353 340 ?   ?   ?   B . n 
B 1 354 ASP 354 341 ?   ?   ?   B . n 
B 1 355 ILE 355 342 ?   ?   ?   B . n 
B 1 356 THR 356 343 ?   ?   ?   B . n 
B 1 357 GLN 357 344 ?   ?   ?   B . n 
B 1 358 LEU 358 345 ?   ?   ?   B . n 
B 1 359 ASN 359 346 ?   ?   ?   B . n 
B 1 360 ASN 360 347 ?   ?   ?   B . n 
B 1 361 ILE 361 348 ?   ?   ?   B . n 
B 1 362 PRO 362 349 ?   ?   ?   B . n 
B 1 363 PRO 363 350 350 PRO PRO B . n 
B 1 364 THR 364 351 351 THR THR B . n 
B 1 365 GLN 365 352 352 GLN GLN B . n 
B 1 366 GLU 366 353 353 GLU GLU B . n 
B 1 367 SER 367 354 354 SER SER B . n 
B 1 368 TYR 368 355 355 TYR TYR B . n 
B 1 369 TYR 369 356 356 TYR TYR B . n 
B 1 370 ASP 370 357 357 ASP ASP B . n 
B 1 371 PRO 371 358 358 PRO PRO B . n 
B 1 372 ASN 372 359 359 ASN ASN B . n 
B 1 373 LEU 373 360 360 LEU LEU B . n 
B 1 374 PRO 374 361 361 PRO PRO B . n 
B 1 375 PRO 375 362 362 PRO PRO B . n 
B 1 376 VAL 376 363 363 VAL VAL B . n 
B 1 377 THR 377 364 364 THR THR B . n 
B 1 378 LYS 378 365 365 LYS LYS B . n 
B 1 379 SER 379 366 366 SER SER B . n 
B 1 380 LEU 380 367 367 LEU LEU B . n 
B 1 381 VAL 381 368 368 VAL VAL B . n 
B 1 382 THR 382 369 369 THR THR B . n 
B 1 383 ASN 383 370 370 ASN ASN B . n 
B 1 384 CYS 384 371 371 CYS CYS B . n 
B 1 385 LYS 385 372 372 LYS LYS B . n 
B 1 386 PRO 386 373 373 PRO PRO B . n 
B 1 387 VAL 387 374 374 VAL VAL B . n 
B 1 388 THR 388 375 375 THR THR B . n 
B 1 389 ASP 389 376 376 ASP ASP B . n 
B 1 390 LYS 390 377 377 LYS LYS B . n 
B 1 391 ILE 391 378 378 ILE ILE B . n 
B 1 392 HIS 392 379 379 HIS HIS B . n 
B 1 393 LYS 393 380 380 LYS LYS B . n 
B 1 394 ALA 394 381 381 ALA ALA B . n 
B 1 395 TYR 395 382 382 TYR TYR B . n 
B 1 396 LYS 396 383 383 LYS LYS B . n 
B 1 397 ASP 397 384 384 ASP ASP B . n 
B 1 398 LYS 398 385 385 LYS LYS B . n 
B 1 399 ASN 399 386 386 ASN ASN B . n 
B 1 400 LYS 400 387 387 LYS LYS B . n 
B 1 401 TYR 401 388 388 TYR TYR B . n 
B 1 402 ARG 402 389 389 ARG ARG B . n 
B 1 403 PHE 403 390 390 PHE PHE B . n 
B 1 404 GLU 404 391 391 GLU GLU B . n 
B 1 405 ILE 405 392 392 ILE ILE B . n 
B 1 406 MET 406 393 393 MET MET B . n 
B 1 407 GLY 407 394 394 GLY GLY B . n 
B 1 408 GLU 408 395 395 GLU GLU B . n 
B 1 409 GLU 409 396 396 GLU GLU B . n 
B 1 410 GLU 410 397 397 GLU GLU B . n 
B 1 411 ILE 411 398 398 ILE ILE B . n 
B 1 412 ALA 412 399 399 ALA ALA B . n 
B 1 413 PHE 413 400 400 PHE PHE B . n 
B 1 414 LYS 414 401 401 LYS LYS B . n 
B 1 415 MET 415 402 402 MET MET B . n 
B 1 416 ILE 416 403 403 ILE ILE B . n 
B 1 417 ARG 417 404 404 ARG ARG B . n 
B 1 418 THR 418 405 405 THR THR B . n 
B 1 419 ASN 419 406 406 ASN ASN B . n 
B 1 420 VAL 420 407 407 VAL VAL B . n 
B 1 421 SER 421 408 408 SER SER B . n 
B 1 422 HIS 422 409 409 HIS HIS B . n 
B 1 423 VAL 423 410 410 VAL VAL B . n 
B 1 424 VAL 424 411 411 VAL VAL B . n 
B 1 425 GLY 425 412 412 GLY GLY B . n 
B 1 426 GLN 426 413 413 GLN GLN B . n 
B 1 427 LEU 427 414 414 LEU LEU B . n 
B 1 428 ASP 428 415 415 ASP ASP B . n 
B 1 429 ASP 429 416 416 ASP ASP B . n 
B 1 430 ILE 430 417 417 ILE ILE B . n 
B 1 431 ARG 431 418 418 ARG ARG B . n 
B 1 432 LYS 432 419 419 LYS LYS B . n 
B 1 433 ASN 433 420 420 ASN ASN B . n 
B 1 434 PRO 434 421 421 PRO PRO B . n 
B 1 435 ARG 435 422 422 ARG ARG B . n 
B 1 436 LYS 436 423 423 LYS LYS B . n 
B 1 437 PHE 437 424 424 PHE PHE B . n 
B 1 438 VAL 438 425 425 VAL VAL B . n 
B 1 439 CYS 439 426 426 CYS CYS B . n 
B 1 440 LEU 440 427 427 LEU LEU B . n 
B 1 441 ASN 441 428 428 ASN ASN B . n 
B 1 442 ASP 442 429 429 ASP ASP B . n 
B 1 443 ASN 443 430 430 ASN ASN B . n 
B 1 444 ILE 444 431 431 ILE ILE B . n 
B 1 445 ASP 445 432 432 ASP ASP B . n 
B 1 446 HIS 446 433 433 HIS HIS B . n 
B 1 447 ASN 447 434 434 ASN ASN B . n 
B 1 448 HIS 448 435 435 HIS HIS B . n 
B 1 449 LYS 449 436 436 LYS LYS B . n 
B 1 450 ASP 450 437 437 ASP ASP B . n 
B 1 451 ALA 451 438 438 ALA ALA B . n 
B 1 452 GLN 452 439 439 GLN GLN B . n 
B 1 453 THR 453 440 440 THR THR B . n 
B 1 454 VAL 454 441 441 VAL VAL B . n 
B 1 455 LYS 455 442 442 LYS LYS B . n 
B 1 456 ALA 456 443 443 ALA ALA B . n 
B 1 457 VAL 457 444 444 VAL VAL B . n 
B 1 458 LEU 458 445 445 LEU LEU B . n 
B 1 459 ARG 459 446 446 ARG ARG B . n 
B 1 460 ASP 460 447 447 ASP ASP B . n 
B 1 461 PHE 461 448 448 PHE PHE B . n 
B 1 462 TYR 462 449 449 TYR TYR B . n 
B 1 463 GLU 463 450 450 GLU GLU B . n 
B 1 464 SER 464 451 451 SER SER B . n 
B 1 465 MET 465 452 452 MET MET B . n 
B 1 466 PHE 466 453 453 PHE PHE B . n 
B 1 467 PRO 467 454 454 PRO PRO B . n 
B 1 468 ILE 468 455 455 ILE ILE B . n 
B 1 469 PRO 469 456 456 PRO PRO B . n 
B 1 470 SER 470 457 457 SER SER B . n 
B 1 471 GLN 471 458 458 GLN GLN B . n 
B 1 472 PHE 472 459 459 PHE PHE B . n 
B 1 473 GLU 473 460 460 GLU GLU B . n 
B 1 474 LEU 474 461 461 LEU LEU B . n 
B 1 475 PRO 475 462 462 PRO PRO B . n 
B 1 476 ARG 476 463 463 ARG ARG B . n 
B 1 477 GLU 477 464 464 GLU GLU B . n 
B 1 478 TYR 478 465 465 TYR TYR B . n 
B 1 479 ARG 479 466 466 ARG ARG B . n 
B 1 480 ASN 480 467 ?   ?   ?   B . n 
B 1 481 ARG 481 468 ?   ?   ?   B . n 
B 1 482 PHE 482 469 ?   ?   ?   B . n 
B 1 483 LEU 483 470 ?   ?   ?   B . n 
B 1 484 HIS 484 471 ?   ?   ?   B . n 
B 1 485 MET 485 472 ?   ?   ?   B . n 
B 1 486 HIS 486 473 ?   ?   ?   B . n 
B 1 487 GLU 487 474 ?   ?   ?   B . n 
B 1 488 LEU 488 475 ?   ?   ?   B . n 
B 1 489 GLN 489 476 ?   ?   ?   B . n 
B 1 490 GLU 490 477 ?   ?   ?   B . n 
B 1 491 TRP 491 478 ?   ?   ?   B . n 
B 1 492 ARG 492 479 ?   ?   ?   B . n 
B 1 493 ALA 493 480 ?   ?   ?   B . n 
B 1 494 TYR 494 481 ?   ?   ?   B . n 
B 1 495 ARG 495 482 ?   ?   ?   B . n 
B 1 496 ASP 496 483 ?   ?   ?   B . n 
B 1 497 LYS 497 484 ?   ?   ?   B . n 
B 1 498 LEU 498 485 ?   ?   ?   B . n 
B 1 499 LYS 499 486 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        NAG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   NAG 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 NAG 1 501 3  NAG NAG A . 
D 2 NAG 1 502 4  NAG NAG A . 
E 2 NAG 1 501 11 NAG NAG B . 
F 2 NAG 1 502 12 NAG NAG B . 
# 
_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                     9BGG 
_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                         9BGG 
_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                   9BGG 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9BGG 
_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  ? 7102 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.524  ? 9619 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 14.272 ? 2728 ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.042  ? 1051 ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.004  ? 1240 ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9BGG 
_struct.title                        'Structure of a hyperactive S1S3 truncation of the human GlcNAc-1-phosphotransferase' 
_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        9BGG 
_struct_keywords.text            
'GlcNAc-1-phosphotransferase, lysosomal hydrolases, mannose 6-phosphate trafficking pathway, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 2 ? 
F N N 2 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 PDB 9BGG        9BGG   ? 1 ? 1   
2 UNP GNPTA_HUMAN Q3T906 ? 1 
;DTFADSLRYVNKILNSKFGFTSRKVPAHMPHMIDRIVMQELQDMFPEEFDKTSFHKVRHSEDMQFAFSYFYYLMSAVQPL
NISQVFDEVDTDQSGVLSDREIRTLATRIHELPLSLQDLTGLEHMLINCSKMLPADITQLNNIPPTQESYYDPNLPPVTK
SLVTNCKPVTDKIHKAYKDKNKYRFEIMGEEEIAFKMIRTNVSHVVGQLDDIRKNPRKFVCLNDNIDHNHKDAQTVKAVL
RDFYESMFPIPSQFELPREYRNRFLHMHELQEWRAYRDKLK
;
929 
# 
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 9BGG A 1   ? 218 ? 9BGG   -12 ? 205  ? -12 205 
2 2 9BGG A 219 ? 499 ? Q3T906 929 ? 1209 ? 206 486 
3 1 9BGG B 1   ? 218 ? 9BGG   -12 ? 205  ? -12 205 
4 2 9BGG B 219 ? 499 ? Q3T906 929 ? 1209 ? 206 486 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 20  ? ASP A 28  ? HIS A 7   ASP A 15  1 ? 9  
HELX_P HELX_P2  AA2 PHE A 35  ? CYS A 40  ? PHE A 22  CYS A 27  1 ? 6  
HELX_P HELX_P3  AA3 ASP A 56  ? SER A 69  ? ASP A 43  SER A 56  1 ? 14 
HELX_P HELX_P4  AA4 GLU A 103 ? ALA A 116 ? GLU A 90  ALA A 103 1 ? 14 
HELX_P HELX_P5  AA5 HIS A 146 ? PHE A 150 ? HIS A 133 PHE A 137 1 ? 5  
HELX_P HELX_P6  AA6 ASN A 152 ? LEU A 156 ? ASN A 139 LEU A 143 5 ? 5  
HELX_P HELX_P7  AA7 SER A 160 ? HIS A 167 ? SER A 147 HIS A 154 1 ? 8  
HELX_P HELX_P8  AA8 ILE A 168 ? ILE A 171 ? ILE A 155 ILE A 158 5 ? 4  
HELX_P HELX_P9  AA9 TRP A 192 ? ASP A 195 ? TRP A 179 ASP A 182 5 ? 4  
HELX_P HELX_P10 AB1 VAL A 211 ? GLY A 215 ? VAL A 198 GLY A 202 1 ? 5  
HELX_P HELX_P11 AB2 ASP A 219 ? PHE A 236 ? ASP A 206 PHE A 223 1 ? 18 
HELX_P HELX_P12 AB3 ARG A 253 ? PHE A 263 ? ARG A 240 PHE A 250 1 ? 11 
HELX_P HELX_P13 AB4 PHE A 263 ? HIS A 273 ? PHE A 250 HIS A 260 1 ? 11 
HELX_P HELX_P14 AB5 GLN A 282 ? SER A 293 ? GLN A 269 SER A 280 1 ? 12 
HELX_P HELX_P15 AB6 ASN A 299 ? ASP A 308 ? ASN A 286 ASP A 295 1 ? 10 
HELX_P HELX_P16 AB7 SER A 316 ? HIS A 328 ? SER A 303 HIS A 315 1 ? 13 
HELX_P HELX_P17 AB8 SER A 333 ? LEU A 351 ? SER A 320 LEU A 338 1 ? 19 
HELX_P HELX_P18 AB9 THR A 377 ? THR A 382 ? THR A 364 THR A 369 1 ? 6  
HELX_P HELX_P19 AC1 CYS A 384 ? TYR A 395 ? CYS A 371 TYR A 382 1 ? 12 
HELX_P HELX_P20 AC2 ASN A 419 ? ASN A 433 ? ASN A 406 ASN A 420 1 ? 15 
HELX_P HELX_P21 AC3 ASP A 450 ? PHE A 466 ? ASP A 437 PHE A 453 1 ? 17 
HELX_P HELX_P22 AC4 HIS B 20  ? ASP B 28  ? HIS B 7   ASP B 15  1 ? 9  
HELX_P HELX_P23 AC5 PHE B 35  ? CYS B 40  ? PHE B 22  CYS B 27  1 ? 6  
HELX_P HELX_P24 AC6 THR B 55  ? SER B 69  ? THR B 42  SER B 56  1 ? 15 
HELX_P HELX_P25 AC7 GLU B 103 ? ALA B 116 ? GLU B 90  ALA B 103 1 ? 14 
HELX_P HELX_P26 AC8 THR B 145 ? VAL B 149 ? THR B 132 VAL B 136 5 ? 5  
HELX_P HELX_P27 AC9 ASN B 152 ? LEU B 156 ? ASN B 139 LEU B 143 5 ? 5  
HELX_P HELX_P28 AD1 SER B 160 ? SER B 166 ? SER B 147 SER B 153 1 ? 7  
HELX_P HELX_P29 AD2 HIS B 167 ? ILE B 171 ? HIS B 154 ILE B 158 5 ? 5  
HELX_P HELX_P30 AD3 TRP B 192 ? ASP B 195 ? TRP B 179 ASP B 182 5 ? 4  
HELX_P HELX_P31 AD4 PHE B 221 ? GLY B 237 ? PHE B 208 GLY B 224 1 ? 17 
HELX_P HELX_P32 AD5 ARG B 253 ? PHE B 263 ? ARG B 240 PHE B 250 1 ? 11 
HELX_P HELX_P33 AD6 PHE B 263 ? HIS B 273 ? PHE B 250 HIS B 260 1 ? 11 
HELX_P HELX_P34 AD7 GLN B 282 ? ALA B 294 ? GLN B 269 ALA B 281 1 ? 13 
HELX_P HELX_P35 AD8 ASN B 299 ? ASP B 308 ? ASN B 286 ASP B 295 1 ? 10 
HELX_P HELX_P36 AD9 SER B 316 ? HIS B 328 ? SER B 303 HIS B 315 1 ? 13 
HELX_P HELX_P37 AE1 SER B 333 ? MET B 350 ? SER B 320 MET B 337 1 ? 18 
HELX_P HELX_P38 AE2 THR B 377 ? ASN B 383 ? THR B 364 ASN B 370 1 ? 7  
HELX_P HELX_P39 AE3 CYS B 384 ? TYR B 395 ? CYS B 371 TYR B 382 1 ? 12 
HELX_P HELX_P40 AE4 ASN B 419 ? ASN B 433 ? ASN B 406 ASN B 420 1 ? 15 
HELX_P HELX_P41 AE5 ASP B 450 ? PHE B 466 ? ASP B 437 PHE B 453 1 ? 17 
# 
_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 40  SG  ? ? ? 1_555 B CYS 40 SG ? ? A CYS 27  B CYS 27  1_555 ? ? ? ? ? ? ? 2.031 ? ?               
covale1 covale one ? A ASN 299 ND2 ? ? ? 1_555 C NAG .  C1 ? ? A ASN 286 A NAG 501 1_555 ? ? ? ? ? ? ? 1.439 ? N-Glycosylation 
covale2 covale one ? A ASN 419 ND2 ? ? ? 1_555 D NAG .  C1 ? ? A ASN 406 A NAG 502 1_555 ? ? ? ? ? ? ? 1.444 ? N-Glycosylation 
covale3 covale one ? B ASN 299 ND2 ? ? ? 1_555 E NAG .  C1 ? ? B ASN 286 B NAG 501 1_555 ? ? ? ? ? ? ? 1.445 ? N-Glycosylation 
covale4 covale one ? B ASN 419 ND2 ? ? ? 1_555 F NAG .  C1 ? ? B ASN 406 B NAG 502 1_555 ? ? ? ? ? ? ? 1.445 ? N-Glycosylation 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 NAG C .  ? ASN A 299 ? NAG A 501 ? 1_555 ASN A 286 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2 NAG D .  ? ASN A 419 ? NAG A 502 ? 1_555 ASN A 406 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3 NAG E .  ? ASN B 299 ? NAG B 501 ? 1_555 ASN B 286 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4 NAG F .  ? ASN B 419 ? NAG B 502 ? 1_555 ASN B 406 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5 CYS A 40 ? CYS B 40  ? CYS A 27  ? 1_555 CYS B 27  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 MET 43  A . ? MET 30  A PRO 44  A ? PRO 31  A 1 -1.03 
2 LEU 330 A . ? LEU 317 A PRO 331 A ? PRO 318 A 1 -6.07 
3 MET 43  B . ? MET 30  B PRO 44  B ? PRO 31  B 1 -0.99 
4 LEU 330 B . ? LEU 317 B PRO 331 B ? PRO 318 B 1 -2.18 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
AA4 ? 3 ? 
AA5 ? 2 ? 
AA6 ? 5 ? 
AA7 ? 3 ? 
AA8 ? 3 ? 
AA9 ? 3 ? 
# 
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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? parallel      
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? parallel      
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? 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 141 ? THR A 145 ? VAL A 128 THR A 132 
AA1 2 ILE A 122 ? THR A 126 ? ILE A 109 THR A 113 
AA1 3 ASP A 46  ? THR A 50  ? ASP A 33  THR A 37  
AA1 4 LYS A 177 ? TYR A 180 ? LYS A 164 TYR A 167 
AA1 5 HIS A 249 ? ASP A 252 ? HIS A 236 ASP A 239 
AA2 1 VAL A 185 ? MET A 186 ? VAL A 172 MET A 173 
AA2 2 PHE A 437 ? CYS A 439 ? PHE A 424 CYS A 426 
AA2 3 ILE A 411 ? PHE A 413 ? ILE A 398 PHE A 400 
AA3 1 TYR A 197 ? SER A 198 ? TYR A 184 SER A 185 
AA3 2 GLY A 202 ? PRO A 210 ? GLY A 189 PRO A 197 
AA3 3 LYS A 242 ? PRO A 244 ? LYS A 229 PRO A 231 
AA4 1 TYR A 197 ? SER A 198 ? TYR A 184 SER A 185 
AA4 2 GLY A 202 ? PRO A 210 ? GLY A 189 PRO A 197 
AA4 3 PHE A 403 ? MET A 406 ? PHE A 390 MET A 393 
AA5 1 VAL A 295 ? GLN A 296 ? VAL A 282 GLN A 283 
AA5 2 LYS A 398 ? ASN A 399 ? LYS A 385 ASN A 386 
AA6 1 VAL B 141 ? VAL B 144 ? VAL B 128 VAL B 131 
AA6 2 ILE B 122 ? VAL B 125 ? ILE B 109 VAL B 112 
AA6 3 ASP B 46  ? THR B 50  ? ASP B 33  THR B 37  
AA6 4 LYS B 177 ? LEU B 181 ? LYS B 164 LEU B 168 
AA6 5 HIS B 249 ? ASP B 252 ? HIS B 236 ASP B 239 
AA7 1 VAL B 185 ? PHE B 187 ? VAL B 172 PHE B 174 
AA7 2 PHE B 437 ? ASN B 441 ? PHE B 424 ASN B 428 
AA7 3 ILE B 411 ? MET B 415 ? ILE B 398 MET B 402 
AA8 1 TYR B 197 ? SER B 198 ? TYR B 184 SER B 185 
AA8 2 GLY B 202 ? PRO B 210 ? GLY B 189 PRO B 197 
AA8 3 LYS B 242 ? PRO B 244 ? LYS B 229 PRO B 231 
AA9 1 TYR B 197 ? SER B 198 ? TYR B 184 SER B 185 
AA9 2 GLY B 202 ? PRO B 210 ? GLY B 189 PRO B 197 
AA9 3 PHE B 403 ? MET B 406 ? PHE B 390 MET B 393 
# 
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 O THR A 142 ? O THR A 129 N ILE A 122 ? N ILE A 109 
AA1 2 3 O PHE A 123 ? O PHE A 110 N TYR A 49  ? N TYR A 36  
AA1 3 4 N VAL A 48  ? N VAL A 35  O ILE A 179 ? O ILE A 166 
AA1 4 5 N PHE A 178 ? N PHE A 165 O ILE A 251 ? O ILE A 238 
AA2 1 2 N MET A 186 ? N MET A 173 O VAL A 438 ? O VAL A 425 
AA2 2 3 O CYS A 439 ? O CYS A 426 N ALA A 412 ? N ALA A 399 
AA3 1 2 N SER A 198 ? N SER A 185 O GLY A 202 ? O GLY A 189 
AA3 2 3 N TRP A 209 ? N TRP A 196 O VAL A 243 ? O VAL A 230 
AA4 1 2 N SER A 198 ? N SER A 185 O GLY A 202 ? O GLY A 189 
AA4 2 3 N VAL A 205 ? N VAL A 192 O GLU A 404 ? O GLU A 391 
AA5 1 2 N GLN A 296 ? N GLN A 283 O LYS A 398 ? O LYS A 385 
AA6 1 2 O VAL B 144 ? O VAL B 131 N ILE B 124 ? N ILE B 111 
AA6 2 3 O PHE B 123 ? O PHE B 110 N VAL B 47  ? N VAL B 34  
AA6 3 4 N VAL B 48  ? N VAL B 35  O LEU B 181 ? O LEU B 168 
AA6 4 5 N PHE B 178 ? N PHE B 165 O ILE B 251 ? O ILE B 238 
AA7 1 2 N MET B 186 ? N MET B 173 O VAL B 438 ? O VAL B 425 
AA7 2 3 O CYS B 439 ? O CYS B 426 N LYS B 414 ? N LYS B 401 
AA8 1 2 N SER B 198 ? N SER B 185 O GLY B 202 ? O GLY B 189 
AA8 2 3 N THR B 208 ? N THR B 195 O VAL B 243 ? O VAL B 230 
AA9 1 2 N SER B 198 ? N SER B 185 O GLY B 202 ? O GLY B 189 
AA9 2 3 N VAL B 205 ? N VAL B 192 O GLU B 404 ? O GLU B 391 
# 
_pdbx_entry_details.entry_id                   9BGG 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LEU A 28  ? ? 64.94   162.93  
2  1 ASP A 43  ? ? 60.03   -98.24  
3  1 ARG A 107 ? ? -91.85  -60.10  
4  1 HIS A 156 ? ? -69.26  2.63    
5  1 THR A 195 ? ? -146.47 -158.98 
6  1 GLU A 395 ? ? -87.92  37.70   
7  1 LEU B 28  ? ? 66.62   159.23  
8  1 PRO B 126 ? ? -84.23  42.29   
9  1 VAL B 136 ? ? -122.82 -51.93  
10 1 PHE B 146 ? ? 55.47   18.35   
11 1 ASP B 170 ? ? 73.92   -3.99   
12 1 LYS B 176 ? ? 52.03   -109.73 
13 1 THR B 195 ? ? -92.74  -61.15  
14 1 ASP B 206 ? ? -95.19  -62.01  
15 1 GLU B 266 ? ? -97.33  31.39   
16 1 THR B 405 ? ? 67.75   -6.03   
17 1 HIS B 433 ? ? 68.09   -2.82   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BGG 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  7s05 
_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                7s05 
_em_3d_fitting_list.initial_refinement_model_id   1 
# 
_em_3d_reconstruction.entry_id                    9BGG 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.4 
_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               275102 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.8 
# 
_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                 GlcNAc-1-phosphotransferase 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_image_scans.entry_id                9BGG 
_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                        9BGG 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   0.05 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_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               OTHER 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             1000 
_em_imaging.nominal_defocus_max             1600 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           105000 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   193 
_em_imaging.recording_temperature_maximum   193 
_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    COPPER 
_em_sample_support.grid_mesh_size   300 
_em_sample_support.grid_type        'Quantifoil R2/1' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              9BGG 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              95 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   299 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9BGG 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A ASP -12 ? A ASP 1   
2   1 Y 1 A GLU -11 ? A GLU 2   
3   1 Y 1 A ASP -10 ? A ASP 3   
4   1 Y 1 A GLN -9  ? A GLN 4   
5   1 Y 1 A VAL -8  ? A VAL 5   
6   1 Y 1 A ASP -7  ? A ASP 6   
7   1 Y 1 A PRO -6  ? A PRO 7   
8   1 Y 1 A ARG -5  ? A ARG 8   
9   1 Y 1 A LEU -4  ? A LEU 9   
10  1 Y 1 A ILE -3  ? A ILE 10  
11  1 Y 1 A ASP -2  ? A ASP 11  
12  1 Y 1 A GLY -1  ? A GLY 12  
13  1 Y 1 A LYS 0   ? A LYS 13  
14  1 Y 1 A TRP 1   ? A TRP 14  
15  1 Y 1 A SER 2   ? A SER 15  
16  1 Y 1 A ARG 3   ? A ARG 16  
17  1 Y 1 A ASP 4   ? A ASP 17  
18  1 Y 1 A GLN 5   ? A GLN 18  
19  1 Y 1 A LYS 57  ? A LYS 70  
20  1 Y 1 A ARG 58  ? A ARG 71  
21  1 Y 1 A ASP 59  ? A ASP 72  
22  1 Y 1 A PRO 60  ? A PRO 73  
23  1 Y 1 A LEU 61  ? A LEU 74  
24  1 Y 1 A ILE 62  ? A ILE 75  
25  1 Y 1 A PRO 63  ? A PRO 76  
26  1 Y 1 A GLU 64  ? A GLU 77  
27  1 Y 1 A CYS 65  ? A CYS 78  
28  1 Y 1 A GLN 66  ? A GLN 79  
29  1 Y 1 A GLY 67  ? A GLY 80  
30  1 Y 1 A LYS 68  ? A LYS 81  
31  1 Y 1 A GLN 69  ? A GLN 82  
32  1 Y 1 A THR 70  ? A THR 83  
33  1 Y 1 A PRO 71  ? A PRO 84  
34  1 Y 1 A GLU 72  ? A GLU 85  
35  1 Y 1 A LYS 73  ? A LYS 86  
36  1 Y 1 A ASP 74  ? A ASP 87  
37  1 Y 1 A LYS 75  ? A LYS 88  
38  1 Y 1 A CYS 76  ? A CYS 89  
39  1 Y 1 A TYR 77  ? A TYR 90  
40  1 Y 1 A ARG 78  ? A ARG 91  
41  1 Y 1 A ASP 79  ? A ASP 92  
42  1 Y 1 A ASP 80  ? A ASP 93  
43  1 Y 1 A ILE 81  ? A ILE 94  
44  1 Y 1 A SER 82  ? A SER 95  
45  1 Y 1 A ALA 83  ? A ALA 96  
46  1 Y 1 A SER 84  ? A SER 97  
47  1 Y 1 A ARG 85  ? A ARG 98  
48  1 Y 1 A PHE 86  ? A PHE 99  
49  1 Y 1 A GLU 87  ? A GLU 100 
50  1 Y 1 A ASP 88  ? A ASP 101 
51  1 Y 1 A ASP 341 ? A ASP 354 
52  1 Y 1 A ILE 342 ? A ILE 355 
53  1 Y 1 A THR 343 ? A THR 356 
54  1 Y 1 A GLN 344 ? A GLN 357 
55  1 Y 1 A LEU 345 ? A LEU 358 
56  1 Y 1 A ASN 346 ? A ASN 359 
57  1 Y 1 A ASN 347 ? A ASN 360 
58  1 Y 1 A ILE 348 ? A ILE 361 
59  1 Y 1 A PRO 349 ? A PRO 362 
60  1 Y 1 A PRO 350 ? A PRO 363 
61  1 Y 1 A GLU 464 ? A GLU 477 
62  1 Y 1 A TYR 465 ? A TYR 478 
63  1 Y 1 A ARG 466 ? A ARG 479 
64  1 Y 1 A ASN 467 ? A ASN 480 
65  1 Y 1 A ARG 468 ? A ARG 481 
66  1 Y 1 A PHE 469 ? A PHE 482 
67  1 Y 1 A LEU 470 ? A LEU 483 
68  1 Y 1 A HIS 471 ? A HIS 484 
69  1 Y 1 A MET 472 ? A MET 485 
70  1 Y 1 A HIS 473 ? A HIS 486 
71  1 Y 1 A GLU 474 ? A GLU 487 
72  1 Y 1 A LEU 475 ? A LEU 488 
73  1 Y 1 A GLN 476 ? A GLN 489 
74  1 Y 1 A GLU 477 ? A GLU 490 
75  1 Y 1 A TRP 478 ? A TRP 491 
76  1 Y 1 A ARG 479 ? A ARG 492 
77  1 Y 1 A ALA 480 ? A ALA 493 
78  1 Y 1 A TYR 481 ? A TYR 494 
79  1 Y 1 A ARG 482 ? A ARG 495 
80  1 Y 1 A ASP 483 ? A ASP 496 
81  1 Y 1 A LYS 484 ? A LYS 497 
82  1 Y 1 A LEU 485 ? A LEU 498 
83  1 Y 1 A LYS 486 ? A LYS 499 
84  1 Y 1 B ASP -12 ? B ASP 1   
85  1 Y 1 B GLU -11 ? B GLU 2   
86  1 Y 1 B ASP -10 ? B ASP 3   
87  1 Y 1 B GLN -9  ? B GLN 4   
88  1 Y 1 B VAL -8  ? B VAL 5   
89  1 Y 1 B ASP -7  ? B ASP 6   
90  1 Y 1 B PRO -6  ? B PRO 7   
91  1 Y 1 B ARG -5  ? B ARG 8   
92  1 Y 1 B LEU -4  ? B LEU 9   
93  1 Y 1 B ILE -3  ? B ILE 10  
94  1 Y 1 B ASP -2  ? B ASP 11  
95  1 Y 1 B GLY -1  ? B GLY 12  
96  1 Y 1 B LYS 0   ? B LYS 13  
97  1 Y 1 B TRP 1   ? B TRP 14  
98  1 Y 1 B SER 2   ? B SER 15  
99  1 Y 1 B ARG 3   ? B ARG 16  
100 1 Y 1 B ASP 4   ? B ASP 17  
101 1 Y 1 B GLN 5   ? B GLN 18  
102 1 Y 1 B LYS 57  ? B LYS 70  
103 1 Y 1 B ARG 58  ? B ARG 71  
104 1 Y 1 B ASP 59  ? B ASP 72  
105 1 Y 1 B PRO 60  ? B PRO 73  
106 1 Y 1 B LEU 61  ? B LEU 74  
107 1 Y 1 B ILE 62  ? B ILE 75  
108 1 Y 1 B PRO 63  ? B PRO 76  
109 1 Y 1 B GLU 64  ? B GLU 77  
110 1 Y 1 B CYS 65  ? B CYS 78  
111 1 Y 1 B GLN 66  ? B GLN 79  
112 1 Y 1 B GLY 67  ? B GLY 80  
113 1 Y 1 B LYS 68  ? B LYS 81  
114 1 Y 1 B GLN 69  ? B GLN 82  
115 1 Y 1 B THR 70  ? B THR 83  
116 1 Y 1 B PRO 71  ? B PRO 84  
117 1 Y 1 B GLU 72  ? B GLU 85  
118 1 Y 1 B LYS 73  ? B LYS 86  
119 1 Y 1 B ASP 74  ? B ASP 87  
120 1 Y 1 B LYS 75  ? B LYS 88  
121 1 Y 1 B CYS 76  ? B CYS 89  
122 1 Y 1 B TYR 77  ? B TYR 90  
123 1 Y 1 B ARG 78  ? B ARG 91  
124 1 Y 1 B ASP 79  ? B ASP 92  
125 1 Y 1 B ASP 80  ? B ASP 93  
126 1 Y 1 B ILE 81  ? B ILE 94  
127 1 Y 1 B SER 82  ? B SER 95  
128 1 Y 1 B ALA 83  ? B ALA 96  
129 1 Y 1 B SER 84  ? B SER 97  
130 1 Y 1 B ARG 85  ? B ARG 98  
131 1 Y 1 B PHE 86  ? B PHE 99  
132 1 Y 1 B GLU 87  ? B GLU 100 
133 1 Y 1 B PRO 339 ? B PRO 352 
134 1 Y 1 B ALA 340 ? B ALA 353 
135 1 Y 1 B ASP 341 ? B ASP 354 
136 1 Y 1 B ILE 342 ? B ILE 355 
137 1 Y 1 B THR 343 ? B THR 356 
138 1 Y 1 B GLN 344 ? B GLN 357 
139 1 Y 1 B LEU 345 ? B LEU 358 
140 1 Y 1 B ASN 346 ? B ASN 359 
141 1 Y 1 B ASN 347 ? B ASN 360 
142 1 Y 1 B ILE 348 ? B ILE 361 
143 1 Y 1 B PRO 349 ? B PRO 362 
144 1 Y 1 B ASN 467 ? B ASN 480 
145 1 Y 1 B ARG 468 ? B ARG 481 
146 1 Y 1 B PHE 469 ? B PHE 482 
147 1 Y 1 B LEU 470 ? B LEU 483 
148 1 Y 1 B HIS 471 ? B HIS 484 
149 1 Y 1 B MET 472 ? B MET 485 
150 1 Y 1 B HIS 473 ? B HIS 486 
151 1 Y 1 B GLU 474 ? B GLU 487 
152 1 Y 1 B LEU 475 ? B LEU 488 
153 1 Y 1 B GLN 476 ? B GLN 489 
154 1 Y 1 B GLU 477 ? B GLU 490 
155 1 Y 1 B TRP 478 ? B TRP 491 
156 1 Y 1 B ARG 479 ? B ARG 492 
157 1 Y 1 B ALA 480 ? B ALA 493 
158 1 Y 1 B TYR 481 ? B TYR 494 
159 1 Y 1 B ARG 482 ? B ARG 495 
160 1 Y 1 B ASP 483 ? B ASP 496 
161 1 Y 1 B LYS 484 ? B LYS 497 
162 1 Y 1 B LEU 485 ? B LEU 498 
163 1 Y 1 B LYS 486 ? B LYS 499 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
NAG C1   C N R 247 
NAG C2   C N R 248 
NAG C3   C N R 249 
NAG C4   C N S 250 
NAG C5   C N R 251 
NAG C6   C N N 252 
NAG C7   C N N 253 
NAG C8   C N N 254 
NAG N2   N N N 255 
NAG O1   O N N 256 
NAG O3   O N N 257 
NAG O4   O N N 258 
NAG O5   O N N 259 
NAG O6   O N N 260 
NAG O7   O N N 261 
NAG H1   H N N 262 
NAG H2   H N N 263 
NAG H3   H N N 264 
NAG H4   H N N 265 
NAG H5   H N N 266 
NAG H61  H N N 267 
NAG H62  H N N 268 
NAG H81  H N N 269 
NAG H82  H N N 270 
NAG H83  H N N 271 
NAG HN2  H N N 272 
NAG HO1  H N N 273 
NAG HO3  H N N 274 
NAG HO4  H N N 275 
NAG HO6  H N N 276 
PHE N    N N N 277 
PHE CA   C N S 278 
PHE C    C N N 279 
PHE O    O N N 280 
PHE CB   C N N 281 
PHE CG   C Y N 282 
PHE CD1  C Y N 283 
PHE CD2  C Y N 284 
PHE CE1  C Y N 285 
PHE CE2  C Y N 286 
PHE CZ   C Y N 287 
PHE OXT  O N N 288 
PHE H    H N N 289 
PHE H2   H N N 290 
PHE HA   H N N 291 
PHE HB2  H N N 292 
PHE HB3  H N N 293 
PHE HD1  H N N 294 
PHE HD2  H N N 295 
PHE HE1  H N N 296 
PHE HE2  H N N 297 
PHE HZ   H N N 298 
PHE HXT  H N N 299 
PRO N    N N N 300 
PRO CA   C N S 301 
PRO C    C N N 302 
PRO O    O N N 303 
PRO CB   C N N 304 
PRO CG   C N N 305 
PRO CD   C N N 306 
PRO OXT  O N N 307 
PRO H    H N N 308 
PRO HA   H N N 309 
PRO HB2  H N N 310 
PRO HB3  H N N 311 
PRO HG2  H N N 312 
PRO HG3  H N N 313 
PRO HD2  H N N 314 
PRO HD3  H N N 315 
PRO HXT  H N N 316 
SER N    N N N 317 
SER CA   C N S 318 
SER C    C N N 319 
SER O    O N N 320 
SER CB   C N N 321 
SER OG   O N N 322 
SER OXT  O N N 323 
SER H    H N N 324 
SER H2   H N N 325 
SER HA   H N N 326 
SER HB2  H N N 327 
SER HB3  H N N 328 
SER HG   H N N 329 
SER HXT  H N N 330 
THR N    N N N 331 
THR CA   C N S 332 
THR C    C N N 333 
THR O    O N N 334 
THR CB   C N R 335 
THR OG1  O N N 336 
THR CG2  C N N 337 
THR OXT  O N N 338 
THR H    H N N 339 
THR H2   H N N 340 
THR HA   H N N 341 
THR HB   H N N 342 
THR HG1  H N N 343 
THR HG21 H N N 344 
THR HG22 H N N 345 
THR HG23 H N N 346 
THR HXT  H N N 347 
TRP N    N N N 348 
TRP CA   C N S 349 
TRP C    C N N 350 
TRP O    O N N 351 
TRP CB   C N N 352 
TRP CG   C Y N 353 
TRP CD1  C Y N 354 
TRP CD2  C Y N 355 
TRP NE1  N Y N 356 
TRP CE2  C Y N 357 
TRP CE3  C Y N 358 
TRP CZ2  C Y N 359 
TRP CZ3  C Y N 360 
TRP CH2  C Y N 361 
TRP OXT  O N N 362 
TRP H    H N N 363 
TRP H2   H N N 364 
TRP HA   H N N 365 
TRP HB2  H N N 366 
TRP HB3  H N N 367 
TRP HD1  H N N 368 
TRP HE1  H N N 369 
TRP HE3  H N N 370 
TRP HZ2  H N N 371 
TRP HZ3  H N N 372 
TRP HH2  H N N 373 
TRP HXT  H N N 374 
TYR N    N N N 375 
TYR CA   C N S 376 
TYR C    C N N 377 
TYR O    O N N 378 
TYR CB   C N N 379 
TYR CG   C Y N 380 
TYR CD1  C Y N 381 
TYR CD2  C Y N 382 
TYR CE1  C Y N 383 
TYR CE2  C Y N 384 
TYR CZ   C Y N 385 
TYR OH   O N N 386 
TYR OXT  O N N 387 
TYR H    H N N 388 
TYR H2   H N N 389 
TYR HA   H N N 390 
TYR HB2  H N N 391 
TYR HB3  H N N 392 
TYR HD1  H N N 393 
TYR HD2  H N N 394 
TYR HE1  H N N 395 
TYR HE2  H N N 396 
TYR HH   H N N 397 
TYR HXT  H N N 398 
VAL N    N N N 399 
VAL CA   C N S 400 
VAL C    C N N 401 
VAL O    O N N 402 
VAL CB   C N N 403 
VAL CG1  C N N 404 
VAL CG2  C N N 405 
VAL OXT  O N N 406 
VAL H    H N N 407 
VAL H2   H N N 408 
VAL HA   H N N 409 
VAL HB   H N N 410 
VAL HG11 H N N 411 
VAL HG12 H N N 412 
VAL HG13 H N N 413 
VAL HG21 H N N 414 
VAL HG22 H N N 415 
VAL HG23 H N N 416 
VAL HXT  H N N 417 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
NAG C1  C2   sing N N 235 
NAG C1  O1   sing N N 236 
NAG C1  O5   sing N N 237 
NAG C1  H1   sing N N 238 
NAG C2  C3   sing N N 239 
NAG C2  N2   sing N N 240 
NAG C2  H2   sing N N 241 
NAG C3  C4   sing N N 242 
NAG C3  O3   sing N N 243 
NAG C3  H3   sing N N 244 
NAG C4  C5   sing N N 245 
NAG C4  O4   sing N N 246 
NAG C4  H4   sing N N 247 
NAG C5  C6   sing N N 248 
NAG C5  O5   sing N N 249 
NAG C5  H5   sing N N 250 
NAG C6  O6   sing N N 251 
NAG C6  H61  sing N N 252 
NAG C6  H62  sing N N 253 
NAG C7  C8   sing N N 254 
NAG C7  N2   sing N N 255 
NAG C7  O7   doub N N 256 
NAG C8  H81  sing N N 257 
NAG C8  H82  sing N N 258 
NAG C8  H83  sing N N 259 
NAG N2  HN2  sing N N 260 
NAG O1  HO1  sing N N 261 
NAG O3  HO3  sing N N 262 
NAG O4  HO4  sing N N 263 
NAG O6  HO6  sing N N 264 
PHE N   CA   sing N N 265 
PHE N   H    sing N N 266 
PHE N   H2   sing N N 267 
PHE CA  C    sing N N 268 
PHE CA  CB   sing N N 269 
PHE CA  HA   sing N N 270 
PHE C   O    doub N N 271 
PHE C   OXT  sing N N 272 
PHE CB  CG   sing N N 273 
PHE CB  HB2  sing N N 274 
PHE CB  HB3  sing N N 275 
PHE CG  CD1  doub Y N 276 
PHE CG  CD2  sing Y N 277 
PHE CD1 CE1  sing Y N 278 
PHE CD1 HD1  sing N N 279 
PHE CD2 CE2  doub Y N 280 
PHE CD2 HD2  sing N N 281 
PHE CE1 CZ   doub Y N 282 
PHE CE1 HE1  sing N N 283 
PHE CE2 CZ   sing Y N 284 
PHE CE2 HE2  sing N N 285 
PHE CZ  HZ   sing N N 286 
PHE OXT HXT  sing N N 287 
PRO N   CA   sing N N 288 
PRO N   CD   sing N N 289 
PRO N   H    sing N N 290 
PRO CA  C    sing N N 291 
PRO CA  CB   sing N N 292 
PRO CA  HA   sing N N 293 
PRO C   O    doub N N 294 
PRO C   OXT  sing N N 295 
PRO CB  CG   sing N N 296 
PRO CB  HB2  sing N N 297 
PRO CB  HB3  sing N N 298 
PRO CG  CD   sing N N 299 
PRO CG  HG2  sing N N 300 
PRO CG  HG3  sing N N 301 
PRO CD  HD2  sing N N 302 
PRO CD  HD3  sing N N 303 
PRO OXT HXT  sing N N 304 
SER N   CA   sing N N 305 
SER N   H    sing N N 306 
SER N   H2   sing N N 307 
SER CA  C    sing N N 308 
SER CA  CB   sing N N 309 
SER CA  HA   sing N N 310 
SER C   O    doub N N 311 
SER C   OXT  sing N N 312 
SER CB  OG   sing N N 313 
SER CB  HB2  sing N N 314 
SER CB  HB3  sing N N 315 
SER OG  HG   sing N N 316 
SER OXT HXT  sing N N 317 
THR N   CA   sing N N 318 
THR N   H    sing N N 319 
THR N   H2   sing N N 320 
THR CA  C    sing N N 321 
THR CA  CB   sing N N 322 
THR CA  HA   sing N N 323 
THR C   O    doub N N 324 
THR C   OXT  sing N N 325 
THR CB  OG1  sing N N 326 
THR CB  CG2  sing N N 327 
THR CB  HB   sing N N 328 
THR OG1 HG1  sing N N 329 
THR CG2 HG21 sing N N 330 
THR CG2 HG22 sing N N 331 
THR CG2 HG23 sing N N 332 
THR OXT HXT  sing N N 333 
TRP N   CA   sing N N 334 
TRP N   H    sing N N 335 
TRP N   H2   sing N N 336 
TRP CA  C    sing N N 337 
TRP CA  CB   sing N N 338 
TRP CA  HA   sing N N 339 
TRP C   O    doub N N 340 
TRP C   OXT  sing N N 341 
TRP CB  CG   sing N N 342 
TRP CB  HB2  sing N N 343 
TRP CB  HB3  sing N N 344 
TRP CG  CD1  doub Y N 345 
TRP CG  CD2  sing Y N 346 
TRP CD1 NE1  sing Y N 347 
TRP CD1 HD1  sing N N 348 
TRP CD2 CE2  doub Y N 349 
TRP CD2 CE3  sing Y N 350 
TRP NE1 CE2  sing Y N 351 
TRP NE1 HE1  sing N N 352 
TRP CE2 CZ2  sing Y N 353 
TRP CE3 CZ3  doub Y N 354 
TRP CE3 HE3  sing N N 355 
TRP CZ2 CH2  doub Y N 356 
TRP CZ2 HZ2  sing N N 357 
TRP CZ3 CH2  sing Y N 358 
TRP CZ3 HZ3  sing N N 359 
TRP CH2 HH2  sing N N 360 
TRP OXT HXT  sing N N 361 
TYR N   CA   sing N N 362 
TYR N   H    sing N N 363 
TYR N   H2   sing N N 364 
TYR CA  C    sing N N 365 
TYR CA  CB   sing N N 366 
TYR CA  HA   sing N N 367 
TYR C   O    doub N N 368 
TYR C   OXT  sing N N 369 
TYR CB  CG   sing N N 370 
TYR CB  HB2  sing N N 371 
TYR CB  HB3  sing N N 372 
TYR CG  CD1  doub Y N 373 
TYR CG  CD2  sing Y N 374 
TYR CD1 CE1  sing Y N 375 
TYR CD1 HD1  sing N N 376 
TYR CD2 CE2  doub Y N 377 
TYR CD2 HD2  sing N N 378 
TYR CE1 CZ   doub Y N 379 
TYR CE1 HE1  sing N N 380 
TYR CE2 CZ   sing Y N 381 
TYR CE2 HE2  sing N N 382 
TYR CZ  OH   sing N N 383 
TYR OH  HH   sing N N 384 
TYR OXT HXT  sing N N 385 
VAL N   CA   sing N N 386 
VAL N   H    sing N N 387 
VAL N   H2   sing N N 388 
VAL CA  C    sing N N 389 
VAL CA  CB   sing N N 390 
VAL CA  HA   sing N N 391 
VAL C   O    doub N N 392 
VAL C   OXT  sing N N 393 
VAL CB  CG1  sing N N 394 
VAL CB  CG2  sing N N 395 
VAL CB  HB   sing N N 396 
VAL CG1 HG11 sing N N 397 
VAL CG1 HG12 sing N N 398 
VAL CG1 HG13 sing N N 399 
VAL CG2 HG21 sing N N 400 
VAL CG2 HG22 sing N N 401 
VAL CG2 HG23 sing N N 402 
VAL OXT HXT  sing N N 403 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-04-18 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BGG 
_em_admin.last_update        2025-02-26 
_em_admin.map_release_date   2025-02-26 
_em_admin.title              'Structure of a hyperactive S1S3 truncation of the human GlcNAc-1-phosphotransferase' 
# 
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 75 mM KCl 1 'potassium chloride' 
1 20 mM ?   2 HEPES                
1 10 mM ?   3 2-mercaptoethanol    
# 
_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    YES 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                0.57 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   1 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          1286942 
_em_entity_assembly_recombinant.organism             'Insect BA phytoplasma' 
_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               1 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         60 
_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                     13219 
# 
_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   2249987 
_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 1.21.1_5286: 
'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           0.15 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           NS127292 
_pdbx_audit_support.ordinal                1 
# 
_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   7s05 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9BGG 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . TYR A 1 19  ? 153.777 119.663 123.170 1.00 150.29 ? 6   TYR A N   1 
ATOM   2    C CA  . TYR A 1 19  ? 154.186 121.030 123.473 1.00 153.41 ? 6   TYR A CA  1 
ATOM   3    C C   . TYR A 1 19  ? 153.477 122.020 122.542 1.00 149.70 ? 6   TYR A C   1 
ATOM   4    O O   . TYR A 1 19  ? 152.721 122.877 122.999 1.00 147.35 ? 6   TYR A O   1 
ATOM   5    C CB  . TYR A 1 19  ? 155.717 121.167 123.381 1.00 155.19 ? 6   TYR A CB  1 
ATOM   6    C CG  . TYR A 1 19  ? 156.306 120.984 121.995 1.00 156.95 ? 6   TYR A CG  1 
ATOM   7    C CD1 . TYR A 1 19  ? 156.304 119.742 121.370 1.00 157.63 ? 6   TYR A CD1 1 
ATOM   8    C CD2 . TYR A 1 19  ? 156.863 122.058 121.312 1.00 154.08 ? 6   TYR A CD2 1 
ATOM   9    C CE1 . TYR A 1 19  ? 156.837 119.578 120.105 1.00 156.64 ? 6   TYR A CE1 1 
ATOM   10   C CE2 . TYR A 1 19  ? 157.399 121.902 120.049 1.00 153.71 ? 6   TYR A CE2 1 
ATOM   11   C CZ  . TYR A 1 19  ? 157.384 120.661 119.450 1.00 156.92 ? 6   TYR A CZ  1 
ATOM   12   O OH  . TYR A 1 19  ? 157.918 120.502 118.192 1.00 160.51 ? 6   TYR A OH  1 
ATOM   13   N N   . HIS A 1 20  ? 153.721 121.895 121.238 1.00 146.91 ? 7   HIS A N   1 
ATOM   14   C CA  . HIS A 1 20  ? 153.044 122.700 120.233 1.00 139.97 ? 7   HIS A CA  1 
ATOM   15   C C   . HIS A 1 20  ? 151.795 122.025 119.687 1.00 131.73 ? 7   HIS A C   1 
ATOM   16   O O   . HIS A 1 20  ? 151.067 122.642 118.903 1.00 127.92 ? 7   HIS A O   1 
ATOM   17   C CB  . HIS A 1 20  ? 154.005 123.021 119.081 1.00 141.71 ? 7   HIS A CB  1 
ATOM   18   C CG  . HIS A 1 20  ? 153.479 124.041 118.120 1.00 138.65 ? 7   HIS A CG  1 
ATOM   19   N ND1 . HIS A 1 20  ? 152.731 123.702 117.013 1.00 135.23 ? 7   HIS A ND1 1 
ATOM   20   C CD2 . HIS A 1 20  ? 153.584 125.390 118.105 1.00 139.92 ? 7   HIS A CD2 1 
ATOM   21   C CE1 . HIS A 1 20  ? 152.402 124.799 116.354 1.00 134.63 ? 7   HIS A CE1 1 
ATOM   22   N NE2 . HIS A 1 20  ? 152.908 125.837 116.996 1.00 138.28 ? 7   HIS A NE2 1 
ATOM   23   N N   . VAL A 1 21  ? 151.530 120.778 120.083 1.00 132.74 ? 8   VAL A N   1 
ATOM   24   C CA  . VAL A 1 21  ? 150.353 120.072 119.587 1.00 130.14 ? 8   VAL A CA  1 
ATOM   25   C C   . VAL A 1 21  ? 149.079 120.752 120.072 1.00 127.00 ? 8   VAL A C   1 
ATOM   26   O O   . VAL A 1 21  ? 148.081 120.819 119.346 1.00 122.62 ? 8   VAL A O   1 
ATOM   27   C CB  . VAL A 1 21  ? 150.404 118.590 120.001 1.00 125.65 ? 8   VAL A CB  1 
ATOM   28   C CG1 . VAL A 1 21  ? 149.220 117.831 119.421 1.00 118.17 ? 8   VAL A CG1 1 
ATOM   29   C CG2 . VAL A 1 21  ? 151.713 117.962 119.551 1.00 125.12 ? 8   VAL A CG2 1 
ATOM   30   N N   . LEU A 1 22  ? 149.091 121.270 121.304 1.00 129.80 ? 9   LEU A N   1 
ATOM   31   C CA  . LEU A 1 22  ? 147.913 121.956 121.829 1.00 127.04 ? 9   LEU A CA  1 
ATOM   32   C C   . LEU A 1 22  ? 147.558 123.175 120.985 1.00 123.32 ? 9   LEU A C   1 
ATOM   33   O O   . LEU A 1 22  ? 146.384 123.399 120.670 1.00 118.28 ? 9   LEU A O   1 
ATOM   34   C CB  . LEU A 1 22  ? 148.147 122.362 123.285 1.00 129.61 ? 9   LEU A CB  1 
ATOM   35   C CG  . LEU A 1 22  ? 147.962 121.276 124.345 1.00 131.49 ? 9   LEU A CG  1 
ATOM   36   C CD1 . LEU A 1 22  ? 148.487 121.747 125.691 1.00 135.78 ? 9   LEU A CD1 1 
ATOM   37   C CD2 . LEU A 1 22  ? 146.496 120.885 124.450 1.00 131.66 ? 9   LEU A CD2 1 
ATOM   38   N N   . PHE A 1 23  ? 148.558 123.976 120.614 1.00 122.98 ? 10  PHE A N   1 
ATOM   39   C CA  . PHE A 1 23  ? 148.302 125.129 119.756 1.00 118.57 ? 10  PHE A CA  1 
ATOM   40   C C   . PHE A 1 23  ? 147.900 124.691 118.353 1.00 112.08 ? 10  PHE A C   1 
ATOM   41   O O   . PHE A 1 23  ? 146.955 125.234 117.767 1.00 106.52 ? 10  PHE A O   1 
ATOM   42   C CB  . PHE A 1 23  ? 149.537 126.031 119.705 1.00 124.17 ? 10  PHE A CB  1 
ATOM   43   C CG  . PHE A 1 23  ? 149.867 126.690 121.015 1.00 128.63 ? 10  PHE A CG  1 
ATOM   44   C CD1 . PHE A 1 23  ? 149.225 127.855 121.401 1.00 128.36 ? 10  PHE A CD1 1 
ATOM   45   C CD2 . PHE A 1 23  ? 150.828 126.151 121.857 1.00 133.06 ? 10  PHE A CD2 1 
ATOM   46   C CE1 . PHE A 1 23  ? 149.528 128.466 122.604 1.00 128.05 ? 10  PHE A CE1 1 
ATOM   47   C CE2 . PHE A 1 23  ? 151.135 126.758 123.061 1.00 132.97 ? 10  PHE A CE2 1 
ATOM   48   C CZ  . PHE A 1 23  ? 150.484 127.917 123.435 1.00 131.48 ? 10  PHE A CZ  1 
ATOM   49   N N   . ASP A 1 24  ? 148.608 123.703 117.800 1.00 117.40 ? 11  ASP A N   1 
ATOM   50   C CA  . ASP A 1 24  ? 148.360 123.288 116.424 1.00 114.02 ? 11  ASP A CA  1 
ATOM   51   C C   . ASP A 1 24  ? 146.975 122.677 116.253 1.00 108.65 ? 11  ASP A C   1 
ATOM   52   O O   . ASP A 1 24  ? 146.360 122.831 115.193 1.00 102.81 ? 11  ASP A O   1 
ATOM   53   C CB  . ASP A 1 24  ? 149.437 122.300 115.974 1.00 116.98 ? 11  ASP A CB  1 
ATOM   54   C CG  . ASP A 1 24  ? 149.200 121.782 114.571 1.00 115.42 ? 11  ASP A CG  1 
ATOM   55   O OD1 . ASP A 1 24  ? 149.194 122.600 113.627 1.00 111.96 ? 11  ASP A OD1 1 
ATOM   56   O OD2 . ASP A 1 24  ? 149.023 120.556 114.409 1.00 115.63 ? 11  ASP A OD2 1 
ATOM   57   N N   . SER A 1 25  ? 146.468 121.986 117.277 1.00 109.26 ? 12  SER A N   1 
ATOM   58   C CA  . SER A 1 25  ? 145.151 121.368 117.172 1.00 103.91 ? 12  SER A CA  1 
ATOM   59   C C   . SER A 1 25  ? 144.066 122.414 116.959 1.00 99.06  ? 12  SER A C   1 
ATOM   60   O O   . SER A 1 25  ? 143.170 122.230 116.127 1.00 99.50  ? 12  SER A O   1 
ATOM   61   C CB  . SER A 1 25  ? 144.860 120.541 118.423 1.00 105.45 ? 12  SER A CB  1 
ATOM   62   O OG  . SER A 1 25  ? 144.903 121.352 119.584 1.00 104.27 ? 12  SER A OG  1 
ATOM   63   N N   . TYR A 1 26  ? 144.129 123.520 117.700 1.00 97.03  ? 13  TYR A N   1 
ATOM   64   C CA  . TYR A 1 26  ? 143.166 124.594 117.514 1.00 94.32  ? 13  TYR A CA  1 
ATOM   65   C C   . TYR A 1 26  ? 143.515 125.497 116.341 1.00 90.81  ? 13  TYR A C   1 
ATOM   66   O O   . TYR A 1 26  ? 142.651 126.254 115.885 1.00 83.42  ? 13  TYR A O   1 
ATOM   67   C CB  . TYR A 1 26  ? 143.051 125.423 118.792 1.00 92.66  ? 13  TYR A CB  1 
ATOM   68   C CG  . TYR A 1 26  ? 142.234 124.747 119.864 1.00 94.74  ? 13  TYR A CG  1 
ATOM   69   C CD1 . TYR A 1 26  ? 141.082 124.044 119.539 1.00 96.26  ? 13  TYR A CD1 1 
ATOM   70   C CD2 . TYR A 1 26  ? 142.617 124.800 121.195 1.00 93.96  ? 13  TYR A CD2 1 
ATOM   71   C CE1 . TYR A 1 26  ? 140.330 123.421 120.512 1.00 95.26  ? 13  TYR A CE1 1 
ATOM   72   C CE2 . TYR A 1 26  ? 141.871 124.179 122.175 1.00 95.04  ? 13  TYR A CE2 1 
ATOM   73   C CZ  . TYR A 1 26  ? 140.729 123.491 121.827 1.00 96.07  ? 13  TYR A CZ  1 
ATOM   74   O OH  . TYR A 1 26  ? 139.981 122.868 122.796 1.00 92.66  ? 13  TYR A OH  1 
ATOM   75   N N   . ARG A 1 27  ? 144.750 125.440 115.847 1.00 95.47  ? 14  ARG A N   1 
ATOM   76   C CA  . ARG A 1 27  ? 145.121 126.154 114.633 1.00 91.08  ? 14  ARG A CA  1 
ATOM   77   C C   . ARG A 1 27  ? 144.987 125.298 113.381 1.00 85.94  ? 14  ARG A C   1 
ATOM   78   O O   . ARG A 1 27  ? 145.325 125.768 112.289 1.00 80.55  ? 14  ARG A O   1 
ATOM   79   C CB  . ARG A 1 27  ? 146.555 126.687 114.739 1.00 92.58  ? 14  ARG A CB  1 
ATOM   80   C CG  . ARG A 1 27  ? 146.756 127.725 115.829 1.00 88.65  ? 14  ARG A CG  1 
ATOM   81   C CD  . ARG A 1 27  ? 148.108 128.413 115.705 1.00 93.98  ? 14  ARG A CD  1 
ATOM   82   N NE  . ARG A 1 27  ? 148.076 129.506 114.740 1.00 101.09 ? 14  ARG A NE  1 
ATOM   83   C CZ  . ARG A 1 27  ? 148.472 129.409 113.478 1.00 103.11 ? 14  ARG A CZ  1 
ATOM   84   N NH1 . ARG A 1 27  ? 148.955 128.279 112.990 1.00 104.17 ? 14  ARG A NH1 1 
ATOM   85   N NH2 . ARG A 1 27  ? 148.383 130.475 112.687 1.00 98.56  ? 14  ARG A NH2 1 
ATOM   86   N N   . ASP A 1 28  ? 144.514 124.056 113.508 1.00 84.93  ? 15  ASP A N   1 
ATOM   87   C CA  . ASP A 1 28  ? 144.364 123.156 112.366 1.00 81.30  ? 15  ASP A CA  1 
ATOM   88   C C   . ASP A 1 28  ? 142.905 123.170 111.917 1.00 74.82  ? 15  ASP A C   1 
ATOM   89   O O   . ASP A 1 28  ? 142.117 122.274 112.220 1.00 74.33  ? 15  ASP A O   1 
ATOM   90   C CB  . ASP A 1 28  ? 144.833 121.749 112.718 1.00 85.46  ? 15  ASP A CB  1 
ATOM   91   C CG  . ASP A 1 28  ? 144.909 120.840 111.508 1.00 79.38  ? 15  ASP A CG  1 
ATOM   92   O OD1 . ASP A 1 28  ? 144.688 121.324 110.378 1.00 72.87  ? 15  ASP A OD1 1 
ATOM   93   O OD2 . ASP A 1 28  ? 145.191 119.637 111.689 1.00 84.71  ? 15  ASP A OD2 1 
ATOM   94   N N   . ASN A 1 29  ? 142.550 124.223 111.186 1.00 67.96  ? 16  ASN A N   1 
ATOM   95   C CA  . ASN A 1 29  ? 141.271 124.306 110.499 1.00 60.44  ? 16  ASN A CA  1 
ATOM   96   C C   . ASN A 1 29  ? 141.507 124.966 109.149 1.00 63.26  ? 16  ASN A C   1 
ATOM   97   O O   . ASN A 1 29  ? 142.625 125.376 108.825 1.00 67.29  ? 16  ASN A O   1 
ATOM   98   C CB  . ASN A 1 29  ? 140.226 125.068 111.324 1.00 53.97  ? 16  ASN A CB  1 
ATOM   99   C CG  . ASN A 1 29  ? 140.697 126.445 111.741 1.00 61.49  ? 16  ASN A CG  1 
ATOM   100  O OD1 . ASN A 1 29  ? 140.729 127.375 110.935 1.00 61.57  ? 16  ASN A OD1 1 
ATOM   101  N ND2 . ASN A 1 29  ? 141.055 126.585 113.011 1.00 66.52  ? 16  ASN A ND2 1 
ATOM   102  N N   . ILE A 1 30  ? 140.446 125.053 108.347 1.00 59.51  ? 17  ILE A N   1 
ATOM   103  C CA  . ILE A 1 30  ? 140.589 125.609 107.006 1.00 56.34  ? 17  ILE A CA  1 
ATOM   104  C C   . ILE A 1 30  ? 140.998 127.076 107.072 1.00 61.58  ? 17  ILE A C   1 
ATOM   105  O O   . ILE A 1 30  ? 141.792 127.549 106.251 1.00 66.38  ? 17  ILE A O   1 
ATOM   106  C CB  . ILE A 1 30  ? 139.291 125.409 106.204 1.00 49.22  ? 17  ILE A CB  1 
ATOM   107  C CG1 . ILE A 1 30  ? 138.087 125.909 106.998 1.00 43.57  ? 17  ILE A CG1 1 
ATOM   108  C CG2 . ILE A 1 30  ? 139.109 123.947 105.841 1.00 46.94  ? 17  ILE A CG2 1 
ATOM   109  C CD1 . ILE A 1 30  ? 136.787 125.809 106.247 1.00 41.00  ? 17  ILE A CD1 1 
ATOM   110  N N   . ALA A 1 31  ? 140.474 127.818 108.049 1.00 57.19  ? 18  ALA A N   1 
ATOM   111  C CA  . ALA A 1 31  ? 140.784 129.236 108.166 1.00 63.20  ? 18  ALA A CA  1 
ATOM   112  C C   . ALA A 1 31  ? 142.160 129.501 108.764 1.00 69.57  ? 18  ALA A C   1 
ATOM   113  O O   . ALA A 1 31  ? 142.704 130.592 108.565 1.00 76.25  ? 18  ALA A O   1 
ATOM   114  C CB  . ALA A 1 31  ? 139.718 129.938 109.008 1.00 61.04  ? 18  ALA A CB  1 
ATOM   115  N N   . GLY A 1 32  ? 142.732 128.540 109.487 1.00 66.62  ? 19  GLY A N   1 
ATOM   116  C CA  . GLY A 1 32  ? 144.012 128.745 110.132 1.00 66.71  ? 19  GLY A CA  1 
ATOM   117  C C   . GLY A 1 32  ? 143.962 129.540 111.417 1.00 69.45  ? 19  GLY A C   1 
ATOM   118  O O   . GLY A 1 32  ? 145.019 129.872 111.963 1.00 74.54  ? 19  GLY A O   1 
ATOM   119  N N   . LYS A 1 33  ? 142.770 129.857 111.916 1.00 67.36  ? 20  LYS A N   1 
ATOM   120  C CA  . LYS A 1 33  ? 142.613 130.660 113.116 1.00 65.62  ? 20  LYS A CA  1 
ATOM   121  C C   . LYS A 1 33  ? 142.548 129.767 114.354 1.00 67.21  ? 20  LYS A C   1 
ATOM   122  O O   . LYS A 1 33  ? 142.636 128.540 114.278 1.00 71.94  ? 20  LYS A O   1 
ATOM   123  C CB  . LYS A 1 33  ? 141.361 131.529 113.009 1.00 62.40  ? 20  LYS A CB  1 
ATOM   124  C CG  . LYS A 1 33  ? 141.505 132.721 112.083 1.00 66.02  ? 20  LYS A CG  1 
ATOM   125  C CD  . LYS A 1 33  ? 140.148 133.261 111.665 1.00 67.64  ? 20  LYS A CD  1 
ATOM   126  C CE  . LYS A 1 33  ? 139.225 133.453 112.859 1.00 65.29  ? 20  LYS A CE  1 
ATOM   127  N NZ  . LYS A 1 33  ? 139.758 134.435 113.841 1.00 68.37  ? 20  LYS A NZ  1 
ATOM   128  N N   . SER A 1 34  ? 142.404 130.399 115.515 1.00 62.85  ? 21  SER A N   1 
ATOM   129  C CA  . SER A 1 34  ? 142.170 129.706 116.774 1.00 60.15  ? 21  SER A CA  1 
ATOM   130  C C   . SER A 1 34  ? 140.812 130.128 117.313 1.00 61.32  ? 21  SER A C   1 
ATOM   131  O O   . SER A 1 34  ? 140.508 131.324 117.370 1.00 65.77  ? 21  SER A O   1 
ATOM   132  C CB  . SER A 1 34  ? 143.267 130.015 117.795 1.00 68.50  ? 21  SER A CB  1 
ATOM   133  O OG  . SER A 1 34  ? 143.035 129.326 119.011 1.00 74.33  ? 21  SER A OG  1 
ATOM   134  N N   . PHE A 1 35  ? 140.001 129.149 117.703 1.00 60.13  ? 22  PHE A N   1 
ATOM   135  C CA  . PHE A 1 35  ? 138.639 129.384 118.162 1.00 52.86  ? 22  PHE A CA  1 
ATOM   136  C C   . PHE A 1 35  ? 138.459 128.953 119.612 1.00 53.96  ? 22  PHE A C   1 
ATOM   137  O O   . PHE A 1 35  ? 137.400 128.459 120.004 1.00 53.32  ? 22  PHE A O   1 
ATOM   138  C CB  . PHE A 1 35  ? 137.636 128.669 117.261 1.00 48.60  ? 22  PHE A CB  1 
ATOM   139  C CG  . PHE A 1 35  ? 137.546 129.244 115.879 1.00 45.32  ? 22  PHE A CG  1 
ATOM   140  C CD1 . PHE A 1 35  ? 138.488 128.923 114.917 1.00 49.05  ? 22  PHE A CD1 1 
ATOM   141  C CD2 . PHE A 1 35  ? 136.515 130.100 115.540 1.00 44.43  ? 22  PHE A CD2 1 
ATOM   142  C CE1 . PHE A 1 35  ? 138.404 129.452 113.646 1.00 49.83  ? 22  PHE A CE1 1 
ATOM   143  C CE2 . PHE A 1 35  ? 136.426 130.630 114.271 1.00 47.83  ? 22  PHE A CE2 1 
ATOM   144  C CZ  . PHE A 1 35  ? 137.372 130.306 113.324 1.00 48.59  ? 22  PHE A CZ  1 
ATOM   145  N N   . GLN A 1 36  ? 139.499 129.135 120.430 1.00 59.13  ? 23  GLN A N   1 
ATOM   146  C CA  . GLN A 1 36  ? 139.395 128.777 121.841 1.00 62.63  ? 23  GLN A CA  1 
ATOM   147  C C   . GLN A 1 36  ? 138.328 129.597 122.551 1.00 62.31  ? 23  GLN A C   1 
ATOM   148  O O   . GLN A 1 36  ? 137.685 129.103 123.483 1.00 62.09  ? 23  GLN A O   1 
ATOM   149  C CB  . GLN A 1 36  ? 140.745 128.961 122.533 1.00 74.64  ? 23  GLN A CB  1 
ATOM   150  C CG  . GLN A 1 36  ? 141.869 128.137 121.936 1.00 80.07  ? 23  GLN A CG  1 
ATOM   151  C CD  . GLN A 1 36  ? 143.195 128.378 122.628 1.00 88.94  ? 23  GLN A CD  1 
ATOM   152  O OE1 . GLN A 1 36  ? 143.308 129.244 123.494 1.00 89.48  ? 23  GLN A OE1 1 
ATOM   153  N NE2 . GLN A 1 36  ? 144.208 127.608 122.248 1.00 94.06  ? 23  GLN A NE2 1 
ATOM   154  N N   . ASN A 1 37  ? 138.123 130.846 122.127 1.00 62.23  ? 24  ASN A N   1 
ATOM   155  C CA  . ASN A 1 37  ? 137.107 131.696 122.733 1.00 61.32  ? 24  ASN A CA  1 
ATOM   156  C C   . ASN A 1 37  ? 135.692 131.247 122.401 1.00 59.90  ? 24  ASN A C   1 
ATOM   157  O O   . ASN A 1 37  ? 134.741 131.768 122.993 1.00 56.81  ? 24  ASN A O   1 
ATOM   158  C CB  . ASN A 1 37  ? 137.298 133.144 122.283 1.00 58.75  ? 24  ASN A CB  1 
ATOM   159  C CG  . ASN A 1 37  ? 138.523 133.783 122.893 1.00 63.90  ? 24  ASN A CG  1 
ATOM   160  O OD1 . ASN A 1 37  ? 139.006 133.355 123.940 1.00 73.06  ? 24  ASN A OD1 1 
ATOM   161  N ND2 . ASN A 1 37  ? 139.034 134.819 122.238 1.00 60.62  ? 24  ASN A ND2 1 
ATOM   162  N N   . ARG A 1 38  ? 135.529 130.307 121.468 1.00 53.23  ? 25  ARG A N   1 
ATOM   163  C CA  . ARG A 1 38  ? 134.218 129.855 121.038 1.00 43.70  ? 25  ARG A CA  1 
ATOM   164  C C   . ARG A 1 38  ? 133.980 128.368 121.269 1.00 45.05  ? 25  ARG A C   1 
ATOM   165  O O   . ARG A 1 38  ? 132.844 127.910 121.106 1.00 48.45  ? 25  ARG A O   1 
ATOM   166  C CB  . ARG A 1 38  ? 134.016 130.182 119.547 1.00 44.28  ? 25  ARG A CB  1 
ATOM   167  C CG  . ARG A 1 38  ? 132.584 130.067 119.052 1.00 47.18  ? 25  ARG A CG  1 
ATOM   168  C CD  . ARG A 1 38  ? 131.609 130.682 120.038 1.00 47.75  ? 25  ARG A CD  1 
ATOM   169  N NE  . ARG A 1 38  ? 130.253 130.186 119.838 1.00 44.74  ? 25  ARG A NE  1 
ATOM   170  C CZ  . ARG A 1 38  ? 129.780 129.066 120.367 1.00 42.97  ? 25  ARG A CZ  1 
ATOM   171  N NH1 . ARG A 1 38  ? 130.528 128.298 121.140 1.00 49.83  ? 25  ARG A NH1 1 
ATOM   172  N NH2 . ARG A 1 38  ? 128.524 128.711 120.118 1.00 39.17  ? 25  ARG A NH2 1 
ATOM   173  N N   . LEU A 1 39  ? 134.996 127.606 121.675 1.00 51.40  ? 26  LEU A N   1 
ATOM   174  C CA  . LEU A 1 39  ? 134.851 126.166 121.825 1.00 50.33  ? 26  LEU A CA  1 
ATOM   175  C C   . LEU A 1 39  ? 135.117 125.640 123.228 1.00 54.27  ? 26  LEU A C   1 
ATOM   176  O O   . LEU A 1 39  ? 134.655 124.540 123.543 1.00 58.94  ? 26  LEU A O   1 
ATOM   177  C CB  . LEU A 1 39  ? 135.782 125.432 120.845 1.00 48.03  ? 26  LEU A CB  1 
ATOM   178  C CG  . LEU A 1 39  ? 135.618 125.779 119.362 1.00 44.91  ? 26  LEU A CG  1 
ATOM   179  C CD1 . LEU A 1 39  ? 136.628 125.034 118.503 1.00 41.23  ? 26  LEU A CD1 1 
ATOM   180  C CD2 . LEU A 1 39  ? 134.207 125.487 118.890 1.00 39.88  ? 26  LEU A CD2 1 
ATOM   181  N N   . CYS A 1 40  ? 135.818 126.386 124.083 1.00 53.79  ? 27  CYS A N   1 
ATOM   182  C CA  . CYS A 1 40  ? 136.284 125.851 125.357 1.00 56.99  ? 27  CYS A CA  1 
ATOM   183  C C   . CYS A 1 40  ? 135.669 126.534 126.575 1.00 54.86  ? 27  CYS A C   1 
ATOM   184  O O   . CYS A 1 40  ? 136.153 126.318 127.693 1.00 54.04  ? 27  CYS A O   1 
ATOM   185  C CB  . CYS A 1 40  ? 137.811 125.936 125.437 1.00 68.85  ? 27  CYS A CB  1 
ATOM   186  S SG  . CYS A 1 40  ? 138.716 124.694 124.475 1.00 95.37  ? 27  CYS A SG  1 
ATOM   187  N N   . LEU A 1 41  ? 134.627 127.356 126.396 1.00 53.60  ? 28  LEU A N   1 
ATOM   188  C CA  . LEU A 1 41  ? 133.920 128.036 127.485 1.00 55.45  ? 28  LEU A CA  1 
ATOM   189  C C   . LEU A 1 41  ? 134.819 129.040 128.205 1.00 57.01  ? 28  LEU A C   1 
ATOM   190  O O   . LEU A 1 41  ? 136.047 128.994 128.050 1.00 55.77  ? 28  LEU A O   1 
ATOM   191  C CB  . LEU A 1 41  ? 133.354 127.016 128.481 1.00 47.71  ? 28  LEU A CB  1 
ATOM   192  C CG  . LEU A 1 41  ? 132.137 126.196 128.042 1.00 47.37  ? 28  LEU A CG  1 
ATOM   193  C CD1 . LEU A 1 41  ? 131.977 124.981 128.919 1.00 47.03  ? 28  LEU A CD1 1 
ATOM   194  C CD2 . LEU A 1 41  ? 130.869 127.020 128.092 1.00 41.67  ? 28  LEU A CD2 1 
ATOM   195  N N   . PRO A 1 42  ? 134.257 129.976 128.976 1.00 56.44  ? 29  PRO A N   1 
ATOM   196  C CA  . PRO A 1 42  ? 135.102 130.933 129.707 1.00 55.38  ? 29  PRO A CA  1 
ATOM   197  C C   . PRO A 1 42  ? 135.666 130.315 130.980 1.00 55.13  ? 29  PRO A C   1 
ATOM   198  O O   . PRO A 1 42  ? 134.922 129.810 131.824 1.00 53.58  ? 29  PRO A O   1 
ATOM   199  C CB  . PRO A 1 42  ? 134.141 132.085 130.017 1.00 59.58  ? 29  PRO A CB  1 
ATOM   200  C CG  . PRO A 1 42  ? 132.814 131.442 130.097 1.00 53.71  ? 29  PRO A CG  1 
ATOM   201  C CD  . PRO A 1 42  ? 132.826 130.312 129.101 1.00 54.77  ? 29  PRO A CD  1 
ATOM   202  N N   . MET A 1 43  ? 136.986 130.352 131.114 1.00 53.59  ? 30  MET A N   1 
ATOM   203  C CA  . MET A 1 43  ? 137.647 129.835 132.300 1.00 51.79  ? 30  MET A CA  1 
ATOM   204  C C   . MET A 1 43  ? 138.708 130.819 132.766 1.00 50.28  ? 30  MET A C   1 
ATOM   205  O O   . MET A 1 43  ? 139.258 131.570 131.955 1.00 53.60  ? 30  MET A O   1 
ATOM   206  C CB  . MET A 1 43  ? 138.279 128.463 132.025 1.00 49.11  ? 30  MET A CB  1 
ATOM   207  C CG  . MET A 1 43  ? 137.263 127.330 132.018 1.00 49.54  ? 30  MET A CG  1 
ATOM   208  S SD  . MET A 1 43  ? 136.495 127.090 133.634 1.00 51.56  ? 30  MET A SD  1 
ATOM   209  C CE  . MET A 1 43  ? 134.860 126.540 133.159 1.00 39.95  ? 30  MET A CE  1 
ATOM   210  N N   . PRO A 1 44  ? 139.013 130.848 134.071 1.00 43.22  ? 31  PRO A N   1 
ATOM   211  C CA  . PRO A 1 44  ? 138.448 130.060 135.177 1.00 39.17  ? 31  PRO A CA  1 
ATOM   212  C C   . PRO A 1 44  ? 137.176 130.662 135.769 1.00 36.45  ? 31  PRO A C   1 
ATOM   213  O O   . PRO A 1 44  ? 136.774 131.758 135.395 1.00 36.82  ? 31  PRO A O   1 
ATOM   214  C CB  . PRO A 1 44  ? 139.593 130.062 136.192 1.00 41.22  ? 31  PRO A CB  1 
ATOM   215  C CG  . PRO A 1 44  ? 140.188 131.430 136.024 1.00 40.36  ? 31  PRO A CG  1 
ATOM   216  C CD  . PRO A 1 44  ? 140.095 131.730 134.544 1.00 42.46  ? 31  PRO A CD  1 
ATOM   217  N N   . ILE A 1 45  ? 136.528 129.960 136.699 1.00 36.02  ? 32  ILE A N   1 
ATOM   218  C CA  . ILE A 1 45  ? 135.322 130.436 137.368 1.00 36.42  ? 32  ILE A CA  1 
ATOM   219  C C   . ILE A 1 45  ? 135.527 130.342 138.874 1.00 35.38  ? 32  ILE A C   1 
ATOM   220  O O   . ILE A 1 45  ? 136.018 129.327 139.380 1.00 35.64  ? 32  ILE A O   1 
ATOM   221  C CB  . ILE A 1 45  ? 134.076 129.633 136.937 1.00 33.00  ? 32  ILE A CB  1 
ATOM   222  C CG1 . ILE A 1 45  ? 133.837 129.787 135.437 1.00 32.20  ? 32  ILE A CG1 1 
ATOM   223  C CG2 . ILE A 1 45  ? 132.849 130.081 137.711 1.00 33.15  ? 32  ILE A CG2 1 
ATOM   224  C CD1 . ILE A 1 45  ? 133.633 131.216 135.001 1.00 34.82  ? 32  ILE A CD1 1 
ATOM   225  N N   . ASP A 1 46  ? 135.152 131.399 139.587 1.00 33.21  ? 33  ASP A N   1 
ATOM   226  C CA  . ASP A 1 46  ? 135.300 131.478 141.033 1.00 34.26  ? 33  ASP A CA  1 
ATOM   227  C C   . ASP A 1 46  ? 133.945 131.331 141.716 1.00 33.16  ? 33  ASP A C   1 
ATOM   228  O O   . ASP A 1 46  ? 132.889 131.437 141.090 1.00 36.57  ? 33  ASP A O   1 
ATOM   229  C CB  . ASP A 1 46  ? 135.960 132.800 141.435 1.00 36.37  ? 33  ASP A CB  1 
ATOM   230  C CG  . ASP A 1 46  ? 137.374 132.926 140.911 1.00 42.17  ? 33  ASP A CG  1 
ATOM   231  O OD1 . ASP A 1 46  ? 138.091 131.905 140.887 1.00 41.65  ? 33  ASP A OD1 1 
ATOM   232  O OD2 . ASP A 1 46  ? 137.771 134.043 140.520 1.00 46.87  ? 33  ASP A OD2 1 
ATOM   233  N N   . VAL A 1 47  ? 133.990 131.087 143.025 1.00 27.65  ? 34  VAL A N   1 
ATOM   234  C CA  . VAL A 1 47  ? 132.799 130.887 143.842 1.00 26.48  ? 34  VAL A CA  1 
ATOM   235  C C   . VAL A 1 47  ? 132.839 131.863 145.007 1.00 32.47  ? 34  VAL A C   1 
ATOM   236  O O   . VAL A 1 47  ? 133.866 131.987 145.682 1.00 40.06  ? 34  VAL A O   1 
ATOM   237  C CB  . VAL A 1 47  ? 132.698 129.440 144.354 1.00 30.56  ? 34  VAL A CB  1 
ATOM   238  C CG1 . VAL A 1 47  ? 131.651 129.335 145.442 1.00 33.53  ? 34  VAL A CG1 1 
ATOM   239  C CG2 . VAL A 1 47  ? 132.355 128.507 143.222 1.00 31.60  ? 34  VAL A CG2 1 
ATOM   240  N N   . VAL A 1 48  ? 131.723 132.549 145.244 1.00 31.61  ? 35  VAL A N   1 
ATOM   241  C CA  . VAL A 1 48  ? 131.590 133.486 146.353 1.00 30.61  ? 35  VAL A CA  1 
ATOM   242  C C   . VAL A 1 48  ? 130.460 133.016 147.259 1.00 32.54  ? 35  VAL A C   1 
ATOM   243  O O   . VAL A 1 48  ? 129.320 132.863 146.808 1.00 34.37  ? 35  VAL A O   1 
ATOM   244  C CB  . VAL A 1 48  ? 131.328 134.919 145.858 1.00 24.26  ? 35  VAL A CB  1 
ATOM   245  C CG1 . VAL A 1 48  ? 131.051 135.832 147.035 1.00 31.97  ? 35  VAL A CG1 1 
ATOM   246  C CG2 . VAL A 1 48  ? 132.514 135.423 145.058 1.00 26.92  ? 35  VAL A CG2 1 
ATOM   247  N N   . TYR A 1 49  ? 130.777 132.804 148.533 1.00 33.30  ? 36  TYR A N   1 
ATOM   248  C CA  . TYR A 1 49  ? 129.827 132.405 149.561 1.00 32.23  ? 36  TYR A CA  1 
ATOM   249  C C   . TYR A 1 49  ? 129.521 133.593 150.466 1.00 35.95  ? 36  TYR A C   1 
ATOM   250  O O   . TYR A 1 49  ? 129.995 134.709 150.248 1.00 38.92  ? 36  TYR A O   1 
ATOM   251  C CB  . TYR A 1 49  ? 130.376 131.239 150.386 1.00 35.01  ? 36  TYR A CB  1 
ATOM   252  C CG  . TYR A 1 49  ? 130.074 129.866 149.836 1.00 33.34  ? 36  TYR A CG  1 
ATOM   253  C CD1 . TYR A 1 49  ? 128.885 129.222 150.144 1.00 36.93  ? 36  TYR A CD1 1 
ATOM   254  C CD2 . TYR A 1 49  ? 130.987 129.205 149.028 1.00 32.18  ? 36  TYR A CD2 1 
ATOM   255  C CE1 . TYR A 1 49  ? 128.607 127.967 149.653 1.00 40.62  ? 36  TYR A CE1 1 
ATOM   256  C CE2 . TYR A 1 49  ? 130.718 127.948 148.533 1.00 33.70  ? 36  TYR A CE2 1 
ATOM   257  C CZ  . TYR A 1 49  ? 129.526 127.335 148.848 1.00 40.15  ? 36  TYR A CZ  1 
ATOM   258  O OH  . TYR A 1 49  ? 129.250 126.080 148.357 1.00 45.18  ? 36  TYR A OH  1 
ATOM   259  N N   . THR A 1 50  ? 128.718 133.338 151.497 1.00 38.91  ? 37  THR A N   1 
ATOM   260  C CA  . THR A 1 50  ? 128.495 134.310 152.557 1.00 45.77  ? 37  THR A CA  1 
ATOM   261  C C   . THR A 1 50  ? 128.214 133.556 153.850 1.00 50.55  ? 37  THR A C   1 
ATOM   262  O O   . THR A 1 50  ? 127.503 132.549 153.846 1.00 54.26  ? 37  THR A O   1 
ATOM   263  C CB  . THR A 1 50  ? 127.346 135.270 152.218 1.00 41.61  ? 37  THR A CB  1 
ATOM   264  O OG1 . THR A 1 50  ? 127.100 136.141 153.329 1.00 44.43  ? 37  THR A OG1 1 
ATOM   265  C CG2 . THR A 1 50  ? 126.075 134.506 151.878 1.00 43.21  ? 37  THR A CG2 1 
ATOM   266  N N   . TRP A 1 51  ? 128.780 134.045 154.952 1.00 51.79  ? 38  TRP A N   1 
ATOM   267  C CA  . TRP A 1 51  ? 128.700 133.352 156.232 1.00 60.57  ? 38  TRP A CA  1 
ATOM   268  C C   . TRP A 1 51  ? 128.531 134.366 157.351 1.00 69.85  ? 38  TRP A C   1 
ATOM   269  O O   . TRP A 1 51  ? 129.317 135.310 157.464 1.00 67.40  ? 38  TRP A O   1 
ATOM   270  C CB  . TRP A 1 51  ? 129.951 132.495 156.472 1.00 64.86  ? 38  TRP A CB  1 
ATOM   271  C CG  . TRP A 1 51  ? 130.007 131.803 157.815 1.00 70.77  ? 38  TRP A CG  1 
ATOM   272  C CD1 . TRP A 1 51  ? 128.960 131.530 158.650 1.00 68.97  ? 38  TRP A CD1 1 
ATOM   273  C CD2 . TRP A 1 51  ? 131.180 131.302 158.469 1.00 76.30  ? 38  TRP A CD2 1 
ATOM   274  N NE1 . TRP A 1 51  ? 129.411 130.893 159.781 1.00 69.93  ? 38  TRP A NE1 1 
ATOM   275  C CE2 . TRP A 1 51  ? 130.769 130.741 159.695 1.00 73.33  ? 38  TRP A CE2 1 
ATOM   276  C CE3 . TRP A 1 51  ? 132.538 131.275 158.137 1.00 80.70  ? 38  TRP A CE3 1 
ATOM   277  C CZ2 . TRP A 1 51  ? 131.667 130.159 160.587 1.00 76.05  ? 38  TRP A CZ2 1 
ATOM   278  C CZ3 . TRP A 1 51  ? 133.428 130.697 159.025 1.00 76.34  ? 38  TRP A CZ3 1 
ATOM   279  C CH2 . TRP A 1 51  ? 132.989 130.148 160.235 1.00 74.67  ? 38  TRP A CH2 1 
ATOM   280  N N   . VAL A 1 52  ? 127.504 134.160 158.172 1.00 79.08  ? 39  VAL A N   1 
ATOM   281  C CA  . VAL A 1 52  ? 127.233 134.979 159.345 1.00 81.70  ? 39  VAL A CA  1 
ATOM   282  C C   . VAL A 1 52  ? 126.994 134.050 160.527 1.00 87.39  ? 39  VAL A C   1 
ATOM   283  O O   . VAL A 1 52  ? 126.351 133.004 160.385 1.00 85.48  ? 39  VAL A O   1 
ATOM   284  C CB  . VAL A 1 52  ? 126.025 135.915 159.117 1.00 76.08  ? 39  VAL A CB  1 
ATOM   285  C CG1 . VAL A 1 52  ? 124.833 135.131 158.588 1.00 70.49  ? 39  VAL A CG1 1 
ATOM   286  C CG2 . VAL A 1 52  ? 125.660 136.651 160.396 1.00 76.99  ? 39  VAL A CG2 1 
ATOM   287  N N   . ASN A 1 53  ? 127.531 134.416 161.687 1.00 88.18  ? 40  ASN A N   1 
ATOM   288  C CA  . ASN A 1 53  ? 127.374 133.639 162.910 1.00 88.85  ? 40  ASN A CA  1 
ATOM   289  C C   . ASN A 1 53  ? 126.472 134.410 163.863 1.00 95.08  ? 40  ASN A C   1 
ATOM   290  O O   . ASN A 1 53  ? 126.838 135.495 164.326 1.00 101.09 ? 40  ASN A O   1 
ATOM   291  C CB  . ASN A 1 53  ? 128.731 133.361 163.557 1.00 90.59  ? 40  ASN A CB  1 
ATOM   292  C CG  . ASN A 1 53  ? 128.669 132.256 164.592 1.00 99.38  ? 40  ASN A CG  1 
ATOM   293  O OD1 . ASN A 1 53  ? 127.593 131.879 165.054 1.00 103.64 ? 40  ASN A OD1 1 
ATOM   294  N ND2 . ASN A 1 53  ? 129.831 131.731 164.963 1.00 95.99  ? 40  ASN A ND2 1 
ATOM   295  N N   . GLY A 1 54  ? 125.299 133.853 164.149 1.00 98.92  ? 41  GLY A N   1 
ATOM   296  C CA  . GLY A 1 54  ? 124.375 134.485 165.070 1.00 109.85 ? 41  GLY A CA  1 
ATOM   297  C C   . GLY A 1 54  ? 124.577 134.040 166.503 1.00 114.46 ? 41  GLY A C   1 
ATOM   298  O O   . GLY A 1 54  ? 123.707 133.384 167.085 1.00 110.71 ? 41  GLY A O   1 
ATOM   299  N N   . THR A 1 55  ? 125.723 134.391 167.083 1.00 117.78 ? 42  THR A N   1 
ATOM   300  C CA  . THR A 1 55  ? 126.053 134.014 168.448 1.00 118.39 ? 42  THR A CA  1 
ATOM   301  C C   . THR A 1 55  ? 126.774 135.160 169.140 1.00 123.22 ? 42  THR A C   1 
ATOM   302  O O   . THR A 1 55  ? 127.644 135.805 168.547 1.00 120.73 ? 42  THR A O   1 
ATOM   303  C CB  . THR A 1 55  ? 126.937 132.756 168.497 1.00 114.27 ? 42  THR A CB  1 
ATOM   304  O OG1 . THR A 1 55  ? 128.035 132.902 167.587 1.00 111.78 ? 42  THR A OG1 1 
ATOM   305  C CG2 . THR A 1 55  ? 126.138 131.512 168.134 1.00 109.84 ? 42  THR A CG2 1 
ATOM   306  N N   . ASP A 1 56  ? 126.399 135.402 170.397 1.00 127.83 ? 43  ASP A N   1 
ATOM   307  C CA  . ASP A 1 56  ? 127.105 136.318 171.286 1.00 132.63 ? 43  ASP A CA  1 
ATOM   308  C C   . ASP A 1 56  ? 127.153 137.747 170.754 1.00 131.62 ? 43  ASP A C   1 
ATOM   309  O O   . ASP A 1 56  ? 126.186 138.506 170.895 1.00 131.31 ? 43  ASP A O   1 
ATOM   310  C CB  . ASP A 1 56  ? 128.525 135.796 171.540 1.00 132.34 ? 43  ASP A CB  1 
ATOM   311  C CG  . ASP A 1 56  ? 129.278 136.613 172.572 1.00 131.63 ? 43  ASP A CG  1 
ATOM   312  O OD1 . ASP A 1 56  ? 128.899 136.568 173.760 1.00 130.40 ? 43  ASP A OD1 1 
ATOM   313  O OD2 . ASP A 1 56  ? 130.255 137.294 172.192 1.00 131.27 ? 43  ASP A OD2 1 
ATOM   314  N N   . LEU A 1 57  ? 128.275 138.114 170.127 1.00 129.84 ? 44  LEU A N   1 
ATOM   315  C CA  . LEU A 1 57  ? 128.545 139.521 169.847 1.00 128.84 ? 44  LEU A CA  1 
ATOM   316  C C   . LEU A 1 57  ? 127.610 140.080 168.781 1.00 132.10 ? 44  LEU A C   1 
ATOM   317  O O   . LEU A 1 57  ? 127.151 141.220 168.896 1.00 133.16 ? 44  LEU A O   1 
ATOM   318  C CB  . LEU A 1 57  ? 130.009 139.705 169.441 1.00 125.53 ? 44  LEU A CB  1 
ATOM   319  C CG  . LEU A 1 57  ? 130.556 138.961 168.221 1.00 120.97 ? 44  LEU A CG  1 
ATOM   320  C CD1 . LEU A 1 57  ? 130.532 139.847 166.982 1.00 119.37 ? 44  LEU A CD1 1 
ATOM   321  C CD2 . LEU A 1 57  ? 131.962 138.451 168.494 1.00 115.96 ? 44  LEU A CD2 1 
ATOM   322  N N   . GLU A 1 58  ? 127.331 139.308 167.728 1.00 131.12 ? 45  GLU A N   1 
ATOM   323  C CA  . GLU A 1 58  ? 126.451 139.803 166.672 1.00 129.28 ? 45  GLU A CA  1 
ATOM   324  C C   . GLU A 1 58  ? 125.044 140.057 167.202 1.00 133.27 ? 45  GLU A C   1 
ATOM   325  O O   . GLU A 1 58  ? 124.434 141.094 166.905 1.00 133.49 ? 45  GLU A O   1 
ATOM   326  C CB  . GLU A 1 58  ? 126.418 138.811 165.509 1.00 123.36 ? 45  GLU A CB  1 
ATOM   327  C CG  . GLU A 1 58  ? 127.777 138.546 164.878 1.00 117.93 ? 45  GLU A CG  1 
ATOM   328  C CD  . GLU A 1 58  ? 128.318 139.746 164.124 1.00 109.81 ? 45  GLU A CD  1 
ATOM   329  O OE1 . GLU A 1 58  ? 127.525 140.651 163.790 1.00 112.33 ? 45  GLU A OE1 1 
ATOM   330  O OE2 . GLU A 1 58  ? 129.540 139.782 163.862 1.00 103.66 ? 45  GLU A OE2 1 
ATOM   331  N N   . LEU A 1 59  ? 124.517 139.122 167.998 1.00 133.81 ? 46  LEU A N   1 
ATOM   332  C CA  . LEU A 1 59  ? 123.203 139.319 168.598 1.00 134.41 ? 46  LEU A CA  1 
ATOM   333  C C   . LEU A 1 59  ? 123.213 140.499 169.558 1.00 138.13 ? 46  LEU A C   1 
ATOM   334  O O   . LEU A 1 59  ? 122.229 141.242 169.644 1.00 142.00 ? 46  LEU A O   1 
ATOM   335  C CB  . LEU A 1 59  ? 122.755 138.044 169.312 1.00 129.56 ? 46  LEU A CB  1 
ATOM   336  C CG  . LEU A 1 59  ? 122.473 136.825 168.432 1.00 123.73 ? 46  LEU A CG  1 
ATOM   337  C CD1 . LEU A 1 59  ? 122.076 135.631 169.284 1.00 121.35 ? 46  LEU A CD1 1 
ATOM   338  C CD2 . LEU A 1 59  ? 121.392 137.135 167.408 1.00 122.66 ? 46  LEU A CD2 1 
ATOM   339  N N   . LEU A 1 60  ? 124.316 140.690 170.286 1.00 136.73 ? 47  LEU A N   1 
ATOM   340  C CA  . LEU A 1 60  ? 124.420 141.846 171.172 1.00 139.32 ? 47  LEU A CA  1 
ATOM   341  C C   . LEU A 1 60  ? 124.378 143.148 170.381 1.00 142.08 ? 47  LEU A C   1 
ATOM   342  O O   . LEU A 1 60  ? 123.713 144.110 170.787 1.00 146.77 ? 47  LEU A O   1 
ATOM   343  C CB  . LEU A 1 60  ? 125.703 141.751 172.001 1.00 138.08 ? 47  LEU A CB  1 
ATOM   344  C CG  . LEU A 1 60  ? 125.871 142.662 173.221 1.00 133.16 ? 47  LEU A CG  1 
ATOM   345  C CD1 . LEU A 1 60  ? 126.751 141.979 174.255 1.00 120.88 ? 47  LEU A CD1 1 
ATOM   346  C CD2 . LEU A 1 60  ? 126.463 144.011 172.836 1.00 131.17 ? 47  LEU A CD2 1 
ATOM   347  N N   . LYS A 1 61  ? 125.087 143.199 169.249 1.00 140.98 ? 48  LYS A N   1 
ATOM   348  C CA  . LYS A 1 61  ? 125.075 144.407 168.428 1.00 142.20 ? 48  LYS A CA  1 
ATOM   349  C C   . LYS A 1 61  ? 123.679 144.673 167.879 1.00 145.38 ? 48  LYS A C   1 
ATOM   350  O O   . LYS A 1 61  ? 123.212 145.817 167.875 1.00 146.27 ? 48  LYS A O   1 
ATOM   351  C CB  . LYS A 1 61  ? 126.075 144.301 167.273 1.00 135.46 ? 48  LYS A CB  1 
ATOM   352  C CG  . LYS A 1 61  ? 127.509 143.952 167.658 1.00 135.93 ? 48  LYS A CG  1 
ATOM   353  C CD  . LYS A 1 61  ? 127.932 144.552 168.987 1.00 135.22 ? 48  LYS A CD  1 
ATOM   354  C CE  . LYS A 1 61  ? 129.228 143.921 169.470 1.00 131.68 ? 48  LYS A CE  1 
ATOM   355  N NZ  . LYS A 1 61  ? 129.222 143.709 170.942 1.00 131.91 ? 48  LYS A NZ  1 
ATOM   356  N N   . GLU A 1 62  ? 122.992 143.622 167.421 1.00 147.44 ? 49  GLU A N   1 
ATOM   357  C CA  . GLU A 1 62  ? 121.630 143.803 166.926 1.00 149.48 ? 49  GLU A CA  1 
ATOM   358  C C   . GLU A 1 62  ? 120.704 144.297 168.032 1.00 153.54 ? 49  GLU A C   1 
ATOM   359  O O   . GLU A 1 62  ? 119.875 145.186 167.805 1.00 154.95 ? 49  GLU A O   1 
ATOM   360  C CB  . GLU A 1 62  ? 121.108 142.500 166.323 1.00 143.03 ? 49  GLU A CB  1 
ATOM   361  C CG  . GLU A 1 62  ? 121.926 141.958 165.153 1.00 140.78 ? 49  GLU A CG  1 
ATOM   362  C CD  . GLU A 1 62  ? 121.795 142.792 163.889 1.00 130.08 ? 49  GLU A CD  1 
ATOM   363  O OE1 . GLU A 1 62  ? 122.351 143.910 163.842 1.00 125.05 ? 49  GLU A OE1 1 
ATOM   364  O OE2 . GLU A 1 62  ? 121.134 142.326 162.937 1.00 125.90 ? 49  GLU A OE2 1 
ATOM   365  N N   . LEU A 1 63  ? 120.830 143.736 169.237 1.00 153.54 ? 50  LEU A N   1 
ATOM   366  C CA  . LEU A 1 63  ? 119.968 144.150 170.340 1.00 153.94 ? 50  LEU A CA  1 
ATOM   367  C C   . LEU A 1 63  ? 120.218 145.601 170.731 1.00 158.84 ? 50  LEU A C   1 
ATOM   368  O O   . LEU A 1 63  ? 119.267 146.364 170.946 1.00 161.28 ? 50  LEU A O   1 
ATOM   369  C CB  . LEU A 1 63  ? 120.174 143.231 171.543 1.00 149.68 ? 50  LEU A CB  1 
ATOM   370  C CG  . LEU A 1 63  ? 119.187 143.443 172.693 1.00 150.07 ? 50  LEU A CG  1 
ATOM   371  C CD1 . LEU A 1 63  ? 117.763 143.208 172.213 1.00 153.82 ? 50  LEU A CD1 1 
ATOM   372  C CD2 . LEU A 1 63  ? 119.521 142.531 173.860 1.00 141.83 ? 50  LEU A CD2 1 
ATOM   373  N N   . THR A 1 64  ? 121.488 146.008 170.829 1.00 159.01 ? 51  THR A N   1 
ATOM   374  C CA  . THR A 1 64  ? 121.762 147.392 171.203 1.00 159.33 ? 51  THR A CA  1 
ATOM   375  C C   . THR A 1 64  ? 121.370 148.353 170.089 1.00 157.99 ? 51  THR A C   1 
ATOM   376  O O   . THR A 1 64  ? 120.962 149.486 170.367 1.00 158.64 ? 51  THR A O   1 
ATOM   377  C CB  . THR A 1 64  ? 123.235 147.582 171.587 1.00 160.29 ? 51  THR A CB  1 
ATOM   378  O OG1 . THR A 1 64  ? 123.438 148.924 172.051 1.00 164.37 ? 51  THR A OG1 1 
ATOM   379  C CG2 . THR A 1 64  ? 124.155 147.327 170.410 1.00 157.54 ? 51  THR A CG2 1 
ATOM   380  N N   . GLU A 1 65  ? 121.452 147.915 168.829 1.00 155.43 ? 52  GLU A N   1 
ATOM   381  C CA  . GLU A 1 65  ? 120.968 148.741 167.731 1.00 155.45 ? 52  GLU A CA  1 
ATOM   382  C C   . GLU A 1 65  ? 119.455 148.904 167.786 1.00 157.39 ? 52  GLU A C   1 
ATOM   383  O O   . GLU A 1 65  ? 118.938 149.995 167.520 1.00 158.69 ? 52  GLU A O   1 
ATOM   384  C CB  . GLU A 1 65  ? 121.409 148.133 166.397 1.00 152.89 ? 52  GLU A CB  1 
ATOM   385  C CG  . GLU A 1 65  ? 120.851 148.815 165.162 1.00 153.65 ? 52  GLU A CG  1 
ATOM   386  C CD  . GLU A 1 65  ? 119.575 148.165 164.672 1.00 154.44 ? 52  GLU A CD  1 
ATOM   387  O OE1 . GLU A 1 65  ? 119.269 147.043 165.131 1.00 155.78 ? 52  GLU A OE1 1 
ATOM   388  O OE2 . GLU A 1 65  ? 118.879 148.775 163.834 1.00 148.90 ? 52  GLU A OE2 1 
ATOM   389  N N   . LEU A 1 66  ? 118.734 147.839 168.146 1.00 156.73 ? 53  LEU A N   1 
ATOM   390  C CA  . LEU A 1 66  ? 117.292 147.955 168.341 1.00 156.04 ? 53  LEU A CA  1 
ATOM   391  C C   . LEU A 1 66  ? 116.965 148.905 169.486 1.00 161.25 ? 53  LEU A C   1 
ATOM   392  O O   . LEU A 1 66  ? 116.031 149.710 169.388 1.00 161.91 ? 53  LEU A O   1 
ATOM   393  C CB  . LEU A 1 66  ? 116.682 146.579 168.598 1.00 152.04 ? 53  LEU A CB  1 
ATOM   394  C CG  . LEU A 1 66  ? 116.725 145.597 167.425 1.00 149.61 ? 53  LEU A CG  1 
ATOM   395  C CD1 . LEU A 1 66  ? 116.162 144.245 167.836 1.00 149.56 ? 53  LEU A CD1 1 
ATOM   396  C CD2 . LEU A 1 66  ? 115.966 146.164 166.237 1.00 146.58 ? 53  LEU A CD2 1 
ATOM   397  N N   . LYS A 1 67  ? 117.716 148.816 170.587 1.00 164.29 ? 54  LYS A N   1 
ATOM   398  C CA  . LYS A 1 67  ? 117.477 149.710 171.718 1.00 164.29 ? 54  LYS A CA  1 
ATOM   399  C C   . LYS A 1 67  ? 117.746 151.164 171.342 1.00 163.53 ? 54  LYS A C   1 
ATOM   400  O O   . LYS A 1 67  ? 116.973 152.060 171.701 1.00 163.27 ? 54  LYS A O   1 
ATOM   401  C CB  . LYS A 1 67  ? 118.341 149.305 172.913 1.00 162.28 ? 54  LYS A CB  1 
ATOM   402  C CG  . LYS A 1 67  ? 118.074 147.902 173.434 1.00 158.84 ? 54  LYS A CG  1 
ATOM   403  C CD  . LYS A 1 67  ? 116.595 147.677 173.703 1.00 159.82 ? 54  LYS A CD  1 
ATOM   404  C CE  . LYS A 1 67  ? 116.303 146.209 173.969 1.00 159.49 ? 54  LYS A CE  1 
ATOM   405  N NZ  . LYS A 1 67  ? 114.841 145.935 174.044 1.00 160.42 ? 54  LYS A NZ  1 
ATOM   406  N N   . ARG A 1 68  ? 118.838 151.419 170.615 1.00 163.51 ? 55  ARG A N   1 
ATOM   407  C CA  . ARG A 1 68  ? 119.182 152.791 170.257 1.00 164.69 ? 55  ARG A CA  1 
ATOM   408  C C   . ARG A 1 68  ? 118.240 153.350 169.198 1.00 165.07 ? 55  ARG A C   1 
ATOM   409  O O   . ARG A 1 68  ? 118.012 154.564 169.158 1.00 165.47 ? 55  ARG A O   1 
ATOM   410  C CB  . ARG A 1 68  ? 120.637 152.869 169.785 1.00 164.21 ? 55  ARG A CB  1 
ATOM   411  C CG  . ARG A 1 68  ? 120.891 152.330 168.387 1.00 162.32 ? 55  ARG A CG  1 
ATOM   412  C CD  . ARG A 1 68  ? 122.371 152.342 168.048 1.00 160.46 ? 55  ARG A CD  1 
ATOM   413  N NE  . ARG A 1 68  ? 123.141 151.496 168.950 1.00 160.89 ? 55  ARG A NE  1 
ATOM   414  C CZ  . ARG A 1 68  ? 124.430 151.221 168.804 1.00 158.53 ? 55  ARG A CZ  1 
ATOM   415  N NH1 . ARG A 1 68  ? 125.126 151.697 167.785 1.00 157.60 ? 55  ARG A NH1 1 
ATOM   416  N NH2 . ARG A 1 68  ? 125.035 150.451 169.703 1.00 155.82 ? 55  ARG A NH2 1 
ATOM   417  N N   . SER A 1 69  ? 117.689 152.496 168.341 1.00 162.72 ? 56  SER A N   1 
ATOM   418  C CA  . SER A 1 69  ? 116.779 152.952 167.296 1.00 158.94 ? 56  SER A CA  1 
ATOM   419  C C   . SER A 1 69  ? 115.361 152.440 167.527 1.00 157.45 ? 56  SER A C   1 
ATOM   420  O O   . SER A 1 69  ? 114.405 153.215 167.533 1.00 156.96 ? 56  SER A O   1 
ATOM   421  C CB  . SER A 1 69  ? 117.281 152.508 165.922 1.00 156.41 ? 56  SER A CB  1 
ATOM   422  O OG  . SER A 1 69  ? 118.577 153.019 165.667 1.00 157.06 ? 56  SER A OG  1 
ATOM   423  N N   . ASN A 1 102 ? 122.085 125.079 160.408 1.00 82.79  ? 89  ASN A N   1 
ATOM   424  C CA  . ASN A 1 102 ? 123.421 125.286 160.949 1.00 83.19  ? 89  ASN A CA  1 
ATOM   425  C C   . ASN A 1 102 ? 124.377 124.303 160.305 1.00 74.57  ? 89  ASN A C   1 
ATOM   426  O O   . ASN A 1 102 ? 123.957 123.254 159.825 1.00 71.99  ? 89  ASN A O   1 
ATOM   427  C CB  . ASN A 1 102 ? 123.434 125.110 162.471 1.00 85.52  ? 89  ASN A CB  1 
ATOM   428  C CG  . ASN A 1 102 ? 124.773 125.480 163.091 1.00 79.72  ? 89  ASN A CG  1 
ATOM   429  O OD1 . ASN A 1 102 ? 125.552 126.221 162.501 1.00 74.22  ? 89  ASN A OD1 1 
ATOM   430  N ND2 . ASN A 1 102 ? 125.050 124.950 164.277 1.00 76.96  ? 89  ASN A ND2 1 
ATOM   431  N N   . GLU A 1 103 ? 125.665 124.639 160.303 1.00 68.96  ? 90  GLU A N   1 
ATOM   432  C CA  . GLU A 1 103 ? 126.716 123.750 159.803 1.00 68.44  ? 90  GLU A CA  1 
ATOM   433  C C   . GLU A 1 103 ? 126.488 123.380 158.344 1.00 69.83  ? 90  GLU A C   1 
ATOM   434  O O   . GLU A 1 103 ? 126.923 122.322 157.882 1.00 68.32  ? 90  GLU A O   1 
ATOM   435  C CB  . GLU A 1 103 ? 126.847 122.488 160.665 1.00 65.01  ? 90  GLU A CB  1 
ATOM   436  C CG  . GLU A 1 103 ? 128.210 121.773 160.593 1.00 63.44  ? 90  GLU A CG  1 
ATOM   437  C CD  . GLU A 1 103 ? 129.423 122.693 160.810 1.00 71.16  ? 90  GLU A CD  1 
ATOM   438  O OE1 . GLU A 1 103 ? 129.300 123.707 161.524 1.00 77.50  ? 90  GLU A OE1 1 
ATOM   439  O OE2 . GLU A 1 103 ? 130.508 122.385 160.289 1.00 68.32  ? 90  GLU A OE2 1 
ATOM   440  N N   . GLU A 1 104 ? 125.820 124.266 157.609 1.00 65.92  ? 91  GLU A N   1 
ATOM   441  C CA  . GLU A 1 104 ? 125.579 124.043 156.194 1.00 58.92  ? 91  GLU A CA  1 
ATOM   442  C C   . GLU A 1 104 ? 126.781 124.392 155.330 1.00 58.47  ? 91  GLU A C   1 
ATOM   443  O O   . GLU A 1 104 ? 126.936 123.807 154.255 1.00 59.88  ? 91  GLU A O   1 
ATOM   444  C CB  . GLU A 1 104 ? 124.358 124.851 155.753 1.00 56.04  ? 91  GLU A CB  1 
ATOM   445  C CG  . GLU A 1 104 ? 123.188 124.738 156.721 1.00 64.37  ? 91  GLU A CG  1 
ATOM   446  C CD  . GLU A 1 104 ? 122.048 125.673 156.376 1.00 72.23  ? 91  GLU A CD  1 
ATOM   447  O OE1 . GLU A 1 104 ? 121.757 125.841 155.174 1.00 64.56  ? 91  GLU A OE1 1 
ATOM   448  O OE2 . GLU A 1 104 ? 121.442 126.239 157.312 1.00 81.83  ? 91  GLU A OE2 1 
ATOM   449  N N   . LEU A 1 105 ? 127.635 125.317 155.776 1.00 60.13  ? 92  LEU A N   1 
ATOM   450  C CA  . LEU A 1 105 ? 128.743 125.770 154.939 1.00 58.86  ? 92  LEU A CA  1 
ATOM   451  C C   . LEU A 1 105 ? 129.730 124.643 154.652 1.00 56.81  ? 92  LEU A C   1 
ATOM   452  O O   . LEU A 1 105 ? 130.268 124.547 153.540 1.00 54.53  ? 92  LEU A O   1 
ATOM   453  C CB  . LEU A 1 105 ? 129.444 126.956 155.600 1.00 56.81  ? 92  LEU A CB  1 
ATOM   454  C CG  . LEU A 1 105 ? 130.514 127.685 154.788 1.00 57.57  ? 92  LEU A CG  1 
ATOM   455  C CD1 . LEU A 1 105 ? 129.922 128.187 153.496 1.00 54.14  ? 92  LEU A CD1 1 
ATOM   456  C CD2 . LEU A 1 105 ? 131.102 128.845 155.575 1.00 58.50  ? 92  LEU A CD2 1 
ATOM   457  N N   . ARG A 1 106 ? 129.996 123.789 155.644 1.00 55.48  ? 93  ARG A N   1 
ATOM   458  C CA  . ARG A 1 106 ? 130.895 122.660 155.420 1.00 56.37  ? 93  ARG A CA  1 
ATOM   459  C C   . ARG A 1 106 ? 130.374 121.746 154.319 1.00 55.15  ? 93  ARG A C   1 
ATOM   460  O O   . ARG A 1 106 ? 131.118 121.367 153.409 1.00 53.02  ? 93  ARG A O   1 
ATOM   461  C CB  . ARG A 1 106 ? 131.101 121.870 156.711 1.00 58.89  ? 93  ARG A CB  1 
ATOM   462  C CG  . ARG A 1 106 ? 131.992 120.653 156.519 1.00 58.73  ? 93  ARG A CG  1 
ATOM   463  C CD  . ARG A 1 106 ? 132.635 120.215 157.815 1.00 59.29  ? 93  ARG A CD  1 
ATOM   464  N NE  . ARG A 1 106 ? 131.703 119.506 158.675 1.00 71.03  ? 93  ARG A NE  1 
ATOM   465  C CZ  . ARG A 1 106 ? 132.019 118.987 159.852 1.00 80.49  ? 93  ARG A CZ  1 
ATOM   466  N NH1 . ARG A 1 106 ? 133.256 119.050 160.322 1.00 74.51  ? 93  ARG A NH1 1 
ATOM   467  N NH2 . ARG A 1 106 ? 131.068 118.395 160.580 1.00 84.14  ? 93  ARG A NH2 1 
ATOM   468  N N   . TYR A 1 107 ? 129.096 121.368 154.393 1.00 54.36  ? 94  TYR A N   1 
ATOM   469  C CA  . TYR A 1 107 ? 128.550 120.477 153.375 1.00 53.97  ? 94  TYR A CA  1 
ATOM   470  C C   . TYR A 1 107 ? 128.442 121.174 152.026 1.00 52.82  ? 94  TYR A C   1 
ATOM   471  O O   . TYR A 1 107 ? 128.552 120.519 150.986 1.00 52.10  ? 94  TYR A O   1 
ATOM   472  C CB  . TYR A 1 107 ? 127.198 119.923 153.824 1.00 58.62  ? 94  TYR A CB  1 
ATOM   473  C CG  . TYR A 1 107 ? 127.290 119.172 155.133 1.00 64.02  ? 94  TYR A CG  1 
ATOM   474  C CD1 . TYR A 1 107 ? 127.924 117.937 155.206 1.00 61.37  ? 94  TYR A CD1 1 
ATOM   475  C CD2 . TYR A 1 107 ? 126.767 119.708 156.299 1.00 64.18  ? 94  TYR A CD2 1 
ATOM   476  C CE1 . TYR A 1 107 ? 128.024 117.257 156.405 1.00 62.95  ? 94  TYR A CE1 1 
ATOM   477  C CE2 . TYR A 1 107 ? 126.862 119.037 157.501 1.00 65.22  ? 94  TYR A CE2 1 
ATOM   478  C CZ  . TYR A 1 107 ? 127.491 117.812 157.549 1.00 67.31  ? 94  TYR A CZ  1 
ATOM   479  O OH  . TYR A 1 107 ? 127.582 117.144 158.748 1.00 70.55  ? 94  TYR A OH  1 
ATOM   480  N N   . SER A 1 108 ? 128.252 122.494 152.016 1.00 52.26  ? 95  SER A N   1 
ATOM   481  C CA  . SER A 1 108 ? 128.268 123.224 150.752 1.00 44.95  ? 95  SER A CA  1 
ATOM   482  C C   . SER A 1 108 ? 129.642 123.150 150.096 1.00 44.83  ? 95  SER A C   1 
ATOM   483  O O   . SER A 1 108 ? 129.756 122.906 148.889 1.00 45.72  ? 95  SER A O   1 
ATOM   484  C CB  . SER A 1 108 ? 127.853 124.677 150.977 1.00 43.31  ? 95  SER A CB  1 
ATOM   485  O OG  . SER A 1 108 ? 126.526 124.761 151.467 1.00 47.36  ? 95  SER A OG  1 
ATOM   486  N N   . LEU A 1 109 ? 130.704 123.347 150.880 1.00 49.19  ? 96  LEU A N   1 
ATOM   487  C CA  . LEU A 1 109 ? 132.046 123.217 150.318 1.00 46.71  ? 96  LEU A CA  1 
ATOM   488  C C   . LEU A 1 109 ? 132.347 121.779 149.913 1.00 48.44  ? 96  LEU A C   1 
ATOM   489  O O   . LEU A 1 109 ? 133.064 121.546 148.931 1.00 45.62  ? 96  LEU A O   1 
ATOM   490  C CB  . LEU A 1 109 ? 133.095 123.711 151.310 1.00 39.20  ? 96  LEU A CB  1 
ATOM   491  C CG  . LEU A 1 109 ? 133.037 125.200 151.641 1.00 38.24  ? 96  LEU A CG  1 
ATOM   492  C CD1 . LEU A 1 109 ? 134.021 125.554 152.739 1.00 42.10  ? 96  LEU A CD1 1 
ATOM   493  C CD2 . LEU A 1 109 ? 133.296 126.021 150.390 1.00 40.84  ? 96  LEU A CD2 1 
ATOM   494  N N   . ARG A 1 110 ? 131.816 120.806 150.653 1.00 47.52  ? 97  ARG A N   1 
ATOM   495  C CA  . ARG A 1 110 ? 131.994 119.412 150.264 1.00 44.06  ? 97  ARG A CA  1 
ATOM   496  C C   . ARG A 1 110 ? 131.303 119.125 148.937 1.00 45.13  ? 97  ARG A C   1 
ATOM   497  O O   . ARG A 1 110 ? 131.835 118.391 148.097 1.00 48.42  ? 97  ARG A O   1 
ATOM   498  C CB  . ARG A 1 110 ? 131.485 118.493 151.373 1.00 44.57  ? 97  ARG A CB  1 
ATOM   499  C CG  . ARG A 1 110 ? 132.412 118.477 152.581 1.00 52.04  ? 97  ARG A CG  1 
ATOM   500  C CD  . ARG A 1 110 ? 131.999 117.460 153.630 1.00 57.19  ? 97  ARG A CD  1 
ATOM   501  N NE  . ARG A 1 110 ? 133.161 116.880 154.294 1.00 59.39  ? 97  ARG A NE  1 
ATOM   502  C CZ  . ARG A 1 110 ? 133.114 116.202 155.433 1.00 59.48  ? 97  ARG A CZ  1 
ATOM   503  N NH1 . ARG A 1 110 ? 131.980 116.042 156.094 1.00 59.82  ? 97  ARG A NH1 1 
ATOM   504  N NH2 . ARG A 1 110 ? 134.234 115.675 155.921 1.00 60.48  ? 97  ARG A NH2 1 
ATOM   505  N N   . SER A 1 111 ? 130.121 119.708 148.726 1.00 45.37  ? 98  SER A N   1 
ATOM   506  C CA  . SER A 1 111 ? 129.454 119.596 147.433 1.00 44.07  ? 98  SER A CA  1 
ATOM   507  C C   . SER A 1 111 ? 130.266 120.270 146.337 1.00 40.22  ? 98  SER A C   1 
ATOM   508  O O   . SER A 1 111 ? 130.325 119.776 145.207 1.00 40.37  ? 98  SER A O   1 
ATOM   509  C CB  . SER A 1 111 ? 128.054 120.203 147.512 1.00 43.43  ? 98  SER A CB  1 
ATOM   510  O OG  . SER A 1 111 ? 128.121 121.591 147.785 1.00 44.51  ? 98  SER A OG  1 
ATOM   511  N N   . ILE A 1 112 ? 130.884 121.411 146.647 1.00 42.03  ? 99  ILE A N   1 
ATOM   512  C CA  . ILE A 1 112 ? 131.758 122.074 145.681 1.00 35.94  ? 99  ILE A CA  1 
ATOM   513  C C   . ILE A 1 112 ? 132.888 121.141 145.264 1.00 38.80  ? 99  ILE A C   1 
ATOM   514  O O   . ILE A 1 112 ? 133.199 121.001 144.076 1.00 42.88  ? 99  ILE A O   1 
ATOM   515  C CB  . ILE A 1 112 ? 132.308 123.386 146.267 1.00 37.94  ? 99  ILE A CB  1 
ATOM   516  C CG1 . ILE A 1 112 ? 131.203 124.433 146.372 1.00 39.06  ? 99  ILE A CG1 1 
ATOM   517  C CG2 . ILE A 1 112 ? 133.459 123.904 145.424 1.00 34.39  ? 99  ILE A CG2 1 
ATOM   518  C CD1 . ILE A 1 112 ? 130.735 124.945 145.042 1.00 36.23  ? 99  ILE A CD1 1 
ATOM   519  N N   . GLU A 1 113 ? 133.519 120.492 146.242 1.00 38.61  ? 100 GLU A N   1 
ATOM   520  C CA  . GLU A 1 113 ? 134.609 119.567 145.944 1.00 39.32  ? 100 GLU A CA  1 
ATOM   521  C C   . GLU A 1 113 ? 134.125 118.366 145.136 1.00 44.45  ? 100 GLU A C   1 
ATOM   522  O O   . GLU A 1 113 ? 134.802 117.923 144.201 1.00 44.61  ? 100 GLU A O   1 
ATOM   523  C CB  . GLU A 1 113 ? 135.272 119.117 147.247 1.00 42.27  ? 100 GLU A CB  1 
ATOM   524  C CG  . GLU A 1 113 ? 136.171 117.893 147.130 1.00 49.84  ? 100 GLU A CG  1 
ATOM   525  C CD  . GLU A 1 113 ? 137.430 118.150 146.325 1.00 55.92  ? 100 GLU A CD  1 
ATOM   526  O OE1 . GLU A 1 113 ? 137.412 117.934 145.095 1.00 52.98  ? 100 GLU A OE1 1 
ATOM   527  O OE2 . GLU A 1 113 ? 138.441 118.567 146.924 1.00 61.49  ? 100 GLU A OE2 1 
ATOM   528  N N   . ARG A 1 114 ? 132.956 117.828 145.480 1.00 44.20  ? 101 ARG A N   1 
ATOM   529  C CA  . ARG A 1 114 ? 132.497 116.576 144.884 1.00 40.82  ? 101 ARG A CA  1 
ATOM   530  C C   . ARG A 1 114 ? 131.880 116.780 143.502 1.00 38.25  ? 101 ARG A C   1 
ATOM   531  O O   . ARG A 1 114 ? 132.345 116.204 142.513 1.00 36.27  ? 101 ARG A O   1 
ATOM   532  C CB  . ARG A 1 114 ? 131.498 115.895 145.827 1.00 43.23  ? 101 ARG A CB  1 
ATOM   533  C CG  . ARG A 1 114 ? 130.785 114.681 145.249 1.00 45.50  ? 101 ARG A CG  1 
ATOM   534  C CD  . ARG A 1 114 ? 131.749 113.562 144.880 1.00 42.58  ? 101 ARG A CD  1 
ATOM   535  N NE  . ARG A 1 114 ? 131.111 112.254 144.974 1.00 45.83  ? 101 ARG A NE  1 
ATOM   536  C CZ  . ARG A 1 114 ? 130.385 111.698 144.015 1.00 47.00  ? 101 ARG A CZ  1 
ATOM   537  N NH1 . ARG A 1 114 ? 130.179 112.309 142.860 1.00 45.01  ? 101 ARG A NH1 1 
ATOM   538  N NH2 . ARG A 1 114 ? 129.851 110.497 144.220 1.00 47.18  ? 101 ARG A NH2 1 
ATOM   539  N N   . HIS A 1 115 ? 130.824 117.591 143.417 1.00 41.27  ? 102 HIS A N   1 
ATOM   540  C CA  . HIS A 1 115 ? 130.018 117.694 142.206 1.00 42.94  ? 102 HIS A CA  1 
ATOM   541  C C   . HIS A 1 115 ? 130.464 118.791 141.249 1.00 37.77  ? 102 HIS A C   1 
ATOM   542  O O   . HIS A 1 115 ? 130.172 118.698 140.052 1.00 40.81  ? 102 HIS A O   1 
ATOM   543  C CB  . HIS A 1 115 ? 128.550 117.926 142.572 1.00 42.69  ? 102 HIS A CB  1 
ATOM   544  C CG  . HIS A 1 115 ? 127.906 116.751 143.234 1.00 42.14  ? 102 HIS A CG  1 
ATOM   545  N ND1 . HIS A 1 115 ? 126.918 116.879 144.185 1.00 43.91  ? 102 HIS A ND1 1 
ATOM   546  C CD2 . HIS A 1 115 ? 128.109 115.421 143.079 1.00 47.06  ? 102 HIS A CD2 1 
ATOM   547  C CE1 . HIS A 1 115 ? 126.542 115.679 144.590 1.00 47.40  ? 102 HIS A CE1 1 
ATOM   548  N NE2 . HIS A 1 115 ? 127.249 114.777 143.934 1.00 49.23  ? 102 HIS A NE2 1 
ATOM   549  N N   . ALA A 1 116 ? 131.157 119.820 141.729 1.00 33.06  ? 103 ALA A N   1 
ATOM   550  C CA  . ALA A 1 116 ? 131.563 120.954 140.899 1.00 32.13  ? 103 ALA A CA  1 
ATOM   551  C C   . ALA A 1 116 ? 133.062 121.176 141.044 1.00 34.19  ? 103 ALA A C   1 
ATOM   552  O O   . ALA A 1 116 ? 133.505 122.179 141.614 1.00 37.67  ? 103 ALA A O   1 
ATOM   553  C CB  . ALA A 1 116 ? 130.784 122.214 141.279 1.00 33.45  ? 103 ALA A CB  1 
ATOM   554  N N   . PRO A 1 117 ? 133.876 120.264 140.516 1.00 32.22  ? 104 PRO A N   1 
ATOM   555  C CA  . PRO A 1 117 ? 135.325 120.373 140.714 1.00 30.02  ? 104 PRO A CA  1 
ATOM   556  C C   . PRO A 1 117 ? 136.007 121.310 139.730 1.00 35.33  ? 104 PRO A C   1 
ATOM   557  O O   . PRO A 1 117 ? 137.236 121.310 139.637 1.00 43.94  ? 104 PRO A O   1 
ATOM   558  C CB  . PRO A 1 117 ? 135.798 118.933 140.512 1.00 34.21  ? 104 PRO A CB  1 
ATOM   559  C CG  . PRO A 1 117 ? 134.856 118.407 139.480 1.00 37.70  ? 104 PRO A CG  1 
ATOM   560  C CD  . PRO A 1 117 ? 133.518 119.045 139.772 1.00 38.36  ? 104 PRO A CD  1 
ATOM   561  N N   . TRP A 1 118 ? 135.238 122.102 138.988 1.00 33.84  ? 105 TRP A N   1 
ATOM   562  C CA  . TRP A 1 118 ? 135.784 122.986 137.966 1.00 31.77  ? 105 TRP A CA  1 
ATOM   563  C C   . TRP A 1 118 ? 135.860 124.444 138.403 1.00 33.37  ? 105 TRP A C   1 
ATOM   564  O O   . TRP A 1 118 ? 136.151 125.308 137.572 1.00 34.28  ? 105 TRP A O   1 
ATOM   565  C CB  . TRP A 1 118 ? 134.962 122.876 136.682 1.00 32.18  ? 105 TRP A CB  1 
ATOM   566  C CG  . TRP A 1 118 ? 133.512 122.835 136.950 1.00 30.76  ? 105 TRP A CG  1 
ATOM   567  C CD1 . TRP A 1 118 ? 132.738 121.723 137.053 1.00 33.41  ? 105 TRP A CD1 1 
ATOM   568  C CD2 . TRP A 1 118 ? 132.648 123.952 137.177 1.00 29.51  ? 105 TRP A CD2 1 
ATOM   569  N NE1 . TRP A 1 118 ? 131.442 122.075 137.321 1.00 34.28  ? 105 TRP A NE1 1 
ATOM   570  C CE2 . TRP A 1 118 ? 131.359 123.439 137.402 1.00 30.36  ? 105 TRP A CE2 1 
ATOM   571  C CE3 . TRP A 1 118 ? 132.837 125.335 137.206 1.00 29.18  ? 105 TRP A CE3 1 
ATOM   572  C CZ2 . TRP A 1 118 ? 130.264 124.257 137.652 1.00 30.06  ? 105 TRP A CZ2 1 
ATOM   573  C CZ3 . TRP A 1 118 ? 131.748 126.146 137.456 1.00 26.71  ? 105 TRP A CZ3 1 
ATOM   574  C CH2 . TRP A 1 118 ? 130.478 125.604 137.674 1.00 28.87  ? 105 TRP A CH2 1 
ATOM   575  N N   . VAL A 1 119 ? 135.586 124.743 139.665 1.00 32.53  ? 106 VAL A N   1 
ATOM   576  C CA  . VAL A 1 119 ? 135.729 126.104 140.165 1.00 32.00  ? 106 VAL A CA  1 
ATOM   577  C C   . VAL A 1 119 ? 137.169 126.326 140.611 1.00 37.16  ? 106 VAL A C   1 
ATOM   578  O O   . VAL A 1 119 ? 137.862 125.395 141.031 1.00 40.30  ? 106 VAL A O   1 
ATOM   579  C CB  . VAL A 1 119 ? 134.725 126.365 141.302 1.00 26.11  ? 106 VAL A CB  1 
ATOM   580  C CG1 . VAL A 1 119 ? 133.310 126.161 140.794 1.00 30.58  ? 106 VAL A CG1 1 
ATOM   581  C CG2 . VAL A 1 119 ? 134.997 125.440 142.463 1.00 27.82  ? 106 VAL A CG2 1 
ATOM   582  N N   . ARG A 1 120 ? 137.638 127.570 140.508 1.00 40.47  ? 107 ARG A N   1 
ATOM   583  C CA  . ARG A 1 120 ? 139.045 127.875 140.803 1.00 43.69  ? 107 ARG A CA  1 
ATOM   584  C C   . ARG A 1 120 ? 139.240 128.275 142.263 1.00 43.64  ? 107 ARG A C   1 
ATOM   585  O O   . ARG A 1 120 ? 139.977 127.617 143.003 1.00 41.85  ? 107 ARG A O   1 
ATOM   586  C CB  . ARG A 1 120 ? 139.557 128.973 139.870 1.00 43.97  ? 107 ARG A CB  1 
ATOM   587  C CG  . ARG A 1 120 ? 140.997 129.368 140.139 1.00 48.93  ? 107 ARG A CG  1 
ATOM   588  C CD  . ARG A 1 120 ? 141.383 130.636 139.398 1.00 47.41  ? 107 ARG A CD  1 
ATOM   589  N NE  . ARG A 1 120 ? 140.637 131.798 139.867 1.00 42.08  ? 107 ARG A NE  1 
ATOM   590  C CZ  . ARG A 1 120 ? 140.975 133.055 139.611 1.00 38.53  ? 107 ARG A CZ  1 
ATOM   591  N NH1 . ARG A 1 120 ? 142.049 133.349 138.898 1.00 41.54  ? 107 ARG A NH1 1 
ATOM   592  N NH2 . ARG A 1 120 ? 140.219 134.039 140.088 1.00 38.74  ? 107 ARG A NH2 1 
ATOM   593  N N   . ASN A 1 121 ? 138.578 129.346 142.690 1.00 42.42  ? 108 ASN A N   1 
ATOM   594  C CA  . ASN A 1 121 ? 138.759 129.898 144.023 1.00 37.88  ? 108 ASN A CA  1 
ATOM   595  C C   . ASN A 1 121 ? 137.418 130.018 144.731 1.00 36.35  ? 108 ASN A C   1 
ATOM   596  O O   . ASN A 1 121 ? 136.366 130.119 144.093 1.00 36.90  ? 108 ASN A O   1 
ATOM   597  C CB  . ASN A 1 121 ? 139.437 131.274 143.973 1.00 38.25  ? 108 ASN A CB  1 
ATOM   598  C CG  . ASN A 1 121 ? 140.939 131.177 143.796 1.00 44.22  ? 108 ASN A CG  1 
ATOM   599  O OD1 . ASN A 1 121 ? 141.455 130.175 143.302 1.00 43.61  ? 108 ASN A OD1 1 
ATOM   600  N ND2 . ASN A 1 121 ? 141.650 132.220 144.207 1.00 47.55  ? 108 ASN A ND2 1 
ATOM   601  N N   . ILE A 1 122 ? 137.468 129.997 146.060 1.00 32.76  ? 109 ILE A N   1 
ATOM   602  C CA  . ILE A 1 122 ? 136.288 130.133 146.903 1.00 32.08  ? 109 ILE A CA  1 
ATOM   603  C C   . ILE A 1 122 ? 136.513 131.310 147.841 1.00 40.82  ? 109 ILE A C   1 
ATOM   604  O O   . ILE A 1 122 ? 137.497 131.333 148.589 1.00 47.08  ? 109 ILE A O   1 
ATOM   605  C CB  . ILE A 1 122 ? 136.004 128.847 147.693 1.00 29.73  ? 109 ILE A CB  1 
ATOM   606  C CG1 . ILE A 1 122 ? 135.894 127.657 146.742 1.00 34.93  ? 109 ILE A CG1 1 
ATOM   607  C CG2 . ILE A 1 122 ? 134.734 128.995 148.510 1.00 31.36  ? 109 ILE A CG2 1 
ATOM   608  C CD1 . ILE A 1 122 ? 135.631 126.344 147.437 1.00 37.39  ? 109 ILE A CD1 1 
ATOM   609  N N   . PHE A 1 123 ? 135.604 132.282 147.802 1.00 39.60  ? 110 PHE A N   1 
ATOM   610  C CA  . PHE A 1 123 ? 135.662 133.455 148.663 1.00 35.94  ? 110 PHE A CA  1 
ATOM   611  C C   . PHE A 1 123 ? 134.443 133.481 149.574 1.00 34.34  ? 110 PHE A C   1 
ATOM   612  O O   . PHE A 1 123 ? 133.318 133.239 149.126 1.00 36.36  ? 110 PHE A O   1 
ATOM   613  C CB  . PHE A 1 123 ? 135.715 134.753 147.850 1.00 36.62  ? 110 PHE A CB  1 
ATOM   614  C CG  . PHE A 1 123 ? 136.862 134.823 146.885 1.00 37.54  ? 110 PHE A CG  1 
ATOM   615  C CD1 . PHE A 1 123 ? 138.167 134.839 147.340 1.00 39.70  ? 110 PHE A CD1 1 
ATOM   616  C CD2 . PHE A 1 123 ? 136.632 134.894 145.523 1.00 35.68  ? 110 PHE A CD2 1 
ATOM   617  C CE1 . PHE A 1 123 ? 139.222 134.910 146.453 1.00 39.52  ? 110 PHE A CE1 1 
ATOM   618  C CE2 . PHE A 1 123 ? 137.684 134.965 144.633 1.00 37.42  ? 110 PHE A CE2 1 
ATOM   619  C CZ  . PHE A 1 123 ? 138.980 134.973 145.099 1.00 40.97  ? 110 PHE A CZ  1 
ATOM   620  N N   . ILE A 1 124 ? 134.666 133.783 150.849 1.00 33.71  ? 111 ILE A N   1 
ATOM   621  C CA  . ILE A 1 124 ? 133.597 133.884 151.835 1.00 38.04  ? 111 ILE A CA  1 
ATOM   622  C C   . ILE A 1 124 ? 133.641 135.283 152.431 1.00 45.90  ? 111 ILE A C   1 
ATOM   623  O O   . ILE A 1 124 ? 134.662 135.686 153.002 1.00 50.89  ? 111 ILE A O   1 
ATOM   624  C CB  . ILE A 1 124 ? 133.722 132.820 152.936 1.00 45.08  ? 111 ILE A CB  1 
ATOM   625  C CG1 . ILE A 1 124 ? 133.642 131.409 152.346 1.00 44.20  ? 111 ILE A CG1 1 
ATOM   626  C CG2 . ILE A 1 124 ? 132.645 133.018 153.989 1.00 48.31  ? 111 ILE A CG2 1 
ATOM   627  C CD1 . ILE A 1 124 ? 134.987 130.798 152.018 1.00 41.47  ? 111 ILE A CD1 1 
ATOM   628  N N   . VAL A 1 125 ? 132.540 136.020 152.304 1.00 45.39  ? 112 VAL A N   1 
ATOM   629  C CA  . VAL A 1 125 ? 132.443 137.369 152.852 1.00 47.87  ? 112 VAL A CA  1 
ATOM   630  C C   . VAL A 1 125 ? 131.941 137.284 154.286 1.00 55.74  ? 112 VAL A C   1 
ATOM   631  O O   . VAL A 1 125 ? 130.932 136.626 154.568 1.00 58.73  ? 112 VAL A O   1 
ATOM   632  C CB  . VAL A 1 125 ? 131.522 138.253 151.994 1.00 43.02  ? 112 VAL A CB  1 
ATOM   633  C CG1 . VAL A 1 125 ? 132.244 138.700 150.736 1.00 41.88  ? 112 VAL A CG1 1 
ATOM   634  C CG2 . VAL A 1 125 ? 130.247 137.515 151.635 1.00 43.21  ? 112 VAL A CG2 1 
ATOM   635  N N   . THR A 1 126 ? 132.650 137.948 155.196 1.00 60.28  ? 113 THR A N   1 
ATOM   636  C CA  . THR A 1 126 ? 132.329 137.909 156.614 1.00 63.77  ? 113 THR A CA  1 
ATOM   637  C C   . THR A 1 126 ? 132.487 139.303 157.203 1.00 68.24  ? 113 THR A C   1 
ATOM   638  O O   . THR A 1 126 ? 133.179 140.161 156.649 1.00 68.07  ? 113 THR A O   1 
ATOM   639  C CB  . THR A 1 126 ? 133.219 136.915 157.374 1.00 68.48  ? 113 THR A CB  1 
ATOM   640  O OG1 . THR A 1 126 ? 134.593 137.152 157.043 1.00 66.75  ? 113 THR A OG1 1 
ATOM   641  C CG2 . THR A 1 126 ? 132.854 135.481 157.020 1.00 62.27  ? 113 THR A CG2 1 
ATOM   642  N N   . ASN A 1 127 ? 131.834 139.517 158.343 1.00 71.32  ? 114 ASN A N   1 
ATOM   643  C CA  . ASN A 1 127 ? 131.928 140.767 159.084 1.00 70.45  ? 114 ASN A CA  1 
ATOM   644  C C   . ASN A 1 127 ? 133.199 140.862 159.912 1.00 68.15  ? 114 ASN A C   1 
ATOM   645  O O   . ASN A 1 127 ? 133.280 141.703 160.815 1.00 74.06  ? 114 ASN A O   1 
ATOM   646  C CB  . ASN A 1 127 ? 130.706 140.937 159.990 1.00 75.94  ? 114 ASN A CB  1 
ATOM   647  C CG  . ASN A 1 127 ? 129.397 140.792 159.240 1.00 73.20  ? 114 ASN A CG  1 
ATOM   648  O OD1 . ASN A 1 127 ? 129.357 140.894 158.015 1.00 73.18  ? 114 ASN A OD1 1 
ATOM   649  N ND2 . ASN A 1 127 ? 128.316 140.558 159.975 1.00 76.11  ? 114 ASN A ND2 1 
ATOM   650  N N   . GLY A 1 128 ? 134.187 140.019 159.627 1.00 67.05  ? 115 GLY A N   1 
ATOM   651  C CA  . GLY A 1 128 ? 135.359 139.876 160.462 1.00 77.32  ? 115 GLY A CA  1 
ATOM   652  C C   . GLY A 1 128 ? 135.391 138.600 161.269 1.00 82.27  ? 115 GLY A C   1 
ATOM   653  O O   . GLY A 1 128 ? 136.305 138.425 162.084 1.00 81.15  ? 115 GLY A O   1 
ATOM   654  N N   . GLN A 1 129 ? 134.422 137.709 161.071 1.00 82.04  ? 116 GLN A N   1 
ATOM   655  C CA  . GLN A 1 129 ? 134.377 136.438 161.785 1.00 86.21  ? 116 GLN A CA  1 
ATOM   656  C C   . GLN A 1 129 ? 135.383 135.480 161.166 1.00 84.17  ? 116 GLN A C   1 
ATOM   657  O O   . GLN A 1 129 ? 135.195 135.009 160.040 1.00 81.05  ? 116 GLN A O   1 
ATOM   658  C CB  . GLN A 1 129 ? 132.964 135.866 161.739 1.00 82.35  ? 116 GLN A CB  1 
ATOM   659  C CG  . GLN A 1 129 ? 131.925 136.797 162.338 1.00 81.32  ? 116 GLN A CG  1 
ATOM   660  C CD  . GLN A 1 129 ? 130.552 136.606 161.736 1.00 83.38  ? 116 GLN A CD  1 
ATOM   661  O OE1 . GLN A 1 129 ? 130.127 135.483 161.471 1.00 84.76  ? 116 GLN A OE1 1 
ATOM   662  N NE2 . GLN A 1 129 ? 129.850 137.710 161.506 1.00 85.28  ? 116 GLN A NE2 1 
ATOM   663  N N   . ILE A 1 130 ? 136.451 135.194 161.902 1.00 87.48  ? 117 ILE A N   1 
ATOM   664  C CA  . ILE A 1 130 ? 137.530 134.332 161.432 1.00 84.42  ? 117 ILE A CA  1 
ATOM   665  C C   . ILE A 1 130 ? 136.973 132.932 161.204 1.00 83.03  ? 117 ILE A C   1 
ATOM   666  O O   . ILE A 1 130 ? 136.009 132.536 161.875 1.00 83.09  ? 117 ILE A O   1 
ATOM   667  C CB  . ILE A 1 130 ? 138.699 134.321 162.430 1.00 85.36  ? 117 ILE A CB  1 
ATOM   668  C CG1 . ILE A 1 130 ? 138.202 133.951 163.829 1.00 79.18  ? 117 ILE A CG1 1 
ATOM   669  C CG2 . ILE A 1 130 ? 139.389 135.673 162.451 1.00 87.46  ? 117 ILE A CG2 1 
ATOM   670  C CD1 . ILE A 1 130 ? 139.267 134.048 164.902 1.00 69.71  ? 117 ILE A CD1 1 
ATOM   671  N N   . PRO A 1 131 ? 137.521 132.164 160.262 1.00 80.29  ? 118 PRO A N   1 
ATOM   672  C CA  . PRO A 1 131 ? 136.994 130.818 160.009 1.00 75.90  ? 118 PRO A CA  1 
ATOM   673  C C   . PRO A 1 131 ? 137.120 129.924 161.235 1.00 77.69  ? 118 PRO A C   1 
ATOM   674  O O   . PRO A 1 131 ? 138.106 129.981 161.973 1.00 82.03  ? 118 PRO A O   1 
ATOM   675  C CB  . PRO A 1 131 ? 137.864 130.311 158.854 1.00 73.07  ? 118 PRO A CB  1 
ATOM   676  C CG  . PRO A 1 131 ? 139.134 131.094 158.972 1.00 78.91  ? 118 PRO A CG  1 
ATOM   677  C CD  . PRO A 1 131 ? 138.700 132.457 159.430 1.00 76.49  ? 118 PRO A CD  1 
ATOM   678  N N   . SER A 1 132 ? 136.105 129.086 161.438 1.00 73.86  ? 119 SER A N   1 
ATOM   679  C CA  . SER A 1 132 ? 136.078 128.178 162.577 1.00 73.01  ? 119 SER A CA  1 
ATOM   680  C C   . SER A 1 132 ? 136.636 126.803 162.243 1.00 71.66  ? 119 SER A C   1 
ATOM   681  O O   . SER A 1 132 ? 137.199 126.140 163.121 1.00 74.70  ? 119 SER A O   1 
ATOM   682  C CB  . SER A 1 132 ? 134.645 128.035 163.101 1.00 71.88  ? 119 SER A CB  1 
ATOM   683  O OG  . SER A 1 132 ? 134.076 129.298 163.404 1.00 71.34  ? 119 SER A OG  1 
ATOM   684  N N   . TRP A 1 133 ? 136.488 126.359 160.996 1.00 69.88  ? 120 TRP A N   1 
ATOM   685  C CA  . TRP A 1 133 ? 136.987 125.056 160.583 1.00 64.29  ? 120 TRP A CA  1 
ATOM   686  C C   . TRP A 1 133 ? 137.643 125.063 159.209 1.00 66.73  ? 120 TRP A C   1 
ATOM   687  O O   . TRP A 1 133 ? 138.073 124.001 158.750 1.00 66.78  ? 120 TRP A O   1 
ATOM   688  C CB  . TRP A 1 133 ? 135.848 124.024 160.600 1.00 60.15  ? 120 TRP A CB  1 
ATOM   689  C CG  . TRP A 1 133 ? 134.553 124.582 160.108 1.00 61.35  ? 120 TRP A CG  1 
ATOM   690  C CD1 . TRP A 1 133 ? 133.518 125.039 160.866 1.00 62.98  ? 120 TRP A CD1 1 
ATOM   691  C CD2 . TRP A 1 133 ? 134.161 124.760 158.743 1.00 63.43  ? 120 TRP A CD2 1 
ATOM   692  N NE1 . TRP A 1 133 ? 132.500 125.484 160.059 1.00 62.09  ? 120 TRP A NE1 1 
ATOM   693  C CE2 . TRP A 1 133 ? 132.871 125.324 158.751 1.00 60.01  ? 120 TRP A CE2 1 
ATOM   694  C CE3 . TRP A 1 133 ? 134.773 124.494 157.516 1.00 65.52  ? 120 TRP A CE3 1 
ATOM   695  C CZ2 . TRP A 1 133 ? 132.184 125.626 157.581 1.00 57.05  ? 120 TRP A CZ2 1 
ATOM   696  C CZ3 . TRP A 1 133 ? 134.089 124.794 156.356 1.00 61.90  ? 120 TRP A CZ3 1 
ATOM   697  C CH2 . TRP A 1 133 ? 132.810 125.357 156.396 1.00 58.18  ? 120 TRP A CH2 1 
ATOM   698  N N   . LEU A 1 134 ? 137.732 126.211 158.540 1.00 67.29  ? 121 LEU A N   1 
ATOM   699  C CA  . LEU A 1 134 ? 138.346 126.269 157.224 1.00 61.31  ? 121 LEU A CA  1 
ATOM   700  C C   . LEU A 1 134 ? 139.852 126.045 157.326 1.00 63.08  ? 121 LEU A C   1 
ATOM   701  O O   . LEU A 1 134 ? 140.467 126.225 158.379 1.00 61.40  ? 121 LEU A O   1 
ATOM   702  C CB  . LEU A 1 134 ? 138.069 127.614 156.546 1.00 59.40  ? 121 LEU A CB  1 
ATOM   703  C CG  . LEU A 1 134 ? 136.684 127.889 155.950 1.00 59.93  ? 121 LEU A CG  1 
ATOM   704  C CD1 . LEU A 1 134 ? 135.644 128.133 157.033 1.00 64.01  ? 121 LEU A CD1 1 
ATOM   705  C CD2 . LEU A 1 134 ? 136.735 129.068 154.988 1.00 61.92  ? 121 LEU A CD2 1 
ATOM   706  N N   . ASN A 1 135 ? 140.442 125.636 156.208 1.00 64.30  ? 122 ASN A N   1 
ATOM   707  C CA  . ASN A 1 135 ? 141.873 125.384 156.104 1.00 64.05  ? 122 ASN A CA  1 
ATOM   708  C C   . ASN A 1 135 ? 142.505 126.500 155.283 1.00 61.77  ? 122 ASN A C   1 
ATOM   709  O O   . ASN A 1 135 ? 142.189 126.657 154.100 1.00 62.53  ? 122 ASN A O   1 
ATOM   710  C CB  . ASN A 1 135 ? 142.137 124.021 155.463 1.00 65.97  ? 122 ASN A CB  1 
ATOM   711  C CG  . ASN A 1 135 ? 143.610 123.673 155.408 1.00 68.28  ? 122 ASN A CG  1 
ATOM   712  O OD1 . ASN A 1 135 ? 144.420 124.223 156.156 1.00 70.41  ? 122 ASN A OD1 1 
ATOM   713  N ND2 . ASN A 1 135 ? 143.966 122.751 154.522 1.00 66.29  ? 122 ASN A ND2 1 
ATOM   714  N N   . LEU A 1 136 ? 143.384 127.277 155.911 1.00 62.38  ? 123 LEU A N   1 
ATOM   715  C CA  . LEU A 1 136 ? 144.044 128.380 155.227 1.00 62.39  ? 123 LEU A CA  1 
ATOM   716  C C   . LEU A 1 136 ? 145.388 128.001 154.622 1.00 66.29  ? 123 LEU A C   1 
ATOM   717  O O   . LEU A 1 136 ? 145.961 128.807 153.881 1.00 65.18  ? 123 LEU A O   1 
ATOM   718  C CB  . LEU A 1 136 ? 144.234 129.561 156.182 1.00 62.35  ? 123 LEU A CB  1 
ATOM   719  C CG  . LEU A 1 136 ? 143.147 130.630 156.108 1.00 63.40  ? 123 LEU A CG  1 
ATOM   720  C CD1 . LEU A 1 136 ? 143.028 131.158 154.688 1.00 62.09  ? 123 LEU A CD1 1 
ATOM   721  C CD2 . LEU A 1 136 ? 141.817 130.082 156.590 1.00 68.38  ? 123 LEU A CD2 1 
ATOM   722  N N   . ASP A 1 137 ? 145.908 126.808 154.916 1.00 68.90  ? 124 ASP A N   1 
ATOM   723  C CA  . ASP A 1 137 ? 147.167 126.393 154.307 1.00 70.81  ? 124 ASP A CA  1 
ATOM   724  C C   . ASP A 1 137 ? 147.019 126.184 152.807 1.00 69.82  ? 124 ASP A C   1 
ATOM   725  O O   . ASP A 1 137 ? 147.956 126.457 152.049 1.00 70.60  ? 124 ASP A O   1 
ATOM   726  C CB  . ASP A 1 137 ? 147.686 125.122 154.974 1.00 76.73  ? 124 ASP A CB  1 
ATOM   727  C CG  . ASP A 1 137 ? 148.228 125.376 156.365 1.00 85.53  ? 124 ASP A CG  1 
ATOM   728  O OD1 . ASP A 1 137 ? 147.417 125.570 157.294 1.00 84.85  ? 124 ASP A OD1 1 
ATOM   729  O OD2 . ASP A 1 137 ? 149.467 125.387 156.528 1.00 89.62  ? 124 ASP A OD2 1 
ATOM   730  N N   . ASN A 1 138 ? 145.863 125.706 152.364 1.00 69.86  ? 125 ASN A N   1 
ATOM   731  C CA  . ASN A 1 138 ? 145.596 125.583 150.938 1.00 66.39  ? 125 ASN A CA  1 
ATOM   732  C C   . ASN A 1 138 ? 145.273 126.961 150.375 1.00 62.44  ? 125 ASN A C   1 
ATOM   733  O O   . ASN A 1 138 ? 144.322 127.599 150.839 1.00 61.03  ? 125 ASN A O   1 
ATOM   734  C CB  . ASN A 1 138 ? 144.438 124.626 150.692 1.00 62.29  ? 125 ASN A CB  1 
ATOM   735  C CG  . ASN A 1 138 ? 144.571 123.870 149.385 1.00 65.32  ? 125 ASN A CG  1 
ATOM   736  O OD1 . ASN A 1 138 ? 145.164 124.361 148.425 1.00 69.15  ? 125 ASN A OD1 1 
ATOM   737  N ND2 . ASN A 1 138 ? 144.020 122.664 149.346 1.00 62.00  ? 125 ASN A ND2 1 
ATOM   738  N N   . PRO A 1 139 ? 146.023 127.455 149.390 1.00 57.15  ? 126 PRO A N   1 
ATOM   739  C CA  . PRO A 1 139 ? 145.827 128.827 148.911 1.00 54.15  ? 126 PRO A CA  1 
ATOM   740  C C   . PRO A 1 139 ? 144.641 129.020 147.978 1.00 52.78  ? 126 PRO A C   1 
ATOM   741  O O   . PRO A 1 139 ? 144.539 130.084 147.363 1.00 50.77  ? 126 PRO A O   1 
ATOM   742  C CB  . PRO A 1 139 ? 147.144 129.107 148.173 1.00 55.77  ? 126 PRO A CB  1 
ATOM   743  C CG  . PRO A 1 139 ? 147.549 127.776 147.655 1.00 56.53  ? 126 PRO A CG  1 
ATOM   744  C CD  . PRO A 1 139 ? 147.170 126.801 148.735 1.00 55.97  ? 126 PRO A CD  1 
ATOM   745  N N   . ARG A 1 140 ? 143.747 128.041 147.847 1.00 52.97  ? 127 ARG A N   1 
ATOM   746  C CA  . ARG A 1 140 ? 142.608 128.152 146.945 1.00 51.10  ? 127 ARG A CA  1 
ATOM   747  C C   . ARG A 1 140 ? 141.341 128.639 147.633 1.00 46.92  ? 127 ARG A C   1 
ATOM   748  O O   . ARG A 1 140 ? 140.289 128.700 146.991 1.00 44.69  ? 127 ARG A O   1 
ATOM   749  C CB  . ARG A 1 140 ? 142.345 126.809 146.254 1.00 48.95  ? 127 ARG A CB  1 
ATOM   750  C CG  . ARG A 1 140 ? 143.489 126.373 145.355 1.00 48.65  ? 127 ARG A CG  1 
ATOM   751  C CD  . ARG A 1 140 ? 143.063 125.339 144.333 1.00 45.06  ? 127 ARG A CD  1 
ATOM   752  N NE  . ARG A 1 140 ? 144.112 125.126 143.344 1.00 51.03  ? 127 ARG A NE  1 
ATOM   753  C CZ  . ARG A 1 140 ? 144.243 125.830 142.227 1.00 61.56  ? 127 ARG A CZ  1 
ATOM   754  N NH1 . ARG A 1 140 ? 143.388 126.788 141.910 1.00 63.13  ? 127 ARG A NH1 1 
ATOM   755  N NH2 . ARG A 1 140 ? 145.256 125.564 141.408 1.00 65.27  ? 127 ARG A NH2 1 
ATOM   756  N N   . VAL A 1 141 ? 141.410 128.985 148.915 1.00 45.67  ? 128 VAL A N   1 
ATOM   757  C CA  . VAL A 1 141 ? 140.286 129.578 149.629 1.00 43.89  ? 128 VAL A CA  1 
ATOM   758  C C   . VAL A 1 141 ? 140.811 130.716 150.495 1.00 47.99  ? 128 VAL A C   1 
ATOM   759  O O   . VAL A 1 141 ? 141.811 130.554 151.202 1.00 51.87  ? 128 VAL A O   1 
ATOM   760  C CB  . VAL A 1 141 ? 139.534 128.535 150.480 1.00 47.04  ? 128 VAL A CB  1 
ATOM   761  C CG1 . VAL A 1 141 ? 140.443 127.971 151.560 1.00 53.92  ? 128 VAL A CG1 1 
ATOM   762  C CG2 . VAL A 1 141 ? 138.281 129.144 151.089 1.00 42.98  ? 128 VAL A CG2 1 
ATOM   763  N N   . THR A 1 142 ? 140.150 131.870 150.426 1.00 49.41  ? 129 THR A N   1 
ATOM   764  C CA  . THR A 1 142 ? 140.514 133.029 151.229 1.00 50.63  ? 129 THR A CA  1 
ATOM   765  C C   . THR A 1 142 ? 139.248 133.685 151.759 1.00 48.26  ? 129 THR A C   1 
ATOM   766  O O   . THR A 1 142 ? 138.160 133.519 151.204 1.00 44.39  ? 129 THR A O   1 
ATOM   767  C CB  . THR A 1 142 ? 141.328 134.059 150.431 1.00 50.72  ? 129 THR A CB  1 
ATOM   768  O OG1 . THR A 1 142 ? 140.594 134.453 149.266 1.00 49.93  ? 129 THR A OG1 1 
ATOM   769  C CG2 . THR A 1 142 ? 142.675 133.487 150.011 1.00 50.55  ? 129 THR A CG2 1 
ATOM   770  N N   . ILE A 1 143 ? 139.403 134.441 152.842 1.00 47.55  ? 130 ILE A N   1 
ATOM   771  C CA  . ILE A 1 143 ? 138.302 135.164 153.467 1.00 48.47  ? 130 ILE A CA  1 
ATOM   772  C C   . ILE A 1 143 ? 138.488 136.643 153.168 1.00 48.33  ? 130 ILE A C   1 
ATOM   773  O O   . ILE A 1 143 ? 139.556 137.208 153.436 1.00 52.20  ? 130 ILE A O   1 
ATOM   774  C CB  . ILE A 1 143 ? 138.236 134.918 154.982 1.00 54.46  ? 130 ILE A CB  1 
ATOM   775  C CG1 . ILE A 1 143 ? 138.343 133.424 155.300 1.00 57.79  ? 130 ILE A CG1 1 
ATOM   776  C CG2 . ILE A 1 143 ? 136.948 135.485 155.555 1.00 57.24  ? 130 ILE A CG2 1 
ATOM   777  C CD1 . ILE A 1 143 ? 139.727 132.988 155.722 1.00 57.13  ? 130 ILE A CD1 1 
ATOM   778  N N   . VAL A 1 144 ? 137.456 137.271 152.612 1.00 47.54  ? 131 VAL A N   1 
ATOM   779  C CA  . VAL A 1 144 ? 137.481 138.688 152.270 1.00 53.90  ? 131 VAL A CA  1 
ATOM   780  C C   . VAL A 1 144 ? 136.542 139.425 153.215 1.00 60.75  ? 131 VAL A C   1 
ATOM   781  O O   . VAL A 1 144 ? 135.349 139.106 153.295 1.00 58.45  ? 131 VAL A O   1 
ATOM   782  C CB  . VAL A 1 144 ? 137.097 138.925 150.802 1.00 49.77  ? 131 VAL A CB  1 
ATOM   783  C CG1 . VAL A 1 144 ? 138.282 138.642 149.901 1.00 52.38  ? 131 VAL A CG1 1 
ATOM   784  C CG2 . VAL A 1 144 ? 135.923 138.045 150.410 1.00 47.41  ? 131 VAL A CG2 1 
ATOM   785  N N   . THR A 1 145 ? 137.080 140.405 153.934 1.00 65.09  ? 132 THR A N   1 
ATOM   786  C CA  . THR A 1 145 ? 136.279 141.205 154.846 1.00 61.65  ? 132 THR A CA  1 
ATOM   787  C C   . THR A 1 145 ? 135.517 142.275 154.074 1.00 63.54  ? 132 THR A C   1 
ATOM   788  O O   . THR A 1 145 ? 135.897 142.659 152.964 1.00 69.86  ? 132 THR A O   1 
ATOM   789  C CB  . THR A 1 145 ? 137.161 141.854 155.914 1.00 67.64  ? 132 THR A CB  1 
ATOM   790  O OG1 . THR A 1 145 ? 138.227 140.961 156.259 1.00 73.89  ? 132 THR A OG1 1 
ATOM   791  C CG2 . THR A 1 145 ? 136.352 142.154 157.169 1.00 72.84  ? 132 THR A CG2 1 
ATOM   792  N N   . HIS A 1 146 ? 134.428 142.757 154.677 1.00 62.39  ? 133 HIS A N   1 
ATOM   793  C CA  . HIS A 1 146 ? 133.561 143.721 154.006 1.00 66.78  ? 133 HIS A CA  1 
ATOM   794  C C   . HIS A 1 146 ? 134.255 145.049 153.730 1.00 73.92  ? 133 HIS A C   1 
ATOM   795  O O   . HIS A 1 146 ? 133.744 145.842 152.931 1.00 76.04  ? 133 HIS A O   1 
ATOM   796  C CB  . HIS A 1 146 ? 132.302 143.954 154.839 1.00 67.01  ? 133 HIS A CB  1 
ATOM   797  C CG  . HIS A 1 146 ? 131.340 142.809 154.806 1.00 61.00  ? 133 HIS A CG  1 
ATOM   798  N ND1 . HIS A 1 146 ? 131.751 141.495 154.760 1.00 58.53  ? 133 HIS A ND1 1 
ATOM   799  C CD2 . HIS A 1 146 ? 129.987 142.780 154.812 1.00 62.97  ? 133 HIS A CD2 1 
ATOM   800  C CE1 . HIS A 1 146 ? 130.693 140.705 154.738 1.00 60.32  ? 133 HIS A CE1 1 
ATOM   801  N NE2 . HIS A 1 146 ? 129.610 141.460 154.770 1.00 62.65  ? 133 HIS A NE2 1 
ATOM   802  N N   . GLN A 1 147 ? 135.397 145.315 154.371 1.00 75.21  ? 134 GLN A N   1 
ATOM   803  C CA  . GLN A 1 147 ? 136.137 146.540 154.079 1.00 79.46  ? 134 GLN A CA  1 
ATOM   804  C C   . GLN A 1 147 ? 136.570 146.601 152.619 1.00 80.23  ? 134 GLN A C   1 
ATOM   805  O O   . GLN A 1 147 ? 136.685 147.693 152.052 1.00 83.92  ? 134 GLN A O   1 
ATOM   806  C CB  . GLN A 1 147 ? 137.356 146.658 154.996 1.00 80.09  ? 134 GLN A CB  1 
ATOM   807  C CG  . GLN A 1 147 ? 137.112 147.451 156.275 1.00 81.43  ? 134 GLN A CG  1 
ATOM   808  C CD  . GLN A 1 147 ? 136.413 146.643 157.351 1.00 83.34  ? 134 GLN A CD  1 
ATOM   809  O OE1 . GLN A 1 147 ? 135.292 146.957 157.749 1.00 88.97  ? 134 GLN A OE1 1 
ATOM   810  N NE2 . GLN A 1 147 ? 137.081 145.603 157.839 1.00 78.17  ? 134 GLN A NE2 1 
ATOM   811  N N   . ASP A 1 148 ? 136.831 145.447 152.002 1.00 77.59  ? 135 ASP A N   1 
ATOM   812  C CA  . ASP A 1 148 ? 137.244 145.424 150.602 1.00 82.07  ? 135 ASP A CA  1 
ATOM   813  C C   . ASP A 1 148 ? 136.083 145.771 149.674 1.00 80.97  ? 135 ASP A C   1 
ATOM   814  O O   . ASP A 1 148 ? 136.230 146.587 148.756 1.00 79.65  ? 135 ASP A O   1 
ATOM   815  C CB  . ASP A 1 148 ? 137.822 144.049 150.258 1.00 84.23  ? 135 ASP A CB  1 
ATOM   816  C CG  . ASP A 1 148 ? 138.643 144.053 148.979 1.00 89.03  ? 135 ASP A CG  1 
ATOM   817  O OD1 . ASP A 1 148 ? 138.344 144.847 148.063 1.00 89.40  ? 135 ASP A OD1 1 
ATOM   818  O OD2 . ASP A 1 148 ? 139.596 143.252 148.888 1.00 90.44  ? 135 ASP A OD2 1 
ATOM   819  N N   . VAL A 1 149 ? 134.918 145.156 149.896 1.00 77.88  ? 136 VAL A N   1 
ATOM   820  C CA  . VAL A 1 149 ? 133.802 145.325 148.969 1.00 75.22  ? 136 VAL A CA  1 
ATOM   821  C C   . VAL A 1 149 ? 133.177 146.711 149.090 1.00 77.29  ? 136 VAL A C   1 
ATOM   822  O O   . VAL A 1 149 ? 132.691 147.266 148.097 1.00 78.77  ? 136 VAL A O   1 
ATOM   823  C CB  . VAL A 1 149 ? 132.760 144.210 149.184 1.00 66.86  ? 136 VAL A CB  1 
ATOM   824  C CG1 . VAL A 1 149 ? 133.378 142.851 148.901 1.00 59.09  ? 136 VAL A CG1 1 
ATOM   825  C CG2 . VAL A 1 149 ? 132.205 144.255 150.596 1.00 68.76  ? 136 VAL A CG2 1 
ATOM   826  N N   . PHE A 1 150 ? 133.171 147.293 150.286 1.00 76.91  ? 137 PHE A N   1 
ATOM   827  C CA  . PHE A 1 150 ? 132.517 148.577 150.498 1.00 78.55  ? 137 PHE A CA  1 
ATOM   828  C C   . PHE A 1 150 ? 133.381 149.714 149.972 1.00 83.17  ? 137 PHE A C   1 
ATOM   829  O O   . PHE A 1 150 ? 134.572 149.802 150.286 1.00 81.56  ? 137 PHE A O   1 
ATOM   830  C CB  . PHE A 1 150 ? 132.218 148.786 151.982 1.00 81.39  ? 137 PHE A CB  1 
ATOM   831  C CG  . PHE A 1 150 ? 130.962 148.110 152.446 1.00 83.22  ? 137 PHE A CG  1 
ATOM   832  C CD1 . PHE A 1 150 ? 129.796 148.209 151.709 1.00 80.29  ? 137 PHE A CD1 1 
ATOM   833  C CD2 . PHE A 1 150 ? 130.948 147.372 153.617 1.00 85.69  ? 137 PHE A CD2 1 
ATOM   834  C CE1 . PHE A 1 150 ? 128.636 147.587 152.132 1.00 80.46  ? 137 PHE A CE1 1 
ATOM   835  C CE2 . PHE A 1 150 ? 129.792 146.747 154.044 1.00 86.64  ? 137 PHE A CE2 1 
ATOM   836  C CZ  . PHE A 1 150 ? 128.635 146.855 153.301 1.00 82.86  ? 137 PHE A CZ  1 
ATOM   837  N N   . ARG A 1 151 ? 132.774 150.588 149.168 1.00 83.02  ? 138 ARG A N   1 
ATOM   838  C CA  . ARG A 1 151 ? 133.483 151.769 148.690 1.00 84.03  ? 138 ARG A CA  1 
ATOM   839  C C   . ARG A 1 151 ? 133.714 152.765 149.819 1.00 93.30  ? 138 ARG A C   1 
ATOM   840  O O   . ARG A 1 151 ? 134.738 153.456 149.844 1.00 94.63  ? 138 ARG A O   1 
ATOM   841  C CB  . ARG A 1 151 ? 132.706 152.415 147.544 1.00 78.99  ? 138 ARG A CB  1 
ATOM   842  C CG  . ARG A 1 151 ? 131.229 152.625 147.830 1.00 76.52  ? 138 ARG A CG  1 
ATOM   843  C CD  . ARG A 1 151 ? 130.522 153.284 146.655 1.00 83.57  ? 138 ARG A CD  1 
ATOM   844  N NE  . ARG A 1 151 ? 130.419 152.403 145.498 1.00 81.39  ? 138 ARG A NE  1 
ATOM   845  C CZ  . ARG A 1 151 ? 131.270 152.392 144.480 1.00 82.00  ? 138 ARG A CZ  1 
ATOM   846  N NH1 . ARG A 1 151 ? 132.316 153.200 144.444 1.00 85.34  ? 138 ARG A NH1 1 
ATOM   847  N NH2 . ARG A 1 151 ? 131.064 151.549 143.473 1.00 83.92  ? 138 ARG A NH2 1 
ATOM   848  N N   . ASN A 1 152 ? 132.772 152.860 150.751 1.00 96.18  ? 139 ASN A N   1 
ATOM   849  C CA  . ASN A 1 152 ? 132.880 153.724 151.916 1.00 92.62  ? 139 ASN A CA  1 
ATOM   850  C C   . ASN A 1 152 ? 132.968 152.870 153.173 1.00 89.38  ? 139 ASN A C   1 
ATOM   851  O O   . ASN A 1 152 ? 132.221 151.899 153.321 1.00 89.57  ? 139 ASN A O   1 
ATOM   852  C CB  . ASN A 1 152 ? 131.686 154.674 152.002 1.00 91.01  ? 139 ASN A CB  1 
ATOM   853  C CG  . ASN A 1 152 ? 130.369 153.944 152.123 1.00 92.80  ? 139 ASN A CG  1 
ATOM   854  O OD1 . ASN A 1 152 ? 129.891 153.688 153.230 1.00 90.86  ? 139 ASN A OD1 1 
ATOM   855  N ND2 . ASN A 1 152 ? 129.772 153.602 150.986 1.00 90.23  ? 139 ASN A ND2 1 
ATOM   856  N N   . LEU A 1 153 ? 133.878 153.233 154.074 1.00 88.99  ? 140 LEU A N   1 
ATOM   857  C CA  . LEU A 1 153 ? 134.067 152.484 155.310 1.00 91.00  ? 140 LEU A CA  1 
ATOM   858  C C   . LEU A 1 153 ? 133.004 152.783 156.359 1.00 97.14  ? 140 LEU A C   1 
ATOM   859  O O   . LEU A 1 153 ? 132.957 152.090 157.382 1.00 101.73 ? 140 LEU A O   1 
ATOM   860  C CB  . LEU A 1 153 ? 135.456 152.773 155.890 1.00 91.57  ? 140 LEU A CB  1 
ATOM   861  C CG  . LEU A 1 153 ? 136.629 152.436 154.966 1.00 86.52  ? 140 LEU A CG  1 
ATOM   862  C CD1 . LEU A 1 153 ? 137.958 152.787 155.617 1.00 81.38  ? 140 LEU A CD1 1 
ATOM   863  C CD2 . LEU A 1 153 ? 136.595 150.968 154.572 1.00 78.27  ? 140 LEU A CD2 1 
ATOM   864  N N   . SER A 1 154 ? 132.157 153.790 156.137 1.00 99.08  ? 141 SER A N   1 
ATOM   865  C CA  . SER A 1 154 ? 131.120 154.137 157.102 1.00 103.26 ? 141 SER A CA  1 
ATOM   866  C C   . SER A 1 154 ? 129.980 153.128 157.142 1.00 101.30 ? 141 SER A C   1 
ATOM   867  O O   . SER A 1 154 ? 129.143 153.204 158.048 1.00 100.94 ? 141 SER A O   1 
ATOM   868  C CB  . SER A 1 154 ? 130.565 155.528 156.792 1.00 103.24 ? 141 SER A CB  1 
ATOM   869  O OG  . SER A 1 154 ? 129.986 155.567 155.500 1.00 99.66  ? 141 SER A OG  1 
ATOM   870  N N   . HIS A 1 155 ? 129.924 152.194 156.195 1.00 96.99  ? 142 HIS A N   1 
ATOM   871  C CA  . HIS A 1 155 ? 128.866 151.196 156.135 1.00 96.07  ? 142 HIS A CA  1 
ATOM   872  C C   . HIS A 1 155 ? 129.329 149.812 156.579 1.00 94.27  ? 142 HIS A C   1 
ATOM   873  O O   . HIS A 1 155 ? 128.638 148.824 156.305 1.00 92.39  ? 142 HIS A O   1 
ATOM   874  C CB  . HIS A 1 155 ? 128.289 151.128 154.718 1.00 96.03  ? 142 HIS A CB  1 
ATOM   875  C CG  . HIS A 1 155 ? 127.351 152.249 154.391 1.00 92.71  ? 142 HIS A CG  1 
ATOM   876  N ND1 . HIS A 1 155 ? 127.019 152.590 153.097 1.00 84.95  ? 142 HIS A ND1 1 
ATOM   877  C CD2 . HIS A 1 155 ? 126.667 153.100 155.191 1.00 95.53  ? 142 HIS A CD2 1 
ATOM   878  C CE1 . HIS A 1 155 ? 126.176 153.606 153.114 1.00 87.80  ? 142 HIS A CE1 1 
ATOM   879  N NE2 . HIS A 1 155 ? 125.945 153.934 154.373 1.00 95.49  ? 142 HIS A NE2 1 
ATOM   880  N N   . LEU A 1 156 ? 130.472 149.714 157.261 1.00 94.28  ? 143 LEU A N   1 
ATOM   881  C CA  . LEU A 1 156 ? 131.018 148.416 157.651 1.00 97.41  ? 143 LEU A CA  1 
ATOM   882  C C   . LEU A 1 156 ? 130.115 147.653 158.626 1.00 103.50 ? 143 LEU A C   1 
ATOM   883  O O   . LEU A 1 156 ? 130.086 146.417 158.565 1.00 103.08 ? 143 LEU A O   1 
ATOM   884  C CB  . LEU A 1 156 ? 132.436 148.575 158.224 1.00 95.38  ? 143 LEU A CB  1 
ATOM   885  C CG  . LEU A 1 156 ? 132.775 149.281 159.542 1.00 93.96  ? 143 LEU A CG  1 
ATOM   886  C CD1 . LEU A 1 156 ? 132.678 148.328 160.732 1.00 88.08  ? 143 LEU A CD1 1 
ATOM   887  C CD2 . LEU A 1 156 ? 134.154 149.920 159.474 1.00 95.03  ? 143 LEU A CD2 1 
ATOM   888  N N   . PRO A 1 157 ? 129.355 148.313 159.540 1.00 105.11 ? 144 PRO A N   1 
ATOM   889  C CA  . PRO A 1 157 ? 128.369 147.545 160.315 1.00 104.82 ? 144 PRO A CA  1 
ATOM   890  C C   . PRO A 1 157 ? 127.163 147.180 159.467 1.00 104.59 ? 144 PRO A C   1 
ATOM   891  O O   . PRO A 1 157 ? 126.071 147.718 159.668 1.00 104.53 ? 144 PRO A O   1 
ATOM   892  C CB  . PRO A 1 157 ? 127.989 148.497 161.459 1.00 102.30 ? 144 PRO A CB  1 
ATOM   893  C CG  . PRO A 1 157 ? 129.054 149.546 161.469 1.00 99.00  ? 144 PRO A CG  1 
ATOM   894  C CD  . PRO A 1 157 ? 129.433 149.698 160.038 1.00 100.69 ? 144 PRO A CD  1 
ATOM   895  N N   . THR A 1 158 ? 127.352 146.266 158.515 1.00 99.48  ? 145 THR A N   1 
ATOM   896  C CA  . THR A 1 158 ? 126.344 145.995 157.498 1.00 97.13  ? 145 THR A CA  1 
ATOM   897  C C   . THR A 1 158 ? 125.020 145.529 158.091 1.00 96.51  ? 145 THR A C   1 
ATOM   898  O O   . THR A 1 158 ? 124.011 146.233 157.987 1.00 95.69  ? 145 THR A O   1 
ATOM   899  C CB  . THR A 1 158 ? 126.856 144.944 156.515 1.00 93.32  ? 145 THR A CB  1 
ATOM   900  O OG1 . THR A 1 158 ? 128.246 145.172 156.255 1.00 92.41  ? 145 THR A OG1 1 
ATOM   901  C CG2 . THR A 1 158 ? 126.085 145.036 155.214 1.00 90.27  ? 145 THR A CG2 1 
ATOM   902  N N   . PHE A 1 159 ? 125.018 144.344 158.705 1.00 95.85  ? 146 PHE A N   1 
ATOM   903  C CA  . PHE A 1 159 ? 123.827 143.771 159.338 1.00 95.62  ? 146 PHE A CA  1 
ATOM   904  C C   . PHE A 1 159 ? 122.659 143.645 158.360 1.00 89.74  ? 146 PHE A C   1 
ATOM   905  O O   . PHE A 1 159 ? 121.494 143.686 158.763 1.00 88.97  ? 146 PHE A O   1 
ATOM   906  C CB  . PHE A 1 159 ? 123.410 144.582 160.570 1.00 103.07 ? 146 PHE A CB  1 
ATOM   907  C CG  . PHE A 1 159 ? 124.457 144.627 161.647 1.00 106.49 ? 146 PHE A CG  1 
ATOM   908  C CD1 . PHE A 1 159 ? 125.336 143.571 161.824 1.00 105.96 ? 146 PHE A CD1 1 
ATOM   909  C CD2 . PHE A 1 159 ? 124.565 145.728 162.480 1.00 109.15 ? 146 PHE A CD2 1 
ATOM   910  C CE1 . PHE A 1 159 ? 126.301 143.611 162.814 1.00 110.52 ? 146 PHE A CE1 1 
ATOM   911  C CE2 . PHE A 1 159 ? 125.527 145.774 163.471 1.00 114.19 ? 146 PHE A CE2 1 
ATOM   912  C CZ  . PHE A 1 159 ? 126.396 144.713 163.638 1.00 114.48 ? 146 PHE A CZ  1 
ATOM   913  N N   . SER A 1 160 ? 122.959 143.483 157.072 1.00 92.06  ? 147 SER A N   1 
ATOM   914  C CA  . SER A 1 160 ? 121.929 143.345 156.052 1.00 92.94  ? 147 SER A CA  1 
ATOM   915  C C   . SER A 1 160 ? 122.510 142.593 154.863 1.00 85.57  ? 147 SER A C   1 
ATOM   916  O O   . SER A 1 160 ? 123.681 142.771 154.523 1.00 82.36  ? 147 SER A O   1 
ATOM   917  C CB  . SER A 1 160 ? 121.390 144.710 155.609 1.00 91.59  ? 147 SER A CB  1 
ATOM   918  O OG  . SER A 1 160 ? 122.412 145.490 155.014 1.00 89.22  ? 147 SER A OG  1 
ATOM   919  N N   . SER A 1 161 ? 121.681 141.757 154.241 1.00 83.19  ? 148 SER A N   1 
ATOM   920  C CA  . SER A 1 161 ? 122.107 140.863 153.168 1.00 80.07  ? 148 SER A CA  1 
ATOM   921  C C   . SER A 1 161 ? 122.216 141.533 151.796 1.00 79.59  ? 148 SER A C   1 
ATOM   922  O O   . SER A 1 161 ? 123.207 141.295 151.092 1.00 76.11  ? 148 SER A O   1 
ATOM   923  C CB  . SER A 1 161 ? 121.169 139.652 153.098 1.00 81.08  ? 148 SER A CB  1 
ATOM   924  O OG  . SER A 1 161 ? 121.254 138.855 154.267 1.00 78.77  ? 148 SER A OG  1 
ATOM   925  N N   . PRO A 1 162 ? 121.233 142.331 151.348 1.00 85.97  ? 149 PRO A N   1 
ATOM   926  C CA  . PRO A 1 162 ? 121.383 142.965 150.024 1.00 81.41  ? 149 PRO A CA  1 
ATOM   927  C C   . PRO A 1 162 ? 122.585 143.887 149.922 1.00 78.38  ? 149 PRO A C   1 
ATOM   928  O O   . PRO A 1 162 ? 123.206 143.968 148.855 1.00 74.92  ? 149 PRO A O   1 
ATOM   929  C CB  . PRO A 1 162 ? 120.064 143.730 149.851 1.00 84.47  ? 149 PRO A CB  1 
ATOM   930  C CG  . PRO A 1 162 ? 119.111 143.047 150.751 1.00 84.10  ? 149 PRO A CG  1 
ATOM   931  C CD  . PRO A 1 162 ? 119.927 142.662 151.940 1.00 88.89  ? 149 PRO A CD  1 
ATOM   932  N N   . ALA A 1 163 ? 122.927 144.595 151.001 1.00 81.42  ? 150 ALA A N   1 
ATOM   933  C CA  . ALA A 1 163 ? 124.102 145.460 150.968 1.00 82.35  ? 150 ALA A CA  1 
ATOM   934  C C   . ALA A 1 163 ? 125.369 144.648 150.741 1.00 78.12  ? 150 ALA A C   1 
ATOM   935  O O   . ALA A 1 163 ? 126.276 145.082 150.020 1.00 75.09  ? 150 ALA A O   1 
ATOM   936  C CB  . ALA A 1 163 ? 124.199 146.265 152.263 1.00 80.60  ? 150 ALA A CB  1 
ATOM   937  N N   . ILE A 1 164 ? 125.452 143.467 151.354 1.00 76.39  ? 151 ILE A N   1 
ATOM   938  C CA  . ILE A 1 164 ? 126.581 142.576 151.105 1.00 71.46  ? 151 ILE A CA  1 
ATOM   939  C C   . ILE A 1 164 ? 126.562 142.091 149.661 1.00 72.67  ? 151 ILE A C   1 
ATOM   940  O O   . ILE A 1 164 ? 127.582 142.118 148.962 1.00 76.58  ? 151 ILE A O   1 
ATOM   941  C CB  . ILE A 1 164 ? 126.559 141.397 152.093 1.00 71.07  ? 151 ILE A CB  1 
ATOM   942  C CG1 . ILE A 1 164 ? 126.591 141.912 153.533 1.00 73.64  ? 151 ILE A CG1 1 
ATOM   943  C CG2 . ILE A 1 164 ? 127.724 140.458 151.822 1.00 65.04  ? 151 ILE A CG2 1 
ATOM   944  C CD1 . ILE A 1 164 ? 126.341 140.845 154.575 1.00 76.05  ? 151 ILE A CD1 1 
ATOM   945  N N   . GLU A 1 165 ? 125.392 141.649 149.190 1.00 71.90  ? 152 GLU A N   1 
ATOM   946  C CA  . GLU A 1 165 ? 125.302 141.021 147.874 1.00 68.30  ? 152 GLU A CA  1 
ATOM   947  C C   . GLU A 1 165 ? 125.557 142.007 146.742 1.00 68.55  ? 152 GLU A C   1 
ATOM   948  O O   . GLU A 1 165 ? 125.991 141.603 145.658 1.00 61.55  ? 152 GLU A O   1 
ATOM   949  C CB  . GLU A 1 165 ? 123.932 140.370 147.702 1.00 68.22  ? 152 GLU A CB  1 
ATOM   950  C CG  . GLU A 1 165 ? 123.667 139.276 148.711 1.00 69.51  ? 152 GLU A CG  1 
ATOM   951  C CD  . GLU A 1 165 ? 122.254 138.734 148.655 1.00 75.95  ? 152 GLU A CD  1 
ATOM   952  O OE1 . GLU A 1 165 ? 121.476 139.165 147.779 1.00 74.77  ? 152 GLU A OE1 1 
ATOM   953  O OE2 . GLU A 1 165 ? 121.921 137.874 149.499 1.00 76.64  ? 152 GLU A OE2 1 
ATOM   954  N N   . SER A 1 166 ? 125.284 143.294 146.965 1.00 72.65  ? 153 SER A N   1 
ATOM   955  C CA  . SER A 1 166 ? 125.399 144.268 145.886 1.00 71.66  ? 153 SER A CA  1 
ATOM   956  C C   . SER A 1 166 ? 126.846 144.507 145.472 1.00 69.69  ? 153 SER A C   1 
ATOM   957  O O   . SER A 1 166 ? 127.106 144.841 144.311 1.00 74.13  ? 153 SER A O   1 
ATOM   958  C CB  . SER A 1 166 ? 124.745 145.586 146.301 1.00 71.74  ? 153 SER A CB  1 
ATOM   959  O OG  . SER A 1 166 ? 123.363 145.411 146.557 1.00 70.03  ? 153 SER A OG  1 
ATOM   960  N N   . HIS A 1 167 ? 127.798 144.338 146.391 1.00 67.05  ? 154 HIS A N   1 
ATOM   961  C CA  . HIS A 1 167 ? 129.175 144.765 146.173 1.00 65.21  ? 154 HIS A CA  1 
ATOM   962  C C   . HIS A 1 167 ? 130.134 143.594 145.988 1.00 60.49  ? 154 HIS A C   1 
ATOM   963  O O   . HIS A 1 167 ? 131.337 143.742 146.225 1.00 62.62  ? 154 HIS A O   1 
ATOM   964  C CB  . HIS A 1 167 ? 129.641 145.643 147.335 1.00 69.36  ? 154 HIS A CB  1 
ATOM   965  C CG  . HIS A 1 167 ? 128.726 146.790 147.635 1.00 72.89  ? 154 HIS A CG  1 
ATOM   966  N ND1 . HIS A 1 167 ? 128.742 147.457 148.841 1.00 73.53  ? 154 HIS A ND1 1 
ATOM   967  C CD2 . HIS A 1 167 ? 127.770 147.390 146.886 1.00 75.19  ? 154 HIS A CD2 1 
ATOM   968  C CE1 . HIS A 1 167 ? 127.835 148.418 148.823 1.00 73.18  ? 154 HIS A CE1 1 
ATOM   969  N NE2 . HIS A 1 167 ? 127.232 148.399 147.648 1.00 78.80  ? 154 HIS A NE2 1 
ATOM   970  N N   . ILE A 1 168 ? 129.629 142.434 145.568 1.00 57.90  ? 155 ILE A N   1 
ATOM   971  C CA  . ILE A 1 168 ? 130.477 141.254 145.441 1.00 50.90  ? 155 ILE A CA  1 
ATOM   972  C C   . ILE A 1 168 ? 131.493 141.429 144.317 1.00 52.64  ? 155 ILE A C   1 
ATOM   973  O O   . ILE A 1 168 ? 132.653 141.019 144.442 1.00 47.43  ? 155 ILE A O   1 
ATOM   974  C CB  . ILE A 1 168 ? 129.610 140.002 145.226 1.00 47.71  ? 155 ILE A CB  1 
ATOM   975  C CG1 . ILE A 1 168 ? 128.617 139.838 146.377 1.00 49.80  ? 155 ILE A CG1 1 
ATOM   976  C CG2 . ILE A 1 168 ? 130.482 138.772 145.108 1.00 46.39  ? 155 ILE A CG2 1 
ATOM   977  C CD1 . ILE A 1 168 ? 129.270 139.565 147.709 1.00 45.06  ? 155 ILE A CD1 1 
ATOM   978  N N   . HIS A 1 169 ? 131.082 142.042 143.206 1.00 59.96  ? 156 HIS A N   1 
ATOM   979  C CA  . HIS A 1 169 ? 131.906 142.097 142.002 1.00 57.88  ? 156 HIS A CA  1 
ATOM   980  C C   . HIS A 1 169 ? 133.143 142.978 142.140 1.00 60.01  ? 156 HIS A C   1 
ATOM   981  O O   . HIS A 1 169 ? 133.876 143.126 141.157 1.00 54.71  ? 156 HIS A O   1 
ATOM   982  C CB  . HIS A 1 169 ? 131.067 142.578 140.818 1.00 55.17  ? 156 HIS A CB  1 
ATOM   983  C CG  . HIS A 1 169 ? 130.282 143.821 141.100 1.00 62.74  ? 156 HIS A CG  1 
ATOM   984  N ND1 . HIS A 1 169 ? 128.964 143.791 141.502 1.00 59.55  ? 156 HIS A ND1 1 
ATOM   985  C CD2 . HIS A 1 169 ? 130.629 145.129 141.043 1.00 64.21  ? 156 HIS A CD2 1 
ATOM   986  C CE1 . HIS A 1 169 ? 128.532 145.027 141.677 1.00 64.48  ? 156 HIS A CE1 1 
ATOM   987  N NE2 . HIS A 1 169 ? 129.522 145.857 141.407 1.00 63.78  ? 156 HIS A NE2 1 
ATOM   988  N N   . ARG A 1 170 ? 133.399 143.561 143.310 1.00 62.93  ? 157 ARG A N   1 
ATOM   989  C CA  . ARG A 1 170 ? 134.562 144.413 143.514 1.00 67.47  ? 157 ARG A CA  1 
ATOM   990  C C   . ARG A 1 170 ? 135.664 143.719 144.307 1.00 65.18  ? 157 ARG A C   1 
ATOM   991  O O   . ARG A 1 170 ? 136.513 144.394 144.900 1.00 71.60  ? 157 ARG A O   1 
ATOM   992  C CB  . ARG A 1 170 ? 134.148 145.718 144.197 1.00 72.60  ? 157 ARG A CB  1 
ATOM   993  C CG  . ARG A 1 170 ? 133.673 146.783 143.223 1.00 75.81  ? 157 ARG A CG  1 
ATOM   994  C CD  . ARG A 1 170 ? 133.283 148.063 143.940 1.00 74.59  ? 157 ARG A CD  1 
ATOM   995  N NE  . ARG A 1 170 ? 131.981 147.959 144.586 1.00 74.80  ? 157 ARG A NE  1 
ATOM   996  C CZ  . ARG A 1 170 ? 130.831 148.269 144.004 1.00 73.65  ? 157 ARG A CZ  1 
ATOM   997  N NH1 . ARG A 1 170 ? 130.781 148.684 142.750 1.00 72.39  ? 157 ARG A NH1 1 
ATOM   998  N NH2 . ARG A 1 170 ? 129.703 148.161 144.699 1.00 70.84  ? 157 ARG A NH2 1 
ATOM   999  N N   . ILE A 1 171 ? 135.668 142.391 144.329 1.00 56.27  ? 158 ILE A N   1 
ATOM   1000 C CA  . ILE A 1 171 ? 136.726 141.640 144.993 1.00 54.00  ? 158 ILE A CA  1 
ATOM   1001 C C   . ILE A 1 171 ? 137.901 141.491 144.037 1.00 57.31  ? 158 ILE A C   1 
ATOM   1002 O O   . ILE A 1 171 ? 137.735 141.054 142.892 1.00 56.34  ? 158 ILE A O   1 
ATOM   1003 C CB  . ILE A 1 171 ? 136.212 140.269 145.456 1.00 48.50  ? 158 ILE A CB  1 
ATOM   1004 C CG1 . ILE A 1 171 ? 135.064 140.440 146.451 1.00 53.82  ? 158 ILE A CG1 1 
ATOM   1005 C CG2 . ILE A 1 171 ? 137.338 139.464 146.077 1.00 49.41  ? 158 ILE A CG2 1 
ATOM   1006 C CD1 . ILE A 1 171 ? 134.449 139.135 146.901 1.00 49.14  ? 158 ILE A CD1 1 
ATOM   1007 N N   . GLU A 1 172 ? 139.091 141.864 144.500 1.00 59.83  ? 159 GLU A N   1 
ATOM   1008 C CA  . GLU A 1 172 ? 140.284 141.743 143.673 1.00 59.25  ? 159 GLU A CA  1 
ATOM   1009 C C   . GLU A 1 172 ? 140.649 140.279 143.467 1.00 56.55  ? 159 GLU A C   1 
ATOM   1010 O O   . GLU A 1 172 ? 140.511 139.453 144.372 1.00 54.61  ? 159 GLU A O   1 
ATOM   1011 C CB  . GLU A 1 172 ? 141.453 142.491 144.311 1.00 62.59  ? 159 GLU A CB  1 
ATOM   1012 C CG  . GLU A 1 172 ? 141.282 144.002 144.355 1.00 71.02  ? 159 GLU A CG  1 
ATOM   1013 C CD  . GLU A 1 172 ? 141.116 144.616 142.977 1.00 77.23  ? 159 GLU A CD  1 
ATOM   1014 O OE1 . GLU A 1 172 ? 139.973 144.658 142.472 1.00 77.75  ? 159 GLU A OE1 1 
ATOM   1015 O OE2 . GLU A 1 172 ? 142.130 145.055 142.396 1.00 79.04  ? 159 GLU A OE2 1 
ATOM   1016 N N   . GLY A 1 173 ? 141.118 139.962 142.262 1.00 56.75  ? 160 GLY A N   1 
ATOM   1017 C CA  . GLY A 1 173 ? 141.483 138.608 141.907 1.00 50.26  ? 160 GLY A CA  1 
ATOM   1018 C C   . GLY A 1 173 ? 140.349 137.763 141.374 1.00 43.28  ? 160 GLY A C   1 
ATOM   1019 O O   . GLY A 1 173 ? 140.593 136.626 140.950 1.00 43.38  ? 160 GLY A O   1 
ATOM   1020 N N   . LEU A 1 174 ? 139.124 138.278 141.381 1.00 43.21  ? 161 LEU A N   1 
ATOM   1021 C CA  . LEU A 1 174 ? 137.981 137.526 140.884 1.00 38.34  ? 161 LEU A CA  1 
ATOM   1022 C C   . LEU A 1 174 ? 138.077 137.345 139.374 1.00 43.73  ? 161 LEU A C   1 
ATOM   1023 O O   . LEU A 1 174 ? 138.564 138.223 138.656 1.00 48.33  ? 161 LEU A O   1 
ATOM   1024 C CB  . LEU A 1 174 ? 136.686 138.249 141.249 1.00 35.14  ? 161 LEU A CB  1 
ATOM   1025 C CG  . LEU A 1 174 ? 135.377 137.467 141.197 1.00 27.27  ? 161 LEU A CG  1 
ATOM   1026 C CD1 . LEU A 1 174 ? 135.438 136.277 142.126 1.00 33.05  ? 161 LEU A CD1 1 
ATOM   1027 C CD2 . LEU A 1 174 ? 134.225 138.372 141.579 1.00 30.03  ? 161 LEU A CD2 1 
ATOM   1028 N N   . SER A 1 175 ? 137.613 136.196 138.891 1.00 43.12  ? 162 SER A N   1 
ATOM   1029 C CA  . SER A 1 175 ? 137.575 135.949 137.459 1.00 41.90  ? 162 SER A CA  1 
ATOM   1030 C C   . SER A 1 175 ? 136.435 136.749 136.831 1.00 43.36  ? 162 SER A C   1 
ATOM   1031 O O   . SER A 1 175 ? 135.680 137.444 137.516 1.00 46.37  ? 162 SER A O   1 
ATOM   1032 C CB  . SER A 1 175 ? 137.431 134.456 137.179 1.00 38.18  ? 162 SER A CB  1 
ATOM   1033 O OG  . SER A 1 175 ? 138.540 133.733 137.686 1.00 40.47  ? 162 SER A OG  1 
ATOM   1034 N N   . GLN A 1 176 ? 136.307 136.651 135.505 1.00 42.19  ? 163 GLN A N   1 
ATOM   1035 C CA  . GLN A 1 176 ? 135.288 137.426 134.804 1.00 38.50  ? 163 GLN A CA  1 
ATOM   1036 C C   . GLN A 1 176 ? 133.888 137.055 135.274 1.00 35.38  ? 163 GLN A C   1 
ATOM   1037 O O   . GLN A 1 176 ? 133.034 137.929 135.457 1.00 33.57  ? 163 GLN A O   1 
ATOM   1038 C CB  . GLN A 1 176 ? 135.416 137.223 133.295 1.00 40.34  ? 163 GLN A CB  1 
ATOM   1039 C CG  . GLN A 1 176 ? 134.350 137.942 132.487 1.00 42.57  ? 163 GLN A CG  1 
ATOM   1040 C CD  . GLN A 1 176 ? 134.443 137.642 131.006 1.00 48.25  ? 163 GLN A CD  1 
ATOM   1041 O OE1 . GLN A 1 176 ? 135.339 136.924 130.562 1.00 56.04  ? 163 GLN A OE1 1 
ATOM   1042 N NE2 . GLN A 1 176 ? 133.514 138.189 130.231 1.00 39.74  ? 163 GLN A NE2 1 
ATOM   1043 N N   . LYS A 1 177 ? 133.636 135.766 135.480 1.00 34.91  ? 164 LYS A N   1 
ATOM   1044 C CA  . LYS A 1 177 ? 132.356 135.281 135.971 1.00 33.64  ? 164 LYS A CA  1 
ATOM   1045 C C   . LYS A 1 177 ? 132.566 134.521 137.272 1.00 33.08  ? 164 LYS A C   1 
ATOM   1046 O O   . LYS A 1 177 ? 133.568 133.820 137.438 1.00 37.06  ? 164 LYS A O   1 
ATOM   1047 C CB  . LYS A 1 177 ? 131.671 134.377 134.943 1.00 32.65  ? 164 LYS A CB  1 
ATOM   1048 C CG  . LYS A 1 177 ? 131.352 135.062 133.628 1.00 32.82  ? 164 LYS A CG  1 
ATOM   1049 C CD  . LYS A 1 177 ? 130.656 134.110 132.675 1.00 31.76  ? 164 LYS A CD  1 
ATOM   1050 C CE  . LYS A 1 177 ? 130.473 134.736 131.306 1.00 34.80  ? 164 LYS A CE  1 
ATOM   1051 N NZ  . LYS A 1 177 ? 131.779 135.061 130.670 1.00 35.43  ? 164 LYS A NZ  1 
ATOM   1052 N N   . PHE A 1 178 ? 131.617 134.668 138.193 1.00 29.45  ? 165 PHE A N   1 
ATOM   1053 C CA  . PHE A 1 178 ? 131.695 134.024 139.495 1.00 28.90  ? 165 PHE A CA  1 
ATOM   1054 C C   . PHE A 1 178 ? 130.323 133.483 139.866 1.00 27.85  ? 165 PHE A C   1 
ATOM   1055 O O   . PHE A 1 178 ? 129.295 133.942 139.365 1.00 32.25  ? 165 PHE A O   1 
ATOM   1056 C CB  . PHE A 1 178 ? 132.201 134.991 140.573 1.00 34.63  ? 165 PHE A CB  1 
ATOM   1057 C CG  . PHE A 1 178 ? 131.269 136.133 140.847 1.00 31.37  ? 165 PHE A CG  1 
ATOM   1058 C CD1 . PHE A 1 178 ? 131.260 137.248 140.032 1.00 31.13  ? 165 PHE A CD1 1 
ATOM   1059 C CD2 . PHE A 1 178 ? 130.404 136.092 141.923 1.00 30.81  ? 165 PHE A CD2 1 
ATOM   1060 C CE1 . PHE A 1 178 ? 130.404 138.295 140.281 1.00 32.31  ? 165 PHE A CE1 1 
ATOM   1061 C CE2 . PHE A 1 178 ? 129.545 137.136 142.175 1.00 27.19  ? 165 PHE A CE2 1 
ATOM   1062 C CZ  . PHE A 1 178 ? 129.547 138.239 141.355 1.00 29.06  ? 165 PHE A CZ  1 
ATOM   1063 N N   . ILE A 1 179 ? 130.317 132.495 140.757 1.00 24.55  ? 166 ILE A N   1 
ATOM   1064 C CA  . ILE A 1 179 ? 129.101 131.811 141.179 1.00 23.46  ? 166 ILE A CA  1 
ATOM   1065 C C   . ILE A 1 179 ? 128.818 132.168 142.630 1.00 27.03  ? 166 ILE A C   1 
ATOM   1066 O O   . ILE A 1 179 ? 129.716 132.104 143.478 1.00 31.37  ? 166 ILE A O   1 
ATOM   1067 C CB  . ILE A 1 179 ? 129.224 130.290 140.999 1.00 24.67  ? 166 ILE A CB  1 
ATOM   1068 C CG1 . ILE A 1 179 ? 129.621 129.967 139.562 1.00 27.41  ? 166 ILE A CG1 1 
ATOM   1069 C CG2 . ILE A 1 179 ? 127.918 129.608 141.342 1.00 26.47  ? 166 ILE A CG2 1 
ATOM   1070 C CD1 . ILE A 1 179 ? 129.668 128.501 139.273 1.00 26.62  ? 166 ILE A CD1 1 
ATOM   1071 N N   . TYR A 1 180 ? 127.573 132.540 142.913 1.00 27.84  ? 167 TYR A N   1 
ATOM   1072 C CA  . TYR A 1 180 ? 127.169 133.045 144.220 1.00 30.62  ? 167 TYR A CA  1 
ATOM   1073 C C   . TYR A 1 180 ? 126.250 132.043 144.910 1.00 31.75  ? 167 TYR A C   1 
ATOM   1074 O O   . TYR A 1 180 ? 125.215 131.661 144.355 1.00 31.64  ? 167 TYR A O   1 
ATOM   1075 C CB  . TYR A 1 180 ? 126.478 134.399 144.074 1.00 27.17  ? 167 TYR A CB  1 
ATOM   1076 C CG  . TYR A 1 180 ? 125.882 134.904 145.358 1.00 26.33  ? 167 TYR A CG  1 
ATOM   1077 C CD1 . TYR A 1 180 ? 126.688 135.426 146.355 1.00 27.73  ? 167 TYR A CD1 1 
ATOM   1078 C CD2 . TYR A 1 180 ? 124.515 134.856 145.576 1.00 32.17  ? 167 TYR A CD2 1 
ATOM   1079 C CE1 . TYR A 1 180 ? 126.151 135.884 147.534 1.00 34.00  ? 167 TYR A CE1 1 
ATOM   1080 C CE2 . TYR A 1 180 ? 123.968 135.313 146.753 1.00 38.46  ? 167 TYR A CE2 1 
ATOM   1081 C CZ  . TYR A 1 180 ? 124.791 135.826 147.728 1.00 39.92  ? 167 TYR A CZ  1 
ATOM   1082 O OH  . TYR A 1 180 ? 124.253 136.281 148.907 1.00 51.10  ? 167 TYR A OH  1 
ATOM   1083 N N   . LEU A 1 181 ? 126.624 131.632 146.123 1.00 32.65  ? 168 LEU A N   1 
ATOM   1084 C CA  . LEU A 1 181 ? 125.841 130.703 146.931 1.00 32.02  ? 168 LEU A CA  1 
ATOM   1085 C C   . LEU A 1 181 ? 125.571 131.316 148.300 1.00 35.04  ? 168 LEU A C   1 
ATOM   1086 O O   . LEU A 1 181 ? 126.454 131.945 148.894 1.00 39.01  ? 168 LEU A O   1 
ATOM   1087 C CB  . LEU A 1 181 ? 126.557 129.356 147.094 1.00 30.29  ? 168 LEU A CB  1 
ATOM   1088 C CG  . LEU A 1 181 ? 126.761 128.491 145.846 1.00 30.01  ? 168 LEU A CG  1 
ATOM   1089 C CD1 . LEU A 1 181 ? 128.007 128.905 145.077 1.00 31.47  ? 168 LEU A CD1 1 
ATOM   1090 C CD2 . LEU A 1 181 ? 126.818 127.015 146.209 1.00 31.08  ? 168 LEU A CD2 1 
ATOM   1091 N N   . ASN A 1 182 ? 124.353 131.125 148.805 1.00 35.87  ? 169 ASN A N   1 
ATOM   1092 C CA  . ASN A 1 182 ? 123.923 131.759 150.052 1.00 41.26  ? 169 ASN A CA  1 
ATOM   1093 C C   . ASN A 1 182 ? 123.888 130.784 151.225 1.00 50.73  ? 169 ASN A C   1 
ATOM   1094 O O   . ASN A 1 182 ? 123.025 130.895 152.105 1.00 55.48  ? 169 ASN A O   1 
ATOM   1095 C CB  . ASN A 1 182 ? 122.565 132.428 149.870 1.00 42.77  ? 169 ASN A CB  1 
ATOM   1096 C CG  . ASN A 1 182 ? 121.628 131.619 149.001 1.00 41.43  ? 169 ASN A CG  1 
ATOM   1097 O OD1 . ASN A 1 182 ? 121.842 131.486 147.797 1.00 39.13  ? 169 ASN A OD1 1 
ATOM   1098 N ND2 . ASN A 1 182 ? 120.571 131.090 149.601 1.00 44.02  ? 169 ASN A ND2 1 
ATOM   1099 N N   . ASP A 1 183 ? 124.821 129.831 151.263 1.00 51.31  ? 170 ASP A N   1 
ATOM   1100 C CA  . ASP A 1 183 ? 125.097 129.024 152.447 1.00 52.10  ? 170 ASP A CA  1 
ATOM   1101 C C   . ASP A 1 183 ? 123.891 128.199 152.884 1.00 54.84  ? 170 ASP A C   1 
ATOM   1102 O O   . ASP A 1 183 ? 123.853 127.705 154.014 1.00 56.46  ? 170 ASP A O   1 
ATOM   1103 C CB  . ASP A 1 183 ? 125.594 129.917 153.598 1.00 54.84  ? 170 ASP A CB  1 
ATOM   1104 C CG  . ASP A 1 183 ? 126.656 129.227 154.471 1.00 60.82  ? 170 ASP A CG  1 
ATOM   1105 O OD1 . ASP A 1 183 ? 126.503 128.021 154.756 1.00 56.12  ? 170 ASP A OD1 1 
ATOM   1106 O OD2 . ASP A 1 183 ? 127.635 129.887 154.862 1.00 69.26  ? 170 ASP A OD2 1 
ATOM   1107 N N   . ASP A 1 184 ? 122.881 128.075 152.023 1.00 54.02  ? 171 ASP A N   1 
ATOM   1108 C CA  . ASP A 1 184 ? 121.835 127.077 152.209 1.00 55.16  ? 171 ASP A CA  1 
ATOM   1109 C C   . ASP A 1 184 ? 121.556 126.274 150.942 1.00 54.15  ? 171 ASP A C   1 
ATOM   1110 O O   . ASP A 1 184 ? 120.547 125.562 150.880 1.00 59.40  ? 171 ASP A O   1 
ATOM   1111 C CB  . ASP A 1 184 ? 120.548 127.729 152.725 1.00 60.51  ? 171 ASP A CB  1 
ATOM   1112 C CG  . ASP A 1 184 ? 119.923 128.661 151.721 1.00 61.95  ? 171 ASP A CG  1 
ATOM   1113 O OD1 . ASP A 1 184 ? 120.650 129.513 151.170 1.00 58.02  ? 171 ASP A OD1 1 
ATOM   1114 O OD2 . ASP A 1 184 ? 118.706 128.531 151.466 1.00 68.23  ? 171 ASP A OD2 1 
ATOM   1115 N N   . VAL A 1 185 ? 122.425 126.364 149.933 1.00 52.14  ? 172 VAL A N   1 
ATOM   1116 C CA  . VAL A 1 185 ? 122.271 125.623 148.689 1.00 49.17  ? 172 VAL A CA  1 
ATOM   1117 C C   . VAL A 1 185 ? 123.556 124.854 148.413 1.00 47.98  ? 172 VAL A C   1 
ATOM   1118 O O   . VAL A 1 185 ? 124.620 125.155 148.957 1.00 49.58  ? 172 VAL A O   1 
ATOM   1119 C CB  . VAL A 1 185 ? 121.925 126.536 147.493 1.00 40.46  ? 172 VAL A CB  1 
ATOM   1120 C CG1 . VAL A 1 185 ? 120.603 127.234 147.732 1.00 42.90  ? 172 VAL A CG1 1 
ATOM   1121 C CG2 . VAL A 1 185 ? 123.029 127.548 147.257 1.00 40.60  ? 172 VAL A CG2 1 
ATOM   1122 N N   . MET A 1 186 ? 123.443 123.841 147.558 1.00 43.83  ? 173 MET A N   1 
ATOM   1123 C CA  . MET A 1 186 ? 124.577 122.986 147.231 1.00 42.91  ? 173 MET A CA  1 
ATOM   1124 C C   . MET A 1 186 ? 124.289 122.270 145.920 1.00 37.22  ? 173 MET A C   1 
ATOM   1125 O O   . MET A 1 186 ? 123.197 122.373 145.358 1.00 38.99  ? 173 MET A O   1 
ATOM   1126 C CB  . MET A 1 186 ? 124.854 121.983 148.352 1.00 45.83  ? 173 MET A CB  1 
ATOM   1127 C CG  . MET A 1 186 ? 123.880 120.826 148.391 1.00 46.42  ? 173 MET A CG  1 
ATOM   1128 S SD  . MET A 1 186 ? 123.941 119.963 149.967 1.00 75.93  ? 173 MET A SD  1 
ATOM   1129 C CE  . MET A 1 186 ? 123.473 121.291 151.072 1.00 65.89  ? 173 MET A CE  1 
ATOM   1130 N N   . PHE A 1 187 ? 125.285 121.536 145.438 1.00 34.98  ? 174 PHE A N   1 
ATOM   1131 C CA  . PHE A 1 187 ? 125.167 120.774 144.203 1.00 42.06  ? 174 PHE A CA  1 
ATOM   1132 C C   . PHE A 1 187 ? 124.974 119.302 144.545 1.00 49.07  ? 174 PHE A C   1 
ATOM   1133 O O   . PHE A 1 187 ? 125.827 118.693 145.202 1.00 52.89  ? 174 PHE A O   1 
ATOM   1134 C CB  . PHE A 1 187 ? 126.402 120.975 143.324 1.00 39.44  ? 174 PHE A CB  1 
ATOM   1135 C CG  . PHE A 1 187 ? 126.662 122.411 142.967 1.00 37.80  ? 174 PHE A CG  1 
ATOM   1136 C CD1 . PHE A 1 187 ? 127.490 123.194 143.749 1.00 39.30  ? 174 PHE A CD1 1 
ATOM   1137 C CD2 . PHE A 1 187 ? 126.070 122.979 141.854 1.00 34.84  ? 174 PHE A CD2 1 
ATOM   1138 C CE1 . PHE A 1 187 ? 127.727 124.513 143.424 1.00 35.36  ? 174 PHE A CE1 1 
ATOM   1139 C CE2 . PHE A 1 187 ? 126.306 124.298 141.525 1.00 33.46  ? 174 PHE A CE2 1 
ATOM   1140 C CZ  . PHE A 1 187 ? 127.136 125.065 142.312 1.00 32.57  ? 174 PHE A CZ  1 
ATOM   1141 N N   . GLY A 1 188 ? 123.855 118.736 144.101 1.00 47.96  ? 175 GLY A N   1 
ATOM   1142 C CA  . GLY A 1 188 ? 123.545 117.342 144.315 1.00 42.22  ? 175 GLY A CA  1 
ATOM   1143 C C   . GLY A 1 188 ? 123.797 116.451 143.125 1.00 42.32  ? 175 GLY A C   1 
ATOM   1144 O O   . GLY A 1 188 ? 123.619 115.234 143.228 1.00 50.75  ? 175 GLY A O   1 
ATOM   1145 N N   . LYS A 1 189 ? 124.204 117.020 141.993 1.00 39.54  ? 176 LYS A N   1 
ATOM   1146 C CA  . LYS A 1 189 ? 124.551 116.256 140.806 1.00 44.18  ? 176 LYS A CA  1 
ATOM   1147 C C   . LYS A 1 189 ? 125.722 116.947 140.124 1.00 47.58  ? 176 LYS A C   1 
ATOM   1148 O O   . LYS A 1 189 ? 126.016 118.113 140.394 1.00 49.15  ? 176 LYS A O   1 
ATOM   1149 C CB  . LYS A 1 189 ? 123.354 116.127 139.850 1.00 41.15  ? 176 LYS A CB  1 
ATOM   1150 C CG  . LYS A 1 189 ? 123.514 115.067 138.767 1.00 42.21  ? 176 LYS A CG  1 
ATOM   1151 C CD  . LYS A 1 189 ? 122.266 114.963 137.907 1.00 47.47  ? 176 LYS A CD  1 
ATOM   1152 C CE  . LYS A 1 189 ? 121.097 114.412 138.702 1.00 51.07  ? 176 LYS A CE  1 
ATOM   1153 N NZ  . LYS A 1 189 ? 119.823 114.477 137.937 1.00 50.96  ? 176 LYS A NZ  1 
ATOM   1154 N N   . ASP A 1 190 ? 126.401 116.211 139.246 1.00 46.28  ? 177 ASP A N   1 
ATOM   1155 C CA  . ASP A 1 190 ? 127.520 116.778 138.506 1.00 44.52  ? 177 ASP A CA  1 
ATOM   1156 C C   . ASP A 1 190 ? 127.061 117.990 137.706 1.00 44.69  ? 177 ASP A C   1 
ATOM   1157 O O   . ASP A 1 190 ? 126.232 117.871 136.798 1.00 46.44  ? 177 ASP A O   1 
ATOM   1158 C CB  . ASP A 1 190 ? 128.132 115.726 137.584 1.00 43.10  ? 177 ASP A CB  1 
ATOM   1159 C CG  . ASP A 1 190 ? 128.835 114.625 138.348 1.00 53.83  ? 177 ASP A CG  1 
ATOM   1160 O OD1 . ASP A 1 190 ? 129.380 114.910 139.434 1.00 47.06  ? 177 ASP A OD1 1 
ATOM   1161 O OD2 . ASP A 1 190 ? 128.842 113.474 137.865 1.00 68.47  ? 177 ASP A OD2 1 
ATOM   1162 N N   . VAL A 1 191 ? 127.601 119.155 138.050 1.00 42.45  ? 178 VAL A N   1 
ATOM   1163 C CA  . VAL A 1 191 ? 127.235 120.424 137.436 1.00 38.53  ? 178 VAL A CA  1 
ATOM   1164 C C   . VAL A 1 191 ? 128.439 120.957 136.677 1.00 39.83  ? 178 VAL A C   1 
ATOM   1165 O O   . VAL A 1 191 ? 129.569 120.908 137.175 1.00 41.83  ? 178 VAL A O   1 
ATOM   1166 C CB  . VAL A 1 191 ? 126.750 121.436 138.490 1.00 36.62  ? 178 VAL A CB  1 
ATOM   1167 C CG1 . VAL A 1 191 ? 126.629 122.822 137.887 1.00 33.73  ? 178 VAL A CG1 1 
ATOM   1168 C CG2 . VAL A 1 191 ? 125.419 120.992 139.061 1.00 36.70  ? 178 VAL A CG2 1 
ATOM   1169 N N   . TRP A 1 192 ? 128.198 121.451 135.472 1.00 36.74  ? 179 TRP A N   1 
ATOM   1170 C CA  . TRP A 1 192 ? 129.225 121.960 134.579 1.00 34.04  ? 179 TRP A CA  1 
ATOM   1171 C C   . TRP A 1 192 ? 128.854 123.365 134.137 1.00 33.84  ? 179 TRP A C   1 
ATOM   1172 O O   . TRP A 1 192 ? 127.683 123.751 134.198 1.00 35.24  ? 179 TRP A O   1 
ATOM   1173 C CB  . TRP A 1 192 ? 129.388 121.031 133.368 1.00 35.45  ? 179 TRP A CB  1 
ATOM   1174 C CG  . TRP A 1 192 ? 129.865 119.674 133.766 1.00 32.29  ? 179 TRP A CG  1 
ATOM   1175 C CD1 . TRP A 1 192 ? 129.094 118.594 134.075 1.00 32.22  ? 179 TRP A CD1 1 
ATOM   1176 C CD2 . TRP A 1 192 ? 131.224 119.255 133.922 1.00 33.08  ? 179 TRP A CD2 1 
ATOM   1177 N NE1 . TRP A 1 192 ? 129.890 117.525 134.403 1.00 36.54  ? 179 TRP A NE1 1 
ATOM   1178 C CE2 . TRP A 1 192 ? 131.202 117.906 134.316 1.00 35.81  ? 179 TRP A CE2 1 
ATOM   1179 C CE3 . TRP A 1 192 ? 132.458 119.889 133.759 1.00 35.16  ? 179 TRP A CE3 1 
ATOM   1180 C CZ2 . TRP A 1 192 ? 132.364 117.180 134.551 1.00 39.55  ? 179 TRP A CZ2 1 
ATOM   1181 C CZ3 . TRP A 1 192 ? 133.609 119.167 133.993 1.00 33.59  ? 179 TRP A CZ3 1 
ATOM   1182 C CH2 . TRP A 1 192 ? 133.556 117.827 134.384 1.00 35.17  ? 179 TRP A CH2 1 
ATOM   1183 N N   . PRO A 1 193 ? 129.833 124.170 133.712 1.00 31.19  ? 180 PRO A N   1 
ATOM   1184 C CA  . PRO A 1 193 ? 129.525 125.573 133.390 1.00 27.23  ? 180 PRO A CA  1 
ATOM   1185 C C   . PRO A 1 193 ? 128.491 125.736 132.292 1.00 34.64  ? 180 PRO A C   1 
ATOM   1186 O O   . PRO A 1 193 ? 127.784 126.751 132.272 1.00 33.41  ? 180 PRO A O   1 
ATOM   1187 C CB  . PRO A 1 193 ? 130.888 126.144 132.975 1.00 26.12  ? 180 PRO A CB  1 
ATOM   1188 C CG  . PRO A 1 193 ? 131.692 124.956 132.584 1.00 29.00  ? 180 PRO A CG  1 
ATOM   1189 C CD  . PRO A 1 193 ? 131.259 123.869 133.507 1.00 30.74  ? 180 PRO A CD  1 
ATOM   1190 N N   . ASP A 1 194 ? 128.373 124.770 131.376 1.00 37.51  ? 181 ASP A N   1 
ATOM   1191 C CA  . ASP A 1 194 ? 127.330 124.849 130.359 1.00 35.84  ? 181 ASP A CA  1 
ATOM   1192 C C   . ASP A 1 194 ? 125.936 124.728 130.959 1.00 36.88  ? 181 ASP A C   1 
ATOM   1193 O O   . ASP A 1 194 ? 124.955 125.059 130.286 1.00 40.12  ? 181 ASP A O   1 
ATOM   1194 C CB  . ASP A 1 194 ? 127.540 123.778 129.288 1.00 34.27  ? 181 ASP A CB  1 
ATOM   1195 C CG  . ASP A 1 194 ? 127.486 122.374 129.844 1.00 39.36  ? 181 ASP A CG  1 
ATOM   1196 O OD1 . ASP A 1 194 ? 126.371 121.871 130.092 1.00 40.58  ? 181 ASP A OD1 1 
ATOM   1197 O OD2 . ASP A 1 194 ? 128.561 121.770 130.027 1.00 44.81  ? 181 ASP A OD2 1 
ATOM   1198 N N   . ASP A 1 195 ? 125.825 124.243 132.197 1.00 34.90  ? 182 ASP A N   1 
ATOM   1199 C CA  . ASP A 1 195 ? 124.547 124.297 132.898 1.00 33.87  ? 182 ASP A CA  1 
ATOM   1200 C C   . ASP A 1 195 ? 124.168 125.730 133.249 1.00 34.56  ? 182 ASP A C   1 
ATOM   1201 O O   . ASP A 1 195 ? 122.982 126.032 133.421 1.00 38.71  ? 182 ASP A O   1 
ATOM   1202 C CB  . ASP A 1 195 ? 124.600 123.431 134.156 1.00 34.89  ? 182 ASP A CB  1 
ATOM   1203 C CG  . ASP A 1 195 ? 123.230 123.174 134.744 1.00 40.52  ? 182 ASP A CG  1 
ATOM   1204 O OD1 . ASP A 1 195 ? 122.224 123.408 134.042 1.00 43.20  ? 182 ASP A OD1 1 
ATOM   1205 O OD2 . ASP A 1 195 ? 123.158 122.739 135.911 1.00 40.49  ? 182 ASP A OD2 1 
ATOM   1206 N N   . PHE A 1 196 ? 125.154 126.618 133.375 1.00 32.15  ? 183 PHE A N   1 
ATOM   1207 C CA  . PHE A 1 196 ? 124.901 128.026 133.652 1.00 31.87  ? 183 PHE A CA  1 
ATOM   1208 C C   . PHE A 1 196 ? 125.064 128.926 132.436 1.00 32.20  ? 183 PHE A C   1 
ATOM   1209 O O   . PHE A 1 196 ? 124.336 129.916 132.315 1.00 37.04  ? 183 PHE A O   1 
ATOM   1210 C CB  . PHE A 1 196 ? 125.829 128.530 134.764 1.00 33.58  ? 183 PHE A CB  1 
ATOM   1211 C CG  . PHE A 1 196 ? 125.599 127.873 136.095 1.00 31.13  ? 183 PHE A CG  1 
ATOM   1212 C CD1 . PHE A 1 196 ? 124.475 128.171 136.843 1.00 29.39  ? 183 PHE A CD1 1 
ATOM   1213 C CD2 . PHE A 1 196 ? 126.515 126.970 136.604 1.00 34.94  ? 183 PHE A CD2 1 
ATOM   1214 C CE1 . PHE A 1 196 ? 124.264 127.571 138.065 1.00 33.84  ? 183 PHE A CE1 1 
ATOM   1215 C CE2 . PHE A 1 196 ? 126.309 126.369 137.827 1.00 36.21  ? 183 PHE A CE2 1 
ATOM   1216 C CZ  . PHE A 1 196 ? 125.183 126.671 138.558 1.00 37.04  ? 183 PHE A CZ  1 
ATOM   1217 N N   . TYR A 1 197 ? 125.996 128.618 131.536 1.00 32.74  ? 184 TYR A N   1 
ATOM   1218 C CA  . TYR A 1 197 ? 126.308 129.523 130.437 1.00 37.45  ? 184 TYR A CA  1 
ATOM   1219 C C   . TYR A 1 197 ? 126.772 128.742 129.218 1.00 40.92  ? 184 TYR A C   1 
ATOM   1220 O O   . TYR A 1 197 ? 127.726 127.964 129.302 1.00 39.75  ? 184 TYR A O   1 
ATOM   1221 C CB  . TYR A 1 197 ? 127.385 130.530 130.854 1.00 36.35  ? 184 TYR A CB  1 
ATOM   1222 C CG  . TYR A 1 197 ? 127.939 131.353 129.713 1.00 38.56  ? 184 TYR A CG  1 
ATOM   1223 C CD1 . TYR A 1 197 ? 127.215 132.408 129.178 1.00 39.61  ? 184 TYR A CD1 1 
ATOM   1224 C CD2 . TYR A 1 197 ? 129.189 131.080 129.178 1.00 41.14  ? 184 TYR A CD2 1 
ATOM   1225 C CE1 . TYR A 1 197 ? 127.716 133.164 128.137 1.00 41.22  ? 184 TYR A CE1 1 
ATOM   1226 C CE2 . TYR A 1 197 ? 129.699 131.832 128.138 1.00 44.27  ? 184 TYR A CE2 1 
ATOM   1227 C CZ  . TYR A 1 197 ? 128.959 132.871 127.622 1.00 43.43  ? 184 TYR A CZ  1 
ATOM   1228 O OH  . TYR A 1 197 ? 129.462 133.622 126.585 1.00 47.08  ? 184 TYR A OH  1 
ATOM   1229 N N   . SER A 1 198 ? 126.103 128.966 128.090 1.00 44.17  ? 185 SER A N   1 
ATOM   1230 C CA  . SER A 1 198 ? 126.510 128.433 126.798 1.00 45.62  ? 185 SER A CA  1 
ATOM   1231 C C   . SER A 1 198 ? 126.606 129.584 125.809 1.00 46.25  ? 185 SER A C   1 
ATOM   1232 O O   . SER A 1 198 ? 125.725 130.447 125.768 1.00 48.54  ? 185 SER A O   1 
ATOM   1233 C CB  . SER A 1 198 ? 125.522 127.376 126.294 1.00 46.56  ? 185 SER A CB  1 
ATOM   1234 O OG  . SER A 1 198 ? 126.002 126.746 125.121 1.00 48.26  ? 185 SER A OG  1 
ATOM   1235 N N   . HIS A 1 199 ? 127.673 129.590 125.004 1.00 44.33  ? 186 HIS A N   1 
ATOM   1236 C CA  . HIS A 1 199 ? 127.949 130.745 124.151 1.00 46.02  ? 186 HIS A CA  1 
ATOM   1237 C C   . HIS A 1 199 ? 126.814 131.003 123.174 1.00 47.91  ? 186 HIS A C   1 
ATOM   1238 O O   . HIS A 1 199 ? 126.388 132.150 122.995 1.00 52.12  ? 186 HIS A O   1 
ATOM   1239 C CB  . HIS A 1 199 ? 129.248 130.534 123.372 1.00 49.03  ? 186 HIS A CB  1 
ATOM   1240 C CG  . HIS A 1 199 ? 130.466 130.432 124.231 1.00 50.29  ? 186 HIS A CG  1 
ATOM   1241 N ND1 . HIS A 1 199 ? 131.718 130.798 123.788 1.00 48.80  ? 186 HIS A ND1 1 
ATOM   1242 C CD2 . HIS A 1 199 ? 130.628 129.998 125.503 1.00 53.21  ? 186 HIS A CD2 1 
ATOM   1243 C CE1 . HIS A 1 199 ? 132.598 130.600 124.752 1.00 53.05  ? 186 HIS A CE1 1 
ATOM   1244 N NE2 . HIS A 1 199 ? 131.962 130.115 125.803 1.00 55.52  ? 186 HIS A NE2 1 
ATOM   1245 N N   . SER A 1 200 ? 126.310 129.946 122.535 1.00 47.60  ? 187 SER A N   1 
ATOM   1246 C CA  . SER A 1 200 ? 125.352 130.115 121.448 1.00 49.98  ? 187 SER A CA  1 
ATOM   1247 C C   . SER A 1 200 ? 124.058 130.752 121.936 1.00 49.59  ? 187 SER A C   1 
ATOM   1248 O O   . SER A 1 200 ? 123.519 131.655 121.286 1.00 51.40  ? 187 SER A O   1 
ATOM   1249 C CB  . SER A 1 200 ? 125.064 128.766 120.791 1.00 48.46  ? 187 SER A CB  1 
ATOM   1250 O OG  . SER A 1 200 ? 126.244 128.190 120.263 1.00 45.68  ? 187 SER A OG  1 
ATOM   1251 N N   . LYS A 1 201 ? 123.546 130.301 123.078 1.00 44.59  ? 188 LYS A N   1 
ATOM   1252 C CA  . LYS A 1 201 ? 122.295 130.811 123.619 1.00 44.72  ? 188 LYS A CA  1 
ATOM   1253 C C   . LYS A 1 201 ? 122.509 131.704 124.831 1.00 45.60  ? 188 LYS A C   1 
ATOM   1254 O O   . LYS A 1 201 ? 121.554 131.978 125.565 1.00 43.95  ? 188 LYS A O   1 
ATOM   1255 C CB  . LYS A 1 201 ? 121.360 129.652 123.968 1.00 49.81  ? 188 LYS A CB  1 
ATOM   1256 C CG  . LYS A 1 201 ? 120.963 128.816 122.761 1.00 54.67  ? 188 LYS A CG  1 
ATOM   1257 C CD  . LYS A 1 201 ? 119.565 128.242 122.913 1.00 57.47  ? 188 LYS A CD  1 
ATOM   1258 C CE  . LYS A 1 201 ? 118.556 129.341 123.200 1.00 59.66  ? 188 LYS A CE  1 
ATOM   1259 N NZ  . LYS A 1 201 ? 117.158 128.834 123.194 1.00 58.42  ? 188 LYS A NZ  1 
ATOM   1260 N N   . GLY A 1 202 ? 123.737 132.158 125.061 1.00 49.59  ? 189 GLY A N   1 
ATOM   1261 C CA  . GLY A 1 202 ? 124.012 133.101 126.121 1.00 46.12  ? 189 GLY A CA  1 
ATOM   1262 C C   . GLY A 1 202 ? 123.916 132.475 127.503 1.00 39.89  ? 189 GLY A C   1 
ATOM   1263 O O   . GLY A 1 202 ? 123.827 131.261 127.678 1.00 42.15  ? 189 GLY A O   1 
ATOM   1264 N N   . GLN A 1 203 ? 123.935 133.352 128.500 1.00 37.28  ? 190 GLN A N   1 
ATOM   1265 C CA  . GLN A 1 203 ? 123.803 132.908 129.878 1.00 34.20  ? 190 GLN A CA  1 
ATOM   1266 C C   . GLN A 1 203 ? 122.419 132.317 130.107 1.00 38.42  ? 190 GLN A C   1 
ATOM   1267 O O   . GLN A 1 203 ? 121.422 132.798 129.564 1.00 45.43  ? 190 GLN A O   1 
ATOM   1268 C CB  . GLN A 1 203 ? 124.056 134.074 130.832 1.00 31.21  ? 190 GLN A CB  1 
ATOM   1269 C CG  . GLN A 1 203 ? 124.139 133.677 132.290 1.00 30.86  ? 190 GLN A CG  1 
ATOM   1270 C CD  . GLN A 1 203 ? 125.031 134.601 133.087 1.00 33.28  ? 190 GLN A CD  1 
ATOM   1271 O OE1 . GLN A 1 203 ? 126.072 135.044 132.604 1.00 34.55  ? 190 GLN A OE1 1 
ATOM   1272 N NE2 . GLN A 1 203 ? 124.626 134.901 134.313 1.00 34.39  ? 190 GLN A NE2 1 
ATOM   1273 N N   . LYS A 1 204 ? 122.361 131.265 130.915 1.00 37.82  ? 191 LYS A N   1 
ATOM   1274 C CA  . LYS A 1 204 ? 121.133 130.518 131.143 1.00 33.41  ? 191 LYS A CA  1 
ATOM   1275 C C   . LYS A 1 204 ? 120.433 131.047 132.387 1.00 34.32  ? 191 LYS A C   1 
ATOM   1276 O O   . LYS A 1 204 ? 121.032 131.106 133.465 1.00 34.62  ? 191 LYS A O   1 
ATOM   1277 C CB  . LYS A 1 204 ? 121.432 129.027 131.289 1.00 31.58  ? 191 LYS A CB  1 
ATOM   1278 C CG  . LYS A 1 204 ? 120.202 128.152 131.310 1.00 37.88  ? 191 LYS A CG  1 
ATOM   1279 C CD  . LYS A 1 204 ? 120.570 126.679 131.314 1.00 37.74  ? 191 LYS A CD  1 
ATOM   1280 C CE  . LYS A 1 204 ? 121.307 126.290 130.044 1.00 37.29  ? 191 LYS A CE  1 
ATOM   1281 N NZ  . LYS A 1 204 ? 121.636 124.839 130.014 1.00 32.13  ? 191 LYS A NZ  1 
ATOM   1282 N N   . VAL A 1 205 ? 119.169 131.430 132.234 1.00 37.33  ? 192 VAL A N   1 
ATOM   1283 C CA  . VAL A 1 205 ? 118.389 132.047 133.300 1.00 37.83  ? 192 VAL A CA  1 
ATOM   1284 C C   . VAL A 1 205 ? 117.267 131.101 133.693 1.00 38.15  ? 192 VAL A C   1 
ATOM   1285 O O   . VAL A 1 205 ? 116.470 130.684 132.844 1.00 42.48  ? 192 VAL A O   1 
ATOM   1286 C CB  . VAL A 1 205 ? 117.826 133.411 132.869 1.00 35.48  ? 192 VAL A CB  1 
ATOM   1287 C CG1 . VAL A 1 205 ? 116.898 133.959 133.939 1.00 35.64  ? 192 VAL A CG1 1 
ATOM   1288 C CG2 . VAL A 1 205 ? 118.957 134.385 132.585 1.00 34.75  ? 192 VAL A CG2 1 
ATOM   1289 N N   . TYR A 1 206 ? 117.197 130.774 134.980 1.00 36.42  ? 193 TYR A N   1 
ATOM   1290 C CA  . TYR A 1 206 ? 116.153 129.915 135.519 1.00 42.08  ? 193 TYR A CA  1 
ATOM   1291 C C   . TYR A 1 206 ? 115.117 130.777 136.224 1.00 42.90  ? 193 TYR A C   1 
ATOM   1292 O O   . TYR A 1 206 ? 115.464 131.601 137.075 1.00 44.93  ? 193 TYR A O   1 
ATOM   1293 C CB  . TYR A 1 206 ? 116.733 128.889 136.493 1.00 40.40  ? 193 TYR A CB  1 
ATOM   1294 C CG  . TYR A 1 206 ? 117.830 128.018 135.920 1.00 40.59  ? 193 TYR A CG  1 
ATOM   1295 C CD1 . TYR A 1 206 ? 119.136 128.479 135.836 1.00 36.05  ? 193 TYR A CD1 1 
ATOM   1296 C CD2 . TYR A 1 206 ? 117.565 126.726 135.490 1.00 39.32  ? 193 TYR A CD2 1 
ATOM   1297 C CE1 . TYR A 1 206 ? 120.142 127.687 135.324 1.00 36.27  ? 193 TYR A CE1 1 
ATOM   1298 C CE2 . TYR A 1 206 ? 118.567 125.925 134.976 1.00 36.38  ? 193 TYR A CE2 1 
ATOM   1299 C CZ  . TYR A 1 206 ? 119.853 126.412 134.897 1.00 36.04  ? 193 TYR A CZ  1 
ATOM   1300 O OH  . TYR A 1 206 ? 120.859 125.624 134.388 1.00 35.45  ? 193 TYR A OH  1 
ATOM   1301 N N   . LEU A 1 207 ? 113.850 130.576 135.879 1.00 45.87  ? 194 LEU A N   1 
ATOM   1302 C CA  . LEU A 1 207 ? 112.761 131.380 136.406 1.00 48.59  ? 194 LEU A CA  1 
ATOM   1303 C C   . LEU A 1 207 ? 111.769 130.495 137.148 1.00 51.19  ? 194 LEU A C   1 
ATOM   1304 O O   . LEU A 1 207 ? 111.802 129.266 137.050 1.00 51.87  ? 194 LEU A O   1 
ATOM   1305 C CB  . LEU A 1 207 ? 112.055 132.155 135.287 1.00 52.69  ? 194 LEU A CB  1 
ATOM   1306 C CG  . LEU A 1 207 ? 112.890 133.250 134.623 1.00 46.93  ? 194 LEU A CG  1 
ATOM   1307 C CD1 . LEU A 1 207 ? 112.121 133.910 133.493 1.00 49.88  ? 194 LEU A CD1 1 
ATOM   1308 C CD2 . LEU A 1 207 ? 113.322 134.283 135.650 1.00 48.13  ? 194 LEU A CD2 1 
ATOM   1309 N N   . THR A 1 208 ? 110.881 131.143 137.892 1.00 55.62  ? 195 THR A N   1 
ATOM   1310 C CA  . THR A 1 208 ? 109.961 130.463 138.795 1.00 62.14  ? 195 THR A CA  1 
ATOM   1311 C C   . THR A 1 208 ? 108.653 131.249 138.822 1.00 71.90  ? 195 THR A C   1 
ATOM   1312 O O   . THR A 1 208 ? 108.348 131.997 137.887 1.00 73.53  ? 195 THR A O   1 
ATOM   1313 C CB  . THR A 1 208 ? 110.583 130.303 140.194 1.00 63.04  ? 195 THR A CB  1 
ATOM   1314 O OG1 . THR A 1 208 ? 111.276 131.505 140.554 1.00 62.40  ? 195 THR A OG1 1 
ATOM   1315 C CG2 . THR A 1 208 ? 111.544 129.123 140.229 1.00 61.57  ? 195 THR A CG2 1 
ATOM   1316 N N   . TRP A 1 209 ? 107.873 131.048 139.880 1.00 79.58  ? 196 TRP A N   1 
ATOM   1317 C CA  . TRP A 1 209 ? 106.556 131.655 140.010 1.00 84.48  ? 196 TRP A CA  1 
ATOM   1318 C C   . TRP A 1 209 ? 106.623 133.163 139.771 1.00 84.45  ? 196 TRP A C   1 
ATOM   1319 O O   . TRP A 1 209 ? 107.617 133.806 140.135 1.00 78.37  ? 196 TRP A O   1 
ATOM   1320 C CB  . TRP A 1 209 ? 105.988 131.377 141.405 1.00 85.49  ? 196 TRP A CB  1 
ATOM   1321 C CG  . TRP A 1 209 ? 106.824 131.952 142.516 1.00 89.35  ? 196 TRP A CG  1 
ATOM   1322 C CD1 . TRP A 1 209 ? 106.725 133.203 143.054 1.00 94.19  ? 196 TRP A CD1 1 
ATOM   1323 C CD2 . TRP A 1 209 ? 107.889 131.298 143.220 1.00 86.96  ? 196 TRP A CD2 1 
ATOM   1324 N NE1 . TRP A 1 209 ? 107.659 133.368 144.049 1.00 92.58  ? 196 TRP A NE1 1 
ATOM   1325 C CE2 . TRP A 1 209 ? 108.386 132.213 144.171 1.00 87.96  ? 196 TRP A CE2 1 
ATOM   1326 C CE3 . TRP A 1 209 ? 108.469 130.028 143.141 1.00 82.18  ? 196 TRP A CE3 1 
ATOM   1327 C CZ2 . TRP A 1 209 ? 109.435 131.899 145.034 1.00 86.06  ? 196 TRP A CZ2 1 
ATOM   1328 C CZ3 . TRP A 1 209 ? 109.511 129.718 143.999 1.00 84.46  ? 196 TRP A CZ3 1 
ATOM   1329 C CH2 . TRP A 1 209 ? 109.982 130.650 144.933 1.00 87.33  ? 196 TRP A CH2 1 
ATOM   1330 N N   . PRO A 1 210 ? 105.600 133.755 139.160 1.00 90.69  ? 197 PRO A N   1 
ATOM   1331 C CA  . PRO A 1 210 ? 105.589 135.208 138.962 1.00 91.87  ? 197 PRO A CA  1 
ATOM   1332 C C   . PRO A 1 210 ? 105.491 135.951 140.286 1.00 96.21  ? 197 PRO A C   1 
ATOM   1333 O O   . PRO A 1 210 ? 105.040 135.417 141.302 1.00 99.16  ? 197 PRO A O   1 
ATOM   1334 C CB  . PRO A 1 210 ? 104.344 135.442 138.100 1.00 98.45  ? 197 PRO A CB  1 
ATOM   1335 C CG  . PRO A 1 210 ? 104.018 134.099 137.507 1.00 92.94  ? 197 PRO A CG  1 
ATOM   1336 C CD  . PRO A 1 210 ? 104.440 133.101 138.535 1.00 92.53  ? 197 PRO A CD  1 
ATOM   1337 N N   . VAL A 1 211 ? 105.939 137.209 140.262 1.00 97.01  ? 198 VAL A N   1 
ATOM   1338 C CA  . VAL A 1 211 ? 105.954 138.015 141.486 1.00 103.81 ? 198 VAL A CA  1 
ATOM   1339 C C   . VAL A 1 211 ? 104.559 138.220 142.066 1.00 113.21 ? 198 VAL A C   1 
ATOM   1340 O O   . VAL A 1 211 ? 104.370 137.962 143.267 1.00 113.65 ? 198 VAL A O   1 
ATOM   1341 C CB  . VAL A 1 211 ? 106.686 139.344 141.236 1.00 97.79  ? 198 VAL A CB  1 
ATOM   1342 C CG1 . VAL A 1 211 ? 106.745 140.162 142.519 1.00 95.91  ? 198 VAL A CG1 1 
ATOM   1343 C CG2 . VAL A 1 211 ? 108.077 139.098 140.681 1.00 86.62  ? 198 VAL A CG2 1 
ATOM   1344 N N   . PRO A 1 212 ? 103.554 138.689 141.309 1.00 117.12 ? 199 PRO A N   1 
ATOM   1345 C CA  . PRO A 1 212 ? 102.237 138.907 141.934 1.00 120.98 ? 199 PRO A CA  1 
ATOM   1346 C C   . PRO A 1 212 ? 101.596 137.637 142.468 1.00 124.26 ? 199 PRO A C   1 
ATOM   1347 O O   . PRO A 1 212 ? 100.932 137.675 143.510 1.00 126.41 ? 199 PRO A O   1 
ATOM   1348 C CB  . PRO A 1 212 ? 101.407 139.527 140.799 1.00 120.06 ? 199 PRO A CB  1 
ATOM   1349 C CG  . PRO A 1 212 ? 102.407 140.066 139.839 1.00 114.16 ? 199 PRO A CG  1 
ATOM   1350 C CD  . PRO A 1 212 ? 103.546 139.103 139.894 1.00 109.52 ? 199 PRO A CD  1 
ATOM   1351 N N   . ASN A 1 213 ? 101.780 136.508 141.780 1.00 123.46 ? 200 ASN A N   1 
ATOM   1352 C CA  . ASN A 1 213 ? 101.110 135.278 142.191 1.00 124.07 ? 200 ASN A CA  1 
ATOM   1353 C C   . ASN A 1 213 ? 101.743 134.687 143.445 1.00 126.90 ? 200 ASN A C   1 
ATOM   1354 O O   . ASN A 1 213 ? 101.033 134.262 144.364 1.00 129.67 ? 200 ASN A O   1 
ATOM   1355 C CB  . ASN A 1 213 ? 101.135 134.262 141.049 1.00 117.27 ? 200 ASN A CB  1 
ATOM   1356 C CG  . ASN A 1 213 ? 100.433 134.768 139.803 1.00 119.80 ? 200 ASN A CG  1 
ATOM   1357 O OD1 . ASN A 1 213 ? 101.027 135.469 138.983 1.00 113.50 ? 200 ASN A OD1 1 
ATOM   1358 N ND2 . ASN A 1 213 ? 99.164  134.410 139.653 1.00 125.66 ? 200 ASN A ND2 1 
ATOM   1359 N N   . GLY A 1 214 ? 103.074 134.652 143.504 1.00 125.36 ? 201 GLY A N   1 
ATOM   1360 C CA  . GLY A 1 214 ? 103.755 134.029 144.623 1.00 125.51 ? 201 GLY A CA  1 
ATOM   1361 C C   . GLY A 1 214 ? 103.915 134.893 145.853 1.00 129.50 ? 201 GLY A C   1 
ATOM   1362 O O   . GLY A 1 214 ? 104.404 134.402 146.875 1.00 125.85 ? 201 GLY A O   1 
ATOM   1363 N N   . GLY A 1 215 ? 103.517 136.164 145.785 1.00 132.21 ? 202 GLY A N   1 
ATOM   1364 C CA  . GLY A 1 215 ? 103.661 137.066 146.906 1.00 131.16 ? 202 GLY A CA  1 
ATOM   1365 C C   . GLY A 1 215 ? 102.453 137.057 147.827 1.00 133.65 ? 202 GLY A C   1 
ATOM   1366 O O   . GLY A 1 215 ? 101.430 136.426 147.566 1.00 134.99 ? 202 GLY A O   1 
ATOM   1367 N N   . SER A 1 216 ? 102.592 137.782 148.934 1.00 133.30 ? 203 SER A N   1 
ATOM   1368 C CA  . SER A 1 216 ? 101.521 137.912 149.909 1.00 135.28 ? 203 SER A CA  1 
ATOM   1369 C C   . SER A 1 216 ? 101.678 139.238 150.638 1.00 134.75 ? 203 SER A C   1 
ATOM   1370 O O   . SER A 1 216 ? 102.768 139.813 150.694 1.00 132.25 ? 203 SER A O   1 
ATOM   1371 C CB  . SER A 1 216 ? 101.517 136.746 150.906 1.00 136.43 ? 203 SER A CB  1 
ATOM   1372 O OG  . SER A 1 216 ? 101.365 135.504 150.241 1.00 140.10 ? 203 SER A OG  1 
ATOM   1373 N N   . GLY A 1 217 ? 100.571 139.717 151.197 1.00 136.65 ? 204 GLY A N   1 
ATOM   1374 C CA  . GLY A 1 217 ? 100.597 140.982 151.909 1.00 134.10 ? 204 GLY A CA  1 
ATOM   1375 C C   . GLY A 1 217 ? 101.346 140.870 153.226 1.00 135.15 ? 204 GLY A C   1 
ATOM   1376 O O   . GLY A 1 217 ? 101.296 139.848 153.912 1.00 136.51 ? 204 GLY A O   1 
ATOM   1377 N N   . GLY A 1 218 ? 102.048 141.944 153.579 1.00 134.34 ? 205 GLY A N   1 
ATOM   1378 C CA  . GLY A 1 218 ? 102.785 141.993 154.824 1.00 133.82 ? 205 GLY A CA  1 
ATOM   1379 C C   . GLY A 1 218 ? 104.138 141.321 154.809 1.00 132.32 ? 205 GLY A C   1 
ATOM   1380 O O   . GLY A 1 218 ? 104.726 141.130 155.879 1.00 131.07 ? 205 GLY A O   1 
ATOM   1381 N N   . ASP A 1 219 ? 104.650 140.950 153.639 1.00 130.25 ? 206 ASP A N   1 
ATOM   1382 C CA  . ASP A 1 219 ? 105.953 140.309 153.521 1.00 123.58 ? 206 ASP A CA  1 
ATOM   1383 C C   . ASP A 1 219 ? 106.998 141.354 153.156 1.00 116.74 ? 206 ASP A C   1 
ATOM   1384 O O   . ASP A 1 219 ? 106.861 142.047 152.142 1.00 115.59 ? 206 ASP A O   1 
ATOM   1385 C CB  . ASP A 1 219 ? 105.922 139.194 152.476 1.00 123.06 ? 206 ASP A CB  1 
ATOM   1386 C CG  . ASP A 1 219 ? 105.048 138.032 152.894 1.00 129.49 ? 206 ASP A CG  1 
ATOM   1387 O OD1 . ASP A 1 219 ? 104.894 137.813 154.114 1.00 127.82 ? 206 ASP A OD1 1 
ATOM   1388 O OD2 . ASP A 1 219 ? 104.518 137.337 152.003 1.00 134.98 ? 206 ASP A OD2 1 
ATOM   1389 N N   . THR A 1 220 ? 108.042 141.460 153.981 1.00 113.96 ? 207 THR A N   1 
ATOM   1390 C CA  . THR A 1 220 ? 109.108 142.418 153.711 1.00 111.30 ? 207 THR A CA  1 
ATOM   1391 C C   . THR A 1 220 ? 109.825 142.090 152.406 1.00 107.50 ? 207 THR A C   1 
ATOM   1392 O O   . THR A 1 220 ? 110.159 142.991 151.628 1.00 104.40 ? 207 THR A O   1 
ATOM   1393 C CB  . THR A 1 220 ? 110.097 142.444 154.878 1.00 111.94 ? 207 THR A CB  1 
ATOM   1394 O OG1 . THR A 1 220 ? 109.398 142.760 156.088 1.00 115.30 ? 207 THR A OG1 1 
ATOM   1395 C CG2 . THR A 1 220 ? 111.177 143.487 154.641 1.00 107.17 ? 207 THR A CG2 1 
ATOM   1396 N N   . PHE A 1 221 ? 110.070 140.805 152.145 1.00 107.05 ? 208 PHE A N   1 
ATOM   1397 C CA  . PHE A 1 221 ? 110.796 140.423 150.938 1.00 108.34 ? 208 PHE A CA  1 
ATOM   1398 C C   . PHE A 1 221 ? 109.942 140.596 149.687 1.00 107.91 ? 208 PHE A C   1 
ATOM   1399 O O   . PHE A 1 221 ? 110.459 140.958 148.624 1.00 104.17 ? 208 PHE A O   1 
ATOM   1400 C CB  . PHE A 1 221 ? 111.290 138.982 151.052 1.00 103.17 ? 208 PHE A CB  1 
ATOM   1401 C CG  . PHE A 1 221 ? 112.084 138.526 149.866 1.00 103.38 ? 208 PHE A CG  1 
ATOM   1402 C CD1 . PHE A 1 221 ? 113.437 138.797 149.779 1.00 100.81 ? 208 PHE A CD1 1 
ATOM   1403 C CD2 . PHE A 1 221 ? 111.476 137.836 148.829 1.00 103.35 ? 208 PHE A CD2 1 
ATOM   1404 C CE1 . PHE A 1 221 ? 114.170 138.386 148.685 1.00 100.51 ? 208 PHE A CE1 1 
ATOM   1405 C CE2 . PHE A 1 221 ? 112.204 137.422 147.732 1.00 102.09 ? 208 PHE A CE2 1 
ATOM   1406 C CZ  . PHE A 1 221 ? 113.552 137.696 147.660 1.00 102.30 ? 208 PHE A CZ  1 
ATOM   1407 N N   . ALA A 1 222 ? 108.640 140.314 149.782 1.00 105.95 ? 209 ALA A N   1 
ATOM   1408 C CA  . ALA A 1 222 ? 107.769 140.475 148.622 1.00 101.61 ? 209 ALA A CA  1 
ATOM   1409 C C   . ALA A 1 222 ? 107.632 141.941 148.232 1.00 104.29 ? 209 ALA A C   1 
ATOM   1410 O O   . ALA A 1 222 ? 107.585 142.270 147.041 1.00 101.52 ? 209 ALA A O   1 
ATOM   1411 C CB  . ALA A 1 222 ? 106.399 139.862 148.904 1.00 108.98 ? 209 ALA A CB  1 
ATOM   1412 N N   . ASP A 1 223 ? 107.558 142.833 149.222 1.00 108.57 ? 210 ASP A N   1 
ATOM   1413 C CA  . ASP A 1 223 ? 107.437 144.257 148.927 1.00 111.07 ? 210 ASP A CA  1 
ATOM   1414 C C   . ASP A 1 223 ? 108.671 144.778 148.202 1.00 106.58 ? 210 ASP A C   1 
ATOM   1415 O O   . ASP A 1 223 ? 108.561 145.608 147.293 1.00 104.95 ? 210 ASP A O   1 
ATOM   1416 C CB  . ASP A 1 223 ? 107.193 145.039 150.218 1.00 115.71 ? 210 ASP A CB  1 
ATOM   1417 C CG  . ASP A 1 223 ? 105.863 144.693 150.865 1.00 118.12 ? 210 ASP A CG  1 
ATOM   1418 O OD1 . ASP A 1 223 ? 104.920 144.328 150.131 1.00 120.64 ? 210 ASP A OD1 1 
ATOM   1419 O OD2 . ASP A 1 223 ? 105.760 144.788 152.106 1.00 114.28 ? 210 ASP A OD2 1 
ATOM   1420 N N   . SER A 1 224 ? 109.857 144.305 148.593 1.00 104.38 ? 211 SER A N   1 
ATOM   1421 C CA  . SER A 1 224 ? 111.079 144.713 147.905 1.00 101.87 ? 211 SER A CA  1 
ATOM   1422 C C   . SER A 1 224 ? 111.075 144.251 146.454 1.00 98.10  ? 211 SER A C   1 
ATOM   1423 O O   . SER A 1 224 ? 111.483 144.996 145.553 1.00 96.29  ? 211 SER A O   1 
ATOM   1424 C CB  . SER A 1 224 ? 112.302 144.166 148.639 1.00 96.17  ? 211 SER A CB  1 
ATOM   1425 O OG  . SER A 1 224 ? 112.330 142.751 148.598 1.00 88.72  ? 211 SER A OG  1 
ATOM   1426 N N   . LEU A 1 225 ? 110.626 143.019 146.208 1.00 95.56  ? 212 LEU A N   1 
ATOM   1427 C CA  . LEU A 1 225 ? 110.553 142.525 144.838 1.00 89.28  ? 212 LEU A CA  1 
ATOM   1428 C C   . LEU A 1 225 ? 109.536 143.315 144.025 1.00 89.02  ? 212 LEU A C   1 
ATOM   1429 O O   . LEU A 1 225 ? 109.771 143.612 142.850 1.00 86.93  ? 212 LEU A O   1 
ATOM   1430 C CB  . LEU A 1 225 ? 110.218 141.035 144.835 1.00 89.20  ? 212 LEU A CB  1 
ATOM   1431 C CG  . LEU A 1 225 ? 110.379 140.297 143.505 1.00 82.73  ? 212 LEU A CG  1 
ATOM   1432 C CD1 . LEU A 1 225 ? 111.543 140.854 142.695 1.00 75.60  ? 212 LEU A CD1 1 
ATOM   1433 C CD2 . LEU A 1 225 ? 110.583 138.817 143.770 1.00 79.07  ? 212 LEU A CD2 1 
ATOM   1434 N N   . ARG A 1 226 ? 108.404 143.671 144.636 1.00 94.16  ? 213 ARG A N   1 
ATOM   1435 C CA  . ARG A 1 226 ? 107.423 144.504 143.946 1.00 97.91  ? 213 ARG A CA  1 
ATOM   1436 C C   . ARG A 1 226 ? 107.993 145.881 143.630 1.00 95.22  ? 213 ARG A C   1 
ATOM   1437 O O   . ARG A 1 226 ? 107.709 146.450 142.572 1.00 93.80  ? 213 ARG A O   1 
ATOM   1438 C CB  . ARG A 1 226 ? 106.154 144.626 144.789 1.00 100.27 ? 213 ARG A CB  1 
ATOM   1439 C CG  . ARG A 1 226 ? 105.405 143.318 144.968 1.00 102.82 ? 213 ARG A CG  1 
ATOM   1440 C CD  . ARG A 1 226 ? 104.495 143.366 146.183 1.00 109.16 ? 213 ARG A CD  1 
ATOM   1441 N NE  . ARG A 1 226 ? 103.811 142.097 146.402 1.00 117.85 ? 213 ARG A NE  1 
ATOM   1442 C CZ  . ARG A 1 226 ? 103.032 141.836 147.442 1.00 118.15 ? 213 ARG A CZ  1 
ATOM   1443 N NH1 . ARG A 1 226 ? 102.819 142.734 148.390 1.00 111.52 ? 213 ARG A NH1 1 
ATOM   1444 N NH2 . ARG A 1 226 ? 102.451 140.643 147.534 1.00 125.02 ? 213 ARG A NH2 1 
ATOM   1445 N N   . TYR A 1 227 ? 108.791 146.440 144.542 1.00 94.79  ? 214 TYR A N   1 
ATOM   1446 C CA  . TYR A 1 227 ? 109.400 147.744 144.295 1.00 95.55  ? 214 TYR A CA  1 
ATOM   1447 C C   . TYR A 1 227 ? 110.422 147.677 143.163 1.00 93.30  ? 214 TYR A C   1 
ATOM   1448 O O   . TYR A 1 227 ? 110.484 148.578 142.317 1.00 94.21  ? 214 TYR A O   1 
ATOM   1449 C CB  . TYR A 1 227 ? 110.041 148.265 145.580 1.00 99.18  ? 214 TYR A CB  1 
ATOM   1450 C CG  . TYR A 1 227 ? 110.589 149.667 145.473 1.00 100.32 ? 214 TYR A CG  1 
ATOM   1451 C CD1 . TYR A 1 227 ? 109.740 150.766 145.463 1.00 100.82 ? 214 TYR A CD1 1 
ATOM   1452 C CD2 . TYR A 1 227 ? 111.954 149.893 145.391 1.00 97.15  ? 214 TYR A CD2 1 
ATOM   1453 C CE1 . TYR A 1 227 ? 110.237 152.052 145.367 1.00 98.16  ? 214 TYR A CE1 1 
ATOM   1454 C CE2 . TYR A 1 227 ? 112.460 151.175 145.298 1.00 96.37  ? 214 TYR A CE2 1 
ATOM   1455 C CZ  . TYR A 1 227 ? 111.599 152.250 145.284 1.00 98.45  ? 214 TYR A CZ  1 
ATOM   1456 O OH  . TYR A 1 227 ? 112.102 153.527 145.189 1.00 100.51 ? 214 TYR A OH  1 
ATOM   1457 N N   . VAL A 1 228 ? 111.229 146.614 143.129 1.00 90.79  ? 215 VAL A N   1 
ATOM   1458 C CA  . VAL A 1 228 ? 112.164 146.426 142.021 1.00 89.42  ? 215 VAL A CA  1 
ATOM   1459 C C   . VAL A 1 228 ? 111.402 146.247 140.712 1.00 86.60  ? 215 VAL A C   1 
ATOM   1460 O O   . VAL A 1 228 ? 111.806 146.762 139.658 1.00 83.49  ? 215 VAL A O   1 
ATOM   1461 C CB  . VAL A 1 228 ? 113.100 145.237 142.307 1.00 85.54  ? 215 VAL A CB  1 
ATOM   1462 C CG1 . VAL A 1 228 ? 113.974 144.941 141.104 1.00 77.36  ? 215 VAL A CG1 1 
ATOM   1463 C CG2 . VAL A 1 228 ? 113.962 145.522 143.525 1.00 80.79  ? 215 VAL A CG2 1 
ATOM   1464 N N   . ASN A 1 229 ? 110.290 145.505 140.758 1.00 86.23  ? 216 ASN A N   1 
ATOM   1465 C CA  . ASN A 1 229 ? 109.422 145.375 139.593 1.00 86.52  ? 216 ASN A CA  1 
ATOM   1466 C C   . ASN A 1 229 ? 108.922 146.731 139.126 1.00 92.46  ? 216 ASN A C   1 
ATOM   1467 O O   . ASN A 1 229 ? 108.904 147.013 137.924 1.00 94.92  ? 216 ASN A O   1 
ATOM   1468 C CB  . ASN A 1 229 ? 108.235 144.469 139.923 1.00 86.01  ? 216 ASN A CB  1 
ATOM   1469 C CG  . ASN A 1 229 ? 108.475 143.032 139.536 1.00 87.00  ? 216 ASN A CG  1 
ATOM   1470 O OD1 . ASN A 1 229 ? 109.604 142.635 139.269 1.00 83.94  ? 216 ASN A OD1 1 
ATOM   1471 N ND2 . ASN A 1 229 ? 107.410 142.241 139.500 1.00 90.80  ? 216 ASN A ND2 1 
ATOM   1472 N N   . LYS A 1 230 ? 108.498 147.577 140.065 1.00 94.01  ? 217 LYS A N   1 
ATOM   1473 C CA  . LYS A 1 230 ? 108.034 148.912 139.712 1.00 91.58  ? 217 LYS A CA  1 
ATOM   1474 C C   . LYS A 1 230 ? 109.142 149.711 139.044 1.00 89.41  ? 217 LYS A C   1 
ATOM   1475 O O   . LYS A 1 230 ? 108.913 150.379 138.029 1.00 93.10  ? 217 LYS A O   1 
ATOM   1476 C CB  . LYS A 1 230 ? 107.525 149.633 140.961 1.00 89.20  ? 217 LYS A CB  1 
ATOM   1477 C CG  . LYS A 1 230 ? 106.779 150.925 140.682 1.00 90.14  ? 217 LYS A CG  1 
ATOM   1478 C CD  . LYS A 1 230 ? 105.522 150.668 139.869 1.00 93.16  ? 217 LYS A CD  1 
ATOM   1479 C CE  . LYS A 1 230 ? 104.568 149.740 140.603 1.00 95.22  ? 217 LYS A CE  1 
ATOM   1480 N NZ  . LYS A 1 230 ? 103.386 149.393 139.767 1.00 91.93  ? 217 LYS A NZ  1 
ATOM   1481 N N   . ILE A 1 231 ? 110.359 149.631 139.587 1.00 86.79  ? 218 ILE A N   1 
ATOM   1482 C CA  . ILE A 1 231 ? 111.483 150.364 139.008 1.00 83.68  ? 218 ILE A CA  1 
ATOM   1483 C C   . ILE A 1 231 ? 111.726 149.920 137.572 1.00 86.94  ? 218 ILE A C   1 
ATOM   1484 O O   . ILE A 1 231 ? 111.823 150.745 136.654 1.00 89.26  ? 218 ILE A O   1 
ATOM   1485 C CB  . ILE A 1 231 ? 112.748 150.180 139.864 1.00 77.82  ? 218 ILE A CB  1 
ATOM   1486 C CG1 . ILE A 1 231 ? 112.544 150.751 141.263 1.00 86.62  ? 218 ILE A CG1 1 
ATOM   1487 C CG2 . ILE A 1 231 ? 113.941 150.838 139.190 1.00 64.28  ? 218 ILE A CG2 1 
ATOM   1488 C CD1 . ILE A 1 231 ? 113.698 150.468 142.186 1.00 86.12  ? 218 ILE A CD1 1 
ATOM   1489 N N   . LEU A 1 232 ? 111.820 148.607 137.352 1.00 88.09  ? 219 LEU A N   1 
ATOM   1490 C CA  . LEU A 1 232 ? 112.157 148.133 136.013 1.00 84.23  ? 219 LEU A CA  1 
ATOM   1491 C C   . LEU A 1 232 ? 111.013 148.341 135.030 1.00 83.72  ? 219 LEU A C   1 
ATOM   1492 O O   . LEU A 1 232 ? 111.260 148.588 133.846 1.00 82.95  ? 219 LEU A O   1 
ATOM   1493 C CB  . LEU A 1 232 ? 112.574 146.663 136.048 1.00 82.11  ? 219 LEU A CB  1 
ATOM   1494 C CG  . LEU A 1 232 ? 114.052 146.444 136.382 1.00 76.98  ? 219 LEU A CG  1 
ATOM   1495 C CD1 . LEU A 1 232 ? 114.362 146.881 137.799 1.00 75.61  ? 219 LEU A CD1 1 
ATOM   1496 C CD2 . LEU A 1 232 ? 114.475 145.000 136.157 1.00 68.31  ? 219 LEU A CD2 1 
ATOM   1497 N N   . ASN A 1 233 ? 109.762 148.251 135.486 1.00 84.85  ? 220 ASN A N   1 
ATOM   1498 C CA  . ASN A 1 233 ? 108.642 148.492 134.584 1.00 86.47  ? 220 ASN A CA  1 
ATOM   1499 C C   . ASN A 1 233 ? 108.503 149.970 134.248 1.00 90.28  ? 220 ASN A C   1 
ATOM   1500 O O   . ASN A 1 233 ? 108.022 150.313 133.162 1.00 91.90  ? 220 ASN A O   1 
ATOM   1501 C CB  . ASN A 1 233 ? 107.350 147.954 135.196 1.00 87.43  ? 220 ASN A CB  1 
ATOM   1502 C CG  . ASN A 1 233 ? 107.381 146.451 135.390 1.00 90.88  ? 220 ASN A CG  1 
ATOM   1503 O OD1 . ASN A 1 233 ? 108.179 145.750 134.769 1.00 88.09  ? 220 ASN A OD1 1 
ATOM   1504 N ND2 . ASN A 1 233 ? 106.508 145.947 136.256 1.00 95.75  ? 220 ASN A ND2 1 
ATOM   1505 N N   . SER A 1 234 ? 108.913 150.858 135.157 1.00 91.89  ? 221 SER A N   1 
ATOM   1506 C CA  . SER A 1 234 ? 108.910 152.282 134.854 1.00 91.67  ? 221 SER A CA  1 
ATOM   1507 C C   . SER A 1 234 ? 110.127 152.707 134.044 1.00 87.91  ? 221 SER A C   1 
ATOM   1508 O O   . SER A 1 234 ? 110.096 153.774 133.421 1.00 83.44  ? 221 SER A O   1 
ATOM   1509 C CB  . SER A 1 234 ? 108.838 153.095 136.148 1.00 88.44  ? 221 SER A CB  1 
ATOM   1510 O OG  . SER A 1 234 ? 107.667 152.780 136.883 1.00 93.24  ? 221 SER A OG  1 
ATOM   1511 N N   . LYS A 1 235 ? 111.192 151.904 134.038 1.00 87.87  ? 222 LYS A N   1 
ATOM   1512 C CA  . LYS A 1 235 ? 112.393 152.227 133.275 1.00 80.70  ? 222 LYS A CA  1 
ATOM   1513 C C   . LYS A 1 235 ? 112.401 151.608 131.881 1.00 83.24  ? 222 LYS A C   1 
ATOM   1514 O O   . LYS A 1 235 ? 112.486 152.332 130.885 1.00 81.05  ? 222 LYS A O   1 
ATOM   1515 C CB  . LYS A 1 235 ? 113.638 151.776 134.047 1.00 78.90  ? 222 LYS A CB  1 
ATOM   1516 C CG  . LYS A 1 235 ? 114.941 151.956 133.284 1.00 73.85  ? 222 LYS A CG  1 
ATOM   1517 C CD  . LYS A 1 235 ? 115.150 153.406 132.887 1.00 72.24  ? 222 LYS A CD  1 
ATOM   1518 C CE  . LYS A 1 235 ? 116.418 153.584 132.071 1.00 72.79  ? 222 LYS A CE  1 
ATOM   1519 N NZ  . LYS A 1 235 ? 117.640 153.278 132.863 1.00 69.46  ? 222 LYS A NZ  1 
ATOM   1520 N N   . PHE A 1 236 ? 112.317 150.282 131.788 1.00 85.39  ? 223 PHE A N   1 
ATOM   1521 C CA  . PHE A 1 236 ? 112.379 149.571 130.517 1.00 81.98  ? 223 PHE A CA  1 
ATOM   1522 C C   . PHE A 1 236 ? 111.008 149.276 129.919 1.00 83.24  ? 223 PHE A C   1 
ATOM   1523 O O   . PHE A 1 236 ? 110.938 148.693 128.833 1.00 81.82  ? 223 PHE A O   1 
ATOM   1524 C CB  . PHE A 1 236 ? 113.150 148.256 130.683 1.00 77.43  ? 223 PHE A CB  1 
ATOM   1525 C CG  . PHE A 1 236 ? 114.642 148.428 130.786 1.00 77.45  ? 223 PHE A CG  1 
ATOM   1526 C CD1 . PHE A 1 236 ? 115.251 149.604 130.384 1.00 77.52  ? 223 PHE A CD1 1 
ATOM   1527 C CD2 . PHE A 1 236 ? 115.434 147.405 131.279 1.00 69.09  ? 223 PHE A CD2 1 
ATOM   1528 C CE1 . PHE A 1 236 ? 116.623 149.757 130.477 1.00 73.34  ? 223 PHE A CE1 1 
ATOM   1529 C CE2 . PHE A 1 236 ? 116.804 147.553 131.373 1.00 59.68  ? 223 PHE A CE2 1 
ATOM   1530 C CZ  . PHE A 1 236 ? 117.399 148.729 130.972 1.00 64.48  ? 223 PHE A CZ  1 
ATOM   1531 N N   . GLY A 1 237 ? 109.926 149.656 130.589 1.00 87.13  ? 224 GLY A N   1 
ATOM   1532 C CA  . GLY A 1 237 ? 108.592 149.400 130.091 1.00 88.41  ? 224 GLY A CA  1 
ATOM   1533 C C   . GLY A 1 237 ? 107.919 148.240 130.810 1.00 92.10  ? 224 GLY A C   1 
ATOM   1534 O O   . GLY A 1 237 ? 108.561 147.384 131.424 1.00 89.87  ? 224 GLY A O   1 
ATOM   1535 N N   . PHE A 1 238 ? 106.590 148.221 130.731 1.00 98.56  ? 225 PHE A N   1 
ATOM   1536 C CA  . PHE A 1 238 ? 105.813 147.205 131.427 1.00 99.10  ? 225 PHE A CA  1 
ATOM   1537 C C   . PHE A 1 238 ? 106.039 145.829 130.811 1.00 103.01 ? 225 PHE A C   1 
ATOM   1538 O O   . PHE A 1 238 ? 106.064 145.671 129.588 1.00 104.58 ? 225 PHE A O   1 
ATOM   1539 C CB  . PHE A 1 238 ? 104.323 147.561 131.403 1.00 101.15 ? 225 PHE A CB  1 
ATOM   1540 C CG  . PHE A 1 238 ? 103.776 147.824 130.025 1.00 108.74 ? 225 PHE A CG  1 
ATOM   1541 C CD1 . PHE A 1 238 ? 103.814 149.099 129.483 1.00 109.28 ? 225 PHE A CD1 1 
ATOM   1542 C CD2 . PHE A 1 238 ? 103.208 146.803 129.281 1.00 112.01 ? 225 PHE A CD2 1 
ATOM   1543 C CE1 . PHE A 1 238 ? 103.307 149.347 128.221 1.00 112.44 ? 225 PHE A CE1 1 
ATOM   1544 C CE2 . PHE A 1 238 ? 102.700 147.045 128.017 1.00 113.58 ? 225 PHE A CE2 1 
ATOM   1545 C CZ  . PHE A 1 238 ? 102.749 148.319 127.487 1.00 113.53 ? 225 PHE A CZ  1 
ATOM   1546 N N   . THR A 1 239 ? 106.208 144.829 131.672 1.00 101.96 ? 226 THR A N   1 
ATOM   1547 C CA  . THR A 1 239 ? 106.431 143.456 131.240 1.00 99.29  ? 226 THR A CA  1 
ATOM   1548 C C   . THR A 1 239 ? 106.038 142.524 132.378 1.00 95.81  ? 226 THR A C   1 
ATOM   1549 O O   . THR A 1 239 ? 106.052 142.914 133.548 1.00 91.71  ? 226 THR A O   1 
ATOM   1550 C CB  . THR A 1 239 ? 107.895 143.213 130.833 1.00 95.68  ? 226 THR A CB  1 
ATOM   1551 O OG1 . THR A 1 239 ? 108.367 144.301 130.030 1.00 101.43 ? 226 THR A OG1 1 
ATOM   1552 C CG2 . THR A 1 239 ? 108.031 141.923 130.034 1.00 92.87  ? 226 THR A CG2 1 
ATOM   1553 N N   . SER A 1 240 ? 105.660 141.300 132.018 1.00 99.23  ? 227 SER A N   1 
ATOM   1554 C CA  . SER A 1 240 ? 105.425 140.265 133.015 1.00 95.28  ? 227 SER A CA  1 
ATOM   1555 C C   . SER A 1 240 ? 106.758 139.730 133.526 1.00 87.89  ? 227 SER A C   1 
ATOM   1556 O O   . SER A 1 240 ? 107.625 139.342 132.737 1.00 89.07  ? 227 SER A O   1 
ATOM   1557 C CB  . SER A 1 240 ? 104.586 139.135 132.419 1.00 95.86  ? 227 SER A CB  1 
ATOM   1558 O OG  . SER A 1 240 ? 103.341 139.620 131.948 1.00 96.81  ? 227 SER A OG  1 
ATOM   1559 N N   . ARG A 1 241 ? 106.926 139.716 134.846 1.00 79.25  ? 228 ARG A N   1 
ATOM   1560 C CA  . ARG A 1 241 ? 108.183 139.332 135.473 1.00 72.89  ? 228 ARG A CA  1 
ATOM   1561 C C   . ARG A 1 241 ? 108.020 138.027 136.240 1.00 72.70  ? 228 ARG A C   1 
ATOM   1562 O O   . ARG A 1 241 ? 106.974 137.779 136.849 1.00 81.41  ? 228 ARG A O   1 
ATOM   1563 C CB  . ARG A 1 241 ? 108.686 140.423 136.423 1.00 77.88  ? 228 ARG A CB  1 
ATOM   1564 C CG  . ARG A 1 241 ? 108.166 141.817 136.118 1.00 83.32  ? 228 ARG A CG  1 
ATOM   1565 C CD  . ARG A 1 241 ? 108.761 142.390 134.844 1.00 84.81  ? 228 ARG A CD  1 
ATOM   1566 N NE  . ARG A 1 241 ? 110.157 142.780 134.994 1.00 83.19  ? 228 ARG A NE  1 
ATOM   1567 C CZ  . ARG A 1 241 ? 110.809 143.547 134.132 1.00 80.12  ? 228 ARG A CZ  1 
ATOM   1568 N NH1 . ARG A 1 241 ? 110.212 144.047 133.063 1.00 80.60  ? 228 ARG A NH1 1 
ATOM   1569 N NH2 . ARG A 1 241 ? 112.092 143.816 134.345 1.00 74.76  ? 228 ARG A NH2 1 
ATOM   1570 N N   . LYS A 1 242 ? 109.064 137.203 136.220 1.00 66.72  ? 229 LYS A N   1 
ATOM   1571 C CA  . LYS A 1 242 ? 109.093 135.941 136.944 1.00 63.08  ? 229 LYS A CA  1 
ATOM   1572 C C   . LYS A 1 242 ? 110.293 135.914 137.879 1.00 57.54  ? 229 LYS A C   1 
ATOM   1573 O O   . LYS A 1 242 ? 111.390 136.343 137.508 1.00 54.23  ? 229 LYS A O   1 
ATOM   1574 C CB  . LYS A 1 242 ? 109.146 134.753 135.977 1.00 59.84  ? 229 LYS A CB  1 
ATOM   1575 C CG  . LYS A 1 242 ? 107.884 134.583 135.146 1.00 63.16  ? 229 LYS A CG  1 
ATOM   1576 C CD  . LYS A 1 242 ? 108.058 133.526 134.066 1.00 50.07  ? 229 LYS A CD  1 
ATOM   1577 C CE  . LYS A 1 242 ? 108.454 132.185 134.659 1.00 54.49  ? 229 LYS A CE  1 
ATOM   1578 N NZ  . LYS A 1 242 ? 107.458 131.697 135.649 1.00 60.10  ? 229 LYS A NZ  1 
ATOM   1579 N N   . VAL A 1 243 ? 110.078 135.414 139.088 1.00 60.72  ? 230 VAL A N   1 
ATOM   1580 C CA  . VAL A 1 243 ? 111.136 135.385 140.106 1.00 56.28  ? 230 VAL A CA  1 
ATOM   1581 C C   . VAL A 1 243 ? 112.204 134.376 139.697 1.00 54.17  ? 230 VAL A C   1 
ATOM   1582 O O   . VAL A 1 243 ? 111.864 133.260 139.267 1.00 59.28  ? 230 VAL A O   1 
ATOM   1583 C CB  . VAL A 1 243 ? 110.548 135.031 141.473 1.00 66.01  ? 230 VAL A CB  1 
ATOM   1584 C CG1 . VAL A 1 243 ? 111.637 134.994 142.532 1.00 63.61  ? 230 VAL A CG1 1 
ATOM   1585 C CG2 . VAL A 1 243 ? 109.463 136.016 141.852 1.00 76.30  ? 230 VAL A CG2 1 
ATOM   1586 N N   . PRO A 1 244 ? 113.488 134.713 139.793 1.00 46.11  ? 231 PRO A N   1 
ATOM   1587 C CA  . PRO A 1 244 ? 114.529 133.709 139.566 1.00 45.33  ? 231 PRO A CA  1 
ATOM   1588 C C   . PRO A 1 244 ? 114.524 132.655 140.661 1.00 49.18  ? 231 PRO A C   1 
ATOM   1589 O O   . PRO A 1 244 ? 114.152 132.916 141.808 1.00 51.19  ? 231 PRO A O   1 
ATOM   1590 C CB  . PRO A 1 244 ? 115.827 134.526 139.590 1.00 41.06  ? 231 PRO A CB  1 
ATOM   1591 C CG  . PRO A 1 244 ? 115.401 135.942 139.391 1.00 43.17  ? 231 PRO A CG  1 
ATOM   1592 C CD  . PRO A 1 244 ? 114.057 136.047 140.030 1.00 48.60  ? 231 PRO A CD  1 
ATOM   1593 N N   . ALA A 1 245 ? 114.946 131.449 140.293 1.00 48.63  ? 232 ALA A N   1 
ATOM   1594 C CA  . ALA A 1 245 ? 115.004 130.354 141.250 1.00 44.36  ? 232 ALA A CA  1 
ATOM   1595 C C   . ALA A 1 245 ? 116.077 130.612 142.299 1.00 39.82  ? 232 ALA A C   1 
ATOM   1596 O O   . ALA A 1 245 ? 117.075 131.288 142.046 1.00 42.77  ? 232 ALA A O   1 
ATOM   1597 C CB  . ALA A 1 245 ? 115.283 129.034 140.534 1.00 43.14  ? 232 ALA A CB  1 
ATOM   1598 N N   . HIS A 1 246 ? 115.861 130.068 143.493 1.00 38.26  ? 233 HIS A N   1 
ATOM   1599 C CA  . HIS A 1 246 ? 116.843 130.153 144.572 1.00 35.92  ? 233 HIS A CA  1 
ATOM   1600 C C   . HIS A 1 246 ? 117.880 129.063 144.332 1.00 35.17  ? 233 HIS A C   1 
ATOM   1601 O O   . HIS A 1 246 ? 117.633 127.885 144.595 1.00 39.58  ? 233 HIS A O   1 
ATOM   1602 C CB  . HIS A 1 246 ? 116.165 129.996 145.927 1.00 40.63  ? 233 HIS A CB  1 
ATOM   1603 C CG  . HIS A 1 246 ? 116.833 130.751 147.032 1.00 43.66  ? 233 HIS A CG  1 
ATOM   1604 N ND1 . HIS A 1 246 ? 116.325 130.796 148.312 1.00 47.36  ? 233 HIS A ND1 1 
ATOM   1605 C CD2 . HIS A 1 246 ? 117.963 131.495 147.050 1.00 46.83  ? 233 HIS A CD2 1 
ATOM   1606 C CE1 . HIS A 1 246 ? 117.115 131.534 149.072 1.00 47.44  ? 233 HIS A CE1 1 
ATOM   1607 N NE2 . HIS A 1 246 ? 118.116 131.971 148.329 1.00 46.30  ? 233 HIS A NE2 1 
ATOM   1608 N N   . MET A 1 247 ? 119.048 129.452 143.837 1.00 32.76  ? 234 MET A N   1 
ATOM   1609 C CA  . MET A 1 247 ? 120.017 128.494 143.324 1.00 29.23  ? 234 MET A CA  1 
ATOM   1610 C C   . MET A 1 247 ? 121.395 129.136 143.369 1.00 31.30  ? 234 MET A C   1 
ATOM   1611 O O   . MET A 1 247 ? 121.521 130.335 143.650 1.00 39.23  ? 234 MET A O   1 
ATOM   1612 C CB  . MET A 1 247 ? 119.661 128.067 141.892 1.00 30.84  ? 234 MET A CB  1 
ATOM   1613 C CG  . MET A 1 247 ? 119.701 129.214 140.908 1.00 33.80  ? 234 MET A CG  1 
ATOM   1614 S SD  . MET A 1 247 ? 119.888 128.633 139.223 1.00 60.56  ? 234 MET A SD  1 
ATOM   1615 C CE  . MET A 1 247 ? 118.610 127.392 139.199 1.00 42.12  ? 234 MET A CE  1 
ATOM   1616 N N   . PRO A 1 248 ? 122.456 128.362 143.104 1.00 27.58  ? 235 PRO A N   1 
ATOM   1617 C CA  . PRO A 1 248 ? 123.789 128.964 142.967 1.00 28.88  ? 235 PRO A CA  1 
ATOM   1618 C C   . PRO A 1 248 ? 123.955 129.728 141.665 1.00 30.20  ? 235 PRO A C   1 
ATOM   1619 O O   . PRO A 1 248 ? 124.444 129.177 140.675 1.00 29.63  ? 235 PRO A O   1 
ATOM   1620 C CB  . PRO A 1 248 ? 124.727 127.753 143.024 1.00 28.10  ? 235 PRO A CB  1 
ATOM   1621 C CG  . PRO A 1 248 ? 123.886 126.606 142.620 1.00 29.14  ? 235 PRO A CG  1 
ATOM   1622 C CD  . PRO A 1 248 ? 122.535 126.894 143.184 1.00 29.68  ? 235 PRO A CD  1 
ATOM   1623 N N   . HIS A 1 249 ? 123.551 130.996 141.659 1.00 33.05  ? 236 HIS A N   1 
ATOM   1624 C CA  . HIS A 1 249 ? 123.556 131.796 140.443 1.00 30.87  ? 236 HIS A CA  1 
ATOM   1625 C C   . HIS A 1 249 ? 124.969 132.016 139.918 1.00 30.75  ? 236 HIS A C   1 
ATOM   1626 O O   . HIS A 1 249 ? 125.945 132.015 140.670 1.00 28.54  ? 236 HIS A O   1 
ATOM   1627 C CB  . HIS A 1 249 ? 122.905 133.150 140.696 1.00 27.37  ? 236 HIS A CB  1 
ATOM   1628 C CG  . HIS A 1 249 ? 121.476 133.062 141.118 1.00 28.31  ? 236 HIS A CG  1 
ATOM   1629 N ND1 . HIS A 1 249 ? 120.476 132.650 140.266 1.00 25.92  ? 236 HIS A ND1 1 
ATOM   1630 C CD2 . HIS A 1 249 ? 120.875 133.337 142.299 1.00 30.66  ? 236 HIS A CD2 1 
ATOM   1631 C CE1 . HIS A 1 249 ? 119.320 132.679 140.902 1.00 31.35  ? 236 HIS A CE1 1 
ATOM   1632 N NE2 . HIS A 1 249 ? 119.535 133.089 142.138 1.00 33.92  ? 236 HIS A NE2 1 
ATOM   1633 N N   . MET A 1 250 ? 125.065 132.212 138.606 1.00 30.31  ? 237 MET A N   1 
ATOM   1634 C CA  . MET A 1 250 ? 126.299 132.620 137.950 1.00 30.58  ? 237 MET A CA  1 
ATOM   1635 C C   . MET A 1 250 ? 126.178 134.080 137.544 1.00 30.17  ? 237 MET A C   1 
ATOM   1636 O O   . MET A 1 250 ? 125.179 134.481 136.938 1.00 34.82  ? 237 MET A O   1 
ATOM   1637 C CB  . MET A 1 250 ? 126.599 131.753 136.726 1.00 30.02  ? 237 MET A CB  1 
ATOM   1638 C CG  . MET A 1 250 ? 127.677 132.333 135.824 1.00 30.22  ? 237 MET A CG  1 
ATOM   1639 S SD  . MET A 1 250 ? 128.327 131.159 134.625 1.00 34.56  ? 237 MET A SD  1 
ATOM   1640 C CE  . MET A 1 250 ? 129.165 130.010 135.709 1.00 22.80  ? 237 MET A CE  1 
ATOM   1641 N N   . ILE A 1 251 ? 127.195 134.869 137.877 1.00 27.89  ? 238 ILE A N   1 
ATOM   1642 C CA  . ILE A 1 251 ? 127.179 136.308 137.666 1.00 30.68  ? 238 ILE A CA  1 
ATOM   1643 C C   . ILE A 1 251 ? 128.409 136.691 136.858 1.00 31.01  ? 238 ILE A C   1 
ATOM   1644 O O   . ILE A 1 251 ? 129.442 136.017 136.909 1.00 34.30  ? 238 ILE A O   1 
ATOM   1645 C CB  . ILE A 1 251 ? 127.139 137.069 139.011 1.00 33.20  ? 238 ILE A CB  1 
ATOM   1646 C CG1 . ILE A 1 251 ? 126.058 136.486 139.921 1.00 32.25  ? 238 ILE A CG1 1 
ATOM   1647 C CG2 . ILE A 1 251 ? 126.880 138.547 138.799 1.00 38.44  ? 238 ILE A CG2 1 
ATOM   1648 C CD1 . ILE A 1 251 ? 124.650 136.720 139.430 1.00 31.60  ? 238 ILE A CD1 1 
ATOM   1649 N N   . ASP A 1 252 ? 128.290 137.775 136.098 1.00 28.62  ? 239 ASP A N   1 
ATOM   1650 C CA  . ASP A 1 252 ? 129.388 138.332 135.324 1.00 30.86  ? 239 ASP A CA  1 
ATOM   1651 C C   . ASP A 1 252 ? 129.729 139.707 135.877 1.00 39.42  ? 239 ASP A C   1 
ATOM   1652 O O   . ASP A 1 252 ? 128.836 140.483 136.230 1.00 42.71  ? 239 ASP A O   1 
ATOM   1653 C CB  . ASP A 1 252 ? 129.023 138.430 133.837 1.00 33.98  ? 239 ASP A CB  1 
ATOM   1654 C CG  . ASP A 1 252 ? 130.166 138.939 132.979 1.00 37.79  ? 239 ASP A CG  1 
ATOM   1655 O OD1 . ASP A 1 252 ? 131.305 139.033 133.481 1.00 38.38  ? 239 ASP A OD1 1 
ATOM   1656 O OD2 . ASP A 1 252 ? 129.922 139.245 131.794 1.00 35.54  ? 239 ASP A OD2 1 
ATOM   1657 N N   . ARG A 1 253 ? 131.027 140.001 135.968 1.00 41.28  ? 240 ARG A N   1 
ATOM   1658 C CA  . ARG A 1 253 ? 131.443 141.292 136.502 1.00 39.44  ? 240 ARG A CA  1 
ATOM   1659 C C   . ARG A 1 253 ? 131.103 142.432 135.553 1.00 39.75  ? 240 ARG A C   1 
ATOM   1660 O O   . ARG A 1 253 ? 130.740 143.520 136.006 1.00 44.16  ? 240 ARG A O   1 
ATOM   1661 C CB  . ARG A 1 253 ? 132.942 141.292 136.795 1.00 38.31  ? 240 ARG A CB  1 
ATOM   1662 C CG  . ARG A 1 253 ? 133.393 140.212 137.754 1.00 37.00  ? 240 ARG A CG  1 
ATOM   1663 C CD  . ARG A 1 253 ? 134.846 140.409 138.136 1.00 39.69  ? 240 ARG A CD  1 
ATOM   1664 N NE  . ARG A 1 253 ? 135.011 141.435 139.158 1.00 48.83  ? 240 ARG A NE  1 
ATOM   1665 C CZ  . ARG A 1 253 ? 136.185 141.881 139.583 1.00 55.75  ? 240 ARG A CZ  1 
ATOM   1666 N NH1 . ARG A 1 253 ? 137.320 141.435 139.071 1.00 57.39  ? 240 ARG A NH1 1 
ATOM   1667 N NH2 . ARG A 1 253 ? 136.220 142.798 140.546 1.00 56.73  ? 240 ARG A NH2 1 
ATOM   1668 N N   . ILE A 1 254 ? 131.216 142.207 134.242 1.00 38.18  ? 241 ILE A N   1 
ATOM   1669 C CA  . ILE A 1 254 ? 131.000 143.284 133.280 1.00 37.97  ? 241 ILE A CA  1 
ATOM   1670 C C   . ILE A 1 254 ? 129.541 143.722 133.282 1.00 40.67  ? 241 ILE A C   1 
ATOM   1671 O O   . ILE A 1 254 ? 129.238 144.919 133.334 1.00 46.42  ? 241 ILE A O   1 
ATOM   1672 C CB  . ILE A 1 254 ? 131.450 142.848 131.875 1.00 46.09  ? 241 ILE A CB  1 
ATOM   1673 C CG1 . ILE A 1 254 ? 132.947 142.539 131.861 1.00 50.29  ? 241 ILE A CG1 1 
ATOM   1674 C CG2 . ILE A 1 254 ? 131.115 143.924 130.856 1.00 49.08  ? 241 ILE A CG2 1 
ATOM   1675 C CD1 . ILE A 1 254 ? 133.495 142.270 130.476 1.00 53.00  ? 241 ILE A CD1 1 
ATOM   1676 N N   . VAL A 1 255 ? 128.618 142.762 133.217 1.00 38.95  ? 242 VAL A N   1 
ATOM   1677 C CA  . VAL A 1 255 ? 127.199 143.102 133.186 1.00 37.08  ? 242 VAL A CA  1 
ATOM   1678 C C   . VAL A 1 255 ? 126.784 143.774 134.486 1.00 43.33  ? 242 VAL A C   1 
ATOM   1679 O O   . VAL A 1 255 ? 126.046 144.767 134.483 1.00 53.59  ? 242 VAL A O   1 
ATOM   1680 C CB  . VAL A 1 255 ? 126.354 141.849 132.909 1.00 34.56  ? 242 VAL A CB  1 
ATOM   1681 C CG1 . VAL A 1 255 ? 124.896 142.230 132.737 1.00 35.34  ? 242 VAL A CG1 1 
ATOM   1682 C CG2 . VAL A 1 255 ? 126.875 141.118 131.686 1.00 36.54  ? 242 VAL A CG2 1 
ATOM   1683 N N   . MET A 1 256 ? 127.251 143.246 135.618 1.00 41.69  ? 243 MET A N   1 
ATOM   1684 C CA  . MET A 1 256 ? 126.905 143.841 136.901 1.00 42.50  ? 243 MET A CA  1 
ATOM   1685 C C   . MET A 1 256 ? 127.480 145.244 137.038 1.00 49.78  ? 243 MET A C   1 
ATOM   1686 O O   . MET A 1 256 ? 126.811 146.132 137.571 1.00 50.81  ? 243 MET A O   1 
ATOM   1687 C CB  . MET A 1 256 ? 127.392 142.947 138.040 1.00 44.59  ? 243 MET A CB  1 
ATOM   1688 C CG  . MET A 1 256 ? 126.632 143.135 139.338 1.00 52.08  ? 243 MET A CG  1 
ATOM   1689 S SD  . MET A 1 256 ? 124.871 142.801 139.153 1.00 71.69  ? 243 MET A SD  1 
ATOM   1690 C CE  . MET A 1 256 ? 124.326 142.900 140.855 1.00 52.05  ? 243 MET A CE  1 
ATOM   1691 N N   . GLN A 1 257 ? 128.701 145.467 136.547 1.00 52.31  ? 244 GLN A N   1 
ATOM   1692 C CA  . GLN A 1 257 ? 129.301 146.797 136.598 1.00 53.57  ? 244 GLN A CA  1 
ATOM   1693 C C   . GLN A 1 257 ? 128.561 147.771 135.690 1.00 54.72  ? 244 GLN A C   1 
ATOM   1694 O O   . GLN A 1 257 ? 128.417 148.954 136.022 1.00 59.62  ? 244 GLN A O   1 
ATOM   1695 C CB  . GLN A 1 257 ? 130.779 146.716 136.214 1.00 53.76  ? 244 GLN A CB  1 
ATOM   1696 C CG  . GLN A 1 257 ? 131.527 148.035 136.302 1.00 62.07  ? 244 GLN A CG  1 
ATOM   1697 C CD  . GLN A 1 257 ? 131.796 148.465 137.729 1.00 76.22  ? 244 GLN A CD  1 
ATOM   1698 O OE1 . GLN A 1 257 ? 130.925 149.022 138.400 1.00 74.77  ? 244 GLN A OE1 1 
ATOM   1699 N NE2 . GLN A 1 257 ? 133.008 148.209 138.203 1.00 88.13  ? 244 GLN A NE2 1 
ATOM   1700 N N   . GLU A 1 258 ? 128.095 147.295 134.532 1.00 53.56  ? 245 GLU A N   1 
ATOM   1701 C CA  . GLU A 1 258 ? 127.257 148.131 133.679 1.00 55.77  ? 245 GLU A CA  1 
ATOM   1702 C C   . GLU A 1 258 ? 125.958 148.495 134.383 1.00 59.85  ? 245 GLU A C   1 
ATOM   1703 O O   . GLU A 1 258 ? 125.474 149.625 134.261 1.00 68.62  ? 245 GLU A O   1 
ATOM   1704 C CB  . GLU A 1 258 ? 126.969 147.421 132.357 1.00 47.92  ? 245 GLU A CB  1 
ATOM   1705 C CG  . GLU A 1 258 ? 128.168 147.305 131.437 1.00 48.72  ? 245 GLU A CG  1 
ATOM   1706 C CD  . GLU A 1 258 ? 127.814 146.685 130.101 1.00 54.45  ? 245 GLU A CD  1 
ATOM   1707 O OE1 . GLU A 1 258 ? 126.620 146.395 129.878 1.00 53.85  ? 245 GLU A OE1 1 
ATOM   1708 O OE2 . GLU A 1 258 ? 128.728 146.488 129.273 1.00 59.69  ? 245 GLU A OE2 1 
ATOM   1709 N N   . LEU A 1 259 ? 125.376 147.547 135.121 1.00 51.89  ? 246 LEU A N   1 
ATOM   1710 C CA  . LEU A 1 259 ? 124.181 147.855 135.900 1.00 49.29  ? 246 LEU A CA  1 
ATOM   1711 C C   . LEU A 1 259 ? 124.485 148.877 136.990 1.00 57.85  ? 246 LEU A C   1 
ATOM   1712 O O   . LEU A 1 259 ? 123.674 149.772 137.256 1.00 62.91  ? 246 LEU A O   1 
ATOM   1713 C CB  . LEU A 1 259 ? 123.604 146.574 136.503 1.00 48.50  ? 246 LEU A CB  1 
ATOM   1714 C CG  . LEU A 1 259 ? 122.197 146.652 137.098 1.00 49.33  ? 246 LEU A CG  1 
ATOM   1715 C CD1 . LEU A 1 259 ? 121.236 147.258 136.100 1.00 46.68  ? 246 LEU A CD1 1 
ATOM   1716 C CD2 . LEU A 1 259 ? 121.723 145.272 137.512 1.00 42.65  ? 246 LEU A CD2 1 
ATOM   1717 N N   . GLN A 1 260 ? 125.651 148.756 137.630 1.00 58.89  ? 247 GLN A N   1 
ATOM   1718 C CA  . GLN A 1 260 ? 126.067 149.737 138.630 1.00 64.64  ? 247 GLN A CA  1 
ATOM   1719 C C   . GLN A 1 260 ? 126.151 151.130 138.023 1.00 66.80  ? 247 GLN A C   1 
ATOM   1720 O O   . GLN A 1 260 ? 125.610 152.097 138.572 1.00 67.29  ? 247 GLN A O   1 
ATOM   1721 C CB  . GLN A 1 260 ? 127.420 149.346 139.228 1.00 63.26  ? 247 GLN A CB  1 
ATOM   1722 C CG  . GLN A 1 260 ? 127.483 147.958 139.829 1.00 67.30  ? 247 GLN A CG  1 
ATOM   1723 C CD  . GLN A 1 260 ? 126.686 147.833 141.105 1.00 67.03  ? 247 GLN A CD  1 
ATOM   1724 O OE1 . GLN A 1 260 ? 126.116 146.781 141.395 1.00 61.38  ? 247 GLN A OE1 1 
ATOM   1725 N NE2 . GLN A 1 260 ? 126.651 148.905 141.886 1.00 71.69  ? 247 GLN A NE2 1 
ATOM   1726 N N   . ASP A 1 261 ? 126.830 151.248 136.881 1.00 64.40  ? 248 ASP A N   1 
ATOM   1727 C CA  . ASP A 1 261 ? 126.959 152.546 136.228 1.00 62.44  ? 248 ASP A CA  1 
ATOM   1728 C C   . ASP A 1 261 ? 125.601 153.077 135.789 1.00 63.43  ? 248 ASP A C   1 
ATOM   1729 O O   . ASP A 1 261 ? 125.345 154.284 135.859 1.00 69.14  ? 248 ASP A O   1 
ATOM   1730 C CB  . ASP A 1 261 ? 127.912 152.445 135.037 1.00 66.21  ? 248 ASP A CB  1 
ATOM   1731 C CG  . ASP A 1 261 ? 129.356 152.276 135.461 1.00 73.04  ? 248 ASP A CG  1 
ATOM   1732 O OD1 . ASP A 1 261 ? 129.617 152.224 136.682 1.00 71.55  ? 248 ASP A OD1 1 
ATOM   1733 O OD2 . ASP A 1 261 ? 130.232 152.199 134.575 1.00 84.54  ? 248 ASP A OD2 1 
ATOM   1734 N N   . MET A 1 262 ? 124.719 152.189 135.332 1.00 62.76  ? 249 MET A N   1 
ATOM   1735 C CA  . MET A 1 262 ? 123.396 152.605 134.886 1.00 67.41  ? 249 MET A CA  1 
ATOM   1736 C C   . MET A 1 262 ? 122.472 152.929 136.053 1.00 68.76  ? 249 MET A C   1 
ATOM   1737 O O   . MET A 1 262 ? 121.626 153.820 135.932 1.00 70.48  ? 249 MET A O   1 
ATOM   1738 C CB  . MET A 1 262 ? 122.779 151.517 134.005 1.00 65.52  ? 249 MET A CB  1 
ATOM   1739 C CG  . MET A 1 262 ? 121.653 151.995 133.110 1.00 66.75  ? 249 MET A CG  1 
ATOM   1740 S SD  . MET A 1 262 ? 121.290 150.799 131.813 1.00 69.29  ? 249 MET A SD  1 
ATOM   1741 C CE  . MET A 1 262 ? 119.956 151.628 130.956 1.00 68.26  ? 249 MET A CE  1 
ATOM   1742 N N   . PHE A 1 263 ? 122.626 152.239 137.183 1.00 66.43  ? 250 PHE A N   1 
ATOM   1743 C CA  . PHE A 1 263 ? 121.797 152.453 138.371 1.00 71.12  ? 250 PHE A CA  1 
ATOM   1744 C C   . PHE A 1 263 ? 122.688 152.666 139.590 1.00 77.22  ? 250 PHE A C   1 
ATOM   1745 O O   . PHE A 1 263 ? 122.746 151.816 140.485 1.00 78.04  ? 250 PHE A O   1 
ATOM   1746 C CB  . PHE A 1 263 ? 120.857 151.269 138.607 1.00 67.60  ? 250 PHE A CB  1 
ATOM   1747 C CG  . PHE A 1 263 ? 119.816 151.082 137.540 1.00 67.61  ? 250 PHE A CG  1 
ATOM   1748 C CD1 . PHE A 1 263 ? 119.328 152.161 136.828 1.00 68.79  ? 250 PHE A CD1 1 
ATOM   1749 C CD2 . PHE A 1 263 ? 119.315 149.822 137.262 1.00 70.14  ? 250 PHE A CD2 1 
ATOM   1750 C CE1 . PHE A 1 263 ? 118.370 151.986 135.849 1.00 74.28  ? 250 PHE A CE1 1 
ATOM   1751 C CE2 . PHE A 1 263 ? 118.358 149.640 136.284 1.00 71.75  ? 250 PHE A CE2 1 
ATOM   1752 C CZ  . PHE A 1 263 ? 117.884 150.724 135.578 1.00 75.70  ? 250 PHE A CZ  1 
ATOM   1753 N N   . PRO A 1 264 ? 123.413 153.793 139.655 1.00 77.68  ? 251 PRO A N   1 
ATOM   1754 C CA  . PRO A 1 264 ? 124.271 154.034 140.824 1.00 78.03  ? 251 PRO A CA  1 
ATOM   1755 C C   . PRO A 1 264 ? 123.507 154.476 142.064 1.00 77.29  ? 251 PRO A C   1 
ATOM   1756 O O   . PRO A 1 264 ? 123.761 153.979 143.168 1.00 75.62  ? 251 PRO A O   1 
ATOM   1757 C CB  . PRO A 1 264 ? 125.223 155.130 140.333 1.00 77.69  ? 251 PRO A CB  1 
ATOM   1758 C CG  . PRO A 1 264 ? 124.427 155.884 139.328 1.00 74.84  ? 251 PRO A CG  1 
ATOM   1759 C CD  . PRO A 1 264 ? 123.495 154.892 138.674 1.00 74.45  ? 251 PRO A CD  1 
ATOM   1760 N N   . GLU A 1 265 ? 122.561 155.403 141.891 1.00 78.67  ? 252 GLU A N   1 
ATOM   1761 C CA  . GLU A 1 265 ? 121.916 156.018 143.047 1.00 79.04  ? 252 GLU A CA  1 
ATOM   1762 C C   . GLU A 1 265 ? 121.045 155.018 143.794 1.00 82.20  ? 252 GLU A C   1 
ATOM   1763 O O   . GLU A 1 265 ? 121.027 155.007 145.030 1.00 84.52  ? 252 GLU A O   1 
ATOM   1764 C CB  . GLU A 1 265 ? 121.105 157.247 142.617 1.00 80.43  ? 252 GLU A CB  1 
ATOM   1765 C CG  . GLU A 1 265 ? 119.742 156.968 141.982 1.00 84.51  ? 252 GLU A CG  1 
ATOM   1766 C CD  . GLU A 1 265 ? 119.838 156.366 140.590 1.00 85.28  ? 252 GLU A CD  1 
ATOM   1767 O OE1 . GLU A 1 265 ? 120.913 156.473 139.963 1.00 85.00  ? 252 GLU A OE1 1 
ATOM   1768 O OE2 . GLU A 1 265 ? 118.834 155.788 140.123 1.00 84.17  ? 252 GLU A OE2 1 
ATOM   1769 N N   . GLU A 1 266 ? 120.338 154.150 143.067 1.00 80.47  ? 253 GLU A N   1 
ATOM   1770 C CA  . GLU A 1 266 ? 119.450 153.194 143.718 1.00 76.72  ? 253 GLU A CA  1 
ATOM   1771 C C   . GLU A 1 266 ? 120.237 152.120 144.458 1.00 76.11  ? 253 GLU A C   1 
ATOM   1772 O O   . GLU A 1 266 ? 119.861 151.719 145.567 1.00 77.02  ? 253 GLU A O   1 
ATOM   1773 C CB  . GLU A 1 266 ? 118.510 152.571 142.687 1.00 70.44  ? 253 GLU A CB  1 
ATOM   1774 C CG  . GLU A 1 266 ? 117.547 151.539 143.250 1.00 74.53  ? 253 GLU A CG  1 
ATOM   1775 C CD  . GLU A 1 266 ? 116.651 152.081 144.349 1.00 79.93  ? 253 GLU A CD  1 
ATOM   1776 O OE1 . GLU A 1 266 ? 117.091 152.123 145.517 1.00 84.39  ? 253 GLU A OE1 1 
ATOM   1777 O OE2 . GLU A 1 266 ? 115.502 152.461 144.046 1.00 81.01  ? 253 GLU A OE2 1 
ATOM   1778 N N   . PHE A 1 267 ? 121.334 151.644 143.865 1.00 73.75  ? 254 PHE A N   1 
ATOM   1779 C CA  . PHE A 1 267 ? 122.179 150.681 144.561 1.00 71.36  ? 254 PHE A CA  1 
ATOM   1780 C C   . PHE A 1 267 ? 122.826 151.301 145.793 1.00 77.71  ? 254 PHE A C   1 
ATOM   1781 O O   . PHE A 1 267 ? 122.918 150.655 146.843 1.00 82.46  ? 254 PHE A O   1 
ATOM   1782 C CB  . PHE A 1 267 ? 123.241 150.123 143.615 1.00 69.41  ? 254 PHE A CB  1 
ATOM   1783 C CG  . PHE A 1 267 ? 122.725 149.066 142.681 1.00 69.10  ? 254 PHE A CG  1 
ATOM   1784 C CD1 . PHE A 1 267 ? 121.400 148.674 142.717 1.00 70.59  ? 254 PHE A CD1 1 
ATOM   1785 C CD2 . PHE A 1 267 ? 123.569 148.455 141.776 1.00 64.01  ? 254 PHE A CD2 1 
ATOM   1786 C CE1 . PHE A 1 267 ? 120.929 147.701 141.861 1.00 62.76  ? 254 PHE A CE1 1 
ATOM   1787 C CE2 . PHE A 1 267 ? 123.105 147.482 140.921 1.00 61.63  ? 254 PHE A CE2 1 
ATOM   1788 C CZ  . PHE A 1 267 ? 121.783 147.104 140.963 1.00 60.49  ? 254 PHE A CZ  1 
ATOM   1789 N N   . ASP A 1 268 ? 123.276 152.554 145.690 1.00 82.00  ? 255 ASP A N   1 
ATOM   1790 C CA  . ASP A 1 268 ? 123.830 153.222 146.864 1.00 83.69  ? 255 ASP A CA  1 
ATOM   1791 C C   . ASP A 1 268 ? 122.777 153.375 147.954 1.00 82.21  ? 255 ASP A C   1 
ATOM   1792 O O   . ASP A 1 268 ? 123.064 153.167 149.139 1.00 85.19  ? 255 ASP A O   1 
ATOM   1793 C CB  . ASP A 1 268 ? 124.409 154.582 146.478 1.00 85.00  ? 255 ASP A CB  1 
ATOM   1794 C CG  . ASP A 1 268 ? 125.132 155.254 147.629 1.00 85.16  ? 255 ASP A CG  1 
ATOM   1795 O OD1 . ASP A 1 268 ? 126.052 154.630 148.199 1.00 81.37  ? 255 ASP A OD1 1 
ATOM   1796 O OD2 . ASP A 1 268 ? 124.784 156.405 147.962 1.00 93.08  ? 255 ASP A OD2 1 
ATOM   1797 N N   . LYS A 1 269 ? 121.549 153.732 147.572 1.00 77.58  ? 256 LYS A N   1 
ATOM   1798 C CA  . LYS A 1 269 ? 120.475 153.864 148.550 1.00 78.09  ? 256 LYS A CA  1 
ATOM   1799 C C   . LYS A 1 269 ? 120.175 152.535 149.232 1.00 85.02  ? 256 LYS A C   1 
ATOM   1800 O O   . LYS A 1 269 ? 120.015 152.483 150.457 1.00 90.45  ? 256 LYS A O   1 
ATOM   1801 C CB  . LYS A 1 269 ? 119.217 154.409 147.877 1.00 76.30  ? 256 LYS A CB  1 
ATOM   1802 C CG  . LYS A 1 269 ? 117.957 154.198 148.692 1.00 79.45  ? 256 LYS A CG  1 
ATOM   1803 C CD  . LYS A 1 269 ? 116.717 154.305 147.828 1.00 77.49  ? 256 LYS A CD  1 
ATOM   1804 C CE  . LYS A 1 269 ? 115.512 153.715 148.535 1.00 83.16  ? 256 LYS A CE  1 
ATOM   1805 N NZ  . LYS A 1 269 ? 115.715 152.280 148.884 1.00 85.72  ? 256 LYS A NZ  1 
ATOM   1806 N N   . THR A 1 270 ? 120.094 151.448 148.461 1.00 84.67  ? 257 THR A N   1 
ATOM   1807 C CA  . THR A 1 270 ? 119.768 150.161 149.067 1.00 86.17  ? 257 THR A CA  1 
ATOM   1808 C C   . THR A 1 270 ? 120.927 149.593 149.877 1.00 84.91  ? 257 THR A C   1 
ATOM   1809 O O   . THR A 1 270 ? 120.694 148.773 150.770 1.00 86.17  ? 257 THR A O   1 
ATOM   1810 C CB  . THR A 1 270 ? 119.321 149.150 148.006 1.00 86.20  ? 257 THR A CB  1 
ATOM   1811 O OG1 . THR A 1 270 ? 118.756 148.004 148.653 1.00 84.32  ? 257 THR A OG1 1 
ATOM   1812 C CG2 . THR A 1 270 ? 120.490 148.700 147.152 1.00 84.96  ? 257 THR A CG2 1 
ATOM   1813 N N   . SER A 1 271 ? 122.166 150.000 149.585 1.00 83.85  ? 258 SER A N   1 
ATOM   1814 C CA  . SER A 1 271 ? 123.287 149.644 150.446 1.00 84.42  ? 258 SER A CA  1 
ATOM   1815 C C   . SER A 1 271 ? 123.394 150.548 151.667 1.00 90.99  ? 258 SER A C   1 
ATOM   1816 O O   . SER A 1 271 ? 124.062 150.178 152.640 1.00 88.36  ? 258 SER A O   1 
ATOM   1817 C CB  . SER A 1 271 ? 124.596 149.692 149.657 1.00 75.53  ? 258 SER A CB  1 
ATOM   1818 O OG  . SER A 1 271 ? 124.564 148.793 148.563 1.00 70.87  ? 258 SER A OG  1 
ATOM   1819 N N   . PHE A 1 272 ? 122.752 151.718 151.636 1.00 92.58  ? 259 PHE A N   1 
ATOM   1820 C CA  . PHE A 1 272 ? 122.813 152.637 152.768 1.00 87.10  ? 259 PHE A CA  1 
ATOM   1821 C C   . PHE A 1 272 ? 122.133 152.050 153.997 1.00 87.77  ? 259 PHE A C   1 
ATOM   1822 O O   . PHE A 1 272 ? 122.542 152.325 155.132 1.00 88.44  ? 259 PHE A O   1 
ATOM   1823 C CB  . PHE A 1 272 ? 122.175 153.973 152.387 1.00 88.77  ? 259 PHE A CB  1 
ATOM   1824 C CG  . PHE A 1 272 ? 122.135 154.971 153.508 1.00 96.10  ? 259 PHE A CG  1 
ATOM   1825 C CD1 . PHE A 1 272 ? 123.216 155.802 153.750 1.00 101.68 ? 259 PHE A CD1 1 
ATOM   1826 C CD2 . PHE A 1 272 ? 121.013 155.088 154.314 1.00 96.74  ? 259 PHE A CD2 1 
ATOM   1827 C CE1 . PHE A 1 272 ? 123.183 156.724 154.778 1.00 102.16 ? 259 PHE A CE1 1 
ATOM   1828 C CE2 . PHE A 1 272 ? 120.974 156.006 155.344 1.00 99.01  ? 259 PHE A CE2 1 
ATOM   1829 C CZ  . PHE A 1 272 ? 122.060 156.826 155.576 1.00 102.72 ? 259 PHE A CZ  1 
ATOM   1830 N N   . HIS A 1 273 ? 121.087 151.253 153.794 1.00 87.75  ? 260 HIS A N   1 
ATOM   1831 C CA  . HIS A 1 273 ? 120.339 150.700 154.914 1.00 91.23  ? 260 HIS A CA  1 
ATOM   1832 C C   . HIS A 1 273 ? 121.215 149.763 155.737 1.00 92.40  ? 260 HIS A C   1 
ATOM   1833 O O   . HIS A 1 273 ? 121.999 148.979 155.195 1.00 90.99  ? 260 HIS A O   1 
ATOM   1834 C CB  . HIS A 1 273 ? 119.102 149.953 154.416 1.00 88.97  ? 260 HIS A CB  1 
ATOM   1835 C CG  . HIS A 1 273 ? 118.180 150.792 153.587 1.00 86.88  ? 260 HIS A CG  1 
ATOM   1836 N ND1 . HIS A 1 273 ? 117.247 151.644 154.141 1.00 90.16  ? 260 HIS A ND1 1 
ATOM   1837 C CD2 . HIS A 1 273 ? 118.039 150.900 152.244 1.00 85.59  ? 260 HIS A CD2 1 
ATOM   1838 C CE1 . HIS A 1 273 ? 116.576 152.245 153.175 1.00 90.15  ? 260 HIS A CE1 1 
ATOM   1839 N NE2 . HIS A 1 273 ? 117.037 151.812 152.015 1.00 87.08  ? 260 HIS A NE2 1 
ATOM   1840 N N   . LYS A 1 274 ? 121.084 149.860 157.059 1.00 93.15  ? 261 LYS A N   1 
ATOM   1841 C CA  . LYS A 1 274 ? 121.825 149.015 157.985 1.00 93.85  ? 261 LYS A CA  1 
ATOM   1842 C C   . LYS A 1 274 ? 121.058 147.765 158.398 1.00 94.66  ? 261 LYS A C   1 
ATOM   1843 O O   . LYS A 1 274 ? 121.644 146.874 159.021 1.00 96.60  ? 261 LYS A O   1 
ATOM   1844 C CB  . LYS A 1 274 ? 122.207 149.813 159.236 1.00 98.60  ? 261 LYS A CB  1 
ATOM   1845 C CG  . LYS A 1 274 ? 122.704 151.226 158.952 1.00 99.90  ? 261 LYS A CG  1 
ATOM   1846 C CD  . LYS A 1 274 ? 123.909 151.222 158.030 1.00 100.05 ? 261 LYS A CD  1 
ATOM   1847 C CE  . LYS A 1 274 ? 125.072 150.486 158.658 1.00 96.38  ? 261 LYS A CE  1 
ATOM   1848 N NZ  . LYS A 1 274 ? 126.107 150.146 157.646 1.00 95.24  ? 261 LYS A NZ  1 
ATOM   1849 N N   . VAL A 1 275 ? 119.762 147.692 158.102 1.00 97.64  ? 262 VAL A N   1 
ATOM   1850 C CA  . VAL A 1 275 ? 118.961 146.498 158.342 1.00 97.42  ? 262 VAL A CA  1 
ATOM   1851 C C   . VAL A 1 275 ? 118.145 146.239 157.083 1.00 95.07  ? 262 VAL A C   1 
ATOM   1852 O O   . VAL A 1 275 ? 117.889 147.153 156.292 1.00 99.11  ? 262 VAL A O   1 
ATOM   1853 C CB  . VAL A 1 275 ? 118.050 146.647 159.588 1.00 98.74  ? 262 VAL A CB  1 
ATOM   1854 C CG1 . VAL A 1 275 ? 117.395 145.320 159.953 1.00 92.25  ? 262 VAL A CG1 1 
ATOM   1855 C CG2 . VAL A 1 275 ? 118.837 147.187 160.777 1.00 99.86  ? 262 VAL A CG2 1 
ATOM   1856 N N   . ARG A 1 276 ? 117.764 144.977 156.882 1.00 88.76  ? 263 ARG A N   1 
ATOM   1857 C CA  . ARG A 1 276 ? 116.933 144.594 155.746 1.00 96.18  ? 263 ARG A CA  1 
ATOM   1858 C C   . ARG A 1 276 ? 115.675 145.447 155.685 1.00 98.70  ? 263 ARG A C   1 
ATOM   1859 O O   . ARG A 1 276 ? 114.870 145.455 156.621 1.00 96.67  ? 263 ARG A O   1 
ATOM   1860 C CB  . ARG A 1 276 ? 116.567 143.113 155.851 1.00 98.52  ? 263 ARG A CB  1 
ATOM   1861 C CG  . ARG A 1 276 ? 117.432 142.187 155.016 1.00 88.50  ? 263 ARG A CG  1 
ATOM   1862 C CD  . ARG A 1 276 ? 116.906 142.095 153.598 1.00 83.43  ? 263 ARG A CD  1 
ATOM   1863 N NE  . ARG A 1 276 ? 115.508 141.685 153.563 1.00 86.54  ? 263 ARG A NE  1 
ATOM   1864 C CZ  . ARG A 1 276 ? 114.767 141.645 152.466 1.00 94.34  ? 263 ARG A CZ  1 
ATOM   1865 N NH1 . ARG A 1 276 ? 115.261 141.980 151.285 1.00 99.17  ? 263 ARG A NH1 1 
ATOM   1866 N NH2 . ARG A 1 276 ? 113.497 141.262 152.555 1.00 96.03  ? 263 ARG A NH2 1 
ATOM   1867 N N   . HIS A 1 277 ? 115.504 146.156 154.575 1.00 98.72  ? 264 HIS A N   1 
ATOM   1868 C CA  . HIS A 1 277 ? 114.425 147.118 154.413 1.00 99.95  ? 264 HIS A CA  1 
ATOM   1869 C C   . HIS A 1 277 ? 113.395 146.597 153.419 1.00 97.46  ? 264 HIS A C   1 
ATOM   1870 O O   . HIS A 1 277 ? 113.645 145.666 152.650 1.00 94.34  ? 264 HIS A O   1 
ATOM   1871 C CB  . HIS A 1 277 ? 114.974 148.475 153.956 1.00 99.90  ? 264 HIS A CB  1 
ATOM   1872 C CG  . HIS A 1 277 ? 114.008 149.605 154.130 1.00 97.52  ? 264 HIS A CG  1 
ATOM   1873 N ND1 . HIS A 1 277 ? 113.826 150.582 153.175 1.00 96.47  ? 264 HIS A ND1 1 
ATOM   1874 C CD2 . HIS A 1 277 ? 113.176 149.917 155.151 1.00 96.97  ? 264 HIS A CD2 1 
ATOM   1875 C CE1 . HIS A 1 277 ? 112.918 151.443 153.597 1.00 96.13  ? 264 HIS A CE1 1 
ATOM   1876 N NE2 . HIS A 1 277 ? 112.508 151.063 154.794 1.00 99.61  ? 264 HIS A NE2 1 
ATOM   1877 N N   . SER A 1 278 ? 112.221 147.229 153.442 1.00 101.97 ? 265 SER A N   1 
ATOM   1878 C CA  . SER A 1 278 ? 111.096 146.808 152.617 1.00 106.12 ? 265 SER A CA  1 
ATOM   1879 C C   . SER A 1 278 ? 111.289 147.109 151.137 1.00 102.41 ? 265 SER A C   1 
ATOM   1880 O O   . SER A 1 278 ? 110.467 146.668 150.328 1.00 99.97  ? 265 SER A O   1 
ATOM   1881 C CB  . SER A 1 278 ? 109.813 147.476 153.110 1.00 105.22 ? 265 SER A CB  1 
ATOM   1882 O OG  . SER A 1 278 ? 109.626 147.254 154.497 1.00 100.71 ? 265 SER A OG  1 
ATOM   1883 N N   . GLU A 1 279 ? 112.327 147.856 150.762 1.00 99.56  ? 266 GLU A N   1 
ATOM   1884 C CA  . GLU A 1 279 ? 112.511 148.270 149.375 1.00 100.23 ? 266 GLU A CA  1 
ATOM   1885 C C   . GLU A 1 279 ? 113.955 148.071 148.933 1.00 98.74  ? 266 GLU A C   1 
ATOM   1886 O O   . GLU A 1 279 ? 114.518 148.890 148.199 1.00 94.67  ? 266 GLU A O   1 
ATOM   1887 C CB  . GLU A 1 279 ? 112.075 149.721 149.176 1.00 99.71  ? 266 GLU A CB  1 
ATOM   1888 C CG  . GLU A 1 279 ? 112.771 150.715 150.089 1.00 98.03  ? 266 GLU A CG  1 
ATOM   1889 C CD  . GLU A 1 279 ? 112.120 152.083 150.058 1.00 99.29  ? 266 GLU A CD  1 
ATOM   1890 O OE1 . GLU A 1 279 ? 111.194 152.326 150.861 1.00 103.51 ? 266 GLU A OE1 1 
ATOM   1891 O OE2 . GLU A 1 279 ? 112.527 152.914 149.221 1.00 97.50  ? 266 GLU A OE2 1 
ATOM   1892 N N   . ASP A 1 280 ? 114.575 146.979 149.371 1.00 98.20  ? 267 ASP A N   1 
ATOM   1893 C CA  . ASP A 1 280 ? 115.905 146.630 148.899 1.00 96.67  ? 267 ASP A CA  1 
ATOM   1894 C C   . ASP A 1 280 ? 115.829 146.016 147.501 1.00 95.61  ? 267 ASP A C   1 
ATOM   1895 O O   . ASP A 1 280 ? 114.767 145.597 147.033 1.00 96.91  ? 267 ASP A O   1 
ATOM   1896 C CB  . ASP A 1 280 ? 116.583 145.667 149.871 1.00 95.98  ? 267 ASP A CB  1 
ATOM   1897 C CG  . ASP A 1 280 ? 116.900 146.314 151.203 1.00 94.26  ? 267 ASP A CG  1 
ATOM   1898 O OD1 . ASP A 1 280 ? 117.296 147.498 151.210 1.00 98.04  ? 267 ASP A OD1 1 
ATOM   1899 O OD2 . ASP A 1 280 ? 116.753 145.641 152.244 1.00 92.18  ? 267 ASP A OD2 1 
ATOM   1900 N N   . MET A 1 281 ? 116.976 145.960 146.831 1.00 88.43  ? 268 MET A N   1 
ATOM   1901 C CA  . MET A 1 281 ? 117.066 145.404 145.488 1.00 79.01  ? 268 MET A CA  1 
ATOM   1902 C C   . MET A 1 281 ? 117.735 144.039 145.538 1.00 71.38  ? 268 MET A C   1 
ATOM   1903 O O   . MET A 1 281 ? 118.864 143.914 146.020 1.00 73.38  ? 268 MET A O   1 
ATOM   1904 C CB  . MET A 1 281 ? 117.839 146.335 144.554 1.00 76.41  ? 268 MET A CB  1 
ATOM   1905 C CG  . MET A 1 281 ? 117.090 147.596 144.177 1.00 81.10  ? 268 MET A CG  1 
ATOM   1906 S SD  . MET A 1 281 ? 117.612 148.223 142.572 1.00 75.41  ? 268 MET A SD  1 
ATOM   1907 C CE  . MET A 1 281 ? 117.064 146.904 141.500 1.00 70.16  ? 268 MET A CE  1 
ATOM   1908 N N   . GLN A 1 282 ? 117.043 143.028 145.020 1.00 65.47  ? 269 GLN A N   1 
ATOM   1909 C CA  . GLN A 1 282 ? 117.558 141.666 145.038 1.00 58.15  ? 269 GLN A CA  1 
ATOM   1910 C C   . GLN A 1 282 ? 118.796 141.550 144.161 1.00 55.73  ? 269 GLN A C   1 
ATOM   1911 O O   . GLN A 1 282 ? 118.967 142.295 143.193 1.00 60.37  ? 269 GLN A O   1 
ATOM   1912 C CB  . GLN A 1 282 ? 116.493 140.679 144.564 1.00 56.65  ? 269 GLN A CB  1 
ATOM   1913 C CG  . GLN A 1 282 ? 115.259 140.626 145.446 1.00 72.25  ? 269 GLN A CG  1 
ATOM   1914 C CD  . GLN A 1 282 ? 114.304 141.778 145.193 1.00 82.25  ? 269 GLN A CD  1 
ATOM   1915 O OE1 . GLN A 1 282 ? 114.131 142.217 144.056 1.00 76.23  ? 269 GLN A OE1 1 
ATOM   1916 N NE2 . GLN A 1 282 ? 113.684 142.279 146.255 1.00 87.48  ? 269 GLN A NE2 1 
ATOM   1917 N N   . PHE A 1 283 ? 119.679 140.622 144.524 1.00 54.77  ? 270 PHE A N   1 
ATOM   1918 C CA  . PHE A 1 283 ? 120.924 140.465 143.786 1.00 53.58  ? 270 PHE A CA  1 
ATOM   1919 C C   . PHE A 1 283 ? 120.730 139.706 142.479 1.00 52.13  ? 270 PHE A C   1 
ATOM   1920 O O   . PHE A 1 283 ? 121.344 140.052 141.463 1.00 57.16  ? 270 PHE A O   1 
ATOM   1921 C CB  . PHE A 1 283 ? 121.958 139.752 144.651 1.00 52.76  ? 270 PHE A CB  1 
ATOM   1922 C CG  . PHE A 1 283 ? 123.200 139.382 143.908 1.00 57.32  ? 270 PHE A CG  1 
ATOM   1923 C CD1 . PHE A 1 283 ? 123.479 138.061 143.606 1.00 54.46  ? 270 PHE A CD1 1 
ATOM   1924 C CD2 . PHE A 1 283 ? 124.081 140.362 143.491 1.00 56.40  ? 270 PHE A CD2 1 
ATOM   1925 C CE1 . PHE A 1 283 ? 124.628 137.724 142.916 1.00 54.90  ? 270 PHE A CE1 1 
ATOM   1926 C CE2 . PHE A 1 283 ? 125.227 140.033 142.802 1.00 57.94  ? 270 PHE A CE2 1 
ATOM   1927 C CZ  . PHE A 1 283 ? 125.502 138.714 142.514 1.00 56.71  ? 270 PHE A CZ  1 
ATOM   1928 N N   . ALA A 1 284 ? 119.896 138.667 142.482 1.00 43.16  ? 271 ALA A N   1 
ATOM   1929 C CA  . ALA A 1 284 ? 119.769 137.834 141.292 1.00 42.37  ? 271 ALA A CA  1 
ATOM   1930 C C   . ALA A 1 284 ? 118.752 138.399 140.309 1.00 43.10  ? 271 ALA A C   1 
ATOM   1931 O O   . ALA A 1 284 ? 118.989 138.387 139.096 1.00 43.32  ? 271 ALA A O   1 
ATOM   1932 C CB  . ALA A 1 284 ? 119.385 136.410 141.690 1.00 43.34  ? 271 ALA A CB  1 
ATOM   1933 N N   . PHE A 1 285 ? 117.614 138.878 140.815 1.00 47.21  ? 272 PHE A N   1 
ATOM   1934 C CA  . PHE A 1 285 ? 116.548 139.358 139.942 1.00 44.65  ? 272 PHE A CA  1 
ATOM   1935 C C   . PHE A 1 285 ? 117.008 140.547 139.108 1.00 40.18  ? 272 PHE A C   1 
ATOM   1936 O O   . PHE A 1 285 ? 116.754 140.607 137.899 1.00 42.75  ? 272 PHE A O   1 
ATOM   1937 C CB  . PHE A 1 285 ? 115.323 139.727 140.777 1.00 43.55  ? 272 PHE A CB  1 
ATOM   1938 C CG  . PHE A 1 285 ? 114.183 140.259 139.967 1.00 41.49  ? 272 PHE A CG  1 
ATOM   1939 C CD1 . PHE A 1 285 ? 113.268 139.399 139.392 1.00 46.87  ? 272 PHE A CD1 1 
ATOM   1940 C CD2 . PHE A 1 285 ? 114.023 141.619 139.780 1.00 47.78  ? 272 PHE A CD2 1 
ATOM   1941 C CE1 . PHE A 1 285 ? 112.219 139.882 138.647 1.00 48.09  ? 272 PHE A CE1 1 
ATOM   1942 C CE2 . PHE A 1 285 ? 112.976 142.106 139.034 1.00 55.90  ? 272 PHE A CE2 1 
ATOM   1943 C CZ  . PHE A 1 285 ? 112.076 141.235 138.465 1.00 50.32  ? 272 PHE A CZ  1 
ATOM   1944 N N   . SER A 1 286 ? 117.676 141.511 139.744 1.00 36.56  ? 273 SER A N   1 
ATOM   1945 C CA  . SER A 1 286 ? 118.133 142.694 139.023 1.00 36.48  ? 273 SER A CA  1 
ATOM   1946 C C   . SER A 1 286 ? 119.091 142.310 137.907 1.00 42.03  ? 273 SER A C   1 
ATOM   1947 O O   . SER A 1 286 ? 118.921 142.728 136.756 1.00 54.08  ? 273 SER A O   1 
ATOM   1948 C CB  . SER A 1 286 ? 118.802 143.667 139.991 1.00 38.83  ? 273 SER A CB  1 
ATOM   1949 O OG  . SER A 1 286 ? 118.005 143.853 141.145 1.00 56.35  ? 273 SER A OG  1 
ATOM   1950 N N   . TYR A 1 287 ? 120.094 141.492 138.232 1.00 33.36  ? 274 TYR A N   1 
ATOM   1951 C CA  . TYR A 1 287 ? 121.079 141.079 137.240 1.00 31.88  ? 274 TYR A CA  1 
ATOM   1952 C C   . TYR A 1 287 ? 120.417 140.338 136.087 1.00 31.52  ? 274 TYR A C   1 
ATOM   1953 O O   . TYR A 1 287 ? 120.683 140.625 134.914 1.00 35.96  ? 274 TYR A O   1 
ATOM   1954 C CB  . TYR A 1 287 ? 122.144 140.205 137.899 1.00 28.80  ? 274 TYR A CB  1 
ATOM   1955 C CG  . TYR A 1 287 ? 123.152 139.630 136.933 1.00 24.85  ? 274 TYR A CG  1 
ATOM   1956 C CD1 . TYR A 1 287 ? 124.274 140.353 136.563 1.00 27.91  ? 274 TYR A CD1 1 
ATOM   1957 C CD2 . TYR A 1 287 ? 122.987 138.361 136.402 1.00 28.47  ? 274 TYR A CD2 1 
ATOM   1958 C CE1 . TYR A 1 287 ? 125.197 139.830 135.686 1.00 27.99  ? 274 TYR A CE1 1 
ATOM   1959 C CE2 . TYR A 1 287 ? 123.905 137.833 135.525 1.00 27.84  ? 274 TYR A CE2 1 
ATOM   1960 C CZ  . TYR A 1 287 ? 125.006 138.569 135.171 1.00 29.49  ? 274 TYR A CZ  1 
ATOM   1961 O OH  . TYR A 1 287 ? 125.919 138.039 134.295 1.00 38.08  ? 274 TYR A OH  1 
ATOM   1962 N N   . PHE A 1 288 ? 119.539 139.382 136.401 1.00 31.10  ? 275 PHE A N   1 
ATOM   1963 C CA  . PHE A 1 288 ? 118.931 138.576 135.349 1.00 34.12  ? 275 PHE A CA  1 
ATOM   1964 C C   . PHE A 1 288 ? 118.030 139.409 134.452 1.00 36.79  ? 275 PHE A C   1 
ATOM   1965 O O   . PHE A 1 288 ? 118.081 139.277 133.226 1.00 41.23  ? 275 PHE A O   1 
ATOM   1966 C CB  . PHE A 1 288 ? 118.155 137.416 135.961 1.00 36.94  ? 275 PHE A CB  1 
ATOM   1967 C CG  . PHE A 1 288 ? 119.033 136.334 136.499 1.00 31.27  ? 275 PHE A CG  1 
ATOM   1968 C CD1 . PHE A 1 288 ? 120.265 136.086 135.926 1.00 28.77  ? 275 PHE A CD1 1 
ATOM   1969 C CD2 . PHE A 1 288 ? 118.637 135.576 137.581 1.00 29.96  ? 275 PHE A CD2 1 
ATOM   1970 C CE1 . PHE A 1 288 ? 121.082 135.097 136.416 1.00 28.11  ? 275 PHE A CE1 1 
ATOM   1971 C CE2 . PHE A 1 288 ? 119.449 134.586 138.075 1.00 31.44  ? 275 PHE A CE2 1 
ATOM   1972 C CZ  . PHE A 1 288 ? 120.675 134.346 137.492 1.00 32.53  ? 275 PHE A CZ  1 
ATOM   1973 N N   . TYR A 1 289 ? 117.201 140.279 135.027 1.00 35.88  ? 276 TYR A N   1 
ATOM   1974 C CA  . TYR A 1 289 ? 116.290 141.023 134.169 1.00 41.03  ? 276 TYR A CA  1 
ATOM   1975 C C   . TYR A 1 289 ? 116.991 142.150 133.421 1.00 42.66  ? 276 TYR A C   1 
ATOM   1976 O O   . TYR A 1 289 ? 116.546 142.525 132.330 1.00 50.15  ? 276 TYR A O   1 
ATOM   1977 C CB  . TYR A 1 289 ? 115.099 141.534 134.975 1.00 48.48  ? 276 TYR A CB  1 
ATOM   1978 C CG  . TYR A 1 289 ? 113.952 140.554 134.932 1.00 47.85  ? 276 TYR A CG  1 
ATOM   1979 C CD1 . TYR A 1 289 ? 113.986 139.389 135.684 1.00 44.88  ? 276 TYR A CD1 1 
ATOM   1980 C CD2 . TYR A 1 289 ? 112.855 140.770 134.111 1.00 52.23  ? 276 TYR A CD2 1 
ATOM   1981 C CE1 . TYR A 1 289 ? 112.953 138.479 135.637 1.00 53.08  ? 276 TYR A CE1 1 
ATOM   1982 C CE2 . TYR A 1 289 ? 111.813 139.865 134.059 1.00 59.58  ? 276 TYR A CE2 1 
ATOM   1983 C CZ  . TYR A 1 289 ? 111.868 138.721 134.825 1.00 60.89  ? 276 TYR A CZ  1 
ATOM   1984 O OH  . TYR A 1 289 ? 110.841 137.809 134.782 1.00 67.32  ? 276 TYR A OH  1 
ATOM   1985 N N   . TYR A 1 290 ? 118.095 142.682 133.955 1.00 35.06  ? 277 TYR A N   1 
ATOM   1986 C CA  . TYR A 1 290 ? 118.907 143.580 133.145 1.00 35.82  ? 277 TYR A CA  1 
ATOM   1987 C C   . TYR A 1 290 ? 119.593 142.832 132.013 1.00 38.80  ? 277 TYR A C   1 
ATOM   1988 O O   . TYR A 1 290 ? 119.767 143.386 130.923 1.00 47.04  ? 277 TYR A O   1 
ATOM   1989 C CB  . TYR A 1 290 ? 119.948 144.294 133.999 1.00 39.12  ? 277 TYR A CB  1 
ATOM   1990 C CG  . TYR A 1 290 ? 120.891 145.133 133.174 1.00 46.75  ? 277 TYR A CG  1 
ATOM   1991 C CD1 . TYR A 1 290 ? 120.466 146.324 132.602 1.00 46.76  ? 277 TYR A CD1 1 
ATOM   1992 C CD2 . TYR A 1 290 ? 122.200 144.732 132.954 1.00 48.38  ? 277 TYR A CD2 1 
ATOM   1993 C CE1 . TYR A 1 290 ? 121.318 147.095 131.842 1.00 41.71  ? 277 TYR A CE1 1 
ATOM   1994 C CE2 . TYR A 1 290 ? 123.062 145.499 132.195 1.00 50.10  ? 277 TYR A CE2 1 
ATOM   1995 C CZ  . TYR A 1 290 ? 122.614 146.678 131.642 1.00 44.92  ? 277 TYR A CZ  1 
ATOM   1996 O OH  . TYR A 1 290 ? 123.466 147.446 130.886 1.00 49.85  ? 277 TYR A OH  1 
ATOM   1997 N N   . LEU A 1 291 ? 119.998 141.584 132.254 1.00 36.97  ? 278 LEU A N   1 
ATOM   1998 C CA  . LEU A 1 291 ? 120.516 140.754 131.172 1.00 38.75  ? 278 LEU A CA  1 
ATOM   1999 C C   . LEU A 1 291 ? 119.456 140.535 130.102 1.00 42.65  ? 278 LEU A C   1 
ATOM   2000 O O   . LEU A 1 291 ? 119.746 140.604 128.902 1.00 42.03  ? 278 LEU A O   1 
ATOM   2001 C CB  . LEU A 1 291 ? 120.993 139.417 131.736 1.00 32.80  ? 278 LEU A CB  1 
ATOM   2002 C CG  . LEU A 1 291 ? 121.687 138.443 130.791 1.00 29.96  ? 278 LEU A CG  1 
ATOM   2003 C CD1 . LEU A 1 291 ? 123.149 138.818 130.627 1.00 32.59  ? 278 LEU A CD1 1 
ATOM   2004 C CD2 . LEU A 1 291 ? 121.542 137.024 131.308 1.00 37.10  ? 278 LEU A CD2 1 
ATOM   2005 N N   . MET A 1 292 ? 118.219 140.271 130.526 1.00 46.52  ? 279 MET A N   1 
ATOM   2006 C CA  . MET A 1 292 ? 117.131 140.040 129.581 1.00 46.68  ? 279 MET A CA  1 
ATOM   2007 C C   . MET A 1 292 ? 116.845 141.287 128.753 1.00 44.36  ? 279 MET A C   1 
ATOM   2008 O O   . MET A 1 292 ? 116.752 141.221 127.523 1.00 45.79  ? 279 MET A O   1 
ATOM   2009 C CB  . MET A 1 292 ? 115.868 139.599 130.326 1.00 44.60  ? 279 MET A CB  1 
ATOM   2010 C CG  . MET A 1 292 ? 116.034 138.377 131.215 1.00 42.44  ? 279 MET A CG  1 
ATOM   2011 S SD  . MET A 1 292 ? 115.665 136.808 130.418 1.00 49.52  ? 279 MET A SD  1 
ATOM   2012 C CE  . MET A 1 292 ? 113.875 136.839 130.415 1.00 53.14  ? 279 MET A CE  1 
ATOM   2013 N N   . SER A 1 293 ? 116.709 142.439 129.413 1.00 46.44  ? 280 SER A N   1 
ATOM   2014 C CA  . SER A 1 293 ? 116.192 143.644 128.777 1.00 53.73  ? 280 SER A CA  1 
ATOM   2015 C C   . SER A 1 293 ? 117.279 144.656 128.424 1.00 55.67  ? 280 SER A C   1 
ATOM   2016 O O   . SER A 1 293 ? 116.987 145.852 128.319 1.00 60.22  ? 280 SER A O   1 
ATOM   2017 C CB  . SER A 1 293 ? 115.138 144.292 129.674 1.00 59.12  ? 280 SER A CB  1 
ATOM   2018 O OG  . SER A 1 293 ? 114.106 143.373 129.983 1.00 62.11  ? 280 SER A OG  1 
ATOM   2019 N N   . ALA A 1 294 ? 118.520 144.213 128.244 1.00 52.06  ? 281 ALA A N   1 
ATOM   2020 C CA  . ALA A 1 294 ? 119.590 145.111 127.827 1.00 48.55  ? 281 ALA A CA  1 
ATOM   2021 C C   . ALA A 1 294 ? 119.475 145.380 126.332 1.00 55.42  ? 281 ALA A C   1 
ATOM   2022 O O   . ALA A 1 294 ? 119.547 144.450 125.523 1.00 60.52  ? 281 ALA A O   1 
ATOM   2023 C CB  . ALA A 1 294 ? 120.953 144.514 128.163 1.00 46.84  ? 281 ALA A CB  1 
ATOM   2024 N N   . VAL A 1 295 ? 119.316 146.648 125.963 1.00 60.43  ? 282 VAL A N   1 
ATOM   2025 C CA  . VAL A 1 295 ? 119.098 147.044 124.576 1.00 67.39  ? 282 VAL A CA  1 
ATOM   2026 C C   . VAL A 1 295 ? 120.427 147.458 123.959 1.00 69.78  ? 282 VAL A C   1 
ATOM   2027 O O   . VAL A 1 295 ? 121.280 148.057 124.626 1.00 69.30  ? 282 VAL A O   1 
ATOM   2028 C CB  . VAL A 1 295 ? 118.054 148.176 124.480 1.00 67.40  ? 282 VAL A CB  1 
ATOM   2029 C CG1 . VAL A 1 295 ? 118.547 149.435 125.180 1.00 68.18  ? 282 VAL A CG1 1 
ATOM   2030 C CG2 . VAL A 1 295 ? 117.697 148.461 123.030 1.00 72.25  ? 282 VAL A CG2 1 
ATOM   2031 N N   . GLN A 1 296 ? 120.612 147.120 122.685 1.00 70.63  ? 283 GLN A N   1 
ATOM   2032 C CA  . GLN A 1 296 ? 121.826 147.426 121.952 1.00 73.09  ? 283 GLN A CA  1 
ATOM   2033 C C   . GLN A 1 296 ? 121.509 148.386 120.812 1.00 81.95  ? 283 GLN A C   1 
ATOM   2034 O O   . GLN A 1 296 ? 120.547 148.155 120.066 1.00 82.81  ? 283 GLN A O   1 
ATOM   2035 C CB  . GLN A 1 296 ? 122.464 146.146 121.392 1.00 73.73  ? 283 GLN A CB  1 
ATOM   2036 C CG  . GLN A 1 296 ? 123.815 146.355 120.733 1.00 73.93  ? 283 GLN A CG  1 
ATOM   2037 C CD  . GLN A 1 296 ? 124.345 145.091 120.086 1.00 76.21  ? 283 GLN A CD  1 
ATOM   2038 O OE1 . GLN A 1 296 ? 123.577 144.249 119.624 1.00 76.30  ? 283 GLN A OE1 1 
ATOM   2039 N NE2 . GLN A 1 296 ? 125.666 144.951 120.054 1.00 72.81  ? 283 GLN A NE2 1 
ATOM   2040 N N   . PRO A 1 297 ? 122.272 149.463 120.647 1.00 82.70  ? 284 PRO A N   1 
ATOM   2041 C CA  . PRO A 1 297 ? 122.005 150.391 119.544 1.00 74.87  ? 284 PRO A CA  1 
ATOM   2042 C C   . PRO A 1 297 ? 122.208 149.728 118.191 1.00 76.72  ? 284 PRO A C   1 
ATOM   2043 O O   . PRO A 1 297 ? 123.059 148.851 118.020 1.00 77.72  ? 284 PRO A O   1 
ATOM   2044 C CB  . PRO A 1 297 ? 123.024 151.514 119.770 1.00 73.47  ? 284 PRO A CB  1 
ATOM   2045 C CG  . PRO A 1 297 ? 124.116 150.876 120.562 1.00 79.79  ? 284 PRO A CG  1 
ATOM   2046 C CD  . PRO A 1 297 ? 123.433 149.880 121.452 1.00 81.72  ? 284 PRO A CD  1 
ATOM   2047 N N   . LEU A 1 298 ? 121.408 150.164 117.222 1.00 80.04  ? 285 LEU A N   1 
ATOM   2048 C CA  . LEU A 1 298 ? 121.464 149.624 115.865 1.00 75.52  ? 285 LEU A CA  1 
ATOM   2049 C C   . LEU A 1 298 ? 122.631 150.273 115.135 1.00 71.99  ? 285 LEU A C   1 
ATOM   2050 O O   . LEU A 1 298 ? 122.544 151.420 114.690 1.00 73.47  ? 285 LEU A O   1 
ATOM   2051 C CB  . LEU A 1 298 ? 120.151 149.863 115.129 1.00 76.27  ? 285 LEU A CB  1 
ATOM   2052 C CG  . LEU A 1 298 ? 118.979 148.917 115.410 1.00 76.46  ? 285 LEU A CG  1 
ATOM   2053 C CD1 . LEU A 1 298 ? 118.355 149.179 116.774 1.00 81.31  ? 285 LEU A CD1 1 
ATOM   2054 C CD2 . LEU A 1 298 ? 117.935 149.028 114.312 1.00 77.69  ? 285 LEU A CD2 1 
ATOM   2055 N N   . ASN A 1 299 ? 123.728 149.536 115.004 1.00 69.56  ? 286 ASN A N   1 
ATOM   2056 C CA  . ASN A 1 299 ? 124.911 150.020 114.304 1.00 71.39  ? 286 ASN A CA  1 
ATOM   2057 C C   . ASN A 1 299 ? 124.742 149.718 112.820 1.00 74.51  ? 286 ASN A C   1 
ATOM   2058 O O   . ASN A 1 299 ? 124.822 148.559 112.400 1.00 76.55  ? 286 ASN A O   1 
ATOM   2059 C CB  . ASN A 1 299 ? 126.171 149.368 114.867 1.00 73.91  ? 286 ASN A CB  1 
ATOM   2060 C CG  . ASN A 1 299 ? 127.440 150.000 114.339 1.00 76.27  ? 286 ASN A CG  1 
ATOM   2061 O OD1 . ASN A 1 299 ? 127.426 151.116 113.821 1.00 77.67  ? 286 ASN A OD1 1 
ATOM   2062 N ND2 . ASN A 1 299 ? 128.551 149.287 114.475 1.00 76.50  ? 286 ASN A ND2 1 
ATOM   2063 N N   . ILE A 1 300 ? 124.501 150.765 112.027 1.00 72.84  ? 287 ILE A N   1 
ATOM   2064 C CA  . ILE A 1 300 ? 124.255 150.588 110.599 1.00 70.14  ? 287 ILE A CA  1 
ATOM   2065 C C   . ILE A 1 300 ? 125.499 150.067 109.889 1.00 73.78  ? 287 ILE A C   1 
ATOM   2066 O O   . ILE A 1 300 ? 125.397 149.382 108.862 1.00 78.91  ? 287 ILE A O   1 
ATOM   2067 C CB  . ILE A 1 300 ? 123.760 151.912 109.988 1.00 64.41  ? 287 ILE A CB  1 
ATOM   2068 C CG1 . ILE A 1 300 ? 122.547 152.424 110.765 1.00 68.14  ? 287 ILE A CG1 1 
ATOM   2069 C CG2 . ILE A 1 300 ? 123.406 151.735 108.521 1.00 66.88  ? 287 ILE A CG2 1 
ATOM   2070 C CD1 . ILE A 1 300 ? 121.944 153.685 110.198 1.00 75.65  ? 287 ILE A CD1 1 
ATOM   2071 N N   . SER A 1 301 ? 126.686 150.379 110.412 1.00 73.06  ? 288 SER A N   1 
ATOM   2072 C CA  . SER A 1 301 ? 127.919 149.945 109.763 1.00 72.83  ? 288 SER A CA  1 
ATOM   2073 C C   . SER A 1 301 ? 128.015 148.424 109.709 1.00 78.66  ? 288 SER A C   1 
ATOM   2074 O O   . SER A 1 301 ? 128.422 147.860 108.689 1.00 79.60  ? 288 SER A O   1 
ATOM   2075 C CB  . SER A 1 301 ? 129.127 150.540 110.484 1.00 74.77  ? 288 SER A CB  1 
ATOM   2076 O OG  . SER A 1 301 ? 130.329 150.278 109.780 1.00 75.76  ? 288 SER A OG  1 
ATOM   2077 N N   . GLN A 1 302 ? 127.652 147.743 110.798 1.00 80.45  ? 289 GLN A N   1 
ATOM   2078 C CA  . GLN A 1 302 ? 127.655 146.282 110.789 1.00 79.22  ? 289 GLN A CA  1 
ATOM   2079 C C   . GLN A 1 302 ? 126.620 145.732 109.814 1.00 79.21  ? 289 GLN A C   1 
ATOM   2080 O O   . GLN A 1 302 ? 126.853 144.707 109.161 1.00 79.20  ? 289 GLN A O   1 
ATOM   2081 C CB  . GLN A 1 302 ? 127.409 145.750 112.200 1.00 78.18  ? 289 GLN A CB  1 
ATOM   2082 C CG  . GLN A 1 302 ? 128.467 146.179 113.199 1.00 78.48  ? 289 GLN A CG  1 
ATOM   2083 C CD  . GLN A 1 302 ? 128.153 145.733 114.610 1.00 82.76  ? 289 GLN A CD  1 
ATOM   2084 O OE1 . GLN A 1 302 ? 127.117 145.119 114.864 1.00 83.47  ? 289 GLN A OE1 1 
ATOM   2085 N NE2 . GLN A 1 302 ? 129.049 146.040 115.540 1.00 87.56  ? 289 GLN A NE2 1 
ATOM   2086 N N   . VAL A 1 303 ? 125.464 146.392 109.713 1.00 77.69  ? 290 VAL A N   1 
ATOM   2087 C CA  . VAL A 1 303 ? 124.444 145.972 108.755 1.00 75.80  ? 290 VAL A CA  1 
ATOM   2088 C C   . VAL A 1 303 ? 124.992 146.045 107.335 1.00 73.32  ? 290 VAL A C   1 
ATOM   2089 O O   . VAL A 1 303 ? 124.823 145.117 106.536 1.00 74.37  ? 290 VAL A O   1 
ATOM   2090 C CB  . VAL A 1 303 ? 123.172 146.824 108.919 1.00 72.89  ? 290 VAL A CB  1 
ATOM   2091 C CG1 . VAL A 1 303 ? 122.148 146.458 107.860 1.00 73.74  ? 290 VAL A CG1 1 
ATOM   2092 C CG2 . VAL A 1 303 ? 122.588 146.639 110.310 1.00 73.07  ? 290 VAL A CG2 1 
ATOM   2093 N N   . PHE A 1 304 ? 125.657 147.151 106.997 1.00 71.96  ? 291 PHE A N   1 
ATOM   2094 C CA  . PHE A 1 304 ? 126.260 147.245 105.672 1.00 71.36  ? 291 PHE A CA  1 
ATOM   2095 C C   . PHE A 1 304 ? 127.384 146.232 105.491 1.00 77.19  ? 291 PHE A C   1 
ATOM   2096 O O   . PHE A 1 304 ? 127.539 145.668 104.402 1.00 80.96  ? 291 PHE A O   1 
ATOM   2097 C CB  . PHE A 1 304 ? 126.782 148.656 105.418 1.00 72.44  ? 291 PHE A CB  1 
ATOM   2098 C CG  . PHE A 1 304 ? 127.216 148.891 103.999 1.00 73.65  ? 291 PHE A CG  1 
ATOM   2099 C CD1 . PHE A 1 304 ? 128.494 148.554 103.584 1.00 76.05  ? 291 PHE A CD1 1 
ATOM   2100 C CD2 . PHE A 1 304 ? 126.345 149.445 103.078 1.00 75.60  ? 291 PHE A CD2 1 
ATOM   2101 C CE1 . PHE A 1 304 ? 128.896 148.764 102.285 1.00 80.02  ? 291 PHE A CE1 1 
ATOM   2102 C CE2 . PHE A 1 304 ? 126.743 149.661 101.775 1.00 77.70  ? 291 PHE A CE2 1 
ATOM   2103 C CZ  . PHE A 1 304 ? 128.022 149.319 101.378 1.00 80.96  ? 291 PHE A CZ  1 
ATOM   2104 N N   . ASP A 1 305 ? 128.183 145.993 106.535 1.00 77.39  ? 292 ASP A N   1 
ATOM   2105 C CA  . ASP A 1 305 ? 129.279 145.036 106.422 1.00 77.51  ? 292 ASP A CA  1 
ATOM   2106 C C   . ASP A 1 305 ? 128.754 143.644 106.109 1.00 76.62  ? 292 ASP A C   1 
ATOM   2107 O O   . ASP A 1 305 ? 129.314 142.934 105.266 1.00 76.12  ? 292 ASP A O   1 
ATOM   2108 C CB  . ASP A 1 305 ? 130.104 145.013 107.709 1.00 79.18  ? 292 ASP A CB  1 
ATOM   2109 C CG  . ASP A 1 305 ? 131.152 146.102 107.751 1.00 85.02  ? 292 ASP A CG  1 
ATOM   2110 O OD1 . ASP A 1 305 ? 131.341 146.789 106.725 1.00 85.40  ? 292 ASP A OD1 1 
ATOM   2111 O OD2 . ASP A 1 305 ? 131.789 146.268 108.813 1.00 85.22  ? 292 ASP A OD2 1 
ATOM   2112 N N   . GLU A 1 306 ? 127.673 143.239 106.777 1.00 76.03  ? 293 GLU A N   1 
ATOM   2113 C CA  . GLU A 1 306 ? 127.061 141.950 106.482 1.00 77.41  ? 293 GLU A CA  1 
ATOM   2114 C C   . GLU A 1 306 ? 126.374 141.948 105.122 1.00 74.45  ? 293 GLU A C   1 
ATOM   2115 O O   . GLU A 1 306 ? 126.334 140.905 104.460 1.00 74.79  ? 293 GLU A O   1 
ATOM   2116 C CB  . GLU A 1 306 ? 126.068 141.567 107.585 1.00 85.65  ? 293 GLU A CB  1 
ATOM   2117 C CG  . GLU A 1 306 ? 124.725 142.286 107.528 1.00 83.37  ? 293 GLU A CG  1 
ATOM   2118 C CD  . GLU A 1 306 ? 124.038 142.372 108.881 1.00 91.15  ? 293 GLU A CD  1 
ATOM   2119 O OE1 . GLU A 1 306 ? 124.713 142.163 109.912 1.00 91.70  ? 293 GLU A OE1 1 
ATOM   2120 O OE2 . GLU A 1 306 ? 122.820 142.649 108.915 1.00 93.53  ? 293 GLU A OE2 1 
ATOM   2121 N N   . VAL A 1 307 ? 125.826 143.088 104.691 1.00 76.40  ? 294 VAL A N   1 
ATOM   2122 C CA  . VAL A 1 307 ? 125.223 143.164 103.362 1.00 73.12  ? 294 VAL A CA  1 
ATOM   2123 C C   . VAL A 1 307 ? 126.296 143.110 102.282 1.00 64.37  ? 294 VAL A C   1 
ATOM   2124 O O   . VAL A 1 307 ? 126.177 142.364 101.303 1.00 61.78  ? 294 VAL A O   1 
ATOM   2125 C CB  . VAL A 1 307 ? 124.349 144.427 103.237 1.00 74.53  ? 294 VAL A CB  1 
ATOM   2126 C CG1 . VAL A 1 307 ? 124.019 144.708 101.780 1.00 66.41  ? 294 VAL A CG1 1 
ATOM   2127 C CG2 . VAL A 1 307 ? 123.069 144.263 104.041 1.00 76.43  ? 294 VAL A CG2 1 
ATOM   2128 N N   . ASP A 1 308 ? 127.367 143.882 102.450 1.00 64.03  ? 295 ASP A N   1 
ATOM   2129 C CA  . ASP A 1 308 ? 128.443 143.946 101.463 1.00 66.87  ? 295 ASP A CA  1 
ATOM   2130 C C   . ASP A 1 308 ? 129.364 142.753 101.679 1.00 69.83  ? 295 ASP A C   1 
ATOM   2131 O O   . ASP A 1 308 ? 130.301 142.796 102.476 1.00 73.13  ? 295 ASP A O   1 
ATOM   2132 C CB  . ASP A 1 308 ? 129.200 145.262 101.574 1.00 73.87  ? 295 ASP A CB  1 
ATOM   2133 C CG  . ASP A 1 308 ? 130.412 145.313 100.666 1.00 75.42  ? 295 ASP A CG  1 
ATOM   2134 O OD1 . ASP A 1 308 ? 130.236 145.248 99.432  1.00 75.76  ? 295 ASP A OD1 1 
ATOM   2135 O OD2 . ASP A 1 308 ? 131.541 145.419 101.186 1.00 74.79  ? 295 ASP A OD2 1 
ATOM   2136 N N   . THR A 1 309 ? 129.096 141.671 100.947 1.00 68.24  ? 296 THR A N   1 
ATOM   2137 C CA  . THR A 1 309 ? 129.873 140.450 101.127 1.00 68.61  ? 296 THR A CA  1 
ATOM   2138 C C   . THR A 1 309 ? 131.272 140.571 100.536 1.00 71.67  ? 296 THR A C   1 
ATOM   2139 O O   . THR A 1 309 ? 132.206 139.929 101.029 1.00 71.37  ? 296 THR A O   1 
ATOM   2140 C CB  . THR A 1 309 ? 129.136 139.267 100.501 1.00 61.70  ? 296 THR A CB  1 
ATOM   2141 O OG1 . THR A 1 309 ? 128.927 139.522 99.108  1.00 65.28  ? 296 THR A OG1 1 
ATOM   2142 C CG2 . THR A 1 309 ? 127.789 139.063 101.177 1.00 60.67  ? 296 THR A CG2 1 
ATOM   2143 N N   . ASP A 1 310 ? 131.443 141.389 99.493  1.00 72.08  ? 297 ASP A N   1 
ATOM   2144 C CA  . ASP A 1 310 ? 132.742 141.522 98.838  1.00 72.38  ? 297 ASP A CA  1 
ATOM   2145 C C   . ASP A 1 310 ? 133.794 142.149 99.743  1.00 76.20  ? 297 ASP A C   1 
ATOM   2146 O O   . ASP A 1 310 ? 134.989 142.033 99.450  1.00 76.39  ? 297 ASP A O   1 
ATOM   2147 C CB  . ASP A 1 310 ? 132.613 142.368 97.567  1.00 70.21  ? 297 ASP A CB  1 
ATOM   2148 C CG  . ASP A 1 310 ? 131.753 141.711 96.510  1.00 71.39  ? 297 ASP A CG  1 
ATOM   2149 O OD1 . ASP A 1 310 ? 131.907 140.494 96.287  1.00 70.87  ? 297 ASP A OD1 1 
ATOM   2150 O OD2 . ASP A 1 310 ? 130.923 142.416 95.897  1.00 78.03  ? 297 ASP A OD2 1 
ATOM   2151 N N   . GLN A 1 311 ? 133.372 142.808 100.825 1.00 76.75  ? 298 GLN A N   1 
ATOM   2152 C CA  . GLN A 1 311 ? 134.227 143.609 101.701 1.00 77.60  ? 298 GLN A CA  1 
ATOM   2153 C C   . GLN A 1 311 ? 134.926 144.738 100.948 1.00 77.76  ? 298 GLN A C   1 
ATOM   2154 O O   . GLN A 1 311 ? 135.934 145.277 101.419 1.00 77.77  ? 298 GLN A O   1 
ATOM   2155 C CB  . GLN A 1 311 ? 135.258 142.739 102.434 1.00 79.84  ? 298 GLN A CB  1 
ATOM   2156 C CG  . GLN A 1 311 ? 134.731 141.387 102.906 1.00 81.22  ? 298 GLN A CG  1 
ATOM   2157 C CD  . GLN A 1 311 ? 133.561 141.493 103.871 1.00 80.71  ? 298 GLN A CD  1 
ATOM   2158 O OE1 . GLN A 1 311 ? 133.535 142.357 104.750 1.00 81.89  ? 298 GLN A OE1 1 
ATOM   2159 N NE2 . GLN A 1 311 ? 132.588 140.602 103.712 1.00 77.93  ? 298 GLN A NE2 1 
ATOM   2160 N N   . SER A 1 312 ? 134.394 145.115 99.787  1.00 75.26  ? 299 SER A N   1 
ATOM   2161 C CA  . SER A 1 312 ? 134.959 146.164 98.948  1.00 76.24  ? 299 SER A CA  1 
ATOM   2162 C C   . SER A 1 312 ? 134.379 147.539 99.244  1.00 85.13  ? 299 SER A C   1 
ATOM   2163 O O   . SER A 1 312 ? 134.858 148.531 98.686  1.00 87.21  ? 299 SER A O   1 
ATOM   2164 C CB  . SER A 1 312 ? 134.735 145.830 97.471  1.00 76.54  ? 299 SER A CB  1 
ATOM   2165 O OG  . SER A 1 312 ? 133.349 145.736 97.187  1.00 78.30  ? 299 SER A OG  1 
ATOM   2166 N N   . GLY A 1 313 ? 133.357 147.618 100.092 1.00 85.89  ? 300 GLY A N   1 
ATOM   2167 C CA  . GLY A 1 313 ? 132.743 148.874 100.454 1.00 84.34  ? 300 GLY A CA  1 
ATOM   2168 C C   . GLY A 1 313 ? 131.709 149.392 99.482  1.00 85.70  ? 300 GLY A C   1 
ATOM   2169 O O   . GLY A 1 313 ? 131.070 150.410 99.774  1.00 87.60  ? 300 GLY A O   1 
ATOM   2170 N N   . VAL A 1 314 ? 131.497 148.718 98.354  1.00 85.72  ? 301 VAL A N   1 
ATOM   2171 C CA  . VAL A 1 314 ? 130.527 149.144 97.354  1.00 84.47  ? 301 VAL A CA  1 
ATOM   2172 C C   . VAL A 1 314 ? 129.598 147.978 97.049  1.00 82.27  ? 301 VAL A C   1 
ATOM   2173 O O   . VAL A 1 314 ? 130.031 146.821 96.993  1.00 79.42  ? 301 VAL A O   1 
ATOM   2174 C CB  . VAL A 1 314 ? 131.217 149.661 96.070  1.00 86.61  ? 301 VAL A CB  1 
ATOM   2175 C CG1 . VAL A 1 314 ? 132.057 148.569 95.418  1.00 86.54  ? 301 VAL A CG1 1 
ATOM   2176 C CG2 . VAL A 1 314 ? 130.188 150.219 95.095  1.00 88.75  ? 301 VAL A CG2 1 
ATOM   2177 N N   . LEU A 1 315 ? 128.315 148.280 96.875  1.00 78.74  ? 302 LEU A N   1 
ATOM   2178 C CA  . LEU A 1 315 ? 127.299 147.270 96.622  1.00 74.91  ? 302 LEU A CA  1 
ATOM   2179 C C   . LEU A 1 315 ? 127.076 147.119 95.124  1.00 79.68  ? 302 LEU A C   1 
ATOM   2180 O O   . LEU A 1 315 ? 126.883 148.112 94.415  1.00 82.00  ? 302 LEU A O   1 
ATOM   2181 C CB  . LEU A 1 315 ? 125.980 147.630 97.307  1.00 69.01  ? 302 LEU A CB  1 
ATOM   2182 C CG  . LEU A 1 315 ? 126.027 147.914 98.807  1.00 70.48  ? 302 LEU A CG  1 
ATOM   2183 C CD1 . LEU A 1 315 ? 124.658 148.331 99.316  1.00 69.77  ? 302 LEU A CD1 1 
ATOM   2184 C CD2 . LEU A 1 315 ? 126.537 146.708 99.573  1.00 75.07  ? 302 LEU A CD2 1 
ATOM   2185 N N   . SER A 1 316 ? 127.105 145.877 94.651  1.00 78.24  ? 303 SER A N   1 
ATOM   2186 C CA  . SER A 1 316 ? 126.755 145.584 93.273  1.00 73.16  ? 303 SER A CA  1 
ATOM   2187 C C   . SER A 1 316 ? 125.236 145.517 93.138  1.00 71.79  ? 303 SER A C   1 
ATOM   2188 O O   . SER A 1 316 ? 124.490 145.746 94.093  1.00 71.42  ? 303 SER A O   1 
ATOM   2189 C CB  . SER A 1 316 ? 127.417 144.283 92.825  1.00 68.43  ? 303 SER A CB  1 
ATOM   2190 O OG  . SER A 1 316 ? 128.822 144.346 92.996  1.00 66.97  ? 303 SER A OG  1 
ATOM   2191 N N   . ASP A 1 317 ? 124.766 145.201 91.931  1.00 72.34  ? 304 ASP A N   1 
ATOM   2192 C CA  . ASP A 1 317 ? 123.327 145.134 91.700  1.00 75.16  ? 304 ASP A CA  1 
ATOM   2193 C C   . ASP A 1 317 ? 122.678 144.006 92.494  1.00 72.69  ? 304 ASP A C   1 
ATOM   2194 O O   . ASP A 1 317 ? 121.490 144.084 92.823  1.00 72.17  ? 304 ASP A O   1 
ATOM   2195 C CB  . ASP A 1 317 ? 123.043 144.969 90.208  1.00 83.49  ? 304 ASP A CB  1 
ATOM   2196 C CG  . ASP A 1 317 ? 121.737 145.614 89.790  1.00 90.42  ? 304 ASP A CG  1 
ATOM   2197 O OD1 . ASP A 1 317 ? 120.816 145.692 90.629  1.00 85.70  ? 304 ASP A OD1 1 
ATOM   2198 O OD2 . ASP A 1 317 ? 121.635 146.050 88.625  1.00 95.19  ? 304 ASP A OD2 1 
ATOM   2199 N N   . ARG A 1 318 ? 123.432 142.950 92.803  1.00 72.51  ? 305 ARG A N   1 
ATOM   2200 C CA  . ARG A 1 318 ? 122.858 141.809 93.510  1.00 68.12  ? 305 ARG A CA  1 
ATOM   2201 C C   . ARG A 1 318 ? 122.739 142.048 95.011  1.00 68.51  ? 305 ARG A C   1 
ATOM   2202 O O   . ARG A 1 318 ? 121.838 141.492 95.648  1.00 70.98  ? 305 ARG A O   1 
ATOM   2203 C CB  . ARG A 1 318 ? 123.687 140.554 93.237  1.00 64.36  ? 305 ARG A CB  1 
ATOM   2204 C CG  . ARG A 1 318 ? 125.174 140.718 93.489  1.00 64.91  ? 305 ARG A CG  1 
ATOM   2205 C CD  . ARG A 1 318 ? 125.960 139.620 92.793  1.00 61.91  ? 305 ARG A CD  1 
ATOM   2206 N NE  . ARG A 1 318 ? 125.620 139.534 91.377  1.00 61.71  ? 305 ARG A NE  1 
ATOM   2207 C CZ  . ARG A 1 318 ? 126.185 138.699 90.516  1.00 58.66  ? 305 ARG A CZ  1 
ATOM   2208 N NH1 . ARG A 1 318 ? 127.137 137.861 90.889  1.00 61.29  ? 305 ARG A NH1 1 
ATOM   2209 N NH2 . ARG A 1 318 ? 125.786 138.707 89.247  1.00 54.46  ? 305 ARG A NH2 1 
ATOM   2210 N N   . GLU A 1 319 ? 123.628 142.852 95.595  1.00 63.00  ? 306 GLU A N   1 
ATOM   2211 C CA  . GLU A 1 319 ? 123.574 143.106 97.030  1.00 58.81  ? 306 GLU A CA  1 
ATOM   2212 C C   . GLU A 1 319 ? 122.470 144.085 97.408  1.00 66.16  ? 306 GLU A C   1 
ATOM   2213 O O   . GLU A 1 319 ? 121.985 144.050 98.549  1.00 71.31  ? 306 GLU A O   1 
ATOM   2214 C CB  . GLU A 1 319 ? 124.936 143.607 97.511  1.00 61.37  ? 306 GLU A CB  1 
ATOM   2215 C CG  . GLU A 1 319 ? 126.025 142.547 97.386  1.00 61.33  ? 306 GLU A CG  1 
ATOM   2216 C CD  . GLU A 1 319 ? 127.427 143.116 97.409  1.00 63.37  ? 306 GLU A CD  1 
ATOM   2217 O OE1 . GLU A 1 319 ? 127.587 144.311 97.725  1.00 68.17  ? 306 GLU A OE1 1 
ATOM   2218 O OE2 . GLU A 1 319 ? 128.375 142.364 97.106  1.00 61.08  ? 306 GLU A OE2 1 
ATOM   2219 N N   . ILE A 1 320 ? 122.054 144.945 96.475  1.00 70.47  ? 307 ILE A N   1 
ATOM   2220 C CA  . ILE A 1 320 ? 120.893 145.794 96.717  1.00 70.93  ? 307 ILE A CA  1 
ATOM   2221 C C   . ILE A 1 320 ? 119.650 144.942 96.916  1.00 71.87  ? 307 ILE A C   1 
ATOM   2222 O O   . ILE A 1 320 ? 118.740 145.325 97.656  1.00 75.21  ? 307 ILE A O   1 
ATOM   2223 C CB  . ILE A 1 320 ? 120.714 146.805 95.567  1.00 70.08  ? 307 ILE A CB  1 
ATOM   2224 C CG1 . ILE A 1 320 ? 122.036 147.510 95.269  1.00 66.42  ? 307 ILE A CG1 1 
ATOM   2225 C CG2 . ILE A 1 320 ? 119.660 147.836 95.930  1.00 68.61  ? 307 ILE A CG2 1 
ATOM   2226 C CD1 . ILE A 1 320 ? 122.511 148.387 96.395  1.00 66.11  ? 307 ILE A CD1 1 
ATOM   2227 N N   . ARG A 1 321 ? 119.593 143.773 96.273  1.00 69.26  ? 308 ARG A N   1 
ATOM   2228 C CA  . ARG A 1 321 ? 118.483 142.851 96.492  1.00 66.95  ? 308 ARG A CA  1 
ATOM   2229 C C   . ARG A 1 321 ? 118.399 142.432 97.955  1.00 70.78  ? 308 ARG A C   1 
ATOM   2230 O O   . ARG A 1 321 ? 117.331 142.500 98.575  1.00 73.64  ? 308 ARG A O   1 
ATOM   2231 C CB  . ARG A 1 321 ? 118.648 141.625 95.593  1.00 67.06  ? 308 ARG A CB  1 
ATOM   2232 C CG  . ARG A 1 321 ? 117.396 140.783 95.421  1.00 74.45  ? 308 ARG A CG  1 
ATOM   2233 C CD  . ARG A 1 321 ? 116.585 141.270 94.233  1.00 74.60  ? 308 ARG A CD  1 
ATOM   2234 N NE  . ARG A 1 321 ? 115.253 140.683 94.182  1.00 77.35  ? 308 ARG A NE  1 
ATOM   2235 C CZ  . ARG A 1 321 ? 114.211 141.119 94.876  1.00 78.57  ? 308 ARG A CZ  1 
ATOM   2236 N NH1 . ARG A 1 321 ? 114.323 142.119 95.732  1.00 73.40  ? 308 ARG A NH1 1 
ATOM   2237 N NH2 . ARG A 1 321 ? 113.028 140.534 94.707  1.00 81.33  ? 308 ARG A NH2 1 
ATOM   2238 N N   . THR A 1 322 ? 119.526 141.991 98.523  1.00 69.62  ? 309 THR A N   1 
ATOM   2239 C CA  . THR A 1 322 ? 119.542 141.570 99.920  1.00 66.75  ? 309 THR A CA  1 
ATOM   2240 C C   . THR A 1 322 ? 119.230 142.736 100.850 1.00 69.78  ? 309 THR A C   1 
ATOM   2241 O O   . THR A 1 322 ? 118.473 142.585 101.818 1.00 71.88  ? 309 THR A O   1 
ATOM   2242 C CB  . THR A 1 322 ? 120.897 140.956 100.269 1.00 63.66  ? 309 THR A CB  1 
ATOM   2243 O OG1 . THR A 1 322 ? 121.191 139.890 99.357  1.00 66.33  ? 309 THR A OG1 1 
ATOM   2244 C CG2 . THR A 1 322 ? 120.886 140.410 101.686 1.00 67.83  ? 309 THR A CG2 1 
ATOM   2245 N N   . LEU A 1 323 ? 119.801 143.910 100.570 1.00 71.30  ? 310 LEU A N   1 
ATOM   2246 C CA  . LEU A 1 323 ? 119.519 145.073 101.407 1.00 71.62  ? 310 LEU A CA  1 
ATOM   2247 C C   . LEU A 1 323 ? 118.034 145.417 101.386 1.00 75.66  ? 310 LEU A C   1 
ATOM   2248 O O   . LEU A 1 323 ? 117.420 145.639 102.437 1.00 77.71  ? 310 LEU A O   1 
ATOM   2249 C CB  . LEU A 1 323 ? 120.353 146.270 100.952 1.00 70.27  ? 310 LEU A CB  1 
ATOM   2250 C CG  . LEU A 1 323 ? 120.079 147.570 101.712 1.00 73.86  ? 310 LEU A CG  1 
ATOM   2251 C CD1 . LEU A 1 323 ? 120.405 147.414 103.190 1.00 73.15  ? 310 LEU A CD1 1 
ATOM   2252 C CD2 . LEU A 1 323 ? 120.853 148.730 101.105 1.00 72.06  ? 310 LEU A CD2 1 
ATOM   2253 N N   . ALA A 1 324 ? 117.433 145.446 100.194 1.00 76.25  ? 311 ALA A N   1 
ATOM   2254 C CA  . ALA A 1 324 ? 116.021 145.785 100.075 1.00 75.74  ? 311 ALA A CA  1 
ATOM   2255 C C   . ALA A 1 324 ? 115.139 144.743 100.747 1.00 77.53  ? 311 ALA A C   1 
ATOM   2256 O O   . ALA A 1 324 ? 114.168 145.091 101.429 1.00 80.82  ? 311 ALA A O   1 
ATOM   2257 C CB  . ALA A 1 324 ? 115.641 145.937 98.603  1.00 76.94  ? 311 ALA A CB  1 
ATOM   2258 N N   . THR A 1 325 ? 115.455 143.458 100.569 1.00 76.90  ? 312 THR A N   1 
ATOM   2259 C CA  . THR A 1 325 ? 114.612 142.426 101.160 1.00 77.29  ? 312 THR A CA  1 
ATOM   2260 C C   . THR A 1 325 ? 114.716 142.424 102.679 1.00 74.73  ? 312 THR A C   1 
ATOM   2261 O O   . THR A 1 325 ? 113.723 142.149 103.361 1.00 76.21  ? 312 THR A O   1 
ATOM   2262 C CB  . THR A 1 325 ? 114.953 141.049 100.582 1.00 75.12  ? 312 THR A CB  1 
ATOM   2263 O OG1 . THR A 1 325 ? 113.919 140.119 100.926 1.00 75.00  ? 312 THR A OG1 1 
ATOM   2264 C CG2 . THR A 1 325 ? 116.271 140.530 101.116 1.00 69.30  ? 312 THR A CG2 1 
ATOM   2265 N N   . ARG A 1 326 ? 115.891 142.743 103.230 1.00 75.72  ? 313 ARG A N   1 
ATOM   2266 C CA  . ARG A 1 326 ? 115.989 142.896 104.676 1.00 78.13  ? 313 ARG A CA  1 
ATOM   2267 C C   . ARG A 1 326 ? 115.251 144.141 105.148 1.00 78.42  ? 313 ARG A C   1 
ATOM   2268 O O   . ARG A 1 326 ? 114.685 144.145 106.247 1.00 82.66  ? 313 ARG A O   1 
ATOM   2269 C CB  . ARG A 1 326 ? 117.456 142.935 105.104 1.00 76.72  ? 313 ARG A CB  1 
ATOM   2270 C CG  . ARG A 1 326 ? 118.151 141.585 105.002 1.00 74.38  ? 313 ARG A CG  1 
ATOM   2271 C CD  . ARG A 1 326 ? 119.646 141.689 105.255 1.00 74.85  ? 313 ARG A CD  1 
ATOM   2272 N NE  . ARG A 1 326 ? 120.301 140.391 105.146 1.00 75.69  ? 313 ARG A NE  1 
ATOM   2273 C CZ  . ARG A 1 326 ? 121.615 140.210 105.148 1.00 74.77  ? 313 ARG A CZ  1 
ATOM   2274 N NH1 . ARG A 1 326 ? 122.453 141.229 105.245 1.00 70.51  ? 313 ARG A NH1 1 
ATOM   2275 N NH2 . ARG A 1 326 ? 122.100 138.976 105.044 1.00 68.92  ? 313 ARG A NH2 1 
ATOM   2276 N N   . ILE A 1 327 ? 115.248 145.201 104.338 1.00 75.10  ? 314 ILE A N   1 
ATOM   2277 C CA  . ILE A 1 327 ? 114.488 146.398 104.681 1.00 75.59  ? 314 ILE A CA  1 
ATOM   2278 C C   . ILE A 1 327 ? 112.989 146.151 104.542 1.00 78.00  ? 314 ILE A C   1 
ATOM   2279 O O   . ILE A 1 327 ? 112.196 146.563 105.398 1.00 76.09  ? 314 ILE A O   1 
ATOM   2280 C CB  . ILE A 1 327 ? 114.951 147.582 103.814 1.00 73.18  ? 314 ILE A CB  1 
ATOM   2281 C CG1 . ILE A 1 327 ? 116.363 148.011 104.208 1.00 71.39  ? 314 ILE A CG1 1 
ATOM   2282 C CG2 . ILE A 1 327 ? 113.992 148.747 103.946 1.00 74.94  ? 314 ILE A CG2 1 
ATOM   2283 C CD1 . ILE A 1 327 ? 116.937 149.086 103.318 1.00 75.59  ? 314 ILE A CD1 1 
ATOM   2284 N N   . HIS A 1 328 ? 112.575 145.473 103.476 1.00 80.16  ? 315 HIS A N   1 
ATOM   2285 C CA  . HIS A 1 328 ? 111.163 145.359 103.145 1.00 83.92  ? 315 HIS A CA  1 
ATOM   2286 C C   . HIS A 1 328 ? 110.537 144.118 103.778 1.00 88.80  ? 315 HIS A C   1 
ATOM   2287 O O   . HIS A 1 328 ? 111.217 143.248 104.328 1.00 88.10  ? 315 HIS A O   1 
ATOM   2288 C CB  . HIS A 1 328 ? 110.969 145.328 101.629 1.00 82.68  ? 315 HIS A CB  1 
ATOM   2289 C CG  . HIS A 1 328 ? 111.360 146.600 100.945 1.00 84.09  ? 315 HIS A CG  1 
ATOM   2290 N ND1 . HIS A 1 328 ? 111.944 146.625 99.698  1.00 86.32  ? 315 HIS A ND1 1 
ATOM   2291 C CD2 . HIS A 1 328 ? 111.249 147.892 101.333 1.00 85.64  ? 315 HIS A CD2 1 
ATOM   2292 C CE1 . HIS A 1 328 ? 112.179 147.876 99.347  1.00 88.46  ? 315 HIS A CE1 1 
ATOM   2293 N NE2 . HIS A 1 328 ? 111.766 148.665 100.321 1.00 86.40  ? 315 HIS A NE2 1 
ATOM   2294 N N   . GLU A 1 329 ? 109.211 144.053 103.694 1.00 93.03  ? 316 GLU A N   1 
ATOM   2295 C CA  . GLU A 1 329 ? 108.422 142.948 104.215 1.00 90.93  ? 316 GLU A CA  1 
ATOM   2296 C C   . GLU A 1 329 ? 107.826 142.146 103.065 1.00 95.53  ? 316 GLU A C   1 
ATOM   2297 O O   . GLU A 1 329 ? 107.487 142.696 102.014 1.00 97.51  ? 316 GLU A O   1 
ATOM   2298 C CB  . GLU A 1 329 ? 107.304 143.461 105.127 1.00 90.17  ? 316 GLU A CB  1 
ATOM   2299 C CG  . GLU A 1 329 ? 107.794 144.310 106.286 1.00 97.11  ? 316 GLU A CG  1 
ATOM   2300 C CD  . GLU A 1 329 ? 106.850 145.450 106.606 1.00 104.81 ? 316 GLU A CD  1 
ATOM   2301 O OE1 . GLU A 1 329 ? 105.968 145.744 105.773 1.00 105.50 ? 316 GLU A OE1 1 
ATOM   2302 O OE2 . GLU A 1 329 ? 106.989 146.055 107.689 1.00 108.93 ? 316 GLU A OE2 1 
ATOM   2303 N N   . LEU A 1 330 ? 107.700 140.840 103.277 1.00 97.81  ? 317 LEU A N   1 
ATOM   2304 C CA  . LEU A 1 330 ? 107.200 139.960 102.231 1.00 101.76 ? 317 LEU A CA  1 
ATOM   2305 C C   . LEU A 1 330 ? 105.731 140.261 101.934 1.00 104.41 ? 317 LEU A C   1 
ATOM   2306 O O   . LEU A 1 330 ? 104.970 140.606 102.845 1.00 103.95 ? 317 LEU A O   1 
ATOM   2307 C CB  . LEU A 1 330 ? 107.352 138.496 102.644 1.00 100.98 ? 317 LEU A CB  1 
ATOM   2308 C CG  . LEU A 1 330 ? 108.678 137.782 102.357 1.00 98.77  ? 317 LEU A CG  1 
ATOM   2309 C CD1 . LEU A 1 330 ? 108.972 137.778 100.865 1.00 93.02  ? 317 LEU A CD1 1 
ATOM   2310 C CD2 . LEU A 1 330 ? 109.838 138.387 103.137 1.00 91.35  ? 317 LEU A CD2 1 
ATOM   2311 N N   . PRO A 1 331 ? 105.299 140.141 100.666 1.00 104.31 ? 318 PRO A N   1 
ATOM   2312 C CA  . PRO A 1 331 ? 106.091 139.864 99.453  1.00 98.76  ? 318 PRO A CA  1 
ATOM   2313 C C   . PRO A 1 331 ? 106.784 141.117 98.932  1.00 100.56 ? 318 PRO A C   1 
ATOM   2314 O O   . PRO A 1 331 ? 106.505 142.216 99.402  1.00 100.43 ? 318 PRO A O   1 
ATOM   2315 C CB  . PRO A 1 331 ? 105.043 139.341 98.451  1.00 95.94  ? 318 PRO A CB  1 
ATOM   2316 C CG  . PRO A 1 331 ? 103.780 139.105 99.248  1.00 98.65  ? 318 PRO A CG  1 
ATOM   2317 C CD  . PRO A 1 331 ? 103.858 140.081 100.380 1.00 101.24 ? 318 PRO A CD  1 
ATOM   2318 N N   . LEU A 1 332 ? 107.688 140.993 97.963  1.00 100.22 ? 319 LEU A N   1 
ATOM   2319 C CA  . LEU A 1 332 ? 108.466 142.120 97.464  1.00 97.98  ? 319 LEU A CA  1 
ATOM   2320 C C   . LEU A 1 332 ? 108.158 142.353 95.990  1.00 99.53  ? 319 LEU A C   1 
ATOM   2321 O O   . LEU A 1 332 ? 108.318 141.446 95.165  1.00 101.22 ? 319 LEU A O   1 
ATOM   2322 C CB  . LEU A 1 332 ? 109.959 141.874 97.675  1.00 89.13  ? 319 LEU A CB  1 
ATOM   2323 C CG  . LEU A 1 332 ? 110.870 143.100 97.621  1.00 88.86  ? 319 LEU A CG  1 
ATOM   2324 C CD1 . LEU A 1 332 ? 112.063 142.932 98.552  1.00 85.03  ? 319 LEU A CD1 1 
ATOM   2325 C CD2 . LEU A 1 332 ? 111.342 143.330 96.201  1.00 89.37  ? 319 LEU A CD2 1 
ATOM   2326 N N   . SER A 1 333 ? 107.742 143.572 95.662  1.00 99.02  ? 320 SER A N   1 
ATOM   2327 C CA  . SER A 1 333 ? 107.486 143.978 94.289  1.00 102.99 ? 320 SER A CA  1 
ATOM   2328 C C   . SER A 1 333 ? 108.638 144.829 93.769  1.00 102.52 ? 320 SER A C   1 
ATOM   2329 O O   . SER A 1 333 ? 109.410 145.411 94.535  1.00 102.88 ? 320 SER A O   1 
ATOM   2330 C CB  . SER A 1 333 ? 106.170 144.755 94.183  1.00 107.28 ? 320 SER A CB  1 
ATOM   2331 O OG  . SER A 1 333 ? 106.256 146.010 94.839  1.00 104.46 ? 320 SER A OG  1 
ATOM   2332 N N   . LEU A 1 334 ? 108.740 144.898 92.440  1.00 101.08 ? 321 LEU A N   1 
ATOM   2333 C CA  . LEU A 1 334 ? 109.811 145.665 91.813  1.00 100.16 ? 321 LEU A CA  1 
ATOM   2334 C C   . LEU A 1 334 ? 109.675 147.158 92.088  1.00 99.15  ? 321 LEU A C   1 
ATOM   2335 O O   . LEU A 1 334 ? 110.673 147.889 92.039  1.00 98.11  ? 321 LEU A O   1 
ATOM   2336 C CB  . LEU A 1 334 ? 109.832 145.409 90.306  1.00 103.44 ? 321 LEU A CB  1 
ATOM   2337 C CG  . LEU A 1 334 ? 108.789 146.111 89.432  1.00 103.23 ? 321 LEU A CG  1 
ATOM   2338 C CD1 . LEU A 1 334 ? 109.204 146.027 87.975  1.00 102.21 ? 321 LEU A CD1 1 
ATOM   2339 C CD2 . LEU A 1 334 ? 107.395 145.526 89.620  1.00 104.01 ? 321 LEU A CD2 1 
ATOM   2340 N N   . GLN A 1 335 ? 108.457 147.627 92.371  1.00 99.30  ? 322 GLN A N   1 
ATOM   2341 C CA  . GLN A 1 335 ? 108.248 149.051 92.613  1.00 101.62 ? 322 GLN A CA  1 
ATOM   2342 C C   . GLN A 1 335 ? 109.039 149.528 93.821  1.00 102.11 ? 322 GLN A C   1 
ATOM   2343 O O   . GLN A 1 335 ? 109.632 150.613 93.794  1.00 103.52 ? 322 GLN A O   1 
ATOM   2344 C CB  . GLN A 1 335 ? 106.761 149.343 92.809  1.00 103.20 ? 322 GLN A CB  1 
ATOM   2345 C CG  . GLN A 1 335 ? 105.921 149.131 91.570  1.00 104.91 ? 322 GLN A CG  1 
ATOM   2346 C CD  . GLN A 1 335 ? 106.445 149.905 90.378  1.00 105.70 ? 322 GLN A CD  1 
ATOM   2347 O OE1 . GLN A 1 335 ? 106.585 149.358 89.285  1.00 107.02 ? 322 GLN A OE1 1 
ATOM   2348 N NE2 . GLN A 1 335 ? 106.736 151.185 90.582  1.00 103.60 ? 322 GLN A NE2 1 
ATOM   2349 N N   . ASP A 1 336 ? 109.050 148.735 94.894  1.00 102.52 ? 323 ASP A N   1 
ATOM   2350 C CA  . ASP A 1 336 ? 109.783 149.125 96.093  1.00 102.71 ? 323 ASP A CA  1 
ATOM   2351 C C   . ASP A 1 336 ? 111.278 149.219 95.822  1.00 101.27 ? 323 ASP A C   1 
ATOM   2352 O O   . ASP A 1 336 ? 111.946 150.140 96.305  1.00 104.36 ? 323 ASP A O   1 
ATOM   2353 C CB  . ASP A 1 336 ? 109.498 148.140 97.227  1.00 103.97 ? 323 ASP A CB  1 
ATOM   2354 C CG  . ASP A 1 336 ? 108.128 148.344 97.842  1.00 105.34 ? 323 ASP A CG  1 
ATOM   2355 O OD1 . ASP A 1 336 ? 107.648 149.498 97.853  1.00 111.99 ? 323 ASP A OD1 1 
ATOM   2356 O OD2 . ASP A 1 336 ? 107.529 147.354 98.316  1.00 101.65 ? 323 ASP A OD2 1 
ATOM   2357 N N   . LEU A 1 337 ? 111.825 148.267 95.062  1.00 96.86  ? 324 LEU A N   1 
ATOM   2358 C CA  . LEU A 1 337 ? 113.245 148.306 94.725  1.00 97.27  ? 324 LEU A CA  1 
ATOM   2359 C C   . LEU A 1 337 ? 113.574 149.507 93.844  1.00 102.04 ? 324 LEU A C   1 
ATOM   2360 O O   . LEU A 1 337 ? 114.617 150.152 94.014  1.00 99.77  ? 324 LEU A O   1 
ATOM   2361 C CB  . LEU A 1 337 ? 113.656 147.002 94.043  1.00 91.03  ? 324 LEU A CB  1 
ATOM   2362 C CG  . LEU A 1 337 ? 115.123 146.876 93.637  1.00 86.22  ? 324 LEU A CG  1 
ATOM   2363 C CD1 . LEU A 1 337 ? 116.032 147.025 94.844  1.00 83.73  ? 324 LEU A CD1 1 
ATOM   2364 C CD2 . LEU A 1 337 ? 115.374 145.554 92.934  1.00 83.93  ? 324 LEU A CD2 1 
ATOM   2365 N N   . THR A 1 338 ? 112.699 149.816 92.882  1.00 104.24 ? 325 THR A N   1 
ATOM   2366 C CA  . THR A 1 338 ? 112.916 151.002 92.060  1.00 104.30 ? 325 THR A CA  1 
ATOM   2367 C C   . THR A 1 338 ? 112.874 152.266 92.906  1.00 103.93 ? 325 THR A C   1 
ATOM   2368 O O   . THR A 1 338 ? 113.666 153.185 92.693  1.00 103.48 ? 325 THR A O   1 
ATOM   2369 C CB  . THR A 1 338 ? 111.884 151.076 90.932  1.00 106.00 ? 325 THR A CB  1 
ATOM   2370 O OG1 . THR A 1 338 ? 110.564 150.947 91.472  1.00 107.21 ? 325 THR A OG1 1 
ATOM   2371 C CG2 . THR A 1 338 ? 112.127 149.971 89.917  1.00 102.99 ? 325 THR A CG2 1 
ATOM   2372 N N   . GLY A 1 339 ? 111.955 152.327 93.875  1.00 106.61 ? 326 GLY A N   1 
ATOM   2373 C CA  . GLY A 1 339 ? 111.901 153.473 94.769  1.00 106.84 ? 326 GLY A CA  1 
ATOM   2374 C C   . GLY A 1 339 ? 113.112 153.590 95.672  1.00 104.42 ? 326 GLY A C   1 
ATOM   2375 O O   . GLY A 1 339 ? 113.558 154.698 95.980  1.00 107.08 ? 326 GLY A O   1 
ATOM   2376 N N   . LEU A 1 340 ? 113.651 152.455 96.121  1.00 99.64  ? 327 LEU A N   1 
ATOM   2377 C CA  . LEU A 1 340 ? 114.904 152.474 96.870  1.00 99.34  ? 327 LEU A CA  1 
ATOM   2378 C C   . LEU A 1 340 ? 116.033 153.032 96.011  1.00 102.25 ? 327 LEU A C   1 
ATOM   2379 O O   . LEU A 1 340 ? 116.819 153.876 96.459  1.00 104.26 ? 327 LEU A O   1 
ATOM   2380 C CB  . LEU A 1 340 ? 115.246 151.068 97.365  1.00 96.62  ? 327 LEU A CB  1 
ATOM   2381 C CG  . LEU A 1 340 ? 116.617 150.869 98.016  1.00 89.66  ? 327 LEU A CG  1 
ATOM   2382 C CD1 . LEU A 1 340 ? 116.685 151.578 99.356  1.00 89.43  ? 327 LEU A CD1 1 
ATOM   2383 C CD2 . LEU A 1 340 ? 116.926 149.390 98.181  1.00 90.54  ? 327 LEU A CD2 1 
ATOM   2384 N N   . GLU A 1 341 ? 116.111 152.585 94.755  1.00 99.67  ? 328 GLU A N   1 
ATOM   2385 C CA  . GLU A 1 341 ? 117.121 153.117 93.844  1.00 100.21 ? 328 GLU A CA  1 
ATOM   2386 C C   . GLU A 1 341 ? 116.907 154.608 93.587  1.00 106.04 ? 328 GLU A C   1 
ATOM   2387 O O   . GLU A 1 341 ? 117.874 155.383 93.538  1.00 107.79 ? 328 GLU A O   1 
ATOM   2388 C CB  . GLU A 1 341 ? 117.097 152.311 92.539  1.00 98.93  ? 328 GLU A CB  1 
ATOM   2389 C CG  . GLU A 1 341 ? 117.379 150.831 92.777  1.00 94.24  ? 328 GLU A CG  1 
ATOM   2390 C CD  . GLU A 1 341 ? 116.909 149.907 91.654  1.00 92.73  ? 328 GLU A CD  1 
ATOM   2391 O OE1 . GLU A 1 341 ? 116.978 148.677 91.866  1.00 92.59  ? 328 GLU A OE1 1 
ATOM   2392 O OE2 . GLU A 1 341 ? 116.484 150.384 90.583  1.00 95.56  ? 328 GLU A OE2 1 
ATOM   2393 N N   . HIS A 1 342 ? 115.647 155.033 93.477  1.00 105.84 ? 329 HIS A N   1 
ATOM   2394 C CA  . HIS A 1 342 ? 115.335 156.436 93.232  1.00 104.54 ? 329 HIS A CA  1 
ATOM   2395 C C   . HIS A 1 342 ? 115.704 157.309 94.424  1.00 107.20 ? 329 HIS A C   1 
ATOM   2396 O O   . HIS A 1 342 ? 116.239 158.407 94.250  1.00 109.19 ? 329 HIS A O   1 
ATOM   2397 C CB  . HIS A 1 342 ? 113.854 156.583 92.895  1.00 101.78 ? 329 HIS A CB  1 
ATOM   2398 C CG  . HIS A 1 342 ? 113.465 155.959 91.591  1.00 106.99 ? 329 HIS A CG  1 
ATOM   2399 N ND1 . HIS A 1 342 ? 114.382 155.651 90.609  1.00 107.66 ? 329 HIS A ND1 1 
ATOM   2400 C CD2 . HIS A 1 342 ? 112.257 155.586 91.108  1.00 110.24 ? 329 HIS A CD2 1 
ATOM   2401 C CE1 . HIS A 1 342 ? 113.755 155.118 89.576  1.00 109.83 ? 329 HIS A CE1 1 
ATOM   2402 N NE2 . HIS A 1 342 ? 112.464 155.067 89.853  1.00 108.90 ? 329 HIS A NE2 1 
ATOM   2403 N N   . MET A 1 343 ? 115.410 156.854 95.642  1.00 106.33 ? 330 MET A N   1 
ATOM   2404 C CA  . MET A 1 343 ? 115.803 157.632 96.809  1.00 105.59 ? 330 MET A CA  1 
ATOM   2405 C C   . MET A 1 343 ? 117.318 157.656 96.962  1.00 105.27 ? 330 MET A C   1 
ATOM   2406 O O   . MET A 1 343 ? 117.877 158.670 97.396  1.00 109.42 ? 330 MET A O   1 
ATOM   2407 C CB  . MET A 1 343 ? 115.121 157.097 98.071  1.00 102.90 ? 330 MET A CB  1 
ATOM   2408 C CG  . MET A 1 343 ? 115.708 155.826 98.650  1.00 104.95 ? 330 MET A CG  1 
ATOM   2409 S SD  . MET A 1 343 ? 114.772 155.253 100.080 1.00 120.62 ? 330 MET A SD  1 
ATOM   2410 C CE  . MET A 1 343 ? 113.179 154.929 99.329  1.00 107.63 ? 330 MET A CE  1 
ATOM   2411 N N   . LEU A 1 344 ? 118.001 156.574 96.575  1.00 101.91 ? 331 LEU A N   1 
ATOM   2412 C CA  . LEU A 1 344 ? 119.460 156.585 96.588  1.00 102.96 ? 331 LEU A CA  1 
ATOM   2413 C C   . LEU A 1 344 ? 120.012 157.653 95.649  1.00 108.81 ? 331 LEU A C   1 
ATOM   2414 O O   . LEU A 1 344 ? 120.896 158.433 96.027  1.00 110.58 ? 331 LEU A O   1 
ATOM   2415 C CB  . LEU A 1 344 ? 119.998 155.203 96.214  1.00 103.56 ? 331 LEU A CB  1 
ATOM   2416 C CG  . LEU A 1 344 ? 120.455 154.294 97.359  1.00 95.95  ? 331 LEU A CG  1 
ATOM   2417 C CD1 . LEU A 1 344 ? 120.836 152.907 96.846  1.00 81.34  ? 331 LEU A CD1 1 
ATOM   2418 C CD2 . LEU A 1 344 ? 121.622 154.927 98.102  1.00 96.49  ? 331 LEU A CD2 1 
ATOM   2419 N N   . ILE A 1 345 ? 119.494 157.715 94.418  1.00 110.84 ? 332 ILE A N   1 
ATOM   2420 C CA  . ILE A 1 345 ? 120.013 158.707 93.476  1.00 112.66 ? 332 ILE A CA  1 
ATOM   2421 C C   . ILE A 1 345 ? 119.616 160.118 93.903  1.00 109.56 ? 332 ILE A C   1 
ATOM   2422 O O   . ILE A 1 345 ? 120.389 161.068 93.729  1.00 107.81 ? 332 ILE A O   1 
ATOM   2423 C CB  . ILE A 1 345 ? 119.579 158.403 92.028  1.00 116.63 ? 332 ILE A CB  1 
ATOM   2424 C CG1 . ILE A 1 345 ? 118.061 158.420 91.863  1.00 113.49 ? 332 ILE A CG1 1 
ATOM   2425 C CG2 . ILE A 1 345 ? 120.156 157.084 91.569  1.00 115.51 ? 332 ILE A CG2 1 
ATOM   2426 C CD1 . ILE A 1 345 ? 117.606 158.238 90.428  1.00 110.18 ? 332 ILE A CD1 1 
ATOM   2427 N N   . ASN A 1 346 ? 118.415 160.284 94.467  1.00 107.74 ? 333 ASN A N   1 
ATOM   2428 C CA  . ASN A 1 346 ? 118.014 161.597 94.962  1.00 107.06 ? 333 ASN A CA  1 
ATOM   2429 C C   . ASN A 1 346 ? 118.948 162.072 96.067  1.00 108.41 ? 333 ASN A C   1 
ATOM   2430 O O   . ASN A 1 346 ? 119.367 163.235 96.079  1.00 110.43 ? 333 ASN A O   1 
ATOM   2431 C CB  . ASN A 1 346 ? 116.569 161.559 95.465  1.00 106.76 ? 333 ASN A CB  1 
ATOM   2432 C CG  . ASN A 1 346 ? 115.554 161.540 94.336  1.00 107.02 ? 333 ASN A CG  1 
ATOM   2433 O OD1 . ASN A 1 346 ? 114.621 160.736 94.335  1.00 105.45 ? 333 ASN A OD1 1 
ATOM   2434 N ND2 . ASN A 1 346 ? 115.730 162.432 93.369  1.00 106.81 ? 333 ASN A ND2 1 
ATOM   2435 N N   . CYS A 1 347 ? 119.296 161.179 96.998  1.00 108.07 ? 334 CYS A N   1 
ATOM   2436 C CA  . CYS A 1 347 ? 120.215 161.542 98.071  1.00 107.24 ? 334 CYS A CA  1 
ATOM   2437 C C   . CYS A 1 347 ? 121.606 161.843 97.532  1.00 110.34 ? 334 CYS A C   1 
ATOM   2438 O O   . CYS A 1 347 ? 122.276 162.766 98.012  1.00 112.31 ? 334 CYS A O   1 
ATOM   2439 C CB  . CYS A 1 347 ? 120.276 160.428 99.112  1.00 104.29 ? 334 CYS A CB  1 
ATOM   2440 S SG  . CYS A 1 347 ? 121.488 160.718 100.417 1.00 110.58 ? 334 CYS A SG  1 
ATOM   2441 N N   . SER A 1 348 ? 122.066 161.069 96.546  1.00 110.64 ? 335 SER A N   1 
ATOM   2442 C CA  . SER A 1 348 ? 123.385 161.323 95.976  1.00 112.62 ? 335 SER A CA  1 
ATOM   2443 C C   . SER A 1 348 ? 123.432 162.671 95.269  1.00 117.77 ? 335 SER A C   1 
ATOM   2444 O O   . SER A 1 348 ? 124.437 163.386 95.350  1.00 120.18 ? 335 SER A O   1 
ATOM   2445 C CB  . SER A 1 348 ? 123.769 160.203 95.012  1.00 108.04 ? 335 SER A CB  1 
ATOM   2446 O OG  . SER A 1 348 ? 125.072 160.412 94.495  1.00 104.97 ? 335 SER A OG  1 
ATOM   2447 N N   . LYS A 1 349 ? 122.358 163.033 94.566  1.00 117.65 ? 336 LYS A N   1 
ATOM   2448 C CA  . LYS A 1 349 ? 122.349 164.290 93.826  1.00 118.07 ? 336 LYS A CA  1 
ATOM   2449 C C   . LYS A 1 349 ? 122.154 165.493 94.743  1.00 118.77 ? 336 LYS A C   1 
ATOM   2450 O O   . LYS A 1 349 ? 122.743 166.553 94.506  1.00 120.58 ? 336 LYS A O   1 
ATOM   2451 C CB  . LYS A 1 349 ? 121.271 164.249 92.743  1.00 119.51 ? 336 LYS A CB  1 
ATOM   2452 C CG  . LYS A 1 349 ? 121.571 163.257 91.626  1.00 122.23 ? 336 LYS A CG  1 
ATOM   2453 C CD  . LYS A 1 349 ? 120.453 163.203 90.598  1.00 122.88 ? 336 LYS A CD  1 
ATOM   2454 C CE  . LYS A 1 349 ? 120.742 162.165 89.524  1.00 125.62 ? 336 LYS A CE  1 
ATOM   2455 N NZ  . LYS A 1 349 ? 119.662 162.102 88.501  1.00 123.36 ? 336 LYS A NZ  1 
ATOM   2456 N N   . MET A 1 350 ? 121.335 165.359 95.792  1.00 118.74 ? 337 MET A N   1 
ATOM   2457 C CA  . MET A 1 350 ? 121.092 166.500 96.672  1.00 118.14 ? 337 MET A CA  1 
ATOM   2458 C C   . MET A 1 350 ? 122.299 166.807 97.551  1.00 119.54 ? 337 MET A C   1 
ATOM   2459 O O   . MET A 1 350 ? 122.535 167.972 97.889  1.00 121.14 ? 337 MET A O   1 
ATOM   2460 C CB  . MET A 1 350 ? 119.847 166.258 97.532  1.00 116.40 ? 337 MET A CB  1 
ATOM   2461 C CG  . MET A 1 350 ? 119.953 165.118 98.540  1.00 115.06 ? 337 MET A CG  1 
ATOM   2462 S SD  . MET A 1 350 ? 120.725 165.567 100.107 1.00 115.17 ? 337 MET A SD  1 
ATOM   2463 C CE  . MET A 1 350 ? 119.689 166.936 100.610 1.00 118.86 ? 337 MET A CE  1 
ATOM   2464 N N   . LEU A 1 351 ? 123.062 165.786 97.938  1.00 120.41 ? 338 LEU A N   1 
ATOM   2465 C CA  . LEU A 1 351 ? 124.239 165.980 98.769  1.00 123.98 ? 338 LEU A CA  1 
ATOM   2466 C C   . LEU A 1 351 ? 125.480 165.971 97.897  1.00 128.13 ? 338 LEU A C   1 
ATOM   2467 O O   . LEU A 1 351 ? 125.747 164.957 97.232  1.00 127.85 ? 338 LEU A O   1 
ATOM   2468 C CB  . LEU A 1 351 ? 124.334 164.890 99.830  1.00 122.06 ? 338 LEU A CB  1 
ATOM   2469 C CG  . LEU A 1 351 ? 125.567 164.923 100.736 1.00 122.14 ? 338 LEU A CG  1 
ATOM   2470 C CD1 . LEU A 1 351 ? 125.592 166.191 101.577 1.00 123.44 ? 338 LEU A CD1 1 
ATOM   2471 C CD2 . LEU A 1 351 ? 125.621 163.687 101.621 1.00 113.84 ? 338 LEU A CD2 1 
ATOM   2472 N N   . PRO A 1 352 ? 126.254 167.054 97.851  1.00 132.65 ? 339 PRO A N   1 
ATOM   2473 C CA  . PRO A 1 352 ? 127.476 167.050 97.039  1.00 136.38 ? 339 PRO A CA  1 
ATOM   2474 C C   . PRO A 1 352 ? 128.468 166.006 97.530  1.00 140.85 ? 339 PRO A C   1 
ATOM   2475 O O   . PRO A 1 352 ? 128.590 165.742 98.728  1.00 139.96 ? 339 PRO A O   1 
ATOM   2476 C CB  . PRO A 1 352 ? 128.025 168.471 97.215  1.00 134.41 ? 339 PRO A CB  1 
ATOM   2477 C CG  . PRO A 1 352 ? 127.423 168.955 98.496  1.00 133.63 ? 339 PRO A CG  1 
ATOM   2478 C CD  . PRO A 1 352 ? 126.064 168.327 98.565  1.00 130.71 ? 339 PRO A CD  1 
ATOM   2479 N N   . ALA A 1 353 ? 129.181 165.409 96.580  1.00 143.37 ? 340 ALA A N   1 
ATOM   2480 C CA  . ALA A 1 353 ? 130.157 164.371 96.894  1.00 148.08 ? 340 ALA A CA  1 
ATOM   2481 C C   . ALA A 1 353 ? 131.576 164.843 96.593  1.00 152.83 ? 340 ALA A C   1 
ATOM   2482 O O   . ALA A 1 353 ? 131.851 166.043 96.567  1.00 149.62 ? 340 ALA A O   1 
ATOM   2483 C CB  . ALA A 1 353 ? 129.845 163.100 96.119  1.00 146.67 ? 340 ALA A CB  1 
ATOM   2484 N N   . THR A 1 364 ? 137.107 148.630 86.509  1.00 141.60 ? 351 THR A N   1 
ATOM   2485 C CA  . THR A 1 364 ? 136.448 148.400 87.790  1.00 136.77 ? 351 THR A CA  1 
ATOM   2486 C C   . THR A 1 364 ? 135.076 149.061 87.819  1.00 130.37 ? 351 THR A C   1 
ATOM   2487 O O   . THR A 1 364 ? 134.471 149.216 88.879  1.00 128.08 ? 351 THR A O   1 
ATOM   2488 C CB  . THR A 1 364 ? 137.292 148.929 88.962  1.00 140.44 ? 351 THR A CB  1 
ATOM   2489 O OG1 . THR A 1 364 ? 136.544 148.820 90.180  1.00 139.41 ? 351 THR A OG1 1 
ATOM   2490 C CG2 . THR A 1 364 ? 137.675 150.382 88.732  1.00 137.67 ? 351 THR A CG2 1 
ATOM   2491 N N   . GLN A 1 365 ? 134.593 149.445 86.637  1.00 132.95 ? 352 GLN A N   1 
ATOM   2492 C CA  . GLN A 1 365 ? 133.286 150.085 86.483  1.00 134.30 ? 352 GLN A CA  1 
ATOM   2493 C C   . GLN A 1 365 ? 132.209 149.004 86.492  1.00 130.78 ? 352 GLN A C   1 
ATOM   2494 O O   . GLN A 1 365 ? 131.836 148.437 85.462  1.00 130.22 ? 352 GLN A O   1 
ATOM   2495 C CB  . GLN A 1 365 ? 133.240 150.911 85.205  1.00 136.65 ? 352 GLN A CB  1 
ATOM   2496 C CG  . GLN A 1 365 ? 131.938 151.669 84.991  1.00 133.31 ? 352 GLN A CG  1 
ATOM   2497 C CD  . GLN A 1 365 ? 131.884 152.979 85.757  1.00 139.72 ? 352 GLN A CD  1 
ATOM   2498 O OE1 . GLN A 1 365 ? 132.488 153.122 86.820  1.00 139.05 ? 352 GLN A OE1 1 
ATOM   2499 N NE2 . GLN A 1 365 ? 131.159 153.948 85.211  1.00 141.03 ? 352 GLN A NE2 1 
ATOM   2500 N N   . GLU A 1 366 ? 131.709 148.709 87.689  1.00 126.49 ? 353 GLU A N   1 
ATOM   2501 C CA  . GLU A 1 366 ? 130.668 147.701 87.838  1.00 119.16 ? 353 GLU A CA  1 
ATOM   2502 C C   . GLU A 1 366 ? 129.400 148.137 87.117  1.00 116.07 ? 353 GLU A C   1 
ATOM   2503 O O   . GLU A 1 366 ? 128.965 149.286 87.236  1.00 112.69 ? 353 GLU A O   1 
ATOM   2504 C CB  . GLU A 1 366 ? 130.373 147.451 89.317  1.00 112.49 ? 353 GLU A CB  1 
ATOM   2505 C CG  . GLU A 1 366 ? 131.606 147.330 90.195  1.00 116.92 ? 353 GLU A CG  1 
ATOM   2506 C CD  . GLU A 1 366 ? 132.110 148.676 90.677  1.00 121.16 ? 353 GLU A CD  1 
ATOM   2507 O OE1 . GLU A 1 366 ? 131.530 149.707 90.275  1.00 123.01 ? 353 GLU A OE1 1 
ATOM   2508 O OE2 . GLU A 1 366 ? 133.086 148.707 91.455  1.00 121.20 ? 353 GLU A OE2 1 
ATOM   2509 N N   . SER A 1 367 ? 128.809 147.214 86.363  1.00 116.39 ? 354 SER A N   1 
ATOM   2510 C CA  . SER A 1 367 ? 127.588 147.508 85.627  1.00 112.87 ? 354 SER A CA  1 
ATOM   2511 C C   . SER A 1 367 ? 126.377 147.355 86.538  1.00 107.07 ? 354 SER A C   1 
ATOM   2512 O O   . SER A 1 367 ? 126.265 146.375 87.281  1.00 109.55 ? 354 SER A O   1 
ATOM   2513 C CB  . SER A 1 367 ? 127.464 146.589 84.413  1.00 116.91 ? 354 SER A CB  1 
ATOM   2514 O OG  . SER A 1 367 ? 128.548 146.783 83.521  1.00 112.88 ? 354 SER A OG  1 
ATOM   2515 N N   . TYR A 1 368 ? 125.479 148.331 86.485  1.00 98.97  ? 355 TYR A N   1 
ATOM   2516 C CA  . TYR A 1 368 ? 124.243 148.333 87.250  1.00 100.65 ? 355 TYR A CA  1 
ATOM   2517 C C   . TYR A 1 368 ? 123.053 148.235 86.302  1.00 100.56 ? 355 TYR A C   1 
ATOM   2518 O O   . TYR A 1 368 ? 123.201 148.180 85.078  1.00 101.64 ? 355 TYR A O   1 
ATOM   2519 C CB  . TYR A 1 368 ? 124.150 149.590 88.118  1.00 101.44 ? 355 TYR A CB  1 
ATOM   2520 C CG  . TYR A 1 368 ? 125.101 149.604 89.291  1.00 96.92  ? 355 TYR A CG  1 
ATOM   2521 C CD1 . TYR A 1 368 ? 126.461 149.809 89.108  1.00 97.98  ? 355 TYR A CD1 1 
ATOM   2522 C CD2 . TYR A 1 368 ? 124.635 149.422 90.585  1.00 92.27  ? 355 TYR A CD2 1 
ATOM   2523 C CE1 . TYR A 1 368 ? 127.331 149.823 90.180  1.00 100.19 ? 355 TYR A CE1 1 
ATOM   2524 C CE2 . TYR A 1 368 ? 125.496 149.436 91.662  1.00 90.66  ? 355 TYR A CE2 1 
ATOM   2525 C CZ  . TYR A 1 368 ? 126.842 149.637 91.454  1.00 94.96  ? 355 TYR A CZ  1 
ATOM   2526 O OH  . TYR A 1 368 ? 127.704 149.652 92.527  1.00 93.84  ? 355 TYR A OH  1 
ATOM   2527 N N   . TYR A 1 369 ? 121.853 148.216 86.883  1.00 99.13  ? 356 TYR A N   1 
ATOM   2528 C CA  . TYR A 1 369 ? 120.642 148.222 86.070  1.00 100.04 ? 356 TYR A CA  1 
ATOM   2529 C C   . TYR A 1 369 ? 120.373 149.616 85.516  1.00 106.66 ? 356 TYR A C   1 
ATOM   2530 O O   . TYR A 1 369 ? 120.302 149.811 84.298  1.00 110.31 ? 356 TYR A O   1 
ATOM   2531 C CB  . TYR A 1 369 ? 119.448 147.729 86.891  1.00 100.20 ? 356 TYR A CB  1 
ATOM   2532 C CG  . TYR A 1 369 ? 118.211 147.451 86.064  1.00 99.48  ? 356 TYR A CG  1 
ATOM   2533 C CD1 . TYR A 1 369 ? 118.291 147.311 84.684  1.00 94.74  ? 356 TYR A CD1 1 
ATOM   2534 C CD2 . TYR A 1 369 ? 116.964 147.337 86.662  1.00 100.45 ? 356 TYR A CD2 1 
ATOM   2535 C CE1 . TYR A 1 369 ? 117.166 147.062 83.925  1.00 94.11  ? 356 TYR A CE1 1 
ATOM   2536 C CE2 . TYR A 1 369 ? 115.833 147.087 85.910  1.00 99.87  ? 356 TYR A CE2 1 
ATOM   2537 C CZ  . TYR A 1 369 ? 115.939 146.950 84.543  1.00 98.40  ? 356 TYR A CZ  1 
ATOM   2538 O OH  . TYR A 1 369 ? 114.815 146.701 83.790  1.00 103.49 ? 356 TYR A OH  1 
ATOM   2539 N N   . ASP A 1 370 ? 120.218 150.597 86.400  1.00 109.03 ? 357 ASP A N   1 
ATOM   2540 C CA  . ASP A 1 370 ? 120.020 151.975 85.978  1.00 113.69 ? 357 ASP A CA  1 
ATOM   2541 C C   . ASP A 1 370 ? 121.367 152.682 85.930  1.00 116.33 ? 357 ASP A C   1 
ATOM   2542 O O   . ASP A 1 370 ? 122.034 152.786 86.968  1.00 114.73 ? 357 ASP A O   1 
ATOM   2543 C CB  . ASP A 1 370 ? 119.083 152.698 86.930  1.00 111.84 ? 357 ASP A CB  1 
ATOM   2544 C CG  . ASP A 1 370 ? 118.473 153.946 86.318  1.00 115.62 ? 357 ASP A CG  1 
ATOM   2545 O OD1 . ASP A 1 370 ? 119.124 154.582 85.464  1.00 115.02 ? 357 ASP A OD1 1 
ATOM   2546 O OD2 . ASP A 1 370 ? 117.333 154.291 86.693  1.00 120.29 ? 357 ASP A OD2 1 
ATOM   2547 N N   . PRO A 1 371 ? 121.807 153.172 84.768  1.00 118.92 ? 358 PRO A N   1 
ATOM   2548 C CA  . PRO A 1 371 ? 123.090 153.889 84.716  1.00 117.52 ? 358 PRO A CA  1 
ATOM   2549 C C   . PRO A 1 371 ? 123.107 155.162 85.542  1.00 120.05 ? 358 PRO A C   1 
ATOM   2550 O O   . PRO A 1 371 ? 124.193 155.658 85.865  1.00 120.75 ? 358 PRO A O   1 
ATOM   2551 C CB  . PRO A 1 371 ? 123.266 154.187 83.220  1.00 122.00 ? 358 PRO A CB  1 
ATOM   2552 C CG  . PRO A 1 371 ? 121.879 154.137 82.658  1.00 121.98 ? 358 PRO A CG  1 
ATOM   2553 C CD  . PRO A 1 371 ? 121.163 153.084 83.447  1.00 119.10 ? 358 PRO A CD  1 
ATOM   2554 N N   . ASN A 1 372 ? 121.941 155.708 85.893  1.00 121.01 ? 359 ASN A N   1 
ATOM   2555 C CA  . ASN A 1 372 ? 121.886 156.895 86.737  1.00 121.14 ? 359 ASN A CA  1 
ATOM   2556 C C   . ASN A 1 372 ? 122.274 156.612 88.182  1.00 121.92 ? 359 ASN A C   1 
ATOM   2557 O O   . ASN A 1 372 ? 122.445 157.562 88.953  1.00 122.43 ? 359 ASN A O   1 
ATOM   2558 C CB  . ASN A 1 372 ? 120.482 157.504 86.697  1.00 120.25 ? 359 ASN A CB  1 
ATOM   2559 C CG  . ASN A 1 372 ? 120.077 157.944 85.304  1.00 124.49 ? 359 ASN A CG  1 
ATOM   2560 O OD1 . ASN A 1 372 ? 120.908 158.398 84.518  1.00 124.90 ? 359 ASN A OD1 1 
ATOM   2561 N ND2 . ASN A 1 372 ? 118.792 157.811 84.991  1.00 126.12 ? 359 ASN A ND2 1 
ATOM   2562 N N   . LEU A 1 373 ? 122.410 155.346 88.566  1.00 119.69 ? 360 LEU A N   1 
ATOM   2563 C CA  . LEU A 1 373 ? 122.791 155.003 89.931  1.00 114.07 ? 360 LEU A CA  1 
ATOM   2564 C C   . LEU A 1 373 ? 124.289 155.201 90.124  1.00 113.86 ? 360 LEU A C   1 
ATOM   2565 O O   . LEU A 1 373 ? 125.083 154.547 89.437  1.00 117.33 ? 360 LEU A O   1 
ATOM   2566 C CB  . LEU A 1 373 ? 122.422 153.557 90.242  1.00 113.54 ? 360 LEU A CB  1 
ATOM   2567 C CG  . LEU A 1 373 ? 121.141 153.254 91.023  1.00 116.14 ? 360 LEU A CG  1 
ATOM   2568 C CD1 . LEU A 1 373 ? 121.225 153.812 92.437  1.00 106.86 ? 360 LEU A CD1 1 
ATOM   2569 C CD2 . LEU A 1 373 ? 119.915 153.783 90.295  1.00 115.95 ? 360 LEU A CD2 1 
ATOM   2570 N N   . PRO A 1 374 ? 124.717 156.077 91.026  1.00 112.51 ? 361 PRO A N   1 
ATOM   2571 C CA  . PRO A 1 374 ? 126.136 156.165 91.359  1.00 111.09 ? 361 PRO A CA  1 
ATOM   2572 C C   . PRO A 1 374 ? 126.531 155.031 92.285  1.00 107.99 ? 361 PRO A C   1 
ATOM   2573 O O   . PRO A 1 374 ? 125.664 154.425 92.934  1.00 107.54 ? 361 PRO A O   1 
ATOM   2574 C CB  . PRO A 1 374 ? 126.244 157.525 92.061  1.00 112.63 ? 361 PRO A CB  1 
ATOM   2575 C CG  . PRO A 1 374 ? 124.914 157.692 92.704  1.00 113.13 ? 361 PRO A CG  1 
ATOM   2576 C CD  . PRO A 1 374 ? 123.912 157.059 91.774  1.00 114.98 ? 361 PRO A CD  1 
ATOM   2577 N N   . PRO A 1 375 ? 127.818 154.699 92.368  1.00 107.06 ? 362 PRO A N   1 
ATOM   2578 C CA  . PRO A 1 375 ? 128.238 153.661 93.313  1.00 105.33 ? 362 PRO A CA  1 
ATOM   2579 C C   . PRO A 1 375 ? 127.915 154.072 94.741  1.00 103.34 ? 362 PRO A C   1 
ATOM   2580 O O   . PRO A 1 375 ? 128.082 155.231 95.128  1.00 104.72 ? 362 PRO A O   1 
ATOM   2581 C CB  . PRO A 1 375 ? 129.749 153.551 93.077  1.00 107.02 ? 362 PRO A CB  1 
ATOM   2582 C CG  . PRO A 1 375 ? 130.130 154.846 92.433  1.00 107.44 ? 362 PRO A CG  1 
ATOM   2583 C CD  . PRO A 1 375 ? 128.952 155.228 91.593  1.00 105.95 ? 362 PRO A CD  1 
ATOM   2584 N N   . VAL A 1 376 ? 127.448 153.104 95.526  1.00 97.32  ? 363 VAL A N   1 
ATOM   2585 C CA  . VAL A 1 376 ? 126.990 153.339 96.890  1.00 92.09  ? 363 VAL A CA  1 
ATOM   2586 C C   . VAL A 1 376 ? 128.077 152.875 97.850  1.00 87.89  ? 363 VAL A C   1 
ATOM   2587 O O   . VAL A 1 376 ? 128.659 151.798 97.670  1.00 82.86  ? 363 VAL A O   1 
ATOM   2588 C CB  . VAL A 1 376 ? 125.658 152.616 97.162  1.00 85.72  ? 363 VAL A CB  1 
ATOM   2589 C CG1 . VAL A 1 376 ? 124.520 153.276 96.387  1.00 90.01  ? 363 VAL A CG1 1 
ATOM   2590 C CG2 . VAL A 1 376 ? 125.761 151.150 96.785  1.00 83.88  ? 363 VAL A CG2 1 
ATOM   2591 N N   . THR A 1 377 ? 128.374 153.696 98.854  1.00 88.51  ? 364 THR A N   1 
ATOM   2592 C CA  . THR A 1 377 ? 129.423 153.407 99.820  1.00 89.52  ? 364 THR A CA  1 
ATOM   2593 C C   . THR A 1 377 ? 128.917 153.729 101.221 1.00 84.70  ? 364 THR A C   1 
ATOM   2594 O O   . THR A 1 377 ? 127.803 154.225 101.405 1.00 85.96  ? 364 THR A O   1 
ATOM   2595 C CB  . THR A 1 377 ? 130.704 154.202 99.514  1.00 97.23  ? 364 THR A CB  1 
ATOM   2596 O OG1 . THR A 1 377 ? 131.771 153.738 100.352 1.00 102.40 ? 364 THR A OG1 1 
ATOM   2597 C CG2 . THR A 1 377 ? 130.500 155.696 99.767  1.00 96.76  ? 364 THR A CG2 1 
ATOM   2598 N N   . LYS A 1 378 ? 129.757 153.432 102.216 1.00 82.02  ? 365 LYS A N   1 
ATOM   2599 C CA  . LYS A 1 378 ? 129.435 153.755 103.603 1.00 83.18  ? 365 LYS A CA  1 
ATOM   2600 C C   . LYS A 1 378 ? 129.144 155.242 103.775 1.00 88.66  ? 365 LYS A C   1 
ATOM   2601 O O   . LYS A 1 378 ? 128.168 155.624 104.430 1.00 90.14  ? 365 LYS A O   1 
ATOM   2602 C CB  . LYS A 1 378 ? 130.582 153.316 104.513 1.00 83.43  ? 365 LYS A CB  1 
ATOM   2603 C CG  . LYS A 1 378 ? 130.687 151.811 104.679 1.00 79.91  ? 365 LYS A CG  1 
ATOM   2604 C CD  . LYS A 1 378 ? 129.490 151.276 105.440 1.00 79.19  ? 365 LYS A CD  1 
ATOM   2605 C CE  . LYS A 1 378 ? 129.429 151.875 106.831 1.00 81.16  ? 365 LYS A CE  1 
ATOM   2606 N NZ  . LYS A 1 378 ? 130.647 151.546 107.617 1.00 82.44  ? 365 LYS A NZ  1 
ATOM   2607 N N   . SER A 1 379 ? 129.981 156.098 103.179 1.00 92.86  ? 366 SER A N   1 
ATOM   2608 C CA  . SER A 1 379 ? 129.771 157.539 103.273 1.00 92.27  ? 366 SER A CA  1 
ATOM   2609 C C   . SER A 1 379 ? 128.445 157.969 102.659 1.00 88.37  ? 366 SER A C   1 
ATOM   2610 O O   . SER A 1 379 ? 127.940 159.045 102.996 1.00 87.98  ? 366 SER A O   1 
ATOM   2611 C CB  . SER A 1 379 ? 130.921 158.287 102.592 1.00 93.43  ? 366 SER A CB  1 
ATOM   2612 O OG  . SER A 1 379 ? 132.172 157.931 103.151 1.00 100.43 ? 366 SER A OG  1 
ATOM   2613 N N   . LEU A 1 380 ? 127.869 157.153 101.775 1.00 87.92  ? 367 LEU A N   1 
ATOM   2614 C CA  . LEU A 1 380 ? 126.581 157.449 101.161 1.00 90.85  ? 367 LEU A CA  1 
ATOM   2615 C C   . LEU A 1 380 ? 125.420 156.840 101.941 1.00 87.69  ? 367 LEU A C   1 
ATOM   2616 O O   . LEU A 1 380 ? 124.448 157.535 102.247 1.00 85.59  ? 367 LEU A O   1 
ATOM   2617 C CB  . LEU A 1 380 ? 126.560 156.947 99.712  1.00 91.54  ? 367 LEU A CB  1 
ATOM   2618 C CG  . LEU A 1 380 ? 125.242 157.160 98.957  1.00 89.34  ? 367 LEU A CG  1 
ATOM   2619 C CD1 . LEU A 1 380 ? 124.850 158.630 98.984  1.00 96.85  ? 367 LEU A CD1 1 
ATOM   2620 C CD2 . LEU A 1 380 ? 125.326 156.651 97.523  1.00 86.05  ? 367 LEU A CD2 1 
ATOM   2621 N N   . VAL A 1 381 ? 125.508 155.549 102.268 1.00 86.46  ? 368 VAL A N   1 
ATOM   2622 C CA  . VAL A 1 381 ? 124.394 154.877 102.930 1.00 81.01  ? 368 VAL A CA  1 
ATOM   2623 C C   . VAL A 1 381 ? 124.216 155.389 104.356 1.00 87.73  ? 368 VAL A C   1 
ATOM   2624 O O   . VAL A 1 381 ? 123.086 155.576 104.822 1.00 89.78  ? 368 VAL A O   1 
ATOM   2625 C CB  . VAL A 1 381 ? 124.581 153.349 102.887 1.00 75.78  ? 368 VAL A CB  1 
ATOM   2626 C CG1 . VAL A 1 381 ? 124.598 152.863 101.452 1.00 74.78  ? 368 VAL A CG1 1 
ATOM   2627 C CG2 . VAL A 1 381 ? 125.858 152.934 103.596 1.00 80.94  ? 368 VAL A CG2 1 
ATOM   2628 N N   . THR A 1 382 ? 125.318 155.632 105.074 1.00 90.06  ? 369 THR A N   1 
ATOM   2629 C CA  . THR A 1 382 ? 125.201 156.090 106.454 1.00 87.41  ? 369 THR A CA  1 
ATOM   2630 C C   . THR A 1 382 ? 124.668 157.513 106.531 1.00 89.11  ? 369 THR A C   1 
ATOM   2631 O O   . THR A 1 382 ? 123.967 157.858 107.488 1.00 91.11  ? 369 THR A O   1 
ATOM   2632 C CB  . THR A 1 382 ? 126.553 156.006 107.158 1.00 86.97  ? 369 THR A CB  1 
ATOM   2633 O OG1 . THR A 1 382 ? 127.525 156.765 106.425 1.00 89.03  ? 369 THR A OG1 1 
ATOM   2634 C CG2 . THR A 1 382 ? 127.011 154.564 107.254 1.00 82.87  ? 369 THR A CG2 1 
ATOM   2635 N N   . ASN A 1 383 ? 124.985 158.347 105.545 1.00 85.48  ? 370 ASN A N   1 
ATOM   2636 C CA  . ASN A 1 383 ? 124.537 159.730 105.522 1.00 82.60  ? 370 ASN A CA  1 
ATOM   2637 C C   . ASN A 1 383 ? 123.238 159.914 104.745 1.00 80.62  ? 370 ASN A C   1 
ATOM   2638 O O   . ASN A 1 383 ? 122.785 161.050 104.580 1.00 80.17  ? 370 ASN A O   1 
ATOM   2639 C CB  . ASN A 1 383 ? 125.632 160.626 104.936 1.00 81.68  ? 370 ASN A CB  1 
ATOM   2640 C CG  . ASN A 1 383 ? 126.974 160.449 105.634 1.00 79.30  ? 370 ASN A CG  1 
ATOM   2641 O OD1 . ASN A 1 383 ? 127.256 159.396 106.214 1.00 75.39  ? 370 ASN A OD1 1 
ATOM   2642 N ND2 . ASN A 1 383 ? 127.812 161.481 105.573 1.00 82.12  ? 370 ASN A ND2 1 
ATOM   2643 N N   . CYS A 1 384 ? 122.633 158.828 104.271 1.00 83.21  ? 371 CYS A N   1 
ATOM   2644 C CA  . CYS A 1 384 ? 121.354 158.885 103.572 1.00 87.78  ? 371 CYS A CA  1 
ATOM   2645 C C   . CYS A 1 384 ? 120.243 158.684 104.595 1.00 89.42  ? 371 CYS A C   1 
ATOM   2646 O O   . CYS A 1 384 ? 119.983 157.557 105.027 1.00 91.44  ? 371 CYS A O   1 
ATOM   2647 C CB  . CYS A 1 384 ? 121.294 157.831 102.470 1.00 88.68  ? 371 CYS A CB  1 
ATOM   2648 S SG  . CYS A 1 384 ? 119.742 157.786 101.546 1.00 100.71 ? 371 CYS A SG  1 
ATOM   2649 N N   . LYS A 1 385 ? 119.590 159.778 104.979 1.00 87.71  ? 372 LYS A N   1 
ATOM   2650 C CA  . LYS A 1 385 ? 118.598 159.721 106.052 1.00 89.21  ? 372 LYS A CA  1 
ATOM   2651 C C   . LYS A 1 385 ? 117.419 158.801 105.754 1.00 86.73  ? 372 LYS A C   1 
ATOM   2652 O O   . LYS A 1 385 ? 117.030 158.031 106.651 1.00 86.68  ? 372 LYS A O   1 
ATOM   2653 C CB  . LYS A 1 385 ? 118.121 161.139 106.379 1.00 93.39  ? 372 LYS A CB  1 
ATOM   2654 C CG  . LYS A 1 385 ? 117.188 161.216 107.576 1.00 94.32  ? 372 LYS A CG  1 
ATOM   2655 C CD  . LYS A 1 385 ? 117.850 160.654 108.820 1.00 95.48  ? 372 LYS A CD  1 
ATOM   2656 C CE  . LYS A 1 385 ? 119.102 161.439 109.177 1.00 97.55  ? 372 LYS A CE  1 
ATOM   2657 N NZ  . LYS A 1 385 ? 119.855 160.788 110.282 1.00 99.00  ? 372 LYS A NZ  1 
ATOM   2658 N N   . PRO A 1 386 ? 116.785 158.840 104.572 1.00 86.36  ? 373 PRO A N   1 
ATOM   2659 C CA  . PRO A 1 386 ? 115.594 157.992 104.376 1.00 89.87  ? 373 PRO A CA  1 
ATOM   2660 C C   . PRO A 1 386 ? 115.862 156.505 104.530 1.00 90.77  ? 373 PRO A C   1 
ATOM   2661 O O   . PRO A 1 386 ? 115.063 155.801 105.162 1.00 89.33  ? 373 PRO A O   1 
ATOM   2662 C CB  . PRO A 1 386 ? 115.144 158.347 102.950 1.00 87.88  ? 373 PRO A CB  1 
ATOM   2663 C CG  . PRO A 1 386 ? 116.349 158.921 102.299 1.00 90.74  ? 373 PRO A CG  1 
ATOM   2664 C CD  . PRO A 1 386 ? 117.052 159.666 103.381 1.00 86.49  ? 373 PRO A CD  1 
ATOM   2665 N N   . VAL A 1 387 ? 116.973 156.003 103.985 1.00 91.49  ? 374 VAL A N   1 
ATOM   2666 C CA  . VAL A 1 387 ? 117.253 154.575 104.099 1.00 89.86  ? 374 VAL A CA  1 
ATOM   2667 C C   . VAL A 1 387 ? 117.567 154.205 105.544 1.00 84.66  ? 374 VAL A C   1 
ATOM   2668 O O   . VAL A 1 387 ? 117.190 153.127 106.013 1.00 82.53  ? 374 VAL A O   1 
ATOM   2669 C CB  . VAL A 1 387 ? 118.379 154.155 103.134 1.00 88.00  ? 374 VAL A CB  1 
ATOM   2670 C CG1 . VAL A 1 387 ? 118.019 154.534 101.705 1.00 88.83  ? 374 VAL A CG1 1 
ATOM   2671 C CG2 . VAL A 1 387 ? 119.713 154.761 103.534 1.00 86.31  ? 374 VAL A CG2 1 
ATOM   2672 N N   . THR A 1 388 ? 118.256 155.087 106.274 1.00 83.07  ? 375 THR A N   1 
ATOM   2673 C CA  . THR A 1 388 ? 118.534 154.814 107.681 1.00 83.18  ? 375 THR A CA  1 
ATOM   2674 C C   . THR A 1 388 ? 117.248 154.754 108.493 1.00 82.14  ? 375 THR A C   1 
ATOM   2675 O O   . THR A 1 388 ? 117.077 153.866 109.338 1.00 81.74  ? 375 THR A O   1 
ATOM   2676 C CB  . THR A 1 388 ? 119.473 155.876 108.255 1.00 86.12  ? 375 THR A CB  1 
ATOM   2677 O OG1 . THR A 1 388 ? 118.873 157.170 108.121 1.00 89.92  ? 375 THR A OG1 1 
ATOM   2678 C CG2 . THR A 1 388 ? 120.809 155.858 107.528 1.00 85.06  ? 375 THR A CG2 1 
ATOM   2679 N N   . ASP A 1 389 ? 116.330 155.691 108.250 1.00 82.43  ? 376 ASP A N   1 
ATOM   2680 C CA  . ASP A 1 389 ? 115.050 155.663 108.948 1.00 80.82  ? 376 ASP A CA  1 
ATOM   2681 C C   . ASP A 1 389 ? 114.264 154.407 108.601 1.00 80.70  ? 376 ASP A C   1 
ATOM   2682 O O   . ASP A 1 389 ? 113.630 153.800 109.472 1.00 83.22  ? 376 ASP A O   1 
ATOM   2683 C CB  . ASP A 1 389 ? 114.238 156.914 108.614 1.00 84.61  ? 376 ASP A CB  1 
ATOM   2684 C CG  . ASP A 1 389 ? 114.848 158.175 109.190 1.00 91.57  ? 376 ASP A CG  1 
ATOM   2685 O OD1 . ASP A 1 389 ? 115.453 158.099 110.280 1.00 91.10  ? 376 ASP A OD1 1 
ATOM   2686 O OD2 . ASP A 1 389 ? 114.723 159.241 108.552 1.00 94.07  ? 376 ASP A OD2 1 
ATOM   2687 N N   . LYS A 1 390 ? 114.296 153.999 107.330 1.00 80.51  ? 377 LYS A N   1 
ATOM   2688 C CA  . LYS A 1 390 ? 113.577 152.795 106.929 1.00 81.88  ? 377 LYS A CA  1 
ATOM   2689 C C   . LYS A 1 390 ? 114.180 151.546 107.558 1.00 78.78  ? 377 LYS A C   1 
ATOM   2690 O O   . LYS A 1 390 ? 113.444 150.628 107.936 1.00 76.83  ? 377 LYS A O   1 
ATOM   2691 C CB  . LYS A 1 390 ? 113.571 152.677 105.405 1.00 84.28  ? 377 LYS A CB  1 
ATOM   2692 C CG  . LYS A 1 390 ? 112.430 151.843 104.846 1.00 88.86  ? 377 LYS A CG  1 
ATOM   2693 C CD  . LYS A 1 390 ? 112.374 151.953 103.330 1.00 90.41  ? 377 LYS A CD  1 
ATOM   2694 C CE  . LYS A 1 390 ? 111.147 151.260 102.761 1.00 84.79  ? 377 LYS A CE  1 
ATOM   2695 N NZ  . LYS A 1 390 ? 111.040 151.457 101.289 1.00 84.80  ? 377 LYS A NZ  1 
ATOM   2696 N N   . ILE A 1 391 ? 115.507 151.494 107.680 1.00 78.09  ? 378 ILE A N   1 
ATOM   2697 C CA  . ILE A 1 391 ? 116.159 150.369 108.347 1.00 75.73  ? 378 ILE A CA  1 
ATOM   2698 C C   . ILE A 1 391 ? 115.780 150.335 109.823 1.00 77.61  ? 378 ILE A C   1 
ATOM   2699 O O   . ILE A 1 391 ? 115.457 149.277 110.376 1.00 78.58  ? 378 ILE A O   1 
ATOM   2700 C CB  . ILE A 1 391 ? 117.684 150.445 108.156 1.00 72.69  ? 378 ILE A CB  1 
ATOM   2701 C CG1 . ILE A 1 391 ? 118.051 150.205 106.692 1.00 74.45  ? 378 ILE A CG1 1 
ATOM   2702 C CG2 . ILE A 1 391 ? 118.388 149.439 109.050 1.00 72.42  ? 378 ILE A CG2 1 
ATOM   2703 C CD1 . ILE A 1 391 ? 119.520 150.395 106.398 1.00 74.79  ? 378 ILE A CD1 1 
ATOM   2704 N N   . HIS A 1 392 ? 115.815 151.497 110.483 1.00 76.51  ? 379 HIS A N   1 
ATOM   2705 C CA  . HIS A 1 392 ? 115.454 151.551 111.897 1.00 73.69  ? 379 HIS A CA  1 
ATOM   2706 C C   . HIS A 1 392 ? 114.012 151.113 112.116 1.00 78.95  ? 379 HIS A C   1 
ATOM   2707 O O   . HIS A 1 392 ? 113.716 150.382 113.069 1.00 77.68  ? 379 HIS A O   1 
ATOM   2708 C CB  . HIS A 1 392 ? 115.673 152.961 112.445 1.00 74.33  ? 379 HIS A CB  1 
ATOM   2709 C CG  . HIS A 1 392 ? 117.103 153.275 112.752 1.00 78.82  ? 379 HIS A CG  1 
ATOM   2710 N ND1 . HIS A 1 392 ? 117.494 154.451 113.357 1.00 83.59  ? 379 HIS A ND1 1 
ATOM   2711 C CD2 . HIS A 1 392 ? 118.237 152.566 112.541 1.00 78.98  ? 379 HIS A CD2 1 
ATOM   2712 C CE1 . HIS A 1 392 ? 118.806 154.453 113.503 1.00 82.76  ? 379 HIS A CE1 1 
ATOM   2713 N NE2 . HIS A 1 392 ? 119.282 153.321 113.017 1.00 80.65  ? 379 HIS A NE2 1 
ATOM   2714 N N   . LYS A 1 393 ? 113.098 151.554 111.249 1.00 82.12  ? 380 LYS A N   1 
ATOM   2715 C CA  . LYS A 1 393 ? 111.714 151.105 111.349 1.00 82.92  ? 380 LYS A CA  1 
ATOM   2716 C C   . LYS A 1 393 ? 111.601 149.606 111.096 1.00 83.90  ? 380 LYS A C   1 
ATOM   2717 O O   . LYS A 1 393 ? 110.828 148.912 111.766 1.00 84.74  ? 380 LYS A O   1 
ATOM   2718 C CB  . LYS A 1 393 ? 110.836 151.885 110.370 1.00 84.49  ? 380 LYS A CB  1 
ATOM   2719 C CG  . LYS A 1 393 ? 109.368 151.489 110.406 1.00 87.16  ? 380 LYS A CG  1 
ATOM   2720 C CD  . LYS A 1 393 ? 108.526 152.397 109.525 1.00 87.47  ? 380 LYS A CD  1 
ATOM   2721 C CE  . LYS A 1 393 ? 108.540 153.825 110.040 1.00 84.48  ? 380 LYS A CE  1 
ATOM   2722 N NZ  . LYS A 1 393 ? 108.062 153.905 111.447 1.00 86.93  ? 380 LYS A NZ  1 
ATOM   2723 N N   . ALA A 1 394 ? 112.367 149.089 110.133 1.00 82.92  ? 381 ALA A N   1 
ATOM   2724 C CA  . ALA A 1 394 ? 112.282 147.673 109.792 1.00 83.87  ? 381 ALA A CA  1 
ATOM   2725 C C   . ALA A 1 394 ? 112.938 146.803 110.857 1.00 83.53  ? 381 ALA A C   1 
ATOM   2726 O O   . ALA A 1 394 ? 112.327 145.851 111.357 1.00 89.87  ? 381 ALA A O   1 
ATOM   2727 C CB  . ALA A 1 394 ? 112.923 147.425 108.428 1.00 85.02  ? 381 ALA A CB  1 
ATOM   2728 N N   . TYR A 1 395 ? 114.182 147.108 111.214 1.00 77.73  ? 382 TYR A N   1 
ATOM   2729 C CA  . TYR A 1 395 ? 114.915 146.296 112.176 1.00 76.91  ? 382 TYR A CA  1 
ATOM   2730 C C   . TYR A 1 395 ? 114.432 146.601 113.587 1.00 79.50  ? 382 TYR A C   1 
ATOM   2731 O O   . TYR A 1 395 ? 114.530 147.742 114.052 1.00 79.41  ? 382 TYR A O   1 
ATOM   2732 C CB  . TYR A 1 395 ? 116.417 146.546 112.066 1.00 77.30  ? 382 TYR A CB  1 
ATOM   2733 C CG  . TYR A 1 395 ? 117.099 145.768 110.967 1.00 72.39  ? 382 TYR A CG  1 
ATOM   2734 C CD1 . TYR A 1 395 ? 116.363 145.088 110.009 1.00 71.34  ? 382 TYR A CD1 1 
ATOM   2735 C CD2 . TYR A 1 395 ? 118.483 145.703 110.899 1.00 71.65  ? 382 TYR A CD2 1 
ATOM   2736 C CE1 . TYR A 1 395 ? 116.987 144.374 109.006 1.00 75.63  ? 382 TYR A CE1 1 
ATOM   2737 C CE2 . TYR A 1 395 ? 119.115 144.991 109.903 1.00 73.58  ? 382 TYR A CE2 1 
ATOM   2738 C CZ  . TYR A 1 395 ? 118.364 144.328 108.959 1.00 77.07  ? 382 TYR A CZ  1 
ATOM   2739 O OH  . TYR A 1 395 ? 118.994 143.618 107.963 1.00 76.88  ? 382 TYR A OH  1 
ATOM   2740 N N   . LYS A 1 396 ? 113.918 145.582 114.266 1.00 81.62  ? 383 LYS A N   1 
ATOM   2741 C CA  . LYS A 1 396 ? 113.524 145.733 115.656 1.00 87.62  ? 383 LYS A CA  1 
ATOM   2742 C C   . LYS A 1 396 ? 114.757 145.860 116.545 1.00 90.65  ? 383 LYS A C   1 
ATOM   2743 O O   . LYS A 1 396 ? 115.865 145.457 116.180 1.00 90.45  ? 383 LYS A O   1 
ATOM   2744 C CB  . LYS A 1 396 ? 112.673 144.545 116.103 1.00 87.56  ? 383 LYS A CB  1 
ATOM   2745 C CG  . LYS A 1 396 ? 113.401 143.212 116.053 1.00 84.67  ? 383 LYS A CG  1 
ATOM   2746 C CD  . LYS A 1 396 ? 112.503 142.079 116.514 1.00 86.77  ? 383 LYS A CD  1 
ATOM   2747 C CE  . LYS A 1 396 ? 113.259 140.764 116.570 1.00 94.73  ? 383 LYS A CE  1 
ATOM   2748 N NZ  . LYS A 1 396 ? 112.401 139.665 117.089 1.00 101.19 ? 383 LYS A NZ  1 
ATOM   2749 N N   . ASP A 1 397 ? 114.555 146.446 117.723 1.00 91.40  ? 384 ASP A N   1 
ATOM   2750 C CA  . ASP A 1 397 ? 115.631 146.533 118.700 1.00 89.90  ? 384 ASP A CA  1 
ATOM   2751 C C   . ASP A 1 397 ? 116.050 145.136 119.139 1.00 89.54  ? 384 ASP A C   1 
ATOM   2752 O O   . ASP A 1 397 ? 115.207 144.293 119.457 1.00 88.04  ? 384 ASP A O   1 
ATOM   2753 C CB  . ASP A 1 397 ? 115.186 147.361 119.905 1.00 91.51  ? 384 ASP A CB  1 
ATOM   2754 C CG  . ASP A 1 397 ? 114.897 148.805 119.546 1.00 99.63  ? 384 ASP A CG  1 
ATOM   2755 O OD1 . ASP A 1 397 ? 115.520 149.318 118.593 1.00 99.91  ? 384 ASP A OD1 1 
ATOM   2756 O OD2 . ASP A 1 397 ? 114.050 149.428 120.219 1.00 109.02 ? 384 ASP A OD2 1 
ATOM   2757 N N   . LYS A 1 398 ? 117.357 144.893 119.158 1.00 89.25  ? 385 LYS A N   1 
ATOM   2758 C CA  . LYS A 1 398 ? 117.906 143.593 119.509 1.00 83.43  ? 385 LYS A CA  1 
ATOM   2759 C C   . LYS A 1 398 ? 118.592 143.675 120.865 1.00 80.12  ? 385 LYS A C   1 
ATOM   2760 O O   . LYS A 1 398 ? 119.221 144.687 121.195 1.00 76.73  ? 385 LYS A O   1 
ATOM   2761 C CB  . LYS A 1 398 ? 118.890 143.103 118.440 1.00 79.13  ? 385 LYS A CB  1 
ATOM   2762 C CG  . LYS A 1 398 ? 120.168 143.920 118.329 1.00 81.76  ? 385 LYS A CG  1 
ATOM   2763 C CD  . LYS A 1 398 ? 121.007 143.487 117.138 1.00 88.90  ? 385 LYS A CD  1 
ATOM   2764 C CE  . LYS A 1 398 ? 120.499 144.108 115.848 1.00 90.13  ? 385 LYS A CE  1 
ATOM   2765 N NZ  . LYS A 1 398 ? 120.631 145.591 115.868 1.00 87.80  ? 385 LYS A NZ  1 
ATOM   2766 N N   . ASN A 1 399 ? 118.447 142.616 121.657 1.00 75.54  ? 386 ASN A N   1 
ATOM   2767 C CA  . ASN A 1 399 ? 119.030 142.590 122.990 1.00 64.26  ? 386 ASN A CA  1 
ATOM   2768 C C   . ASN A 1 399 ? 120.549 142.516 122.914 1.00 61.48  ? 386 ASN A C   1 
ATOM   2769 O O   . ASN A 1 399 ? 121.113 141.875 122.023 1.00 64.46  ? 386 ASN A O   1 
ATOM   2770 C CB  . ASN A 1 399 ? 118.485 141.407 123.786 1.00 59.11  ? 386 ASN A CB  1 
ATOM   2771 C CG  . ASN A 1 399 ? 117.025 141.572 124.146 1.00 57.36  ? 386 ASN A CG  1 
ATOM   2772 O OD1 . ASN A 1 399 ? 116.319 142.391 123.560 1.00 59.71  ? 386 ASN A OD1 1 
ATOM   2773 N ND2 . ASN A 1 399 ? 116.565 140.794 125.118 1.00 55.85  ? 386 ASN A ND2 1 
ATOM   2774 N N   . LYS A 1 400 ? 121.212 143.182 123.861 1.00 58.82  ? 387 LYS A N   1 
ATOM   2775 C CA  . LYS A 1 400 ? 122.670 143.191 123.866 1.00 57.93  ? 387 LYS A CA  1 
ATOM   2776 C C   . LYS A 1 400 ? 123.239 141.832 124.253 1.00 56.54  ? 387 LYS A C   1 
ATOM   2777 O O   . LYS A 1 400 ? 124.300 141.442 123.753 1.00 57.08  ? 387 LYS A O   1 
ATOM   2778 C CB  . LYS A 1 400 ? 123.183 144.282 124.807 1.00 54.66  ? 387 LYS A CB  1 
ATOM   2779 C CG  . LYS A 1 400 ? 124.684 144.510 124.738 1.00 51.14  ? 387 LYS A CG  1 
ATOM   2780 C CD  . LYS A 1 400 ? 125.028 145.983 124.896 1.00 54.69  ? 387 LYS A CD  1 
ATOM   2781 C CE  . LYS A 1 400 ? 124.463 146.557 126.183 1.00 51.97  ? 387 LYS A CE  1 
ATOM   2782 N NZ  . LYS A 1 400 ? 125.034 145.895 127.385 1.00 48.52  ? 387 LYS A NZ  1 
ATOM   2783 N N   . TYR A 1 401 ? 122.556 141.099 125.128 1.00 53.86  ? 388 TYR A N   1 
ATOM   2784 C CA  . TYR A 1 401 ? 122.983 139.773 125.544 1.00 49.10  ? 388 TYR A CA  1 
ATOM   2785 C C   . TYR A 1 401 ? 121.905 138.752 125.205 1.00 55.36  ? 388 TYR A C   1 
ATOM   2786 O O   . TYR A 1 401 ? 120.722 139.088 125.093 1.00 58.60  ? 388 TYR A O   1 
ATOM   2787 C CB  . TYR A 1 401 ? 123.283 139.717 127.049 1.00 42.89  ? 388 TYR A CB  1 
ATOM   2788 C CG  . TYR A 1 401 ? 124.084 140.883 127.584 1.00 42.53  ? 388 TYR A CG  1 
ATOM   2789 C CD1 . TYR A 1 401 ? 125.468 140.913 127.475 1.00 45.51  ? 388 TYR A CD1 1 
ATOM   2790 C CD2 . TYR A 1 401 ? 123.455 141.947 128.215 1.00 41.19  ? 388 TYR A CD2 1 
ATOM   2791 C CE1 . TYR A 1 401 ? 126.199 141.977 127.969 1.00 44.02  ? 388 TYR A CE1 1 
ATOM   2792 C CE2 . TYR A 1 401 ? 124.177 143.011 128.711 1.00 42.10  ? 388 TYR A CE2 1 
ATOM   2793 C CZ  . TYR A 1 401 ? 125.547 143.022 128.586 1.00 42.72  ? 388 TYR A CZ  1 
ATOM   2794 O OH  . TYR A 1 401 ? 126.266 144.084 129.079 1.00 46.94  ? 388 TYR A OH  1 
ATOM   2795 N N   . ARG A 1 402 ? 122.325 137.503 125.039 1.00 53.81  ? 389 ARG A N   1 
ATOM   2796 C CA  . ARG A 1 402 ? 121.429 136.391 124.764 1.00 46.54  ? 389 ARG A CA  1 
ATOM   2797 C C   . ARG A 1 402 ? 121.163 135.597 126.037 1.00 43.40  ? 389 ARG A C   1 
ATOM   2798 O O   . ARG A 1 402 ? 121.891 135.701 127.027 1.00 40.69  ? 389 ARG A O   1 
ATOM   2799 C CB  . ARG A 1 402 ? 122.014 135.473 123.689 1.00 46.71  ? 389 ARG A CB  1 
ATOM   2800 C CG  . ARG A 1 402 ? 122.239 136.142 122.349 1.00 52.12  ? 389 ARG A CG  1 
ATOM   2801 C CD  . ARG A 1 402 ? 123.107 135.269 121.468 1.00 53.83  ? 389 ARG A CD  1 
ATOM   2802 N NE  . ARG A 1 402 ? 124.265 134.772 122.200 1.00 53.27  ? 389 ARG A NE  1 
ATOM   2803 C CZ  . ARG A 1 402 ? 125.393 135.447 122.372 1.00 56.90  ? 389 ARG A CZ  1 
ATOM   2804 N NH1 . ARG A 1 402 ? 125.549 136.666 121.884 1.00 64.51  ? 389 ARG A NH1 1 
ATOM   2805 N NH2 . ARG A 1 402 ? 126.389 134.883 123.049 1.00 54.89  ? 389 ARG A NH2 1 
ATOM   2806 N N   . PHE A 1 403 ? 120.102 134.793 126.000 1.00 44.37  ? 390 PHE A N   1 
ATOM   2807 C CA  . PHE A 1 403 ? 119.680 134.058 127.183 1.00 42.15  ? 390 PHE A CA  1 
ATOM   2808 C C   . PHE A 1 403 ? 118.808 132.882 126.771 1.00 45.01  ? 390 PHE A C   1 
ATOM   2809 O O   . PHE A 1 403 ? 118.307 132.817 125.646 1.00 48.98  ? 390 PHE A O   1 
ATOM   2810 C CB  . PHE A 1 403 ? 118.928 134.967 128.157 1.00 38.38  ? 390 PHE A CB  1 
ATOM   2811 C CG  . PHE A 1 403 ? 117.740 135.648 127.549 1.00 41.36  ? 390 PHE A CG  1 
ATOM   2812 C CD1 . PHE A 1 403 ? 117.880 136.853 126.885 1.00 42.58  ? 390 PHE A CD1 1 
ATOM   2813 C CD2 . PHE A 1 403 ? 116.482 135.080 127.636 1.00 47.88  ? 390 PHE A CD2 1 
ATOM   2814 C CE1 . PHE A 1 403 ? 116.788 137.480 126.321 1.00 46.25  ? 390 PHE A CE1 1 
ATOM   2815 C CE2 . PHE A 1 403 ? 115.384 135.704 127.076 1.00 50.44  ? 390 PHE A CE2 1 
ATOM   2816 C CZ  . PHE A 1 403 ? 115.538 136.905 126.417 1.00 49.94  ? 390 PHE A CZ  1 
ATOM   2817 N N   . GLU A 1 404 ? 118.637 131.950 127.708 1.00 40.64  ? 391 GLU A N   1 
ATOM   2818 C CA  . GLU A 1 404 ? 117.719 130.831 127.560 1.00 42.74  ? 391 GLU A CA  1 
ATOM   2819 C C   . GLU A 1 404 ? 116.908 130.700 128.839 1.00 42.90  ? 391 GLU A C   1 
ATOM   2820 O O   . GLU A 1 404 ? 117.436 130.890 129.937 1.00 45.58  ? 391 GLU A O   1 
ATOM   2821 C CB  . GLU A 1 404 ? 118.454 129.518 127.265 1.00 45.67  ? 391 GLU A CB  1 
ATOM   2822 C CG  . GLU A 1 404 ? 117.526 128.319 127.128 1.00 50.26  ? 391 GLU A CG  1 
ATOM   2823 C CD  . GLU A 1 404 ? 118.108 127.212 126.271 1.00 61.07  ? 391 GLU A CD  1 
ATOM   2824 O OE1 . GLU A 1 404 ? 119.341 127.192 126.075 1.00 64.30  ? 391 GLU A OE1 1 
ATOM   2825 O OE2 . GLU A 1 404 ? 117.327 126.366 125.786 1.00 65.90  ? 391 GLU A OE2 1 
ATOM   2826 N N   . ILE A 1 405 ? 115.629 130.372 128.690 1.00 44.11  ? 392 ILE A N   1 
ATOM   2827 C CA  . ILE A 1 405 ? 114.681 130.349 129.797 1.00 47.28  ? 392 ILE A CA  1 
ATOM   2828 C C   . ILE A 1 405 ? 114.153 128.931 129.970 1.00 54.47  ? 392 ILE A C   1 
ATOM   2829 O O   . ILE A 1 405 ? 113.754 128.288 128.993 1.00 55.71  ? 392 ILE A O   1 
ATOM   2830 C CB  . ILE A 1 405 ? 113.523 131.336 129.561 1.00 46.84  ? 392 ILE A CB  1 
ATOM   2831 C CG1 . ILE A 1 405 ? 114.065 132.743 129.308 1.00 42.58  ? 392 ILE A CG1 1 
ATOM   2832 C CG2 . ILE A 1 405 ? 112.566 131.329 130.739 1.00 46.75  ? 392 ILE A CG2 1 
ATOM   2833 C CD1 . ILE A 1 405 ? 114.989 133.239 130.385 1.00 43.47  ? 392 ILE A CD1 1 
ATOM   2834 N N   . MET A 1 406 ? 114.161 128.446 131.211 1.00 55.90  ? 393 MET A N   1 
ATOM   2835 C CA  . MET A 1 406 ? 113.493 127.202 131.582 1.00 56.22  ? 393 MET A CA  1 
ATOM   2836 C C   . MET A 1 406 ? 112.853 127.409 132.951 1.00 56.08  ? 393 MET A C   1 
ATOM   2837 O O   . MET A 1 406 ? 112.666 128.542 133.404 1.00 52.61  ? 393 MET A O   1 
ATOM   2838 C CB  . MET A 1 406 ? 114.460 126.011 131.564 1.00 54.57  ? 393 MET A CB  1 
ATOM   2839 C CG  . MET A 1 406 ? 115.640 126.147 132.500 1.00 47.16  ? 393 MET A CG  1 
ATOM   2840 S SD  . MET A 1 406 ? 116.961 127.047 131.690 1.00 39.07  ? 393 MET A SD  1 
ATOM   2841 C CE  . MET A 1 406 ? 117.187 126.024 130.238 1.00 48.65  ? 393 MET A CE  1 
ATOM   2842 N N   . GLY A 1 407 ? 112.491 126.312 133.611 1.00 60.59  ? 394 GLY A N   1 
ATOM   2843 C CA  . GLY A 1 407 ? 111.845 126.421 134.905 1.00 63.44  ? 394 GLY A CA  1 
ATOM   2844 C C   . GLY A 1 407 ? 112.501 125.650 136.034 1.00 60.57  ? 394 GLY A C   1 
ATOM   2845 O O   . GLY A 1 407 ? 113.729 125.638 136.175 1.00 58.91  ? 394 GLY A O   1 
ATOM   2846 N N   . GLU A 1 408 ? 111.674 125.003 136.851 1.00 62.74  ? 395 GLU A N   1 
ATOM   2847 C CA  . GLU A 1 408 ? 112.113 124.259 138.021 1.00 65.32  ? 395 GLU A CA  1 
ATOM   2848 C C   . GLU A 1 408 ? 112.467 122.810 137.683 1.00 63.04  ? 395 GLU A C   1 
ATOM   2849 O O   . GLU A 1 408 ? 112.148 121.899 138.458 1.00 62.10  ? 395 GLU A O   1 
ATOM   2850 C CB  . GLU A 1 408 ? 111.030 124.325 139.100 1.00 67.34  ? 395 GLU A CB  1 
ATOM   2851 C CG  . GLU A 1 408 ? 111.496 124.051 140.518 1.00 62.14  ? 395 GLU A CG  1 
ATOM   2852 C CD  . GLU A 1 408 ? 110.852 122.809 141.095 1.00 72.91  ? 395 GLU A CD  1 
ATOM   2853 O OE1 . GLU A 1 408 ? 110.112 122.123 140.357 1.00 75.72  ? 395 GLU A OE1 1 
ATOM   2854 O OE2 . GLU A 1 408 ? 111.078 122.521 142.288 1.00 73.92  ? 395 GLU A OE2 1 
ATOM   2855 N N   . GLU A 1 409 ? 113.077 122.582 136.517 1.00 61.86  ? 396 GLU A N   1 
ATOM   2856 C CA  . GLU A 1 409 ? 113.334 121.225 136.042 1.00 64.02  ? 396 GLU A CA  1 
ATOM   2857 C C   . GLU A 1 409 ? 114.155 120.414 137.038 1.00 64.69  ? 396 GLU A C   1 
ATOM   2858 O O   . GLU A 1 409 ? 113.783 119.289 137.390 1.00 65.25  ? 396 GLU A O   1 
ATOM   2859 C CB  . GLU A 1 409 ? 114.037 121.275 134.684 1.00 64.93  ? 396 GLU A CB  1 
ATOM   2860 C CG  . GLU A 1 409 ? 113.884 120.002 133.850 1.00 70.13  ? 396 GLU A CG  1 
ATOM   2861 C CD  . GLU A 1 409 ? 112.446 119.740 133.424 1.00 72.59  ? 396 GLU A CD  1 
ATOM   2862 O OE1 . GLU A 1 409 ? 111.624 119.333 134.272 1.00 75.22  ? 396 GLU A OE1 1 
ATOM   2863 O OE2 . GLU A 1 409 ? 112.131 119.949 132.234 1.00 68.02  ? 396 GLU A OE2 1 
ATOM   2864 N N   . GLU A 1 410 ? 115.280 120.960 137.498 1.00 62.37  ? 397 GLU A N   1 
ATOM   2865 C CA  . GLU A 1 410 ? 116.214 120.223 138.352 1.00 59.12  ? 397 GLU A CA  1 
ATOM   2866 C C   . GLU A 1 410 ? 116.628 121.062 139.555 1.00 57.59  ? 397 GLU A C   1 
ATOM   2867 O O   . GLU A 1 410 ? 117.804 121.141 139.915 1.00 55.60  ? 397 GLU A O   1 
ATOM   2868 C CB  . GLU A 1 410 ? 117.449 119.783 137.569 1.00 52.91  ? 397 GLU A CB  1 
ATOM   2869 C CG  . GLU A 1 410 ? 117.160 119.064 136.261 1.00 62.87  ? 397 GLU A CG  1 
ATOM   2870 C CD  . GLU A 1 410 ? 116.540 117.694 136.460 1.00 74.01  ? 397 GLU A CD  1 
ATOM   2871 O OE1 . GLU A 1 410 ? 116.685 117.119 137.559 1.00 71.11  ? 397 GLU A OE1 1 
ATOM   2872 O OE2 . GLU A 1 410 ? 115.905 117.190 135.510 1.00 75.23  ? 397 GLU A OE2 1 
ATOM   2873 N N   . ILE A 1 411 ? 115.655 121.696 140.203 1.00 58.26  ? 398 ILE A N   1 
ATOM   2874 C CA  . ILE A 1 411 ? 115.893 122.553 141.359 1.00 49.51  ? 398 ILE A CA  1 
ATOM   2875 C C   . ILE A 1 411 ? 115.083 122.022 142.532 1.00 50.70  ? 398 ILE A C   1 
ATOM   2876 O O   . ILE A 1 411 ? 113.859 121.882 142.433 1.00 59.70  ? 398 ILE A O   1 
ATOM   2877 C CB  . ILE A 1 411 ? 115.524 124.016 141.057 1.00 47.44  ? 398 ILE A CB  1 
ATOM   2878 C CG1 . ILE A 1 411 ? 116.444 124.577 139.975 1.00 45.56  ? 398 ILE A CG1 1 
ATOM   2879 C CG2 . ILE A 1 411 ? 115.593 124.856 142.319 1.00 47.57  ? 398 ILE A CG2 1 
ATOM   2880 C CD1 . ILE A 1 411 ? 115.717 125.404 138.951 1.00 50.37  ? 398 ILE A CD1 1 
ATOM   2881 N N   . ALA A 1 412 ? 115.763 121.738 143.643 1.00 46.99  ? 399 ALA A N   1 
ATOM   2882 C CA  . ALA A 1 412 ? 115.123 121.159 144.823 1.00 49.97  ? 399 ALA A CA  1 
ATOM   2883 C C   . ALA A 1 412 ? 114.878 122.257 145.853 1.00 55.28  ? 399 ALA A C   1 
ATOM   2884 O O   . ALA A 1 412 ? 115.622 122.424 146.818 1.00 56.39  ? 399 ALA A O   1 
ATOM   2885 C CB  . ALA A 1 412 ? 115.976 120.036 145.398 1.00 53.05  ? 399 ALA A CB  1 
ATOM   2886 N N   . PHE A 1 413 ? 113.806 123.015 145.643 1.00 59.86  ? 400 PHE A N   1 
ATOM   2887 C CA  . PHE A 1 413 ? 113.392 124.014 146.626 1.00 63.06  ? 400 PHE A CA  1 
ATOM   2888 C C   . PHE A 1 413 ? 112.552 123.305 147.680 1.00 65.75  ? 400 PHE A C   1 
ATOM   2889 O O   . PHE A 1 413 ? 111.323 123.258 147.604 1.00 70.76  ? 400 PHE A O   1 
ATOM   2890 C CB  . PHE A 1 413 ? 112.630 125.154 145.965 1.00 70.14  ? 400 PHE A CB  1 
ATOM   2891 C CG  . PHE A 1 413 ? 112.085 126.158 146.938 1.00 73.37  ? 400 PHE A CG  1 
ATOM   2892 C CD1 . PHE A 1 413 ? 112.933 126.841 147.793 1.00 73.08  ? 400 PHE A CD1 1 
ATOM   2893 C CD2 . PHE A 1 413 ? 110.727 126.419 146.997 1.00 76.66  ? 400 PHE A CD2 1 
ATOM   2894 C CE1 . PHE A 1 413 ? 112.436 127.763 148.691 1.00 73.12  ? 400 PHE A CE1 1 
ATOM   2895 C CE2 . PHE A 1 413 ? 110.223 127.341 147.893 1.00 78.22  ? 400 PHE A CE2 1 
ATOM   2896 C CZ  . PHE A 1 413 ? 111.079 128.014 148.741 1.00 76.47  ? 400 PHE A CZ  1 
ATOM   2897 N N   . LYS A 1 414 ? 113.230 122.748 148.679 1.00 66.58  ? 401 LYS A N   1 
ATOM   2898 C CA  . LYS A 1 414 ? 112.592 121.966 149.730 1.00 71.07  ? 401 LYS A CA  1 
ATOM   2899 C C   . LYS A 1 414 ? 112.422 122.823 150.975 1.00 79.65  ? 401 LYS A C   1 
ATOM   2900 O O   . LYS A 1 414 ? 113.370 123.482 151.415 1.00 80.99  ? 401 LYS A O   1 
ATOM   2901 C CB  . LYS A 1 414 ? 113.417 120.721 150.056 1.00 66.39  ? 401 LYS A CB  1 
ATOM   2902 C CG  . LYS A 1 414 ? 113.740 119.862 148.849 1.00 64.40  ? 401 LYS A CG  1 
ATOM   2903 C CD  . LYS A 1 414 ? 112.474 119.398 148.154 1.00 66.51  ? 401 LYS A CD  1 
ATOM   2904 C CE  . LYS A 1 414 ? 112.782 118.453 147.008 1.00 66.69  ? 401 LYS A CE  1 
ATOM   2905 N NZ  . LYS A 1 414 ? 111.543 117.851 146.442 1.00 70.01  ? 401 LYS A NZ  1 
ATOM   2906 N N   . MET A 1 415 ? 111.221 122.803 151.544 1.00 84.03  ? 402 MET A N   1 
ATOM   2907 C CA  . MET A 1 415 ? 110.873 123.627 152.694 1.00 92.63  ? 402 MET A CA  1 
ATOM   2908 C C   . MET A 1 415 ? 110.803 122.763 153.945 1.00 94.94  ? 402 MET A C   1 
ATOM   2909 O O   . MET A 1 415 ? 110.157 121.710 153.942 1.00 94.64  ? 402 MET A O   1 
ATOM   2910 C CB  . MET A 1 415 ? 109.537 124.339 152.469 1.00 94.62  ? 402 MET A CB  1 
ATOM   2911 C CG  . MET A 1 415 ? 109.236 125.420 153.493 1.00 99.24  ? 402 MET A CG  1 
ATOM   2912 S SD  . MET A 1 415 ? 110.573 126.626 153.591 1.00 99.89  ? 402 MET A SD  1 
ATOM   2913 C CE  . MET A 1 415 ? 109.886 127.824 154.729 1.00 102.29 ? 402 MET A CE  1 
ATOM   2914 N N   . ILE A 1 416 ? 111.468 123.208 155.006 1.00 98.01  ? 403 ILE A N   1 
ATOM   2915 C CA  . ILE A 1 416 ? 111.451 122.510 156.287 1.00 100.10 ? 403 ILE A CA  1 
ATOM   2916 C C   . ILE A 1 416 ? 110.404 123.164 157.180 1.00 104.02 ? 403 ILE A C   1 
ATOM   2917 O O   . ILE A 1 416 ? 110.533 124.337 157.547 1.00 104.41 ? 403 ILE A O   1 
ATOM   2918 C CB  . ILE A 1 416 ? 112.834 122.531 156.951 1.00 99.97  ? 403 ILE A CB  1 
ATOM   2919 C CG1 . ILE A 1 416 ? 113.873 121.895 156.029 1.00 95.49  ? 403 ILE A CG1 1 
ATOM   2920 C CG2 . ILE A 1 416 ? 112.786 121.812 158.290 1.00 100.19 ? 403 ILE A CG2 1 
ATOM   2921 C CD1 . ILE A 1 416 ? 113.547 120.473 155.633 1.00 91.27  ? 403 ILE A CD1 1 
ATOM   2922 N N   . ARG A 1 417 ? 109.372 122.401 157.538 1.00 105.99 ? 404 ARG A N   1 
ATOM   2923 C CA  . ARG A 1 417 ? 108.246 122.910 158.308 1.00 110.32 ? 404 ARG A CA  1 
ATOM   2924 C C   . ARG A 1 417 ? 108.197 122.358 159.725 1.00 107.28 ? 404 ARG A C   1 
ATOM   2925 O O   . ARG A 1 417 ? 107.149 122.449 160.376 1.00 106.57 ? 404 ARG A O   1 
ATOM   2926 C CB  . ARG A 1 417 ? 106.937 122.608 157.578 1.00 108.85 ? 404 ARG A CB  1 
ATOM   2927 C CG  . ARG A 1 417 ? 106.918 121.255 156.893 1.00 103.96 ? 404 ARG A CG  1 
ATOM   2928 C CD  . ARG A 1 417 ? 105.686 121.095 156.023 1.00 102.78 ? 404 ARG A CD  1 
ATOM   2929 N NE  . ARG A 1 417 ? 105.738 119.869 155.238 1.00 104.76 ? 404 ARG A NE  1 
ATOM   2930 C CZ  . ARG A 1 417 ? 106.289 119.773 154.036 1.00 103.58 ? 404 ARG A CZ  1 
ATOM   2931 N NH1 . ARG A 1 417 ? 106.842 120.819 153.444 1.00 102.83 ? 404 ARG A NH1 1 
ATOM   2932 N NH2 . ARG A 1 417 ? 106.287 118.598 153.412 1.00 101.21 ? 404 ARG A NH2 1 
ATOM   2933 N N   . THR A 1 418 ? 109.297 121.785 160.215 1.00 104.00 ? 405 THR A N   1 
ATOM   2934 C CA  . THR A 1 418 ? 109.378 121.245 161.573 1.00 106.58 ? 405 THR A CA  1 
ATOM   2935 C C   . THR A 1 418 ? 108.358 120.125 161.786 1.00 107.07 ? 405 THR A C   1 
ATOM   2936 O O   . THR A 1 418 ? 107.601 120.113 162.758 1.00 111.14 ? 405 THR A O   1 
ATOM   2937 C CB  . THR A 1 418 ? 109.208 122.353 162.616 1.00 112.67 ? 405 THR A CB  1 
ATOM   2938 O OG1 . THR A 1 418 ? 109.500 121.833 163.920 1.00 117.27 ? 405 THR A OG1 1 
ATOM   2939 C CG2 . THR A 1 418 ? 107.783 122.875 162.603 1.00 112.20 ? 405 THR A CG2 1 
ATOM   2940 N N   . ASN A 1 419 ? 108.353 119.167 160.858 1.00 106.68 ? 406 ASN A N   1 
ATOM   2941 C CA  . ASN A 1 419 ? 107.511 117.975 160.968 1.00 107.19 ? 406 ASN A CA  1 
ATOM   2942 C C   . ASN A 1 419 ? 108.318 116.826 160.368 1.00 101.74 ? 406 ASN A C   1 
ATOM   2943 O O   . ASN A 1 419 ? 108.397 116.696 159.142 1.00 98.40  ? 406 ASN A O   1 
ATOM   2944 C CB  . ASN A 1 419 ? 106.174 118.165 160.262 1.00 108.60 ? 406 ASN A CB  1 
ATOM   2945 C CG  . ASN A 1 419 ? 105.179 117.059 160.581 1.00 107.92 ? 406 ASN A CG  1 
ATOM   2946 O OD1 . ASN A 1 419 ? 105.499 116.102 161.284 1.00 107.26 ? 406 ASN A OD1 1 
ATOM   2947 N ND2 . ASN A 1 419 ? 103.957 117.195 160.069 1.00 110.80 ? 406 ASN A ND2 1 
ATOM   2948 N N   . VAL A 1 420 ? 108.907 116.003 161.241 1.00 102.82 ? 407 VAL A N   1 
ATOM   2949 C CA  . VAL A 1 420 ? 109.873 114.999 160.803 1.00 102.91 ? 407 VAL A CA  1 
ATOM   2950 C C   . VAL A 1 420 ? 109.250 114.034 159.805 1.00 96.74  ? 407 VAL A C   1 
ATOM   2951 O O   . VAL A 1 420 ? 109.935 113.534 158.904 1.00 92.41  ? 407 VAL A O   1 
ATOM   2952 C CB  . VAL A 1 420 ? 110.458 114.261 162.026 1.00 105.24 ? 407 VAL A CB  1 
ATOM   2953 C CG1 . VAL A 1 420 ? 109.366 113.516 162.784 1.00 100.53 ? 407 VAL A CG1 1 
ATOM   2954 C CG2 . VAL A 1 420 ? 111.574 113.317 161.603 1.00 98.60  ? 407 VAL A CG2 1 
ATOM   2955 N N   . SER A 1 421 ? 107.944 113.780 159.924 1.00 95.67  ? 408 SER A N   1 
ATOM   2956 C CA  . SER A 1 421 ? 107.268 112.918 158.961 1.00 95.27  ? 408 SER A CA  1 
ATOM   2957 C C   . SER A 1 421 ? 107.343 113.501 157.556 1.00 95.48  ? 408 SER A C   1 
ATOM   2958 O O   . SER A 1 421 ? 107.452 112.761 156.571 1.00 91.98  ? 408 SER A O   1 
ATOM   2959 C CB  . SER A 1 421 ? 105.812 112.707 159.377 1.00 98.12  ? 408 SER A CB  1 
ATOM   2960 O OG  . SER A 1 421 ? 105.094 113.928 159.352 1.00 101.45 ? 408 SER A OG  1 
ATOM   2961 N N   . HIS A 1 422 ? 107.283 114.828 157.443 1.00 97.02  ? 409 HIS A N   1 
ATOM   2962 C CA  . HIS A 1 422 ? 107.416 115.491 156.153 1.00 92.53  ? 409 HIS A CA  1 
ATOM   2963 C C   . HIS A 1 422 ? 108.864 115.789 155.793 1.00 86.48  ? 409 HIS A C   1 
ATOM   2964 O O   . HIS A 1 422 ? 109.208 115.809 154.604 1.00 83.83  ? 409 HIS A O   1 
ATOM   2965 C CB  . HIS A 1 422 ? 106.602 116.786 156.150 1.00 96.57  ? 409 HIS A CB  1 
ATOM   2966 C CG  . HIS A 1 422 ? 105.136 116.570 156.354 1.00 102.73 ? 409 HIS A CG  1 
ATOM   2967 N ND1 . HIS A 1 422 ? 104.519 115.369 156.080 1.00 101.15 ? 409 HIS A ND1 1 
ATOM   2968 C CD2 . HIS A 1 422 ? 104.166 117.396 156.812 1.00 108.59 ? 409 HIS A CD2 1 
ATOM   2969 C CE1 . HIS A 1 422 ? 103.231 115.465 156.355 1.00 103.93 ? 409 HIS A CE1 1 
ATOM   2970 N NE2 . HIS A 1 422 ? 102.991 116.685 156.801 1.00 111.67 ? 409 HIS A NE2 1 
ATOM   2971 N N   . VAL A 1 423 ? 109.723 116.010 156.790 1.00 86.02  ? 410 VAL A N   1 
ATOM   2972 C CA  . VAL A 1 423 ? 111.139 116.240 156.513 1.00 83.50  ? 410 VAL A CA  1 
ATOM   2973 C C   . VAL A 1 423 ? 111.761 115.002 155.879 1.00 78.64  ? 410 VAL A C   1 
ATOM   2974 O O   . VAL A 1 423 ? 112.506 115.093 154.894 1.00 75.72  ? 410 VAL A O   1 
ATOM   2975 C CB  . VAL A 1 423 ? 111.882 116.648 157.797 1.00 81.37  ? 410 VAL A CB  1 
ATOM   2976 C CG1 . VAL A 1 423 ? 113.361 116.847 157.510 1.00 76.26  ? 410 VAL A CG1 1 
ATOM   2977 C CG2 . VAL A 1 423 ? 111.276 117.912 158.381 1.00 87.25  ? 410 VAL A CG2 1 
ATOM   2978 N N   . VAL A 1 424 ? 111.463 113.824 156.434 1.00 77.24  ? 411 VAL A N   1 
ATOM   2979 C CA  . VAL A 1 424 ? 112.003 112.597 155.858 1.00 73.09  ? 411 VAL A CA  1 
ATOM   2980 C C   . VAL A 1 424 ? 111.441 112.373 154.464 1.00 74.38  ? 411 VAL A C   1 
ATOM   2981 O O   . VAL A 1 424 ? 112.143 111.873 153.581 1.00 70.48  ? 411 VAL A O   1 
ATOM   2982 C CB  . VAL A 1 424 ? 111.742 111.388 156.781 1.00 74.99  ? 411 VAL A CB  1 
ATOM   2983 C CG1 . VAL A 1 424 ? 112.399 111.604 158.134 1.00 79.01  ? 411 VAL A CG1 1 
ATOM   2984 C CG2 . VAL A 1 424 ? 110.252 111.119 156.933 1.00 78.06  ? 411 VAL A CG2 1 
ATOM   2985 N N   . GLY A 1 425 ? 110.181 112.748 154.234 1.00 80.51  ? 412 GLY A N   1 
ATOM   2986 C CA  . GLY A 1 425 ? 109.621 112.626 152.898 1.00 80.80  ? 412 GLY A CA  1 
ATOM   2987 C C   . GLY A 1 425 ? 110.337 113.504 151.890 1.00 77.59  ? 412 GLY A C   1 
ATOM   2988 O O   . GLY A 1 425 ? 110.648 113.070 150.779 1.00 75.43  ? 412 GLY A O   1 
ATOM   2989 N N   . GLN A 1 426 ? 110.617 114.752 152.271 1.00 75.62  ? 413 GLN A N   1 
ATOM   2990 C CA  . GLN A 1 426 ? 111.347 115.648 151.378 1.00 72.49  ? 413 GLN A CA  1 
ATOM   2991 C C   . GLN A 1 426 ? 112.754 115.125 151.102 1.00 69.64  ? 413 GLN A C   1 
ATOM   2992 O O   . GLN A 1 426 ? 113.229 115.155 149.957 1.00 70.33  ? 413 GLN A O   1 
ATOM   2993 C CB  . GLN A 1 426 ? 111.408 117.052 151.981 1.00 73.54  ? 413 GLN A CB  1 
ATOM   2994 C CG  . GLN A 1 426 ? 110.052 117.701 152.197 1.00 79.24  ? 413 GLN A CG  1 
ATOM   2995 C CD  . GLN A 1 426 ? 109.399 118.136 150.903 1.00 83.38  ? 413 GLN A CD  1 
ATOM   2996 O OE1 . GLN A 1 426 ? 110.076 118.536 149.959 1.00 78.05  ? 413 GLN A OE1 1 
ATOM   2997 N NE2 . GLN A 1 426 ? 108.075 118.059 150.853 1.00 90.15  ? 413 GLN A NE2 1 
ATOM   2998 N N   . LEU A 1 427 ? 113.435 114.634 152.140 1.00 67.22  ? 414 LEU A N   1 
ATOM   2999 C CA  . LEU A 1 427 ? 114.788 114.123 151.949 1.00 65.60  ? 414 LEU A CA  1 
ATOM   3000 C C   . LEU A 1 427 ? 114.788 112.869 151.083 1.00 68.24  ? 414 LEU A C   1 
ATOM   3001 O O   . LEU A 1 427 ? 115.697 112.668 150.271 1.00 68.00  ? 414 LEU A O   1 
ATOM   3002 C CB  . LEU A 1 427 ? 115.441 113.860 153.303 1.00 68.45  ? 414 LEU A CB  1 
ATOM   3003 C CG  . LEU A 1 427 ? 115.604 115.116 154.160 1.00 64.57  ? 414 LEU A CG  1 
ATOM   3004 C CD1 . LEU A 1 427 ? 116.219 114.780 155.504 1.00 69.25  ? 414 LEU A CD1 1 
ATOM   3005 C CD2 . LEU A 1 427 ? 116.434 116.158 153.430 1.00 58.79  ? 414 LEU A CD2 1 
ATOM   3006 N N   . ASP A 1 428 ? 113.774 112.014 151.234 1.00 67.48  ? 415 ASP A N   1 
ATOM   3007 C CA  . ASP A 1 428 ? 113.650 110.850 150.364 1.00 62.98  ? 415 ASP A CA  1 
ATOM   3008 C C   . ASP A 1 428 ? 113.346 111.264 148.932 1.00 64.99  ? 415 ASP A C   1 
ATOM   3009 O O   . ASP A 1 428 ? 113.782 110.602 147.984 1.00 63.93  ? 415 ASP A O   1 
ATOM   3010 C CB  . ASP A 1 428 ? 112.568 109.914 150.896 1.00 65.78  ? 415 ASP A CB  1 
ATOM   3011 C CG  . ASP A 1 428 ? 112.902 109.361 152.262 1.00 65.84  ? 415 ASP A CG  1 
ATOM   3012 O OD1 . ASP A 1 428 ? 114.104 109.220 152.565 1.00 62.79  ? 415 ASP A OD1 1 
ATOM   3013 O OD2 . ASP A 1 428 ? 111.967 109.077 153.037 1.00 72.36  ? 415 ASP A OD2 1 
ATOM   3014 N N   . ASP A 1 429 ? 112.582 112.344 148.756 1.00 69.17  ? 416 ASP A N   1 
ATOM   3015 C CA  . ASP A 1 429 ? 112.350 112.873 147.416 1.00 72.14  ? 416 ASP A CA  1 
ATOM   3016 C C   . ASP A 1 429 ? 113.658 113.319 146.781 1.00 70.88  ? 416 ASP A C   1 
ATOM   3017 O O   . ASP A 1 429 ? 113.891 113.090 145.588 1.00 70.88  ? 416 ASP A O   1 
ATOM   3018 C CB  . ASP A 1 429 ? 111.360 114.039 147.469 1.00 76.07  ? 416 ASP A CB  1 
ATOM   3019 C CG  . ASP A 1 429 ? 110.722 114.324 146.122 1.00 82.60  ? 416 ASP A CG  1 
ATOM   3020 O OD1 . ASP A 1 429 ? 109.477 114.249 146.017 1.00 89.17  ? 416 ASP A OD1 1 
ATOM   3021 O OD2 . ASP A 1 429 ? 111.468 114.599 145.159 1.00 79.52  ? 416 ASP A OD2 1 
ATOM   3022 N N   . ILE A 1 430 ? 114.517 113.974 147.565 1.00 69.43  ? 417 ILE A N   1 
ATOM   3023 C CA  . ILE A 1 430 ? 115.836 114.355 147.062 1.00 64.78  ? 417 ILE A CA  1 
ATOM   3024 C C   . ILE A 1 430 ? 116.661 113.117 146.729 1.00 61.27  ? 417 ILE A C   1 
ATOM   3025 O O   . ILE A 1 430 ? 117.331 113.058 145.692 1.00 59.23  ? 417 ILE A O   1 
ATOM   3026 C CB  . ILE A 1 430 ? 116.561 115.254 148.079 1.00 62.59  ? 417 ILE A CB  1 
ATOM   3027 C CG1 . ILE A 1 430 ? 115.792 116.559 148.282 1.00 61.07  ? 417 ILE A CG1 1 
ATOM   3028 C CG2 . ILE A 1 430 ? 117.984 115.529 147.621 1.00 58.09  ? 417 ILE A CG2 1 
ATOM   3029 C CD1 . ILE A 1 430 ? 116.531 117.578 149.119 1.00 61.04  ? 417 ILE A CD1 1 
ATOM   3030 N N   . ARG A 1 431 ? 116.627 112.112 147.606 1.00 61.30  ? 418 ARG A N   1 
ATOM   3031 C CA  . ARG A 1 431 ? 117.503 110.956 147.447 1.00 60.21  ? 418 ARG A CA  1 
ATOM   3032 C C   . ARG A 1 431 ? 117.103 110.096 146.253 1.00 61.96  ? 418 ARG A C   1 
ATOM   3033 O O   . ARG A 1 431 ? 117.970 109.634 145.502 1.00 61.19  ? 418 ARG A O   1 
ATOM   3034 C CB  . ARG A 1 431 ? 117.517 110.130 148.733 1.00 57.39  ? 418 ARG A CB  1 
ATOM   3035 C CG  . ARG A 1 431 ? 118.521 110.625 149.762 1.00 57.04  ? 418 ARG A CG  1 
ATOM   3036 C CD  . ARG A 1 431 ? 118.508 109.787 151.028 1.00 54.70  ? 418 ARG A CD  1 
ATOM   3037 N NE  . ARG A 1 431 ? 117.552 110.294 152.005 1.00 51.56  ? 418 ARG A NE  1 
ATOM   3038 C CZ  . ARG A 1 431 ? 117.550 109.964 153.288 1.00 53.17  ? 418 ARG A CZ  1 
ATOM   3039 N NH1 . ARG A 1 431 ? 118.438 109.120 153.787 1.00 51.29  ? 418 ARG A NH1 1 
ATOM   3040 N NH2 . ARG A 1 431 ? 116.637 110.499 154.093 1.00 57.71  ? 418 ARG A NH2 1 
ATOM   3041 N N   . LYS A 1 432 ? 115.802 109.853 146.063 1.00 61.55  ? 419 LYS A N   1 
ATOM   3042 C CA  . LYS A 1 432 ? 115.367 109.051 144.922 1.00 60.63  ? 419 LYS A CA  1 
ATOM   3043 C C   . LYS A 1 432 ? 115.651 109.764 143.606 1.00 63.70  ? 419 LYS A C   1 
ATOM   3044 O O   . LYS A 1 432 ? 116.119 109.146 142.643 1.00 67.27  ? 419 LYS A O   1 
ATOM   3045 C CB  . LYS A 1 432 ? 113.881 108.708 145.036 1.00 63.86  ? 419 LYS A CB  1 
ATOM   3046 C CG  . LYS A 1 432 ? 113.318 108.070 143.766 1.00 66.41  ? 419 LYS A CG  1 
ATOM   3047 C CD  . LYS A 1 432 ? 112.165 107.115 144.040 1.00 64.81  ? 419 LYS A CD  1 
ATOM   3048 C CE  . LYS A 1 432 ? 110.907 107.847 144.459 1.00 65.31  ? 419 LYS A CE  1 
ATOM   3049 N NZ  . LYS A 1 432 ? 109.802 106.900 144.772 1.00 74.55  ? 419 LYS A NZ  1 
ATOM   3050 N N   . ASN A 1 433 ? 115.373 111.067 143.545 1.00 63.31  ? 420 ASN A N   1 
ATOM   3051 C CA  . ASN A 1 433 ? 115.591 111.866 142.343 1.00 59.35  ? 420 ASN A CA  1 
ATOM   3052 C C   . ASN A 1 433 ? 116.724 112.848 142.606 1.00 56.67  ? 420 ASN A C   1 
ATOM   3053 O O   . ASN A 1 433 ? 116.483 113.967 143.081 1.00 59.67  ? 420 ASN A O   1 
ATOM   3054 C CB  . ASN A 1 433 ? 114.315 112.612 141.941 1.00 63.35  ? 420 ASN A CB  1 
ATOM   3055 C CG  . ASN A 1 433 ? 113.059 111.799 142.183 1.00 71.41  ? 420 ASN A CG  1 
ATOM   3056 O OD1 . ASN A 1 433 ? 112.656 110.989 141.348 1.00 72.53  ? 420 ASN A OD1 1 
ATOM   3057 N ND2 . ASN A 1 433 ? 112.426 112.021 143.329 1.00 71.40  ? 420 ASN A ND2 1 
ATOM   3058 N N   . PRO A 1 434 ? 117.974 112.483 142.325 1.00 51.84  ? 421 PRO A N   1 
ATOM   3059 C CA  . PRO A 1 434 ? 119.074 113.436 142.510 1.00 48.88  ? 421 PRO A CA  1 
ATOM   3060 C C   . PRO A 1 434 ? 118.902 114.639 141.596 1.00 52.90  ? 421 PRO A C   1 
ATOM   3061 O O   . PRO A 1 434 ? 118.445 114.518 140.458 1.00 58.28  ? 421 PRO A O   1 
ATOM   3062 C CB  . PRO A 1 434 ? 120.317 112.617 142.148 1.00 40.46  ? 421 PRO A CB  1 
ATOM   3063 C CG  . PRO A 1 434 ? 119.810 111.553 141.240 1.00 46.10  ? 421 PRO A CG  1 
ATOM   3064 C CD  . PRO A 1 434 ? 118.434 111.214 141.736 1.00 52.43  ? 421 PRO A CD  1 
ATOM   3065 N N   . ARG A 1 435 ? 119.270 115.812 142.105 1.00 43.82  ? 422 ARG A N   1 
ATOM   3066 C CA  . ARG A 1 435 ? 119.041 117.060 141.394 1.00 43.43  ? 422 ARG A CA  1 
ATOM   3067 C C   . ARG A 1 435 ? 120.313 117.894 141.411 1.00 42.69  ? 422 ARG A C   1 
ATOM   3068 O O   . ARG A 1 435 ? 121.174 117.722 142.276 1.00 40.32  ? 422 ARG A O   1 
ATOM   3069 C CB  . ARG A 1 435 ? 117.865 117.838 142.004 1.00 47.82  ? 422 ARG A CB  1 
ATOM   3070 C CG  . ARG A 1 435 ? 116.566 117.040 142.042 1.00 48.95  ? 422 ARG A CG  1 
ATOM   3071 C CD  . ARG A 1 435 ? 115.441 117.795 142.724 1.00 50.97  ? 422 ARG A CD  1 
ATOM   3072 N NE  . ARG A 1 435 ? 114.377 116.899 143.162 1.00 60.78  ? 422 ARG A NE  1 
ATOM   3073 C CZ  . ARG A 1 435 ? 113.229 116.722 142.524 1.00 69.49  ? 422 ARG A CZ  1 
ATOM   3074 N NH1 . ARG A 1 435 ? 112.939 117.396 141.423 1.00 69.90  ? 422 ARG A NH1 1 
ATOM   3075 N NH2 . ARG A 1 435 ? 112.348 115.849 143.003 1.00 71.45  ? 422 ARG A NH2 1 
ATOM   3076 N N   . LYS A 1 436 ? 120.432 118.788 140.426 1.00 44.29  ? 423 LYS A N   1 
ATOM   3077 C CA  . LYS A 1 436 ? 121.646 119.587 140.294 1.00 39.52  ? 423 LYS A CA  1 
ATOM   3078 C C   . LYS A 1 436 ? 121.716 120.701 141.330 1.00 42.41  ? 423 LYS A C   1 
ATOM   3079 O O   . LYS A 1 436 ? 122.813 121.065 141.768 1.00 46.26  ? 423 LYS A O   1 
ATOM   3080 C CB  . LYS A 1 436 ? 121.737 120.173 138.886 1.00 34.89  ? 423 LYS A CB  1 
ATOM   3081 C CG  . LYS A 1 436 ? 121.863 119.134 137.789 1.00 39.87  ? 423 LYS A CG  1 
ATOM   3082 C CD  . LYS A 1 436 ? 121.809 119.779 136.417 1.00 43.28  ? 423 LYS A CD  1 
ATOM   3083 C CE  . LYS A 1 436 ? 120.569 120.642 136.276 1.00 41.74  ? 423 LYS A CE  1 
ATOM   3084 N NZ  . LYS A 1 436 ? 120.405 121.191 134.904 1.00 40.93  ? 423 LYS A NZ  1 
ATOM   3085 N N   . PHE A 1 437 ? 120.575 121.263 141.718 1.00 40.07  ? 424 PHE A N   1 
ATOM   3086 C CA  . PHE A 1 437 ? 120.517 122.365 142.670 1.00 35.49  ? 424 PHE A CA  1 
ATOM   3087 C C   . PHE A 1 437 ? 119.574 121.985 143.801 1.00 41.05  ? 424 PHE A C   1 
ATOM   3088 O O   . PHE A 1 437 ? 118.422 121.617 143.553 1.00 47.06  ? 424 PHE A O   1 
ATOM   3089 C CB  . PHE A 1 437 ? 120.052 123.651 141.986 1.00 31.51  ? 424 PHE A CB  1 
ATOM   3090 C CG  . PHE A 1 437 ? 120.849 124.008 140.764 1.00 32.85  ? 424 PHE A CG  1 
ATOM   3091 C CD1 . PHE A 1 437 ? 122.231 123.995 140.793 1.00 34.39  ? 424 PHE A CD1 1 
ATOM   3092 C CD2 . PHE A 1 437 ? 120.214 124.342 139.581 1.00 33.75  ? 424 PHE A CD2 1 
ATOM   3093 C CE1 . PHE A 1 437 ? 122.965 124.318 139.670 1.00 34.91  ? 424 PHE A CE1 1 
ATOM   3094 C CE2 . PHE A 1 437 ? 120.944 124.666 138.455 1.00 35.09  ? 424 PHE A CE2 1 
ATOM   3095 C CZ  . PHE A 1 437 ? 122.319 124.653 138.500 1.00 36.10  ? 424 PHE A CZ  1 
ATOM   3096 N N   . VAL A 1 438 ? 120.058 122.076 145.037 1.00 40.05  ? 425 VAL A N   1 
ATOM   3097 C CA  . VAL A 1 438 ? 119.294 121.679 146.214 1.00 41.05  ? 425 VAL A CA  1 
ATOM   3098 C C   . VAL A 1 438 ? 119.229 122.859 147.173 1.00 43.00  ? 425 VAL A C   1 
ATOM   3099 O O   . VAL A 1 438 ? 120.253 123.484 147.463 1.00 45.32  ? 425 VAL A O   1 
ATOM   3100 C CB  . VAL A 1 438 ? 119.915 120.451 146.908 1.00 40.76  ? 425 VAL A CB  1 
ATOM   3101 C CG1 . VAL A 1 438 ? 119.093 120.055 148.121 1.00 49.27  ? 425 VAL A CG1 1 
ATOM   3102 C CG2 . VAL A 1 438 ? 120.027 119.289 145.933 1.00 38.70  ? 425 VAL A CG2 1 
ATOM   3103 N N   . CYS A 1 439 ? 118.027 123.166 147.659 1.00 49.05  ? 426 CYS A N   1 
ATOM   3104 C CA  . CYS A 1 439 ? 117.810 124.235 148.626 1.00 56.46  ? 426 CYS A CA  1 
ATOM   3105 C C   . CYS A 1 439 ? 117.253 123.626 149.904 1.00 63.04  ? 426 CYS A C   1 
ATOM   3106 O O   . CYS A 1 439 ? 116.197 122.984 149.881 1.00 65.48  ? 426 CYS A O   1 
ATOM   3107 C CB  . CYS A 1 439 ? 116.858 125.297 148.071 1.00 57.50  ? 426 CYS A CB  1 
ATOM   3108 S SG  . CYS A 1 439 ? 116.664 126.765 149.111 1.00 68.85  ? 426 CYS A SG  1 
ATOM   3109 N N   . LEU A 1 440 ? 117.955 123.835 151.015 1.00 65.18  ? 427 LEU A N   1 
ATOM   3110 C CA  . LEU A 1 440 ? 117.647 123.205 152.297 1.00 72.93  ? 427 LEU A CA  1 
ATOM   3111 C C   . LEU A 1 440 ? 117.699 124.228 153.424 1.00 84.06  ? 427 LEU A C   1 
ATOM   3112 O O   . LEU A 1 440 ? 118.367 124.034 154.442 1.00 85.92  ? 427 LEU A O   1 
ATOM   3113 C CB  . LEU A 1 440 ? 118.597 122.044 152.572 1.00 70.48  ? 427 LEU A CB  1 
ATOM   3114 C CG  . LEU A 1 440 ? 118.423 120.792 151.713 1.00 68.20  ? 427 LEU A CG  1 
ATOM   3115 C CD1 . LEU A 1 440 ? 119.617 119.871 151.877 1.00 62.68  ? 427 LEU A CD1 1 
ATOM   3116 C CD2 . LEU A 1 440 ? 117.138 120.069 152.080 1.00 69.35  ? 427 LEU A CD2 1 
ATOM   3117 N N   . ASN A 1 441 ? 117.001 125.349 153.239 1.00 85.75  ? 428 ASN A N   1 
ATOM   3118 C CA  . ASN A 1 441 ? 117.005 126.416 154.232 1.00 85.82  ? 428 ASN A CA  1 
ATOM   3119 C C   . ASN A 1 441 ? 116.563 125.894 155.596 1.00 92.46  ? 428 ASN A C   1 
ATOM   3120 O O   . ASN A 1 441 ? 115.634 125.089 155.704 1.00 95.41  ? 428 ASN A O   1 
ATOM   3121 C CB  . ASN A 1 441 ? 116.091 127.556 153.785 1.00 82.94  ? 428 ASN A CB  1 
ATOM   3122 C CG  . ASN A 1 441 ? 114.642 127.131 153.683 1.00 90.23  ? 428 ASN A CG  1 
ATOM   3123 O OD1 . ASN A 1 441 ? 113.868 127.289 154.629 1.00 92.96  ? 428 ASN A OD1 1 
ATOM   3124 N ND2 . ASN A 1 441 ? 114.267 126.579 152.535 1.00 86.20  ? 428 ASN A ND2 1 
ATOM   3125 N N   . ASP A 1 442 ? 117.244 126.363 156.643 1.00 90.69  ? 429 ASP A N   1 
ATOM   3126 C CA  . ASP A 1 442 ? 117.081 125.830 157.996 1.00 95.75  ? 429 ASP A CA  1 
ATOM   3127 C C   . ASP A 1 442 ? 116.016 126.642 158.729 1.00 101.68 ? 429 ASP A C   1 
ATOM   3128 O O   . ASP A 1 442 ? 116.295 127.633 159.408 1.00 104.04 ? 429 ASP A O   1 
ATOM   3129 C CB  . ASP A 1 442 ? 118.413 125.850 158.735 1.00 95.65  ? 429 ASP A CB  1 
ATOM   3130 C CG  . ASP A 1 442 ? 118.402 124.994 159.986 1.00 99.61  ? 429 ASP A CG  1 
ATOM   3131 O OD1 . ASP A 1 442 ? 117.387 124.310 160.229 1.00 98.78  ? 429 ASP A OD1 1 
ATOM   3132 O OD2 . ASP A 1 442 ? 119.410 125.004 160.724 1.00 99.54  ? 429 ASP A OD2 1 
ATOM   3133 N N   . ASN A 1 443 ? 114.766 126.210 158.581 1.00 103.10 ? 430 ASN A N   1 
ATOM   3134 C CA  . ASN A 1 443 ? 113.625 126.852 159.231 1.00 106.94 ? 430 ASN A CA  1 
ATOM   3135 C C   . ASN A 1 443 ? 113.056 125.891 160.273 1.00 111.70 ? 430 ASN A C   1 
ATOM   3136 O O   . ASN A 1 443 ? 112.342 124.943 159.933 1.00 110.99 ? 430 ASN A O   1 
ATOM   3137 C CB  . ASN A 1 443 ? 112.572 127.252 158.204 1.00 104.96 ? 430 ASN A CB  1 
ATOM   3138 C CG  . ASN A 1 443 ? 111.421 128.016 158.823 1.00 110.01 ? 430 ASN A CG  1 
ATOM   3139 O OD1 . ASN A 1 443 ? 111.566 128.629 159.883 1.00 116.30 ? 430 ASN A OD1 1 
ATOM   3140 N ND2 . ASN A 1 443 ? 110.265 127.979 158.166 1.00 106.30 ? 430 ASN A ND2 1 
ATOM   3141 N N   . ILE A 1 444 ? 113.371 126.140 161.542 1.00 114.04 ? 431 ILE A N   1 
ATOM   3142 C CA  . ILE A 1 444 ? 112.933 125.306 162.654 1.00 118.29 ? 431 ILE A CA  1 
ATOM   3143 C C   . ILE A 1 444 ? 112.154 126.177 163.629 1.00 121.63 ? 431 ILE A C   1 
ATOM   3144 O O   . ILE A 1 444 ? 112.510 127.339 163.852 1.00 122.46 ? 431 ILE A O   1 
ATOM   3145 C CB  . ILE A 1 444 ? 114.126 124.629 163.362 1.00 117.33 ? 431 ILE A CB  1 
ATOM   3146 C CG1 . ILE A 1 444 ? 115.035 123.937 162.348 1.00 112.68 ? 431 ILE A CG1 1 
ATOM   3147 C CG2 . ILE A 1 444 ? 113.649 123.629 164.402 1.00 117.78 ? 431 ILE A CG2 1 
ATOM   3148 C CD1 . ILE A 1 444 ? 114.372 122.810 161.601 1.00 111.42 ? 431 ILE A CD1 1 
ATOM   3149 N N   . ASP A 1 445 ? 111.083 125.623 164.203 1.00 122.93 ? 432 ASP A N   1 
ATOM   3150 C CA  . ASP A 1 445 ? 110.316 126.389 165.180 1.00 124.56 ? 432 ASP A CA  1 
ATOM   3151 C C   . ASP A 1 445 ? 111.090 126.592 166.480 1.00 128.84 ? 432 ASP A C   1 
ATOM   3152 O O   . ASP A 1 445 ? 110.854 127.581 167.182 1.00 129.50 ? 432 ASP A O   1 
ATOM   3153 C CB  . ASP A 1 445 ? 108.974 125.712 165.457 1.00 124.34 ? 432 ASP A CB  1 
ATOM   3154 C CG  . ASP A 1 445 ? 108.007 126.629 166.178 1.00 131.88 ? 432 ASP A CG  1 
ATOM   3155 O OD1 . ASP A 1 445 ? 107.405 127.504 165.516 1.00 135.66 ? 432 ASP A OD1 1 
ATOM   3156 O OD2 . ASP A 1 445 ? 107.859 126.484 167.408 1.00 133.98 ? 432 ASP A OD2 1 
ATOM   3157 N N   . HIS A 1 446 ? 111.974 125.655 166.839 1.00 128.77 ? 433 HIS A N   1 
ATOM   3158 C CA  . HIS A 1 446 ? 112.847 125.767 168.010 1.00 127.45 ? 433 HIS A CA  1 
ATOM   3159 C C   . HIS A 1 446 ? 112.080 125.896 169.325 1.00 129.75 ? 433 HIS A C   1 
ATOM   3160 O O   . HIS A 1 446 ? 112.689 126.050 170.389 1.00 125.75 ? 433 HIS A O   1 
ATOM   3161 C CB  . HIS A 1 446 ? 113.807 126.952 167.855 1.00 126.12 ? 433 HIS A CB  1 
ATOM   3162 C CG  . HIS A 1 446 ? 114.841 126.760 166.789 1.00 124.40 ? 433 HIS A CG  1 
ATOM   3163 N ND1 . HIS A 1 446 ? 115.816 125.788 166.865 1.00 119.41 ? 433 HIS A ND1 1 
ATOM   3164 C CD2 . HIS A 1 446 ? 115.059 127.421 165.627 1.00 124.89 ? 433 HIS A CD2 1 
ATOM   3165 C CE1 . HIS A 1 446 ? 116.586 125.855 165.793 1.00 119.65 ? 433 HIS A CE1 1 
ATOM   3166 N NE2 . HIS A 1 446 ? 116.148 126.837 165.026 1.00 123.72 ? 433 HIS A NE2 1 
ATOM   3167 N N   . ASN A 1 447 ? 110.750 125.853 169.265 1.00 131.19 ? 434 ASN A N   1 
ATOM   3168 C CA  . ASN A 1 447 ? 109.899 125.802 170.448 1.00 130.43 ? 434 ASN A CA  1 
ATOM   3169 C C   . ASN A 1 447 ? 109.054 124.533 170.439 1.00 132.71 ? 434 ASN A C   1 
ATOM   3170 O O   . ASN A 1 447 ? 107.974 124.483 171.030 1.00 135.22 ? 434 ASN A O   1 
ATOM   3171 C CB  . ASN A 1 447 ? 109.016 127.049 170.544 1.00 132.54 ? 434 ASN A CB  1 
ATOM   3172 C CG  . ASN A 1 447 ? 109.826 128.332 170.651 1.00 136.92 ? 434 ASN A CG  1 
ATOM   3173 O OD1 . ASN A 1 447 ? 110.987 128.312 171.060 1.00 141.70 ? 434 ASN A OD1 1 
ATOM   3174 N ND2 . ASN A 1 447 ? 109.216 129.454 170.281 1.00 135.52 ? 434 ASN A ND2 1 
ATOM   3175 N N   . HIS A 1 448 ? 109.549 123.496 169.773 1.00 133.61 ? 435 HIS A N   1 
ATOM   3176 C CA  . HIS A 1 448 ? 108.831 122.247 169.593 1.00 133.30 ? 435 HIS A CA  1 
ATOM   3177 C C   . HIS A 1 448 ? 109.584 121.148 170.317 1.00 132.61 ? 435 HIS A C   1 
ATOM   3178 O O   . HIS A 1 448 ? 110.808 121.199 170.431 1.00 131.45 ? 435 HIS A O   1 
ATOM   3179 C CB  . HIS A 1 448 ? 108.711 121.899 168.109 1.00 127.63 ? 435 HIS A CB  1 
ATOM   3180 C CG  . HIS A 1 448 ? 108.081 120.567 167.836 1.00 129.34 ? 435 HIS A CG  1 
ATOM   3181 N ND1 . HIS A 1 448 ? 106.965 120.110 168.502 1.00 132.26 ? 435 HIS A ND1 1 
ATOM   3182 C CD2 . HIS A 1 448 ? 108.395 119.608 166.934 1.00 128.55 ? 435 HIS A CD2 1 
ATOM   3183 C CE1 . HIS A 1 448 ? 106.624 118.922 168.030 1.00 132.41 ? 435 HIS A CE1 1 
ATOM   3184 N NE2 . HIS A 1 448 ? 107.477 118.594 167.077 1.00 130.43 ? 435 HIS A NE2 1 
ATOM   3185 N N   . LYS A 1 449 ? 108.842 120.156 170.808 1.00 133.11 ? 436 LYS A N   1 
ATOM   3186 C CA  . LYS A 1 449 ? 109.464 119.084 171.577 1.00 133.33 ? 436 LYS A CA  1 
ATOM   3187 C C   . LYS A 1 449 ? 110.463 118.295 170.735 1.00 129.84 ? 436 LYS A C   1 
ATOM   3188 O O   . LYS A 1 449 ? 111.544 117.939 171.216 1.00 129.09 ? 436 LYS A O   1 
ATOM   3189 C CB  . LYS A 1 449 ? 108.392 118.156 172.142 1.00 136.20 ? 436 LYS A CB  1 
ATOM   3190 C CG  . LYS A 1 449 ? 107.538 118.766 173.244 1.00 141.08 ? 436 LYS A CG  1 
ATOM   3191 C CD  . LYS A 1 449 ? 108.381 119.156 174.447 1.00 141.15 ? 436 LYS A CD  1 
ATOM   3192 C CE  . LYS A 1 449 ? 107.537 119.863 175.486 1.00 143.48 ? 436 LYS A CE  1 
ATOM   3193 N NZ  . LYS A 1 449 ? 106.736 120.960 174.879 1.00 139.20 ? 436 LYS A NZ  1 
ATOM   3194 N N   . ASP A 1 450 ? 110.116 118.002 169.482 1.00 128.47 ? 437 ASP A N   1 
ATOM   3195 C CA  . ASP A 1 450 ? 110.957 117.223 168.579 1.00 124.61 ? 437 ASP A CA  1 
ATOM   3196 C C   . ASP A 1 450 ? 111.727 118.100 167.597 1.00 120.99 ? 437 ASP A C   1 
ATOM   3197 O O   . ASP A 1 450 ? 112.067 117.654 166.496 1.00 117.33 ? 437 ASP A O   1 
ATOM   3198 C CB  . ASP A 1 450 ? 110.106 116.204 167.826 1.00 124.71 ? 437 ASP A CB  1 
ATOM   3199 C CG  . ASP A 1 450 ? 109.369 115.267 168.757 1.00 126.07 ? 437 ASP A CG  1 
ATOM   3200 O OD1 . ASP A 1 450 ? 109.889 114.999 169.864 1.00 122.44 ? 437 ASP A OD1 1 
ATOM   3201 O OD2 . ASP A 1 450 ? 108.273 114.795 168.397 1.00 129.68 ? 437 ASP A OD2 1 
ATOM   3202 N N   . ALA A 1 451 ? 112.006 119.347 167.975 1.00 121.23 ? 438 ALA A N   1 
ATOM   3203 C CA  . ALA A 1 451 ? 112.705 120.247 167.065 1.00 115.29 ? 438 ALA A CA  1 
ATOM   3204 C C   . ALA A 1 451 ? 114.150 119.816 166.856 1.00 109.15 ? 438 ALA A C   1 
ATOM   3205 O O   . ALA A 1 451 ? 114.691 119.956 165.753 1.00 106.65 ? 438 ALA A O   1 
ATOM   3206 C CB  . ALA A 1 451 ? 112.640 121.677 167.588 1.00 116.36 ? 438 ALA A CB  1 
ATOM   3207 N N   . GLN A 1 452 ? 114.802 119.313 167.909 1.00 106.45 ? 439 GLN A N   1 
ATOM   3208 C CA  . GLN A 1 452 ? 116.168 118.821 167.761 1.00 104.32 ? 439 GLN A CA  1 
ATOM   3209 C C   . GLN A 1 452 ? 116.221 117.600 166.853 1.00 101.31 ? 439 GLN A C   1 
ATOM   3210 O O   . GLN A 1 452 ? 117.232 117.368 166.183 1.00 99.44  ? 439 GLN A O   1 
ATOM   3211 C CB  . GLN A 1 452 ? 116.770 118.491 169.127 1.00 103.30 ? 439 GLN A CB  1 
ATOM   3212 C CG  . GLN A 1 452 ? 118.195 117.959 169.058 1.00 104.01 ? 439 GLN A CG  1 
ATOM   3213 C CD  . GLN A 1 452 ? 119.162 118.965 168.463 1.00 101.14 ? 439 GLN A CD  1 
ATOM   3214 O OE1 . GLN A 1 452 ? 119.013 120.172 168.654 1.00 96.50  ? 439 GLN A OE1 1 
ATOM   3215 N NE2 . GLN A 1 452 ? 120.161 118.473 167.737 1.00 100.08 ? 439 GLN A NE2 1 
ATOM   3216 N N   . THR A 1 453 ? 115.145 116.814 166.816 1.00 102.17 ? 440 THR A N   1 
ATOM   3217 C CA  . THR A 1 453 ? 115.117 115.637 165.955 1.00 100.77 ? 440 THR A CA  1 
ATOM   3218 C C   . THR A 1 453 ? 115.141 116.024 164.480 1.00 96.76  ? 440 THR A C   1 
ATOM   3219 O O   . THR A 1 453 ? 115.726 115.312 163.656 1.00 89.77  ? 440 THR A O   1 
ATOM   3220 C CB  . THR A 1 453 ? 113.886 114.792 166.273 1.00 105.60 ? 440 THR A CB  1 
ATOM   3221 O OG1 . THR A 1 453 ? 112.707 115.488 165.855 1.00 110.12 ? 440 THR A OG1 1 
ATOM   3222 C CG2 . THR A 1 453 ? 113.801 114.534 167.769 1.00 105.13 ? 440 THR A CG2 1 
ATOM   3223 N N   . VAL A 1 454 ? 114.504 117.143 164.126 1.00 99.95  ? 441 VAL A N   1 
ATOM   3224 C CA  . VAL A 1 454 ? 114.551 117.617 162.745 1.00 92.35  ? 441 VAL A CA  1 
ATOM   3225 C C   . VAL A 1 454 ? 115.984 117.959 162.354 1.00 87.25  ? 441 VAL A C   1 
ATOM   3226 O O   . VAL A 1 454 ? 116.455 117.600 161.269 1.00 83.92  ? 441 VAL A O   1 
ATOM   3227 C CB  . VAL A 1 454 ? 113.608 118.817 162.555 1.00 88.63  ? 441 VAL A CB  1 
ATOM   3228 C CG1 . VAL A 1 454 ? 113.621 119.264 161.107 1.00 86.25  ? 441 VAL A CG1 1 
ATOM   3229 C CG2 . VAL A 1 454 ? 112.200 118.453 162.994 1.00 92.65  ? 441 VAL A CG2 1 
ATOM   3230 N N   . LYS A 1 455 ? 116.702 118.653 163.240 1.00 89.26  ? 442 LYS A N   1 
ATOM   3231 C CA  . LYS A 1 455 ? 118.111 118.935 162.985 1.00 86.08  ? 442 LYS A CA  1 
ATOM   3232 C C   . LYS A 1 455 ? 118.921 117.648 162.897 1.00 84.16  ? 442 LYS A C   1 
ATOM   3233 O O   . LYS A 1 455 ? 119.821 117.530 162.059 1.00 79.43  ? 442 LYS A O   1 
ATOM   3234 C CB  . LYS A 1 455 ? 118.665 119.860 164.072 1.00 87.15  ? 442 LYS A CB  1 
ATOM   3235 C CG  . LYS A 1 455 ? 120.182 119.801 164.277 1.00 85.28  ? 442 LYS A CG  1 
ATOM   3236 C CD  . LYS A 1 455 ? 120.973 120.239 163.046 1.00 86.17  ? 442 LYS A CD  1 
ATOM   3237 C CE  . LYS A 1 455 ? 120.651 121.666 162.634 1.00 89.88  ? 442 LYS A CE  1 
ATOM   3238 N NZ  . LYS A 1 455 ? 121.403 122.071 161.410 1.00 76.03  ? 442 LYS A NZ  1 
ATOM   3239 N N   . ALA A 1 456 ? 118.617 116.675 163.754 1.00 86.92  ? 443 ALA A N   1 
ATOM   3240 C CA  . ALA A 1 456 ? 119.354 115.415 163.733 1.00 83.28  ? 443 ALA A CA  1 
ATOM   3241 C C   . ALA A 1 456 ? 119.181 114.696 162.400 1.00 76.92  ? 443 ALA A C   1 
ATOM   3242 O O   . ALA A 1 456 ? 120.158 114.236 161.800 1.00 71.28  ? 443 ALA A O   1 
ATOM   3243 C CB  . ALA A 1 456 ? 118.904 114.522 164.891 1.00 88.64  ? 443 ALA A CB  1 
ATOM   3244 N N   . VAL A 1 457 ? 117.942 114.603 161.909 1.00 80.41  ? 444 VAL A N   1 
ATOM   3245 C CA  . VAL A 1 457 ? 117.725 113.907 160.643 1.00 77.85  ? 444 VAL A CA  1 
ATOM   3246 C C   . VAL A 1 457 ? 118.273 114.719 159.473 1.00 72.31  ? 444 VAL A C   1 
ATOM   3247 O O   . VAL A 1 457 ? 118.762 114.147 158.490 1.00 69.86  ? 444 VAL A O   1 
ATOM   3248 C CB  . VAL A 1 457 ? 116.237 113.553 160.450 1.00 80.74  ? 444 VAL A CB  1 
ATOM   3249 C CG1 . VAL A 1 457 ? 115.790 112.564 161.516 1.00 86.56  ? 444 VAL A CG1 1 
ATOM   3250 C CG2 . VAL A 1 457 ? 115.368 114.795 160.468 1.00 76.23  ? 444 VAL A CG2 1 
ATOM   3251 N N   . LEU A 1 458 ? 118.219 116.052 159.550 1.00 73.82  ? 445 LEU A N   1 
ATOM   3252 C CA  . LEU A 1 458 ? 118.808 116.866 158.492 1.00 70.13  ? 445 LEU A CA  1 
ATOM   3253 C C   . LEU A 1 458 ? 120.317 116.665 158.422 1.00 74.22  ? 445 LEU A C   1 
ATOM   3254 O O   . LEU A 1 458 ? 120.883 116.514 157.332 1.00 72.09  ? 445 LEU A O   1 
ATOM   3255 C CB  . LEU A 1 458 ? 118.469 118.339 158.716 1.00 67.29  ? 445 LEU A CB  1 
ATOM   3256 C CG  . LEU A 1 458 ? 118.729 119.277 157.539 1.00 67.76  ? 445 LEU A CG  1 
ATOM   3257 C CD1 . LEU A 1 458 ? 117.897 118.863 156.339 1.00 70.77  ? 445 LEU A CD1 1 
ATOM   3258 C CD2 . LEU A 1 458 ? 118.430 120.714 157.927 1.00 72.55  ? 445 LEU A CD2 1 
ATOM   3259 N N   . ARG A 1 459 ? 120.987 116.647 159.577 1.00 78.55  ? 446 ARG A N   1 
ATOM   3260 C CA  . ARG A 1 459 ? 122.421 116.381 159.589 1.00 72.89  ? 446 ARG A CA  1 
ATOM   3261 C C   . ARG A 1 459 ? 122.725 114.953 159.161 1.00 70.23  ? 446 ARG A C   1 
ATOM   3262 O O   . ARG A 1 459 ? 123.774 114.701 158.565 1.00 67.19  ? 446 ARG A O   1 
ATOM   3263 C CB  . ARG A 1 459 ? 123.006 116.654 160.974 1.00 73.22  ? 446 ARG A CB  1 
ATOM   3264 C CG  . ARG A 1 459 ? 124.443 117.151 160.935 1.00 77.41  ? 446 ARG A CG  1 
ATOM   3265 C CD  . ARG A 1 459 ? 125.154 116.918 162.255 1.00 85.02  ? 446 ARG A CD  1 
ATOM   3266 N NE  . ARG A 1 459 ? 125.498 115.514 162.444 1.00 86.31  ? 446 ARG A NE  1 
ATOM   3267 C CZ  . ARG A 1 459 ? 126.667 114.979 162.116 1.00 85.45  ? 446 ARG A CZ  1 
ATOM   3268 N NH1 . ARG A 1 459 ? 127.636 115.707 161.588 1.00 80.37  ? 446 ARG A NH1 1 
ATOM   3269 N NH2 . ARG A 1 459 ? 126.867 113.681 162.326 1.00 87.64  ? 446 ARG A NH2 1 
ATOM   3270 N N   . ASP A 1 460 ? 121.831 114.008 159.462 1.00 71.09  ? 447 ASP A N   1 
ATOM   3271 C CA  . ASP A 1 460 ? 122.013 112.643 158.978 1.00 67.86  ? 447 ASP A CA  1 
ATOM   3272 C C   . ASP A 1 460 ? 121.962 112.594 157.457 1.00 64.84  ? 447 ASP A C   1 
ATOM   3273 O O   . ASP A 1 460 ? 122.771 111.910 156.822 1.00 65.55  ? 447 ASP A O   1 
ATOM   3274 C CB  . ASP A 1 460 ? 120.949 111.728 159.583 1.00 69.44  ? 447 ASP A CB  1 
ATOM   3275 C CG  . ASP A 1 460 ? 121.167 111.477 161.063 1.00 68.13  ? 447 ASP A CG  1 
ATOM   3276 O OD1 . ASP A 1 460 ? 122.277 111.767 161.557 1.00 68.80  ? 447 ASP A OD1 1 
ATOM   3277 O OD2 . ASP A 1 460 ? 120.231 110.992 161.733 1.00 63.98  ? 447 ASP A OD2 1 
ATOM   3278 N N   . PHE A 1 461 ? 121.019 113.323 156.855 1.00 64.31  ? 448 PHE A N   1 
ATOM   3279 C CA  . PHE A 1 461 ? 120.973 113.428 155.399 1.00 63.75  ? 448 PHE A CA  1 
ATOM   3280 C C   . PHE A 1 461 ? 122.238 114.081 154.855 1.00 65.95  ? 448 PHE A C   1 
ATOM   3281 O O   . PHE A 1 461 ? 122.791 113.636 153.841 1.00 67.50  ? 448 PHE A O   1 
ATOM   3282 C CB  . PHE A 1 461 ? 119.735 114.216 154.968 1.00 62.27  ? 448 PHE A CB  1 
ATOM   3283 C CG  . PHE A 1 461 ? 119.757 114.644 153.527 1.00 61.00  ? 448 PHE A CG  1 
ATOM   3284 C CD1 . PHE A 1 461 ? 119.514 113.733 152.514 1.00 62.48  ? 448 PHE A CD1 1 
ATOM   3285 C CD2 . PHE A 1 461 ? 120.010 115.961 153.186 1.00 58.18  ? 448 PHE A CD2 1 
ATOM   3286 C CE1 . PHE A 1 461 ? 119.531 114.126 151.189 1.00 55.49  ? 448 PHE A CE1 1 
ATOM   3287 C CE2 . PHE A 1 461 ? 120.028 116.358 151.863 1.00 58.09  ? 448 PHE A CE2 1 
ATOM   3288 C CZ  . PHE A 1 461 ? 119.787 115.440 150.865 1.00 52.59  ? 448 PHE A CZ  1 
ATOM   3289 N N   . TYR A 1 462 ? 122.706 115.144 155.515 1.00 67.29  ? 449 TYR A N   1 
ATOM   3290 C CA  . TYR A 1 462 ? 123.932 115.810 155.082 1.00 68.22  ? 449 TYR A CA  1 
ATOM   3291 C C   . TYR A 1 462 ? 125.122 114.858 155.121 1.00 68.60  ? 449 TYR A C   1 
ATOM   3292 O O   . TYR A 1 462 ? 125.937 114.829 154.192 1.00 67.02  ? 449 TYR A O   1 
ATOM   3293 C CB  . TYR A 1 462 ? 124.202 117.035 155.957 1.00 69.29  ? 449 TYR A CB  1 
ATOM   3294 C CG  . TYR A 1 462 ? 123.371 118.247 155.609 1.00 64.26  ? 449 TYR A CG  1 
ATOM   3295 C CD1 . TYR A 1 462 ? 123.218 118.650 154.291 1.00 68.46  ? 449 TYR A CD1 1 
ATOM   3296 C CD2 . TYR A 1 462 ? 122.745 118.991 156.598 1.00 62.42  ? 449 TYR A CD2 1 
ATOM   3297 C CE1 . TYR A 1 462 ? 122.464 119.755 153.967 1.00 67.54  ? 449 TYR A CE1 1 
ATOM   3298 C CE2 . TYR A 1 462 ? 121.987 120.101 156.282 1.00 68.37  ? 449 TYR A CE2 1 
ATOM   3299 C CZ  . TYR A 1 462 ? 121.851 120.477 154.963 1.00 70.48  ? 449 TYR A CZ  1 
ATOM   3300 O OH  . TYR A 1 462 ? 121.098 121.580 154.634 1.00 71.49  ? 449 TYR A OH  1 
ATOM   3301 N N   . GLU A 1 463 ? 125.239 114.074 156.195 1.00 65.73  ? 450 GLU A N   1 
ATOM   3302 C CA  . GLU A 1 463 ? 126.314 113.092 156.296 1.00 62.93  ? 450 GLU A CA  1 
ATOM   3303 C C   . GLU A 1 463 ? 126.172 112.015 155.230 1.00 66.54  ? 450 GLU A C   1 
ATOM   3304 O O   . GLU A 1 463 ? 127.171 111.541 154.676 1.00 69.94  ? 450 GLU A O   1 
ATOM   3305 C CB  . GLU A 1 463 ? 126.325 112.466 157.691 1.00 66.78  ? 450 GLU A CB  1 
ATOM   3306 C CG  . GLU A 1 463 ? 126.644 113.436 158.817 1.00 69.61  ? 450 GLU A CG  1 
ATOM   3307 C CD  . GLU A 1 463 ? 128.112 113.798 158.881 1.00 70.68  ? 450 GLU A CD  1 
ATOM   3308 O OE1 . GLU A 1 463 ? 128.955 112.899 158.678 1.00 71.89  ? 450 GLU A OE1 1 
ATOM   3309 O OE2 . GLU A 1 463 ? 128.423 114.981 159.131 1.00 73.34  ? 450 GLU A OE2 1 
ATOM   3310 N N   . SER A 1 464 ? 124.934 111.607 154.938 1.00 67.94  ? 451 SER A N   1 
ATOM   3311 C CA  . SER A 1 464 ? 124.705 110.602 153.907 1.00 65.78  ? 451 SER A CA  1 
ATOM   3312 C C   . SER A 1 464 ? 125.157 111.099 152.543 1.00 67.34  ? 451 SER A C   1 
ATOM   3313 O O   . SER A 1 464 ? 125.753 110.346 151.766 1.00 68.86  ? 451 SER A O   1 
ATOM   3314 C CB  . SER A 1 464 ? 123.226 110.224 153.865 1.00 64.12  ? 451 SER A CB  1 
ATOM   3315 O OG  . SER A 1 464 ? 122.441 111.300 153.377 1.00 62.83  ? 451 SER A OG  1 
ATOM   3316 N N   . MET A 1 465 ? 124.873 112.364 152.232 1.00 67.05  ? 452 MET A N   1 
ATOM   3317 C CA  . MET A 1 465 ? 125.197 112.891 150.911 1.00 66.86  ? 452 MET A CA  1 
ATOM   3318 C C   . MET A 1 465 ? 126.704 112.984 150.698 1.00 65.08  ? 452 MET A C   1 
ATOM   3319 O O   . MET A 1 465 ? 127.228 112.504 149.687 1.00 67.01  ? 452 MET A O   1 
ATOM   3320 C CB  . MET A 1 465 ? 124.536 114.256 150.720 1.00 63.51  ? 452 MET A CB  1 
ATOM   3321 C CG  . MET A 1 465 ? 123.029 114.190 150.576 1.00 66.16  ? 452 MET A CG  1 
ATOM   3322 S SD  . MET A 1 465 ? 122.507 113.683 148.928 1.00 92.31  ? 452 MET A SD  1 
ATOM   3323 C CE  . MET A 1 465 ? 122.966 115.130 147.977 1.00 67.66  ? 452 MET A CE  1 
ATOM   3324 N N   . PHE A 1 466 ? 127.420 113.600 151.638 1.00 61.83  ? 453 PHE A N   1 
ATOM   3325 C CA  . PHE A 1 466 ? 128.850 113.878 151.490 1.00 61.20  ? 453 PHE A CA  1 
ATOM   3326 C C   . PHE A 1 466 ? 129.595 113.500 152.762 1.00 63.53  ? 453 PHE A C   1 
ATOM   3327 O O   . PHE A 1 466 ? 129.880 114.359 153.607 1.00 64.91  ? 453 PHE A O   1 
ATOM   3328 C CB  . PHE A 1 466 ? 129.082 115.347 151.138 1.00 65.36  ? 453 PHE A CB  1 
ATOM   3329 C CG  . PHE A 1 466 ? 128.183 115.852 150.051 1.00 57.55  ? 453 PHE A CG  1 
ATOM   3330 C CD1 . PHE A 1 466 ? 128.397 115.485 148.734 1.00 52.03  ? 453 PHE A CD1 1 
ATOM   3331 C CD2 . PHE A 1 466 ? 127.122 116.690 150.345 1.00 55.60  ? 453 PHE A CD2 1 
ATOM   3332 C CE1 . PHE A 1 466 ? 127.571 115.944 147.734 1.00 51.06  ? 453 PHE A CE1 1 
ATOM   3333 C CE2 . PHE A 1 466 ? 126.292 117.153 149.348 1.00 52.84  ? 453 PHE A CE2 1 
ATOM   3334 C CZ  . PHE A 1 466 ? 126.517 116.780 148.041 1.00 54.86  ? 453 PHE A CZ  1 
ATOM   3335 N N   . PRO A 1 467 ? 129.922 112.217 152.937 1.00 64.74  ? 454 PRO A N   1 
ATOM   3336 C CA  . PRO A 1 467 ? 130.738 111.807 154.084 1.00 64.02  ? 454 PRO A CA  1 
ATOM   3337 C C   . PRO A 1 467 ? 132.238 111.823 153.835 1.00 65.62  ? 454 PRO A C   1 
ATOM   3338 O O   . PRO A 1 467 ? 133.005 111.754 154.805 1.00 60.94  ? 454 PRO A O   1 
ATOM   3339 C CB  . PRO A 1 467 ? 130.251 110.376 154.337 1.00 68.86  ? 454 PRO A CB  1 
ATOM   3340 C CG  . PRO A 1 467 ? 129.930 109.872 152.970 1.00 69.49  ? 454 PRO A CG  1 
ATOM   3341 C CD  . PRO A 1 467 ? 129.416 111.057 152.182 1.00 67.53  ? 454 PRO A CD  1 
ATOM   3342 N N   . ILE A 1 468 ? 132.672 111.903 152.583 1.00 71.62  ? 455 ILE A N   1 
ATOM   3343 C CA  . ILE A 1 468 ? 134.107 111.865 152.276 1.00 69.89  ? 455 ILE A CA  1 
ATOM   3344 C C   . ILE A 1 468 ? 134.772 113.122 152.824 1.00 65.81  ? 455 ILE A C   1 
ATOM   3345 O O   . ILE A 1 468 ? 134.184 114.215 152.741 1.00 62.47  ? 455 ILE A O   1 
ATOM   3346 C CB  . ILE A 1 468 ? 134.323 111.732 150.763 1.00 76.16  ? 455 ILE A CB  1 
ATOM   3347 C CG1 . ILE A 1 468 ? 135.816 111.662 150.426 1.00 75.12  ? 455 ILE A CG1 1 
ATOM   3348 C CG2 . ILE A 1 468 ? 133.648 112.877 150.012 1.00 71.36  ? 455 ILE A CG2 1 
ATOM   3349 C CD1 . ILE A 1 468 ? 136.102 111.388 148.964 1.00 79.80  ? 455 ILE A CD1 1 
ATOM   3350 N N   . PRO A 1 469 ? 135.962 113.024 153.413 1.00 71.10  ? 456 PRO A N   1 
ATOM   3351 C CA  . PRO A 1 469 ? 136.653 114.232 153.873 1.00 74.92  ? 456 PRO A CA  1 
ATOM   3352 C C   . PRO A 1 469 ? 137.085 115.111 152.710 1.00 73.30  ? 456 PRO A C   1 
ATOM   3353 O O   . PRO A 1 469 ? 137.338 114.639 151.599 1.00 74.52  ? 456 PRO A O   1 
ATOM   3354 C CB  . PRO A 1 469 ? 137.866 113.682 154.633 1.00 78.11  ? 456 PRO A CB  1 
ATOM   3355 C CG  . PRO A 1 469 ? 138.065 112.305 154.087 1.00 78.12  ? 456 PRO A CG  1 
ATOM   3356 C CD  . PRO A 1 469 ? 136.687 111.798 153.787 1.00 74.73  ? 456 PRO A CD  1 
ATOM   3357 N N   . SER A 1 470 ? 137.162 116.410 152.983 1.00 69.78  ? 457 SER A N   1 
ATOM   3358 C CA  . SER A 1 470 ? 137.606 117.400 152.015 1.00 68.18  ? 457 SER A CA  1 
ATOM   3359 C C   . SER A 1 470 ? 138.894 118.045 152.508 1.00 70.64  ? 457 SER A C   1 
ATOM   3360 O O   . SER A 1 470 ? 139.134 118.143 153.715 1.00 72.63  ? 457 SER A O   1 
ATOM   3361 C CB  . SER A 1 470 ? 136.538 118.474 151.783 1.00 58.41  ? 457 SER A CB  1 
ATOM   3362 O OG  . SER A 1 470 ? 136.216 119.139 152.992 1.00 61.02  ? 457 SER A OG  1 
ATOM   3363 N N   . GLN A 1 471 ? 139.724 118.487 151.561 1.00 66.57  ? 458 GLN A N   1 
ATOM   3364 C CA  . GLN A 1 471 ? 141.019 119.056 151.914 1.00 67.35  ? 458 GLN A CA  1 
ATOM   3365 C C   . GLN A 1 471 ? 140.909 120.438 152.547 1.00 66.67  ? 458 GLN A C   1 
ATOM   3366 O O   . GLN A 1 471 ? 141.916 120.949 153.048 1.00 70.30  ? 458 GLN A O   1 
ATOM   3367 C CB  . GLN A 1 471 ? 141.921 119.129 150.681 1.00 64.57  ? 458 GLN A CB  1 
ATOM   3368 C CG  . GLN A 1 471 ? 141.661 120.319 149.772 1.00 64.67  ? 458 GLN A CG  1 
ATOM   3369 C CD  . GLN A 1 471 ? 140.447 120.139 148.883 1.00 61.62  ? 458 GLN A CD  1 
ATOM   3370 O OE1 . GLN A 1 471 ? 139.365 119.785 149.349 1.00 59.58  ? 458 GLN A OE1 1 
ATOM   3371 N NE2 . GLN A 1 471 ? 140.624 120.386 147.590 1.00 58.97  ? 458 GLN A NE2 1 
ATOM   3372 N N   . PHE A 1 472 ? 139.725 121.050 152.540 1.00 59.73  ? 459 PHE A N   1 
ATOM   3373 C CA  . PHE A 1 472 ? 139.520 122.360 153.143 1.00 60.06  ? 459 PHE A CA  1 
ATOM   3374 C C   . PHE A 1 472 ? 139.200 122.290 154.635 1.00 62.87  ? 459 PHE A C   1 
ATOM   3375 O O   . PHE A 1 472 ? 138.662 123.260 155.180 1.00 64.01  ? 459 PHE A O   1 
ATOM   3376 C CB  . PHE A 1 472 ? 138.402 123.107 152.412 1.00 57.47  ? 459 PHE A CB  1 
ATOM   3377 C CG  . PHE A 1 472 ? 138.713 123.413 150.976 1.00 57.21  ? 459 PHE A CG  1 
ATOM   3378 C CD1 . PHE A 1 472 ? 140.018 123.621 150.563 1.00 59.89  ? 459 PHE A CD1 1 
ATOM   3379 C CD2 . PHE A 1 472 ? 137.700 123.491 150.037 1.00 52.20  ? 459 PHE A CD2 1 
ATOM   3380 C CE1 . PHE A 1 472 ? 140.304 123.903 149.239 1.00 58.80  ? 459 PHE A CE1 1 
ATOM   3381 C CE2 . PHE A 1 472 ? 137.981 123.771 148.714 1.00 46.26  ? 459 PHE A CE2 1 
ATOM   3382 C CZ  . PHE A 1 472 ? 139.284 123.977 148.315 1.00 50.15  ? 459 PHE A CZ  1 
ATOM   3383 N N   . GLU A 1 473 ? 139.514 121.183 155.305 1.00 66.02  ? 460 GLU A N   1 
ATOM   3384 C CA  . GLU A 1 473 ? 139.200 120.996 156.715 1.00 71.93  ? 460 GLU A CA  1 
ATOM   3385 C C   . GLU A 1 473 ? 140.454 120.583 157.473 1.00 78.27  ? 460 GLU A C   1 
ATOM   3386 O O   . GLU A 1 473 ? 141.290 119.843 156.946 1.00 79.30  ? 460 GLU A O   1 
ATOM   3387 C CB  . GLU A 1 473 ? 138.109 119.935 156.906 1.00 70.65  ? 460 GLU A CB  1 
ATOM   3388 C CG  . GLU A 1 473 ? 136.848 120.163 156.083 1.00 70.68  ? 460 GLU A CG  1 
ATOM   3389 C CD  . GLU A 1 473 ? 135.975 121.273 156.636 1.00 71.68  ? 460 GLU A CD  1 
ATOM   3390 O OE1 . GLU A 1 473 ? 136.221 121.715 157.777 1.00 76.47  ? 460 GLU A OE1 1 
ATOM   3391 O OE2 . GLU A 1 473 ? 135.041 121.702 155.926 1.00 68.59  ? 460 GLU A OE2 1 
ATOM   3392 N N   . LEU A 1 474 ? 140.581 121.063 158.708 1.00 79.99  ? 461 LEU A N   1 
ATOM   3393 C CA  . LEU A 1 474 ? 141.727 120.698 159.537 1.00 86.24  ? 461 LEU A CA  1 
ATOM   3394 C C   . LEU A 1 474 ? 141.565 119.274 160.056 1.00 89.32  ? 461 LEU A C   1 
ATOM   3395 O O   . LEU A 1 474 ? 140.531 118.951 160.649 1.00 89.00  ? 461 LEU A O   1 
ATOM   3396 C CB  . LEU A 1 474 ? 141.882 121.657 160.712 1.00 86.77  ? 461 LEU A CB  1 
ATOM   3397 C CG  . LEU A 1 474 ? 142.052 123.142 160.395 1.00 84.65  ? 461 LEU A CG  1 
ATOM   3398 C CD1 . LEU A 1 474 ? 140.740 123.880 160.597 1.00 79.98  ? 461 LEU A CD1 1 
ATOM   3399 C CD2 . LEU A 1 474 ? 143.153 123.747 161.249 1.00 82.12  ? 461 LEU A CD2 1 
ATOM   3400 N N   . PRO A 1 475 ? 142.555 118.402 159.858 1.00 94.05  ? 462 PRO A N   1 
ATOM   3401 C CA  . PRO A 1 475 ? 142.440 117.024 160.356 1.00 98.80  ? 462 PRO A CA  1 
ATOM   3402 C C   . PRO A 1 475 ? 142.531 116.939 161.872 1.00 103.44 ? 462 PRO A C   1 
ATOM   3403 O O   . PRO A 1 475 ? 143.559 116.528 162.419 1.00 104.14 ? 462 PRO A O   1 
ATOM   3404 C CB  . PRO A 1 475 ? 143.622 116.306 159.686 1.00 99.10  ? 462 PRO A CB  1 
ATOM   3405 C CG  . PRO A 1 475 ? 144.041 117.201 158.558 1.00 92.31  ? 462 PRO A CG  1 
ATOM   3406 C CD  . PRO A 1 475 ? 143.752 118.589 159.024 1.00 90.06  ? 462 PRO A CD  1 
ATOM   3407 N N   . ARG A 1 476 ? 141.459 117.323 162.557 1.00 102.99 ? 463 ARG A N   1 
ATOM   3408 C CA  . ARG A 1 476 ? 141.414 117.268 164.015 1.00 101.28 ? 463 ARG A CA  1 
ATOM   3409 C C   . ARG A 1 476 ? 141.278 115.831 164.508 1.00 98.25  ? 463 ARG A C   1 
ATOM   3410 O O   . ARG A 1 476 ? 141.205 115.581 165.711 1.00 96.45  ? 463 ARG A O   1 
ATOM   3411 C CB  . ARG A 1 476 ? 140.259 118.120 164.547 1.00 96.09  ? 463 ARG A CB  1 
ATOM   3412 C CG  . ARG A 1 476 ? 140.473 119.619 164.408 1.00 95.27  ? 463 ARG A CG  1 
ATOM   3413 C CD  . ARG A 1 476 ? 141.336 120.161 165.537 1.00 91.26  ? 463 ARG A CD  1 
ATOM   3414 N NE  . ARG A 1 476 ? 141.752 121.537 165.293 1.00 85.01  ? 463 ARG A NE  1 
ATOM   3415 C CZ  . ARG A 1 476 ? 141.030 122.608 165.593 1.00 81.78  ? 463 ARG A CZ  1 
ATOM   3416 N NH1 . ARG A 1 476 ? 139.833 122.503 166.148 1.00 82.30  ? 463 ARG A NH1 1 
ATOM   3417 N NH2 . ARG A 1 476 ? 141.521 123.815 165.329 1.00 79.61  ? 463 ARG A NH2 1 
ATOM   3418 N N   . TYR B 1 19  ? 156.371 128.166 129.245 1.00 172.94 ? 6   TYR B N   1 
ATOM   3419 C CA  . TYR B 1 19  ? 156.207 128.770 130.562 1.00 172.30 ? 6   TYR B CA  1 
ATOM   3420 C C   . TYR B 1 19  ? 155.242 127.939 131.402 1.00 169.86 ? 6   TYR B C   1 
ATOM   3421 O O   . TYR B 1 19  ? 154.348 127.282 130.866 1.00 166.49 ? 6   TYR B O   1 
ATOM   3422 C CB  . TYR B 1 19  ? 155.704 130.210 130.431 1.00 170.49 ? 6   TYR B CB  1 
ATOM   3423 C CG  . TYR B 1 19  ? 156.210 131.155 131.500 1.00 172.37 ? 6   TYR B CG  1 
ATOM   3424 C CD1 . TYR B 1 19  ? 155.467 131.403 132.646 1.00 172.16 ? 6   TYR B CD1 1 
ATOM   3425 C CD2 . TYR B 1 19  ? 157.429 131.808 131.357 1.00 172.97 ? 6   TYR B CD2 1 
ATOM   3426 C CE1 . TYR B 1 19  ? 155.924 132.270 133.622 1.00 170.95 ? 6   TYR B CE1 1 
ATOM   3427 C CE2 . TYR B 1 19  ? 157.895 132.677 132.328 1.00 172.19 ? 6   TYR B CE2 1 
ATOM   3428 C CZ  . TYR B 1 19  ? 157.138 132.904 133.458 1.00 171.97 ? 6   TYR B CZ  1 
ATOM   3429 O OH  . TYR B 1 19  ? 157.598 133.767 134.426 1.00 175.50 ? 6   TYR B OH  1 
ATOM   3430 N N   . HIS B 1 20  ? 155.432 127.964 132.723 1.00 171.17 ? 7   HIS B N   1 
ATOM   3431 C CA  . HIS B 1 20  ? 154.590 127.159 133.602 1.00 168.57 ? 7   HIS B CA  1 
ATOM   3432 C C   . HIS B 1 20  ? 153.153 127.664 133.627 1.00 164.15 ? 7   HIS B C   1 
ATOM   3433 O O   . HIS B 1 20  ? 152.226 126.880 133.859 1.00 155.78 ? 7   HIS B O   1 
ATOM   3434 C CB  . HIS B 1 20  ? 155.172 127.136 135.016 1.00 171.65 ? 7   HIS B CB  1 
ATOM   3435 C CG  . HIS B 1 20  ? 154.909 128.383 135.801 1.00 172.43 ? 7   HIS B CG  1 
ATOM   3436 N ND1 . HIS B 1 20  ? 155.648 129.535 135.642 1.00 173.14 ? 7   HIS B ND1 1 
ATOM   3437 C CD2 . HIS B 1 20  ? 153.990 128.655 136.757 1.00 168.56 ? 7   HIS B CD2 1 
ATOM   3438 C CE1 . HIS B 1 20  ? 155.194 130.464 136.464 1.00 170.82 ? 7   HIS B CE1 1 
ATOM   3439 N NE2 . HIS B 1 20  ? 154.188 129.956 137.152 1.00 168.46 ? 7   HIS B NE2 1 
ATOM   3440 N N   . VAL B 1 21  ? 152.947 128.963 133.398 1.00 168.28 ? 8   VAL B N   1 
ATOM   3441 C CA  . VAL B 1 21  ? 151.598 129.521 133.425 1.00 164.92 ? 8   VAL B CA  1 
ATOM   3442 C C   . VAL B 1 21  ? 150.751 128.935 132.302 1.00 158.28 ? 8   VAL B C   1 
ATOM   3443 O O   . VAL B 1 21  ? 149.577 128.601 132.501 1.00 155.64 ? 8   VAL B O   1 
ATOM   3444 C CB  . VAL B 1 21  ? 151.655 131.058 133.352 1.00 165.67 ? 8   VAL B CB  1 
ATOM   3445 C CG1 . VAL B 1 21  ? 150.252 131.648 133.372 1.00 163.53 ? 8   VAL B CG1 1 
ATOM   3446 C CG2 . VAL B 1 21  ? 152.482 131.612 134.500 1.00 165.79 ? 8   VAL B CG2 1 
ATOM   3447 N N   . LEU B 1 22  ? 151.331 128.796 131.106 1.00 159.27 ? 9   LEU B N   1 
ATOM   3448 C CA  . LEU B 1 22  ? 150.582 128.256 129.976 1.00 155.45 ? 9   LEU B CA  1 
ATOM   3449 C C   . LEU B 1 22  ? 150.124 126.828 130.247 1.00 152.24 ? 9   LEU B C   1 
ATOM   3450 O O   . LEU B 1 22  ? 148.986 126.462 129.931 1.00 145.88 ? 9   LEU B O   1 
ATOM   3451 C CB  . LEU B 1 22  ? 151.428 128.315 128.703 1.00 158.12 ? 9   LEU B CB  1 
ATOM   3452 C CG  . LEU B 1 22  ? 151.583 129.662 127.985 1.00 158.35 ? 9   LEU B CG  1 
ATOM   3453 C CD1 . LEU B 1 22  ? 152.464 130.633 128.763 1.00 160.18 ? 9   LEU B CD1 1 
ATOM   3454 C CD2 . LEU B 1 22  ? 152.127 129.456 126.578 1.00 155.97 ? 9   LEU B CD2 1 
ATOM   3455 N N   . PHE B 1 23  ? 150.999 126.007 130.832 1.00 153.56 ? 10  PHE B N   1 
ATOM   3456 C CA  . PHE B 1 23  ? 150.621 124.636 131.162 1.00 148.89 ? 10  PHE B CA  1 
ATOM   3457 C C   . PHE B 1 23  ? 149.596 124.595 132.289 1.00 141.88 ? 10  PHE B C   1 
ATOM   3458 O O   . PHE B 1 23  ? 148.622 123.836 132.222 1.00 130.70 ? 10  PHE B O   1 
ATOM   3459 C CB  . PHE B 1 23  ? 151.866 123.830 131.535 1.00 145.45 ? 10  PHE B CB  1 
ATOM   3460 C CG  . PHE B 1 23  ? 151.587 122.663 132.439 1.00 143.10 ? 10  PHE B CG  1 
ATOM   3461 C CD1 . PHE B 1 23  ? 150.984 121.517 131.949 1.00 140.53 ? 10  PHE B CD1 1 
ATOM   3462 C CD2 . PHE B 1 23  ? 151.938 122.710 133.778 1.00 141.71 ? 10  PHE B CD2 1 
ATOM   3463 C CE1 . PHE B 1 23  ? 150.730 120.442 132.780 1.00 134.25 ? 10  PHE B CE1 1 
ATOM   3464 C CE2 . PHE B 1 23  ? 151.688 121.637 134.613 1.00 138.11 ? 10  PHE B CE2 1 
ATOM   3465 C CZ  . PHE B 1 23  ? 151.082 120.503 134.114 1.00 132.99 ? 10  PHE B CZ  1 
ATOM   3466 N N   . ASP B 1 24  ? 149.795 125.406 133.331 1.00 141.99 ? 11  ASP B N   1 
ATOM   3467 C CA  . ASP B 1 24  ? 148.914 125.365 134.492 1.00 135.60 ? 11  ASP B CA  1 
ATOM   3468 C C   . ASP B 1 24  ? 147.557 126.003 134.232 1.00 128.51 ? 11  ASP B C   1 
ATOM   3469 O O   . ASP B 1 24  ? 146.633 125.784 135.020 1.00 123.01 ? 11  ASP B O   1 
ATOM   3470 C CB  . ASP B 1 24  ? 149.579 126.052 135.685 1.00 141.01 ? 11  ASP B CB  1 
ATOM   3471 C CG  . ASP B 1 24  ? 150.347 125.084 136.562 1.00 141.49 ? 11  ASP B CG  1 
ATOM   3472 O OD1 . ASP B 1 24  ? 150.313 123.869 136.281 1.00 134.66 ? 11  ASP B OD1 1 
ATOM   3473 O OD2 . ASP B 1 24  ? 150.982 125.539 137.537 1.00 146.70 ? 11  ASP B OD2 1 
ATOM   3474 N N   . SER B 1 25  ? 147.414 126.781 133.155 1.00 130.41 ? 12  SER B N   1 
ATOM   3475 C CA  . SER B 1 25  ? 146.155 127.479 132.915 1.00 123.97 ? 12  SER B CA  1 
ATOM   3476 C C   . SER B 1 25  ? 144.990 126.507 132.784 1.00 115.73 ? 12  SER B C   1 
ATOM   3477 O O   . SER B 1 25  ? 143.901 126.755 133.317 1.00 111.14 ? 12  SER B O   1 
ATOM   3478 C CB  . SER B 1 25  ? 146.270 128.348 131.663 1.00 124.45 ? 12  SER B CB  1 
ATOM   3479 O OG  . SER B 1 25  ? 146.557 127.559 130.522 1.00 127.63 ? 12  SER B OG  1 
ATOM   3480 N N   . TYR B 1 26  ? 145.195 125.397 132.078 1.00 113.97 ? 13  TYR B N   1 
ATOM   3481 C CA  . TYR B 1 26  ? 144.129 124.419 131.908 1.00 106.25 ? 13  TYR B CA  1 
ATOM   3482 C C   . TYR B 1 26  ? 143.968 123.503 133.113 1.00 96.27  ? 13  TYR B C   1 
ATOM   3483 O O   . TYR B 1 26  ? 142.899 122.906 133.278 1.00 91.29  ? 13  TYR B O   1 
ATOM   3484 C CB  . TYR B 1 26  ? 144.381 123.589 130.647 1.00 107.83 ? 13  TYR B CB  1 
ATOM   3485 C CG  . TYR B 1 26  ? 144.417 124.416 129.381 1.00 114.56 ? 13  TYR B CG  1 
ATOM   3486 C CD1 . TYR B 1 26  ? 143.244 124.843 128.775 1.00 114.08 ? 13  TYR B CD1 1 
ATOM   3487 C CD2 . TYR B 1 26  ? 145.625 124.772 128.793 1.00 120.45 ? 13  TYR B CD2 1 
ATOM   3488 C CE1 . TYR B 1 26  ? 143.269 125.600 127.618 1.00 119.80 ? 13  TYR B CE1 1 
ATOM   3489 C CE2 . TYR B 1 26  ? 145.661 125.529 127.635 1.00 122.72 ? 13  TYR B CE2 1 
ATOM   3490 C CZ  . TYR B 1 26  ? 144.479 125.940 127.052 1.00 124.81 ? 13  TYR B CZ  1 
ATOM   3491 O OH  . TYR B 1 26  ? 144.507 126.693 125.901 1.00 126.10 ? 13  TYR B OH  1 
ATOM   3492 N N   . ARG B 1 27  ? 144.994 123.378 133.955 1.00 96.55  ? 14  ARG B N   1 
ATOM   3493 C CA  . ARG B 1 27  ? 144.947 122.508 135.122 1.00 94.65  ? 14  ARG B CA  1 
ATOM   3494 C C   . ARG B 1 27  ? 144.861 123.271 136.440 1.00 91.95  ? 14  ARG B C   1 
ATOM   3495 O O   . ARG B 1 27  ? 144.994 122.658 137.504 1.00 84.82  ? 14  ARG B O   1 
ATOM   3496 C CB  . ARG B 1 27  ? 146.166 121.583 135.142 1.00 94.28  ? 14  ARG B CB  1 
ATOM   3497 C CG  . ARG B 1 27  ? 146.133 120.482 134.098 1.00 90.06  ? 14  ARG B CG  1 
ATOM   3498 C CD  . ARG B 1 27  ? 147.272 119.491 134.297 1.00 97.47  ? 14  ARG B CD  1 
ATOM   3499 N NE  . ARG B 1 27  ? 147.186 118.798 135.578 1.00 94.10  ? 14  ARG B NE  1 
ATOM   3500 C CZ  . ARG B 1 27  ? 147.908 119.102 136.648 1.00 98.88  ? 14  ARG B CZ  1 
ATOM   3501 N NH1 . ARG B 1 27  ? 148.793 120.085 136.628 1.00 103.16 ? 14  ARG B NH1 1 
ATOM   3502 N NH2 . ARG B 1 27  ? 147.738 118.402 137.766 1.00 93.51  ? 14  ARG B NH2 1 
ATOM   3503 N N   . ASP B 1 28  ? 144.643 124.583 136.402 1.00 94.82  ? 15  ASP B N   1 
ATOM   3504 C CA  . ASP B 1 28  ? 144.529 125.375 137.625 1.00 86.96  ? 15  ASP B CA  1 
ATOM   3505 C C   . ASP B 1 28  ? 143.098 125.266 138.130 1.00 77.00  ? 15  ASP B C   1 
ATOM   3506 O O   . ASP B 1 28  ? 142.198 125.955 137.642 1.00 74.44  ? 15  ASP B O   1 
ATOM   3507 C CB  . ASP B 1 28  ? 144.921 126.825 137.368 1.00 93.62  ? 15  ASP B CB  1 
ATOM   3508 C CG  . ASP B 1 28  ? 144.449 127.761 138.460 1.00 82.87  ? 15  ASP B CG  1 
ATOM   3509 O OD1 . ASP B 1 28  ? 145.030 127.738 139.565 1.00 81.59  ? 15  ASP B OD1 1 
ATOM   3510 O OD2 . ASP B 1 28  ? 143.491 128.522 138.208 1.00 73.27  ? 15  ASP B OD2 1 
ATOM   3511 N N   . ASN B 1 29  ? 142.885 124.402 139.116 1.00 72.31  ? 16  ASN B N   1 
ATOM   3512 C CA  . ASN B 1 29  ? 141.556 124.178 139.675 1.00 64.09  ? 16  ASN B CA  1 
ATOM   3513 C C   . ASN B 1 29  ? 141.711 123.449 141.004 1.00 65.63  ? 16  ASN B C   1 
ATOM   3514 O O   . ASN B 1 29  ? 142.812 123.044 141.390 1.00 71.81  ? 16  ASN B O   1 
ATOM   3515 C CB  . ASN B 1 29  ? 140.669 123.388 138.716 1.00 52.83  ? 16  ASN B CB  1 
ATOM   3516 C CG  . ASN B 1 29  ? 139.224 123.794 138.811 1.00 50.20  ? 16  ASN B CG  1 
ATOM   3517 O OD1 . ASN B 1 29  ? 138.777 124.693 138.104 1.00 50.17  ? 16  ASN B OD1 1 
ATOM   3518 N ND2 . ASN B 1 29  ? 138.489 123.155 139.704 1.00 54.22  ? 16  ASN B ND2 1 
ATOM   3519 N N   . ILE B 1 30  ? 140.584 123.280 141.699 1.00 59.23  ? 17  ILE B N   1 
ATOM   3520 C CA  . ILE B 1 30  ? 140.588 122.602 142.993 1.00 55.06  ? 17  ILE B CA  1 
ATOM   3521 C C   . ILE B 1 30  ? 140.986 121.140 142.829 1.00 58.88  ? 17  ILE B C   1 
ATOM   3522 O O   . ILE B 1 30  ? 141.843 120.625 143.556 1.00 66.46  ? 17  ILE B O   1 
ATOM   3523 C CB  . ILE B 1 30  ? 139.213 122.736 143.669 1.00 44.62  ? 17  ILE B CB  1 
ATOM   3524 C CG1 . ILE B 1 30  ? 138.848 124.209 143.839 1.00 41.38  ? 17  ILE B CG1 1 
ATOM   3525 C CG2 . ILE B 1 30  ? 139.209 122.030 145.009 1.00 51.68  ? 17  ILE B CG2 1 
ATOM   3526 C CD1 . ILE B 1 30  ? 137.646 124.438 144.710 1.00 32.57  ? 17  ILE B CD1 1 
ATOM   3527 N N   . ALA B 1 31  ? 140.368 120.451 141.868 1.00 51.01  ? 18  ALA B N   1 
ATOM   3528 C CA  . ALA B 1 31  ? 140.662 119.040 141.656 1.00 54.41  ? 18  ALA B CA  1 
ATOM   3529 C C   . ALA B 1 31  ? 142.059 118.809 141.100 1.00 61.94  ? 18  ALA B C   1 
ATOM   3530 O O   . ALA B 1 31  ? 142.583 117.697 141.222 1.00 67.78  ? 18  ALA B O   1 
ATOM   3531 C CB  . ALA B 1 31  ? 139.625 118.421 140.720 1.00 54.92  ? 18  ALA B CB  1 
ATOM   3532 N N   . GLY B 1 32  ? 142.671 119.822 140.489 1.00 61.60  ? 19  GLY B N   1 
ATOM   3533 C CA  . GLY B 1 32  ? 143.980 119.643 139.898 1.00 67.17  ? 19  GLY B CA  1 
ATOM   3534 C C   . GLY B 1 32  ? 143.996 118.836 138.622 1.00 75.23  ? 19  GLY B C   1 
ATOM   3535 O O   . GLY B 1 32  ? 145.071 118.414 138.186 1.00 81.14  ? 19  GLY B O   1 
ATOM   3536 N N   . LYS B 1 33  ? 142.839 118.605 138.009 1.00 69.71  ? 20  LYS B N   1 
ATOM   3537 C CA  . LYS B 1 33  ? 142.727 117.779 136.818 1.00 65.08  ? 20  LYS B CA  1 
ATOM   3538 C C   . LYS B 1 33  ? 142.287 118.629 135.634 1.00 64.32  ? 20  LYS B C   1 
ATOM   3539 O O   . LYS B 1 33  ? 141.621 119.656 135.798 1.00 63.47  ? 20  LYS B O   1 
ATOM   3540 C CB  . LYS B 1 33  ? 141.732 116.635 137.030 1.00 65.83  ? 20  LYS B CB  1 
ATOM   3541 C CG  . LYS B 1 33  ? 141.840 115.965 138.389 1.00 64.33  ? 20  LYS B CG  1 
ATOM   3542 C CD  . LYS B 1 33  ? 140.804 114.865 138.544 1.00 68.61  ? 20  LYS B CD  1 
ATOM   3543 C CE  . LYS B 1 33  ? 140.628 114.480 140.003 1.00 69.87  ? 20  LYS B CE  1 
ATOM   3544 N NZ  . LYS B 1 33  ? 141.917 114.103 140.645 1.00 65.62  ? 20  LYS B NZ  1 
ATOM   3545 N N   . SER B 1 34  ? 142.665 118.188 134.439 1.00 67.60  ? 21  SER B N   1 
ATOM   3546 C CA  . SER B 1 34  ? 142.330 118.892 133.208 1.00 67.73  ? 21  SER B CA  1 
ATOM   3547 C C   . SER B 1 34  ? 141.019 118.345 132.654 1.00 67.43  ? 21  SER B C   1 
ATOM   3548 O O   . SER B 1 34  ? 140.912 117.149 132.364 1.00 70.02  ? 21  SER B O   1 
ATOM   3549 C CB  . SER B 1 34  ? 143.453 118.744 132.183 1.00 73.67  ? 21  SER B CB  1 
ATOM   3550 O OG  . SER B 1 34  ? 143.132 119.411 130.976 1.00 70.26  ? 21  SER B OG  1 
ATOM   3551 N N   . PHE B 1 35  ? 140.025 119.224 132.507 1.00 66.14  ? 22  PHE B N   1 
ATOM   3552 C CA  . PHE B 1 35  ? 138.712 118.859 131.988 1.00 61.05  ? 22  PHE B CA  1 
ATOM   3553 C C   . PHE B 1 35  ? 138.544 119.248 130.522 1.00 61.99  ? 22  PHE B C   1 
ATOM   3554 O O   . PHE B 1 35  ? 137.430 119.558 130.085 1.00 58.03  ? 22  PHE B O   1 
ATOM   3555 C CB  . PHE B 1 35  ? 137.609 119.503 132.831 1.00 51.50  ? 22  PHE B CB  1 
ATOM   3556 C CG  . PHE B 1 35  ? 137.592 119.055 134.268 1.00 44.82  ? 22  PHE B CG  1 
ATOM   3557 C CD1 . PHE B 1 35  ? 138.225 117.889 134.660 1.00 50.44  ? 22  PHE B CD1 1 
ATOM   3558 C CD2 . PHE B 1 35  ? 136.928 119.803 135.225 1.00 44.71  ? 22  PHE B CD2 1 
ATOM   3559 C CE1 . PHE B 1 35  ? 138.202 117.483 135.983 1.00 55.88  ? 22  PHE B CE1 1 
ATOM   3560 C CE2 . PHE B 1 35  ? 136.902 119.401 136.546 1.00 45.88  ? 22  PHE B CE2 1 
ATOM   3561 C CZ  . PHE B 1 35  ? 137.539 118.240 136.925 1.00 44.95  ? 22  PHE B CZ  1 
ATOM   3562 N N   . GLN B 1 36  ? 139.634 119.234 129.752 1.00 65.55  ? 23  GLN B N   1 
ATOM   3563 C CA  . GLN B 1 36  ? 139.576 119.691 128.366 1.00 66.62  ? 23  GLN B CA  1 
ATOM   3564 C C   . GLN B 1 36  ? 138.755 118.747 127.496 1.00 71.35  ? 23  GLN B C   1 
ATOM   3565 O O   . GLN B 1 36  ? 138.105 119.184 126.540 1.00 74.67  ? 23  GLN B O   1 
ATOM   3566 C CB  . GLN B 1 36  ? 140.988 119.848 127.806 1.00 67.40  ? 23  GLN B CB  1 
ATOM   3567 C CG  . GLN B 1 36  ? 141.781 120.957 128.466 1.00 78.32  ? 23  GLN B CG  1 
ATOM   3568 C CD  . GLN B 1 36  ? 141.095 122.302 128.350 1.00 89.23  ? 23  GLN B CD  1 
ATOM   3569 O OE1 . GLN B 1 36  ? 140.734 122.918 129.352 1.00 89.44  ? 23  GLN B OE1 1 
ATOM   3570 N NE2 . GLN B 1 36  ? 140.916 122.767 127.121 1.00 90.09  ? 23  GLN B NE2 1 
ATOM   3571 N N   . ASN B 1 37  ? 138.777 117.448 127.804 1.00 69.33  ? 24  ASN B N   1 
ATOM   3572 C CA  . ASN B 1 37  ? 138.022 116.478 127.022 1.00 66.38  ? 24  ASN B CA  1 
ATOM   3573 C C   . ASN B 1 37  ? 136.515 116.657 127.149 1.00 64.03  ? 24  ASN B C   1 
ATOM   3574 O O   . ASN B 1 37  ? 135.770 116.067 126.359 1.00 57.47  ? 24  ASN B O   1 
ATOM   3575 C CB  . ASN B 1 37  ? 138.412 115.057 127.434 1.00 71.14  ? 24  ASN B CB  1 
ATOM   3576 C CG  . ASN B 1 37  ? 138.339 114.842 128.934 1.00 71.08  ? 24  ASN B CG  1 
ATOM   3577 O OD1 . ASN B 1 37  ? 137.703 115.611 129.656 1.00 64.81  ? 24  ASN B OD1 1 
ATOM   3578 N ND2 . ASN B 1 37  ? 138.993 113.791 129.412 1.00 80.60  ? 24  ASN B ND2 1 
ATOM   3579 N N   . ARG B 1 38  ? 136.051 117.440 128.119 1.00 63.05  ? 25  ARG B N   1 
ATOM   3580 C CA  . ARG B 1 38  ? 134.629 117.684 128.325 1.00 58.31  ? 25  ARG B CA  1 
ATOM   3581 C C   . ARG B 1 38  ? 134.210 119.110 128.012 1.00 59.85  ? 25  ARG B C   1 
ATOM   3582 O O   . ARG B 1 38  ? 133.137 119.319 127.444 1.00 67.95  ? 25  ARG B O   1 
ATOM   3583 C CB  . ARG B 1 38  ? 134.249 117.350 129.774 1.00 52.33  ? 25  ARG B CB  1 
ATOM   3584 C CG  . ARG B 1 38  ? 132.810 116.901 129.976 1.00 47.58  ? 25  ARG B CG  1 
ATOM   3585 C CD  . ARG B 1 38  ? 131.857 118.078 130.065 1.00 41.73  ? 25  ARG B CD  1 
ATOM   3586 N NE  . ARG B 1 38  ? 130.475 117.653 130.239 1.00 43.75  ? 25  ARG B NE  1 
ATOM   3587 C CZ  . ARG B 1 38  ? 129.432 118.468 130.176 1.00 41.93  ? 25  ARG B CZ  1 
ATOM   3588 N NH1 . ARG B 1 38  ? 129.578 119.758 129.924 1.00 42.52  ? 25  ARG B NH1 1 
ATOM   3589 N NH2 . ARG B 1 38  ? 128.212 117.977 130.369 1.00 43.61  ? 25  ARG B NH2 1 
ATOM   3590 N N   . LEU B 1 39  ? 135.028 120.102 128.360 1.00 56.00  ? 26  LEU B N   1 
ATOM   3591 C CA  . LEU B 1 39  ? 134.633 121.498 128.235 1.00 58.15  ? 26  LEU B CA  1 
ATOM   3592 C C   . LEU B 1 39  ? 134.927 122.099 126.867 1.00 58.70  ? 26  LEU B C   1 
ATOM   3593 O O   . LEU B 1 39  ? 134.453 123.203 126.583 1.00 58.44  ? 26  LEU B O   1 
ATOM   3594 C CB  . LEU B 1 39  ? 135.331 122.344 129.308 1.00 56.15  ? 26  LEU B CB  1 
ATOM   3595 C CG  . LEU B 1 39  ? 134.968 122.077 130.770 1.00 54.21  ? 26  LEU B CG  1 
ATOM   3596 C CD1 . LEU B 1 39  ? 135.734 123.006 131.697 1.00 42.45  ? 26  LEU B CD1 1 
ATOM   3597 C CD2 . LEU B 1 39  ? 133.473 122.225 130.980 1.00 51.37  ? 26  LEU B CD2 1 
ATOM   3598 N N   . CYS B 1 40  ? 135.682 121.413 126.011 1.00 59.21  ? 27  CYS B N   1 
ATOM   3599 C CA  . CYS B 1 40  ? 136.173 122.018 124.780 1.00 61.86  ? 27  CYS B CA  1 
ATOM   3600 C C   . CYS B 1 40  ? 135.499 121.469 123.526 1.00 61.66  ? 27  CYS B C   1 
ATOM   3601 O O   . CYS B 1 40  ? 136.017 121.668 122.423 1.00 64.71  ? 27  CYS B O   1 
ATOM   3602 C CB  . CYS B 1 40  ? 137.687 121.843 124.677 1.00 66.92  ? 27  CYS B CB  1 
ATOM   3603 S SG  . CYS B 1 40  ? 138.666 123.024 125.630 1.00 87.28  ? 27  CYS B SG  1 
ATOM   3604 N N   . LEU B 1 41  ? 134.361 120.777 123.671 1.00 53.77  ? 28  LEU B N   1 
ATOM   3605 C CA  . LEU B 1 41  ? 133.568 120.251 122.560 1.00 53.29  ? 28  LEU B CA  1 
ATOM   3606 C C   . LEU B 1 41  ? 134.324 119.152 121.813 1.00 54.68  ? 28  LEU B C   1 
ATOM   3607 O O   . LEU B 1 41  ? 135.553 119.059 121.918 1.00 55.91  ? 28  LEU B O   1 
ATOM   3608 C CB  . LEU B 1 41  ? 133.160 121.380 121.606 1.00 47.95  ? 28  LEU B CB  1 
ATOM   3609 C CG  . LEU B 1 41  ? 132.028 122.303 122.067 1.00 48.08  ? 28  LEU B CG  1 
ATOM   3610 C CD1 . LEU B 1 41  ? 131.816 123.444 121.084 1.00 44.21  ? 28  LEU B CD1 1 
ATOM   3611 C CD2 . LEU B 1 41  ? 130.738 121.520 122.263 1.00 41.48  ? 28  LEU B CD2 1 
ATOM   3612 N N   . PRO B 1 42  ? 133.630 118.281 121.062 1.00 53.74  ? 29  PRO B N   1 
ATOM   3613 C CA  . PRO B 1 42  ? 134.321 117.214 120.323 1.00 51.22  ? 29  PRO B CA  1 
ATOM   3614 C C   . PRO B 1 42  ? 134.988 117.749 119.066 1.00 47.37  ? 29  PRO B C   1 
ATOM   3615 O O   . PRO B 1 42  ? 134.321 118.077 118.079 1.00 44.44  ? 29  PRO B O   1 
ATOM   3616 C CB  . PRO B 1 42  ? 133.187 116.232 119.996 1.00 51.57  ? 29  PRO B CB  1 
ATOM   3617 C CG  . PRO B 1 42  ? 131.982 117.085 119.924 1.00 51.15  ? 29  PRO B CG  1 
ATOM   3618 C CD  . PRO B 1 42  ? 132.165 118.145 120.971 1.00 52.77  ? 29  PRO B CD  1 
ATOM   3619 N N   . MET B 1 43  ? 136.314 117.825 119.094 1.00 47.56  ? 30  MET B N   1 
ATOM   3620 C CA  . MET B 1 43  ? 137.104 118.302 117.971 1.00 45.16  ? 30  MET B CA  1 
ATOM   3621 C C   . MET B 1 43  ? 138.170 117.273 117.630 1.00 40.58  ? 30  MET B C   1 
ATOM   3622 O O   . MET B 1 43  ? 138.629 116.540 118.511 1.00 45.47  ? 30  MET B O   1 
ATOM   3623 C CB  . MET B 1 43  ? 137.772 119.647 118.297 1.00 44.99  ? 30  MET B CB  1 
ATOM   3624 C CG  . MET B 1 43  ? 136.869 120.648 119.003 1.00 51.80  ? 30  MET B CG  1 
ATOM   3625 S SD  . MET B 1 43  ? 135.410 121.095 118.043 1.00 55.88  ? 30  MET B SD  1 
ATOM   3626 C CE  . MET B 1 43  ? 136.165 121.771 116.569 1.00 38.15  ? 30  MET B CE  1 
ATOM   3627 N N   . PRO B 1 44  ? 138.593 117.193 116.358 1.00 33.80  ? 31  PRO B N   1 
ATOM   3628 C CA  . PRO B 1 44  ? 138.159 117.962 115.184 1.00 33.93  ? 31  PRO B CA  1 
ATOM   3629 C C   . PRO B 1 44  ? 136.895 117.405 114.536 1.00 30.25  ? 31  PRO B C   1 
ATOM   3630 O O   . PRO B 1 44  ? 136.378 116.373 114.950 1.00 31.76  ? 31  PRO B O   1 
ATOM   3631 C CB  . PRO B 1 44  ? 139.370 117.848 114.255 1.00 36.11  ? 31  PRO B CB  1 
ATOM   3632 C CG  . PRO B 1 44  ? 139.871 116.459 114.520 1.00 34.70  ? 31  PRO B CG  1 
ATOM   3633 C CD  . PRO B 1 44  ? 139.655 116.234 116.002 1.00 34.98  ? 31  PRO B CD  1 
ATOM   3634 N N   . ILE B 1 45  ? 136.376 118.085 113.515 1.00 27.53  ? 32  ILE B N   1 
ATOM   3635 C CA  . ILE B 1 45  ? 135.196 117.652 112.778 1.00 28.62  ? 32  ILE B CA  1 
ATOM   3636 C C   . ILE B 1 45  ? 135.468 117.821 111.289 1.00 30.96  ? 32  ILE B C   1 
ATOM   3637 O O   . ILE B 1 45  ? 136.001 118.850 110.860 1.00 34.07  ? 32  ILE B O   1 
ATOM   3638 C CB  . ILE B 1 45  ? 133.943 118.447 113.207 1.00 27.75  ? 32  ILE B CB  1 
ATOM   3639 C CG1 . ILE B 1 45  ? 133.564 118.104 114.648 1.00 24.37  ? 32  ILE B CG1 1 
ATOM   3640 C CG2 . ILE B 1 45  ? 132.778 118.173 112.277 1.00 26.77  ? 32  ILE B CG2 1 
ATOM   3641 C CD1 . ILE B 1 45  ? 132.382 118.883 115.174 1.00 29.29  ? 32  ILE B CD1 1 
ATOM   3642 N N   . ASP B 1 46  ? 135.106 116.811 110.502 1.00 30.62  ? 33  ASP B N   1 
ATOM   3643 C CA  . ASP B 1 46  ? 135.316 116.807 109.061 1.00 32.36  ? 33  ASP B CA  1 
ATOM   3644 C C   . ASP B 1 46  ? 133.989 116.945 108.326 1.00 30.53  ? 33  ASP B C   1 
ATOM   3645 O O   . ASP B 1 46  ? 132.908 116.856 108.912 1.00 30.92  ? 33  ASP B O   1 
ATOM   3646 C CB  . ASP B 1 46  ? 136.037 115.530 108.619 1.00 33.85  ? 33  ASP B CB  1 
ATOM   3647 C CG  . ASP B 1 46  ? 137.412 115.411 109.225 1.00 38.61  ? 33  ASP B CG  1 
ATOM   3648 O OD1 . ASP B 1 46  ? 137.775 116.300 110.020 1.00 37.97  ? 33  ASP B OD1 1 
ATOM   3649 O OD2 . ASP B 1 46  ? 138.134 114.442 108.910 1.00 42.28  ? 33  ASP B OD2 1 
ATOM   3650 N N   . VAL B 1 47  ? 134.090 117.173 107.020 1.00 30.40  ? 34  VAL B N   1 
ATOM   3651 C CA  . VAL B 1 47  ? 132.936 117.351 106.147 1.00 31.87  ? 34  VAL B CA  1 
ATOM   3652 C C   . VAL B 1 47  ? 133.066 116.386 104.978 1.00 39.29  ? 34  VAL B C   1 
ATOM   3653 O O   . VAL B 1 47  ? 134.142 116.274 104.380 1.00 43.80  ? 34  VAL B O   1 
ATOM   3654 C CB  . VAL B 1 47  ? 132.825 118.803 105.647 1.00 34.10  ? 34  VAL B CB  1 
ATOM   3655 C CG1 . VAL B 1 47  ? 131.799 118.907 104.541 1.00 37.55  ? 34  VAL B CG1 1 
ATOM   3656 C CG2 . VAL B 1 47  ? 132.462 119.725 106.797 1.00 38.31  ? 34  VAL B CG2 1 
ATOM   3657 N N   . VAL B 1 48  ? 131.978 115.689 104.654 1.00 37.70  ? 35  VAL B N   1 
ATOM   3658 C CA  . VAL B 1 48  ? 131.963 114.699 103.584 1.00 33.43  ? 35  VAL B CA  1 
ATOM   3659 C C   . VAL B 1 48  ? 130.889 115.070 102.569 1.00 36.06  ? 35  VAL B C   1 
ATOM   3660 O O   . VAL B 1 48  ? 129.779 115.466 102.940 1.00 39.69  ? 35  VAL B O   1 
ATOM   3661 C CB  . VAL B 1 48  ? 131.739 113.274 104.131 1.00 27.16  ? 35  VAL B CB  1 
ATOM   3662 C CG1 . VAL B 1 48  ? 133.000 112.768 104.810 1.00 30.05  ? 35  VAL B CG1 1 
ATOM   3663 C CG2 . VAL B 1 48  ? 130.577 113.255 105.101 1.00 28.95  ? 35  VAL B CG2 1 
ATOM   3664 N N   . TYR B 1 49  ? 131.228 114.948 101.286 1.00 34.62  ? 36  TYR B N   1 
ATOM   3665 C CA  . TYR B 1 49  ? 130.336 115.291 100.189 1.00 38.26  ? 36  TYR B CA  1 
ATOM   3666 C C   . TYR B 1 49  ? 130.079 114.073 99.313  1.00 47.35  ? 36  TYR B C   1 
ATOM   3667 O O   . TYR B 1 49  ? 130.952 113.218 99.141  1.00 50.91  ? 36  TYR B O   1 
ATOM   3668 C CB  . TYR B 1 49  ? 130.917 116.410 99.315  1.00 43.31  ? 36  TYR B CB  1 
ATOM   3669 C CG  . TYR B 1 49  ? 130.725 117.811 99.845  1.00 47.84  ? 36  TYR B CG  1 
ATOM   3670 C CD1 . TYR B 1 49  ? 129.559 118.515 99.585  1.00 49.71  ? 36  TYR B CD1 1 
ATOM   3671 C CD2 . TYR B 1 49  ? 131.719 118.439 100.580 1.00 48.01  ? 36  TYR B CD2 1 
ATOM   3672 C CE1 . TYR B 1 49  ? 129.383 119.799 100.056 1.00 50.39  ? 36  TYR B CE1 1 
ATOM   3673 C CE2 . TYR B 1 49  ? 131.549 119.721 101.056 1.00 46.60  ? 36  TYR B CE2 1 
ATOM   3674 C CZ  . TYR B 1 49  ? 130.379 120.396 100.792 1.00 48.59  ? 36  TYR B CZ  1 
ATOM   3675 O OH  . TYR B 1 49  ? 130.205 121.675 101.263 1.00 52.64  ? 36  TYR B OH  1 
ATOM   3676 N N   . THR B 1 50  ? 128.874 114.009 98.751  1.00 50.51  ? 37  THR B N   1 
ATOM   3677 C CA  . THR B 1 50  ? 128.504 112.993 97.766  1.00 52.33  ? 37  THR B CA  1 
ATOM   3678 C C   . THR B 1 50  ? 128.045 113.724 96.508  1.00 60.38  ? 37  THR B C   1 
ATOM   3679 O O   . THR B 1 50  ? 126.927 114.248 96.459  1.00 65.22  ? 37  THR B O   1 
ATOM   3680 C CB  . THR B 1 50  ? 127.415 112.066 98.298  1.00 46.53  ? 37  THR B CB  1 
ATOM   3681 O OG1 . THR B 1 50  ? 126.254 112.832 98.640  1.00 51.99  ? 37  THR B OG1 1 
ATOM   3682 C CG2 . THR B 1 50  ? 127.904 111.320 99.526  1.00 37.19  ? 37  THR B CG2 1 
ATOM   3683 N N   . TRP B 1 51  ? 128.903 113.754 95.492  1.00 57.99  ? 38  TRP B N   1 
ATOM   3684 C CA  . TRP B 1 51  ? 128.634 114.475 94.258  1.00 63.58  ? 38  TRP B CA  1 
ATOM   3685 C C   . TRP B 1 51  ? 128.825 113.548 93.067  1.00 70.15  ? 38  TRP B C   1 
ATOM   3686 O O   . TRP B 1 51  ? 129.666 112.645 93.089  1.00 71.92  ? 38  TRP B O   1 
ATOM   3687 C CB  . TRP B 1 51  ? 129.543 115.711 94.134  1.00 63.92  ? 38  TRP B CB  1 
ATOM   3688 C CG  . TRP B 1 51  ? 129.657 116.267 92.748  1.00 67.52  ? 38  TRP B CG  1 
ATOM   3689 C CD1 . TRP B 1 51  ? 128.705 116.955 92.055  1.00 66.27  ? 38  TRP B CD1 1 
ATOM   3690 C CD2 . TRP B 1 51  ? 130.800 116.191 91.891  1.00 69.85  ? 38  TRP B CD2 1 
ATOM   3691 N NE1 . TRP B 1 51  ? 129.183 117.306 90.816  1.00 63.72  ? 38  TRP B NE1 1 
ATOM   3692 C CE2 . TRP B 1 51  ? 130.468 116.849 90.692  1.00 67.68  ? 38  TRP B CE2 1 
ATOM   3693 C CE3 . TRP B 1 51  ? 132.072 115.628 92.021  1.00 72.65  ? 38  TRP B CE3 1 
ATOM   3694 C CZ2 . TRP B 1 51  ? 131.361 116.958 89.631  1.00 72.36  ? 38  TRP B CZ2 1 
ATOM   3695 C CZ3 . TRP B 1 51  ? 132.956 115.736 90.967  1.00 65.85  ? 38  TRP B CZ3 1 
ATOM   3696 C CH2 . TRP B 1 51  ? 132.598 116.396 89.787  1.00 67.74  ? 38  TRP B CH2 1 
ATOM   3697 N N   . VAL B 1 52  ? 128.018 113.770 92.032  1.00 73.11  ? 39  VAL B N   1 
ATOM   3698 C CA  . VAL B 1 52  ? 128.092 113.013 90.787  1.00 73.31  ? 39  VAL B CA  1 
ATOM   3699 C C   . VAL B 1 52  ? 127.778 113.962 89.638  1.00 79.27  ? 39  VAL B C   1 
ATOM   3700 O O   . VAL B 1 52  ? 126.966 114.882 89.784  1.00 82.47  ? 39  VAL B O   1 
ATOM   3701 C CB  . VAL B 1 52  ? 127.132 111.802 90.799  1.00 75.53  ? 39  VAL B CB  1 
ATOM   3702 C CG1 . VAL B 1 52  ? 125.682 112.260 90.897  1.00 74.47  ? 39  VAL B CG1 1 
ATOM   3703 C CG2 . VAL B 1 52  ? 127.347 110.930 89.573  1.00 82.59  ? 39  VAL B CG2 1 
ATOM   3704 N N   . ASN B 1 53  ? 128.434 113.751 88.502  1.00 82.22  ? 40  ASN B N   1 
ATOM   3705 C CA  . ASN B 1 53  ? 128.280 114.614 87.341  1.00 87.11  ? 40  ASN B CA  1 
ATOM   3706 C C   . ASN B 1 53  ? 127.639 113.849 86.192  1.00 97.61  ? 40  ASN B C   1 
ATOM   3707 O O   . ASN B 1 53  ? 127.867 112.649 86.017  1.00 103.55 ? 40  ASN B O   1 
ATOM   3708 C CB  . ASN B 1 53  ? 129.629 115.180 86.892  1.00 86.72  ? 40  ASN B CB  1 
ATOM   3709 C CG  . ASN B 1 53  ? 129.494 116.174 85.758  1.00 92.42  ? 40  ASN B CG  1 
ATOM   3710 O OD1 . ASN B 1 53  ? 128.446 116.797 85.586  1.00 97.03  ? 40  ASN B OD1 1 
ATOM   3711 N ND2 . ASN B 1 53  ? 130.555 116.326 84.975  1.00 87.76  ? 40  ASN B ND2 1 
ATOM   3712 N N   . GLY B 1 54  ? 126.832 114.559 85.407  1.00 104.77 ? 41  GLY B N   1 
ATOM   3713 C CA  . GLY B 1 54  ? 126.205 113.971 84.240  1.00 111.85 ? 41  GLY B CA  1 
ATOM   3714 C C   . GLY B 1 54  ? 127.104 114.002 83.022  1.00 111.85 ? 41  GLY B C   1 
ATOM   3715 O O   . GLY B 1 54  ? 126.815 114.697 82.043  1.00 108.40 ? 41  GLY B O   1 
ATOM   3716 N N   . THR B 1 55  ? 128.198 113.250 83.074  1.00 115.35 ? 42  THR B N   1 
ATOM   3717 C CA  . THR B 1 55  ? 129.160 113.199 81.985  1.00 118.37 ? 42  THR B CA  1 
ATOM   3718 C C   . THR B 1 55  ? 128.740 112.161 80.948  1.00 130.93 ? 42  THR B C   1 
ATOM   3719 O O   . THR B 1 55  ? 127.764 111.428 81.118  1.00 133.60 ? 42  THR B O   1 
ATOM   3720 C CB  . THR B 1 55  ? 130.558 112.882 82.514  1.00 116.04 ? 42  THR B CB  1 
ATOM   3721 O OG1 . THR B 1 55  ? 131.494 112.905 81.430  1.00 125.21 ? 42  THR B OG1 1 
ATOM   3722 C CG2 . THR B 1 55  ? 130.583 111.507 83.160  1.00 114.60 ? 42  THR B CG2 1 
ATOM   3723 N N   . ASP B 1 56  ? 129.498 112.111 79.850  1.00 137.09 ? 43  ASP B N   1 
ATOM   3724 C CA  . ASP B 1 56  ? 129.177 111.183 78.771  1.00 140.21 ? 43  ASP B CA  1 
ATOM   3725 C C   . ASP B 1 56  ? 129.329 109.735 79.219  1.00 137.72 ? 43  ASP B C   1 
ATOM   3726 O O   . ASP B 1 56  ? 128.492 108.887 78.892  1.00 135.57 ? 43  ASP B O   1 
ATOM   3727 C CB  . ASP B 1 56  ? 130.062 111.466 77.557  1.00 143.46 ? 43  ASP B CB  1 
ATOM   3728 C CG  . ASP B 1 56  ? 129.574 110.766 76.304  1.00 140.19 ? 43  ASP B CG  1 
ATOM   3729 O OD1 . ASP B 1 56  ? 128.466 110.190 76.336  1.00 139.62 ? 43  ASP B OD1 1 
ATOM   3730 O OD2 . ASP B 1 56  ? 130.297 110.792 75.287  1.00 135.64 ? 43  ASP B OD2 1 
ATOM   3731 N N   . LEU B 1 57  ? 130.397 109.429 79.959  1.00 135.94 ? 44  LEU B N   1 
ATOM   3732 C CA  . LEU B 1 57  ? 130.630 108.053 80.389  1.00 139.18 ? 44  LEU B CA  1 
ATOM   3733 C C   . LEU B 1 57  ? 129.549 107.579 81.354  1.00 140.84 ? 44  LEU B C   1 
ATOM   3734 O O   . LEU B 1 57  ? 129.076 106.442 81.253  1.00 140.88 ? 44  LEU B O   1 
ATOM   3735 C CB  . LEU B 1 57  ? 132.017 107.925 81.020  1.00 139.24 ? 44  LEU B CB  1 
ATOM   3736 C CG  . LEU B 1 57  ? 133.163 107.578 80.063  1.00 138.64 ? 44  LEU B CG  1 
ATOM   3737 C CD1 . LEU B 1 57  ? 133.327 108.635 78.978  1.00 134.59 ? 44  LEU B CD1 1 
ATOM   3738 C CD2 . LEU B 1 57  ? 134.467 107.382 80.821  1.00 132.74 ? 44  LEU B CD2 1 
ATOM   3739 N N   . GLU B 1 58  ? 129.146 108.436 82.297  1.00 138.70 ? 45  GLU B N   1 
ATOM   3740 C CA  . GLU B 1 58  ? 128.092 108.056 83.234  1.00 136.69 ? 45  GLU B CA  1 
ATOM   3741 C C   . GLU B 1 58  ? 126.774 107.803 82.511  1.00 139.02 ? 45  GLU B C   1 
ATOM   3742 O O   . GLU B 1 58  ? 126.076 106.819 82.798  1.00 139.62 ? 45  GLU B O   1 
ATOM   3743 C CB  . GLU B 1 58  ? 127.920 109.141 84.300  1.00 130.59 ? 45  GLU B CB  1 
ATOM   3744 C CG  . GLU B 1 58  ? 126.566 109.138 85.006  1.00 125.56 ? 45  GLU B CG  1 
ATOM   3745 C CD  . GLU B 1 58  ? 126.452 108.071 86.081  1.00 123.03 ? 45  GLU B CD  1 
ATOM   3746 O OE1 . GLU B 1 58  ? 127.436 107.335 86.305  1.00 118.01 ? 45  GLU B OE1 1 
ATOM   3747 O OE2 . GLU B 1 58  ? 125.375 107.977 86.709  1.00 124.33 ? 45  GLU B OE2 1 
ATOM   3748 N N   . LEU B 1 59  ? 126.416 108.681 81.569  1.00 138.38 ? 46  LEU B N   1 
ATOM   3749 C CA  . LEU B 1 59  ? 125.193 108.483 80.797  1.00 138.40 ? 46  LEU B CA  1 
ATOM   3750 C C   . LEU B 1 59  ? 125.265 107.205 79.971  1.00 141.78 ? 46  LEU B C   1 
ATOM   3751 O O   . LEU B 1 59  ? 124.281 106.461 79.879  1.00 143.12 ? 46  LEU B O   1 
ATOM   3752 C CB  . LEU B 1 59  ? 124.934 109.690 79.893  1.00 136.31 ? 46  LEU B CB  1 
ATOM   3753 C CG  . LEU B 1 59  ? 124.550 111.013 80.555  1.00 131.24 ? 46  LEU B CG  1 
ATOM   3754 C CD1 . LEU B 1 59  ? 124.421 112.115 79.510  1.00 126.19 ? 46  LEU B CD1 1 
ATOM   3755 C CD2 . LEU B 1 59  ? 123.261 110.870 81.354  1.00 130.11 ? 46  LEU B CD2 1 
ATOM   3756 N N   . LEU B 1 60  ? 126.424 106.934 79.363  1.00 141.06 ? 47  LEU B N   1 
ATOM   3757 C CA  . LEU B 1 60  ? 126.583 105.711 78.582  1.00 143.70 ? 47  LEU B CA  1 
ATOM   3758 C C   . LEU B 1 60  ? 126.427 104.472 79.455  1.00 143.44 ? 47  LEU B C   1 
ATOM   3759 O O   . LEU B 1 60  ? 125.781 103.496 79.052  1.00 143.87 ? 47  LEU B O   1 
ATOM   3760 C CB  . LEU B 1 60  ? 127.941 105.698 77.882  1.00 144.16 ? 47  LEU B CB  1 
ATOM   3761 C CG  . LEU B 1 60  ? 128.253 104.443 77.063  1.00 148.66 ? 47  LEU B CG  1 
ATOM   3762 C CD1 . LEU B 1 60  ? 127.258 104.262 75.920  1.00 147.95 ? 47  LEU B CD1 1 
ATOM   3763 C CD2 . LEU B 1 60  ? 129.681 104.481 76.537  1.00 145.34 ? 47  LEU B CD2 1 
ATOM   3764 N N   . LYS B 1 61  ? 127.018 104.484 80.652  1.00 140.57 ? 48  LYS B N   1 
ATOM   3765 C CA  . LYS B 1 61  ? 126.909 103.324 81.532  1.00 135.67 ? 48  LYS B CA  1 
ATOM   3766 C C   . LYS B 1 61  ? 125.480 103.139 82.028  1.00 136.36 ? 48  LYS B C   1 
ATOM   3767 O O   . LYS B 1 61  ? 124.998 102.005 82.135  1.00 136.82 ? 48  LYS B O   1 
ATOM   3768 C CB  . LYS B 1 61  ? 127.882 103.454 82.703  1.00 131.14 ? 48  LYS B CB  1 
ATOM   3769 C CG  . LYS B 1 61  ? 129.344 103.455 82.281  1.00 129.61 ? 48  LYS B CG  1 
ATOM   3770 C CD  . LYS B 1 61  ? 130.249 102.927 83.381  1.00 123.66 ? 48  LYS B CD  1 
ATOM   3771 C CE  . LYS B 1 61  ? 130.014 101.443 83.623  1.00 122.11 ? 48  LYS B CE  1 
ATOM   3772 N NZ  . LYS B 1 61  ? 130.191 100.647 82.377  1.00 119.16 ? 48  LYS B NZ  1 
ATOM   3773 N N   . GLU B 1 62  ? 124.782 104.238 82.332  1.00 137.99 ? 49  GLU B N   1 
ATOM   3774 C CA  . GLU B 1 62  ? 123.377 104.126 82.711  1.00 141.33 ? 49  GLU B CA  1 
ATOM   3775 C C   . GLU B 1 62  ? 122.540 103.565 81.569  1.00 145.78 ? 49  GLU B C   1 
ATOM   3776 O O   . GLU B 1 62  ? 121.664 102.719 81.792  1.00 146.61 ? 49  GLU B O   1 
ATOM   3777 C CB  . GLU B 1 62  ? 122.832 105.484 83.146  1.00 138.10 ? 49  GLU B CB  1 
ATOM   3778 C CG  . GLU B 1 62  ? 123.275 105.919 84.526  1.00 133.99 ? 49  GLU B CG  1 
ATOM   3779 C CD  . GLU B 1 62  ? 122.511 107.126 85.027  1.00 133.35 ? 49  GLU B CD  1 
ATOM   3780 O OE1 . GLU B 1 62  ? 121.898 107.831 84.198  1.00 132.89 ? 49  GLU B OE1 1 
ATOM   3781 O OE2 . GLU B 1 62  ? 122.517 107.367 86.252  1.00 131.51 ? 49  GLU B OE2 1 
ATOM   3782 N N   . LEU B 1 63  ? 122.792 104.025 80.340  1.00 146.20 ? 50  LEU B N   1 
ATOM   3783 C CA  . LEU B 1 63  ? 122.059 103.503 79.193  1.00 146.47 ? 50  LEU B CA  1 
ATOM   3784 C C   . LEU B 1 63  ? 122.329 102.019 79.000  1.00 149.17 ? 50  LEU B C   1 
ATOM   3785 O O   . LEU B 1 63  ? 121.406 101.244 78.723  1.00 149.46 ? 50  LEU B O   1 
ATOM   3786 C CB  . LEU B 1 63  ? 122.424 104.278 77.929  1.00 146.33 ? 50  LEU B CB  1 
ATOM   3787 C CG  . LEU B 1 63  ? 121.912 105.717 77.823  1.00 145.24 ? 50  LEU B CG  1 
ATOM   3788 C CD1 . LEU B 1 63  ? 122.173 106.261 76.432  1.00 143.50 ? 50  LEU B CD1 1 
ATOM   3789 C CD2 . LEU B 1 63  ? 120.433 105.784 78.135  1.00 146.48 ? 50  LEU B CD2 1 
ATOM   3790 N N   . THR B 1 64  ? 123.590 101.604 79.145  1.00 152.21 ? 51  THR B N   1 
ATOM   3791 C CA  . THR B 1 64  ? 123.920 100.188 79.033  1.00 152.00 ? 51  THR B CA  1 
ATOM   3792 C C   . THR B 1 64  ? 123.214 99.374  80.110  1.00 151.06 ? 51  THR B C   1 
ATOM   3793 O O   . THR B 1 64  ? 122.675 98.300  79.829  1.00 150.29 ? 51  THR B O   1 
ATOM   3794 C CB  . THR B 1 64  ? 125.435 99.986  79.114  1.00 152.97 ? 51  THR B CB  1 
ATOM   3795 O OG1 . THR B 1 64  ? 126.077 100.757 78.092  1.00 150.67 ? 51  THR B OG1 1 
ATOM   3796 C CG2 . THR B 1 64  ? 125.793 98.515  78.920  1.00 149.79 ? 51  THR B CG2 1 
ATOM   3797 N N   . GLU B 1 65  ? 123.195 99.875  81.347  1.00 152.38 ? 52  GLU B N   1 
ATOM   3798 C CA  . GLU B 1 65  ? 122.542 99.141  82.426  1.00 152.23 ? 52  GLU B CA  1 
ATOM   3799 C C   . GLU B 1 65  ? 121.045 99.005  82.175  1.00 151.22 ? 52  GLU B C   1 
ATOM   3800 O O   . GLU B 1 65  ? 120.470 97.924  82.372  1.00 153.00 ? 52  GLU B O   1 
ATOM   3801 C CB  . GLU B 1 65  ? 122.811 99.836  83.763  1.00 148.42 ? 52  GLU B CB  1 
ATOM   3802 C CG  . GLU B 1 65  ? 122.232 99.133  84.984  1.00 146.77 ? 52  GLU B CG  1 
ATOM   3803 C CD  . GLU B 1 65  ? 120.776 99.485  85.230  1.00 144.46 ? 52  GLU B CD  1 
ATOM   3804 O OE1 . GLU B 1 65  ? 120.021 98.609  85.699  1.00 141.43 ? 52  GLU B OE1 1 
ATOM   3805 O OE2 . GLU B 1 65  ? 120.386 100.636 84.944  1.00 146.45 ? 52  GLU B OE2 1 
ATOM   3806 N N   . LEU B 1 66  ? 120.397 100.082 81.725  1.00 149.41 ? 53  LEU B N   1 
ATOM   3807 C CA  . LEU B 1 66  ? 118.955 100.017 81.503  1.00 150.03 ? 53  LEU B CA  1 
ATOM   3808 C C   . LEU B 1 66  ? 118.616 99.131  80.308  1.00 153.33 ? 53  LEU B C   1 
ATOM   3809 O O   . LEU B 1 66  ? 117.613 98.409  80.333  1.00 153.12 ? 53  LEU B O   1 
ATOM   3810 C CB  . LEU B 1 66  ? 118.374 101.424 81.337  1.00 150.05 ? 53  LEU B CB  1 
ATOM   3811 C CG  . LEU B 1 66  ? 118.778 102.347 80.183  1.00 150.60 ? 53  LEU B CG  1 
ATOM   3812 C CD1 . LEU B 1 66  ? 117.934 102.104 78.937  1.00 150.62 ? 53  LEU B CD1 1 
ATOM   3813 C CD2 . LEU B 1 66  ? 118.684 103.802 80.618  1.00 147.19 ? 53  LEU B CD2 1 
ATOM   3814 N N   . LYS B 1 67  ? 119.438 99.164  79.254  1.00 154.87 ? 54  LYS B N   1 
ATOM   3815 C CA  . LYS B 1 67  ? 119.176 98.311  78.099  1.00 152.95 ? 54  LYS B CA  1 
ATOM   3816 C C   . LYS B 1 67  ? 119.503 96.851  78.391  1.00 152.98 ? 54  LYS B C   1 
ATOM   3817 O O   . LYS B 1 67  ? 118.899 95.952  77.795  1.00 149.39 ? 54  LYS B O   1 
ATOM   3818 C CB  . LYS B 1 67  ? 119.960 98.815  76.886  1.00 150.44 ? 54  LYS B CB  1 
ATOM   3819 C CG  . LYS B 1 67  ? 119.122 99.654  75.927  1.00 144.55 ? 54  LYS B CG  1 
ATOM   3820 C CD  . LYS B 1 67  ? 119.984 100.495 74.999  1.00 143.41 ? 54  LYS B CD  1 
ATOM   3821 C CE  . LYS B 1 67  ? 120.580 101.682 75.735  1.00 141.36 ? 54  LYS B CE  1 
ATOM   3822 N NZ  . LYS B 1 67  ? 121.342 102.595 74.840  1.00 140.26 ? 54  LYS B NZ  1 
ATOM   3823 N N   . ARG B 1 68  ? 120.448 96.593  79.297  1.00 154.54 ? 55  ARG B N   1 
ATOM   3824 C CA  . ARG B 1 68  ? 120.745 95.223  79.699  1.00 154.85 ? 55  ARG B CA  1 
ATOM   3825 C C   . ARG B 1 68  ? 119.627 94.655  80.562  1.00 158.33 ? 55  ARG B C   1 
ATOM   3826 O O   . ARG B 1 68  ? 119.188 93.517  80.355  1.00 162.86 ? 55  ARG B O   1 
ATOM   3827 C CB  . ARG B 1 68  ? 122.086 95.178  80.436  1.00 154.53 ? 55  ARG B CB  1 
ATOM   3828 C CG  . ARG B 1 68  ? 122.166 94.159  81.569  1.00 159.06 ? 55  ARG B CG  1 
ATOM   3829 C CD  . ARG B 1 68  ? 122.244 92.725  81.060  1.00 165.76 ? 55  ARG B CD  1 
ATOM   3830 N NE  . ARG B 1 68  ? 122.202 91.766  82.157  1.00 169.17 ? 55  ARG B NE  1 
ATOM   3831 C CZ  . ARG B 1 68  ? 121.087 91.310  82.710  1.00 169.35 ? 55  ARG B CZ  1 
ATOM   3832 N NH1 . ARG B 1 68  ? 119.896 91.698  82.284  1.00 169.06 ? 55  ARG B NH1 1 
ATOM   3833 N NH2 . ARG B 1 68  ? 121.168 90.444  83.716  1.00 170.01 ? 55  ARG B NH2 1 
ATOM   3834 N N   . SER B 1 69  ? 119.153 95.429  81.532  1.00 157.72 ? 56  SER B N   1 
ATOM   3835 C CA  . SER B 1 69  ? 118.108 94.946  82.426  1.00 156.14 ? 56  SER B CA  1 
ATOM   3836 C C   . SER B 1 69  ? 116.760 94.876  81.717  1.00 151.10 ? 56  SER B C   1 
ATOM   3837 O O   . SER B 1 69  ? 116.375 95.797  80.997  1.00 148.48 ? 56  SER B O   1 
ATOM   3838 C CB  . SER B 1 69  ? 118.006 95.839  83.661  1.00 154.73 ? 56  SER B CB  1 
ATOM   3839 O OG  . SER B 1 69  ? 117.717 97.175  83.293  1.00 158.32 ? 56  SER B OG  1 
ATOM   3840 N N   . ASP B 1 101 ? 125.754 121.284 84.638  1.00 107.99 ? 88  ASP B N   1 
ATOM   3841 C CA  . ASP B 1 101 ? 125.238 121.026 85.977  1.00 103.35 ? 88  ASP B CA  1 
ATOM   3842 C C   . ASP B 1 101 ? 125.088 122.321 86.768  1.00 98.20  ? 88  ASP B C   1 
ATOM   3843 O O   . ASP B 1 101 ? 125.572 123.373 86.353  1.00 97.57  ? 88  ASP B O   1 
ATOM   3844 C CB  . ASP B 1 101 ? 126.150 120.050 86.723  1.00 99.99  ? 88  ASP B CB  1 
ATOM   3845 C CG  . ASP B 1 101 ? 127.610 120.450 86.656  1.00 98.65  ? 88  ASP B CG  1 
ATOM   3846 O OD1 . ASP B 1 101 ? 127.999 121.123 85.680  1.00 102.16 ? 88  ASP B OD1 1 
ATOM   3847 O OD2 . ASP B 1 101 ? 128.370 120.085 87.578  1.00 93.51  ? 88  ASP B OD2 1 
ATOM   3848 N N   . ASN B 1 102 ? 124.407 122.236 87.913  1.00 93.43  ? 89  ASN B N   1 
ATOM   3849 C CA  . ASN B 1 102 ? 124.193 123.416 88.741  1.00 89.49  ? 89  ASN B CA  1 
ATOM   3850 C C   . ASN B 1 102 ? 125.468 123.865 89.443  1.00 85.35  ? 89  ASN B C   1 
ATOM   3851 O O   . ASN B 1 102 ? 125.563 125.034 89.835  1.00 77.82  ? 89  ASN B O   1 
ATOM   3852 C CB  . ASN B 1 102 ? 123.096 123.140 89.769  1.00 84.02  ? 89  ASN B CB  1 
ATOM   3853 C CG  . ASN B 1 102 ? 122.721 124.372 90.569  1.00 79.98  ? 89  ASN B CG  1 
ATOM   3854 O OD1 . ASN B 1 102 ? 123.487 125.335 90.643  1.00 76.93  ? 89  ASN B OD1 1 
ATOM   3855 N ND2 . ASN B 1 102 ? 121.543 124.349 91.178  1.00 76.80  ? 89  ASN B ND2 1 
ATOM   3856 N N   . GLU B 1 103 ? 126.442 122.967 89.605  1.00 85.31  ? 90  GLU B N   1 
ATOM   3857 C CA  . GLU B 1 103 ? 127.721 123.284 90.242  1.00 83.12  ? 90  GLU B CA  1 
ATOM   3858 C C   . GLU B 1 103 ? 127.521 123.841 91.648  1.00 74.05  ? 90  GLU B C   1 
ATOM   3859 O O   . GLU B 1 103 ? 128.167 124.809 92.051  1.00 73.05  ? 90  GLU B O   1 
ATOM   3860 C CB  . GLU B 1 103 ? 128.540 124.250 89.384  1.00 85.28  ? 90  GLU B CB  1 
ATOM   3861 C CG  . GLU B 1 103 ? 128.964 123.670 88.045  1.00 96.86  ? 90  GLU B CG  1 
ATOM   3862 C CD  . GLU B 1 103 ? 129.440 124.732 87.075  1.00 105.29 ? 90  GLU B CD  1 
ATOM   3863 O OE1 . GLU B 1 103 ? 129.083 125.913 87.265  1.00 108.50 ? 90  GLU B OE1 1 
ATOM   3864 O OE2 . GLU B 1 103 ? 130.170 124.385 86.122  1.00 106.37 ? 90  GLU B OE2 1 
ATOM   3865 N N   . GLU B 1 104 ? 126.614 123.222 92.403  1.00 72.19  ? 91  GLU B N   1 
ATOM   3866 C CA  . GLU B 1 104 ? 126.370 123.638 93.776  1.00 65.11  ? 91  GLU B CA  1 
ATOM   3867 C C   . GLU B 1 104 ? 127.495 123.224 94.715  1.00 57.24  ? 91  GLU B C   1 
ATOM   3868 O O   . GLU B 1 104 ? 127.557 123.720 95.844  1.00 56.02  ? 91  GLU B O   1 
ATOM   3869 C CB  . GLU B 1 104 ? 125.036 123.070 94.263  1.00 69.08  ? 91  GLU B CB  1 
ATOM   3870 C CG  . GLU B 1 104 ? 123.872 123.381 93.332  1.00 72.97  ? 91  GLU B CG  1 
ATOM   3871 C CD  . GLU B 1 104 ? 122.558 122.802 93.816  1.00 72.43  ? 91  GLU B CD  1 
ATOM   3872 O OE1 . GLU B 1 104 ? 122.467 122.445 95.007  1.00 67.73  ? 91  GLU B OE1 1 
ATOM   3873 O OE2 . GLU B 1 104 ? 121.615 122.702 93.003  1.00 79.67  ? 91  GLU B OE2 1 
ATOM   3874 N N   . LEU B 1 105 ? 128.378 122.324 94.274  1.00 55.57  ? 92  LEU B N   1 
ATOM   3875 C CA  . LEU B 1 105 ? 129.532 121.954 95.085  1.00 54.25  ? 92  LEU B CA  1 
ATOM   3876 C C   . LEU B 1 105 ? 130.459 123.143 95.302  1.00 58.52  ? 92  LEU B C   1 
ATOM   3877 O O   . LEU B 1 105 ? 130.945 123.367 96.419  1.00 62.00  ? 92  LEU B O   1 
ATOM   3878 C CB  . LEU B 1 105 ? 130.291 120.808 94.421  1.00 54.94  ? 92  LEU B CB  1 
ATOM   3879 C CG  . LEU B 1 105 ? 131.456 120.219 95.214  1.00 59.10  ? 92  LEU B CG  1 
ATOM   3880 C CD1 . LEU B 1 105 ? 130.965 119.609 96.514  1.00 55.55  ? 92  LEU B CD1 1 
ATOM   3881 C CD2 . LEU B 1 105 ? 132.203 119.188 94.387  1.00 64.68  ? 92  LEU B CD2 1 
ATOM   3882 N N   . ARG B 1 106 ? 130.720 123.918 94.244  1.00 59.33  ? 93  ARG B N   1 
ATOM   3883 C CA  . ARG B 1 106 ? 131.650 125.036 94.359  1.00 56.61  ? 93  ARG B CA  1 
ATOM   3884 C C   . ARG B 1 106 ? 131.125 126.107 95.304  1.00 51.82  ? 93  ARG B C   1 
ATOM   3885 O O   . ARG B 1 106 ? 131.914 126.856 95.891  1.00 54.60  ? 93  ARG B O   1 
ATOM   3886 C CB  . ARG B 1 106 ? 131.934 125.641 92.983  1.00 68.06  ? 93  ARG B CB  1 
ATOM   3887 C CG  . ARG B 1 106 ? 130.880 126.628 92.498  1.00 69.06  ? 93  ARG B CG  1 
ATOM   3888 C CD  . ARG B 1 106 ? 131.437 127.572 91.445  1.00 68.84  ? 93  ARG B CD  1 
ATOM   3889 N NE  . ARG B 1 106 ? 131.751 126.884 90.199  1.00 80.64  ? 93  ARG B NE  1 
ATOM   3890 C CZ  . ARG B 1 106 ? 132.394 127.437 89.180  1.00 90.95  ? 93  ARG B CZ  1 
ATOM   3891 N NH1 . ARG B 1 106 ? 132.830 128.685 89.233  1.00 92.95  ? 93  ARG B NH1 1 
ATOM   3892 N NH2 . ARG B 1 106 ? 132.605 126.720 88.079  1.00 93.38  ? 93  ARG B NH2 1 
ATOM   3893 N N   . TYR B 1 107 ? 129.806 126.197 95.466  1.00 47.94  ? 94  TYR B N   1 
ATOM   3894 C CA  . TYR B 1 107 ? 129.222 127.173 96.375  1.00 45.83  ? 94  TYR B CA  1 
ATOM   3895 C C   . TYR B 1 107 ? 129.055 126.627 97.783  1.00 46.62  ? 94  TYR B C   1 
ATOM   3896 O O   . TYR B 1 107 ? 129.172 127.385 98.753  1.00 49.29  ? 94  TYR B O   1 
ATOM   3897 C CB  . TYR B 1 107 ? 127.877 127.655 95.830  1.00 48.75  ? 94  TYR B CB  1 
ATOM   3898 C CG  . TYR B 1 107 ? 128.024 128.381 94.516  1.00 53.69  ? 94  TYR B CG  1 
ATOM   3899 C CD1 . TYR B 1 107 ? 127.636 127.788 93.324  1.00 60.23  ? 94  TYR B CD1 1 
ATOM   3900 C CD2 . TYR B 1 107 ? 128.572 129.652 94.468  1.00 53.42  ? 94  TYR B CD2 1 
ATOM   3901 C CE1 . TYR B 1 107 ? 127.782 128.450 92.119  1.00 62.60  ? 94  TYR B CE1 1 
ATOM   3902 C CE2 . TYR B 1 107 ? 128.721 130.319 93.272  1.00 54.96  ? 94  TYR B CE2 1 
ATOM   3903 C CZ  . TYR B 1 107 ? 128.326 129.716 92.103  1.00 59.62  ? 94  TYR B CZ  1 
ATOM   3904 O OH  . TYR B 1 107 ? 128.479 130.384 90.914  1.00 65.89  ? 94  TYR B OH  1 
ATOM   3905 N N   . SER B 1 108 ? 128.802 125.325 97.925  1.00 46.99  ? 95  SER B N   1 
ATOM   3906 C CA  . SER B 1 108 ? 128.820 124.728 99.254  1.00 42.73  ? 95  SER B CA  1 
ATOM   3907 C C   . SER B 1 108 ? 130.215 124.780 99.860  1.00 40.32  ? 95  SER B C   1 
ATOM   3908 O O   . SER B 1 108 ? 130.356 124.923 101.078 1.00 39.90  ? 95  SER B O   1 
ATOM   3909 C CB  . SER B 1 108 ? 128.313 123.289 99.198  1.00 46.29  ? 95  SER B CB  1 
ATOM   3910 O OG  . SER B 1 108 ? 128.245 122.730 100.497 1.00 43.07  ? 95  SER B OG  1 
ATOM   3911 N N   . LEU B 1 109 ? 131.256 124.684 99.030  1.00 42.89  ? 96  LEU B N   1 
ATOM   3912 C CA  . LEU B 1 109 ? 132.613 124.857 99.539  1.00 41.60  ? 96  LEU B CA  1 
ATOM   3913 C C   . LEU B 1 109 ? 132.826 126.267 100.076 1.00 45.72  ? 96  LEU B C   1 
ATOM   3914 O O   . LEU B 1 109 ? 133.443 126.451 101.133 1.00 48.88  ? 96  LEU B O   1 
ATOM   3915 C CB  . LEU B 1 109 ? 133.631 124.545 98.445  1.00 46.97  ? 96  LEU B CB  1 
ATOM   3916 C CG  . LEU B 1 109 ? 133.756 123.074 98.061  1.00 50.04  ? 96  LEU B CG  1 
ATOM   3917 C CD1 . LEU B 1 109 ? 134.846 122.881 97.021  1.00 62.56  ? 96  LEU B CD1 1 
ATOM   3918 C CD2 . LEU B 1 109 ? 134.030 122.237 99.292  1.00 46.77  ? 96  LEU B CD2 1 
ATOM   3919 N N   . ARG B 1 110 ? 132.331 127.277 99.357  1.00 42.60  ? 97  ARG B N   1 
ATOM   3920 C CA  . ARG B 1 110 ? 132.411 128.648 99.848  1.00 40.26  ? 97  ARG B CA  1 
ATOM   3921 C C   . ARG B 1 110 ? 131.631 128.815 101.144 1.00 44.49  ? 97  ARG B C   1 
ATOM   3922 O O   . ARG B 1 110 ? 132.061 129.540 102.048 1.00 44.72  ? 97  ARG B O   1 
ATOM   3923 C CB  . ARG B 1 110 ? 131.895 129.620 98.788  1.00 39.35  ? 97  ARG B CB  1 
ATOM   3924 C CG  . ARG B 1 110 ? 132.791 129.755 97.573  1.00 44.55  ? 97  ARG B CG  1 
ATOM   3925 C CD  . ARG B 1 110 ? 132.147 130.647 96.526  1.00 46.71  ? 97  ARG B CD  1 
ATOM   3926 N NE  . ARG B 1 110 ? 133.054 130.926 95.420  1.00 49.74  ? 97  ARG B NE  1 
ATOM   3927 C CZ  . ARG B 1 110 ? 133.263 130.108 94.399  1.00 53.76  ? 97  ARG B CZ  1 
ATOM   3928 N NH1 . ARG B 1 110 ? 132.647 128.941 94.312  1.00 54.11  ? 97  ARG B NH1 1 
ATOM   3929 N NH2 . ARG B 1 110 ? 134.113 130.470 93.442  1.00 59.30  ? 97  ARG B NH2 1 
ATOM   3930 N N   . SER B 1 111 ? 130.467 128.168 101.243 1.00 45.68  ? 98  SER B N   1 
ATOM   3931 C CA  . SER B 1 111 ? 129.691 128.230 102.478 1.00 42.69  ? 98  SER B CA  1 
ATOM   3932 C C   . SER B 1 111 ? 130.452 127.599 103.639 1.00 37.88  ? 98  SER B C   1 
ATOM   3933 O O   . SER B 1 111 ? 130.429 128.119 104.759 1.00 36.33  ? 98  SER B O   1 
ATOM   3934 C CB  . SER B 1 111 ? 128.338 127.549 102.285 1.00 39.67  ? 98  SER B CB  1 
ATOM   3935 O OG  . SER B 1 111 ? 127.473 127.825 103.372 1.00 36.13  ? 98  SER B OG  1 
ATOM   3936 N N   . ILE B 1 112 ? 131.126 126.475 103.392 1.00 39.43  ? 99  ILE B N   1 
ATOM   3937 C CA  . ILE B 1 112 ? 131.948 125.856 104.430 1.00 35.48  ? 99  ILE B CA  1 
ATOM   3938 C C   . ILE B 1 112 ? 133.075 126.794 104.842 1.00 37.64  ? 99  ILE B C   1 
ATOM   3939 O O   . ILE B 1 112 ? 133.364 126.963 106.031 1.00 39.29  ? 99  ILE B O   1 
ATOM   3940 C CB  . ILE B 1 112 ? 132.497 124.500 103.952 1.00 39.68  ? 99  ILE B CB  1 
ATOM   3941 C CG1 . ILE B 1 112 ? 131.358 123.515 103.694 1.00 40.51  ? 99  ILE B CG1 1 
ATOM   3942 C CG2 . ILE B 1 112 ? 133.457 123.928 104.976 1.00 38.28  ? 99  ILE B CG2 1 
ATOM   3943 C CD1 . ILE B 1 112 ? 130.516 123.228 104.905 1.00 40.07  ? 99  ILE B CD1 1 
ATOM   3944 N N   . GLU B 1 113 ? 133.733 127.414 103.859 1.00 40.15  ? 100 GLU B N   1 
ATOM   3945 C CA  . GLU B 1 113 ? 134.850 128.307 104.159 1.00 43.13  ? 100 GLU B CA  1 
ATOM   3946 C C   . GLU B 1 113 ? 134.401 129.514 104.974 1.00 43.40  ? 100 GLU B C   1 
ATOM   3947 O O   . GLU B 1 113 ? 135.083 129.922 105.920 1.00 42.20  ? 100 GLU B O   1 
ATOM   3948 C CB  . GLU B 1 113 ? 135.519 128.766 102.865 1.00 45.48  ? 100 GLU B CB  1 
ATOM   3949 C CG  . GLU B 1 113 ? 136.524 129.890 103.060 1.00 48.11  ? 100 GLU B CG  1 
ATOM   3950 C CD  . GLU B 1 113 ? 136.588 130.833 101.874 1.00 55.39  ? 100 GLU B CD  1 
ATOM   3951 O OE1 . GLU B 1 113 ? 136.109 130.459 100.784 1.00 58.29  ? 100 GLU B OE1 1 
ATOM   3952 O OE2 . GLU B 1 113 ? 137.112 131.956 102.033 1.00 54.99  ? 100 GLU B OE2 1 
ATOM   3953 N N   . ARG B 1 114 ? 133.258 130.097 104.623 1.00 42.32  ? 101 ARG B N   1 
ATOM   3954 C CA  . ARG B 1 114 ? 132.822 131.343 105.240 1.00 39.12  ? 101 ARG B CA  1 
ATOM   3955 C C   . ARG B 1 114 ? 132.102 131.132 106.567 1.00 38.13  ? 101 ARG B C   1 
ATOM   3956 O O   . ARG B 1 114 ? 132.380 131.847 107.537 1.00 43.30  ? 101 ARG B O   1 
ATOM   3957 C CB  . ARG B 1 114 ? 131.918 132.112 104.272 1.00 39.04  ? 101 ARG B CB  1 
ATOM   3958 C CG  . ARG B 1 114 ? 131.087 133.205 104.921 1.00 44.23  ? 101 ARG B CG  1 
ATOM   3959 C CD  . ARG B 1 114 ? 131.939 134.356 105.429 1.00 49.50  ? 101 ARG B CD  1 
ATOM   3960 N NE  . ARG B 1 114 ? 131.224 135.133 106.435 1.00 48.91  ? 101 ARG B NE  1 
ATOM   3961 C CZ  . ARG B 1 114 ? 130.275 136.019 106.166 1.00 56.12  ? 101 ARG B CZ  1 
ATOM   3962 N NH1 . ARG B 1 114 ? 129.902 136.279 104.923 1.00 54.87  ? 101 ARG B NH1 1 
ATOM   3963 N NH2 . ARG B 1 114 ? 129.681 136.659 107.170 1.00 63.61  ? 101 ARG B NH2 1 
ATOM   3964 N N   . HIS B 1 115 ? 131.188 130.165 106.640 1.00 34.50  ? 102 HIS B N   1 
ATOM   3965 C CA  . HIS B 1 115 ? 130.351 129.986 107.820 1.00 31.27  ? 102 HIS B CA  1 
ATOM   3966 C C   . HIS B 1 115 ? 130.848 128.909 108.773 1.00 31.26  ? 102 HIS B C   1 
ATOM   3967 O O   . HIS B 1 115 ? 130.502 128.951 109.958 1.00 29.90  ? 102 HIS B O   1 
ATOM   3968 C CB  . HIS B 1 115 ? 128.916 129.648 107.404 1.00 31.60  ? 102 HIS B CB  1 
ATOM   3969 C CG  . HIS B 1 115 ? 128.198 130.778 106.737 1.00 31.73  ? 102 HIS B CG  1 
ATOM   3970 N ND1 . HIS B 1 115 ? 127.197 131.491 107.359 1.00 35.16  ? 102 HIS B ND1 1 
ATOM   3971 C CD2 . HIS B 1 115 ? 128.335 131.317 105.502 1.00 36.81  ? 102 HIS B CD2 1 
ATOM   3972 C CE1 . HIS B 1 115 ? 126.747 132.422 106.536 1.00 42.97  ? 102 HIS B CE1 1 
ATOM   3973 N NE2 . HIS B 1 115 ? 127.422 132.338 105.403 1.00 42.19  ? 102 HIS B NE2 1 
ATOM   3974 N N   . ALA B 1 116 ? 131.654 127.962 108.302 1.00 35.40  ? 103 ALA B N   1 
ATOM   3975 C CA  . ALA B 1 116 ? 132.154 126.863 109.127 1.00 35.18  ? 103 ALA B CA  1 
ATOM   3976 C C   . ALA B 1 116 ? 133.669 126.790 109.005 1.00 36.55  ? 103 ALA B C   1 
ATOM   3977 O O   . ALA B 1 116 ? 134.217 125.825 108.460 1.00 37.75  ? 103 ALA B O   1 
ATOM   3978 C CB  . ALA B 1 116 ? 131.515 125.536 108.720 1.00 41.18  ? 103 ALA B CB  1 
ATOM   3979 N N   . PRO B 1 117 ? 134.383 127.795 109.520 1.00 36.94  ? 104 PRO B N   1 
ATOM   3980 C CA  . PRO B 1 117 ? 135.845 127.790 109.391 1.00 35.18  ? 104 PRO B CA  1 
ATOM   3981 C C   . PRO B 1 117 ? 136.536 126.809 110.319 1.00 39.08  ? 104 PRO B C   1 
ATOM   3982 O O   . PRO B 1 117 ? 137.751 126.620 110.188 1.00 45.73  ? 104 PRO B O   1 
ATOM   3983 C CB  . PRO B 1 117 ? 136.226 129.234 109.727 1.00 34.40  ? 104 PRO B CB  1 
ATOM   3984 C CG  . PRO B 1 117 ? 135.169 129.671 110.675 1.00 38.19  ? 104 PRO B CG  1 
ATOM   3985 C CD  . PRO B 1 117 ? 133.901 128.971 110.265 1.00 39.08  ? 104 PRO B CD  1 
ATOM   3986 N N   . TRP B 1 118 ? 135.813 126.178 111.242 1.00 34.54  ? 105 TRP B N   1 
ATOM   3987 C CA  . TRP B 1 118 ? 136.418 125.307 112.240 1.00 31.10  ? 105 TRP B CA  1 
ATOM   3988 C C   . TRP B 1 118 ? 136.520 123.854 111.799 1.00 33.09  ? 105 TRP B C   1 
ATOM   3989 O O   . TRP B 1 118 ? 137.018 123.027 112.568 1.00 35.40  ? 105 TRP B O   1 
ATOM   3990 C CB  . TRP B 1 118 ? 135.633 125.386 113.551 1.00 29.07  ? 105 TRP B CB  1 
ATOM   3991 C CG  . TRP B 1 118 ? 134.150 125.413 113.369 1.00 30.44  ? 105 TRP B CG  1 
ATOM   3992 C CD1 . TRP B 1 118 ? 133.342 126.505 113.428 1.00 31.73  ? 105 TRP B CD1 1 
ATOM   3993 C CD2 . TRP B 1 118 ? 133.296 124.296 113.098 1.00 30.88  ? 105 TRP B CD2 1 
ATOM   3994 N NE1 . TRP B 1 118 ? 132.036 126.142 113.214 1.00 32.97  ? 105 TRP B NE1 1 
ATOM   3995 C CE2 . TRP B 1 118 ? 131.981 124.790 113.007 1.00 31.30  ? 105 TRP B CE2 1 
ATOM   3996 C CE3 . TRP B 1 118 ? 133.514 122.928 112.924 1.00 31.44  ? 105 TRP B CE3 1 
ATOM   3997 C CZ2 . TRP B 1 118 ? 130.891 123.966 112.749 1.00 30.97  ? 105 TRP B CZ2 1 
ATOM   3998 C CZ3 . TRP B 1 118 ? 132.431 122.112 112.667 1.00 31.27  ? 105 TRP B CZ3 1 
ATOM   3999 C CH2 . TRP B 1 118 ? 131.136 122.632 112.582 1.00 31.74  ? 105 TRP B CH2 1 
ATOM   4000 N N   . VAL B 1 119 ? 136.061 123.515 110.592 1.00 34.56  ? 106 VAL B N   1 
ATOM   4001 C CA  . VAL B 1 119 ? 136.211 122.142 110.124 1.00 29.76  ? 106 VAL B CA  1 
ATOM   4002 C C   . VAL B 1 119 ? 137.669 121.878 109.765 1.00 34.43  ? 106 VAL B C   1 
ATOM   4003 O O   . VAL B 1 119 ? 138.448 122.791 109.465 1.00 43.78  ? 106 VAL B O   1 
ATOM   4004 C CB  . VAL B 1 119 ? 135.280 121.857 108.934 1.00 28.56  ? 106 VAL B CB  1 
ATOM   4005 C CG1 . VAL B 1 119 ? 133.843 122.194 109.294 1.00 26.45  ? 106 VAL B CG1 1 
ATOM   4006 C CG2 . VAL B 1 119 ? 135.723 122.637 107.715 1.00 34.27  ? 106 VAL B CG2 1 
ATOM   4007 N N   . ARG B 1 120 ? 138.048 120.602 109.806 1.00 32.95  ? 107 ARG B N   1 
ATOM   4008 C CA  . ARG B 1 120 ? 139.444 120.232 109.599 1.00 39.20  ? 107 ARG B CA  1 
ATOM   4009 C C   . ARG B 1 120 ? 139.729 119.874 108.143 1.00 42.88  ? 107 ARG B C   1 
ATOM   4010 O O   . ARG B 1 120 ? 140.576 120.499 107.497 1.00 48.77  ? 107 ARG B O   1 
ATOM   4011 C CB  . ARG B 1 120 ? 139.817 119.066 110.520 1.00 41.44  ? 107 ARG B CB  1 
ATOM   4012 C CG  . ARG B 1 120 ? 141.308 118.907 110.749 1.00 42.74  ? 107 ARG B CG  1 
ATOM   4013 C CD  . ARG B 1 120 ? 141.611 117.538 111.315 1.00 41.00  ? 107 ARG B CD  1 
ATOM   4014 N NE  . ARG B 1 120 ? 141.365 116.495 110.327 1.00 42.64  ? 107 ARG B NE  1 
ATOM   4015 C CZ  . ARG B 1 120 ? 141.188 115.214 110.617 1.00 44.33  ? 107 ARG B CZ  1 
ATOM   4016 N NH1 . ARG B 1 120 ? 141.203 114.780 111.866 1.00 44.18  ? 107 ARG B NH1 1 
ATOM   4017 N NH2 . ARG B 1 120 ? 140.985 114.348 109.628 1.00 44.89  ? 107 ARG B NH2 1 
ATOM   4018 N N   . ASN B 1 121 ? 139.031 118.871 107.615 1.00 40.48  ? 108 ASN B N   1 
ATOM   4019 C CA  . ASN B 1 121 ? 139.245 118.414 106.251 1.00 42.17  ? 108 ASN B CA  1 
ATOM   4020 C C   . ASN B 1 121 ? 137.902 118.179 105.578 1.00 44.20  ? 108 ASN B C   1 
ATOM   4021 O O   . ASN B 1 121 ? 136.884 117.949 106.235 1.00 40.19  ? 108 ASN B O   1 
ATOM   4022 C CB  . ASN B 1 121 ? 140.087 117.133 106.207 1.00 41.32  ? 108 ASN B CB  1 
ATOM   4023 C CG  . ASN B 1 121 ? 141.490 117.341 106.735 1.00 42.33  ? 108 ASN B CG  1 
ATOM   4024 O OD1 . ASN B 1 121 ? 141.733 117.254 107.939 1.00 43.71  ? 108 ASN B OD1 1 
ATOM   4025 N ND2 . ASN B 1 121 ? 142.425 117.615 105.835 1.00 42.79  ? 108 ASN B ND2 1 
ATOM   4026 N N   . ILE B 1 122 ? 137.912 118.243 104.249 1.00 48.92  ? 109 ILE B N   1 
ATOM   4027 C CA  . ILE B 1 122 ? 136.725 118.014 103.433 1.00 46.23  ? 109 ILE B CA  1 
ATOM   4028 C C   . ILE B 1 122 ? 137.002 116.830 102.518 1.00 49.08  ? 109 ILE B C   1 
ATOM   4029 O O   . ILE B 1 122 ? 137.940 116.867 101.713 1.00 55.51  ? 109 ILE B O   1 
ATOM   4030 C CB  . ILE B 1 122 ? 136.342 119.258 102.619 1.00 42.22  ? 109 ILE B CB  1 
ATOM   4031 C CG1 . ILE B 1 122 ? 136.017 120.424 103.552 1.00 43.39  ? 109 ILE B CG1 1 
ATOM   4032 C CG2 . ILE B 1 122 ? 135.161 118.956 101.716 1.00 41.03  ? 109 ILE B CG2 1 
ATOM   4033 C CD1 . ILE B 1 122 ? 135.512 121.649 102.836 1.00 47.87  ? 109 ILE B CD1 1 
ATOM   4034 N N   . PHE B 1 123 ? 136.186 115.788 102.638 1.00 42.16  ? 110 PHE B N   1 
ATOM   4035 C CA  . PHE B 1 123 ? 136.289 114.598 101.806 1.00 41.24  ? 110 PHE B CA  1 
ATOM   4036 C C   . PHE B 1 123 ? 135.102 114.549 100.858 1.00 44.48  ? 110 PHE B C   1 
ATOM   4037 O O   . PHE B 1 123 ? 133.963 114.779 101.272 1.00 46.80  ? 110 PHE B O   1 
ATOM   4038 C CB  . PHE B 1 123 ? 136.329 113.329 102.659 1.00 38.03  ? 110 PHE B CB  1 
ATOM   4039 C CG  . PHE B 1 123 ? 137.547 113.215 103.524 1.00 40.81  ? 110 PHE B CG  1 
ATOM   4040 C CD1 . PHE B 1 123 ? 138.725 112.697 103.016 1.00 47.63  ? 110 PHE B CD1 1 
ATOM   4041 C CD2 . PHE B 1 123 ? 137.512 113.614 104.847 1.00 43.79  ? 110 PHE B CD2 1 
ATOM   4042 C CE1 . PHE B 1 123 ? 139.848 112.585 103.811 1.00 52.23  ? 110 PHE B CE1 1 
ATOM   4043 C CE2 . PHE B 1 123 ? 138.632 113.505 105.646 1.00 49.17  ? 110 PHE B CE2 1 
ATOM   4044 C CZ  . PHE B 1 123 ? 139.801 112.990 105.128 1.00 52.48  ? 110 PHE B CZ  1 
ATOM   4045 N N   . ILE B 1 124 ? 135.365 114.259 99.588  1.00 42.57  ? 111 ILE B N   1 
ATOM   4046 C CA  . ILE B 1 124 ? 134.315 114.079 98.595  1.00 40.30  ? 111 ILE B CA  1 
ATOM   4047 C C   . ILE B 1 124 ? 134.437 112.674 98.024  1.00 49.67  ? 111 ILE B C   1 
ATOM   4048 O O   . ILE B 1 124 ? 135.544 112.216 97.718  1.00 55.32  ? 111 ILE B O   1 
ATOM   4049 C CB  . ILE B 1 124 ? 134.379 115.148 97.487  1.00 42.98  ? 111 ILE B CB  1 
ATOM   4050 C CG1 . ILE B 1 124 ? 135.678 115.053 96.690  1.00 49.90  ? 111 ILE B CG1 1 
ATOM   4051 C CG2 . ILE B 1 124 ? 134.261 116.534 98.085  1.00 47.37  ? 111 ILE B CG2 1 
ATOM   4052 C CD1 . ILE B 1 124 ? 135.769 116.067 95.573  1.00 53.04  ? 111 ILE B CD1 1 
ATOM   4053 N N   . VAL B 1 125 ? 133.310 111.977 97.924  1.00 49.14  ? 112 VAL B N   1 
ATOM   4054 C CA  . VAL B 1 125 ? 133.260 110.656 97.312  1.00 47.69  ? 112 VAL B CA  1 
ATOM   4055 C C   . VAL B 1 125 ? 132.562 110.795 95.966  1.00 57.92  ? 112 VAL B C   1 
ATOM   4056 O O   . VAL B 1 125 ? 131.445 111.321 95.881  1.00 59.04  ? 112 VAL B O   1 
ATOM   4057 C CB  . VAL B 1 125 ? 132.565 109.624 98.216  1.00 42.29  ? 112 VAL B CB  1 
ATOM   4058 C CG1 . VAL B 1 125 ? 133.457 109.281 99.399  1.00 42.01  ? 112 VAL B CG1 1 
ATOM   4059 C CG2 . VAL B 1 125 ? 131.222 110.134 98.703  1.00 41.55  ? 112 VAL B CG2 1 
ATOM   4060 N N   . THR B 1 126 ? 133.235 110.344 94.912  1.00 63.02  ? 113 THR B N   1 
ATOM   4061 C CA  . THR B 1 126 ? 132.753 110.501 93.550  1.00 63.43  ? 113 THR B CA  1 
ATOM   4062 C C   . THR B 1 126 ? 133.241 109.309 92.740  1.00 69.96  ? 113 THR B C   1 
ATOM   4063 O O   . THR B 1 126 ? 134.205 108.637 93.113  1.00 69.55  ? 113 THR B O   1 
ATOM   4064 C CB  . THR B 1 126 ? 133.237 111.823 92.934  1.00 58.46  ? 113 THR B CB  1 
ATOM   4065 O OG1 . THR B 1 126 ? 133.048 112.888 93.874  1.00 55.79  ? 113 THR B OG1 1 
ATOM   4066 C CG2 . THR B 1 126 ? 132.464 112.152 91.668  1.00 63.94  ? 113 THR B CG2 1 
ATOM   4067 N N   . ASN B 1 127 ? 132.560 109.048 91.625  1.00 73.64  ? 114 ASN B N   1 
ATOM   4068 C CA  . ASN B 1 127 ? 132.894 107.920 90.757  1.00 71.32  ? 114 ASN B CA  1 
ATOM   4069 C C   . ASN B 1 127 ? 134.126 108.238 89.904  1.00 74.75  ? 114 ASN B C   1 
ATOM   4070 O O   . ASN B 1 127 ? 134.088 108.267 88.675  1.00 74.07  ? 114 ASN B O   1 
ATOM   4071 C CB  . ASN B 1 127 ? 131.694 107.556 89.895  1.00 74.19  ? 114 ASN B CB  1 
ATOM   4072 C CG  . ASN B 1 127 ? 130.501 107.120 90.718  1.00 76.53  ? 114 ASN B CG  1 
ATOM   4073 O OD1 . ASN B 1 127 ? 130.500 107.249 91.942  1.00 67.96  ? 114 ASN B OD1 1 
ATOM   4074 N ND2 . ASN B 1 127 ? 129.476 106.603 90.051  1.00 89.63  ? 114 ASN B ND2 1 
ATOM   4075 N N   . GLY B 1 128 ? 135.239 108.485 90.596  1.00 76.05  ? 115 GLY B N   1 
ATOM   4076 C CA  . GLY B 1 128 ? 136.523 108.699 89.963  1.00 74.19  ? 115 GLY B CA  1 
ATOM   4077 C C   . GLY B 1 128 ? 136.703 110.020 89.250  1.00 72.76  ? 115 GLY B C   1 
ATOM   4078 O O   . GLY B 1 128 ? 137.840 110.362 88.902  1.00 70.70  ? 115 GLY B O   1 
ATOM   4079 N N   . GLN B 1 129 ? 135.636 110.779 89.021  1.00 70.35  ? 116 GLN B N   1 
ATOM   4080 C CA  . GLN B 1 129 ? 135.727 112.026 88.278  1.00 75.87  ? 116 GLN B CA  1 
ATOM   4081 C C   . GLN B 1 129 ? 135.901 113.209 89.224  1.00 73.97  ? 116 GLN B C   1 
ATOM   4082 O O   . GLN B 1 129 ? 135.359 113.233 90.332  1.00 73.79  ? 116 GLN B O   1 
ATOM   4083 C CB  . GLN B 1 129 ? 134.483 112.226 87.413  1.00 84.15  ? 116 GLN B CB  1 
ATOM   4084 C CG  . GLN B 1 129 ? 133.171 112.060 88.162  1.00 81.23  ? 116 GLN B CG  1 
ATOM   4085 C CD  . GLN B 1 129 ? 131.964 112.234 87.265  1.00 85.00  ? 116 GLN B CD  1 
ATOM   4086 O OE1 . GLN B 1 129 ? 130.822 112.167 87.721  1.00 84.08  ? 116 GLN B OE1 1 
ATOM   4087 N NE2 . GLN B 1 129 ? 132.209 112.460 85.981  1.00 86.03  ? 116 GLN B NE2 1 
ATOM   4088 N N   . ILE B 1 130 ? 136.666 114.198 88.770  1.00 71.48  ? 117 ILE B N   1 
ATOM   4089 C CA  . ILE B 1 130 ? 136.973 115.375 89.578  1.00 69.41  ? 117 ILE B CA  1 
ATOM   4090 C C   . ILE B 1 130 ? 136.719 116.634 88.757  1.00 76.22  ? 117 ILE B C   1 
ATOM   4091 O O   . ILE B 1 130 ? 136.931 116.630 87.535  1.00 80.11  ? 117 ILE B O   1 
ATOM   4092 C CB  . ILE B 1 130 ? 138.423 115.335 90.084  1.00 69.35  ? 117 ILE B CB  1 
ATOM   4093 C CG1 . ILE B 1 130 ? 139.390 115.180 88.908  1.00 68.81  ? 117 ILE B CG1 1 
ATOM   4094 C CG2 . ILE B 1 130 ? 138.608 114.203 91.076  1.00 71.15  ? 117 ILE B CG2 1 
ATOM   4095 C CD1 . ILE B 1 130 ? 140.839 115.049 89.314  1.00 65.85  ? 117 ILE B CD1 1 
ATOM   4096 N N   . PRO B 1 131 ? 136.260 117.721 89.373  1.00 77.03  ? 118 PRO B N   1 
ATOM   4097 C CA  . PRO B 1 131 ? 136.106 118.976 88.631  1.00 77.61  ? 118 PRO B CA  1 
ATOM   4098 C C   . PRO B 1 131 ? 137.451 119.547 88.214  1.00 71.19  ? 118 PRO B C   1 
ATOM   4099 O O   . PRO B 1 131 ? 138.458 119.405 88.911  1.00 69.63  ? 118 PRO B O   1 
ATOM   4100 C CB  . PRO B 1 131 ? 135.398 119.898 89.632  1.00 76.32  ? 118 PRO B CB  1 
ATOM   4101 C CG  . PRO B 1 131 ? 134.793 118.978 90.648  1.00 73.03  ? 118 PRO B CG  1 
ATOM   4102 C CD  . PRO B 1 131 ? 135.730 117.818 90.742  1.00 69.70  ? 118 PRO B CD  1 
ATOM   4103 N N   . SER B 1 132 ? 137.456 120.209 87.055  1.00 67.97  ? 119 SER B N   1 
ATOM   4104 C CA  . SER B 1 132 ? 138.685 120.825 86.567  1.00 73.16  ? 119 SER B CA  1 
ATOM   4105 C C   . SER B 1 132 ? 139.104 121.996 87.447  1.00 82.99  ? 119 SER B C   1 
ATOM   4106 O O   . SER B 1 132 ? 140.300 122.207 87.682  1.00 88.44  ? 119 SER B O   1 
ATOM   4107 C CB  . SER B 1 132 ? 138.505 121.279 85.118  1.00 72.17  ? 119 SER B CB  1 
ATOM   4108 O OG  . SER B 1 132 ? 137.399 122.155 84.992  1.00 68.48  ? 119 SER B OG  1 
ATOM   4109 N N   . TRP B 1 133 ? 138.133 122.769 87.943  1.00 84.00  ? 120 TRP B N   1 
ATOM   4110 C CA  . TRP B 1 133 ? 138.447 123.947 88.743  1.00 83.00  ? 120 TRP B CA  1 
ATOM   4111 C C   . TRP B 1 133 ? 138.895 123.604 90.156  1.00 80.78  ? 120 TRP B C   1 
ATOM   4112 O O   . TRP B 1 133 ? 139.483 124.461 90.825  1.00 83.57  ? 120 TRP B O   1 
ATOM   4113 C CB  . TRP B 1 133 ? 137.237 124.878 88.805  1.00 79.50  ? 120 TRP B CB  1 
ATOM   4114 C CG  . TRP B 1 133 ? 135.945 124.172 89.071  1.00 78.48  ? 120 TRP B CG  1 
ATOM   4115 C CD1 . TRP B 1 133 ? 135.014 123.803 88.147  1.00 80.66  ? 120 TRP B CD1 1 
ATOM   4116 C CD2 . TRP B 1 133 ? 135.437 123.747 90.344  1.00 76.82  ? 120 TRP B CD2 1 
ATOM   4117 N NE1 . TRP B 1 133 ? 133.957 123.177 88.762  1.00 79.97  ? 120 TRP B NE1 1 
ATOM   4118 C CE2 . TRP B 1 133 ? 134.192 123.130 90.110  1.00 76.17  ? 120 TRP B CE2 1 
ATOM   4119 C CE3 . TRP B 1 133 ? 135.911 123.830 91.655  1.00 79.14  ? 120 TRP B CE3 1 
ATOM   4120 C CZ2 . TRP B 1 133 ? 133.418 122.598 91.139  1.00 70.59  ? 120 TRP B CZ2 1 
ATOM   4121 C CZ3 . TRP B 1 133 ? 135.140 123.299 92.676  1.00 73.38  ? 120 TRP B CZ3 1 
ATOM   4122 C CH2 . TRP B 1 133 ? 133.908 122.693 92.411  1.00 67.29  ? 120 TRP B CH2 1 
ATOM   4123 N N   . LEU B 1 134 ? 138.635 122.385 90.625  1.00 76.14  ? 121 LEU B N   1 
ATOM   4124 C CA  . LEU B 1 134 ? 138.965 122.028 91.999  1.00 76.30  ? 121 LEU B CA  1 
ATOM   4125 C C   . LEU B 1 134 ? 140.472 122.064 92.219  1.00 79.59  ? 121 LEU B C   1 
ATOM   4126 O O   . LEU B 1 134 ? 141.256 121.654 91.359  1.00 79.34  ? 121 LEU B O   1 
ATOM   4127 C CB  . LEU B 1 134 ? 138.422 120.642 92.336  1.00 75.57  ? 121 LEU B CB  1 
ATOM   4128 C CG  . LEU B 1 134 ? 138.433 120.282 93.824  1.00 72.68  ? 121 LEU B CG  1 
ATOM   4129 C CD1 . LEU B 1 134 ? 137.418 121.122 94.587  1.00 66.31  ? 121 LEU B CD1 1 
ATOM   4130 C CD2 . LEU B 1 134 ? 138.170 118.799 94.023  1.00 69.32  ? 121 LEU B CD2 1 
ATOM   4131 N N   . ASN B 1 135 ? 140.877 122.575 93.382  1.00 81.98  ? 122 ASN B N   1 
ATOM   4132 C CA  . ASN B 1 135 ? 142.290 122.654 93.748  1.00 83.03  ? 122 ASN B CA  1 
ATOM   4133 C C   . ASN B 1 135 ? 142.687 121.353 94.442  1.00 83.92  ? 122 ASN B C   1 
ATOM   4134 O O   . ASN B 1 135 ? 142.692 121.237 95.668  1.00 83.33  ? 122 ASN B O   1 
ATOM   4135 C CB  . ASN B 1 135 ? 142.546 123.872 94.627  1.00 82.22  ? 122 ASN B CB  1 
ATOM   4136 C CG  . ASN B 1 135 ? 144.021 124.187 94.779  1.00 85.00  ? 122 ASN B CG  1 
ATOM   4137 O OD1 . ASN B 1 135 ? 144.869 123.293 94.766  1.00 87.13  ? 122 ASN B OD1 1 
ATOM   4138 N ND2 . ASN B 1 135 ? 144.335 125.468 94.925  1.00 85.56  ? 122 ASN B ND2 1 
ATOM   4139 N N   . LEU B 1 136 ? 143.021 120.351 93.624  1.00 82.30  ? 123 LEU B N   1 
ATOM   4140 C CA  . LEU B 1 136 ? 143.541 119.095 94.154  1.00 83.59  ? 123 LEU B CA  1 
ATOM   4141 C C   . LEU B 1 136 ? 144.921 119.271 94.772  1.00 83.85  ? 123 LEU B C   1 
ATOM   4142 O O   . LEU B 1 136 ? 145.297 118.497 95.658  1.00 82.55  ? 123 LEU B O   1 
ATOM   4143 C CB  . LEU B 1 136 ? 143.586 118.039 93.045  1.00 84.23  ? 123 LEU B CB  1 
ATOM   4144 C CG  . LEU B 1 136 ? 142.275 117.551 92.419  1.00 86.83  ? 123 LEU B CG  1 
ATOM   4145 C CD1 . LEU B 1 136 ? 142.567 116.625 91.251  1.00 83.78  ? 123 LEU B CD1 1 
ATOM   4146 C CD2 . LEU B 1 136 ? 141.384 116.846 93.430  1.00 83.69  ? 123 LEU B CD2 1 
ATOM   4147 N N   . ASP B 1 137 ? 145.679 120.274 94.328  1.00 84.17  ? 124 ASP B N   1 
ATOM   4148 C CA  . ASP B 1 137 ? 146.971 120.567 94.934  1.00 85.02  ? 124 ASP B CA  1 
ATOM   4149 C C   . ASP B 1 137 ? 146.837 121.084 96.361  1.00 84.81  ? 124 ASP B C   1 
ATOM   4150 O O   . ASP B 1 137 ? 147.824 121.075 97.104  1.00 88.68  ? 124 ASP B O   1 
ATOM   4151 C CB  . ASP B 1 137 ? 147.731 121.572 94.068  1.00 86.84  ? 124 ASP B CB  1 
ATOM   4152 C CG  . ASP B 1 137 ? 147.995 121.046 92.669  1.00 90.03  ? 124 ASP B CG  1 
ATOM   4153 O OD1 . ASP B 1 137 ? 148.178 119.820 92.522  1.00 89.25  ? 124 ASP B OD1 1 
ATOM   4154 O OD2 . ASP B 1 137 ? 148.016 121.854 91.718  1.00 91.99  ? 124 ASP B OD2 1 
ATOM   4155 N N   . ASN B 1 138 ? 145.652 121.535 96.755  1.00 81.30  ? 125 ASN B N   1 
ATOM   4156 C CA  . ASN B 1 138 ? 145.414 121.942 98.137  1.00 81.05  ? 125 ASN B CA  1 
ATOM   4157 C C   . ASN B 1 138 ? 145.442 120.709 99.031  1.00 79.04  ? 125 ASN B C   1 
ATOM   4158 O O   . ASN B 1 138 ? 144.647 119.785 98.818  1.00 76.99  ? 125 ASN B O   1 
ATOM   4159 C CB  . ASN B 1 138 ? 144.070 122.661 98.252  1.00 78.27  ? 125 ASN B CB  1 
ATOM   4160 C CG  . ASN B 1 138 ? 143.896 123.384 99.579  1.00 74.77  ? 125 ASN B CG  1 
ATOM   4161 O OD1 . ASN B 1 138 ? 144.267 122.876 100.637 1.00 71.76  ? 125 ASN B OD1 1 
ATOM   4162 N ND2 . ASN B 1 138 ? 143.325 124.583 99.525  1.00 73.96  ? 125 ASN B ND2 1 
ATOM   4163 N N   . PRO B 1 139 ? 146.325 120.646 100.034 1.00 81.13  ? 126 PRO B N   1 
ATOM   4164 C CA  . PRO B 1 139 ? 146.421 119.468 100.907 1.00 76.50  ? 126 PRO B CA  1 
ATOM   4165 C C   . PRO B 1 139 ? 145.419 119.477 102.060 1.00 71.23  ? 126 PRO B C   1 
ATOM   4166 O O   . PRO B 1 139 ? 145.749 119.137 103.197 1.00 68.21  ? 126 PRO B O   1 
ATOM   4167 C CB  . PRO B 1 139 ? 147.864 119.546 101.412 1.00 77.98  ? 126 PRO B CB  1 
ATOM   4168 C CG  . PRO B 1 139 ? 148.136 121.011 101.475 1.00 78.07  ? 126 PRO B CG  1 
ATOM   4169 C CD  . PRO B 1 139 ? 147.375 121.636 100.328 1.00 78.22  ? 126 PRO B CD  1 
ATOM   4170 N N   . ARG B 1 140 ? 144.181 119.871 101.763 1.00 69.03  ? 127 ARG B N   1 
ATOM   4171 C CA  . ARG B 1 140 ? 143.126 119.852 102.767 1.00 61.85  ? 127 ARG B CA  1 
ATOM   4172 C C   . ARG B 1 140 ? 141.806 119.294 102.263 1.00 58.17  ? 127 ARG B C   1 
ATOM   4173 O O   . ARG B 1 140 ? 140.905 119.080 103.079 1.00 52.55  ? 127 ARG B O   1 
ATOM   4174 C CB  . ARG B 1 140 ? 142.892 121.262 103.326 1.00 62.31  ? 127 ARG B CB  1 
ATOM   4175 C CG  . ARG B 1 140 ? 142.548 121.279 104.805 1.00 60.02  ? 127 ARG B CG  1 
ATOM   4176 C CD  . ARG B 1 140 ? 142.503 122.694 105.351 1.00 55.09  ? 127 ARG B CD  1 
ATOM   4177 N NE  . ARG B 1 140 ? 142.573 122.709 106.806 1.00 56.51  ? 127 ARG B NE  1 
ATOM   4178 C CZ  . ARG B 1 140 ? 143.705 122.731 107.496 1.00 60.92  ? 127 ARG B CZ  1 
ATOM   4179 N NH1 . ARG B 1 140 ? 144.880 122.756 106.893 1.00 60.28  ? 127 ARG B NH1 1 
ATOM   4180 N NH2 . ARG B 1 140 ? 143.655 122.724 108.825 1.00 63.75  ? 127 ARG B NH2 1 
ATOM   4181 N N   . VAL B 1 141 ? 141.650 119.059 100.963 1.00 63.12  ? 128 VAL B N   1 
ATOM   4182 C CA  . VAL B 1 141 ? 140.477 118.401 100.401 1.00 57.41  ? 128 VAL B CA  1 
ATOM   4183 C C   . VAL B 1 141 ? 140.952 117.155 99.667  1.00 56.48  ? 128 VAL B C   1 
ATOM   4184 O O   . VAL B 1 141 ? 141.889 117.221 98.863  1.00 59.70  ? 128 VAL B O   1 
ATOM   4185 C CB  . VAL B 1 141 ? 139.687 119.335 99.464  1.00 58.76  ? 128 VAL B CB  1 
ATOM   4186 C CG1 . VAL B 1 141 ? 140.614 120.008 98.461  1.00 66.62  ? 128 VAL B CG1 1 
ATOM   4187 C CG2 . VAL B 1 141 ? 138.589 118.566 98.748  1.00 52.06  ? 128 VAL B CG2 1 
ATOM   4188 N N   . THR B 1 142 ? 140.322 116.019 99.956  1.00 55.44  ? 129 THR B N   1 
ATOM   4189 C CA  . THR B 1 142 ? 140.754 114.731 99.429  1.00 56.64  ? 129 THR B CA  1 
ATOM   4190 C C   . THR B 1 142 ? 139.606 114.078 98.674  1.00 50.79  ? 129 THR B C   1 
ATOM   4191 O O   . THR B 1 142 ? 138.512 113.910 99.225  1.00 45.88  ? 129 THR B O   1 
ATOM   4192 C CB  . THR B 1 142 ? 141.241 113.814 100.552 1.00 59.68  ? 129 THR B CB  1 
ATOM   4193 O OG1 . THR B 1 142 ? 142.411 114.377 101.159 1.00 58.08  ? 129 THR B OG1 1 
ATOM   4194 C CG2 . THR B 1 142 ? 141.574 112.434 100.005 1.00 62.45  ? 129 THR B CG2 1 
ATOM   4195 N N   . ILE B 1 143 ? 139.858 113.716 97.420  1.00 53.63  ? 130 ILE B N   1 
ATOM   4196 C CA  . ILE B 1 143 ? 138.916 112.917 96.647  1.00 55.34  ? 130 ILE B CA  1 
ATOM   4197 C C   . ILE B 1 143 ? 139.030 111.467 97.090  1.00 60.40  ? 130 ILE B C   1 
ATOM   4198 O O   . ILE B 1 143 ? 140.129 110.966 97.359  1.00 64.10  ? 130 ILE B O   1 
ATOM   4199 C CB  . ILE B 1 143 ? 139.183 113.068 95.139  1.00 57.08  ? 130 ILE B CB  1 
ATOM   4200 C CG1 . ILE B 1 143 ? 140.590 112.575 94.793  1.00 65.46  ? 130 ILE B CG1 1 
ATOM   4201 C CG2 . ILE B 1 143 ? 139.014 114.515 94.718  1.00 60.12  ? 130 ILE B CG2 1 
ATOM   4202 C CD1 . ILE B 1 143 ? 140.862 112.477 93.312  1.00 66.98  ? 130 ILE B CD1 1 
ATOM   4203 N N   . VAL B 1 144 ? 137.891 110.789 97.199  1.00 58.35  ? 131 VAL B N   1 
ATOM   4204 C CA  . VAL B 1 144 ? 137.843 109.412 97.676  1.00 56.17  ? 131 VAL B CA  1 
ATOM   4205 C C   . VAL B 1 144 ? 137.105 108.568 96.648  1.00 62.42  ? 131 VAL B C   1 
ATOM   4206 O O   . VAL B 1 144 ? 135.938 108.839 96.336  1.00 61.75  ? 131 VAL B O   1 
ATOM   4207 C CB  . VAL B 1 144 ? 137.172 109.309 99.054  1.00 50.97  ? 131 VAL B CB  1 
ATOM   4208 C CG1 . VAL B 1 144 ? 137.111 107.863 99.497  1.00 58.22  ? 131 VAL B CG1 1 
ATOM   4209 C CG2 . VAL B 1 144 ? 137.926 110.147 100.074 1.00 53.26  ? 131 VAL B CG2 1 
ATOM   4210 N N   . THR B 1 145 ? 137.780 107.547 96.130  1.00 69.29  ? 132 THR B N   1 
ATOM   4211 C CA  . THR B 1 145 ? 137.162 106.576 95.243  1.00 68.57  ? 132 THR B CA  1 
ATOM   4212 C C   . THR B 1 145 ? 136.631 105.394 96.049  1.00 66.53  ? 132 THR B C   1 
ATOM   4213 O O   . THR B 1 145 ? 136.965 105.203 97.219  1.00 70.82  ? 132 THR B O   1 
ATOM   4214 C CB  . THR B 1 145 ? 138.156 106.098 94.185  1.00 71.01  ? 132 THR B CB  1 
ATOM   4215 O OG1 . THR B 1 145 ? 139.368 105.677 94.823  1.00 70.59  ? 132 THR B OG1 1 
ATOM   4216 C CG2 . THR B 1 145 ? 138.464 107.213 93.199  1.00 67.50  ? 132 THR B CG2 1 
ATOM   4217 N N   . HIS B 1 146 ? 135.799 104.583 95.397  1.00 65.22  ? 133 HIS B N   1 
ATOM   4218 C CA  . HIS B 1 146 ? 135.121 103.483 96.069  1.00 70.76  ? 133 HIS B CA  1 
ATOM   4219 C C   . HIS B 1 146 ? 136.035 102.306 96.383  1.00 74.64  ? 133 HIS B C   1 
ATOM   4220 O O   . HIS B 1 146 ? 135.607 101.389 97.091  1.00 73.13  ? 133 HIS B O   1 
ATOM   4221 C CB  . HIS B 1 146 ? 133.935 103.009 95.226  1.00 75.54  ? 133 HIS B CB  1 
ATOM   4222 C CG  . HIS B 1 146 ? 132.773 103.953 95.243  1.00 73.69  ? 133 HIS B CG  1 
ATOM   4223 N ND1 . HIS B 1 146 ? 132.925 105.322 95.211  1.00 66.47  ? 133 HIS B ND1 1 
ATOM   4224 C CD2 . HIS B 1 146 ? 131.439 103.724 95.295  1.00 65.65  ? 133 HIS B CD2 1 
ATOM   4225 C CE1 . HIS B 1 146 ? 131.737 105.897 95.240  1.00 58.83  ? 133 HIS B CE1 1 
ATOM   4226 N NE2 . HIS B 1 146 ? 130.818 104.950 95.291  1.00 53.77  ? 133 HIS B NE2 1 
ATOM   4227 N N   . GLN B 1 147 ? 137.274 102.302 95.883  1.00 80.26  ? 134 GLN B N   1 
ATOM   4228 C CA  . GLN B 1 147 ? 138.195 101.216 96.196  1.00 81.40  ? 134 GLN B CA  1 
ATOM   4229 C C   . GLN B 1 147 ? 138.564 101.171 97.673  1.00 80.63  ? 134 GLN B C   1 
ATOM   4230 O O   . GLN B 1 147 ? 139.047 100.136 98.145  1.00 82.07  ? 134 GLN B O   1 
ATOM   4231 C CB  . GLN B 1 147 ? 139.468 101.332 95.354  1.00 77.66  ? 134 GLN B CB  1 
ATOM   4232 C CG  . GLN B 1 147 ? 139.325 100.864 93.912  1.00 74.73  ? 134 GLN B CG  1 
ATOM   4233 C CD  . GLN B 1 147 ? 138.598 101.865 93.037  1.00 72.38  ? 134 GLN B CD  1 
ATOM   4234 O OE1 . GLN B 1 147 ? 139.204 102.793 92.501  1.00 71.69  ? 134 GLN B OE1 1 
ATOM   4235 N NE2 . GLN B 1 147 ? 137.292 101.681 92.887  1.00 70.01  ? 134 GLN B NE2 1 
ATOM   4236 N N   . ASP B 1 148 ? 138.353 102.263 98.410  1.00 79.76  ? 135 ASP B N   1 
ATOM   4237 C CA  . ASP B 1 148 ? 138.627 102.308 99.842  1.00 86.50  ? 135 ASP B CA  1 
ATOM   4238 C C   . ASP B 1 148 ? 137.373 102.619 100.651 1.00 84.29  ? 135 ASP B C   1 
ATOM   4239 O O   . ASP B 1 148 ? 137.472 103.112 101.780 1.00 83.09  ? 135 ASP B O   1 
ATOM   4240 C CB  . ASP B 1 148 ? 139.721 103.330 100.149 1.00 97.99  ? 135 ASP B CB  1 
ATOM   4241 C CG  . ASP B 1 148 ? 141.081 102.892 99.646  1.00 106.95 ? 135 ASP B CG  1 
ATOM   4242 O OD1 . ASP B 1 148 ? 141.325 101.668 99.596  1.00 109.91 ? 135 ASP B OD1 1 
ATOM   4243 O OD2 . ASP B 1 148 ? 141.902 103.770 99.301  1.00 112.23 ? 135 ASP B OD2 1 
ATOM   4244 N N   . VAL B 1 149 ? 136.192 102.347 100.093 1.00 81.48  ? 136 VAL B N   1 
ATOM   4245 C CA  . VAL B 1 149 ? 134.919 102.612 100.752 1.00 75.42  ? 136 VAL B CA  1 
ATOM   4246 C C   . VAL B 1 149 ? 134.080 101.345 100.876 1.00 73.03  ? 136 VAL B C   1 
ATOM   4247 O O   . VAL B 1 149 ? 133.614 100.999 101.966 1.00 70.01  ? 136 VAL B O   1 
ATOM   4248 C CB  . VAL B 1 149 ? 134.130 103.722 100.024 1.00 70.46  ? 136 VAL B CB  1 
ATOM   4249 C CG1 . VAL B 1 149 ? 132.961 104.174 100.860 1.00 62.37  ? 136 VAL B CG1 1 
ATOM   4250 C CG2 . VAL B 1 149 ? 135.034 104.899 99.721  1.00 70.32  ? 136 VAL B CG2 1 
ATOM   4251 N N   . PHE B 1 150 ? 133.881 100.636 99.767  1.00 72.20  ? 137 PHE B N   1 
ATOM   4252 C CA  . PHE B 1 150 ? 133.112 99.398  99.782  1.00 71.17  ? 137 PHE B CA  1 
ATOM   4253 C C   . PHE B 1 150 ? 133.957 98.239  100.294 1.00 76.09  ? 137 PHE B C   1 
ATOM   4254 O O   . PHE B 1 150 ? 135.141 98.123  99.968  1.00 78.53  ? 137 PHE B O   1 
ATOM   4255 C CB  . PHE B 1 150 ? 132.585 99.079  98.383  1.00 70.58  ? 137 PHE B CB  1 
ATOM   4256 C CG  . PHE B 1 150 ? 131.323 99.811  98.026  1.00 67.67  ? 137 PHE B CG  1 
ATOM   4257 C CD1 . PHE B 1 150 ? 130.373 100.094 98.991  1.00 65.15  ? 137 PHE B CD1 1 
ATOM   4258 C CD2 . PHE B 1 150 ? 131.087 100.213 96.722  1.00 70.52  ? 137 PHE B CD2 1 
ATOM   4259 C CE1 . PHE B 1 150 ? 129.210 100.765 98.663  1.00 60.67  ? 137 PHE B CE1 1 
ATOM   4260 C CE2 . PHE B 1 150 ? 129.927 100.885 96.390  1.00 68.83  ? 137 PHE B CE2 1 
ATOM   4261 C CZ  . PHE B 1 150 ? 128.988 101.161 97.361  1.00 60.28  ? 137 PHE B CZ  1 
ATOM   4262 N N   . ARG B 1 151 ? 133.335 97.378  101.103 1.00 75.85  ? 138 ARG B N   1 
ATOM   4263 C CA  . ARG B 1 151 ? 134.034 96.206  101.624 1.00 80.64  ? 138 ARG B CA  1 
ATOM   4264 C C   . ARG B 1 151 ? 134.333 95.206  100.517 1.00 87.05  ? 138 ARG B C   1 
ATOM   4265 O O   . ARG B 1 151 ? 135.369 94.532  100.545 1.00 93.86  ? 138 ARG B O   1 
ATOM   4266 C CB  . ARG B 1 151 ? 133.207 95.547  102.729 1.00 78.12  ? 138 ARG B CB  1 
ATOM   4267 C CG  . ARG B 1 151 ? 132.815 96.477  103.865 1.00 77.38  ? 138 ARG B CG  1 
ATOM   4268 C CD  . ARG B 1 151 ? 134.026 97.161  104.492 1.00 74.84  ? 138 ARG B CD  1 
ATOM   4269 N NE  . ARG B 1 151 ? 134.351 98.430  103.849 1.00 73.74  ? 138 ARG B NE  1 
ATOM   4270 C CZ  . ARG B 1 151 ? 135.246 99.295  104.305 1.00 73.01  ? 138 ARG B CZ  1 
ATOM   4271 N NH1 . ARG B 1 151 ? 135.919 99.068  105.420 1.00 68.34  ? 138 ARG B NH1 1 
ATOM   4272 N NH2 . ARG B 1 151 ? 135.469 100.416 103.626 1.00 72.63  ? 138 ARG B NH2 1 
ATOM   4273 N N   . ASN B 1 152 ? 133.428 95.077  99.554  1.00 87.07  ? 139 ASN B N   1 
ATOM   4274 C CA  . ASN B 1 152 ? 133.608 94.206  98.405  1.00 88.40  ? 139 ASN B CA  1 
ATOM   4275 C C   . ASN B 1 152 ? 133.661 95.040  97.134  1.00 86.08  ? 139 ASN B C   1 
ATOM   4276 O O   . ASN B 1 152 ? 132.988 96.069  97.026  1.00 84.72  ? 139 ASN B O   1 
ATOM   4277 C CB  . ASN B 1 152 ? 132.481 93.179  98.316  1.00 87.85  ? 139 ASN B CB  1 
ATOM   4278 C CG  . ASN B 1 152 ? 131.123 93.820  98.175  1.00 84.57  ? 139 ASN B CG  1 
ATOM   4279 O OD1 . ASN B 1 152 ? 130.660 94.072  97.066  1.00 81.19  ? 139 ASN B OD1 1 
ATOM   4280 N ND2 . ASN B 1 152 ? 130.473 94.090  99.303  1.00 87.60  ? 139 ASN B ND2 1 
ATOM   4281 N N   . LEU B 1 153 ? 134.459 94.588  96.174  1.00 88.13  ? 140 LEU B N   1 
ATOM   4282 C CA  . LEU B 1 153 ? 134.684 95.322  94.938  1.00 93.77  ? 140 LEU B CA  1 
ATOM   4283 C C   . LEU B 1 153 ? 133.651 95.016  93.862  1.00 94.17  ? 140 LEU B C   1 
ATOM   4284 O O   . LEU B 1 153 ? 133.784 95.515  92.739  1.00 94.22  ? 140 LEU B O   1 
ATOM   4285 C CB  . LEU B 1 153 ? 136.089 95.028  94.398  1.00 97.68  ? 140 LEU B CB  1 
ATOM   4286 C CG  . LEU B 1 153 ? 137.236 95.895  94.924  1.00 89.27  ? 140 LEU B CG  1 
ATOM   4287 C CD1 . LEU B 1 153 ? 136.908 97.372  94.757  1.00 89.71  ? 140 LEU B CD1 1 
ATOM   4288 C CD2 . LEU B 1 153 ? 137.564 95.575  96.375  1.00 85.64  ? 140 LEU B CD2 1 
ATOM   4289 N N   . SER B 1 154 ? 132.637 94.210  94.167  1.00 91.02  ? 141 SER B N   1 
ATOM   4290 C CA  . SER B 1 154 ? 131.617 93.852  93.189  1.00 93.79  ? 141 SER B CA  1 
ATOM   4291 C C   . SER B 1 154 ? 130.512 94.892  93.065  1.00 93.57  ? 141 SER B C   1 
ATOM   4292 O O   . SER B 1 154 ? 129.626 94.730  92.219  1.00 95.69  ? 141 SER B O   1 
ATOM   4293 C CB  . SER B 1 154 ? 131.005 92.493  93.542  1.00 89.03  ? 141 SER B CB  1 
ATOM   4294 O OG  . SER B 1 154 ? 130.425 92.514  94.835  1.00 82.14  ? 141 SER B OG  1 
ATOM   4295 N N   . HIS B 1 155 ? 130.542 95.949  93.874  1.00 89.11  ? 142 HIS B N   1 
ATOM   4296 C CA  . HIS B 1 155 ? 129.518 96.984  93.854  1.00 87.42  ? 142 HIS B CA  1 
ATOM   4297 C C   . HIS B 1 155 ? 130.035 98.314  93.319  1.00 89.92  ? 142 HIS B C   1 
ATOM   4298 O O   . HIS B 1 155 ? 129.379 99.344  93.512  1.00 85.36  ? 142 HIS B O   1 
ATOM   4299 C CB  . HIS B 1 155 ? 128.938 97.175  95.257  1.00 83.17  ? 142 HIS B CB  1 
ATOM   4300 C CG  . HIS B 1 155 ? 128.211 95.977  95.783  1.00 82.00  ? 142 HIS B CG  1 
ATOM   4301 N ND1 . HIS B 1 155 ? 128.562 95.351  96.960  1.00 77.90  ? 142 HIS B ND1 1 
ATOM   4302 C CD2 . HIS B 1 155 ? 127.143 95.300  95.300  1.00 80.45  ? 142 HIS B CD2 1 
ATOM   4303 C CE1 . HIS B 1 155 ? 127.745 94.335  97.175  1.00 75.95  ? 142 HIS B CE1 1 
ATOM   4304 N NE2 . HIS B 1 155 ? 126.876 94.282  96.182  1.00 81.90  ? 142 HIS B NE2 1 
ATOM   4305 N N   . LEU B 1 156 ? 131.190 98.320  92.650  1.00 93.77  ? 143 LEU B N   1 
ATOM   4306 C CA  . LEU B 1 156 ? 131.790 99.562  92.169  1.00 94.94  ? 143 LEU B CA  1 
ATOM   4307 C C   . LEU B 1 156 ? 130.905 100.301 91.163  1.00 93.93  ? 143 LEU B C   1 
ATOM   4308 O O   . LEU B 1 156 ? 130.969 101.536 91.106  1.00 95.17  ? 143 LEU B O   1 
ATOM   4309 C CB  . LEU B 1 156 ? 133.188 99.298  91.585  1.00 97.40  ? 143 LEU B CB  1 
ATOM   4310 C CG  . LEU B 1 156 ? 133.485 98.362  90.408  1.00 99.91  ? 143 LEU B CG  1 
ATOM   4311 C CD1 . LEU B 1 156 ? 133.421 99.106  89.078  1.00 96.42  ? 143 LEU B CD1 1 
ATOM   4312 C CD2 . LEU B 1 156 ? 134.841 97.692  90.581  1.00 99.21  ? 143 LEU B CD2 1 
ATOM   4313 N N   . PRO B 1 157 ? 130.069 99.621  90.346  1.00 92.86  ? 144 PRO B N   1 
ATOM   4314 C CA  . PRO B 1 157 ? 129.036 100.383 89.621  1.00 95.18  ? 144 PRO B CA  1 
ATOM   4315 C C   . PRO B 1 157 ? 127.819 100.660 90.497  1.00 93.62  ? 144 PRO B C   1 
ATOM   4316 O O   . PRO B 1 157 ? 126.700 100.228 90.210  1.00 96.23  ? 144 PRO B O   1 
ATOM   4317 C CB  . PRO B 1 157 ? 128.715 99.462  88.434  1.00 98.18  ? 144 PRO B CB  1 
ATOM   4318 C CG  . PRO B 1 157 ? 129.768 98.398  88.431  1.00 94.92  ? 144 PRO B CG  1 
ATOM   4319 C CD  . PRO B 1 157 ? 130.116 98.234  89.861  1.00 92.61  ? 144 PRO B CD  1 
ATOM   4320 N N   . THR B 1 158 ? 128.046 101.388 91.593  1.00 86.49  ? 145 THR B N   1 
ATOM   4321 C CA  . THR B 1 158 ? 127.000 101.576 92.592  1.00 86.36  ? 145 THR B CA  1 
ATOM   4322 C C   . THR B 1 158 ? 125.777 102.258 91.995  1.00 87.07  ? 145 THR B C   1 
ATOM   4323 O O   . THR B 1 158 ? 124.658 101.747 92.101  1.00 87.43  ? 145 THR B O   1 
ATOM   4324 C CB  . THR B 1 158 ? 127.536 102.391 93.768  1.00 82.39  ? 145 THR B CB  1 
ATOM   4325 O OG1 . THR B 1 158 ? 126.573 102.390 94.830  1.00 76.49  ? 145 THR B OG1 1 
ATOM   4326 C CG2 . THR B 1 158 ? 127.805 103.825 93.340  1.00 86.00  ? 145 THR B CG2 1 
ATOM   4327 N N   . PHE B 1 159 ? 125.973 103.412 91.358  1.00 84.44  ? 146 PHE B N   1 
ATOM   4328 C CA  . PHE B 1 159 ? 124.910 104.144 90.675  1.00 88.17  ? 146 PHE B CA  1 
ATOM   4329 C C   . PHE B 1 159 ? 123.727 104.456 91.584  1.00 85.67  ? 146 PHE B C   1 
ATOM   4330 O O   . PHE B 1 159 ? 122.634 104.753 91.093  1.00 88.15  ? 146 PHE B O   1 
ATOM   4331 C CB  . PHE B 1 159 ? 124.416 103.369 89.448  1.00 93.31  ? 146 PHE B CB  1 
ATOM   4332 C CG  . PHE B 1 159 ? 125.341 103.438 88.266  1.00 95.15  ? 146 PHE B CG  1 
ATOM   4333 C CD1 . PHE B 1 159 ? 126.680 103.746 88.429  1.00 96.79  ? 146 PHE B CD1 1 
ATOM   4334 C CD2 . PHE B 1 159 ? 124.864 103.207 86.988  1.00 100.52 ? 146 PHE B CD2 1 
ATOM   4335 C CE1 . PHE B 1 159 ? 127.526 103.811 87.344  1.00 101.50 ? 146 PHE B CE1 1 
ATOM   4336 C CE2 . PHE B 1 159 ? 125.706 103.274 85.898  1.00 112.12 ? 146 PHE B CE2 1 
ATOM   4337 C CZ  . PHE B 1 159 ? 127.039 103.576 86.078  1.00 112.73 ? 146 PHE B CZ  1 
ATOM   4338 N N   . SER B 1 160 ? 123.922 104.392 92.900  1.00 78.87  ? 147 SER B N   1 
ATOM   4339 C CA  . SER B 1 160 ? 122.834 104.629 93.839  1.00 71.53  ? 147 SER B CA  1 
ATOM   4340 C C   . SER B 1 160 ? 123.404 105.244 95.106  1.00 62.95  ? 147 SER B C   1 
ATOM   4341 O O   . SER B 1 160 ? 124.382 104.733 95.659  1.00 64.33  ? 147 SER B O   1 
ATOM   4342 C CB  . SER B 1 160 ? 122.082 103.333 94.162  1.00 74.00  ? 147 SER B CB  1 
ATOM   4343 O OG  . SER B 1 160 ? 120.858 103.604 94.824  1.00 74.29  ? 147 SER B OG  1 
ATOM   4344 N N   . SER B 1 161 ? 122.793 106.340 95.552  1.00 63.36  ? 148 SER B N   1 
ATOM   4345 C CA  . SER B 1 161 ? 123.310 107.053 96.716  1.00 60.39  ? 148 SER B CA  1 
ATOM   4346 C C   . SER B 1 161 ? 123.353 106.220 97.995  1.00 58.10  ? 148 SER B C   1 
ATOM   4347 O O   . SER B 1 161 ? 124.393 106.260 98.675  1.00 54.78  ? 148 SER B O   1 
ATOM   4348 C CB  . SER B 1 161 ? 122.505 108.342 96.930  1.00 63.67  ? 148 SER B CB  1 
ATOM   4349 O OG  . SER B 1 161 ? 121.120 108.141 96.709  1.00 64.46  ? 148 SER B OG  1 
ATOM   4350 N N   . PRO B 1 162 ? 122.316 105.462 98.383  1.00 58.05  ? 149 PRO B N   1 
ATOM   4351 C CA  . PRO B 1 162 ? 122.374 104.779 99.689  1.00 49.20  ? 149 PRO B CA  1 
ATOM   4352 C C   . PRO B 1 162 ? 123.547 103.828 99.839  1.00 47.66  ? 149 PRO B C   1 
ATOM   4353 O O   . PRO B 1 162 ? 124.071 103.684 100.951 1.00 53.43  ? 149 PRO B O   1 
ATOM   4354 C CB  . PRO B 1 162 ? 121.035 104.033 99.754  1.00 48.41  ? 149 PRO B CB  1 
ATOM   4355 C CG  . PRO B 1 162 ? 120.140 104.799 98.863  1.00 60.22  ? 149 PRO B CG  1 
ATOM   4356 C CD  . PRO B 1 162 ? 121.011 105.245 97.732  1.00 63.48  ? 149 PRO B CD  1 
ATOM   4357 N N   . ALA B 1 163 ? 123.982 103.179 98.758  1.00 49.23  ? 150 ALA B N   1 
ATOM   4358 C CA  . ALA B 1 163 ? 125.145 102.303 98.851  1.00 48.26  ? 150 ALA B CA  1 
ATOM   4359 C C   . ALA B 1 163 ? 126.386 103.086 99.258  1.00 47.86  ? 150 ALA B C   1 
ATOM   4360 O O   . ALA B 1 163 ? 127.172 102.631 100.097 1.00 53.74  ? 150 ALA B O   1 
ATOM   4361 C CB  . ALA B 1 163 ? 125.373 101.588 97.520  1.00 53.05  ? 150 ALA B CB  1 
ATOM   4362 N N   . ILE B 1 164 ? 126.573 104.271 98.678  1.00 49.89  ? 151 ILE B N   1 
ATOM   4363 C CA  . ILE B 1 164 ? 127.711 105.113 99.032  1.00 48.90  ? 151 ILE B CA  1 
ATOM   4364 C C   . ILE B 1 164 ? 127.550 105.669 100.442 1.00 49.65  ? 151 ILE B C   1 
ATOM   4365 O O   . ILE B 1 164 ? 128.526 105.790 101.193 1.00 51.35  ? 151 ILE B O   1 
ATOM   4366 C CB  . ILE B 1 164 ? 127.865 106.236 97.993  1.00 47.25  ? 151 ILE B CB  1 
ATOM   4367 C CG1 . ILE B 1 164 ? 127.765 105.659 96.580  1.00 49.40  ? 151 ILE B CG1 1 
ATOM   4368 C CG2 . ILE B 1 164 ? 129.176 106.975 98.191  1.00 47.88  ? 151 ILE B CG2 1 
ATOM   4369 C CD1 . ILE B 1 164 ? 127.154 106.608 95.582  1.00 51.56  ? 151 ILE B CD1 1 
ATOM   4370 N N   . GLU B 1 165 ? 126.321 106.042 100.810 1.00 49.17  ? 152 GLU B N   1 
ATOM   4371 C CA  . GLU B 1 165 ? 126.073 106.613 102.130 1.00 47.46  ? 152 GLU B CA  1 
ATOM   4372 C C   . GLU B 1 165 ? 126.398 105.613 103.230 1.00 47.43  ? 152 GLU B C   1 
ATOM   4373 O O   . GLU B 1 165 ? 127.057 105.952 104.219 1.00 43.19  ? 152 GLU B O   1 
ATOM   4374 C CB  . GLU B 1 165 ? 124.618 107.067 102.239 1.00 50.42  ? 152 GLU B CB  1 
ATOM   4375 C CG  . GLU B 1 165 ? 124.212 108.117 101.229 1.00 49.89  ? 152 GLU B CG  1 
ATOM   4376 C CD  . GLU B 1 165 ? 122.781 108.580 101.414 1.00 54.67  ? 152 GLU B CD  1 
ATOM   4377 O OE1 . GLU B 1 165 ? 122.024 107.907 102.144 1.00 59.44  ? 152 GLU B OE1 1 
ATOM   4378 O OE2 . GLU B 1 165 ? 122.414 109.622 100.831 1.00 56.50  ? 152 GLU B OE2 1 
ATOM   4379 N N   . SER B 1 166 ? 125.957 104.364 103.065 1.00 48.38  ? 153 SER B N   1 
ATOM   4380 C CA  . SER B 1 166 ? 126.151 103.356 104.100 1.00 42.34  ? 153 SER B CA  1 
ATOM   4381 C C   . SER B 1 166 ? 127.622 103.052 104.349 1.00 45.86  ? 153 SER B C   1 
ATOM   4382 O O   . SER B 1 166 ? 127.952 102.455 105.379 1.00 53.80  ? 153 SER B O   1 
ATOM   4383 C CB  . SER B 1 166 ? 125.409 102.073 103.727 1.00 41.03  ? 153 SER B CB  1 
ATOM   4384 O OG  . SER B 1 166 ? 124.012 102.295 103.668 1.00 47.08  ? 153 SER B OG  1 
ATOM   4385 N N   . HIS B 1 167 ? 128.510 103.442 103.437 1.00 45.55  ? 154 HIS B N   1 
ATOM   4386 C CA  . HIS B 1 167 ? 129.932 103.182 103.591 1.00 49.62  ? 154 HIS B CA  1 
ATOM   4387 C C   . HIS B 1 167 ? 130.770 104.448 103.714 1.00 52.65  ? 154 HIS B C   1 
ATOM   4388 O O   . HIS B 1 167 ? 131.987 104.347 103.908 1.00 55.45  ? 154 HIS B O   1 
ATOM   4389 C CB  . HIS B 1 167 ? 130.448 102.345 102.413 1.00 51.97  ? 154 HIS B CB  1 
ATOM   4390 C CG  . HIS B 1 167 ? 129.794 101.005 102.283 1.00 51.04  ? 154 HIS B CG  1 
ATOM   4391 N ND1 . HIS B 1 167 ? 130.496 99.823  102.380 1.00 56.76  ? 154 HIS B ND1 1 
ATOM   4392 C CD2 . HIS B 1 167 ? 128.506 100.659 102.051 1.00 52.36  ? 154 HIS B CD2 1 
ATOM   4393 C CE1 . HIS B 1 167 ? 129.668 98.807  102.220 1.00 59.77  ? 154 HIS B CE1 1 
ATOM   4394 N NE2 . HIS B 1 167 ? 128.454 99.287  102.019 1.00 56.42  ? 154 HIS B NE2 1 
ATOM   4395 N N   . ILE B 1 168 ? 130.160 105.633 103.608 1.00 53.39  ? 155 ILE B N   1 
ATOM   4396 C CA  . ILE B 1 168 ? 130.918 106.883 103.659 1.00 50.26  ? 155 ILE B CA  1 
ATOM   4397 C C   . ILE B 1 168 ? 131.695 107.062 104.959 1.00 43.87  ? 155 ILE B C   1 
ATOM   4398 O O   . ILE B 1 168 ? 132.668 107.822 104.995 1.00 42.37  ? 155 ILE B O   1 
ATOM   4399 C CB  . ILE B 1 168 ? 129.970 108.079 103.427 1.00 46.22  ? 155 ILE B CB  1 
ATOM   4400 C CG1 . ILE B 1 168 ? 130.755 109.291 102.929 1.00 38.48  ? 155 ILE B CG1 1 
ATOM   4401 C CG2 . ILE B 1 168 ? 129.215 108.431 104.701 1.00 39.02  ? 155 ILE B CG2 1 
ATOM   4402 C CD1 . ILE B 1 168 ? 129.894 110.493 102.654 1.00 37.68  ? 155 ILE B CD1 1 
ATOM   4403 N N   . HIS B 1 169 ? 131.300 106.379 106.031 1.00 42.18  ? 156 HIS B N   1 
ATOM   4404 C CA  . HIS B 1 169 ? 131.939 106.565 107.328 1.00 40.66  ? 156 HIS B CA  1 
ATOM   4405 C C   . HIS B 1 169 ? 133.224 105.762 107.487 1.00 42.90  ? 156 HIS B C   1 
ATOM   4406 O O   . HIS B 1 169 ? 133.882 105.882 108.525 1.00 39.47  ? 156 HIS B O   1 
ATOM   4407 C CB  . HIS B 1 169 ? 130.966 106.187 108.446 1.00 38.57  ? 156 HIS B CB  1 
ATOM   4408 C CG  . HIS B 1 169 ? 130.664 104.723 108.507 1.00 39.48  ? 156 HIS B CG  1 
ATOM   4409 N ND1 . HIS B 1 169 ? 129.840 104.095 107.599 1.00 40.93  ? 156 HIS B ND1 1 
ATOM   4410 C CD2 . HIS B 1 169 ? 131.080 103.763 109.365 1.00 41.21  ? 156 HIS B CD2 1 
ATOM   4411 C CE1 . HIS B 1 169 ? 129.761 102.810 107.895 1.00 43.33  ? 156 HIS B CE1 1 
ATOM   4412 N NE2 . HIS B 1 169 ? 130.503 102.583 108.963 1.00 42.54  ? 156 HIS B NE2 1 
ATOM   4413 N N   . ARG B 1 170 ? 133.599 104.957 106.497 1.00 46.90  ? 157 ARG B N   1 
ATOM   4414 C CA  . ARG B 1 170 ? 134.713 104.030 106.629 1.00 51.47  ? 157 ARG B CA  1 
ATOM   4415 C C   . ARG B 1 170 ? 135.964 104.487 105.889 1.00 58.36  ? 157 ARG B C   1 
ATOM   4416 O O   . ARG B 1 170 ? 136.856 103.670 105.637 1.00 62.60  ? 157 ARG B O   1 
ATOM   4417 C CB  . ARG B 1 170 ? 134.283 102.643 106.153 1.00 53.17  ? 157 ARG B CB  1 
ATOM   4418 C CG  . ARG B 1 170 ? 133.062 102.135 106.899 1.00 50.87  ? 157 ARG B CG  1 
ATOM   4419 C CD  . ARG B 1 170 ? 132.635 100.749 106.465 1.00 52.02  ? 157 ARG B CD  1 
ATOM   4420 N NE  . ARG B 1 170 ? 131.702 100.172 107.427 1.00 47.14  ? 157 ARG B NE  1 
ATOM   4421 C CZ  . ARG B 1 170 ? 131.098 99.001  107.279 1.00 52.65  ? 157 ARG B CZ  1 
ATOM   4422 N NH1 . ARG B 1 170 ? 131.290 98.256  106.204 1.00 58.14  ? 157 ARG B NH1 1 
ATOM   4423 N NH2 . ARG B 1 170 ? 130.282 98.568  108.234 1.00 52.86  ? 157 ARG B NH2 1 
ATOM   4424 N N   . ILE B 1 171 ? 136.051 105.766 105.538 1.00 53.28  ? 158 ILE B N   1 
ATOM   4425 C CA  . ILE B 1 171 ? 137.234 106.303 104.875 1.00 51.21  ? 158 ILE B CA  1 
ATOM   4426 C C   . ILE B 1 171 ? 138.349 106.483 105.895 1.00 54.98  ? 158 ILE B C   1 
ATOM   4427 O O   . ILE B 1 171 ? 138.113 106.914 107.030 1.00 54.29  ? 158 ILE B O   1 
ATOM   4428 C CB  . ILE B 1 171 ? 136.895 107.626 104.168 1.00 48.23  ? 158 ILE B CB  1 
ATOM   4429 C CG1 . ILE B 1 171 ? 136.209 108.587 105.139 1.00 41.34  ? 158 ILE B CG1 1 
ATOM   4430 C CG2 . ILE B 1 171 ? 136.007 107.370 102.963 1.00 55.89  ? 158 ILE B CG2 1 
ATOM   4431 C CD1 . ILE B 1 171 ? 135.538 109.763 104.467 1.00 41.85  ? 158 ILE B CD1 1 
ATOM   4432 N N   . GLU B 1 172 ? 139.573 106.148 105.493 1.00 59.80  ? 159 GLU B N   1 
ATOM   4433 C CA  . GLU B 1 172 ? 140.710 106.235 106.399 1.00 62.62  ? 159 GLU B CA  1 
ATOM   4434 C C   . GLU B 1 172 ? 141.039 107.690 106.715 1.00 59.08  ? 159 GLU B C   1 
ATOM   4435 O O   . GLU B 1 172 ? 140.938 108.569 105.855 1.00 54.61  ? 159 GLU B O   1 
ATOM   4436 C CB  . GLU B 1 172 ? 141.928 105.537 105.790 1.00 63.72  ? 159 GLU B CB  1 
ATOM   4437 C CG  . GLU B 1 172 ? 143.171 105.572 106.667 1.00 68.20  ? 159 GLU B CG  1 
ATOM   4438 C CD  . GLU B 1 172 ? 142.935 104.958 108.034 1.00 73.87  ? 159 GLU B CD  1 
ATOM   4439 O OE1 . GLU B 1 172 ? 142.412 103.828 108.095 1.00 68.84  ? 159 GLU B OE1 1 
ATOM   4440 O OE2 . GLU B 1 172 ? 143.263 105.611 109.048 1.00 82.86  ? 159 GLU B OE2 1 
ATOM   4441 N N   . GLY B 1 173 ? 141.435 107.938 107.961 1.00 59.85  ? 160 GLY B N   1 
ATOM   4442 C CA  . GLY B 1 173 ? 141.758 109.278 108.405 1.00 55.80  ? 160 GLY B CA  1 
ATOM   4443 C C   . GLY B 1 173 ? 140.573 110.137 108.775 1.00 48.83  ? 160 GLY B C   1 
ATOM   4444 O O   . GLY B 1 173 ? 140.756 111.327 109.055 1.00 49.22  ? 160 GLY B O   1 
ATOM   4445 N N   . LEU B 1 174 ? 139.368 109.578 108.787 1.00 43.70  ? 161 LEU B N   1 
ATOM   4446 C CA  . LEU B 1 174 ? 138.180 110.353 109.107 1.00 36.37  ? 161 LEU B CA  1 
ATOM   4447 C C   . LEU B 1 174 ? 138.073 110.583 110.609 1.00 39.20  ? 161 LEU B C   1 
ATOM   4448 O O   . LEU B 1 174 ? 138.418 109.711 111.412 1.00 45.30  ? 161 LEU B O   1 
ATOM   4449 C CB  . LEU B 1 174 ? 136.932 109.639 108.592 1.00 34.15  ? 161 LEU B CB  1 
ATOM   4450 C CG  . LEU B 1 174 ? 135.584 110.316 108.819 1.00 25.44  ? 161 LEU B CG  1 
ATOM   4451 C CD1 . LEU B 1 174 ? 135.568 111.690 108.183 1.00 29.31  ? 161 LEU B CD1 1 
ATOM   4452 C CD2 . LEU B 1 174 ? 134.478 109.453 108.253 1.00 30.27  ? 161 LEU B CD2 1 
ATOM   4453 N N   . SER B 1 175 ? 137.597 111.768 110.982 1.00 37.15  ? 162 SER B N   1 
ATOM   4454 C CA  . SER B 1 175 ? 137.404 112.096 112.386 1.00 31.82  ? 162 SER B CA  1 
ATOM   4455 C C   . SER B 1 175 ? 136.239 111.300 112.966 1.00 31.98  ? 162 SER B C   1 
ATOM   4456 O O   . SER B 1 175 ? 135.319 110.891 112.252 1.00 37.57  ? 162 SER B O   1 
ATOM   4457 C CB  . SER B 1 175 ? 137.154 113.596 112.545 1.00 33.96  ? 162 SER B CB  1 
ATOM   4458 O OG  . SER B 1 175 ? 138.218 114.351 111.987 1.00 39.20  ? 162 SER B OG  1 
ATOM   4459 N N   . GLN B 1 176 ? 136.286 111.080 114.284 1.00 30.51  ? 163 GLN B N   1 
ATOM   4460 C CA  . GLN B 1 176 ? 135.253 110.300 114.958 1.00 37.46  ? 163 GLN B CA  1 
ATOM   4461 C C   . GLN B 1 176 ? 133.872 110.923 114.808 1.00 33.47  ? 163 GLN B C   1 
ATOM   4462 O O   . GLN B 1 176 ? 132.865 110.219 114.943 1.00 32.99  ? 163 GLN B O   1 
ATOM   4463 C CB  . GLN B 1 176 ? 135.611 110.142 116.437 1.00 41.43  ? 163 GLN B CB  1 
ATOM   4464 C CG  . GLN B 1 176 ? 134.936 108.977 117.132 1.00 37.06  ? 163 GLN B CG  1 
ATOM   4465 C CD  . GLN B 1 176 ? 133.670 109.386 117.845 1.00 34.29  ? 163 GLN B CD  1 
ATOM   4466 O OE1 . GLN B 1 176 ? 133.284 110.553 117.822 1.00 40.13  ? 163 GLN B OE1 1 
ATOM   4467 N NE2 . GLN B 1 176 ? 133.019 108.429 118.491 1.00 31.49  ? 163 GLN B NE2 1 
ATOM   4468 N N   . LYS B 1 177 ? 133.801 112.222 114.539 1.00 26.86  ? 164 LYS B N   1 
ATOM   4469 C CA  . LYS B 1 177 ? 132.557 112.893 114.195 1.00 25.10  ? 164 LYS B CA  1 
ATOM   4470 C C   . LYS B 1 177 ? 132.765 113.675 112.910 1.00 24.91  ? 164 LYS B C   1 
ATOM   4471 O O   . LYS B 1 177 ? 133.826 114.269 112.704 1.00 30.04  ? 164 LYS B O   1 
ATOM   4472 C CB  . LYS B 1 177 ? 132.089 113.826 115.313 1.00 31.48  ? 164 LYS B CB  1 
ATOM   4473 C CG  . LYS B 1 177 ? 131.698 113.099 116.578 1.00 36.28  ? 164 LYS B CG  1 
ATOM   4474 C CD  . LYS B 1 177 ? 130.979 114.003 117.555 1.00 38.40  ? 164 LYS B CD  1 
ATOM   4475 C CE  . LYS B 1 177 ? 130.551 113.216 118.779 1.00 45.96  ? 164 LYS B CE  1 
ATOM   4476 N NZ  . LYS B 1 177 ? 129.113 113.420 119.087 1.00 42.63  ? 164 LYS B NZ  1 
ATOM   4477 N N   . PHE B 1 178 ? 131.758 113.660 112.041 1.00 22.49  ? 165 PHE B N   1 
ATOM   4478 C CA  . PHE B 1 178 ? 131.850 114.373 110.777 1.00 24.70  ? 165 PHE B CA  1 
ATOM   4479 C C   . PHE B 1 178 ? 130.463 114.832 110.355 1.00 24.17  ? 165 PHE B C   1 
ATOM   4480 O O   . PHE B 1 178 ? 129.446 114.329 110.838 1.00 25.29  ? 165 PHE B O   1 
ATOM   4481 C CB  . PHE B 1 178 ? 132.496 113.512 109.683 1.00 28.89  ? 165 PHE B CB  1 
ATOM   4482 C CG  . PHE B 1 178 ? 131.812 112.191 109.457 1.00 25.01  ? 165 PHE B CG  1 
ATOM   4483 C CD1 . PHE B 1 178 ? 130.897 112.036 108.432 1.00 20.48  ? 165 PHE B CD1 1 
ATOM   4484 C CD2 . PHE B 1 178 ? 132.099 111.101 110.258 1.00 24.03  ? 165 PHE B CD2 1 
ATOM   4485 C CE1 . PHE B 1 178 ? 130.275 110.826 108.221 1.00 18.40  ? 165 PHE B CE1 1 
ATOM   4486 C CE2 . PHE B 1 178 ? 131.477 109.890 110.050 1.00 21.76  ? 165 PHE B CE2 1 
ATOM   4487 C CZ  . PHE B 1 178 ? 130.567 109.753 109.029 1.00 19.75  ? 165 PHE B CZ  1 
ATOM   4488 N N   . ILE B 1 179 ? 130.438 115.801 109.444 1.00 24.37  ? 166 ILE B N   1 
ATOM   4489 C CA  . ILE B 1 179 ? 129.207 116.406 108.953 1.00 27.94  ? 166 ILE B CA  1 
ATOM   4490 C C   . ILE B 1 179 ? 128.981 115.938 107.524 1.00 37.65  ? 166 ILE B C   1 
ATOM   4491 O O   . ILE B 1 179 ? 129.878 116.044 106.679 1.00 41.84  ? 166 ILE B O   1 
ATOM   4492 C CB  . ILE B 1 179 ? 129.267 117.940 109.031 1.00 31.88  ? 166 ILE B CB  1 
ATOM   4493 C CG1 . ILE B 1 179 ? 129.557 118.389 110.462 1.00 37.57  ? 166 ILE B CG1 1 
ATOM   4494 C CG2 . ILE B 1 179 ? 127.968 118.544 108.557 1.00 35.34  ? 166 ILE B CG2 1 
ATOM   4495 C CD1 . ILE B 1 179 ? 128.503 117.975 111.454 1.00 37.09  ? 166 ILE B CD1 1 
ATOM   4496 N N   . TYR B 1 180 ? 127.784 115.423 107.255 1.00 39.84  ? 167 TYR B N   1 
ATOM   4497 C CA  . TYR B 1 180 ? 127.461 114.832 105.963 1.00 36.54  ? 167 TYR B CA  1 
ATOM   4498 C C   . TYR B 1 180 ? 126.762 115.859 105.082 1.00 37.75  ? 167 TYR B C   1 
ATOM   4499 O O   . TYR B 1 180 ? 125.707 116.385 105.449 1.00 38.98  ? 167 TYR B O   1 
ATOM   4500 C CB  . TYR B 1 180 ? 126.588 113.593 106.150 1.00 34.74  ? 167 TYR B CB  1 
ATOM   4501 C CG  . TYR B 1 180 ? 126.138 112.957 104.858 1.00 32.94  ? 167 TYR B CG  1 
ATOM   4502 C CD1 . TYR B 1 180 ? 127.057 112.413 103.976 1.00 32.26  ? 167 TYR B CD1 1 
ATOM   4503 C CD2 . TYR B 1 180 ? 124.793 112.888 104.529 1.00 38.89  ? 167 TYR B CD2 1 
ATOM   4504 C CE1 . TYR B 1 180 ? 126.650 111.828 102.797 1.00 39.32  ? 167 TYR B CE1 1 
ATOM   4505 C CE2 . TYR B 1 180 ? 124.376 112.304 103.351 1.00 43.18  ? 167 TYR B CE2 1 
ATOM   4506 C CZ  . TYR B 1 180 ? 125.310 111.776 102.489 1.00 46.19  ? 167 TYR B CZ  1 
ATOM   4507 O OH  . TYR B 1 180 ? 124.905 111.192 101.311 1.00 54.58  ? 167 TYR B OH  1 
ATOM   4508 N N   . LEU B 1 181 ? 127.350 116.142 103.925 1.00 40.90  ? 168 LEU B N   1 
ATOM   4509 C CA  . LEU B 1 181 ? 126.803 117.097 102.974 1.00 47.50  ? 168 LEU B CA  1 
ATOM   4510 C C   . LEU B 1 181 ? 126.381 116.359 101.713 1.00 46.96  ? 168 LEU B C   1 
ATOM   4511 O O   . LEU B 1 181 ? 127.150 115.559 101.167 1.00 45.43  ? 168 LEU B O   1 
ATOM   4512 C CB  . LEU B 1 181 ? 127.820 118.187 102.637 1.00 46.69  ? 168 LEU B CB  1 
ATOM   4513 C CG  . LEU B 1 181 ? 127.861 119.456 103.498 1.00 43.59  ? 168 LEU B CG  1 
ATOM   4514 C CD1 . LEU B 1 181 ? 126.581 120.252 103.351 1.00 41.71  ? 168 LEU B CD1 1 
ATOM   4515 C CD2 . LEU B 1 181 ? 128.119 119.133 104.958 1.00 38.42  ? 168 LEU B CD2 1 
ATOM   4516 N N   . ASN B 1 182 ? 125.165 116.636 101.247 1.00 48.64  ? 169 ASN B N   1 
ATOM   4517 C CA  . ASN B 1 182 ? 124.585 115.931 100.115 1.00 50.20  ? 169 ASN B CA  1 
ATOM   4518 C C   . ASN B 1 182 ? 124.740 116.694 98.806  1.00 61.73  ? 169 ASN B C   1 
ATOM   4519 O O   . ASN B 1 182 ? 124.018 116.406 97.846  1.00 70.29  ? 169 ASN B O   1 
ATOM   4520 C CB  . ASN B 1 182 ? 123.110 115.635 100.383 1.00 50.98  ? 169 ASN B CB  1 
ATOM   4521 C CG  . ASN B 1 182 ? 122.637 114.375 99.692  1.00 59.04  ? 169 ASN B CG  1 
ATOM   4522 O OD1 . ASN B 1 182 ? 123.224 113.939 98.702  1.00 60.68  ? 169 ASN B OD1 1 
ATOM   4523 N ND2 . ASN B 1 182 ? 121.558 113.789 100.201 1.00 69.45  ? 169 ASN B ND2 1 
ATOM   4524 N N   . ASP B 1 183 ? 125.651 117.666 98.752  1.00 58.84  ? 170 ASP B N   1 
ATOM   4525 C CA  . ASP B 1 183 ? 126.044 118.416 97.566  1.00 57.82  ? 170 ASP B CA  1 
ATOM   4526 C C   . ASP B 1 183 ? 124.975 119.425 97.148  1.00 57.50  ? 170 ASP B C   1 
ATOM   4527 O O   . ASP B 1 183 ? 125.201 120.179 96.202  1.00 59.41  ? 170 ASP B O   1 
ATOM   4528 C CB  . ASP B 1 183 ? 126.378 117.500 96.371  1.00 64.39  ? 170 ASP B CB  1 
ATOM   4529 C CG  . ASP B 1 183 ? 127.013 118.236 95.213  1.00 71.23  ? 170 ASP B CG  1 
ATOM   4530 O OD1 . ASP B 1 183 ? 126.344 118.379 94.166  1.00 74.74  ? 170 ASP B OD1 1 
ATOM   4531 O OD2 . ASP B 1 183 ? 128.169 118.679 95.347  1.00 70.62  ? 170 ASP B OD2 1 
ATOM   4532 N N   . ASP B 1 184 ? 123.818 119.468 97.810  1.00 58.69  ? 171 ASP B N   1 
ATOM   4533 C CA  . ASP B 1 184 ? 122.818 120.489 97.538  1.00 59.77  ? 171 ASP B CA  1 
ATOM   4534 C C   . ASP B 1 184 ? 122.482 121.365 98.736  1.00 57.03  ? 171 ASP B C   1 
ATOM   4535 O O   . ASP B 1 184 ? 121.908 122.442 98.543  1.00 55.23  ? 171 ASP B O   1 
ATOM   4536 C CB  . ASP B 1 184 ? 121.522 119.852 97.011  1.00 62.42  ? 171 ASP B CB  1 
ATOM   4537 C CG  . ASP B 1 184 ? 120.999 118.763 97.917  1.00 67.03  ? 171 ASP B CG  1 
ATOM   4538 O OD1 . ASP B 1 184 ? 121.790 118.237 98.728  1.00 70.35  ? 171 ASP B OD1 1 
ATOM   4539 O OD2 . ASP B 1 184 ? 119.801 118.427 97.809  1.00 64.57  ? 171 ASP B OD2 1 
ATOM   4540 N N   . VAL B 1 185 ? 122.817 120.944 99.953  1.00 52.88  ? 172 VAL B N   1 
ATOM   4541 C CA  . VAL B 1 185 ? 122.540 121.716 101.158 1.00 47.57  ? 172 VAL B CA  1 
ATOM   4542 C C   . VAL B 1 185 ? 123.753 122.565 101.504 1.00 45.27  ? 172 VAL B C   1 
ATOM   4543 O O   . VAL B 1 185 ? 124.899 122.118 101.382 1.00 47.29  ? 172 VAL B O   1 
ATOM   4544 C CB  . VAL B 1 185 ? 122.157 120.789 102.325 1.00 48.14  ? 172 VAL B CB  1 
ATOM   4545 C CG1 . VAL B 1 185 ? 120.751 120.265 102.128 1.00 59.28  ? 172 VAL B CG1 1 
ATOM   4546 C CG2 . VAL B 1 185 ? 123.138 119.636 102.422 1.00 49.01  ? 172 VAL B CG2 1 
ATOM   4547 N N   . MET B 1 186 ? 123.504 123.799 101.934 1.00 42.23  ? 173 MET B N   1 
ATOM   4548 C CA  . MET B 1 186 ? 124.560 124.741 102.272 1.00 39.81  ? 173 MET B CA  1 
ATOM   4549 C C   . MET B 1 186 ? 124.292 125.330 103.650 1.00 35.16  ? 173 MET B C   1 
ATOM   4550 O O   . MET B 1 186 ? 123.219 125.152 104.231 1.00 39.24  ? 173 MET B O   1 
ATOM   4551 C CB  . MET B 1 186 ? 124.675 125.855 101.222 1.00 40.51  ? 173 MET B CB  1 
ATOM   4552 C CG  . MET B 1 186 ? 124.957 125.352 99.815  1.00 40.43  ? 173 MET B CG  1 
ATOM   4553 S SD  . MET B 1 186 ? 125.274 126.670 98.629  1.00 50.04  ? 173 MET B SD  1 
ATOM   4554 C CE  . MET B 1 186 ? 123.800 127.666 98.827  1.00 55.37  ? 173 MET B CE  1 
ATOM   4555 N N   . PHE B 1 187 ? 125.291 126.032 104.174 1.00 28.94  ? 174 PHE B N   1 
ATOM   4556 C CA  . PHE B 1 187 ? 125.215 126.615 105.503 1.00 30.97  ? 174 PHE B CA  1 
ATOM   4557 C C   . PHE B 1 187 ? 124.744 128.066 105.436 1.00 35.02  ? 174 PHE B C   1 
ATOM   4558 O O   . PHE B 1 187 ? 124.644 128.671 104.368 1.00 33.41  ? 174 PHE B O   1 
ATOM   4559 C CB  . PHE B 1 187 ? 126.573 126.534 106.201 1.00 32.11  ? 174 PHE B CB  1 
ATOM   4560 C CG  . PHE B 1 187 ? 126.826 125.227 106.898 1.00 27.44  ? 174 PHE B CG  1 
ATOM   4561 C CD1 . PHE B 1 187 ? 125.785 124.507 107.455 1.00 31.22  ? 174 PHE B CD1 1 
ATOM   4562 C CD2 . PHE B 1 187 ? 128.109 124.723 107.001 1.00 26.56  ? 174 PHE B CD2 1 
ATOM   4563 C CE1 . PHE B 1 187 ? 126.020 123.309 108.099 1.00 31.19  ? 174 PHE B CE1 1 
ATOM   4564 C CE2 . PHE B 1 187 ? 128.350 123.526 107.644 1.00 29.81  ? 174 PHE B CE2 1 
ATOM   4565 C CZ  . PHE B 1 187 ? 127.304 122.818 108.192 1.00 33.16  ? 174 PHE B CZ  1 
ATOM   4566 N N   . GLY B 1 188 ? 124.454 128.622 106.612 1.00 39.41  ? 175 GLY B N   1 
ATOM   4567 C CA  . GLY B 1 188 ? 124.046 130.008 106.748 1.00 34.40  ? 175 GLY B CA  1 
ATOM   4568 C C   . GLY B 1 188 ? 124.318 130.484 108.157 1.00 38.48  ? 175 GLY B C   1 
ATOM   4569 O O   . GLY B 1 188 ? 124.713 129.709 109.031 1.00 43.60  ? 175 GLY B O   1 
ATOM   4570 N N   . LYS B 1 189 ? 124.096 131.782 108.368 1.00 38.68  ? 176 LYS B N   1 
ATOM   4571 C CA  . LYS B 1 189 ? 124.360 132.422 109.654 1.00 41.60  ? 176 LYS B CA  1 
ATOM   4572 C C   . LYS B 1 189 ? 125.775 132.133 110.135 1.00 41.33  ? 176 LYS B C   1 
ATOM   4573 O O   . LYS B 1 189 ? 126.751 132.635 109.569 1.00 42.53  ? 176 LYS B O   1 
ATOM   4574 C CB  . LYS B 1 189 ? 123.360 131.957 110.715 1.00 38.87  ? 176 LYS B CB  1 
ATOM   4575 C CG  . LYS B 1 189 ? 121.975 132.556 110.612 1.00 43.37  ? 176 LYS B CG  1 
ATOM   4576 C CD  . LYS B 1 189 ? 121.111 132.061 111.757 1.00 43.24  ? 176 LYS B CD  1 
ATOM   4577 C CE  . LYS B 1 189 ? 119.736 132.694 111.734 1.00 50.52  ? 176 LYS B CE  1 
ATOM   4578 N NZ  . LYS B 1 189 ? 119.809 134.178 111.812 1.00 55.11  ? 176 LYS B NZ  1 
ATOM   4579 N N   . ASP B 1 190 ? 125.886 131.323 111.184 1.00 44.00  ? 177 ASP B N   1 
ATOM   4580 C CA  . ASP B 1 190 ? 127.170 130.871 111.703 1.00 43.63  ? 177 ASP B CA  1 
ATOM   4581 C C   . ASP B 1 190 ? 126.944 129.538 112.394 1.00 46.44  ? 177 ASP B C   1 
ATOM   4582 O O   . ASP B 1 190 ? 126.069 129.427 113.257 1.00 49.00  ? 177 ASP B O   1 
ATOM   4583 C CB  . ASP B 1 190 ? 127.772 131.888 112.679 1.00 40.64  ? 177 ASP B CB  1 
ATOM   4584 C CG  . ASP B 1 190 ? 128.506 133.007 111.971 1.00 47.08  ? 177 ASP B CG  1 
ATOM   4585 O OD1 . ASP B 1 190 ? 129.279 132.712 111.034 1.00 43.58  ? 177 ASP B OD1 1 
ATOM   4586 O OD2 . ASP B 1 190 ? 128.307 134.181 112.342 1.00 58.73  ? 177 ASP B OD2 1 
ATOM   4587 N N   . VAL B 1 191 ? 127.729 128.533 112.021 1.00 43.51  ? 178 VAL B N   1 
ATOM   4588 C CA  . VAL B 1 191 ? 127.533 127.173 112.505 1.00 38.08  ? 178 VAL B CA  1 
ATOM   4589 C C   . VAL B 1 191 ? 128.713 126.777 113.379 1.00 35.90  ? 178 VAL B C   1 
ATOM   4590 O O   . VAL B 1 191 ? 129.874 126.995 113.017 1.00 37.58  ? 178 VAL B O   1 
ATOM   4591 C CB  . VAL B 1 191 ? 127.348 126.177 111.343 1.00 38.04  ? 178 VAL B CB  1 
ATOM   4592 C CG1 . VAL B 1 191 ? 125.993 126.380 110.695 1.00 38.53  ? 178 VAL B CG1 1 
ATOM   4593 C CG2 . VAL B 1 191 ? 128.445 126.353 110.319 1.00 37.82  ? 178 VAL B CG2 1 
ATOM   4594 N N   . TRP B 1 192 ? 128.407 126.200 114.530 1.00 35.36  ? 179 TRP B N   1 
ATOM   4595 C CA  . TRP B 1 192 ? 129.380 125.755 115.513 1.00 34.12  ? 179 TRP B CA  1 
ATOM   4596 C C   . TRP B 1 192 ? 129.057 124.320 115.891 1.00 37.45  ? 179 TRP B C   1 
ATOM   4597 O O   . TRP B 1 192 ? 127.938 123.851 115.661 1.00 44.33  ? 179 TRP B O   1 
ATOM   4598 C CB  . TRP B 1 192 ? 129.355 126.646 116.764 1.00 34.33  ? 179 TRP B CB  1 
ATOM   4599 C CG  . TRP B 1 192 ? 129.586 128.094 116.483 1.00 33.80  ? 179 TRP B CG  1 
ATOM   4600 C CD1 . TRP B 1 192 ? 128.657 129.092 116.504 1.00 34.88  ? 179 TRP B CD1 1 
ATOM   4601 C CD2 . TRP B 1 192 ? 130.829 128.709 116.138 1.00 29.89  ? 179 TRP B CD2 1 
ATOM   4602 N NE1 . TRP B 1 192 ? 129.247 130.292 116.194 1.00 35.46  ? 179 TRP B NE1 1 
ATOM   4603 C CE2 . TRP B 1 192 ? 130.581 130.083 115.963 1.00 32.51  ? 179 TRP B CE2 1 
ATOM   4604 C CE3 . TRP B 1 192 ? 132.128 128.231 115.958 1.00 27.41  ? 179 TRP B CE3 1 
ATOM   4605 C CZ2 . TRP B 1 192 ? 131.584 130.980 115.618 1.00 33.50  ? 179 TRP B CZ2 1 
ATOM   4606 C CZ3 . TRP B 1 192 ? 133.119 129.121 115.616 1.00 25.74  ? 179 TRP B CZ3 1 
ATOM   4607 C CH2 . TRP B 1 192 ? 132.844 130.480 115.450 1.00 30.02  ? 179 TRP B CH2 1 
ATOM   4608 N N   . PRO B 1 193 ? 130.019 123.586 116.458 1.00 31.99  ? 180 PRO B N   1 
ATOM   4609 C CA  . PRO B 1 193 ? 129.723 122.208 116.880 1.00 28.86  ? 180 PRO B CA  1 
ATOM   4610 C C   . PRO B 1 193 ? 128.590 122.115 117.883 1.00 34.40  ? 180 PRO B C   1 
ATOM   4611 O O   . PRO B 1 193 ? 128.002 121.036 118.034 1.00 40.19  ? 180 PRO B O   1 
ATOM   4612 C CB  . PRO B 1 193 ? 131.050 121.736 117.486 1.00 29.24  ? 180 PRO B CB  1 
ATOM   4613 C CG  . PRO B 1 193 ? 132.078 122.542 116.787 1.00 26.70  ? 180 PRO B CG  1 
ATOM   4614 C CD  . PRO B 1 193 ? 131.455 123.893 116.563 1.00 31.63  ? 180 PRO B CD  1 
ATOM   4615 N N   . ASP B 1 194 ? 128.270 123.210 118.577 1.00 36.33  ? 181 ASP B N   1 
ATOM   4616 C CA  . ASP B 1 194 ? 127.150 123.209 119.512 1.00 40.97  ? 181 ASP B CA  1 
ATOM   4617 C C   . ASP B 1 194 ? 125.813 123.032 118.798 1.00 44.90  ? 181 ASP B C   1 
ATOM   4618 O O   . ASP B 1 194 ? 124.869 122.485 119.377 1.00 49.49  ? 181 ASP B O   1 
ATOM   4619 C CB  . ASP B 1 194 ? 127.159 124.502 120.331 1.00 43.28  ? 181 ASP B CB  1 
ATOM   4620 C CG  . ASP B 1 194 ? 126.241 124.436 121.534 1.00 49.49  ? 181 ASP B CG  1 
ATOM   4621 O OD1 . ASP B 1 194 ? 125.886 123.314 121.938 1.00 48.76  ? 181 ASP B OD1 1 
ATOM   4622 O OD2 . ASP B 1 194 ? 125.864 125.500 122.071 1.00 53.78  ? 181 ASP B OD2 1 
ATOM   4623 N N   . ASP B 1 195 ? 125.708 123.494 117.548 1.00 41.93  ? 182 ASP B N   1 
ATOM   4624 C CA  . ASP B 1 195 ? 124.470 123.356 116.786 1.00 39.22  ? 182 ASP B CA  1 
ATOM   4625 C C   . ASP B 1 195 ? 124.169 121.910 116.410 1.00 42.43  ? 182 ASP B C   1 
ATOM   4626 O O   . ASP B 1 195 ? 123.043 121.612 115.999 1.00 47.35  ? 182 ASP B O   1 
ATOM   4627 C CB  . ASP B 1 195 ? 124.539 124.218 115.527 1.00 36.28  ? 182 ASP B CB  1 
ATOM   4628 C CG  . ASP B 1 195 ? 124.818 125.672 115.835 1.00 43.24  ? 182 ASP B CG  1 
ATOM   4629 O OD1 . ASP B 1 195 ? 124.213 126.202 116.788 1.00 45.86  ? 182 ASP B OD1 1 
ATOM   4630 O OD2 . ASP B 1 195 ? 125.647 126.283 115.128 1.00 47.95  ? 182 ASP B OD2 1 
ATOM   4631 N N   . PHE B 1 196 ? 125.146 121.014 116.531 1.00 43.07  ? 183 PHE B N   1 
ATOM   4632 C CA  . PHE B 1 196 ? 124.970 119.596 116.246 1.00 43.66  ? 183 PHE B CA  1 
ATOM   4633 C C   . PHE B 1 196 ? 125.056 118.730 117.493 1.00 45.05  ? 183 PHE B C   1 
ATOM   4634 O O   . PHE B 1 196 ? 124.234 117.827 117.680 1.00 51.84  ? 183 PHE B O   1 
ATOM   4635 C CB  . PHE B 1 196 ? 126.022 119.132 115.230 1.00 41.56  ? 183 PHE B CB  1 
ATOM   4636 C CG  . PHE B 1 196 ? 126.085 119.973 113.988 1.00 41.02  ? 183 PHE B CG  1 
ATOM   4637 C CD1 . PHE B 1 196 ? 124.947 120.222 113.243 1.00 43.68  ? 183 PHE B CD1 1 
ATOM   4638 C CD2 . PHE B 1 196 ? 127.285 120.520 113.569 1.00 38.94  ? 183 PHE B CD2 1 
ATOM   4639 C CE1 . PHE B 1 196 ? 125.007 120.995 112.102 1.00 45.67  ? 183 PHE B CE1 1 
ATOM   4640 C CE2 . PHE B 1 196 ? 127.351 121.294 112.430 1.00 40.07  ? 183 PHE B CE2 1 
ATOM   4641 C CZ  . PHE B 1 196 ? 126.210 121.532 111.696 1.00 43.08  ? 183 PHE B CZ  1 
ATOM   4642 N N   . TYR B 1 197 ? 126.041 118.979 118.354 1.00 39.20  ? 184 TYR B N   1 
ATOM   4643 C CA  . TYR B 1 197 ? 126.290 118.153 119.526 1.00 40.50  ? 184 TYR B CA  1 
ATOM   4644 C C   . TYR B 1 197 ? 126.572 119.019 120.743 1.00 45.83  ? 184 TYR B C   1 
ATOM   4645 O O   . TYR B 1 197 ? 127.264 120.037 120.650 1.00 51.09  ? 184 TYR B O   1 
ATOM   4646 C CB  . TYR B 1 197 ? 127.467 117.206 119.290 1.00 43.11  ? 184 TYR B CB  1 
ATOM   4647 C CG  . TYR B 1 197 ? 127.788 116.322 120.472 1.00 48.19  ? 184 TYR B CG  1 
ATOM   4648 C CD1 . TYR B 1 197 ? 127.036 115.188 120.738 1.00 45.61  ? 184 TYR B CD1 1 
ATOM   4649 C CD2 . TYR B 1 197 ? 128.846 116.619 121.318 1.00 46.79  ? 184 TYR B CD2 1 
ATOM   4650 C CE1 . TYR B 1 197 ? 127.326 114.374 121.813 1.00 44.97  ? 184 TYR B CE1 1 
ATOM   4651 C CE2 . TYR B 1 197 ? 129.145 115.810 122.396 1.00 47.41  ? 184 TYR B CE2 1 
ATOM   4652 C CZ  . TYR B 1 197 ? 128.381 114.688 122.640 1.00 50.06  ? 184 TYR B CZ  1 
ATOM   4653 O OH  . TYR B 1 197 ? 128.670 113.876 123.713 1.00 60.48  ? 184 TYR B OH  1 
ATOM   4654 N N   . SER B 1 198 ? 126.032 118.602 121.885 1.00 47.25  ? 185 SER B N   1 
ATOM   4655 C CA  . SER B 1 198 ? 126.319 119.219 123.171 1.00 45.97  ? 185 SER B CA  1 
ATOM   4656 C C   . SER B 1 198 ? 126.549 118.118 124.194 1.00 52.30  ? 185 SER B C   1 
ATOM   4657 O O   . SER B 1 198 ? 125.805 117.136 124.234 1.00 54.50  ? 185 SER B O   1 
ATOM   4658 C CB  . SER B 1 198 ? 125.180 120.134 123.626 1.00 44.60  ? 185 SER B CB  1 
ATOM   4659 O OG  . SER B 1 198 ? 125.473 120.713 124.884 1.00 50.19  ? 185 SER B OG  1 
ATOM   4660 N N   . HIS B 1 199 ? 127.583 118.288 125.021 1.00 51.38  ? 186 HIS B N   1 
ATOM   4661 C CA  . HIS B 1 199 ? 127.970 117.229 125.949 1.00 48.22  ? 186 HIS B CA  1 
ATOM   4662 C C   . HIS B 1 199 ? 126.857 116.913 126.939 1.00 49.96  ? 186 HIS B C   1 
ATOM   4663 O O   . HIS B 1 199 ? 126.581 115.741 127.219 1.00 51.56  ? 186 HIS B O   1 
ATOM   4664 C CB  . HIS B 1 199 ? 129.244 117.625 126.693 1.00 45.12  ? 186 HIS B CB  1 
ATOM   4665 C CG  . HIS B 1 199 ? 130.481 117.559 125.854 1.00 48.63  ? 186 HIS B CG  1 
ATOM   4666 N ND1 . HIS B 1 199 ? 131.266 116.430 125.778 1.00 47.32  ? 186 HIS B ND1 1 
ATOM   4667 C CD2 . HIS B 1 199 ? 131.074 118.484 125.064 1.00 53.61  ? 186 HIS B CD2 1 
ATOM   4668 C CE1 . HIS B 1 199 ? 132.289 116.660 124.974 1.00 50.55  ? 186 HIS B CE1 1 
ATOM   4669 N NE2 . HIS B 1 199 ? 132.196 117.900 124.527 1.00 55.19  ? 186 HIS B NE2 1 
ATOM   4670 N N   . SER B 1 200 ? 126.205 117.942 127.479 1.00 53.74  ? 187 SER B N   1 
ATOM   4671 C CA  . SER B 1 200 ? 125.207 117.711 128.517 1.00 56.76  ? 187 SER B CA  1 
ATOM   4672 C C   . SER B 1 200 ? 123.924 117.116 127.954 1.00 58.19  ? 187 SER B C   1 
ATOM   4673 O O   . SER B 1 200 ? 123.172 116.467 128.691 1.00 56.88  ? 187 SER B O   1 
ATOM   4674 C CB  . SER B 1 200 ? 124.908 119.015 129.253 1.00 50.04  ? 187 SER B CB  1 
ATOM   4675 O OG  . SER B 1 200 ? 126.089 119.551 129.823 1.00 44.55  ? 187 SER B OG  1 
ATOM   4676 N N   . LYS B 1 201 ? 123.644 117.328 126.668 1.00 54.13  ? 188 LYS B N   1 
ATOM   4677 C CA  . LYS B 1 201 ? 122.406 116.849 126.062 1.00 54.32  ? 188 LYS B CA  1 
ATOM   4678 C C   . LYS B 1 201 ? 122.644 115.936 124.867 1.00 57.40  ? 188 LYS B C   1 
ATOM   4679 O O   . LYS B 1 201 ? 121.689 115.616 124.150 1.00 62.05  ? 188 LYS B O   1 
ATOM   4680 C CB  . LYS B 1 201 ? 121.519 118.027 125.642 1.00 57.84  ? 188 LYS B CB  1 
ATOM   4681 C CG  . LYS B 1 201 ? 120.655 118.599 126.756 1.00 61.31  ? 188 LYS B CG  1 
ATOM   4682 C CD  . LYS B 1 201 ? 121.478 119.404 127.747 1.00 66.59  ? 188 LYS B CD  1 
ATOM   4683 C CE  . LYS B 1 201 ? 120.613 119.971 128.856 1.00 68.83  ? 188 LYS B CE  1 
ATOM   4684 N NZ  . LYS B 1 201 ? 121.403 120.788 129.818 1.00 61.60  ? 188 LYS B NZ  1 
ATOM   4685 N N   . GLY B 1 202 ? 123.879 115.501 124.637 1.00 52.91  ? 189 GLY B N   1 
ATOM   4686 C CA  . GLY B 1 202 ? 124.127 114.622 123.516 1.00 49.68  ? 189 GLY B CA  1 
ATOM   4687 C C   . GLY B 1 202 ? 123.954 115.348 122.192 1.00 46.91  ? 189 GLY B C   1 
ATOM   4688 O O   . GLY B 1 202 ? 124.064 116.571 122.093 1.00 50.09  ? 189 GLY B O   1 
ATOM   4689 N N   . GLN B 1 203 ? 123.673 114.562 121.159 1.00 47.63  ? 190 GLN B N   1 
ATOM   4690 C CA  . GLN B 1 203 ? 123.458 115.125 119.838 1.00 48.52  ? 190 GLN B CA  1 
ATOM   4691 C C   . GLN B 1 203 ? 122.087 115.787 119.745 1.00 48.47  ? 190 GLN B C   1 
ATOM   4692 O O   . GLN B 1 203 ? 121.212 115.600 120.595 1.00 46.96  ? 190 GLN B O   1 
ATOM   4693 C CB  . GLN B 1 203 ? 123.585 114.047 118.764 1.00 47.94  ? 190 GLN B CB  1 
ATOM   4694 C CG  . GLN B 1 203 ? 124.915 113.338 118.782 1.00 51.32  ? 190 GLN B CG  1 
ATOM   4695 C CD  . GLN B 1 203 ? 125.424 113.033 117.397 1.00 47.12  ? 190 GLN B CD  1 
ATOM   4696 O OE1 . GLN B 1 203 ? 124.726 113.243 116.406 1.00 43.12  ? 190 GLN B OE1 1 
ATOM   4697 N NE2 . GLN B 1 203 ? 126.652 112.542 117.318 1.00 48.67  ? 190 GLN B NE2 1 
ATOM   4698 N N   . LYS B 1 204 ? 121.913 116.577 118.691 1.00 49.19  ? 191 LYS B N   1 
ATOM   4699 C CA  . LYS B 1 204 ? 120.641 117.210 118.371 1.00 52.75  ? 191 LYS B CA  1 
ATOM   4700 C C   . LYS B 1 204 ? 120.106 116.589 117.089 1.00 59.42  ? 191 LYS B C   1 
ATOM   4701 O O   . LYS B 1 204 ? 120.771 116.636 116.049 1.00 66.86  ? 191 LYS B O   1 
ATOM   4702 C CB  . LYS B 1 204 ? 120.804 118.722 118.205 1.00 49.59  ? 191 LYS B CB  1 
ATOM   4703 C CG  . LYS B 1 204 ? 121.355 119.427 119.427 1.00 50.38  ? 191 LYS B CG  1 
ATOM   4704 C CD  . LYS B 1 204 ? 121.591 120.903 119.158 1.00 49.88  ? 191 LYS B CD  1 
ATOM   4705 C CE  . LYS B 1 204 ? 121.837 121.649 120.459 1.00 53.26  ? 191 LYS B CE  1 
ATOM   4706 N NZ  . LYS B 1 204 ? 122.154 123.086 120.249 1.00 47.84  ? 191 LYS B NZ  1 
ATOM   4707 N N   . VAL B 1 205 ? 118.916 116.005 117.163 1.00 59.12  ? 192 VAL B N   1 
ATOM   4708 C CA  . VAL B 1 205 ? 118.271 115.405 116.002 1.00 59.98  ? 192 VAL B CA  1 
ATOM   4709 C C   . VAL B 1 205 ? 117.157 116.329 115.536 1.00 64.70  ? 192 VAL B C   1 
ATOM   4710 O O   . VAL B 1 205 ? 116.429 116.911 116.352 1.00 69.11  ? 192 VAL B O   1 
ATOM   4711 C CB  . VAL B 1 205 ? 117.741 113.990 116.312 1.00 57.48  ? 192 VAL B CB  1 
ATOM   4712 C CG1 . VAL B 1 205 ? 118.884 113.078 116.722 1.00 50.78  ? 192 VAL B CG1 1 
ATOM   4713 C CG2 . VAL B 1 205 ? 116.673 114.026 117.394 1.00 61.89  ? 192 VAL B CG2 1 
ATOM   4714 N N   . TYR B 1 206 ? 117.039 116.491 114.223 1.00 60.45  ? 193 TYR B N   1 
ATOM   4715 C CA  . TYR B 1 206 ? 116.043 117.370 113.629 1.00 61.34  ? 193 TYR B CA  1 
ATOM   4716 C C   . TYR B 1 206 ? 115.002 116.514 112.922 1.00 60.33  ? 193 TYR B C   1 
ATOM   4717 O O   . TYR B 1 206 ? 115.335 115.753 112.007 1.00 59.47  ? 193 TYR B O   1 
ATOM   4718 C CB  . TYR B 1 206 ? 116.694 118.359 112.661 1.00 63.09  ? 193 TYR B CB  1 
ATOM   4719 C CG  . TYR B 1 206 ? 117.649 119.333 113.327 1.00 64.67  ? 193 TYR B CG  1 
ATOM   4720 C CD1 . TYR B 1 206 ? 117.200 120.554 113.811 1.00 59.03  ? 193 TYR B CD1 1 
ATOM   4721 C CD2 . TYR B 1 206 ? 118.998 119.030 113.471 1.00 62.21  ? 193 TYR B CD2 1 
ATOM   4722 C CE1 . TYR B 1 206 ? 118.066 121.445 114.419 1.00 54.25  ? 193 TYR B CE1 1 
ATOM   4723 C CE2 . TYR B 1 206 ? 119.872 119.917 114.076 1.00 52.43  ? 193 TYR B CE2 1 
ATOM   4724 C CZ  . TYR B 1 206 ? 119.399 121.121 114.549 1.00 51.44  ? 193 TYR B CZ  1 
ATOM   4725 O OH  . TYR B 1 206 ? 120.259 122.007 115.153 1.00 54.72  ? 193 TYR B OH  1 
ATOM   4726 N N   . LEU B 1 207 ? 113.749 116.636 113.354 1.00 64.23  ? 194 LEU B N   1 
ATOM   4727 C CA  . LEU B 1 207 ? 112.637 115.861 112.820 1.00 68.83  ? 194 LEU B CA  1 
ATOM   4728 C C   . LEU B 1 207 ? 111.570 116.823 112.325 1.00 70.83  ? 194 LEU B C   1 
ATOM   4729 O O   . LEU B 1 207 ? 111.169 117.734 113.055 1.00 75.24  ? 194 LEU B O   1 
ATOM   4730 C CB  . LEU B 1 207 ? 112.052 114.916 113.880 1.00 72.32  ? 194 LEU B CB  1 
ATOM   4731 C CG  . LEU B 1 207 ? 112.712 113.558 114.159 1.00 69.11  ? 194 LEU B CG  1 
ATOM   4732 C CD1 . LEU B 1 207 ? 114.148 113.697 114.636 1.00 62.72  ? 194 LEU B CD1 1 
ATOM   4733 C CD2 . LEU B 1 207 ? 111.899 112.779 115.181 1.00 66.11  ? 194 LEU B CD2 1 
ATOM   4734 N N   . THR B 1 208 ? 111.105 116.617 111.093 1.00 69.38  ? 195 THR B N   1 
ATOM   4735 C CA  . THR B 1 208 ? 110.176 117.551 110.464 1.00 75.62  ? 195 THR B CA  1 
ATOM   4736 C C   . THR B 1 208 ? 108.717 117.160 110.690 1.00 77.19  ? 195 THR B C   1 
ATOM   4737 O O   . THR B 1 208 ? 107.952 117.917 111.295 1.00 75.10  ? 195 THR B O   1 
ATOM   4738 C CB  . THR B 1 208 ? 110.469 117.643 108.964 1.00 74.66  ? 195 THR B CB  1 
ATOM   4739 O OG1 . THR B 1 208 ? 110.484 116.325 108.402 1.00 72.26  ? 195 THR B OG1 1 
ATOM   4740 C CG2 . THR B 1 208 ? 111.810 118.306 108.726 1.00 74.76  ? 195 THR B CG2 1 
ATOM   4741 N N   . TRP B 1 209 ? 108.319 115.978 110.212 1.00 78.70  ? 196 TRP B N   1 
ATOM   4742 C CA  . TRP B 1 209 ? 106.927 115.559 110.303 1.00 79.98  ? 196 TRP B CA  1 
ATOM   4743 C C   . TRP B 1 209 ? 106.862 114.043 110.263 1.00 80.99  ? 196 TRP B C   1 
ATOM   4744 O O   . TRP B 1 209 ? 107.662 113.422 109.550 1.00 77.45  ? 196 TRP B O   1 
ATOM   4745 C CB  . TRP B 1 209 ? 106.082 116.163 109.174 1.00 77.12  ? 196 TRP B CB  1 
ATOM   4746 C CG  . TRP B 1 209 ? 106.631 115.944 107.797 1.00 78.14  ? 196 TRP B CG  1 
ATOM   4747 C CD1 . TRP B 1 209 ? 107.682 116.595 107.224 1.00 78.39  ? 196 TRP B CD1 1 
ATOM   4748 C CD2 . TRP B 1 209 ? 106.138 115.031 106.809 1.00 80.49  ? 196 TRP B CD2 1 
ATOM   4749 N NE1 . TRP B 1 209 ? 107.887 116.134 105.946 1.00 79.30  ? 196 TRP B NE1 1 
ATOM   4750 C CE2 . TRP B 1 209 ? 106.950 115.174 105.667 1.00 80.53  ? 196 TRP B CE2 1 
ATOM   4751 C CE3 . TRP B 1 209 ? 105.092 114.104 106.782 1.00 79.94  ? 196 TRP B CE3 1 
ATOM   4752 C CZ2 . TRP B 1 209 ? 106.750 114.423 104.510 1.00 78.71  ? 196 TRP B CZ2 1 
ATOM   4753 C CZ3 . TRP B 1 209 ? 104.896 113.359 105.633 1.00 79.48  ? 196 TRP B CZ3 1 
ATOM   4754 C CH2 . TRP B 1 209 ? 105.721 113.523 104.513 1.00 79.14  ? 196 TRP B CH2 1 
ATOM   4755 N N   . PRO B 1 210 ? 105.946 113.421 111.003 1.00 82.17  ? 197 PRO B N   1 
ATOM   4756 C CA  . PRO B 1 210 ? 105.936 111.956 111.090 1.00 77.83  ? 197 PRO B CA  1 
ATOM   4757 C C   . PRO B 1 210 ? 105.605 111.304 109.759 1.00 76.59  ? 197 PRO B C   1 
ATOM   4758 O O   . PRO B 1 210 ? 104.912 111.873 108.913 1.00 79.89  ? 197 PRO B O   1 
ATOM   4759 C CB  . PRO B 1 210 ? 104.845 111.669 112.130 1.00 80.16  ? 197 PRO B CB  1 
ATOM   4760 C CG  . PRO B 1 210 ? 104.626 112.971 112.848 1.00 79.96  ? 197 PRO B CG  1 
ATOM   4761 C CD  . PRO B 1 210 ? 104.897 114.032 111.834 1.00 80.68  ? 197 PRO B CD  1 
ATOM   4762 N N   . VAL B 1 211 ? 106.122 110.091 109.579 1.00 77.10  ? 198 VAL B N   1 
ATOM   4763 C CA  . VAL B 1 211 ? 105.767 109.311 108.389 1.00 85.31  ? 198 VAL B CA  1 
ATOM   4764 C C   . VAL B 1 211 ? 104.270 109.030 108.408 1.00 94.39  ? 198 VAL B C   1 
ATOM   4765 O O   . VAL B 1 211 ? 103.708 108.739 109.484 1.00 94.72  ? 198 VAL B O   1 
ATOM   4766 C CB  . VAL B 1 211 ? 106.577 108.004 108.329 1.00 82.57  ? 198 VAL B CB  1 
ATOM   4767 C CG1 . VAL B 1 211 ? 108.012 108.288 107.907 1.00 75.69  ? 198 VAL B CG1 1 
ATOM   4768 C CG2 . VAL B 1 211 ? 106.555 107.298 109.674 1.00 84.87  ? 198 VAL B CG2 1 
ATOM   4769 N N   . PRO B 1 212 ? 103.571 109.113 107.273 1.00 98.01  ? 199 PRO B N   1 
ATOM   4770 C CA  . PRO B 1 212 ? 102.105 108.981 107.318 1.00 100.60 ? 199 PRO B CA  1 
ATOM   4771 C C   . PRO B 1 212 ? 101.629 107.566 107.594 1.00 105.56 ? 199 PRO B C   1 
ATOM   4772 O O   . PRO B 1 212 ? 100.588 107.388 108.240 1.00 110.60 ? 199 PRO B O   1 
ATOM   4773 C CB  . PRO B 1 212 ? 101.676 109.466 105.928 1.00 97.20  ? 199 PRO B CB  1 
ATOM   4774 C CG  . PRO B 1 212 ? 102.838 109.120 105.052 1.00 93.80  ? 199 PRO B CG  1 
ATOM   4775 C CD  . PRO B 1 212 ? 104.071 109.304 105.900 1.00 93.55  ? 199 PRO B CD  1 
ATOM   4776 N N   . ASN B 1 213 ? 102.353 106.556 107.111 1.00 103.85 ? 200 ASN B N   1 
ATOM   4777 C CA  . ASN B 1 213 ? 101.992 105.144 107.220 1.00 107.00 ? 200 ASN B CA  1 
ATOM   4778 C C   . ASN B 1 213 ? 100.673 104.819 106.527 1.00 113.98 ? 200 ASN B C   1 
ATOM   4779 O O   . ASN B 1 213 ? 100.137 103.719 106.712 1.00 119.34 ? 200 ASN B O   1 
ATOM   4780 C CB  . ASN B 1 213 ? 101.935 104.681 108.684 1.00 104.34 ? 200 ASN B CB  1 
ATOM   4781 C CG  . ASN B 1 213 ? 103.271 104.808 109.391 1.00 99.45  ? 200 ASN B CG  1 
ATOM   4782 O OD1 . ASN B 1 213 ? 103.577 105.841 109.983 1.00 97.26  ? 200 ASN B OD1 1 
ATOM   4783 N ND2 . ASN B 1 213 ? 104.072 103.749 109.338 1.00 98.30  ? 200 ASN B ND2 1 
ATOM   4784 N N   . GLY B 1 214 ? 100.132 105.749 105.738 1.00 113.21 ? 201 GLY B N   1 
ATOM   4785 C CA  . GLY B 1 214 ? 98.893  105.478 105.029 1.00 120.64 ? 201 GLY B CA  1 
ATOM   4786 C C   . GLY B 1 214 ? 99.046  104.410 103.962 1.00 131.51 ? 201 GLY B C   1 
ATOM   4787 O O   . GLY B 1 214 ? 98.125  103.625 103.720 1.00 138.86 ? 201 GLY B O   1 
ATOM   4788 N N   . GLY B 1 215 ? 100.205 104.368 103.307 1.00 126.94 ? 202 GLY B N   1 
ATOM   4789 C CA  . GLY B 1 215 ? 100.431 103.402 102.253 1.00 127.27 ? 202 GLY B CA  1 
ATOM   4790 C C   . GLY B 1 215 ? 99.617  103.722 101.007 1.00 137.96 ? 202 GLY B C   1 
ATOM   4791 O O   . GLY B 1 215 ? 99.147  104.845 100.800 1.00 142.01 ? 202 GLY B O   1 
ATOM   4792 N N   . SER B 1 216 ? 99.454  102.695 100.170 1.00 141.60 ? 203 SER B N   1 
ATOM   4793 C CA  . SER B 1 216 ? 98.712  102.800 98.914  1.00 143.18 ? 203 SER B CA  1 
ATOM   4794 C C   . SER B 1 216 ? 99.269  103.905 98.019  1.00 146.01 ? 203 SER B C   1 
ATOM   4795 O O   . SER B 1 216 ? 98.524  104.583 97.308  1.00 147.50 ? 203 SER B O   1 
ATOM   4796 C CB  . SER B 1 216 ? 97.217  103.016 99.168  1.00 142.22 ? 203 SER B CB  1 
ATOM   4797 O OG  . SER B 1 216 ? 96.683  101.978 99.973  1.00 142.59 ? 203 SER B OG  1 
ATOM   4798 N N   . GLY B 1 217 ? 100.583 104.088 98.049  1.00 145.32 ? 204 GLY B N   1 
ATOM   4799 C CA  . GLY B 1 217 ? 101.210 105.127 97.258  1.00 141.71 ? 204 GLY B CA  1 
ATOM   4800 C C   . GLY B 1 217 ? 102.699 105.168 97.518  1.00 139.23 ? 204 GLY B C   1 
ATOM   4801 O O   . GLY B 1 217 ? 103.254 104.304 98.199  1.00 136.23 ? 204 GLY B O   1 
ATOM   4802 N N   . GLY B 1 218 ? 103.341 106.193 96.962  1.00 138.11 ? 205 GLY B N   1 
ATOM   4803 C CA  . GLY B 1 218 ? 104.779 106.342 97.089  1.00 131.79 ? 205 GLY B CA  1 
ATOM   4804 C C   . GLY B 1 218 ? 105.536 105.588 96.017  1.00 128.92 ? 205 GLY B C   1 
ATOM   4805 O O   . GLY B 1 218 ? 105.230 104.426 95.736  1.00 128.06 ? 205 GLY B O   1 
ATOM   4806 N N   . ASP B 1 219 ? 106.528 106.235 95.407  1.00 126.92 ? 206 ASP B N   1 
ATOM   4807 C CA  . ASP B 1 219 ? 107.273 105.616 94.314  1.00 122.03 ? 206 ASP B CA  1 
ATOM   4808 C C   . ASP B 1 219 ? 108.556 104.945 94.802  1.00 114.47 ? 206 ASP B C   1 
ATOM   4809 O O   . ASP B 1 219 ? 108.719 103.729 94.658  1.00 110.93 ? 206 ASP B O   1 
ATOM   4810 C CB  . ASP B 1 219 ? 107.574 106.662 93.233  1.00 121.46 ? 206 ASP B CB  1 
ATOM   4811 C CG  . ASP B 1 219 ? 108.006 107.997 93.814  1.00 122.50 ? 206 ASP B CG  1 
ATOM   4812 O OD1 . ASP B 1 219 ? 108.360 108.045 95.010  1.00 120.25 ? 206 ASP B OD1 1 
ATOM   4813 O OD2 . ASP B 1 219 ? 107.983 109.001 93.070  1.00 121.44 ? 206 ASP B OD2 1 
ATOM   4814 N N   . THR B 1 220 ? 109.478 105.724 95.370  1.00 109.17 ? 207 THR B N   1 
ATOM   4815 C CA  . THR B 1 220 ? 110.729 105.168 95.865  1.00 101.60 ? 207 THR B CA  1 
ATOM   4816 C C   . THR B 1 220 ? 111.180 105.751 97.196  1.00 98.37  ? 207 THR B C   1 
ATOM   4817 O O   . THR B 1 220 ? 112.244 105.362 97.687  1.00 95.60  ? 207 THR B O   1 
ATOM   4818 C CB  . THR B 1 220 ? 111.848 105.359 94.828  1.00 96.99  ? 207 THR B CB  1 
ATOM   4819 O OG1 . THR B 1 220 ? 112.014 106.755 94.552  1.00 103.13 ? 207 THR B OG1 1 
ATOM   4820 C CG2 . THR B 1 220 ? 111.495 104.642 93.535  1.00 92.57  ? 207 THR B CG2 1 
ATOM   4821 N N   . PHE B 1 221 ? 110.429 106.679 97.785  1.00 100.72 ? 208 PHE B N   1 
ATOM   4822 C CA  . PHE B 1 221 ? 110.816 107.313 99.040  1.00 96.90  ? 208 PHE B CA  1 
ATOM   4823 C C   . PHE B 1 221 ? 110.088 106.732 100.245 1.00 96.65  ? 208 PHE B C   1 
ATOM   4824 O O   . PHE B 1 221 ? 110.729 106.326 101.218 1.00 93.28  ? 208 PHE B O   1 
ATOM   4825 C CB  . PHE B 1 221 ? 110.574 108.826 98.959  1.00 95.68  ? 208 PHE B CB  1 
ATOM   4826 C CG  . PHE B 1 221 ? 111.278 109.610 100.029 1.00 98.02  ? 208 PHE B CG  1 
ATOM   4827 C CD1 . PHE B 1 221 ? 112.660 109.624 100.096 1.00 99.03  ? 208 PHE B CD1 1 
ATOM   4828 C CD2 . PHE B 1 221 ? 110.558 110.339 100.962 1.00 96.67  ? 208 PHE B CD2 1 
ATOM   4829 C CE1 . PHE B 1 221 ? 113.317 110.344 101.078 1.00 94.50  ? 208 PHE B CE1 1 
ATOM   4830 C CE2 . PHE B 1 221 ? 111.210 111.062 101.946 1.00 94.80  ? 208 PHE B CE2 1 
ATOM   4831 C CZ  . PHE B 1 221 ? 112.591 111.064 102.003 1.00 91.34  ? 208 PHE B CZ  1 
ATOM   4832 N N   . ALA B 1 222 ? 108.755 106.679 100.199 1.00 100.20 ? 209 ALA B N   1 
ATOM   4833 C CA  . ALA B 1 222 ? 107.996 106.163 101.333 1.00 97.19  ? 209 ALA B CA  1 
ATOM   4834 C C   . ALA B 1 222 ? 108.248 104.677 101.561 1.00 94.17  ? 209 ALA B C   1 
ATOM   4835 O O   . ALA B 1 222 ? 108.152 104.205 102.700 1.00 91.00  ? 209 ALA B O   1 
ATOM   4836 C CB  . ALA B 1 222 ? 106.504 106.424 101.129 1.00 98.94  ? 209 ALA B CB  1 
ATOM   4837 N N   . ASP B 1 223 ? 108.561 103.924 100.503 1.00 95.22  ? 210 ASP B N   1 
ATOM   4838 C CA  . ASP B 1 223 ? 108.767 102.487 100.660 1.00 93.46  ? 210 ASP B CA  1 
ATOM   4839 C C   . ASP B 1 223 ? 109.988 102.186 101.523 1.00 90.43  ? 210 ASP B C   1 
ATOM   4840 O O   . ASP B 1 223 ? 109.946 101.296 102.380 1.00 88.30  ? 210 ASP B O   1 
ATOM   4841 C CB  . ASP B 1 223 ? 108.889 101.815 99.291  1.00 93.39  ? 210 ASP B CB  1 
ATOM   4842 C CG  . ASP B 1 223 ? 109.987 102.417 98.430  1.00 95.68  ? 210 ASP B CG  1 
ATOM   4843 O OD1 . ASP B 1 223 ? 110.778 103.238 98.938  1.00 92.73  ? 210 ASP B OD1 1 
ATOM   4844 O OD2 . ASP B 1 223 ? 110.053 102.066 97.233  1.00 98.88  ? 210 ASP B OD2 1 
ATOM   4845 N N   . SER B 1 224 ? 111.086 102.916 101.313 1.00 88.20  ? 211 SER B N   1 
ATOM   4846 C CA  . SER B 1 224 ? 112.273 102.717 102.140 1.00 88.50  ? 211 SER B CA  1 
ATOM   4847 C C   . SER B 1 224 ? 112.007 103.113 103.587 1.00 84.05  ? 211 SER B C   1 
ATOM   4848 O O   . SER B 1 224 ? 112.499 102.462 104.520 1.00 77.24  ? 211 SER B O   1 
ATOM   4849 C CB  . SER B 1 224 ? 113.445 103.513 101.572 1.00 84.90  ? 211 SER B CB  1 
ATOM   4850 O OG  . SER B 1 224 ? 114.642 103.218 102.272 1.00 77.27  ? 211 SER B OG  1 
ATOM   4851 N N   . LEU B 1 225 ? 111.244 104.190 103.791 1.00 83.93  ? 212 LEU B N   1 
ATOM   4852 C CA  . LEU B 1 225 ? 110.870 104.585 105.143 1.00 79.29  ? 212 LEU B CA  1 
ATOM   4853 C C   . LEU B 1 225 ? 110.061 103.493 105.825 1.00 80.68  ? 212 LEU B C   1 
ATOM   4854 O O   . LEU B 1 225 ? 110.299 103.178 106.994 1.00 81.17  ? 212 LEU B O   1 
ATOM   4855 C CB  . LEU B 1 225 ? 110.081 105.893 105.115 1.00 80.97  ? 212 LEU B CB  1 
ATOM   4856 C CG  . LEU B 1 225 ? 110.877 107.191 105.261 1.00 77.64  ? 212 LEU B CG  1 
ATOM   4857 C CD1 . LEU B 1 225 ? 111.720 107.155 106.524 1.00 72.05  ? 212 LEU B CD1 1 
ATOM   4858 C CD2 . LEU B 1 225 ? 111.741 107.450 104.042 1.00 80.47  ? 212 LEU B CD2 1 
ATOM   4859 N N   . ARG B 1 226 ? 109.109 102.892 105.106 1.00 80.32  ? 213 ARG B N   1 
ATOM   4860 C CA  . ARG B 1 226 ? 108.333 101.797 105.682 1.00 78.42  ? 213 ARG B CA  1 
ATOM   4861 C C   . ARG B 1 226 ? 109.207 100.578 105.947 1.00 74.73  ? 213 ARG B C   1 
ATOM   4862 O O   . ARG B 1 226 ? 108.990 99.855  106.924 1.00 72.97  ? 213 ARG B O   1 
ATOM   4863 C CB  . ARG B 1 226 ? 107.171 101.427 104.761 1.00 85.03  ? 213 ARG B CB  1 
ATOM   4864 C CG  . ARG B 1 226 ? 106.176 102.547 104.530 1.00 88.71  ? 213 ARG B CG  1 
ATOM   4865 C CD  . ARG B 1 226 ? 104.933 102.029 103.832 1.00 94.90  ? 213 ARG B CD  1 
ATOM   4866 N NE  . ARG B 1 226 ? 104.232 103.088 103.119 1.00 100.00 ? 213 ARG B NE  1 
ATOM   4867 C CZ  . ARG B 1 226 ? 104.402 103.362 101.833 1.00 102.85 ? 213 ARG B CZ  1 
ATOM   4868 N NH1 . ARG B 1 226 ? 105.241 102.665 101.083 1.00 98.50  ? 213 ARG B NH1 1 
ATOM   4869 N NH2 . ARG B 1 226 ? 103.709 104.355 101.284 1.00 110.61 ? 213 ARG B NH2 1 
ATOM   4870 N N   . TYR B 1 227 ? 110.195 100.330 105.087 1.00 71.71  ? 214 TYR B N   1 
ATOM   4871 C CA  . TYR B 1 227 ? 111.093 99.198  105.292 1.00 71.86  ? 214 TYR B CA  1 
ATOM   4872 C C   . TYR B 1 227 ? 111.894 99.359  106.578 1.00 71.36  ? 214 TYR B C   1 
ATOM   4873 O O   . TYR B 1 227 ? 111.931 98.453  107.424 1.00 71.77  ? 214 TYR B O   1 
ATOM   4874 C CB  . TYR B 1 227 ? 112.023 99.061  104.087 1.00 71.90  ? 214 TYR B CB  1 
ATOM   4875 C CG  . TYR B 1 227 ? 113.126 98.045  104.259 1.00 75.25  ? 214 TYR B CG  1 
ATOM   4876 C CD1 . TYR B 1 227 ? 114.418 98.440  104.573 1.00 75.99  ? 214 TYR B CD1 1 
ATOM   4877 C CD2 . TYR B 1 227 ? 112.876 96.689  104.099 1.00 73.79  ? 214 TYR B CD2 1 
ATOM   4878 C CE1 . TYR B 1 227 ? 115.428 97.514  104.726 1.00 71.74  ? 214 TYR B CE1 1 
ATOM   4879 C CE2 . TYR B 1 227 ? 113.882 95.756  104.251 1.00 71.81  ? 214 TYR B CE2 1 
ATOM   4880 C CZ  . TYR B 1 227 ? 115.155 96.176  104.564 1.00 71.59  ? 214 TYR B CZ  1 
ATOM   4881 O OH  . TYR B 1 227 ? 116.161 95.253  104.716 1.00 73.43  ? 214 TYR B OH  1 
ATOM   4882 N N   . VAL B 1 228 ? 112.527 100.519 106.752 1.00 69.72  ? 215 VAL B N   1 
ATOM   4883 C CA  . VAL B 1 228 ? 113.276 100.756 107.982 1.00 66.24  ? 215 VAL B CA  1 
ATOM   4884 C C   . VAL B 1 228 ? 112.335 100.798 109.179 1.00 63.46  ? 215 VAL B C   1 
ATOM   4885 O O   . VAL B 1 228 ? 112.698 100.363 110.278 1.00 62.65  ? 215 VAL B O   1 
ATOM   4886 C CB  . VAL B 1 228 ? 114.117 102.040 107.874 1.00 71.02  ? 215 VAL B CB  1 
ATOM   4887 C CG1 . VAL B 1 228 ? 114.962 102.222 109.127 1.00 62.89  ? 215 VAL B CG1 1 
ATOM   4888 C CG2 . VAL B 1 228 ? 114.999 101.993 106.635 1.00 71.43  ? 215 VAL B CG2 1 
ATOM   4889 N N   . ASN B 1 229 ? 111.116 101.309 108.991 1.00 65.19  ? 216 ASN B N   1 
ATOM   4890 C CA  . ASN B 1 229 ? 110.148 101.346 110.080 1.00 66.47  ? 216 ASN B CA  1 
ATOM   4891 C C   . ASN B 1 229 ? 109.788 99.943  110.544 1.00 72.73  ? 216 ASN B C   1 
ATOM   4892 O O   . ASN B 1 229 ? 109.709 99.685  111.748 1.00 72.45  ? 216 ASN B O   1 
ATOM   4893 C CB  . ASN B 1 229 ? 108.896 102.101 109.636 1.00 67.49  ? 216 ASN B CB  1 
ATOM   4894 C CG  . ASN B 1 229 ? 108.349 103.010 110.716 1.00 67.39  ? 216 ASN B CG  1 
ATOM   4895 O OD1 . ASN B 1 229 ? 108.657 102.846 111.896 1.00 66.14  ? 216 ASN B OD1 1 
ATOM   4896 N ND2 . ASN B 1 229 ? 107.531 103.978 110.317 1.00 72.85  ? 216 ASN B ND2 1 
ATOM   4897 N N   . LYS B 1 230 ? 109.572 99.017  109.606 1.00 71.93  ? 217 LYS B N   1 
ATOM   4898 C CA  . LYS B 1 230 ? 109.235 97.651  109.994 1.00 67.37  ? 217 LYS B CA  1 
ATOM   4899 C C   . LYS B 1 230 ? 110.431 96.947  110.624 1.00 67.04  ? 217 LYS B C   1 
ATOM   4900 O O   . LYS B 1 230 ? 110.268 96.160  111.565 1.00 65.44  ? 217 LYS B O   1 
ATOM   4901 C CB  . LYS B 1 230 ? 108.696 96.867  108.793 1.00 66.03  ? 217 LYS B CB  1 
ATOM   4902 C CG  . LYS B 1 230 ? 109.742 96.293  107.854 1.00 67.68  ? 217 LYS B CG  1 
ATOM   4903 C CD  . LYS B 1 230 ? 109.094 95.578  106.682 1.00 68.65  ? 217 LYS B CD  1 
ATOM   4904 C CE  . LYS B 1 230 ? 108.213 96.524  105.885 1.00 71.89  ? 217 LYS B CE  1 
ATOM   4905 N NZ  . LYS B 1 230 ? 107.574 95.847  104.725 1.00 65.91  ? 217 LYS B NZ  1 
ATOM   4906 N N   . ILE B 1 231 ? 111.644 97.228  110.136 1.00 67.45  ? 218 ILE B N   1 
ATOM   4907 C CA  . ILE B 1 231 ? 112.836 96.647  110.754 1.00 65.58  ? 218 ILE B CA  1 
ATOM   4908 C C   . ILE B 1 231 ? 112.964 97.115  112.201 1.00 65.22  ? 218 ILE B C   1 
ATOM   4909 O O   . ILE B 1 231 ? 113.178 96.314  113.121 1.00 64.82  ? 218 ILE B O   1 
ATOM   4910 C CB  . ILE B 1 231 ? 114.091 96.992  109.933 1.00 58.42  ? 218 ILE B CB  1 
ATOM   4911 C CG1 . ILE B 1 231 ? 114.091 96.219  108.615 1.00 64.82  ? 218 ILE B CG1 1 
ATOM   4912 C CG2 . ILE B 1 231 ? 115.348 96.686  110.726 1.00 55.55  ? 218 ILE B CG2 1 
ATOM   4913 C CD1 . ILE B 1 231 ? 114.161 94.721  108.792 1.00 67.32  ? 218 ILE B CD1 1 
ATOM   4914 N N   . LEU B 1 232 ? 112.807 98.420  112.427 1.00 62.41  ? 219 LEU B N   1 
ATOM   4915 C CA  . LEU B 1 232 ? 112.916 98.954  113.777 1.00 58.58  ? 219 LEU B CA  1 
ATOM   4916 C C   . LEU B 1 232 ? 111.729 98.571  114.651 1.00 62.46  ? 219 LEU B C   1 
ATOM   4917 O O   . LEU B 1 232 ? 111.868 98.543  115.875 1.00 66.36  ? 219 LEU B O   1 
ATOM   4918 C CB  . LEU B 1 232 ? 113.073 100.474 113.730 1.00 62.30  ? 219 LEU B CB  1 
ATOM   4919 C CG  . LEU B 1 232 ? 114.386 100.995 113.142 1.00 64.82  ? 219 LEU B CG  1 
ATOM   4920 C CD1 . LEU B 1 232 ? 114.328 102.500 112.947 1.00 64.40  ? 219 LEU B CD1 1 
ATOM   4921 C CD2 . LEU B 1 232 ? 115.562 100.616 114.031 1.00 56.87  ? 219 LEU B CD2 1 
ATOM   4922 N N   . ASN B 1 233 ? 110.570 98.275  114.060 1.00 63.72  ? 220 ASN B N   1 
ATOM   4923 C CA  . ASN B 1 233 ? 109.463 97.745  114.848 1.00 68.10  ? 220 ASN B CA  1 
ATOM   4924 C C   . ASN B 1 233 ? 109.752 96.323  115.302 1.00 70.41  ? 220 ASN B C   1 
ATOM   4925 O O   . ASN B 1 233 ? 109.481 95.963  116.454 1.00 68.93  ? 220 ASN B O   1 
ATOM   4926 C CB  . ASN B 1 233 ? 108.165 97.796  114.044 1.00 67.13  ? 220 ASN B CB  1 
ATOM   4927 C CG  . ASN B 1 233 ? 107.649 99.206  113.861 1.00 71.34  ? 220 ASN B CG  1 
ATOM   4928 O OD1 . ASN B 1 233 ? 107.867 100.074 114.705 1.00 73.67  ? 220 ASN B OD1 1 
ATOM   4929 N ND2 . ASN B 1 233 ? 106.963 99.445  112.750 1.00 75.19  ? 220 ASN B ND2 1 
ATOM   4930 N N   . SER B 1 234 ? 110.304 95.500  114.409 1.00 69.32  ? 221 SER B N   1 
ATOM   4931 C CA  . SER B 1 234 ? 110.668 94.142  114.790 1.00 65.87  ? 221 SER B CA  1 
ATOM   4932 C C   . SER B 1 234 ? 111.793 94.130  115.816 1.00 64.29  ? 221 SER B C   1 
ATOM   4933 O O   . SER B 1 234 ? 111.859 93.218  116.648 1.00 68.20  ? 221 SER B O   1 
ATOM   4934 C CB  . SER B 1 234 ? 111.066 93.337  113.553 1.00 61.98  ? 221 SER B CB  1 
ATOM   4935 O OG  . SER B 1 234 ? 110.000 93.275  112.621 1.00 61.31  ? 221 SER B OG  1 
ATOM   4936 N N   . LYS B 1 235 ? 112.680 95.126  115.782 1.00 59.38  ? 222 LYS B N   1 
ATOM   4937 C CA  . LYS B 1 235 ? 113.835 95.100  116.674 1.00 57.51  ? 222 LYS B CA  1 
ATOM   4938 C C   . LYS B 1 235 ? 113.590 95.811  118.004 1.00 60.49  ? 222 LYS B C   1 
ATOM   4939 O O   . LYS B 1 235 ? 113.836 95.236  119.068 1.00 64.60  ? 222 LYS B O   1 
ATOM   4940 C CB  . LYS B 1 235 ? 115.047 95.717  115.974 1.00 60.84  ? 222 LYS B CB  1 
ATOM   4941 C CG  . LYS B 1 235 ? 116.307 95.736  116.825 1.00 60.65  ? 222 LYS B CG  1 
ATOM   4942 C CD  . LYS B 1 235 ? 116.687 94.340  117.284 1.00 59.92  ? 222 LYS B CD  1 
ATOM   4943 C CE  . LYS B 1 235 ? 118.167 94.253  117.608 1.00 58.51  ? 222 LYS B CE  1 
ATOM   4944 N NZ  . LYS B 1 235 ? 118.596 95.319  118.552 1.00 54.06  ? 222 LYS B NZ  1 
ATOM   4945 N N   . PHE B 1 236 ? 113.113 97.056  117.968 1.00 59.31  ? 223 PHE B N   1 
ATOM   4946 C CA  . PHE B 1 236 ? 112.986 97.878  119.164 1.00 55.54  ? 223 PHE B CA  1 
ATOM   4947 C C   . PHE B 1 236 ? 111.547 98.110  119.606 1.00 64.93  ? 223 PHE B C   1 
ATOM   4948 O O   . PHE B 1 236 ? 111.335 98.577  120.730 1.00 70.75  ? 223 PHE B O   1 
ATOM   4949 C CB  . PHE B 1 236 ? 113.656 99.243  118.943 1.00 49.83  ? 223 PHE B CB  1 
ATOM   4950 C CG  . PHE B 1 236 ? 115.145 99.171  118.781 1.00 49.78  ? 223 PHE B CG  1 
ATOM   4951 C CD1 . PHE B 1 236 ? 115.896 98.270  119.515 1.00 51.15  ? 223 PHE B CD1 1 
ATOM   4952 C CD2 . PHE B 1 236 ? 115.796 100.008 117.891 1.00 48.44  ? 223 PHE B CD2 1 
ATOM   4953 C CE1 . PHE B 1 236 ? 117.270 98.206  119.366 1.00 48.78  ? 223 PHE B CE1 1 
ATOM   4954 C CE2 . PHE B 1 236 ? 117.166 99.948  117.737 1.00 49.66  ? 223 PHE B CE2 1 
ATOM   4955 C CZ  . PHE B 1 236 ? 117.904 99.046  118.475 1.00 47.80  ? 223 PHE B CZ  1 
ATOM   4956 N N   . GLY B 1 237 ? 110.564 97.810  118.768 1.00 64.69  ? 224 GLY B N   1 
ATOM   4957 C CA  . GLY B 1 237 ? 109.169 98.012  119.107 1.00 65.36  ? 224 GLY B CA  1 
ATOM   4958 C C   . GLY B 1 237 ? 108.514 99.048  118.208 1.00 68.85  ? 224 GLY B C   1 
ATOM   4959 O O   . GLY B 1 237 ? 109.141 99.647  117.332 1.00 66.33  ? 224 GLY B O   1 
ATOM   4960 N N   . PHE B 1 238 ? 107.226 99.262  118.459 1.00 75.69  ? 225 PHE B N   1 
ATOM   4961 C CA  . PHE B 1 238 ? 106.397 100.112 117.614 1.00 81.96  ? 225 PHE B CA  1 
ATOM   4962 C C   . PHE B 1 238 ? 106.201 101.477 118.260 1.00 85.49  ? 225 PHE B C   1 
ATOM   4963 O O   . PHE B 1 238 ? 105.861 101.568 119.444 1.00 88.18  ? 225 PHE B O   1 
ATOM   4964 C CB  . PHE B 1 238 ? 105.039 99.461  117.348 1.00 82.98  ? 225 PHE B CB  1 
ATOM   4965 C CG  . PHE B 1 238 ? 104.145 100.273 116.452 1.00 88.11  ? 225 PHE B CG  1 
ATOM   4966 C CD1 . PHE B 1 238 ? 104.292 100.222 115.076 1.00 88.78  ? 225 PHE B CD1 1 
ATOM   4967 C CD2 . PHE B 1 238 ? 103.158 101.085 116.986 1.00 92.14  ? 225 PHE B CD2 1 
ATOM   4968 C CE1 . PHE B 1 238 ? 103.473 100.968 114.249 1.00 92.28  ? 225 PHE B CE1 1 
ATOM   4969 C CE2 . PHE B 1 238 ? 102.336 101.833 116.164 1.00 95.34  ? 225 PHE B CE2 1 
ATOM   4970 C CZ  . PHE B 1 238 ? 102.494 101.774 114.794 1.00 96.55  ? 225 PHE B CZ  1 
ATOM   4971 N N   . THR B 1 239 ? 106.413 102.530 117.474 1.00 83.78  ? 226 THR B N   1 
ATOM   4972 C CA  . THR B 1 239 ? 106.188 103.898 117.916 1.00 83.04  ? 226 THR B CA  1 
ATOM   4973 C C   . THR B 1 239 ? 105.999 104.773 116.687 1.00 85.21  ? 226 THR B C   1 
ATOM   4974 O O   . THR B 1 239 ? 106.347 104.387 115.569 1.00 82.35  ? 226 THR B O   1 
ATOM   4975 C CB  . THR B 1 239 ? 107.348 104.417 118.774 1.00 79.50  ? 226 THR B CB  1 
ATOM   4976 O OG1 . THR B 1 239 ? 107.075 105.762 119.185 1.00 78.11  ? 226 THR B OG1 1 
ATOM   4977 C CG2 . THR B 1 239 ? 108.647 104.386 117.984 1.00 77.11  ? 226 THR B CG2 1 
ATOM   4978 N N   . SER B 1 240 ? 105.441 105.961 116.909 1.00 86.40  ? 227 SER B N   1 
ATOM   4979 C CA  . SER B 1 240 ? 105.235 106.922 115.831 1.00 85.29  ? 227 SER B CA  1 
ATOM   4980 C C   . SER B 1 240 ? 106.559 107.618 115.537 1.00 87.14  ? 227 SER B C   1 
ATOM   4981 O O   . SER B 1 240 ? 107.052 108.401 116.356 1.00 86.32  ? 227 SER B O   1 
ATOM   4982 C CB  . SER B 1 240 ? 104.153 107.929 116.208 1.00 80.61  ? 227 SER B CB  1 
ATOM   4983 O OG  . SER B 1 240 ? 103.951 108.871 115.169 1.00 73.27  ? 227 SER B OG  1 
ATOM   4984 N N   . ARG B 1 241 ? 107.136 107.333 114.375 1.00 84.38  ? 228 ARG B N   1 
ATOM   4985 C CA  . ARG B 1 241 ? 108.432 107.872 113.994 1.00 73.37  ? 228 ARG B CA  1 
ATOM   4986 C C   . ARG B 1 241 ? 108.273 109.023 113.009 1.00 73.02  ? 228 ARG B C   1 
ATOM   4987 O O   . ARG B 1 241 ? 107.269 109.127 112.302 1.00 76.96  ? 228 ARG B O   1 
ATOM   4988 C CB  . ARG B 1 241 ? 109.313 106.785 113.378 1.00 70.23  ? 228 ARG B CB  1 
ATOM   4989 C CG  . ARG B 1 241 ? 109.761 105.723 114.361 1.00 69.79  ? 228 ARG B CG  1 
ATOM   4990 C CD  . ARG B 1 241 ? 110.781 104.797 113.728 1.00 64.19  ? 228 ARG B CD  1 
ATOM   4991 N NE  . ARG B 1 241 ? 110.266 103.441 113.588 1.00 65.35  ? 228 ARG B NE  1 
ATOM   4992 C CZ  . ARG B 1 241 ? 110.433 102.484 114.489 1.00 66.14  ? 228 ARG B CZ  1 
ATOM   4993 N NH1 . ARG B 1 241 ? 111.107 102.697 115.607 1.00 61.00  ? 228 ARG B NH1 1 
ATOM   4994 N NH2 . ARG B 1 241 ? 109.913 101.282 114.262 1.00 70.60  ? 228 ARG B NH2 1 
ATOM   4995 N N   . LYS B 1 242 ? 109.279 109.892 112.978 1.00 72.93  ? 229 LYS B N   1 
ATOM   4996 C CA  . LYS B 1 242 ? 109.310 111.032 112.075 1.00 72.91  ? 229 LYS B CA  1 
ATOM   4997 C C   . LYS B 1 242 ? 110.542 110.950 111.184 1.00 67.25  ? 229 LYS B C   1 
ATOM   4998 O O   . LYS B 1 242 ? 111.556 110.350 111.552 1.00 64.95  ? 229 LYS B O   1 
ATOM   4999 C CB  . LYS B 1 242 ? 109.309 112.356 112.849 1.00 69.41  ? 229 LYS B CB  1 
ATOM   5000 C CG  . LYS B 1 242 ? 108.236 112.440 113.925 1.00 71.21  ? 229 LYS B CG  1 
ATOM   5001 C CD  . LYS B 1 242 ? 108.264 113.775 114.649 1.00 67.74  ? 229 LYS B CD  1 
ATOM   5002 C CE  . LYS B 1 242 ? 107.901 114.922 113.724 1.00 71.15  ? 229 LYS B CE  1 
ATOM   5003 N NZ  . LYS B 1 242 ? 107.809 116.211 114.461 1.00 71.52  ? 229 LYS B NZ  1 
ATOM   5004 N N   . VAL B 1 243 ? 110.445 111.555 110.006 1.00 65.88  ? 230 VAL B N   1 
ATOM   5005 C CA  . VAL B 1 243 ? 111.535 111.532 109.035 1.00 67.33  ? 230 VAL B CA  1 
ATOM   5006 C C   . VAL B 1 243 ? 112.524 112.642 109.374 1.00 66.79  ? 230 VAL B C   1 
ATOM   5007 O O   . VAL B 1 243 ? 112.116 113.795 109.582 1.00 66.80  ? 230 VAL B O   1 
ATOM   5008 C CB  . VAL B 1 243 ? 111.005 111.660 107.597 1.00 69.98  ? 230 VAL B CB  1 
ATOM   5009 C CG1 . VAL B 1 243 ? 110.054 112.842 107.470 1.00 72.81  ? 230 VAL B CG1 1 
ATOM   5010 C CG2 . VAL B 1 243 ? 112.156 111.787 106.612 1.00 69.92  ? 230 VAL B CG2 1 
ATOM   5011 N N   . PRO B 1 244 ? 113.818 112.343 109.471 1.00 59.56  ? 231 PRO B N   1 
ATOM   5012 C CA  . PRO B 1 244 ? 114.796 113.397 109.755 1.00 57.47  ? 231 PRO B CA  1 
ATOM   5013 C C   . PRO B 1 244 ? 114.840 114.425 108.635 1.00 60.77  ? 231 PRO B C   1 
ATOM   5014 O O   . PRO B 1 244 ? 114.596 114.117 107.467 1.00 64.35  ? 231 PRO B O   1 
ATOM   5015 C CB  . PRO B 1 244 ? 116.121 112.635 109.866 1.00 51.92  ? 231 PRO B CB  1 
ATOM   5016 C CG  . PRO B 1 244 ? 115.730 111.227 110.159 1.00 47.98  ? 231 PRO B CG  1 
ATOM   5017 C CD  . PRO B 1 244 ? 114.443 111.012 109.428 1.00 53.49  ? 231 PRO B CD  1 
ATOM   5018 N N   . ALA B 1 245 ? 115.146 115.663 109.009 1.00 58.47  ? 232 ALA B N   1 
ATOM   5019 C CA  . ALA B 1 245 ? 115.254 116.734 108.031 1.00 56.82  ? 232 ALA B CA  1 
ATOM   5020 C C   . ALA B 1 245 ? 116.437 116.494 107.101 1.00 55.15  ? 232 ALA B C   1 
ATOM   5021 O O   . ALA B 1 245 ? 117.450 115.906 107.486 1.00 54.16  ? 232 ALA B O   1 
ATOM   5022 C CB  . ALA B 1 245 ? 115.407 118.084 108.729 1.00 56.53  ? 232 ALA B CB  1 
ATOM   5023 N N   . HIS B 1 246 ? 116.299 116.953 105.861 1.00 56.06  ? 233 HIS B N   1 
ATOM   5024 C CA  . HIS B 1 246 ? 117.393 116.869 104.896 1.00 60.89  ? 233 HIS B CA  1 
ATOM   5025 C C   . HIS B 1 246 ? 118.296 118.072 105.123 1.00 58.36  ? 233 HIS B C   1 
ATOM   5026 O O   . HIS B 1 246 ? 117.968 119.197 104.738 1.00 60.38  ? 233 HIS B O   1 
ATOM   5027 C CB  . HIS B 1 246 ? 116.861 116.821 103.469 1.00 65.32  ? 233 HIS B CB  1 
ATOM   5028 C CG  . HIS B 1 246 ? 117.840 116.267 102.481 1.00 69.70  ? 233 HIS B CG  1 
ATOM   5029 N ND1 . HIS B 1 246 ? 117.458 115.474 101.420 1.00 79.60  ? 233 HIS B ND1 1 
ATOM   5030 C CD2 . HIS B 1 246 ? 119.183 116.403 102.383 1.00 65.60  ? 233 HIS B CD2 1 
ATOM   5031 C CE1 . HIS B 1 246 ? 118.525 115.138 100.717 1.00 77.98  ? 233 HIS B CE1 1 
ATOM   5032 N NE2 . HIS B 1 246 ? 119.585 115.689 101.281 1.00 73.34  ? 233 HIS B NE2 1 
ATOM   5033 N N   . MET B 1 247 ? 119.441 117.832 105.750 1.00 53.31  ? 234 MET B N   1 
ATOM   5034 C CA  . MET B 1 247 ? 120.338 118.888 106.196 1.00 48.29  ? 234 MET B CA  1 
ATOM   5035 C C   . MET B 1 247 ? 121.699 118.285 106.517 1.00 47.30  ? 234 MET B C   1 
ATOM   5036 O O   . MET B 1 247 ? 121.825 117.056 106.574 1.00 52.89  ? 234 MET B O   1 
ATOM   5037 C CB  . MET B 1 247 ? 119.751 119.593 107.419 1.00 44.12  ? 234 MET B CB  1 
ATOM   5038 C CG  . MET B 1 247 ? 119.173 118.641 108.446 1.00 45.83  ? 234 MET B CG  1 
ATOM   5039 S SD  . MET B 1 247 ? 118.907 119.429 110.038 1.00 58.97  ? 234 MET B SD  1 
ATOM   5040 C CE  . MET B 1 247 ? 120.599 119.768 110.508 1.00 45.64  ? 234 MET B CE  1 
ATOM   5041 N N   . PRO B 1 248 ? 122.740 119.095 106.708 1.00 41.00  ? 235 PRO B N   1 
ATOM   5042 C CA  . PRO B 1 248 ? 124.028 118.541 107.150 1.00 38.26  ? 235 PRO B CA  1 
ATOM   5043 C C   . PRO B 1 248 ? 123.882 117.814 108.478 1.00 36.98  ? 235 PRO B C   1 
ATOM   5044 O O   . PRO B 1 248 ? 123.453 118.391 109.479 1.00 36.87  ? 235 PRO B O   1 
ATOM   5045 C CB  . PRO B 1 248 ? 124.917 119.782 107.267 1.00 40.39  ? 235 PRO B CB  1 
ATOM   5046 C CG  . PRO B 1 248 ? 124.348 120.727 106.273 1.00 43.52  ? 235 PRO B CG  1 
ATOM   5047 C CD  . PRO B 1 248 ? 122.862 120.511 106.315 1.00 42.82  ? 235 PRO B CD  1 
ATOM   5048 N N   . HIS B 1 249 ? 124.236 116.531 108.477 1.00 34.95  ? 236 HIS B N   1 
ATOM   5049 C CA  . HIS B 1 249 ? 124.043 115.652 109.621 1.00 33.99  ? 236 HIS B CA  1 
ATOM   5050 C C   . HIS B 1 249 ? 125.378 115.300 110.260 1.00 34.24  ? 236 HIS B C   1 
ATOM   5051 O O   . HIS B 1 249 ? 126.340 114.960 109.564 1.00 34.12  ? 236 HIS B O   1 
ATOM   5052 C CB  . HIS B 1 249 ? 123.327 114.362 109.212 1.00 30.64  ? 236 HIS B CB  1 
ATOM   5053 C CG  . HIS B 1 249 ? 121.877 114.546 108.894 1.00 34.62  ? 236 HIS B CG  1 
ATOM   5054 N ND1 . HIS B 1 249 ? 120.978 115.067 109.798 1.00 39.34  ? 236 HIS B ND1 1 
ATOM   5055 C CD2 . HIS B 1 249 ? 121.167 114.264 107.777 1.00 36.53  ? 236 HIS B CD2 1 
ATOM   5056 C CE1 . HIS B 1 249 ? 119.777 115.105 109.250 1.00 40.36  ? 236 HIS B CE1 1 
ATOM   5057 N NE2 . HIS B 1 249 ? 119.865 114.625 108.023 1.00 40.53  ? 236 HIS B NE2 1 
ATOM   5058 N N   . MET B 1 250 ? 125.429 115.376 111.588 1.00 34.74  ? 237 MET B N   1 
ATOM   5059 C CA  . MET B 1 250 ? 126.600 114.932 112.329 1.00 31.44  ? 237 MET B CA  1 
ATOM   5060 C C   . MET B 1 250 ? 126.512 113.434 112.583 1.00 31.85  ? 237 MET B C   1 
ATOM   5061 O O   . MET B 1 250 ? 125.506 112.942 113.103 1.00 34.88  ? 237 MET B O   1 
ATOM   5062 C CB  . MET B 1 250 ? 126.721 115.686 113.651 1.00 34.51  ? 237 MET B CB  1 
ATOM   5063 C CG  . MET B 1 250 ? 127.694 115.049 114.621 1.00 39.42  ? 237 MET B CG  1 
ATOM   5064 S SD  . MET B 1 250 ? 128.200 116.157 115.945 1.00 49.15  ? 237 MET B SD  1 
ATOM   5065 C CE  . MET B 1 250 ? 129.159 117.350 115.021 1.00 38.03  ? 237 MET B CE  1 
ATOM   5066 N N   . ILE B 1 251 ? 127.571 112.712 112.228 1.00 28.98  ? 238 ILE B N   1 
ATOM   5067 C CA  . ILE B 1 251 ? 127.588 111.257 112.277 1.00 29.84  ? 238 ILE B CA  1 
ATOM   5068 C C   . ILE B 1 251 ? 128.765 110.805 113.129 1.00 32.15  ? 238 ILE B C   1 
ATOM   5069 O O   . ILE B 1 251 ? 129.867 111.356 113.026 1.00 36.45  ? 238 ILE B O   1 
ATOM   5070 C CB  . ILE B 1 251 ? 127.676 110.643 110.862 1.00 23.09  ? 238 ILE B CB  1 
ATOM   5071 C CG1 . ILE B 1 251 ? 126.495 111.091 109.999 1.00 21.77  ? 238 ILE B CG1 1 
ATOM   5072 C CG2 . ILE B 1 251 ? 127.711 109.129 110.934 1.00 29.69  ? 238 ILE B CG2 1 
ATOM   5073 C CD1 . ILE B 1 251 ? 125.170 110.512 110.429 1.00 26.89  ? 238 ILE B CD1 1 
ATOM   5074 N N   . ASP B 1 252 ? 128.527 109.814 113.981 1.00 28.81  ? 239 ASP B N   1 
ATOM   5075 C CA  . ASP B 1 252 ? 129.574 109.171 114.761 1.00 27.64  ? 239 ASP B CA  1 
ATOM   5076 C C   . ASP B 1 252 ? 130.015 107.892 114.065 1.00 26.59  ? 239 ASP B C   1 
ATOM   5077 O O   . ASP B 1 252 ? 129.183 107.094 113.627 1.00 25.51  ? 239 ASP B O   1 
ATOM   5078 C CB  . ASP B 1 252 ? 129.082 108.842 116.170 1.00 34.31  ? 239 ASP B CB  1 
ATOM   5079 C CG  . ASP B 1 252 ? 128.673 110.071 116.944 1.00 35.65  ? 239 ASP B CG  1 
ATOM   5080 O OD1 . ASP B 1 252 ? 129.275 110.331 118.006 1.00 33.88  ? 239 ASP B OD1 1 
ATOM   5081 O OD2 . ASP B 1 252 ? 127.761 110.784 116.479 1.00 38.66  ? 239 ASP B OD2 1 
ATOM   5082 N N   . ARG B 1 253 ? 131.330 107.703 113.960 1.00 28.01  ? 240 ARG B N   1 
ATOM   5083 C CA  . ARG B 1 253 ? 131.844 106.464 113.386 1.00 29.59  ? 240 ARG B CA  1 
ATOM   5084 C C   . ARG B 1 253 ? 131.527 105.269 114.277 1.00 35.19  ? 240 ARG B C   1 
ATOM   5085 O O   . ARG B 1 253 ? 131.217 104.183 113.777 1.00 36.70  ? 240 ARG B O   1 
ATOM   5086 C CB  . ARG B 1 253 ? 133.349 106.572 113.150 1.00 29.66  ? 240 ARG B CB  1 
ATOM   5087 C CG  . ARG B 1 253 ? 133.736 107.552 112.061 1.00 26.85  ? 240 ARG B CG  1 
ATOM   5088 C CD  . ARG B 1 253 ? 135.242 107.610 111.892 1.00 32.60  ? 240 ARG B CD  1 
ATOM   5089 N NE  . ARG B 1 253 ? 135.791 106.353 111.398 1.00 40.86  ? 240 ARG B NE  1 
ATOM   5090 C CZ  . ARG B 1 253 ? 137.086 106.111 111.249 1.00 48.61  ? 240 ARG B CZ  1 
ATOM   5091 N NH1 . ARG B 1 253 ? 137.999 107.015 111.563 1.00 44.81  ? 240 ARG B NH1 1 
ATOM   5092 N NH2 . ARG B 1 253 ? 137.475 104.931 110.774 1.00 57.69  ? 240 ARG B NH2 1 
ATOM   5093 N N   . ILE B 1 254 ? 131.603 105.446 115.597 1.00 34.59  ? 241 ILE B N   1 
ATOM   5094 C CA  . ILE B 1 254 ? 131.373 104.333 116.514 1.00 30.08  ? 241 ILE B CA  1 
ATOM   5095 C C   . ILE B 1 254 ? 129.912 103.898 116.480 1.00 36.42  ? 241 ILE B C   1 
ATOM   5096 O O   . ILE B 1 254 ? 129.606 102.703 116.392 1.00 43.94  ? 241 ILE B O   1 
ATOM   5097 C CB  . ILE B 1 254 ? 131.816 104.714 117.936 1.00 27.84  ? 241 ILE B CB  1 
ATOM   5098 C CG1 . ILE B 1 254 ? 133.292 105.109 117.939 1.00 27.94  ? 241 ILE B CG1 1 
ATOM   5099 C CG2 . ILE B 1 254 ? 131.572 103.567 118.896 1.00 32.94  ? 241 ILE B CG2 1 
ATOM   5100 C CD1 . ILE B 1 254 ? 134.204 104.050 117.365 1.00 27.71  ? 241 ILE B CD1 1 
ATOM   5101 N N   . VAL B 1 255 ? 128.989 104.860 116.554 1.00 33.91  ? 242 VAL B N   1 
ATOM   5102 C CA  . VAL B 1 255 ? 127.568 104.525 116.523 1.00 30.16  ? 242 VAL B CA  1 
ATOM   5103 C C   . VAL B 1 255 ? 127.195 103.907 115.183 1.00 35.02  ? 242 VAL B C   1 
ATOM   5104 O O   . VAL B 1 255 ? 126.425 102.943 115.121 1.00 44.75  ? 242 VAL B O   1 
ATOM   5105 C CB  . VAL B 1 255 ? 126.713 105.766 116.830 1.00 28.75  ? 242 VAL B CB  1 
ATOM   5106 C CG1 . VAL B 1 255 ? 125.241 105.395 116.862 1.00 26.83  ? 242 VAL B CG1 1 
ATOM   5107 C CG2 . VAL B 1 255 ? 127.137 106.385 118.147 1.00 35.05  ? 242 VAL B CG2 1 
ATOM   5108 N N   . MET B 1 256 ? 127.731 104.453 114.090 1.00 33.71  ? 243 MET B N   1 
ATOM   5109 C CA  . MET B 1 256 ? 127.448 103.884 112.777 1.00 37.81  ? 243 MET B CA  1 
ATOM   5110 C C   . MET B 1 256 ? 127.995 102.466 112.660 1.00 36.50  ? 243 MET B C   1 
ATOM   5111 O O   . MET B 1 256 ? 127.329 101.586 112.106 1.00 40.55  ? 243 MET B O   1 
ATOM   5112 C CB  . MET B 1 256 ? 128.023 104.778 111.679 1.00 40.74  ? 243 MET B CB  1 
ATOM   5113 C CG  . MET B 1 256 ? 127.769 104.271 110.268 1.00 36.55  ? 243 MET B CG  1 
ATOM   5114 S SD  . MET B 1 256 ? 126.022 104.044 109.891 1.00 39.37  ? 243 MET B SD  1 
ATOM   5115 C CE  . MET B 1 256 ? 125.402 105.703 110.148 1.00 32.14  ? 243 MET B CE  1 
ATOM   5116 N N   . GLN B 1 257 ? 129.201 102.221 113.177 1.00 33.78  ? 244 GLN B N   1 
ATOM   5117 C CA  . GLN B 1 257 ? 129.763 100.875 113.127 1.00 39.52  ? 244 GLN B CA  1 
ATOM   5118 C C   . GLN B 1 257 ? 128.930 99.900  113.946 1.00 42.33  ? 244 GLN B C   1 
ATOM   5119 O O   . GLN B 1 257 ? 128.713 98.756  113.531 1.00 45.26  ? 244 GLN B O   1 
ATOM   5120 C CB  . GLN B 1 257 ? 131.209 100.885 113.618 1.00 46.09  ? 244 GLN B CB  1 
ATOM   5121 C CG  . GLN B 1 257 ? 131.906 99.540  113.496 1.00 52.02  ? 244 GLN B CG  1 
ATOM   5122 C CD  . GLN B 1 257 ? 132.052 99.091  112.056 1.00 57.96  ? 244 GLN B CD  1 
ATOM   5123 O OE1 . GLN B 1 257 ? 132.171 99.912  111.146 1.00 60.76  ? 244 GLN B OE1 1 
ATOM   5124 N NE2 . GLN B 1 257 ? 132.041 97.782  111.841 1.00 56.30  ? 244 GLN B NE2 1 
ATOM   5125 N N   . GLU B 1 258 ? 128.466 100.329 115.121 1.00 44.10  ? 245 GLU B N   1 
ATOM   5126 C CA  . GLU B 1 258 ? 127.598 99.472  115.922 1.00 45.81  ? 245 GLU B CA  1 
ATOM   5127 C C   . GLU B 1 258 ? 126.285 99.195  115.200 1.00 44.45  ? 245 GLU B C   1 
ATOM   5128 O O   . GLU B 1 258 ? 125.756 98.080  115.263 1.00 52.00  ? 245 GLU B O   1 
ATOM   5129 C CB  . GLU B 1 258 ? 127.341 100.107 117.287 1.00 40.49  ? 245 GLU B CB  1 
ATOM   5130 C CG  . GLU B 1 258 ? 128.575 100.193 118.164 1.00 42.54  ? 245 GLU B CG  1 
ATOM   5131 C CD  . GLU B 1 258 ? 128.276 100.764 119.532 1.00 54.21  ? 245 GLU B CD  1 
ATOM   5132 O OE1 . GLU B 1 258 ? 127.082 100.941 119.854 1.00 52.22  ? 245 GLU B OE1 1 
ATOM   5133 O OE2 . GLU B 1 258 ? 129.234 101.037 120.284 1.00 62.64  ? 245 GLU B OE2 1 
ATOM   5134 N N   . LEU B 1 259 ? 125.745 100.200 114.509 1.00 36.87  ? 246 LEU B N   1 
ATOM   5135 C CA  . LEU B 1 259 ? 124.536 99.993  113.720 1.00 37.77  ? 246 LEU B CA  1 
ATOM   5136 C C   . LEU B 1 259 ? 124.771 98.980  112.607 1.00 42.94  ? 246 LEU B C   1 
ATOM   5137 O O   . LEU B 1 259 ? 123.918 98.125  112.343 1.00 45.86  ? 246 LEU B O   1 
ATOM   5138 C CB  . LEU B 1 259 ? 124.055 101.322 113.142 1.00 38.79  ? 246 LEU B CB  1 
ATOM   5139 C CG  . LEU B 1 259 ? 122.786 101.260 112.294 1.00 41.52  ? 246 LEU B CG  1 
ATOM   5140 C CD1 . LEU B 1 259 ? 121.633 100.708 113.110 1.00 40.78  ? 246 LEU B CD1 1 
ATOM   5141 C CD2 . LEU B 1 259 ? 122.445 102.633 111.742 1.00 41.19  ? 246 LEU B CD2 1 
ATOM   5142 N N   . GLN B 1 260 ? 125.922 99.064  111.938 1.00 43.54  ? 247 GLN B N   1 
ATOM   5143 C CA  . GLN B 1 260 ? 126.211 98.136  110.849 1.00 44.74  ? 247 GLN B CA  1 
ATOM   5144 C C   . GLN B 1 260 ? 126.472 96.727  111.365 1.00 48.50  ? 247 GLN B C   1 
ATOM   5145 O O   . GLN B 1 260 ? 126.174 95.751  110.669 1.00 51.03  ? 247 GLN B O   1 
ATOM   5146 C CB  . GLN B 1 260 ? 127.403 98.631  110.030 1.00 45.29  ? 247 GLN B CB  1 
ATOM   5147 C CG  . GLN B 1 260 ? 127.229 100.035 109.471 1.00 45.38  ? 247 GLN B CG  1 
ATOM   5148 C CD  . GLN B 1 260 ? 127.324 100.092 107.962 1.00 42.65  ? 247 GLN B CD  1 
ATOM   5149 O OE1 . GLN B 1 260 ? 127.813 99.163  107.321 1.00 46.01  ? 247 GLN B OE1 1 
ATOM   5150 N NE2 . GLN B 1 260 ? 126.851 101.190 107.385 1.00 42.20  ? 247 GLN B NE2 1 
ATOM   5151 N N   . ASP B 1 261 ? 127.028 96.599  112.571 1.00 46.54  ? 248 ASP B N   1 
ATOM   5152 C CA  . ASP B 1 261 ? 127.243 95.283  113.161 1.00 44.08  ? 248 ASP B CA  1 
ATOM   5153 C C   . ASP B 1 261 ? 125.991 94.719  113.820 1.00 47.78  ? 248 ASP B C   1 
ATOM   5154 O O   . ASP B 1 261 ? 125.947 93.518  114.105 1.00 50.34  ? 248 ASP B O   1 
ATOM   5155 C CB  . ASP B 1 261 ? 128.382 95.339  114.181 1.00 43.47  ? 248 ASP B CB  1 
ATOM   5156 C CG  . ASP B 1 261 ? 129.748 95.322  113.526 1.00 51.25  ? 248 ASP B CG  1 
ATOM   5157 O OD1 . ASP B 1 261 ? 129.808 95.232  112.283 1.00 53.17  ? 248 ASP B OD1 1 
ATOM   5158 O OD2 . ASP B 1 261 ? 130.762 95.394  114.253 1.00 59.82  ? 248 ASP B OD2 1 
ATOM   5159 N N   . MET B 1 262 ? 124.979 95.551  114.069 1.00 47.73  ? 249 MET B N   1 
ATOM   5160 C CA  . MET B 1 262 ? 123.726 95.086  114.649 1.00 49.42  ? 249 MET B CA  1 
ATOM   5161 C C   . MET B 1 262 ? 122.668 94.757  113.604 1.00 54.62  ? 249 MET B C   1 
ATOM   5162 O O   . MET B 1 262 ? 121.776 93.950  113.882 1.00 60.33  ? 249 MET B O   1 
ATOM   5163 C CB  . MET B 1 262 ? 123.175 96.134  115.624 1.00 50.17  ? 249 MET B CB  1 
ATOM   5164 C CG  . MET B 1 262 ? 122.028 95.648  116.493 1.00 51.85  ? 249 MET B CG  1 
ATOM   5165 S SD  . MET B 1 262 ? 121.579 96.835  117.773 1.00 60.33  ? 249 MET B SD  1 
ATOM   5166 C CE  . MET B 1 262 ? 123.076 96.853  118.755 1.00 52.08  ? 249 MET B CE  1 
ATOM   5167 N N   . PHE B 1 263 ? 122.750 95.351  112.415 1.00 51.59  ? 250 PHE B N   1 
ATOM   5168 C CA  . PHE B 1 263 ? 121.878 95.017  111.289 1.00 54.72  ? 250 PHE B CA  1 
ATOM   5169 C C   . PHE B 1 263 ? 122.743 94.751  110.062 1.00 56.71  ? 250 PHE B C   1 
ATOM   5170 O O   . PHE B 1 263 ? 122.693 95.497  109.078 1.00 61.77  ? 250 PHE B O   1 
ATOM   5171 C CB  . PHE B 1 263 ? 120.875 96.137  111.014 1.00 56.76  ? 250 PHE B CB  1 
ATOM   5172 C CG  . PHE B 1 263 ? 119.967 96.441  112.170 1.00 55.13  ? 250 PHE B CG  1 
ATOM   5173 C CD1 . PHE B 1 263 ? 118.742 95.811  112.289 1.00 55.95  ? 250 PHE B CD1 1 
ATOM   5174 C CD2 . PHE B 1 263 ? 120.334 97.367  113.131 1.00 52.78  ? 250 PHE B CD2 1 
ATOM   5175 C CE1 . PHE B 1 263 ? 117.904 96.093  113.347 1.00 59.07  ? 250 PHE B CE1 1 
ATOM   5176 C CE2 . PHE B 1 263 ? 119.498 97.652  114.192 1.00 53.10  ? 250 PHE B CE2 1 
ATOM   5177 C CZ  . PHE B 1 263 ? 118.283 97.015  114.299 1.00 57.64  ? 250 PHE B CZ  1 
ATOM   5178 N N   . PRO B 1 264 ? 123.552 93.687  110.088 1.00 56.26  ? 251 PRO B N   1 
ATOM   5179 C CA  . PRO B 1 264 ? 124.514 93.464  109.000 1.00 56.81  ? 251 PRO B CA  1 
ATOM   5180 C C   . PRO B 1 264 ? 123.850 93.019  107.706 1.00 58.56  ? 251 PRO B C   1 
ATOM   5181 O O   . PRO B 1 264 ? 124.232 93.456  106.612 1.00 60.18  ? 251 PRO B O   1 
ATOM   5182 C CB  . PRO B 1 264 ? 125.433 92.366  109.560 1.00 57.52  ? 251 PRO B CB  1 
ATOM   5183 C CG  . PRO B 1 264 ? 125.027 92.184  111.011 1.00 57.29  ? 251 PRO B CG  1 
ATOM   5184 C CD  . PRO B 1 264 ? 123.603 92.608  111.084 1.00 57.27  ? 251 PRO B CD  1 
ATOM   5185 N N   . GLU B 1 265 ? 122.864 92.128  107.829 1.00 62.54  ? 252 GLU B N   1 
ATOM   5186 C CA  . GLU B 1 265 ? 122.207 91.575  106.650 1.00 70.89  ? 252 GLU B CA  1 
ATOM   5187 C C   . GLU B 1 265 ? 121.510 92.664  105.845 1.00 71.29  ? 252 GLU B C   1 
ATOM   5188 O O   . GLU B 1 265 ? 121.655 92.734  104.619 1.00 76.56  ? 252 GLU B O   1 
ATOM   5189 C CB  . GLU B 1 265 ? 121.217 90.486  107.063 1.00 77.05  ? 252 GLU B CB  1 
ATOM   5190 C CG  . GLU B 1 265 ? 121.874 89.259  107.671 1.00 79.47  ? 252 GLU B CG  1 
ATOM   5191 C CD  . GLU B 1 265 ? 122.802 88.552  106.701 1.00 81.84  ? 252 GLU B CD  1 
ATOM   5192 O OE1 . GLU B 1 265 ? 122.562 88.630  105.477 1.00 85.53  ? 252 GLU B OE1 1 
ATOM   5193 O OE2 . GLU B 1 265 ? 123.773 87.917  107.163 1.00 76.94  ? 252 GLU B OE2 1 
ATOM   5194 N N   . GLU B 1 266 ? 120.763 93.537  106.523 1.00 65.57  ? 253 GLU B N   1 
ATOM   5195 C CA  . GLU B 1 266 ? 120.061 94.602  105.818 1.00 63.54  ? 253 GLU B CA  1 
ATOM   5196 C C   . GLU B 1 266 ? 121.033 95.553  105.136 1.00 58.73  ? 253 GLU B C   1 
ATOM   5197 O O   . GLU B 1 266 ? 120.743 96.068  104.051 1.00 59.44  ? 253 GLU B O   1 
ATOM   5198 C CB  . GLU B 1 266 ? 119.158 95.368  106.784 1.00 64.88  ? 253 GLU B CB  1 
ATOM   5199 C CG  . GLU B 1 266 ? 118.000 94.555  107.349 1.00 67.52  ? 253 GLU B CG  1 
ATOM   5200 C CD  . GLU B 1 266 ? 118.431 93.583  108.431 1.00 65.94  ? 253 GLU B CD  1 
ATOM   5201 O OE1 . GLU B 1 266 ? 119.602 93.645  108.858 1.00 64.03  ? 253 GLU B OE1 1 
ATOM   5202 O OE2 . GLU B 1 266 ? 117.598 92.755  108.854 1.00 68.77  ? 253 GLU B OE2 1 
ATOM   5203 N N   . PHE B 1 267 ? 122.202 95.776  105.736 1.00 56.15  ? 254 PHE B N   1 
ATOM   5204 C CA  . PHE B 1 267 ? 123.137 96.730  105.155 1.00 53.60  ? 254 PHE B CA  1 
ATOM   5205 C C   . PHE B 1 267 ? 123.895 96.145  103.967 1.00 63.69  ? 254 PHE B C   1 
ATOM   5206 O O   . PHE B 1 267 ? 124.119 96.846  102.974 1.00 74.09  ? 254 PHE B O   1 
ATOM   5207 C CB  . PHE B 1 267 ? 124.091 97.253  106.226 1.00 49.69  ? 254 PHE B CB  1 
ATOM   5208 C CG  . PHE B 1 267 ? 123.534 98.418  106.999 1.00 49.08  ? 254 PHE B CG  1 
ATOM   5209 C CD1 . PHE B 1 267 ? 122.376 99.047  106.576 1.00 44.75  ? 254 PHE B CD1 1 
ATOM   5210 C CD2 . PHE B 1 267 ? 124.164 98.887  108.136 1.00 49.35  ? 254 PHE B CD2 1 
ATOM   5211 C CE1 . PHE B 1 267 ? 121.856 100.117 107.274 1.00 42.65  ? 254 PHE B CE1 1 
ATOM   5212 C CE2 . PHE B 1 267 ? 123.648 99.959  108.838 1.00 45.90  ? 254 PHE B CE2 1 
ATOM   5213 C CZ  . PHE B 1 267 ? 122.493 100.574 108.405 1.00 43.78  ? 254 PHE B CZ  1 
ATOM   5214 N N   . ASP B 1 268 ? 124.276 94.866  104.011 1.00 65.52  ? 255 ASP B N   1 
ATOM   5215 C CA  . ASP B 1 268 ? 124.828 94.314  102.776 1.00 68.07  ? 255 ASP B CA  1 
ATOM   5216 C C   . ASP B 1 268 ? 123.745 94.116  101.720 1.00 70.37  ? 255 ASP B C   1 
ATOM   5217 O O   . ASP B 1 268 ? 124.057 94.101  100.525 1.00 72.11  ? 255 ASP B O   1 
ATOM   5218 C CB  . ASP B 1 268 ? 125.590 93.010  103.025 1.00 66.53  ? 255 ASP B CB  1 
ATOM   5219 C CG  . ASP B 1 268 ? 124.680 91.834  103.270 1.00 69.63  ? 255 ASP B CG  1 
ATOM   5220 O OD1 . ASP B 1 268 ? 124.171 91.714  104.396 1.00 67.07  ? 255 ASP B OD1 1 
ATOM   5221 O OD2 . ASP B 1 268 ? 124.479 91.025  102.340 1.00 75.21  ? 255 ASP B OD2 1 
ATOM   5222 N N   . LYS B 1 269 ? 122.476 94.017  102.128 1.00 69.92  ? 256 LYS B N   1 
ATOM   5223 C CA  . LYS B 1 269 ? 121.391 94.011  101.152 1.00 68.95  ? 256 LYS B CA  1 
ATOM   5224 C C   . LYS B 1 269 ? 121.256 95.362  100.460 1.00 71.33  ? 256 LYS B C   1 
ATOM   5225 O O   . LYS B 1 269 ? 121.102 95.423  99.235  1.00 76.65  ? 256 LYS B O   1 
ATOM   5226 C CB  . LYS B 1 269 ? 120.077 93.631  101.832 1.00 64.94  ? 256 LYS B CB  1 
ATOM   5227 C CG  . LYS B 1 269 ? 118.850 93.746  100.940 1.00 70.57  ? 256 LYS B CG  1 
ATOM   5228 C CD  . LYS B 1 269 ? 117.583 93.706  101.773 1.00 75.53  ? 256 LYS B CD  1 
ATOM   5229 C CE  . LYS B 1 269 ? 117.567 92.479  102.668 1.00 74.31  ? 256 LYS B CE  1 
ATOM   5230 N NZ  . LYS B 1 269 ? 116.426 92.484  103.621 1.00 75.81  ? 256 LYS B NZ  1 
ATOM   5231 N N   . THR B 1 270 ? 121.302 96.455  101.226 1.00 68.14  ? 257 THR B N   1 
ATOM   5232 C CA  . THR B 1 270 ? 121.191 97.773  100.607 1.00 67.55  ? 257 THR B CA  1 
ATOM   5233 C C   . THR B 1 270 ? 122.442 98.121  99.812  1.00 65.97  ? 257 THR B C   1 
ATOM   5234 O O   . THR B 1 270 ? 122.370 98.904  98.860  1.00 68.72  ? 257 THR B O   1 
ATOM   5235 C CB  . THR B 1 270 ? 120.906 98.857  101.651 1.00 67.91  ? 257 THR B CB  1 
ATOM   5236 O OG1 . THR B 1 270 ? 120.676 100.104 100.987 1.00 68.91  ? 257 THR B OG1 1 
ATOM   5237 C CG2 . THR B 1 270 ? 122.070 99.031  102.599 1.00 60.41  ? 257 THR B CG2 1 
ATOM   5238 N N   . SER B 1 271 ? 123.593 97.554  100.183 1.00 65.54  ? 258 SER B N   1 
ATOM   5239 C CA  . SER B 1 271 ? 124.774 97.692  99.340  1.00 69.37  ? 258 SER B CA  1 
ATOM   5240 C C   . SER B 1 271 ? 124.666 96.830  98.086  1.00 79.46  ? 258 SER B C   1 
ATOM   5241 O O   . SER B 1 271 ? 125.326 97.116  97.081  1.00 81.96  ? 258 SER B O   1 
ATOM   5242 C CB  . SER B 1 271 ? 126.031 97.330  100.131 1.00 67.16  ? 258 SER B CB  1 
ATOM   5243 O OG  . SER B 1 271 ? 127.191 97.433  99.325  1.00 65.93  ? 258 SER B OG  1 
ATOM   5244 N N   . PHE B 1 272 ? 123.856 95.768  98.131  1.00 78.64  ? 259 PHE B N   1 
ATOM   5245 C CA  . PHE B 1 272 ? 123.670 94.924  96.955  1.00 78.01  ? 259 PHE B CA  1 
ATOM   5246 C C   . PHE B 1 272 ? 122.936 95.665  95.843  1.00 77.93  ? 259 PHE B C   1 
ATOM   5247 O O   . PHE B 1 272 ? 123.279 95.520  94.664  1.00 82.42  ? 259 PHE B O   1 
ATOM   5248 C CB  . PHE B 1 272 ? 122.915 93.652  97.340  1.00 80.34  ? 259 PHE B CB  1 
ATOM   5249 C CG  . PHE B 1 272 ? 122.851 92.625  96.244  1.00 87.50  ? 259 PHE B CG  1 
ATOM   5250 C CD1 . PHE B 1 272 ? 121.811 92.629  95.330  1.00 83.38  ? 259 PHE B CD1 1 
ATOM   5251 C CD2 . PHE B 1 272 ? 123.826 91.648  96.136  1.00 92.00  ? 259 PHE B CD2 1 
ATOM   5252 C CE1 . PHE B 1 272 ? 121.748 91.685  94.326  1.00 84.24  ? 259 PHE B CE1 1 
ATOM   5253 C CE2 . PHE B 1 272 ? 123.767 90.700  95.135  1.00 92.35  ? 259 PHE B CE2 1 
ATOM   5254 C CZ  . PHE B 1 272 ? 122.727 90.719  94.229  1.00 87.99  ? 259 PHE B CZ  1 
ATOM   5255 N N   . HIS B 1 273 ? 121.920 96.453  96.191  1.00 74.88  ? 260 HIS B N   1 
ATOM   5256 C CA  . HIS B 1 273 ? 121.115 97.143  95.186  1.00 81.95  ? 260 HIS B CA  1 
ATOM   5257 C C   . HIS B 1 273 ? 121.925 98.268  94.551  1.00 86.20  ? 260 HIS B C   1 
ATOM   5258 O O   . HIS B 1 273 ? 122.288 99.239  95.221  1.00 86.07  ? 260 HIS B O   1 
ATOM   5259 C CB  . HIS B 1 273 ? 119.834 97.686  95.813  1.00 82.67  ? 260 HIS B CB  1 
ATOM   5260 C CG  . HIS B 1 273 ? 118.760 96.658  95.986  1.00 87.31  ? 260 HIS B CG  1 
ATOM   5261 N ND1 . HIS B 1 273 ? 117.448 96.989  96.245  1.00 87.10  ? 260 HIS B ND1 1 
ATOM   5262 C CD2 . HIS B 1 273 ? 118.804 95.306  95.936  1.00 89.28  ? 260 HIS B CD2 1 
ATOM   5263 C CE1 . HIS B 1 273 ? 116.729 95.885  96.348  1.00 87.80  ? 260 HIS B CE1 1 
ATOM   5264 N NE2 . HIS B 1 273 ? 117.528 94.850  96.165  1.00 91.50  ? 260 HIS B NE2 1 
ATOM   5265 N N   . LYS B 1 274 ? 122.212 98.136  93.255  1.00 87.77  ? 261 LYS B N   1 
ATOM   5266 C CA  . LYS B 1 274 ? 122.837 99.210  92.494  1.00 85.91  ? 261 LYS B CA  1 
ATOM   5267 C C   . LYS B 1 274 ? 121.828 100.220 91.967  1.00 81.66  ? 261 LYS B C   1 
ATOM   5268 O O   . LYS B 1 274 ? 122.223 101.188 91.311  1.00 80.73  ? 261 LYS B O   1 
ATOM   5269 C CB  . LYS B 1 274 ? 123.647 98.637  91.332  1.00 88.51  ? 261 LYS B CB  1 
ATOM   5270 C CG  . LYS B 1 274 ? 124.780 97.727  91.763  1.00 91.71  ? 261 LYS B CG  1 
ATOM   5271 C CD  . LYS B 1 274 ? 125.557 97.215  90.564  1.00 93.00  ? 261 LYS B CD  1 
ATOM   5272 C CE  . LYS B 1 274 ? 126.681 96.287  90.994  1.00 94.26  ? 261 LYS B CE  1 
ATOM   5273 N NZ  . LYS B 1 274 ? 127.575 95.935  89.858  1.00 92.27  ? 261 LYS B NZ  1 
ATOM   5274 N N   . VAL B 1 275 ? 120.540 99.997  92.198  1.00 82.65  ? 262 VAL B N   1 
ATOM   5275 C CA  . VAL B 1 275 ? 119.494 100.965 91.896  1.00 88.81  ? 262 VAL B CA  1 
ATOM   5276 C C   . VAL B 1 275 ? 118.642 101.122 93.146  1.00 90.12  ? 262 VAL B C   1 
ATOM   5277 O O   . VAL B 1 275 ? 118.337 100.130 93.817  1.00 95.52  ? 262 VAL B O   1 
ATOM   5278 C CB  . VAL B 1 275 ? 118.637 100.530 90.692  1.00 94.74  ? 262 VAL B CB  1 
ATOM   5279 C CG1 . VAL B 1 275 ? 117.480 101.495 90.478  1.00 91.12  ? 262 VAL B CG1 1 
ATOM   5280 C CG2 . VAL B 1 275 ? 119.495 100.442 89.439  1.00 98.62  ? 262 VAL B CG2 1 
ATOM   5281 N N   . ARG B 1 276 ? 118.288 102.362 93.476  1.00 85.01  ? 263 ARG B N   1 
ATOM   5282 C CA  . ARG B 1 276 ? 117.466 102.608 94.652  1.00 85.00  ? 263 ARG B CA  1 
ATOM   5283 C C   . ARG B 1 276 ? 116.136 101.876 94.526  1.00 91.60  ? 263 ARG B C   1 
ATOM   5284 O O   . ARG B 1 276 ? 115.463 101.955 93.494  1.00 93.15  ? 263 ARG B O   1 
ATOM   5285 C CB  . ARG B 1 276 ? 117.232 104.108 94.833  1.00 82.12  ? 263 ARG B CB  1 
ATOM   5286 C CG  . ARG B 1 276 ? 116.631 104.474 96.180  1.00 85.51  ? 263 ARG B CG  1 
ATOM   5287 C CD  . ARG B 1 276 ? 116.304 105.954 96.267  1.00 93.31  ? 263 ARG B CD  1 
ATOM   5288 N NE  . ARG B 1 276 ? 115.881 106.342 97.607  1.00 99.87  ? 263 ARG B NE  1 
ATOM   5289 C CZ  . ARG B 1 276 ? 115.485 107.561 97.943  1.00 99.09  ? 263 ARG B CZ  1 
ATOM   5290 N NH1 . ARG B 1 276 ? 115.428 108.539 97.054  1.00 98.11  ? 263 ARG B NH1 1 
ATOM   5291 N NH2 . ARG B 1 276 ? 115.137 107.807 99.203  1.00 94.40  ? 263 ARG B NH2 1 
ATOM   5292 N N   . HIS B 1 277 ? 115.765 101.153 95.581  1.00 92.12  ? 264 HIS B N   1 
ATOM   5293 C CA  . HIS B 1 277 ? 114.582 100.304 95.576  1.00 91.35  ? 264 HIS B CA  1 
ATOM   5294 C C   . HIS B 1 277 ? 113.943 100.346 96.958  1.00 86.94  ? 264 HIS B C   1 
ATOM   5295 O O   . HIS B 1 277 ? 114.459 100.975 97.885  1.00 84.08  ? 264 HIS B O   1 
ATOM   5296 C CB  . HIS B 1 277 ? 114.939 98.869  95.171  1.00 89.82  ? 264 HIS B CB  1 
ATOM   5297 C CG  . HIS B 1 277 ? 113.753 98.022  94.828  1.00 90.81  ? 264 HIS B CG  1 
ATOM   5298 N ND1 . HIS B 1 277 ? 113.697 96.673  95.105  1.00 90.20  ? 264 HIS B ND1 1 
ATOM   5299 C CD2 . HIS B 1 277 ? 112.579 98.333  94.229  1.00 95.61  ? 264 HIS B CD2 1 
ATOM   5300 C CE1 . HIS B 1 277 ? 112.539 96.190  94.692  1.00 93.88  ? 264 HIS B CE1 1 
ATOM   5301 N NE2 . HIS B 1 277 ? 111.842 97.176  94.157  1.00 99.32  ? 264 HIS B NE2 1 
ATOM   5302 N N   . SER B 1 278 ? 112.801 99.670  97.090  1.00 87.72  ? 265 SER B N   1 
ATOM   5303 C CA  . SER B 1 278 ? 112.103 99.600  98.368  1.00 89.27  ? 265 SER B CA  1 
ATOM   5304 C C   . SER B 1 278 ? 112.890 98.843  99.431  1.00 86.83  ? 265 SER B C   1 
ATOM   5305 O O   . SER B 1 278 ? 112.615 99.012  100.624 1.00 83.29  ? 265 SER B O   1 
ATOM   5306 C CB  . SER B 1 278 ? 110.736 98.944  98.173  1.00 90.68  ? 265 SER B CB  1 
ATOM   5307 O OG  . SER B 1 278 ? 110.078 98.753  99.413  1.00 85.48  ? 265 SER B OG  1 
ATOM   5308 N N   . GLU B 1 279 ? 113.853 98.012  99.037  1.00 85.48  ? 266 GLU B N   1 
ATOM   5309 C CA  . GLU B 1 279 ? 114.540 97.122  99.963  1.00 82.46  ? 266 GLU B CA  1 
ATOM   5310 C C   . GLU B 1 279 ? 115.872 97.691  100.445 1.00 82.32  ? 266 GLU B C   1 
ATOM   5311 O O   . GLU B 1 279 ? 116.807 96.932  100.719 1.00 80.77  ? 266 GLU B O   1 
ATOM   5312 C CB  . GLU B 1 279 ? 114.749 95.755  99.314  1.00 79.52  ? 266 GLU B CB  1 
ATOM   5313 C CG  . GLU B 1 279 ? 114.480 94.576  100.227 1.00 75.25  ? 266 GLU B CG  1 
ATOM   5314 C CD  . GLU B 1 279 ? 114.644 93.254  99.506  1.00 84.03  ? 266 GLU B CD  1 
ATOM   5315 O OE1 . GLU B 1 279 ? 114.613 93.251  98.258  1.00 88.28  ? 266 GLU B OE1 1 
ATOM   5316 O OE2 . GLU B 1 279 ? 114.813 92.221  100.189 1.00 87.73  ? 266 GLU B OE2 1 
ATOM   5317 N N   . ASP B 1 280 ? 115.983 99.010  100.553 1.00 83.08  ? 267 ASP B N   1 
ATOM   5318 C CA  . ASP B 1 280 ? 117.196 99.639  101.049 1.00 79.02  ? 267 ASP B CA  1 
ATOM   5319 C C   . ASP B 1 280 ? 116.937 100.304 102.396 1.00 79.09  ? 267 ASP B C   1 
ATOM   5320 O O   . ASP B 1 280 ? 115.815 100.725 102.698 1.00 83.85  ? 267 ASP B O   1 
ATOM   5321 C CB  . ASP B 1 280 ? 117.743 100.662 100.046 1.00 80.45  ? 267 ASP B CB  1 
ATOM   5322 C CG  . ASP B 1 280 ? 116.790 101.810 99.790  1.00 83.43  ? 267 ASP B CG  1 
ATOM   5323 O OD1 . ASP B 1 280 ? 115.611 101.720 100.184 1.00 85.52  ? 267 ASP B OD1 1 
ATOM   5324 O OD2 . ASP B 1 280 ? 117.229 102.814 99.193  1.00 85.71  ? 267 ASP B OD2 1 
ATOM   5325 N N   . MET B 1 281 ? 117.986 100.384 103.210 1.00 74.85  ? 268 MET B N   1 
ATOM   5326 C CA  . MET B 1 281 ? 117.909 100.975 104.539 1.00 68.47  ? 268 MET B CA  1 
ATOM   5327 C C   . MET B 1 281 ? 118.528 102.364 104.486 1.00 60.09  ? 268 MET B C   1 
ATOM   5328 O O   . MET B 1 281 ? 119.702 102.510 104.126 1.00 58.48  ? 268 MET B O   1 
ATOM   5329 C CB  . MET B 1 281 ? 118.617 100.098 105.571 1.00 70.33  ? 268 MET B CB  1 
ATOM   5330 C CG  . MET B 1 281 ? 118.185 100.367 107.002 1.00 65.60  ? 268 MET B CG  1 
ATOM   5331 S SD  . MET B 1 281 ? 118.561 99.022  108.138 1.00 70.14  ? 268 MET B SD  1 
ATOM   5332 C CE  . MET B 1 281 ? 117.776 99.624  109.629 1.00 69.63  ? 268 MET B CE  1 
ATOM   5333 N N   . GLN B 1 282 ? 117.744 103.375 104.847 1.00 61.46  ? 269 GLN B N   1 
ATOM   5334 C CA  . GLN B 1 282 ? 118.189 104.748 104.683 1.00 60.97  ? 269 GLN B CA  1 
ATOM   5335 C C   . GLN B 1 282 ? 119.270 105.092 105.702 1.00 54.77  ? 269 GLN B C   1 
ATOM   5336 O O   . GLN B 1 282 ? 119.450 104.416 106.718 1.00 59.66  ? 269 GLN B O   1 
ATOM   5337 C CB  . GLN B 1 282 ? 117.011 105.712 104.809 1.00 59.39  ? 269 GLN B CB  1 
ATOM   5338 C CG  . GLN B 1 282 ? 117.169 106.968 103.973 1.00 64.35  ? 269 GLN B CG  1 
ATOM   5339 C CD  . GLN B 1 282 ? 115.855 107.672 103.725 1.00 76.73  ? 269 GLN B CD  1 
ATOM   5340 O OE1 . GLN B 1 282 ? 114.911 107.537 104.501 1.00 74.05  ? 269 GLN B OE1 1 
ATOM   5341 N NE2 . GLN B 1 282 ? 115.783 108.424 102.632 1.00 85.46  ? 269 GLN B NE2 1 
ATOM   5342 N N   . PHE B 1 283 ? 120.005 106.163 105.405 1.00 49.26  ? 270 PHE B N   1 
ATOM   5343 C CA  . PHE B 1 283 ? 121.139 106.561 106.231 1.00 49.44  ? 270 PHE B CA  1 
ATOM   5344 C C   . PHE B 1 283 ? 120.687 107.303 107.485 1.00 47.27  ? 270 PHE B C   1 
ATOM   5345 O O   . PHE B 1 283 ? 120.854 106.812 108.610 1.00 44.68  ? 270 PHE B O   1 
ATOM   5346 C CB  . PHE B 1 283 ? 122.084 107.431 105.396 1.00 46.11  ? 270 PHE B CB  1 
ATOM   5347 C CG  . PHE B 1 283 ? 123.453 107.585 105.982 1.00 44.09  ? 270 PHE B CG  1 
ATOM   5348 C CD1 . PHE B 1 283 ? 124.263 106.482 106.183 1.00 44.23  ? 270 PHE B CD1 1 
ATOM   5349 C CD2 . PHE B 1 283 ? 123.943 108.837 106.304 1.00 45.85  ? 270 PHE B CD2 1 
ATOM   5350 C CE1 . PHE B 1 283 ? 125.527 106.624 106.716 1.00 43.82  ? 270 PHE B CE1 1 
ATOM   5351 C CE2 . PHE B 1 283 ? 125.207 108.985 106.833 1.00 48.94  ? 270 PHE B CE2 1 
ATOM   5352 C CZ  . PHE B 1 283 ? 126.001 107.877 107.037 1.00 47.49  ? 270 PHE B CZ  1 
ATOM   5353 N N   . ALA B 1 284 ? 120.084 108.479 107.301 1.00 43.43  ? 271 ALA B N   1 
ATOM   5354 C CA  . ALA B 1 284 ? 119.743 109.333 108.433 1.00 40.96  ? 271 ALA B CA  1 
ATOM   5355 C C   . ALA B 1 284 ? 118.697 108.679 109.323 1.00 48.16  ? 271 ALA B C   1 
ATOM   5356 O O   . ALA B 1 284 ? 118.809 108.714 110.553 1.00 52.61  ? 271 ALA B O   1 
ATOM   5357 C CB  . ALA B 1 284 ? 119.251 110.691 107.936 1.00 42.32  ? 271 ALA B CB  1 
ATOM   5358 N N   . PHE B 1 285 ? 117.673 108.075 108.718 1.00 50.42  ? 272 PHE B N   1 
ATOM   5359 C CA  . PHE B 1 285 ? 116.615 107.441 109.498 1.00 48.04  ? 272 PHE B CA  1 
ATOM   5360 C C   . PHE B 1 285 ? 117.185 106.362 110.410 1.00 47.50  ? 272 PHE B C   1 
ATOM   5361 O O   . PHE B 1 285 ? 116.973 106.382 111.632 1.00 49.20  ? 272 PHE B O   1 
ATOM   5362 C CB  . PHE B 1 285 ? 115.568 106.857 108.550 1.00 47.64  ? 272 PHE B CB  1 
ATOM   5363 C CG  . PHE B 1 285 ? 114.229 106.623 109.183 1.00 52.46  ? 272 PHE B CG  1 
ATOM   5364 C CD1 . PHE B 1 285 ? 113.539 107.661 109.779 1.00 57.82  ? 272 PHE B CD1 1 
ATOM   5365 C CD2 . PHE B 1 285 ? 113.644 105.372 109.152 1.00 53.28  ? 272 PHE B CD2 1 
ATOM   5366 C CE1 . PHE B 1 285 ? 112.299 107.449 110.350 1.00 58.38  ? 272 PHE B CE1 1 
ATOM   5367 C CE2 . PHE B 1 285 ? 112.407 105.154 109.721 1.00 54.88  ? 272 PHE B CE2 1 
ATOM   5368 C CZ  . PHE B 1 285 ? 111.734 106.194 110.321 1.00 56.03  ? 272 PHE B CZ  1 
ATOM   5369 N N   . SER B 1 286 ? 117.952 105.435 109.834 1.00 48.59  ? 273 SER B N   1 
ATOM   5370 C CA  . SER B 1 286 ? 118.508 104.340 110.618 1.00 50.83  ? 273 SER B CA  1 
ATOM   5371 C C   . SER B 1 286 ? 119.451 104.856 111.695 1.00 47.85  ? 273 SER B C   1 
ATOM   5372 O O   . SER B 1 286 ? 119.347 104.458 112.859 1.00 50.13  ? 273 SER B O   1 
ATOM   5373 C CB  . SER B 1 286 ? 119.226 103.346 109.706 1.00 50.72  ? 273 SER B CB  1 
ATOM   5374 O OG  . SER B 1 286 ? 120.346 103.950 109.086 1.00 51.12  ? 273 SER B OG  1 
ATOM   5375 N N   . TYR B 1 287 ? 120.375 105.754 111.334 1.00 42.78  ? 274 TYR B N   1 
ATOM   5376 C CA  . TYR B 1 287 ? 121.343 106.230 112.320 1.00 40.82  ? 274 TYR B CA  1 
ATOM   5377 C C   . TYR B 1 287 ? 120.650 106.950 113.473 1.00 37.28  ? 274 TYR B C   1 
ATOM   5378 O O   . TYR B 1 287 ? 120.907 106.655 114.647 1.00 39.41  ? 274 TYR B O   1 
ATOM   5379 C CB  . TYR B 1 287 ? 122.376 107.150 111.669 1.00 38.36  ? 274 TYR B CB  1 
ATOM   5380 C CG  . TYR B 1 287 ? 123.329 107.782 112.666 1.00 31.04  ? 274 TYR B CG  1 
ATOM   5381 C CD1 . TYR B 1 287 ? 123.137 109.083 113.114 1.00 31.98  ? 274 TYR B CD1 1 
ATOM   5382 C CD2 . TYR B 1 287 ? 124.411 107.074 113.169 1.00 27.46  ? 274 TYR B CD2 1 
ATOM   5383 C CE1 . TYR B 1 287 ? 123.998 109.660 114.026 1.00 31.50  ? 274 TYR B CE1 1 
ATOM   5384 C CE2 . TYR B 1 287 ? 125.277 107.645 114.079 1.00 27.06  ? 274 TYR B CE2 1 
ATOM   5385 C CZ  . TYR B 1 287 ? 125.066 108.935 114.505 1.00 31.91  ? 274 TYR B CZ  1 
ATOM   5386 O OH  . TYR B 1 287 ? 125.926 109.507 115.413 1.00 37.46  ? 274 TYR B OH  1 
ATOM   5387 N N   . PHE B 1 288 ? 119.762 107.898 113.160 1.00 35.07  ? 275 PHE B N   1 
ATOM   5388 C CA  . PHE B 1 288 ? 119.157 108.707 114.209 1.00 36.22  ? 275 PHE B CA  1 
ATOM   5389 C C   . PHE B 1 288 ? 118.236 107.882 115.093 1.00 43.97  ? 275 PHE B C   1 
ATOM   5390 O O   . PHE B 1 288 ? 118.203 108.084 116.311 1.00 52.53  ? 275 PHE B O   1 
ATOM   5391 C CB  . PHE B 1 288 ? 118.417 109.890 113.594 1.00 40.36  ? 275 PHE B CB  1 
ATOM   5392 C CG  . PHE B 1 288 ? 119.331 110.971 113.098 1.00 43.70  ? 275 PHE B CG  1 
ATOM   5393 C CD1 . PHE B 1 288 ? 120.317 111.486 113.921 1.00 43.78  ? 275 PHE B CD1 1 
ATOM   5394 C CD2 . PHE B 1 288 ? 119.224 111.456 111.807 1.00 42.95  ? 275 PHE B CD2 1 
ATOM   5395 C CE1 . PHE B 1 288 ? 121.170 112.473 113.470 1.00 44.79  ? 275 PHE B CE1 1 
ATOM   5396 C CE2 . PHE B 1 288 ? 120.074 112.440 111.350 1.00 43.93  ? 275 PHE B CE2 1 
ATOM   5397 C CZ  . PHE B 1 288 ? 121.047 112.950 112.181 1.00 45.52  ? 275 PHE B CZ  1 
ATOM   5398 N N   . TYR B 1 289 ? 117.496 106.927 114.524 1.00 38.94  ? 276 TYR B N   1 
ATOM   5399 C CA  . TYR B 1 289 ? 116.615 106.158 115.392 1.00 39.05  ? 276 TYR B CA  1 
ATOM   5400 C C   . TYR B 1 289 ? 117.336 105.033 116.122 1.00 37.98  ? 276 TYR B C   1 
ATOM   5401 O O   . TYR B 1 289 ? 116.877 104.627 117.193 1.00 41.06  ? 276 TYR B O   1 
ATOM   5402 C CB  . TYR B 1 289 ? 115.424 105.640 114.592 1.00 42.64  ? 276 TYR B CB  1 
ATOM   5403 C CG  . TYR B 1 289 ? 114.404 106.730 114.378 1.00 50.55  ? 276 TYR B CG  1 
ATOM   5404 C CD1 . TYR B 1 289 ? 113.314 106.860 115.224 1.00 54.89  ? 276 TYR B CD1 1 
ATOM   5405 C CD2 . TYR B 1 289 ? 114.554 107.657 113.357 1.00 51.33  ? 276 TYR B CD2 1 
ATOM   5406 C CE1 . TYR B 1 289 ? 112.388 107.868 115.043 1.00 57.25  ? 276 TYR B CE1 1 
ATOM   5407 C CE2 . TYR B 1 289 ? 113.634 108.668 113.170 1.00 54.18  ? 276 TYR B CE2 1 
ATOM   5408 C CZ  . TYR B 1 289 ? 112.553 108.767 114.013 1.00 60.54  ? 276 TYR B CZ  1 
ATOM   5409 O OH  . TYR B 1 289 ? 111.635 109.772 113.828 1.00 71.79  ? 276 TYR B OH  1 
ATOM   5410 N N   . TYR B 1 290 ? 118.467 104.549 115.604 1.00 38.38  ? 277 TYR B N   1 
ATOM   5411 C CA  . TYR B 1 290 ? 119.328 103.689 116.406 1.00 39.67  ? 277 TYR B CA  1 
ATOM   5412 C C   . TYR B 1 290 ? 119.911 104.457 117.583 1.00 41.98  ? 277 TYR B C   1 
ATOM   5413 O O   . TYR B 1 290 ? 120.002 103.933 118.699 1.00 45.83  ? 277 TYR B O   1 
ATOM   5414 C CB  . TYR B 1 290 ? 120.441 103.099 115.541 1.00 42.42  ? 277 TYR B CB  1 
ATOM   5415 C CG  . TYR B 1 290 ? 121.475 102.335 116.332 1.00 44.92  ? 277 TYR B CG  1 
ATOM   5416 C CD1 . TYR B 1 290 ? 121.104 101.294 117.173 1.00 44.61  ? 277 TYR B CD1 1 
ATOM   5417 C CD2 . TYR B 1 290 ? 122.824 102.647 116.235 1.00 44.18  ? 277 TYR B CD2 1 
ATOM   5418 C CE1 . TYR B 1 290 ? 122.047 100.593 117.899 1.00 46.42  ? 277 TYR B CE1 1 
ATOM   5419 C CE2 . TYR B 1 290 ? 123.774 101.947 116.957 1.00 47.80  ? 277 TYR B CE2 1 
ATOM   5420 C CZ  . TYR B 1 290 ? 123.378 100.923 117.786 1.00 49.86  ? 277 TYR B CZ  1 
ATOM   5421 O OH  . TYR B 1 290 ? 124.309 100.220 118.509 1.00 51.42  ? 277 TYR B OH  1 
ATOM   5422 N N   . LEU B 1 291 ? 120.326 105.703 117.347 1.00 40.83  ? 278 LEU B N   1 
ATOM   5423 C CA  . LEU B 1 291 ? 120.835 106.531 118.436 1.00 42.49  ? 278 LEU B CA  1 
ATOM   5424 C C   . LEU B 1 291 ? 119.748 106.832 119.461 1.00 44.00  ? 278 LEU B C   1 
ATOM   5425 O O   . LEU B 1 291 ? 120.010 106.846 120.668 1.00 42.84  ? 278 LEU B O   1 
ATOM   5426 C CB  . LEU B 1 291 ? 121.418 107.828 117.876 1.00 42.09  ? 278 LEU B CB  1 
ATOM   5427 C CG  . LEU B 1 291 ? 121.989 108.823 118.883 1.00 41.52  ? 278 LEU B CG  1 
ATOM   5428 C CD1 . LEU B 1 291 ? 123.415 109.186 118.510 1.00 35.30  ? 278 LEU B CD1 1 
ATOM   5429 C CD2 . LEU B 1 291 ? 121.120 110.067 118.953 1.00 44.00  ? 278 LEU B CD2 1 
ATOM   5430 N N   . MET B 1 292 ? 118.523 107.081 118.999 1.00 44.94  ? 279 MET B N   1 
ATOM   5431 C CA  . MET B 1 292 ? 117.432 107.429 119.898 1.00 44.11  ? 279 MET B CA  1 
ATOM   5432 C C   . MET B 1 292 ? 116.791 106.220 120.569 1.00 44.11  ? 279 MET B C   1 
ATOM   5433 O O   . MET B 1 292 ? 116.061 106.396 121.550 1.00 44.42  ? 279 MET B O   1 
ATOM   5434 C CB  . MET B 1 292 ? 116.363 108.214 119.135 1.00 43.93  ? 279 MET B CB  1 
ATOM   5435 C CG  . MET B 1 292 ? 116.689 109.685 118.948 1.00 44.00  ? 279 MET B CG  1 
ATOM   5436 S SD  . MET B 1 292 ? 115.686 110.467 117.671 1.00 57.49  ? 279 MET B SD  1 
ATOM   5437 C CE  . MET B 1 292 ? 114.111 109.646 117.912 1.00 50.85  ? 279 MET B CE  1 
ATOM   5438 N N   . SER B 1 293 ? 117.036 105.007 120.074 1.00 42.51  ? 280 SER B N   1 
ATOM   5439 C CA  . SER B 1 293 ? 116.401 103.821 120.630 1.00 42.17  ? 280 SER B CA  1 
ATOM   5440 C C   . SER B 1 293 ? 117.377 102.781 121.163 1.00 45.98  ? 280 SER B C   1 
ATOM   5441 O O   . SER B 1 293 ? 116.930 101.736 121.650 1.00 48.94  ? 280 SER B O   1 
ATOM   5442 C CB  . SER B 1 293 ? 115.492 103.166 119.581 1.00 48.58  ? 280 SER B CB  1 
ATOM   5443 O OG  . SER B 1 293 ? 114.418 104.022 119.234 1.00 52.63  ? 280 SER B OG  1 
ATOM   5444 N N   . ALA B 1 294 ? 118.683 103.020 121.087 1.00 44.78  ? 281 ALA B N   1 
ATOM   5445 C CA  . ALA B 1 294 ? 119.636 102.066 121.637 1.00 50.02  ? 281 ALA B CA  1 
ATOM   5446 C C   . ALA B 1 294 ? 119.531 102.032 123.156 1.00 54.33  ? 281 ALA B C   1 
ATOM   5447 O O   . ALA B 1 294 ? 119.389 103.068 123.808 1.00 54.36  ? 281 ALA B O   1 
ATOM   5448 C CB  . ALA B 1 294 ? 121.061 102.422 121.218 1.00 46.81  ? 281 ALA B CB  1 
ATOM   5449 N N   . VAL B 1 295 ? 119.601 100.826 123.719 1.00 53.87  ? 282 VAL B N   1 
ATOM   5450 C CA  . VAL B 1 295 ? 119.475 100.621 125.155 1.00 55.37  ? 282 VAL B CA  1 
ATOM   5451 C C   . VAL B 1 295 ? 120.664 99.805  125.641 1.00 57.86  ? 282 VAL B C   1 
ATOM   5452 O O   . VAL B 1 295 ? 121.325 99.104  124.872 1.00 57.59  ? 282 VAL B O   1 
ATOM   5453 C CB  . VAL B 1 295 ? 118.155 99.918  125.533 1.00 58.01  ? 282 VAL B CB  1 
ATOM   5454 C CG1 . VAL B 1 295 ? 116.960 100.729 125.058 1.00 57.32  ? 282 VAL B CG1 1 
ATOM   5455 C CG2 . VAL B 1 295 ? 118.117 98.515  124.953 1.00 59.73  ? 282 VAL B CG2 1 
ATOM   5456 N N   . GLN B 1 296 ? 120.937 99.910  126.940 1.00 61.75  ? 283 GLN B N   1 
ATOM   5457 C CA  . GLN B 1 296 ? 121.998 99.119  127.538 1.00 65.66  ? 283 GLN B CA  1 
ATOM   5458 C C   . GLN B 1 296 ? 121.472 98.395  128.770 1.00 70.57  ? 283 GLN B C   1 
ATOM   5459 O O   . GLN B 1 296 ? 120.671 98.954  129.531 1.00 70.87  ? 283 GLN B O   1 
ATOM   5460 C CB  . GLN B 1 296 ? 123.211 99.997  127.907 1.00 61.77  ? 283 GLN B CB  1 
ATOM   5461 C CG  . GLN B 1 296 ? 123.268 100.505 129.347 1.00 61.64  ? 283 GLN B CG  1 
ATOM   5462 C CD  . GLN B 1 296 ? 122.304 101.645 129.621 1.00 58.93  ? 283 GLN B CD  1 
ATOM   5463 O OE1 . GLN B 1 296 ? 121.381 101.895 128.849 1.00 60.08  ? 283 GLN B OE1 1 
ATOM   5464 N NE2 . GLN B 1 296 ? 122.521 102.347 130.726 1.00 57.46  ? 283 GLN B NE2 1 
ATOM   5465 N N   . PRO B 1 297 ? 121.865 97.137  128.965 1.00 72.55  ? 284 PRO B N   1 
ATOM   5466 C CA  . PRO B 1 297 ? 121.474 96.428  130.186 1.00 73.84  ? 284 PRO B CA  1 
ATOM   5467 C C   . PRO B 1 297 ? 122.091 97.079  131.413 1.00 77.80  ? 284 PRO B C   1 
ATOM   5468 O O   . PRO B 1 297 ? 123.206 97.602  131.372 1.00 74.63  ? 284 PRO B O   1 
ATOM   5469 C CB  . PRO B 1 297 ? 122.018 95.010  129.967 1.00 79.51  ? 284 PRO B CB  1 
ATOM   5470 C CG  . PRO B 1 297 ? 122.213 94.898  128.489 1.00 77.47  ? 284 PRO B CG  1 
ATOM   5471 C CD  . PRO B 1 297 ? 122.605 96.269  128.037 1.00 75.12  ? 284 PRO B CD  1 
ATOM   5472 N N   . LEU B 1 298 ? 121.347 97.039  132.515 1.00 84.22  ? 285 LEU B N   1 
ATOM   5473 C CA  . LEU B 1 298 ? 121.793 97.684  133.742 1.00 84.35  ? 285 LEU B CA  1 
ATOM   5474 C C   . LEU B 1 298 ? 122.957 96.918  134.359 1.00 84.06  ? 285 LEU B C   1 
ATOM   5475 O O   . LEU B 1 298 ? 122.952 95.684  134.403 1.00 79.73  ? 285 LEU B O   1 
ATOM   5476 C CB  . LEU B 1 298 ? 120.634 97.787  134.733 1.00 81.39  ? 285 LEU B CB  1 
ATOM   5477 C CG  . LEU B 1 298 ? 120.934 98.532  136.032 1.00 82.54  ? 285 LEU B CG  1 
ATOM   5478 C CD1 . LEU B 1 298 ? 121.528 99.895  135.730 1.00 82.91  ? 285 LEU B CD1 1 
ATOM   5479 C CD2 . LEU B 1 298 ? 119.680 98.669  136.876 1.00 84.21  ? 285 LEU B CD2 1 
ATOM   5480 N N   . ASN B 1 299 ? 123.957 97.655  134.838 1.00 86.01  ? 286 ASN B N   1 
ATOM   5481 C CA  . ASN B 1 299 ? 125.116 97.082  135.511 1.00 90.80  ? 286 ASN B CA  1 
ATOM   5482 C C   . ASN B 1 299 ? 125.029 97.461  136.980 1.00 90.93  ? 286 ASN B C   1 
ATOM   5483 O O   . ASN B 1 299 ? 124.928 98.646  137.313 1.00 88.47  ? 286 ASN B O   1 
ATOM   5484 C CB  . ASN B 1 299 ? 126.423 97.586  134.892 1.00 94.33  ? 286 ASN B CB  1 
ATOM   5485 C CG  . ASN B 1 299 ? 127.594 96.653  135.151 1.00 97.63  ? 286 ASN B CG  1 
ATOM   5486 O OD1 . ASN B 1 299 ? 127.429 95.558  135.688 1.00 98.32  ? 286 ASN B OD1 1 
ATOM   5487 N ND2 . ASN B 1 299 ? 128.789 97.089  134.756 1.00 101.06 ? 286 ASN B ND2 1 
ATOM   5488 N N   . ILE B 1 300 ? 125.050 96.452  137.854 1.00 93.14  ? 287 ILE B N   1 
ATOM   5489 C CA  . ILE B 1 300 ? 124.787 96.691  139.267 1.00 88.77  ? 287 ILE B CA  1 
ATOM   5490 C C   . ILE B 1 300 ? 125.913 97.469  139.932 1.00 85.22  ? 287 ILE B C   1 
ATOM   5491 O O   . ILE B 1 300 ? 125.695 98.098  140.973 1.00 84.20  ? 287 ILE B O   1 
ATOM   5492 C CB  . ILE B 1 300 ? 124.536 95.355  139.992 1.00 87.03  ? 287 ILE B CB  1 
ATOM   5493 C CG1 . ILE B 1 300 ? 123.692 95.579  141.248 1.00 79.59  ? 287 ILE B CG1 1 
ATOM   5494 C CG2 . ILE B 1 300 ? 125.848 94.676  140.341 1.00 88.66  ? 287 ILE B CG2 1 
ATOM   5495 C CD1 . ILE B 1 300 ? 122.275 96.012  140.957 1.00 71.21  ? 287 ILE B CD1 1 
ATOM   5496 N N   . SER B 1 301 ? 127.116 97.456  139.353 1.00 88.94  ? 288 SER B N   1 
ATOM   5497 C CA  . SER B 1 301 ? 128.217 98.210  139.937 1.00 91.20  ? 288 SER B CA  1 
ATOM   5498 C C   . SER B 1 301 ? 127.964 99.711  139.889 1.00 90.38  ? 288 SER B C   1 
ATOM   5499 O O   . SER B 1 301 ? 128.320 100.423 140.831 1.00 85.66  ? 288 SER B O   1 
ATOM   5500 C CB  . SER B 1 301 ? 129.529 97.865  139.233 1.00 93.18  ? 288 SER B CB  1 
ATOM   5501 O OG  . SER B 1 301 ? 130.101 96.693  139.783 1.00 90.67  ? 288 SER B OG  1 
ATOM   5502 N N   . GLN B 1 302 ? 127.349 100.209 138.815 1.00 93.62  ? 289 GLN B N   1 
ATOM   5503 C CA  . GLN B 1 302 ? 127.119 101.647 138.699 1.00 90.25  ? 289 GLN B CA  1 
ATOM   5504 C C   . GLN B 1 302 ? 126.152 102.139 139.771 1.00 85.07  ? 289 GLN B C   1 
ATOM   5505 O O   . GLN B 1 302 ? 126.416 103.138 140.453 1.00 85.44  ? 289 GLN B O   1 
ATOM   5506 C CB  . GLN B 1 302 ? 126.598 101.981 137.300 1.00 88.30  ? 289 GLN B CB  1 
ATOM   5507 C CG  . GLN B 1 302 ? 127.292 101.213 136.185 1.00 89.42  ? 289 GLN B CG  1 
ATOM   5508 C CD  . GLN B 1 302 ? 128.801 101.363 136.218 1.00 88.38  ? 289 GLN B CD  1 
ATOM   5509 O OE1 . GLN B 1 302 ? 129.325 102.448 136.467 1.00 82.85  ? 289 GLN B OE1 1 
ATOM   5510 N NE2 . GLN B 1 302 ? 129.509 100.268 135.966 1.00 92.88  ? 289 GLN B NE2 1 
ATOM   5511 N N   . VAL B 1 303 ? 125.023 101.446 139.937 1.00 85.02  ? 290 VAL B N   1 
ATOM   5512 C CA  . VAL B 1 303 ? 124.068 101.838 140.970 1.00 88.39  ? 290 VAL B CA  1 
ATOM   5513 C C   . VAL B 1 303 ? 124.650 101.601 142.360 1.00 86.28  ? 290 VAL B C   1 
ATOM   5514 O O   . VAL B 1 303 ? 124.405 102.384 143.289 1.00 83.33  ? 290 VAL B O   1 
ATOM   5515 C CB  . VAL B 1 303 ? 122.725 101.108 140.768 1.00 84.43  ? 290 VAL B CB  1 
ATOM   5516 C CG1 . VAL B 1 303 ? 122.921 99.605  140.743 1.00 83.36  ? 290 VAL B CG1 1 
ATOM   5517 C CG2 . VAL B 1 303 ? 121.726 101.508 141.846 1.00 80.51  ? 290 VAL B CG2 1 
ATOM   5518 N N   . PHE B 1 304 ? 125.439 100.538 142.526 1.00 84.03  ? 291 PHE B N   1 
ATOM   5519 C CA  . PHE B 1 304 ? 126.075 100.280 143.812 1.00 81.50  ? 291 PHE B CA  1 
ATOM   5520 C C   . PHE B 1 304 ? 127.047 101.395 144.180 1.00 83.78  ? 291 PHE B C   1 
ATOM   5521 O O   . PHE B 1 304 ? 127.163 101.765 145.353 1.00 84.03  ? 291 PHE B O   1 
ATOM   5522 C CB  . PHE B 1 304 ? 126.786 98.929  143.773 1.00 84.35  ? 291 PHE B CB  1 
ATOM   5523 C CG  . PHE B 1 304 ? 127.254 98.451  145.113 1.00 82.57  ? 291 PHE B CG  1 
ATOM   5524 C CD1 . PHE B 1 304 ? 126.345 98.181  146.119 1.00 81.24  ? 291 PHE B CD1 1 
ATOM   5525 C CD2 . PHE B 1 304 ? 128.602 98.257  145.362 1.00 83.66  ? 291 PHE B CD2 1 
ATOM   5526 C CE1 . PHE B 1 304 ? 126.771 97.735  147.351 1.00 79.49  ? 291 PHE B CE1 1 
ATOM   5527 C CE2 . PHE B 1 304 ? 129.033 97.811  146.593 1.00 86.34  ? 291 PHE B CE2 1 
ATOM   5528 C CZ  . PHE B 1 304 ? 128.115 97.550  147.590 1.00 83.73  ? 291 PHE B CZ  1 
ATOM   5529 N N   . ASP B 1 305 ? 127.757 101.939 143.192 1.00 86.74  ? 292 ASP B N   1 
ATOM   5530 C CA  . ASP B 1 305 ? 128.685 103.032 143.454 1.00 87.34  ? 292 ASP B CA  1 
ATOM   5531 C C   . ASP B 1 305 ? 127.970 104.359 143.667 1.00 82.65  ? 292 ASP B C   1 
ATOM   5532 O O   . ASP B 1 305 ? 128.418 105.170 144.484 1.00 78.33  ? 292 ASP B O   1 
ATOM   5533 C CB  . ASP B 1 305 ? 129.687 103.161 142.305 1.00 93.10  ? 292 ASP B CB  1 
ATOM   5534 C CG  . ASP B 1 305 ? 130.617 101.970 142.210 1.00 92.74  ? 292 ASP B CG  1 
ATOM   5535 O OD1 . ASP B 1 305 ? 130.426 101.003 142.976 1.00 89.49  ? 292 ASP B OD1 1 
ATOM   5536 O OD2 . ASP B 1 305 ? 131.542 102.002 141.371 1.00 95.93  ? 292 ASP B OD2 1 
ATOM   5537 N N   . GLU B 1 306 ? 126.872 104.607 142.947 1.00 82.04  ? 293 GLU B N   1 
ATOM   5538 C CA  . GLU B 1 306 ? 126.141 105.850 143.171 1.00 78.64  ? 293 GLU B CA  1 
ATOM   5539 C C   . GLU B 1 306 ? 125.445 105.851 144.528 1.00 76.02  ? 293 GLU B C   1 
ATOM   5540 O O   . GLU B 1 306 ? 125.272 106.917 145.130 1.00 77.10  ? 293 GLU B O   1 
ATOM   5541 C CB  . GLU B 1 306 ? 125.141 106.108 142.038 1.00 79.35  ? 293 GLU B CB  1 
ATOM   5542 C CG  . GLU B 1 306 ? 123.931 105.188 141.988 1.00 78.55  ? 293 GLU B CG  1 
ATOM   5543 C CD  . GLU B 1 306 ? 122.807 105.623 142.907 1.00 71.26  ? 293 GLU B CD  1 
ATOM   5544 O OE1 . GLU B 1 306 ? 122.789 106.806 143.307 1.00 71.07  ? 293 GLU B OE1 1 
ATOM   5545 O OE2 . GLU B 1 306 ? 121.947 104.780 143.237 1.00 68.43  ? 293 GLU B OE2 1 
ATOM   5546 N N   . VAL B 1 307 ? 125.035 104.680 145.022 1.00 75.89  ? 294 VAL B N   1 
ATOM   5547 C CA  . VAL B 1 307 ? 124.456 104.626 146.361 1.00 76.93  ? 294 VAL B CA  1 
ATOM   5548 C C   . VAL B 1 307 ? 125.528 104.577 147.445 1.00 75.70  ? 294 VAL B C   1 
ATOM   5549 O O   . VAL B 1 307 ? 125.250 104.932 148.597 1.00 72.55  ? 294 VAL B O   1 
ATOM   5550 C CB  . VAL B 1 307 ? 123.499 103.428 146.494 1.00 79.74  ? 294 VAL B CB  1 
ATOM   5551 C CG1 . VAL B 1 307 ? 124.270 102.124 146.631 1.00 82.74  ? 294 VAL B CG1 1 
ATOM   5552 C CG2 . VAL B 1 307 ? 122.550 103.628 147.668 1.00 67.10  ? 294 VAL B CG2 1 
ATOM   5553 N N   . ASP B 1 308 ? 126.751 104.159 147.107 1.00 76.91  ? 295 ASP B N   1 
ATOM   5554 C CA  . ASP B 1 308 ? 127.857 104.103 148.065 1.00 74.19  ? 295 ASP B CA  1 
ATOM   5555 C C   . ASP B 1 308 ? 128.567 105.453 148.060 1.00 76.46  ? 295 ASP B C   1 
ATOM   5556 O O   . ASP B 1 308 ? 129.602 105.654 147.422 1.00 79.12  ? 295 ASP B O   1 
ATOM   5557 C CB  . ASP B 1 308 ? 128.808 102.963 147.722 1.00 74.91  ? 295 ASP B CB  1 
ATOM   5558 C CG  . ASP B 1 308 ? 129.893 102.774 148.761 1.00 84.51  ? 295 ASP B CG  1 
ATOM   5559 O OD1 . ASP B 1 308 ? 129.788 103.373 149.852 1.00 86.52  ? 295 ASP B OD1 1 
ATOM   5560 O OD2 . ASP B 1 308 ? 130.856 102.026 148.487 1.00 86.09  ? 295 ASP B OD2 1 
ATOM   5561 N N   . THR B 1 309 ? 127.981 106.400 148.794 1.00 75.30  ? 296 THR B N   1 
ATOM   5562 C CA  . THR B 1 309 ? 128.538 107.746 148.859 1.00 74.01  ? 296 THR B CA  1 
ATOM   5563 C C   . THR B 1 309 ? 129.912 107.748 149.519 1.00 76.09  ? 296 THR B C   1 
ATOM   5564 O O   . THR B 1 309 ? 130.792 108.526 149.134 1.00 75.48  ? 296 THR B O   1 
ATOM   5565 C CB  . THR B 1 309 ? 127.578 108.662 149.611 1.00 72.63  ? 296 THR B CB  1 
ATOM   5566 O OG1 . THR B 1 309 ? 127.497 108.245 150.979 1.00 76.73  ? 296 THR B OG1 1 
ATOM   5567 C CG2 . THR B 1 309 ? 126.190 108.588 148.994 1.00 68.04  ? 296 THR B CG2 1 
ATOM   5568 N N   . ASP B 1 310 ? 130.109 106.886 150.518 1.00 78.09  ? 297 ASP B N   1 
ATOM   5569 C CA  . ASP B 1 310 ? 131.362 106.847 151.265 1.00 79.91  ? 297 ASP B CA  1 
ATOM   5570 C C   . ASP B 1 310 ? 132.521 106.327 150.420 1.00 81.95  ? 297 ASP B C   1 
ATOM   5571 O O   . ASP B 1 310 ? 133.683 106.605 150.735 1.00 81.30  ? 297 ASP B O   1 
ATOM   5572 C CB  . ASP B 1 310 ? 131.174 105.984 152.514 1.00 82.26  ? 297 ASP B CB  1 
ATOM   5573 C CG  . ASP B 1 310 ? 132.257 106.202 153.553 1.00 86.21  ? 297 ASP B CG  1 
ATOM   5574 O OD1 . ASP B 1 310 ? 133.425 105.851 153.297 1.00 85.31  ? 297 ASP B OD1 1 
ATOM   5575 O OD2 . ASP B 1 310 ? 131.931 106.722 154.641 1.00 90.40  ? 297 ASP B OD2 1 
ATOM   5576 N N   . GLN B 1 311 ? 132.228 105.573 149.357 1.00 81.76  ? 298 GLN B N   1 
ATOM   5577 C CA  . GLN B 1 311 ? 133.251 104.896 148.555 1.00 80.11  ? 298 GLN B CA  1 
ATOM   5578 C C   . GLN B 1 311 ? 134.080 103.951 149.419 1.00 83.28  ? 298 GLN B C   1 
ATOM   5579 O O   . GLN B 1 311 ? 135.296 103.831 149.256 1.00 83.51  ? 298 GLN B O   1 
ATOM   5580 C CB  . GLN B 1 311 ? 134.148 105.895 147.817 1.00 79.29  ? 298 GLN B CB  1 
ATOM   5581 C CG  . GLN B 1 311 ? 133.754 106.138 146.368 1.00 86.57  ? 298 GLN B CG  1 
ATOM   5582 C CD  . GLN B 1 311 ? 134.051 104.949 145.473 1.00 94.76  ? 298 GLN B CD  1 
ATOM   5583 O OE1 . GLN B 1 311 ? 134.929 104.138 145.769 1.00 98.14  ? 298 GLN B OE1 1 
ATOM   5584 N NE2 . GLN B 1 311 ? 133.318 104.839 144.370 1.00 92.69  ? 298 GLN B NE2 1 
ATOM   5585 N N   . SER B 1 312 ? 133.411 103.277 150.354 1.00 83.12  ? 299 SER B N   1 
ATOM   5586 C CA  . SER B 1 312 ? 134.055 102.323 151.242 1.00 82.84  ? 299 SER B CA  1 
ATOM   5587 C C   . SER B 1 312 ? 133.706 100.876 150.926 1.00 87.53  ? 299 SER B C   1 
ATOM   5588 O O   . SER B 1 312 ? 134.374 99.971  151.437 1.00 82.73  ? 299 SER B O   1 
ATOM   5589 C CB  . SER B 1 312 ? 133.685 102.624 152.702 1.00 81.50  ? 299 SER B CB  1 
ATOM   5590 O OG  . SER B 1 312 ? 132.288 102.500 152.913 1.00 82.82  ? 299 SER B OG  1 
ATOM   5591 N N   . GLY B 1 313 ? 132.688 100.635 150.103 1.00 87.19  ? 300 GLY B N   1 
ATOM   5592 C CA  . GLY B 1 313 ? 132.269 99.293  149.768 1.00 84.89  ? 300 GLY B CA  1 
ATOM   5593 C C   . GLY B 1 313 ? 131.277 98.672  150.725 1.00 84.69  ? 300 GLY B C   1 
ATOM   5594 O O   . GLY B 1 313 ? 130.794 97.565  150.456 1.00 84.64  ? 300 GLY B O   1 
ATOM   5595 N N   . VAL B 1 314 ? 130.957 99.342  151.829 1.00 85.60  ? 301 VAL B N   1 
ATOM   5596 C CA  . VAL B 1 314 ? 130.004 98.847  152.815 1.00 83.83  ? 301 VAL B CA  1 
ATOM   5597 C C   . VAL B 1 314 ? 128.970 99.934  153.068 1.00 80.82  ? 301 VAL B C   1 
ATOM   5598 O O   . VAL B 1 314 ? 129.311 101.118 153.162 1.00 80.10  ? 301 VAL B O   1 
ATOM   5599 C CB  . VAL B 1 314 ? 130.700 98.433  154.130 1.00 84.79  ? 301 VAL B CB  1 
ATOM   5600 C CG1 . VAL B 1 314 ? 129.695 97.833  155.101 1.00 83.18  ? 301 VAL B CG1 1 
ATOM   5601 C CG2 . VAL B 1 314 ? 131.824 97.447  153.852 1.00 85.20  ? 301 VAL B CG2 1 
ATOM   5602 N N   . LEU B 1 315 ? 127.706 99.532  153.172 1.00 74.70  ? 302 LEU B N   1 
ATOM   5603 C CA  . LEU B 1 315 ? 126.595 100.466 153.295 1.00 70.60  ? 302 LEU B CA  1 
ATOM   5604 C C   . LEU B 1 315 ? 126.135 100.559 154.743 1.00 71.14  ? 302 LEU B C   1 
ATOM   5605 O O   . LEU B 1 315 ? 125.848 99.539  155.377 1.00 71.06  ? 302 LEU B O   1 
ATOM   5606 C CB  . LEU B 1 315 ? 125.424 100.043 152.405 1.00 68.52  ? 302 LEU B CB  1 
ATOM   5607 C CG  . LEU B 1 315 ? 125.510 100.392 150.917 1.00 73.67  ? 302 LEU B CG  1 
ATOM   5608 C CD1 . LEU B 1 315 ? 126.573 99.567  150.215 1.00 74.14  ? 302 LEU B CD1 1 
ATOM   5609 C CD2 . LEU B 1 315 ? 124.156 100.221 150.244 1.00 72.11  ? 302 LEU B CD2 1 
ATOM   5610 N N   . SER B 1 316 ? 126.061 101.783 155.255 1.00 70.58  ? 303 SER B N   1 
ATOM   5611 C CA  . SER B 1 316 ? 125.535 102.041 156.585 1.00 67.35  ? 303 SER B CA  1 
ATOM   5612 C C   . SER B 1 316 ? 124.017 102.195 156.501 1.00 66.88  ? 303 SER B C   1 
ATOM   5613 O O   . SER B 1 316 ? 123.401 101.917 155.469 1.00 68.83  ? 303 SER B O   1 
ATOM   5614 C CB  . SER B 1 316 ? 126.207 103.273 157.188 1.00 61.57  ? 303 SER B CB  1 
ATOM   5615 O OG  . SER B 1 316 ? 125.963 104.424 156.399 1.00 61.52  ? 303 SER B OG  1 
ATOM   5616 N N   . ASP B 1 317 ? 123.394 102.636 157.596 1.00 66.38  ? 304 ASP B N   1 
ATOM   5617 C CA  . ASP B 1 317 ? 121.948 102.830 157.592 1.00 65.65  ? 304 ASP B CA  1 
ATOM   5618 C C   . ASP B 1 317 ? 121.534 103.906 156.596 1.00 64.76  ? 304 ASP B C   1 
ATOM   5619 O O   . ASP B 1 317 ? 120.495 103.783 155.937 1.00 66.29  ? 304 ASP B O   1 
ATOM   5620 C CB  . ASP B 1 317 ? 121.459 103.185 158.995 1.00 73.09  ? 304 ASP B CB  1 
ATOM   5621 C CG  . ASP B 1 317 ? 121.291 101.967 159.876 1.00 86.06  ? 304 ASP B CG  1 
ATOM   5622 O OD1 . ASP B 1 317 ? 120.859 100.917 159.358 1.00 85.69  ? 304 ASP B OD1 1 
ATOM   5623 O OD2 . ASP B 1 317 ? 121.590 102.059 161.086 1.00 90.50  ? 304 ASP B OD2 1 
ATOM   5624 N N   . ARG B 1 318 ? 122.328 104.973 156.482 1.00 62.02  ? 305 ARG B N   1 
ATOM   5625 C CA  . ARG B 1 318 ? 121.995 106.055 155.560 1.00 61.37  ? 305 ARG B CA  1 
ATOM   5626 C C   . ARG B 1 318 ? 121.981 105.563 154.116 1.00 61.12  ? 305 ARG B C   1 
ATOM   5627 O O   . ARG B 1 318 ? 121.056 105.863 153.350 1.00 59.55  ? 305 ARG B O   1 
ATOM   5628 C CB  . ARG B 1 318 ? 122.991 107.203 155.730 1.00 60.51  ? 305 ARG B CB  1 
ATOM   5629 C CG  . ARG B 1 318 ? 123.113 107.740 157.152 1.00 64.50  ? 305 ARG B CG  1 
ATOM   5630 C CD  . ARG B 1 318 ? 124.127 108.879 157.219 1.00 65.84  ? 305 ARG B CD  1 
ATOM   5631 N NE  . ARG B 1 318 ? 124.201 109.498 158.538 1.00 64.77  ? 305 ARG B NE  1 
ATOM   5632 C CZ  . ARG B 1 318 ? 125.184 109.306 159.408 1.00 63.41  ? 305 ARG B CZ  1 
ATOM   5633 N NH1 . ARG B 1 318 ? 126.203 108.508 159.136 1.00 63.13  ? 305 ARG B NH1 1 
ATOM   5634 N NH2 . ARG B 1 318 ? 125.146 109.936 160.579 1.00 62.84  ? 305 ARG B NH2 1 
ATOM   5635 N N   . GLU B 1 319 ? 122.996 104.789 153.730 1.00 61.05  ? 306 GLU B N   1 
ATOM   5636 C CA  . GLU B 1 319 ? 123.062 104.280 152.364 1.00 59.73  ? 306 GLU B CA  1 
ATOM   5637 C C   . GLU B 1 319 ? 121.974 103.245 152.101 1.00 62.97  ? 306 GLU B C   1 
ATOM   5638 O O   . GLU B 1 319 ? 121.423 103.180 150.995 1.00 70.09  ? 306 GLU B O   1 
ATOM   5639 C CB  . GLU B 1 319 ? 124.448 103.696 152.100 1.00 66.75  ? 306 GLU B CB  1 
ATOM   5640 C CG  . GLU B 1 319 ? 125.549 104.743 152.023 1.00 66.27  ? 306 GLU B CG  1 
ATOM   5641 C CD  . GLU B 1 319 ? 126.865 104.251 152.589 1.00 67.80  ? 306 GLU B CD  1 
ATOM   5642 O OE1 . GLU B 1 319 ? 126.903 103.906 153.788 1.00 67.91  ? 306 GLU B OE1 1 
ATOM   5643 O OE2 . GLU B 1 319 ? 127.860 104.202 151.835 1.00 70.44  ? 306 GLU B OE2 1 
ATOM   5644 N N   . ILE B 1 320 ? 121.649 102.426 153.103 1.00 63.46  ? 307 ILE B N   1 
ATOM   5645 C CA  . ILE B 1 320 ? 120.550 101.477 152.950 1.00 61.69  ? 307 ILE B CA  1 
ATOM   5646 C C   . ILE B 1 320 ? 119.238 102.218 152.738 1.00 61.44  ? 307 ILE B C   1 
ATOM   5647 O O   . ILE B 1 320 ? 118.418 101.830 151.897 1.00 65.93  ? 307 ILE B O   1 
ATOM   5648 C CB  . ILE B 1 320 ? 120.483 100.530 154.162 1.00 63.93  ? 307 ILE B CB  1 
ATOM   5649 C CG1 . ILE B 1 320 ? 121.665 99.564  154.137 1.00 68.94  ? 307 ILE B CG1 1 
ATOM   5650 C CG2 . ILE B 1 320 ? 119.172 99.763  154.173 1.00 62.62  ? 307 ILE B CG2 1 
ATOM   5651 C CD1 . ILE B 1 320 ? 121.823 98.839  152.821 1.00 71.10  ? 307 ILE B CD1 1 
ATOM   5652 N N   . ARG B 1 321 ? 119.018 103.297 153.492 1.00 56.84  ? 308 ARG B N   1 
ATOM   5653 C CA  . ARG B 1 321 ? 117.819 104.103 153.291 1.00 52.33  ? 308 ARG B CA  1 
ATOM   5654 C C   . ARG B 1 321 ? 117.803 104.729 151.905 1.00 55.34  ? 308 ARG B C   1 
ATOM   5655 O O   . ARG B 1 321 ? 116.744 104.826 151.276 1.00 60.01  ? 308 ARG B O   1 
ATOM   5656 C CB  . ARG B 1 321 ? 117.718 105.186 154.361 1.00 52.32  ? 308 ARG B CB  1 
ATOM   5657 C CG  . ARG B 1 321 ? 117.076 104.731 155.654 1.00 51.79  ? 308 ARG B CG  1 
ATOM   5658 C CD  . ARG B 1 321 ? 116.605 105.923 156.463 1.00 48.39  ? 308 ARG B CD  1 
ATOM   5659 N NE  . ARG B 1 321 ? 115.743 106.794 155.673 1.00 48.92  ? 308 ARG B NE  1 
ATOM   5660 C CZ  . ARG B 1 321 ? 114.423 106.684 155.612 1.00 50.51  ? 308 ARG B CZ  1 
ATOM   5661 N NH1 . ARG B 1 321 ? 113.774 105.755 156.293 1.00 57.00  ? 308 ARG B NH1 1 
ATOM   5662 N NH2 . ARG B 1 321 ? 113.737 107.529 154.848 1.00 51.73  ? 308 ARG B NH2 1 
ATOM   5663 N N   . THR B 1 322 ? 118.962 105.182 151.422 1.00 60.71  ? 309 THR B N   1 
ATOM   5664 C CA  . THR B 1 322 ? 119.027 105.751 150.078 1.00 62.59  ? 309 THR B CA  1 
ATOM   5665 C C   . THR B 1 322 ? 118.636 104.718 149.027 1.00 61.30  ? 309 THR B C   1 
ATOM   5666 O O   . THR B 1 322 ? 117.844 105.004 148.122 1.00 59.91  ? 309 THR B O   1 
ATOM   5667 C CB  . THR B 1 322 ? 120.428 106.294 149.800 1.00 59.31  ? 309 THR B CB  1 
ATOM   5668 O OG1 . THR B 1 322 ? 120.730 107.340 150.731 1.00 60.74  ? 309 THR B OG1 1 
ATOM   5669 C CG2 . THR B 1 322 ? 120.511 106.845 148.387 1.00 51.85  ? 309 THR B CG2 1 
ATOM   5670 N N   . LEU B 1 323 ? 119.170 103.501 149.143 1.00 57.76  ? 310 LEU B N   1 
ATOM   5671 C CA  . LEU B 1 323 ? 118.798 102.447 148.203 1.00 52.26  ? 310 LEU B CA  1 
ATOM   5672 C C   . LEU B 1 323 ? 117.311 102.122 148.302 1.00 60.32  ? 310 LEU B C   1 
ATOM   5673 O O   . LEU B 1 323 ? 116.630 101.962 147.279 1.00 66.33  ? 310 LEU B O   1 
ATOM   5674 C CB  . LEU B 1 323 ? 119.640 101.196 148.455 1.00 56.93  ? 310 LEU B CB  1 
ATOM   5675 C CG  . LEU B 1 323 ? 119.441 100.025 147.491 1.00 63.89  ? 310 LEU B CG  1 
ATOM   5676 C CD1 . LEU B 1 323 ? 119.791 100.428 146.068 1.00 65.66  ? 310 LEU B CD1 1 
ATOM   5677 C CD2 . LEU B 1 323 ? 120.268 98.825  147.925 1.00 61.09  ? 310 LEU B CD2 1 
ATOM   5678 N N   . ALA B 1 324 ? 116.786 102.040 149.527 1.00 63.92  ? 311 ALA B N   1 
ATOM   5679 C CA  . ALA B 1 324 ? 115.380 101.700 149.716 1.00 64.74  ? 311 ALA B CA  1 
ATOM   5680 C C   . ALA B 1 324 ? 114.464 102.755 149.110 1.00 65.21  ? 311 ALA B C   1 
ATOM   5681 O O   . ALA B 1 324 ? 113.475 102.420 148.448 1.00 68.29  ? 311 ALA B O   1 
ATOM   5682 C CB  . ALA B 1 324 ? 115.080 101.525 151.204 1.00 67.20  ? 311 ALA B CB  1 
ATOM   5683 N N   . THR B 1 325 ? 114.769 104.035 149.327 1.00 64.03  ? 312 THR B N   1 
ATOM   5684 C CA  . THR B 1 325 ? 113.940 105.090 148.764 1.00 61.29  ? 312 THR B CA  1 
ATOM   5685 C C   . THR B 1 325 ? 114.164 105.266 147.272 1.00 63.38  ? 312 THR B C   1 
ATOM   5686 O O   . THR B 1 325 ? 113.310 105.848 146.599 1.00 66.02  ? 312 THR B O   1 
ATOM   5687 C CB  . THR B 1 325 ? 114.186 106.421 149.476 1.00 57.99  ? 312 THR B CB  1 
ATOM   5688 O OG1 . THR B 1 325 ? 113.228 107.383 149.019 1.00 56.63  ? 312 THR B OG1 1 
ATOM   5689 C CG2 . THR B 1 325 ? 115.579 106.940 149.180 1.00 60.60  ? 312 THR B CG2 1 
ATOM   5690 N N   . ARG B 1 326 ? 115.291 104.787 146.743 1.00 63.96  ? 313 ARG B N   1 
ATOM   5691 C CA  . ARG B 1 326 ? 115.472 104.792 145.298 1.00 64.38  ? 313 ARG B CA  1 
ATOM   5692 C C   . ARG B 1 326 ? 114.632 103.710 144.637 1.00 63.76  ? 313 ARG B C   1 
ATOM   5693 O O   . ARG B 1 326 ? 114.022 103.943 143.588 1.00 63.58  ? 313 ARG B O   1 
ATOM   5694 C CB  . ARG B 1 326 ? 116.950 104.610 144.959 1.00 59.93  ? 313 ARG B CB  1 
ATOM   5695 C CG  . ARG B 1 326 ? 117.267 104.694 143.484 1.00 59.55  ? 313 ARG B CG  1 
ATOM   5696 C CD  . ARG B 1 326 ? 118.750 104.917 143.286 1.00 55.53  ? 313 ARG B CD  1 
ATOM   5697 N NE  . ARG B 1 326 ? 119.251 105.936 144.200 1.00 54.40  ? 313 ARG B NE  1 
ATOM   5698 C CZ  . ARG B 1 326 ? 119.143 107.242 144.002 1.00 58.74  ? 313 ARG B CZ  1 
ATOM   5699 N NH1 . ARG B 1 326 ? 118.550 107.731 142.926 1.00 64.33  ? 313 ARG B NH1 1 
ATOM   5700 N NH2 . ARG B 1 326 ? 119.642 108.079 144.908 1.00 57.31  ? 313 ARG B NH2 1 
ATOM   5701 N N   . ILE B 1 327 ? 114.575 102.529 145.245 1.00 65.02  ? 314 ILE B N   1 
ATOM   5702 C CA  . ILE B 1 327 ? 113.886 101.408 144.617 1.00 68.29  ? 314 ILE B CA  1 
ATOM   5703 C C   . ILE B 1 327 ? 112.384 101.414 144.901 1.00 71.72  ? 314 ILE B C   1 
ATOM   5704 O O   . ILE B 1 327 ? 111.590 101.056 144.025 1.00 75.21  ? 314 ILE B O   1 
ATOM   5705 C CB  . ILE B 1 327 ? 114.529 100.085 145.060 1.00 64.90  ? 314 ILE B CB  1 
ATOM   5706 C CG1 . ILE B 1 327 ? 116.027 100.099 144.757 1.00 62.17  ? 314 ILE B CG1 1 
ATOM   5707 C CG2 . ILE B 1 327 ? 113.882 98.920  144.356 1.00 70.19  ? 314 ILE B CG2 1 
ATOM   5708 C CD1 . ILE B 1 327 ? 116.355 100.488 143.333 1.00 66.53  ? 314 ILE B CD1 1 
ATOM   5709 N N   . HIS B 1 328 ? 111.971 101.825 146.093 1.00 69.58  ? 315 HIS B N   1 
ATOM   5710 C CA  . HIS B 1 328 ? 110.566 101.823 146.468 1.00 71.56  ? 315 HIS B CA  1 
ATOM   5711 C C   . HIS B 1 328 ? 109.934 103.184 146.193 1.00 77.86  ? 315 HIS B C   1 
ATOM   5712 O O   . HIS B 1 328 ? 110.609 104.159 145.855 1.00 82.68  ? 315 HIS B O   1 
ATOM   5713 C CB  . HIS B 1 328 ? 110.401 101.443 147.942 1.00 72.49  ? 315 HIS B CB  1 
ATOM   5714 C CG  . HIS B 1 328 ? 110.837 100.047 148.258 1.00 73.57  ? 315 HIS B CG  1 
ATOM   5715 N ND1 . HIS B 1 328 ? 110.576 99.442  149.468 1.00 82.87  ? 315 HIS B ND1 1 
ATOM   5716 C CD2 . HIS B 1 328 ? 111.515 99.135  147.521 1.00 73.03  ? 315 HIS B CD2 1 
ATOM   5717 C CE1 . HIS B 1 328 ? 111.075 98.219  149.464 1.00 81.85  ? 315 HIS B CE1 1 
ATOM   5718 N NE2 . HIS B 1 328 ? 111.650 98.008  148.295 1.00 73.82  ? 315 HIS B NE2 1 
ATOM   5719 N N   . GLU B 1 329 ? 108.614 103.235 146.334 1.00 81.63  ? 316 GLU B N   1 
ATOM   5720 C CA  . GLU B 1 329 ? 107.841 104.439 146.072 1.00 87.59  ? 316 GLU B CA  1 
ATOM   5721 C C   . GLU B 1 329 ? 107.444 105.115 147.379 1.00 94.23  ? 316 GLU B C   1 
ATOM   5722 O O   . GLU B 1 329 ? 107.318 104.470 148.423 1.00 94.09  ? 316 GLU B O   1 
ATOM   5723 C CB  . GLU B 1 329 ? 106.590 104.113 145.254 1.00 91.45  ? 316 GLU B CB  1 
ATOM   5724 C CG  . GLU B 1 329 ? 105.511 103.378 146.034 1.00 102.38 ? 316 GLU B CG  1 
ATOM   5725 C CD  . GLU B 1 329 ? 104.504 102.691 145.134 1.00 106.69 ? 316 GLU B CD  1 
ATOM   5726 O OE1 . GLU B 1 329 ? 104.898 101.752 144.412 1.00 108.73 ? 316 GLU B OE1 1 
ATOM   5727 O OE2 . GLU B 1 329 ? 103.322 103.092 145.145 1.00 105.26 ? 316 GLU B OE2 1 
ATOM   5728 N N   . LEU B 1 330 ? 107.260 106.431 147.312 1.00 98.65  ? 317 LEU B N   1 
ATOM   5729 C CA  . LEU B 1 330 ? 106.820 107.180 148.476 1.00 105.24 ? 317 LEU B CA  1 
ATOM   5730 C C   . LEU B 1 330 ? 105.345 106.898 148.763 1.00 108.10 ? 317 LEU B C   1 
ATOM   5731 O O   . LEU B 1 330 ? 104.576 106.582 147.850 1.00 105.84 ? 317 LEU B O   1 
ATOM   5732 C CB  . LEU B 1 330 ? 107.030 108.678 148.262 1.00 105.01 ? 317 LEU B CB  1 
ATOM   5733 C CG  . LEU B 1 330 ? 108.408 109.254 148.605 1.00 99.71  ? 317 LEU B CG  1 
ATOM   5734 C CD1 . LEU B 1 330 ? 109.460 108.834 147.590 1.00 87.11  ? 317 LEU B CD1 1 
ATOM   5735 C CD2 . LEU B 1 330 ? 108.343 110.770 148.722 1.00 93.77  ? 317 LEU B CD2 1 
ATOM   5736 N N   . PRO B 1 331 ? 104.919 107.010 150.030 1.00 114.31 ? 318 PRO B N   1 
ATOM   5737 C CA  . PRO B 1 331 ? 105.711 107.336 151.225 1.00 111.76 ? 318 PRO B CA  1 
ATOM   5738 C C   . PRO B 1 331 ? 106.380 106.107 151.831 1.00 112.61 ? 318 PRO B C   1 
ATOM   5739 O O   . PRO B 1 331 ? 105.707 105.157 152.220 1.00 114.13 ? 318 PRO B O   1 
ATOM   5740 C CB  . PRO B 1 331 ? 104.662 107.946 152.163 1.00 111.06 ? 318 PRO B CB  1 
ATOM   5741 C CG  . PRO B 1 331 ? 103.399 107.205 151.822 1.00 114.90 ? 318 PRO B CG  1 
ATOM   5742 C CD  . PRO B 1 331 ? 103.480 106.915 150.338 1.00 115.87 ? 318 PRO B CD  1 
ATOM   5743 N N   . LEU B 1 332 ? 107.707 106.089 151.917 1.00 108.72 ? 319 LEU B N   1 
ATOM   5744 C CA  . LEU B 1 332 ? 108.401 104.952 152.504 1.00 107.61 ? 319 LEU B CA  1 
ATOM   5745 C C   . LEU B 1 332 ? 108.150 104.908 154.005 1.00 110.60 ? 319 LEU B C   1 
ATOM   5746 O O   . LEU B 1 332 ? 108.266 105.924 154.697 1.00 110.90 ? 319 LEU B O   1 
ATOM   5747 C CB  . LEU B 1 332 ? 109.899 105.033 152.211 1.00 100.16 ? 319 LEU B CB  1 
ATOM   5748 C CG  . LEU B 1 332 ? 110.723 103.759 152.416 1.00 93.15  ? 319 LEU B CG  1 
ATOM   5749 C CD1 . LEU B 1 332 ? 111.862 103.705 151.420 1.00 75.95  ? 319 LEU B CD1 1 
ATOM   5750 C CD2 . LEU B 1 332 ? 111.266 103.669 153.832 1.00 92.38  ? 319 LEU B CD2 1 
ATOM   5751 N N   . SER B 1 333 ? 107.804 103.731 154.508 1.00 110.73 ? 320 SER B N   1 
ATOM   5752 C CA  . SER B 1 333 ? 107.518 103.533 155.921 1.00 113.83 ? 320 SER B CA  1 
ATOM   5753 C C   . SER B 1 333 ? 108.498 102.519 156.494 1.00 112.74 ? 320 SER B C   1 
ATOM   5754 O O   . SER B 1 333 ? 109.315 101.933 155.782 1.00 107.74 ? 320 SER B O   1 
ATOM   5755 C CB  . SER B 1 333 ? 106.068 103.077 156.125 1.00 115.56 ? 320 SER B CB  1 
ATOM   5756 O OG  . SER B 1 333 ? 105.737 102.988 157.501 1.00 115.60 ? 320 SER B OG  1 
ATOM   5757 N N   . LEU B 1 334 ? 108.397 102.306 157.803 1.00 114.70 ? 321 LEU B N   1 
ATOM   5758 C CA  . LEU B 1 334 ? 109.285 101.364 158.471 1.00 113.02 ? 321 LEU B CA  1 
ATOM   5759 C C   . LEU B 1 334 ? 109.088 99.934  157.981 1.00 113.17 ? 321 LEU B C   1 
ATOM   5760 O O   . LEU B 1 334 ? 110.019 99.132  158.077 1.00 112.25 ? 321 LEU B O   1 
ATOM   5761 C CB  . LEU B 1 334 ? 109.082 101.434 159.986 1.00 114.52 ? 321 LEU B CB  1 
ATOM   5762 C CG  . LEU B 1 334 ? 107.826 100.772 160.564 1.00 117.52 ? 321 LEU B CG  1 
ATOM   5763 C CD1 . LEU B 1 334 ? 107.973 100.525 162.058 1.00 121.79 ? 321 LEU B CD1 1 
ATOM   5764 C CD2 . LEU B 1 334 ? 106.578 101.597 160.293 1.00 113.47 ? 321 LEU B CD2 1 
ATOM   5765 N N   . GLN B 1 335 ? 107.905 99.599  157.450 1.00 113.54 ? 322 GLN B N   1 
ATOM   5766 C CA  . GLN B 1 335 ? 107.650 98.234  156.988 1.00 110.28 ? 322 GLN B CA  1 
ATOM   5767 C C   . GLN B 1 335 ? 108.570 97.857  155.834 1.00 108.45 ? 322 GLN B C   1 
ATOM   5768 O O   . GLN B 1 335 ? 109.095 96.739  155.788 1.00 104.78 ? 322 GLN B O   1 
ATOM   5769 C CB  . GLN B 1 335 ? 106.188 98.076  156.565 1.00 110.47 ? 322 GLN B CB  1 
ATOM   5770 C CG  . GLN B 1 335 ? 105.618 96.647  156.629 1.00 115.31 ? 322 GLN B CG  1 
ATOM   5771 C CD  . GLN B 1 335 ? 106.022 95.751  155.457 1.00 117.13 ? 322 GLN B CD  1 
ATOM   5772 O OE1 . GLN B 1 335 ? 105.865 96.121  154.288 1.00 121.35 ? 322 GLN B OE1 1 
ATOM   5773 N NE2 . GLN B 1 335 ? 106.515 94.555  155.771 1.00 111.42 ? 322 GLN B NE2 1 
ATOM   5774 N N   . ASP B 1 336 ? 108.773 98.776  154.887 1.00 110.07 ? 323 ASP B N   1 
ATOM   5775 C CA  . ASP B 1 336 ? 109.630 98.484  153.742 1.00 105.40 ? 323 ASP B CA  1 
ATOM   5776 C C   . ASP B 1 336 ? 111.076 98.267  154.169 1.00 102.69 ? 323 ASP B C   1 
ATOM   5777 O O   . ASP B 1 336 ? 111.741 97.345  153.684 1.00 100.78 ? 323 ASP B O   1 
ATOM   5778 C CB  . ASP B 1 336 ? 109.538 99.615  152.718 1.00 103.91 ? 323 ASP B CB  1 
ATOM   5779 C CG  . ASP B 1 336 ? 108.342 99.473  151.799 1.00 104.70 ? 323 ASP B CG  1 
ATOM   5780 O OD1 . ASP B 1 336 ? 107.576 98.499  151.958 1.00 108.48 ? 323 ASP B OD1 1 
ATOM   5781 O OD2 . ASP B 1 336 ? 108.175 100.335 150.913 1.00 98.83  ? 323 ASP B OD2 1 
ATOM   5782 N N   . LEU B 1 337 ? 111.582 99.110  155.073 1.00 106.23 ? 324 LEU B N   1 
ATOM   5783 C CA  . LEU B 1 337 ? 112.945 98.936  155.568 1.00 105.86 ? 324 LEU B CA  1 
ATOM   5784 C C   . LEU B 1 337 ? 113.087 97.642  156.357 1.00 104.93 ? 324 LEU B C   1 
ATOM   5785 O O   . LEU B 1 337 ? 114.108 96.953  156.257 1.00 103.82 ? 324 LEU B O   1 
ATOM   5786 C CB  . LEU B 1 337 ? 113.352 100.129 156.429 1.00 102.35 ? 324 LEU B CB  1 
ATOM   5787 C CG  . LEU B 1 337 ? 113.997 101.321 155.724 1.00 84.79  ? 324 LEU B CG  1 
ATOM   5788 C CD1 . LEU B 1 337 ? 114.288 102.425 156.726 1.00 74.41  ? 324 LEU B CD1 1 
ATOM   5789 C CD2 . LEU B 1 337 ? 115.270 100.892 155.009 1.00 74.91  ? 324 LEU B CD2 1 
ATOM   5790 N N   . THR B 1 338 ? 112.077 97.304  157.162 1.00 106.41 ? 325 THR B N   1 
ATOM   5791 C CA  . THR B 1 338 ? 112.117 96.050  157.905 1.00 110.37 ? 325 THR B CA  1 
ATOM   5792 C C   . THR B 1 338 ? 112.129 94.855  156.959 1.00 110.52 ? 325 THR B C   1 
ATOM   5793 O O   . THR B 1 338 ? 112.859 93.883  157.183 1.00 111.54 ? 325 THR B O   1 
ATOM   5794 C CB  . THR B 1 338 ? 110.929 95.978  158.862 1.00 112.29 ? 325 THR B CB  1 
ATOM   5795 O OG1 . THR B 1 338 ? 110.843 97.201  159.603 1.00 110.23 ? 325 THR B OG1 1 
ATOM   5796 C CG2 . THR B 1 338 ? 111.096 94.825  159.839 1.00 108.88 ? 325 THR B CG2 1 
ATOM   5797 N N   . GLY B 1 339 ? 111.338 94.917  155.885 1.00 108.71 ? 326 GLY B N   1 
ATOM   5798 C CA  . GLY B 1 339 ? 111.360 93.847  154.900 1.00 107.81 ? 326 GLY B CA  1 
ATOM   5799 C C   . GLY B 1 339 ? 112.682 93.759  154.164 1.00 106.61 ? 326 GLY B C   1 
ATOM   5800 O O   . GLY B 1 339 ? 113.162 92.667  153.850 1.00 106.55 ? 326 GLY B O   1 
ATOM   5801 N N   . LEU B 1 340 ? 113.283 94.910  153.865 1.00 105.96 ? 327 LEU B N   1 
ATOM   5802 C CA  . LEU B 1 340 ? 114.592 94.905  153.227 1.00 103.45 ? 327 LEU B CA  1 
ATOM   5803 C C   . LEU B 1 340 ? 115.649 94.295  154.137 1.00 105.18 ? 327 LEU B C   1 
ATOM   5804 O O   . LEU B 1 340 ? 116.492 93.521  153.675 1.00 105.26 ? 327 LEU B O   1 
ATOM   5805 C CB  . LEU B 1 340 ? 114.977 96.329  152.827 1.00 104.74 ? 327 LEU B CB  1 
ATOM   5806 C CG  . LEU B 1 340 ? 115.895 96.481  151.614 1.00 102.17 ? 327 LEU B CG  1 
ATOM   5807 C CD1 . LEU B 1 340 ? 115.660 97.824  150.951 1.00 94.38  ? 327 LEU B CD1 1 
ATOM   5808 C CD2 . LEU B 1 340 ? 117.353 96.325  152.022 1.00 101.34 ? 327 LEU B CD2 1 
ATOM   5809 N N   . GLU B 1 341 ? 115.607 94.611  155.431 1.00 107.14 ? 328 GLU B N   1 
ATOM   5810 C CA  . GLU B 1 341 ? 116.553 94.013  156.368 1.00 106.50 ? 328 GLU B CA  1 
ATOM   5811 C C   . GLU B 1 341 ? 116.305 92.516  156.525 1.00 106.96 ? 328 GLU B C   1 
ATOM   5812 O O   . GLU B 1 341 ? 117.254 91.735  156.670 1.00 107.24 ? 328 GLU B O   1 
ATOM   5813 C CB  . GLU B 1 341 ? 116.479 94.726  157.720 1.00 107.92 ? 328 GLU B CB  1 
ATOM   5814 C CG  . GLU B 1 341 ? 116.851 96.212  157.680 1.00 105.04 ? 328 GLU B CG  1 
ATOM   5815 C CD  . GLU B 1 341 ? 118.356 96.461  157.681 1.00 104.96 ? 328 GLU B CD  1 
ATOM   5816 O OE1 . GLU B 1 341 ? 118.786 97.479  158.272 1.00 110.64 ? 328 GLU B OE1 1 
ATOM   5817 O OE2 . GLU B 1 341 ? 119.106 95.657  157.097 1.00 103.00 ? 328 GLU B OE2 1 
ATOM   5818 N N   . HIS B 1 342 ? 115.035 92.098  156.511 1.00 107.54 ? 329 HIS B N   1 
ATOM   5819 C CA  . HIS B 1 342 ? 114.729 90.670  156.530 1.00 107.95 ? 329 HIS B CA  1 
ATOM   5820 C C   . HIS B 1 342 ? 115.312 89.968  155.308 1.00 107.06 ? 329 HIS B C   1 
ATOM   5821 O O   . HIS B 1 342 ? 115.920 88.897  155.425 1.00 106.46 ? 329 HIS B O   1 
ATOM   5822 C CB  . HIS B 1 342 ? 113.214 90.454  156.593 1.00 109.10 ? 329 HIS B CB  1 
ATOM   5823 C CG  . HIS B 1 342 ? 112.587 90.866  157.893 1.00 112.25 ? 329 HIS B CG  1 
ATOM   5824 N ND1 . HIS B 1 342 ? 111.223 90.871  158.091 1.00 114.73 ? 329 HIS B ND1 1 
ATOM   5825 C CD2 . HIS B 1 342 ? 113.135 91.279  159.061 1.00 114.85 ? 329 HIS B CD2 1 
ATOM   5826 C CE1 . HIS B 1 342 ? 110.957 91.272  159.322 1.00 116.06 ? 329 HIS B CE1 1 
ATOM   5827 N NE2 . HIS B 1 342 ? 112.100 91.526  159.932 1.00 117.14 ? 329 HIS B NE2 1 
ATOM   5828 N N   . MET B 1 343 ? 115.140 90.562  154.124 1.00 105.69 ? 330 MET B N   1 
ATOM   5829 C CA  . MET B 1 343 ? 115.685 89.974  152.901 1.00 103.07 ? 330 MET B CA  1 
ATOM   5830 C C   . MET B 1 343 ? 117.211 89.923  152.948 1.00 103.90 ? 330 MET B C   1 
ATOM   5831 O O   . MET B 1 343 ? 117.826 88.934  152.527 1.00 105.46 ? 330 MET B O   1 
ATOM   5832 C CB  . MET B 1 343 ? 115.198 90.759  151.680 1.00 97.86  ? 330 MET B CB  1 
ATOM   5833 C CG  . MET B 1 343 ? 115.956 90.494  150.392 1.00 96.63  ? 330 MET B CG  1 
ATOM   5834 S SD  . MET B 1 343 ? 117.350 91.618  150.158 1.00 123.77 ? 330 MET B SD  1 
ATOM   5835 C CE  . MET B 1 343 ? 116.565 93.206  150.419 1.00 114.77 ? 330 MET B CE  1 
ATOM   5836 N N   . LEU B 1 344 ? 117.837 90.986  153.470 1.00 102.47 ? 331 LEU B N   1 
ATOM   5837 C CA  . LEU B 1 344 ? 119.290 91.020  153.618 1.00 100.73 ? 331 LEU B CA  1 
ATOM   5838 C C   . LEU B 1 344 ? 119.788 89.910  154.533 1.00 105.45 ? 331 LEU B C   1 
ATOM   5839 O O   . LEU B 1 344 ? 120.731 89.188  154.187 1.00 107.20 ? 331 LEU B O   1 
ATOM   5840 C CB  . LEU B 1 344 ? 119.725 92.384  154.159 1.00 105.90 ? 331 LEU B CB  1 
ATOM   5841 C CG  . LEU B 1 344 ? 119.764 93.563  153.185 1.00 102.35 ? 331 LEU B CG  1 
ATOM   5842 C CD1 . LEU B 1 344 ? 120.154 94.829  153.922 1.00 95.29  ? 331 LEU B CD1 1 
ATOM   5843 C CD2 . LEU B 1 344 ? 120.738 93.284  152.055 1.00 98.29  ? 331 LEU B CD2 1 
ATOM   5844 N N   . ILE B 1 345 ? 119.163 89.748  155.702 1.00 107.05 ? 332 ILE B N   1 
ATOM   5845 C CA  . ILE B 1 345 ? 119.640 88.739  156.642 1.00 105.96 ? 332 ILE B CA  1 
ATOM   5846 C C   . ILE B 1 345 ? 119.380 87.334  156.104 1.00 107.68 ? 332 ILE B C   1 
ATOM   5847 O O   . ILE B 1 345 ? 120.196 86.427  156.296 1.00 107.46 ? 332 ILE B O   1 
ATOM   5848 C CB  . ILE B 1 345 ? 119.029 88.959  158.039 1.00 106.85 ? 332 ILE B CB  1 
ATOM   5849 C CG1 . ILE B 1 345 ? 117.504 88.853  158.008 1.00 106.20 ? 332 ILE B CG1 1 
ATOM   5850 C CG2 . ILE B 1 345 ? 119.481 90.306  158.603 1.00 105.45 ? 332 ILE B CG2 1 
ATOM   5851 C CD1 . ILE B 1 345 ? 116.851 89.121  159.341 1.00 107.16 ? 332 ILE B CD1 1 
ATOM   5852 N N   . ASN B 1 346 ? 118.253 87.129  155.414 1.00 109.25 ? 333 ASN B N   1 
ATOM   5853 C CA  . ASN B 1 346 ? 117.987 85.819  154.824 1.00 107.52 ? 333 ASN B CA  1 
ATOM   5854 C C   . ASN B 1 346 ? 119.003 85.481  153.740 1.00 105.92 ? 333 ASN B C   1 
ATOM   5855 O O   . ASN B 1 346 ? 119.522 84.358  153.695 1.00 110.42 ? 333 ASN B O   1 
ATOM   5856 C CB  . ASN B 1 346 ? 116.572 85.778  154.253 1.00 103.52 ? 333 ASN B CB  1 
ATOM   5857 C CG  . ASN B 1 346 ? 115.510 85.748  155.330 1.00 104.74 ? 333 ASN B CG  1 
ATOM   5858 O OD1 . ASN B 1 346 ? 115.738 85.258  156.435 1.00 106.57 ? 333 ASN B OD1 1 
ATOM   5859 N ND2 . ASN B 1 346 ? 114.332 86.265  155.006 1.00 100.99 ? 333 ASN B ND2 1 
ATOM   5860 N N   . CYS B 1 347 ? 119.296 86.439  152.856 1.00 101.49 ? 334 CYS B N   1 
ATOM   5861 C CA  . CYS B 1 347 ? 120.271 86.200  151.799 1.00 101.55 ? 334 CYS B CA  1 
ATOM   5862 C C   . CYS B 1 347 ? 121.674 86.028  152.366 1.00 102.91 ? 334 CYS B C   1 
ATOM   5863 O O   . CYS B 1 347 ? 122.514 85.368  151.746 1.00 100.96 ? 334 CYS B O   1 
ATOM   5864 C CB  . CYS B 1 347 ? 120.226 87.345  150.786 1.00 103.27 ? 334 CYS B CB  1 
ATOM   5865 S SG  . CYS B 1 347 ? 121.245 87.114  149.307 1.00 101.91 ? 334 CYS B SG  1 
ATOM   5866 N N   . SER B 1 348 ? 121.952 86.619  153.530 1.00 102.87 ? 335 SER B N   1 
ATOM   5867 C CA  . SER B 1 348 ? 123.238 86.384  154.178 1.00 102.00 ? 335 SER B CA  1 
ATOM   5868 C C   . SER B 1 348 ? 123.301 84.992  154.792 1.00 110.26 ? 335 SER B C   1 
ATOM   5869 O O   . SER B 1 348 ? 124.321 84.301  154.681 1.00 112.04 ? 335 SER B O   1 
ATOM   5870 C CB  . SER B 1 348 ? 123.488 87.446  155.246 1.00 102.04 ? 335 SER B CB  1 
ATOM   5871 O OG  . SER B 1 348 ? 122.601 87.284  156.340 1.00 102.32 ? 335 SER B OG  1 
ATOM   5872 N N   . LYS B 1 349 ? 122.217 84.563  155.441 1.00 114.06 ? 336 LYS B N   1 
ATOM   5873 C CA  . LYS B 1 349 ? 122.210 83.274  156.121 1.00 113.14 ? 336 LYS B CA  1 
ATOM   5874 C C   . LYS B 1 349 ? 122.172 82.108  155.141 1.00 112.52 ? 336 LYS B C   1 
ATOM   5875 O O   . LYS B 1 349 ? 122.673 81.023  155.459 1.00 112.10 ? 336 LYS B O   1 
ATOM   5876 C CB  . LYS B 1 349 ? 121.027 83.205  157.090 1.00 113.09 ? 336 LYS B CB  1 
ATOM   5877 C CG  . LYS B 1 349 ? 121.265 83.947  158.398 1.00 115.82 ? 336 LYS B CG  1 
ATOM   5878 C CD  . LYS B 1 349 ? 119.990 84.582  158.931 1.00 115.81 ? 336 LYS B CD  1 
ATOM   5879 C CE  . LYS B 1 349 ? 118.849 83.583  158.995 1.00 115.08 ? 336 LYS B CE  1 
ATOM   5880 N NZ  . LYS B 1 349 ? 117.612 84.198  159.551 1.00 111.13 ? 336 LYS B NZ  1 
ATOM   5881 N N   . MET B 1 350 ? 121.587 82.300  153.954 1.00 113.63 ? 337 MET B N   1 
ATOM   5882 C CA  . MET B 1 350 ? 121.508 81.200  152.997 1.00 113.50 ? 337 MET B CA  1 
ATOM   5883 C C   . MET B 1 350 ? 122.877 80.767  152.487 1.00 114.76 ? 337 MET B C   1 
ATOM   5884 O O   . MET B 1 350 ? 123.016 79.633  152.016 1.00 114.20 ? 337 MET B O   1 
ATOM   5885 C CB  . MET B 1 350 ? 120.601 81.572  151.819 1.00 113.06 ? 337 MET B CB  1 
ATOM   5886 C CG  . MET B 1 350 ? 121.069 82.747  150.965 1.00 111.57 ? 337 MET B CG  1 
ATOM   5887 S SD  . MET B 1 350 ? 122.325 82.361  149.724 1.00 120.01 ? 337 MET B SD  1 
ATOM   5888 C CE  . MET B 1 350 ? 121.542 81.015  148.841 1.00 118.34 ? 337 MET B CE  1 
ATOM   5889 N N   . LEU B 1 351 ? 123.882 81.633  152.562 1.00 116.06 ? 338 LEU B N   1 
ATOM   5890 C CA  . LEU B 1 351 ? 125.221 81.284  152.101 1.00 118.15 ? 338 LEU B CA  1 
ATOM   5891 C C   . LEU B 1 351 ? 125.992 80.542  153.188 1.00 118.21 ? 338 LEU B C   1 
ATOM   5892 O O   . LEU B 1 351 ? 126.501 81.153  154.128 1.00 115.37 ? 338 LEU B O   1 
ATOM   5893 C CB  . LEU B 1 351 ? 125.986 82.537  151.674 1.00 117.42 ? 338 LEU B CB  1 
ATOM   5894 C CG  . LEU B 1 351 ? 127.277 82.322  150.883 1.00 114.52 ? 338 LEU B CG  1 
ATOM   5895 C CD1 . LEU B 1 351 ? 126.977 81.667  149.544 1.00 109.09 ? 338 LEU B CD1 1 
ATOM   5896 C CD2 . LEU B 1 351 ? 128.005 83.640  150.688 1.00 113.07 ? 338 LEU B CD2 1 
ATOM   5897 N N   . PRO B 1 363 ? 138.286 97.925  157.028 1.00 140.04 ? 350 PRO B N   1 
ATOM   5898 C CA  . PRO B 1 363 ? 136.919 97.745  157.525 1.00 142.89 ? 350 PRO B CA  1 
ATOM   5899 C C   . PRO B 1 363 ? 136.677 98.431  158.868 1.00 146.88 ? 350 PRO B C   1 
ATOM   5900 O O   . PRO B 1 363 ? 136.485 97.754  159.877 1.00 147.20 ? 350 PRO B O   1 
ATOM   5901 C CB  . PRO B 1 363 ? 136.802 96.226  157.658 1.00 139.09 ? 350 PRO B CB  1 
ATOM   5902 C CG  . PRO B 1 363 ? 137.688 95.705  156.569 1.00 134.39 ? 350 PRO B CG  1 
ATOM   5903 C CD  . PRO B 1 363 ? 138.836 96.680  156.460 1.00 135.91 ? 350 PRO B CD  1 
ATOM   5904 N N   . THR B 1 364 ? 136.679 99.759  158.873 1.00 147.06 ? 351 THR B N   1 
ATOM   5905 C CA  . THR B 1 364 ? 136.427 100.557 160.066 1.00 148.65 ? 351 THR B CA  1 
ATOM   5906 C C   . THR B 1 364 ? 135.101 101.298 159.911 1.00 146.80 ? 351 THR B C   1 
ATOM   5907 O O   . THR B 1 364 ? 134.382 101.132 158.922 1.00 146.56 ? 351 THR B O   1 
ATOM   5908 C CB  . THR B 1 364 ? 137.572 101.541 160.329 1.00 150.54 ? 351 THR B CB  1 
ATOM   5909 O OG1 . THR B 1 364 ? 137.669 102.469 159.242 1.00 150.30 ? 351 THR B OG1 1 
ATOM   5910 C CG2 . THR B 1 364 ? 138.898 100.801 160.483 1.00 151.31 ? 351 THR B CG2 1 
ATOM   5911 N N   . GLN B 1 365 ? 134.781 102.113 160.916 1.00 143.55 ? 352 GLN B N   1 
ATOM   5912 C CA  . GLN B 1 365 ? 133.535 102.880 160.979 1.00 139.09 ? 352 GLN B CA  1 
ATOM   5913 C C   . GLN B 1 365 ? 132.325 101.966 160.776 1.00 139.84 ? 352 GLN B C   1 
ATOM   5914 O O   . GLN B 1 365 ? 131.530 102.122 159.847 1.00 141.00 ? 352 GLN B O   1 
ATOM   5915 C CB  . GLN B 1 365 ? 133.540 104.028 159.963 1.00 137.31 ? 352 GLN B CB  1 
ATOM   5916 C CG  . GLN B 1 365 ? 132.451 105.072 160.189 1.00 134.82 ? 352 GLN B CG  1 
ATOM   5917 C CD  . GLN B 1 365 ? 132.260 105.978 158.990 1.00 128.00 ? 352 GLN B CD  1 
ATOM   5918 O OE1 . GLN B 1 365 ? 132.847 105.754 157.932 1.00 121.83 ? 352 GLN B OE1 1 
ATOM   5919 N NE2 . GLN B 1 365 ? 131.435 107.007 159.147 1.00 123.82 ? 352 GLN B NE2 1 
ATOM   5920 N N   . GLU B 1 366 ? 132.207 100.992 161.673 1.00 136.98 ? 353 GLU B N   1 
ATOM   5921 C CA  . GLU B 1 366 ? 131.155 99.987  161.615 1.00 130.85 ? 353 GLU B CA  1 
ATOM   5922 C C   . GLU B 1 366 ? 130.095 100.298 162.664 1.00 127.61 ? 353 GLU B C   1 
ATOM   5923 O O   . GLU B 1 366 ? 130.408 100.406 163.854 1.00 131.63 ? 353 GLU B O   1 
ATOM   5924 C CB  . GLU B 1 366 ? 131.731 98.588  161.834 1.00 131.39 ? 353 GLU B CB  1 
ATOM   5925 C CG  . GLU B 1 366 ? 130.696 97.523  162.170 1.00 127.66 ? 353 GLU B CG  1 
ATOM   5926 C CD  . GLU B 1 366 ? 129.952 97.010  160.952 1.00 123.80 ? 353 GLU B CD  1 
ATOM   5927 O OE1 . GLU B 1 366 ? 130.093 97.603  159.862 1.00 123.64 ? 353 GLU B OE1 1 
ATOM   5928 O OE2 . GLU B 1 366 ? 129.228 96.002  161.086 1.00 121.71 ? 353 GLU B OE2 1 
ATOM   5929 N N   . SER B 1 367 ? 128.850 100.447 162.217 1.00 119.68 ? 354 SER B N   1 
ATOM   5930 C CA  . SER B 1 367 ? 127.724 100.671 163.110 1.00 117.20 ? 354 SER B CA  1 
ATOM   5931 C C   . SER B 1 367 ? 126.446 100.267 162.389 1.00 110.63 ? 354 SER B C   1 
ATOM   5932 O O   . SER B 1 367 ? 126.283 100.554 161.200 1.00 105.34 ? 354 SER B O   1 
ATOM   5933 C CB  . SER B 1 367 ? 127.645 102.134 163.564 1.00 121.95 ? 354 SER B CB  1 
ATOM   5934 O OG  . SER B 1 367 ? 128.784 102.497 164.327 1.00 124.45 ? 354 SER B OG  1 
ATOM   5935 N N   . TYR B 1 368 ? 125.548 99.599  163.111 1.00 109.65 ? 355 TYR B N   1 
ATOM   5936 C CA  . TYR B 1 368 ? 124.282 99.162  162.540 1.00 105.44 ? 355 TYR B CA  1 
ATOM   5937 C C   . TYR B 1 368 ? 123.200 99.193  163.608 1.00 103.36 ? 355 TYR B C   1 
ATOM   5938 O O   . TYR B 1 368 ? 123.478 99.034  164.799 1.00 105.82 ? 355 TYR B O   1 
ATOM   5939 C CB  . TYR B 1 368 ? 124.381 97.753  161.946 1.00 104.24 ? 355 TYR B CB  1 
ATOM   5940 C CG  . TYR B 1 368 ? 124.642 97.726  160.459 1.00 100.50 ? 355 TYR B CG  1 
ATOM   5941 C CD1 . TYR B 1 368 ? 123.597 97.839  159.551 1.00 94.65  ? 355 TYR B CD1 1 
ATOM   5942 C CD2 . TYR B 1 368 ? 125.929 97.579  159.964 1.00 101.29 ? 355 TYR B CD2 1 
ATOM   5943 C CE1 . TYR B 1 368 ? 123.831 97.813  158.192 1.00 87.02  ? 355 TYR B CE1 1 
ATOM   5944 C CE2 . TYR B 1 368 ? 126.171 97.550  158.607 1.00 96.32  ? 355 TYR B CE2 1 
ATOM   5945 C CZ  . TYR B 1 368 ? 125.120 97.667  157.727 1.00 88.64  ? 355 TYR B CZ  1 
ATOM   5946 O OH  . TYR B 1 368 ? 125.361 97.639  156.374 1.00 83.24  ? 355 TYR B OH  1 
ATOM   5947 N N   . TYR B 1 369 ? 121.960 99.400  163.163 1.00 100.24 ? 356 TYR B N   1 
ATOM   5948 C CA  . TYR B 1 369 ? 120.823 99.353  164.074 1.00 107.64 ? 356 TYR B CA  1 
ATOM   5949 C C   . TYR B 1 369 ? 120.447 97.923  164.442 1.00 115.37 ? 356 TYR B C   1 
ATOM   5950 O O   . TYR B 1 369 ? 119.932 97.686  165.540 1.00 118.99 ? 356 TYR B O   1 
ATOM   5951 C CB  . TYR B 1 369 ? 119.623 100.071 163.455 1.00 107.04 ? 356 TYR B CB  1 
ATOM   5952 C CG  . TYR B 1 369 ? 118.408 100.121 164.353 1.00 114.82 ? 356 TYR B CG  1 
ATOM   5953 C CD1 . TYR B 1 369 ? 118.335 101.021 165.407 1.00 114.07 ? 356 TYR B CD1 1 
ATOM   5954 C CD2 . TYR B 1 369 ? 117.330 99.271  164.142 1.00 117.59 ? 356 TYR B CD2 1 
ATOM   5955 C CE1 . TYR B 1 369 ? 117.226 101.072 166.230 1.00 119.53 ? 356 TYR B CE1 1 
ATOM   5956 C CE2 . TYR B 1 369 ? 116.216 99.314  164.959 1.00 120.01 ? 356 TYR B CE2 1 
ATOM   5957 C CZ  . TYR B 1 369 ? 116.170 100.216 166.001 1.00 124.03 ? 356 TYR B CZ  1 
ATOM   5958 O OH  . TYR B 1 369 ? 115.062 100.262 166.817 1.00 121.01 ? 356 TYR B OH  1 
ATOM   5959 N N   . ASP B 1 370 ? 120.690 96.968  163.548 1.00 114.62 ? 357 ASP B N   1 
ATOM   5960 C CA  . ASP B 1 370 ? 120.370 95.566  163.791 1.00 112.64 ? 357 ASP B CA  1 
ATOM   5961 C C   . ASP B 1 370 ? 121.652 94.745  163.761 1.00 113.95 ? 357 ASP B C   1 
ATOM   5962 O O   . ASP B 1 370 ? 122.380 94.780  162.754 1.00 114.38 ? 357 ASP B O   1 
ATOM   5963 C CB  . ASP B 1 370 ? 119.376 95.047  162.750 1.00 109.91 ? 357 ASP B CB  1 
ATOM   5964 C CG  . ASP B 1 370 ? 118.873 93.655  163.072 1.00 109.29 ? 357 ASP B CG  1 
ATOM   5965 O OD1 . ASP B 1 370 ? 118.152 93.501  164.079 1.00 111.29 ? 357 ASP B OD1 1 
ATOM   5966 O OD2 . ASP B 1 370 ? 119.197 92.716  162.317 1.00 107.30 ? 357 ASP B OD2 1 
ATOM   5967 N N   . PRO B 1 371 ? 121.973 93.999  164.822 1.00 113.89 ? 358 PRO B N   1 
ATOM   5968 C CA  . PRO B 1 371 ? 123.252 93.272  164.856 1.00 114.06 ? 358 PRO B CA  1 
ATOM   5969 C C   . PRO B 1 371 ? 123.322 92.088  163.906 1.00 114.30 ? 358 PRO B C   1 
ATOM   5970 O O   . PRO B 1 371 ? 124.423 91.572  163.676 1.00 116.37 ? 358 PRO B O   1 
ATOM   5971 C CB  . PRO B 1 371 ? 123.351 92.813  166.315 1.00 112.24 ? 358 PRO B CB  1 
ATOM   5972 C CG  . PRO B 1 371 ? 121.930 92.684  166.752 1.00 108.84 ? 358 PRO B CG  1 
ATOM   5973 C CD  . PRO B 1 371 ? 121.174 93.775  166.040 1.00 112.45 ? 358 PRO B CD  1 
ATOM   5974 N N   . ASN B 1 372 ? 122.195 91.639  163.351 1.00 111.49 ? 359 ASN B N   1 
ATOM   5975 C CA  . ASN B 1 372 ? 122.203 90.481  162.465 1.00 110.61 ? 359 ASN B CA  1 
ATOM   5976 C C   . ASN B 1 372 ? 122.804 90.779  161.099 1.00 109.86 ? 359 ASN B C   1 
ATOM   5977 O O   . ASN B 1 372 ? 123.029 89.842  160.325 1.00 112.98 ? 359 ASN B O   1 
ATOM   5978 C CB  . ASN B 1 372 ? 120.780 89.946  162.288 1.00 108.83 ? 359 ASN B CB  1 
ATOM   5979 C CG  . ASN B 1 372 ? 120.151 89.515  163.596 1.00 108.64 ? 359 ASN B CG  1 
ATOM   5980 O OD1 . ASN B 1 372 ? 119.142 90.072  164.027 1.00 107.07 ? 359 ASN B OD1 1 
ATOM   5981 N ND2 . ASN B 1 372 ? 120.744 88.514  164.235 1.00 111.72 ? 359 ASN B ND2 1 
ATOM   5982 N N   . LEU B 1 373 ? 123.067 92.041  160.784 1.00 106.52 ? 360 LEU B N   1 
ATOM   5983 C CA  . LEU B 1 373 ? 123.478 92.413  159.436 1.00 104.20 ? 360 LEU B CA  1 
ATOM   5984 C C   . LEU B 1 373 ? 124.981 92.236  159.257 1.00 108.04 ? 360 LEU B C   1 
ATOM   5985 O O   . LEU B 1 373 ? 125.759 92.822  160.018 1.00 109.42 ? 360 LEU B O   1 
ATOM   5986 C CB  . LEU B 1 373 ? 123.088 93.855  159.141 1.00 104.36 ? 360 LEU B CB  1 
ATOM   5987 C CG  . LEU B 1 373 ? 121.703 94.073  158.532 1.00 101.46 ? 360 LEU B CG  1 
ATOM   5988 C CD1 . LEU B 1 373 ? 121.538 93.214  157.291 1.00 98.50  ? 360 LEU B CD1 1 
ATOM   5989 C CD2 . LEU B 1 373 ? 120.605 93.783  159.539 1.00 101.99 ? 360 LEU B CD2 1 
ATOM   5990 N N   . PRO B 1 374 ? 125.426 91.446  158.286 1.00 105.74 ? 361 PRO B N   1 
ATOM   5991 C CA  . PRO B 1 374 ? 126.844 91.426  157.932 1.00 102.25 ? 361 PRO B CA  1 
ATOM   5992 C C   . PRO B 1 374 ? 127.190 92.641  157.091 1.00 96.76  ? 361 PRO B C   1 
ATOM   5993 O O   . PRO B 1 374 ? 126.288 93.371  156.653 1.00 94.89  ? 361 PRO B O   1 
ATOM   5994 C CB  . PRO B 1 374 ? 126.980 90.127  157.126 1.00 96.32  ? 361 PRO B CB  1 
ATOM   5995 C CG  . PRO B 1 374 ? 125.656 89.979  156.478 1.00 95.25  ? 361 PRO B CG  1 
ATOM   5996 C CD  . PRO B 1 374 ? 124.639 90.519  157.455 1.00 100.21 ? 361 PRO B CD  1 
ATOM   5997 N N   . PRO B 1 375 ? 128.474 92.907  156.852 1.00 93.87  ? 362 PRO B N   1 
ATOM   5998 C CA  . PRO B 1 375 ? 128.834 94.030  155.972 1.00 89.98  ? 362 PRO B CA  1 
ATOM   5999 C C   . PRO B 1 375 ? 128.292 93.820  154.567 1.00 87.23  ? 362 PRO B C   1 
ATOM   6000 O O   . PRO B 1 375 ? 128.627 92.846  153.888 1.00 89.61  ? 362 PRO B O   1 
ATOM   6001 C CB  . PRO B 1 375 ? 130.368 94.025  156.001 1.00 92.21  ? 362 PRO B CB  1 
ATOM   6002 C CG  . PRO B 1 375 ? 130.746 92.659  156.486 1.00 91.53  ? 362 PRO B CG  1 
ATOM   6003 C CD  . PRO B 1 375 ? 129.663 92.265  157.435 1.00 93.91  ? 362 PRO B CD  1 
ATOM   6004 N N   . VAL B 1 376 ? 127.445 94.751  154.130 1.00 83.28  ? 363 VAL B N   1 
ATOM   6005 C CA  . VAL B 1 376 ? 126.781 94.661  152.831 1.00 78.08  ? 363 VAL B CA  1 
ATOM   6006 C C   . VAL B 1 376 ? 127.775 95.139  151.775 1.00 81.45  ? 363 VAL B C   1 
ATOM   6007 O O   . VAL B 1 376 ? 127.916 96.339  151.537 1.00 84.05  ? 363 VAL B O   1 
ATOM   6008 C CB  . VAL B 1 376 ? 125.486 95.475  152.795 1.00 68.87  ? 363 VAL B CB  1 
ATOM   6009 C CG1 . VAL B 1 376 ? 124.756 95.247  151.484 1.00 64.66  ? 363 VAL B CG1 1 
ATOM   6010 C CG2 . VAL B 1 376 ? 124.599 95.114  153.976 1.00 72.10  ? 363 VAL B CG2 1 
ATOM   6011 N N   . THR B 1 377 ? 128.462 94.200  151.135 1.00 84.04  ? 364 THR B N   1 
ATOM   6012 C CA  . THR B 1 377 ? 129.434 94.510  150.101 1.00 85.72  ? 364 THR B CA  1 
ATOM   6013 C C   . THR B 1 377 ? 128.817 94.264  148.725 1.00 83.02  ? 364 THR B C   1 
ATOM   6014 O O   . THR B 1 377 ? 127.633 93.945  148.593 1.00 80.71  ? 364 THR B O   1 
ATOM   6015 C CB  . THR B 1 377 ? 130.702 93.677  150.298 1.00 86.76  ? 364 THR B CB  1 
ATOM   6016 O OG1 . THR B 1 377 ? 131.282 93.990  151.570 1.00 90.31  ? 364 THR B OG1 1 
ATOM   6017 C CG2 . THR B 1 377 ? 131.718 93.984  149.206 1.00 81.77  ? 364 THR B CG2 1 
ATOM   6018 N N   . LYS B 1 378 ? 129.637 94.422  147.683 1.00 81.66  ? 365 LYS B N   1 
ATOM   6019 C CA  . LYS B 1 378 ? 129.172 94.150  146.327 1.00 83.16  ? 365 LYS B CA  1 
ATOM   6020 C C   . LYS B 1 378 ? 128.719 92.705  146.171 1.00 84.32  ? 365 LYS B C   1 
ATOM   6021 O O   . LYS B 1 378 ? 127.746 92.433  145.458 1.00 84.25  ? 365 LYS B O   1 
ATOM   6022 C CB  . LYS B 1 378 ? 130.275 94.476  145.317 1.00 85.48  ? 365 LYS B CB  1 
ATOM   6023 C CG  . LYS B 1 378 ? 129.904 94.192  143.867 1.00 86.72  ? 365 LYS B CG  1 
ATOM   6024 C CD  . LYS B 1 378 ? 131.013 94.607  142.914 1.00 87.68  ? 365 LYS B CD  1 
ATOM   6025 C CE  . LYS B 1 378 ? 131.324 96.088  143.048 1.00 85.89  ? 365 LYS B CE  1 
ATOM   6026 N NZ  . LYS B 1 378 ? 130.160 96.933  142.666 1.00 87.13  ? 365 LYS B NZ  1 
ATOM   6027 N N   . SER B 1 379 ? 129.399 91.771  146.840 1.00 87.51  ? 366 SER B N   1 
ATOM   6028 C CA  . SER B 1 379 ? 129.052 90.359  146.712 1.00 87.76  ? 366 SER B CA  1 
ATOM   6029 C C   . SER B 1 379 ? 127.647 90.079  147.230 1.00 84.57  ? 366 SER B C   1 
ATOM   6030 O O   . SER B 1 379 ? 126.892 89.324  146.609 1.00 86.25  ? 366 SER B O   1 
ATOM   6031 C CB  . SER B 1 379 ? 130.075 89.497  147.452 1.00 90.10  ? 366 SER B CB  1 
ATOM   6032 O OG  . SER B 1 379 ? 130.004 89.706  148.852 1.00 87.57  ? 366 SER B OG  1 
ATOM   6033 N N   . LEU B 1 380 ? 127.277 90.678  148.365 1.00 82.12  ? 367 LEU B N   1 
ATOM   6034 C CA  . LEU B 1 380 ? 125.987 90.373  148.977 1.00 83.22  ? 367 LEU B CA  1 
ATOM   6035 C C   . LEU B 1 380 ? 124.828 90.993  148.206 1.00 84.57  ? 367 LEU B C   1 
ATOM   6036 O O   . LEU B 1 380 ? 123.728 90.430  148.187 1.00 85.00  ? 367 LEU B O   1 
ATOM   6037 C CB  . LEU B 1 380 ? 125.975 90.846  150.432 1.00 80.71  ? 367 LEU B CB  1 
ATOM   6038 C CG  . LEU B 1 380 ? 124.917 90.266  151.376 1.00 77.78  ? 367 LEU B CG  1 
ATOM   6039 C CD1 . LEU B 1 380 ? 125.466 90.216  152.789 1.00 83.27  ? 367 LEU B CD1 1 
ATOM   6040 C CD2 . LEU B 1 380 ? 123.630 91.075  151.347 1.00 73.72  ? 367 LEU B CD2 1 
ATOM   6041 N N   . VAL B 1 381 ? 125.048 92.144  147.575 1.00 82.88  ? 368 VAL B N   1 
ATOM   6042 C CA  . VAL B 1 381 ? 123.969 92.829  146.874 1.00 79.04  ? 368 VAL B CA  1 
ATOM   6043 C C   . VAL B 1 381 ? 123.867 92.394  145.413 1.00 82.68  ? 368 VAL B C   1 
ATOM   6044 O O   . VAL B 1 381 ? 122.785 92.465  144.822 1.00 88.80  ? 368 VAL B O   1 
ATOM   6045 C CB  . VAL B 1 381 ? 124.155 94.352  146.986 1.00 76.99  ? 368 VAL B CB  1 
ATOM   6046 C CG1 . VAL B 1 381 ? 125.312 94.813  146.115 1.00 81.73  ? 368 VAL B CG1 1 
ATOM   6047 C CG2 . VAL B 1 381 ? 122.870 95.080  146.622 1.00 74.13  ? 368 VAL B CG2 1 
ATOM   6048 N N   . THR B 1 382 ? 124.966 91.932  144.817 1.00 82.73  ? 369 THR B N   1 
ATOM   6049 C CA  . THR B 1 382 ? 124.951 91.558  143.409 1.00 81.16  ? 369 THR B CA  1 
ATOM   6050 C C   . THR B 1 382 ? 124.253 90.223  143.167 1.00 83.97  ? 369 THR B C   1 
ATOM   6051 O O   . THR B 1 382 ? 123.596 90.051  142.135 1.00 87.07  ? 369 THR B O   1 
ATOM   6052 C CB  . THR B 1 382 ? 126.383 91.505  142.874 1.00 81.32  ? 369 THR B CB  1 
ATOM   6053 O OG1 . THR B 1 382 ? 127.044 92.746  143.154 1.00 80.83  ? 369 THR B OG1 1 
ATOM   6054 C CG2 . THR B 1 382 ? 126.394 91.259  141.371 1.00 82.73  ? 369 THR B CG2 1 
ATOM   6055 N N   . ASN B 1 383 ? 124.360 89.281  144.105 1.00 78.99  ? 370 ASN B N   1 
ATOM   6056 C CA  . ASN B 1 383 ? 123.887 87.918  143.903 1.00 78.22  ? 370 ASN B CA  1 
ATOM   6057 C C   . ASN B 1 383 ? 122.479 87.676  144.428 1.00 81.12  ? 370 ASN B C   1 
ATOM   6058 O O   . ASN B 1 383 ? 121.955 86.569  144.260 1.00 86.77  ? 370 ASN B O   1 
ATOM   6059 C CB  . ASN B 1 383 ? 124.837 86.931  144.581 1.00 79.68  ? 370 ASN B CB  1 
ATOM   6060 C CG  . ASN B 1 383 ? 124.828 87.072  146.083 1.00 82.97  ? 370 ASN B CG  1 
ATOM   6061 O OD1 . ASN B 1 383 ? 124.537 88.145  146.610 1.00 83.53  ? 370 ASN B OD1 1 
ATOM   6062 N ND2 . ASN B 1 383 ? 125.132 85.988  146.785 1.00 82.14  ? 370 ASN B ND2 1 
ATOM   6063 N N   . CYS B 1 384 ? 121.864 88.662  145.073 1.00 81.29  ? 371 CYS B N   1 
ATOM   6064 C CA  . CYS B 1 384 ? 120.529 88.495  145.643 1.00 82.59  ? 371 CYS B CA  1 
ATOM   6065 C C   . CYS B 1 384 ? 119.508 88.625  144.520 1.00 78.54  ? 371 CYS B C   1 
ATOM   6066 O O   . CYS B 1 384 ? 119.345 89.696  143.936 1.00 80.83  ? 371 CYS B O   1 
ATOM   6067 C CB  . CYS B 1 384 ? 120.283 89.518  146.743 1.00 84.12  ? 371 CYS B CB  1 
ATOM   6068 S SG  . CYS B 1 384 ? 118.798 89.186  147.714 1.00 95.05  ? 371 CYS B SG  1 
ATOM   6069 N N   . LYS B 1 385 ? 118.824 87.519  144.197 1.00 74.19  ? 372 LYS B N   1 
ATOM   6070 C CA  . LYS B 1 385 ? 117.915 87.537  143.051 1.00 76.57  ? 372 LYS B CA  1 
ATOM   6071 C C   . LYS B 1 385 ? 116.719 88.462  143.251 1.00 78.72  ? 372 LYS B C   1 
ATOM   6072 O O   . LYS B 1 385 ? 116.489 89.336  142.398 1.00 80.96  ? 372 LYS B O   1 
ATOM   6073 C CB  . LYS B 1 385 ? 117.482 86.111  142.701 1.00 80.05  ? 372 LYS B CB  1 
ATOM   6074 C CG  . LYS B 1 385 ? 116.338 86.040  141.695 1.00 79.08  ? 372 LYS B CG  1 
ATOM   6075 C CD  . LYS B 1 385 ? 116.625 86.826  140.416 1.00 79.36  ? 372 LYS B CD  1 
ATOM   6076 C CE  . LYS B 1 385 ? 117.775 86.233  139.625 1.00 83.79  ? 372 LYS B CE  1 
ATOM   6077 N NZ  . LYS B 1 385 ? 118.115 87.067  138.436 1.00 88.51  ? 372 LYS B NZ  1 
ATOM   6078 N N   . PRO B 1 386 ? 115.910 88.325  144.311 1.00 77.54  ? 373 PRO B N   1 
ATOM   6079 C CA  . PRO B 1 386 ? 114.645 89.079  144.349 1.00 80.83  ? 373 PRO B CA  1 
ATOM   6080 C C   . PRO B 1 386 ? 114.827 90.581  144.452 1.00 83.81  ? 373 PRO B C   1 
ATOM   6081 O O   . PRO B 1 386 ? 114.073 91.324  143.807 1.00 84.35  ? 373 PRO B O   1 
ATOM   6082 C CB  . PRO B 1 386 ? 113.937 88.516  145.589 1.00 77.38  ? 373 PRO B CB  1 
ATOM   6083 C CG  . PRO B 1 386 ? 115.040 88.062  146.463 1.00 74.35  ? 373 PRO B CG  1 
ATOM   6084 C CD  . PRO B 1 386 ? 116.118 87.556  145.551 1.00 73.43  ? 373 PRO B CD  1 
ATOM   6085 N N   . VAL B 1 387 ? 115.827 91.061  145.187 1.00 82.22  ? 374 VAL B N   1 
ATOM   6086 C CA  . VAL B 1 387 ? 116.021 92.502  145.265 1.00 76.51  ? 374 VAL B CA  1 
ATOM   6087 C C   . VAL B 1 387 ? 116.648 93.041  143.984 1.00 76.21  ? 374 VAL B C   1 
ATOM   6088 O O   . VAL B 1 387 ? 116.373 94.179  143.602 1.00 74.96  ? 374 VAL B O   1 
ATOM   6089 C CB  . VAL B 1 387 ? 116.853 92.898  146.499 1.00 74.38  ? 374 VAL B CB  1 
ATOM   6090 C CG1 . VAL B 1 387 ? 118.327 92.573  146.305 1.00 73.51  ? 374 VAL B CG1 1 
ATOM   6091 C CG2 . VAL B 1 387 ? 116.664 94.377  146.794 1.00 79.18  ? 374 VAL B CG2 1 
ATOM   6092 N N   . THR B 1 388 ? 117.460 92.240  143.287 1.00 75.09  ? 375 THR B N   1 
ATOM   6093 C CA  . THR B 1 388 ? 117.920 92.649  141.965 1.00 72.03  ? 375 THR B CA  1 
ATOM   6094 C C   . THR B 1 388 ? 116.750 92.747  140.994 1.00 77.40  ? 375 THR B C   1 
ATOM   6095 O O   . THR B 1 388 ? 116.697 93.657  140.159 1.00 81.00  ? 375 THR B O   1 
ATOM   6096 C CB  . THR B 1 388 ? 118.973 91.678  141.438 1.00 66.99  ? 375 THR B CB  1 
ATOM   6097 O OG1 . THR B 1 388 ? 120.069 91.612  142.358 1.00 61.61  ? 375 THR B OG1 1 
ATOM   6098 C CG2 . THR B 1 388 ? 119.487 92.150  140.088 1.00 64.76  ? 375 THR B CG2 1 
ATOM   6099 N N   . ASP B 1 389 ? 115.800 91.814  141.091 1.00 75.68  ? 376 ASP B N   1 
ATOM   6100 C CA  . ASP B 1 389 ? 114.596 91.891  140.270 1.00 77.21  ? 376 ASP B CA  1 
ATOM   6101 C C   . ASP B 1 389 ? 113.801 93.153  140.575 1.00 77.35  ? 376 ASP B C   1 
ATOM   6102 O O   . ASP B 1 389 ? 113.320 93.831  139.657 1.00 77.18  ? 376 ASP B O   1 
ATOM   6103 C CB  . ASP B 1 389 ? 113.734 90.649  140.490 1.00 80.70  ? 376 ASP B CB  1 
ATOM   6104 C CG  . ASP B 1 389 ? 114.337 89.407  139.869 1.00 83.20  ? 376 ASP B CG  1 
ATOM   6105 O OD1 . ASP B 1 389 ? 115.373 89.533  139.182 1.00 78.86  ? 376 ASP B OD1 1 
ATOM   6106 O OD2 . ASP B 1 389 ? 113.784 88.305  140.072 1.00 85.96  ? 376 ASP B OD2 1 
ATOM   6107 N N   . LYS B 1 390 ? 113.661 93.490  141.860 1.00 75.45  ? 377 LYS B N   1 
ATOM   6108 C CA  . LYS B 1 390 ? 112.944 94.709  142.218 1.00 76.95  ? 377 LYS B CA  1 
ATOM   6109 C C   . LYS B 1 390 ? 113.692 95.952  141.750 1.00 76.83  ? 377 LYS B C   1 
ATOM   6110 O O   . LYS B 1 390 ? 113.067 96.940  141.350 1.00 77.76  ? 377 LYS B O   1 
ATOM   6111 C CB  . LYS B 1 390 ? 112.708 94.754  143.726 1.00 76.76  ? 377 LYS B CB  1 
ATOM   6112 C CG  . LYS B 1 390 ? 111.957 95.988  144.193 1.00 76.69  ? 377 LYS B CG  1 
ATOM   6113 C CD  . LYS B 1 390 ? 111.703 95.960  145.690 1.00 77.87  ? 377 LYS B CD  1 
ATOM   6114 C CE  . LYS B 1 390 ? 110.467 95.146  146.021 1.00 77.30  ? 377 LYS B CE  1 
ATOM   6115 N NZ  . LYS B 1 390 ? 109.237 95.755  145.443 1.00 80.30  ? 377 LYS B NZ  1 
ATOM   6116 N N   . ILE B 1 391 ? 115.025 95.913  141.786 1.00 75.95  ? 378 ILE B N   1 
ATOM   6117 C CA  . ILE B 1 391 ? 115.837 97.020  141.288 1.00 75.17  ? 378 ILE B CA  1 
ATOM   6118 C C   . ILE B 1 391 ? 115.618 97.213  139.794 1.00 78.50  ? 378 ILE B C   1 
ATOM   6119 O O   . ILE B 1 391 ? 115.425 98.340  139.319 1.00 79.62  ? 378 ILE B O   1 
ATOM   6120 C CB  . ILE B 1 391 ? 117.321 96.770  141.616 1.00 68.47  ? 378 ILE B CB  1 
ATOM   6121 C CG1 . ILE B 1 391 ? 117.605 97.084  143.086 1.00 70.31  ? 378 ILE B CG1 1 
ATOM   6122 C CG2 . ILE B 1 391 ? 118.224 97.564  140.686 1.00 68.79  ? 378 ILE B CG2 1 
ATOM   6123 C CD1 . ILE B 1 391 ? 119.035 96.833  143.491 1.00 77.78  ? 378 ILE B CD1 1 
ATOM   6124 N N   . HIS B 1 392 ? 115.639 96.117  139.030 1.00 76.83  ? 379 HIS B N   1 
ATOM   6125 C CA  . HIS B 1 392 ? 115.395 96.207  137.593 1.00 75.24  ? 379 HIS B CA  1 
ATOM   6126 C C   . HIS B 1 392 ? 113.988 96.716  137.308 1.00 76.37  ? 379 HIS B C   1 
ATOM   6127 O O   . HIS B 1 392 ? 113.783 97.519  136.390 1.00 77.60  ? 379 HIS B O   1 
ATOM   6128 C CB  . HIS B 1 392 ? 115.615 94.845  136.932 1.00 71.70  ? 379 HIS B CB  1 
ATOM   6129 C CG  . HIS B 1 392 ? 117.038 94.380  136.956 1.00 72.09  ? 379 HIS B CG  1 
ATOM   6130 N ND1 . HIS B 1 392 ? 118.068 95.156  137.442 1.00 70.55  ? 379 HIS B ND1 1 
ATOM   6131 C CD2 . HIS B 1 392 ? 117.602 93.217  136.553 1.00 74.54  ? 379 HIS B CD2 1 
ATOM   6132 C CE1 . HIS B 1 392 ? 119.205 94.491  137.338 1.00 72.66  ? 379 HIS B CE1 1 
ATOM   6133 N NE2 . HIS B 1 392 ? 118.950 93.312  136.802 1.00 73.96  ? 379 HIS B NE2 1 
ATOM   6134 N N   . LYS B 1 393 ? 113.007 96.264  138.090 1.00 75.26  ? 380 LYS B N   1 
ATOM   6135 C CA  . LYS B 1 393 ? 111.637 96.735  137.918 1.00 77.59  ? 380 LYS B CA  1 
ATOM   6136 C C   . LYS B 1 393 ? 111.524 98.227  138.205 1.00 79.05  ? 380 LYS B C   1 
ATOM   6137 O O   . LYS B 1 393 ? 110.782 98.942  137.521 1.00 80.29  ? 380 LYS B O   1 
ATOM   6138 C CB  . LYS B 1 393 ? 110.702 95.929  138.821 1.00 76.75  ? 380 LYS B CB  1 
ATOM   6139 C CG  . LYS B 1 393 ? 109.429 96.642  139.231 1.00 75.23  ? 380 LYS B CG  1 
ATOM   6140 C CD  . LYS B 1 393 ? 108.470 95.671  139.897 1.00 77.53  ? 380 LYS B CD  1 
ATOM   6141 C CE  . LYS B 1 393 ? 109.158 94.883  140.999 1.00 78.82  ? 380 LYS B CE  1 
ATOM   6142 N NZ  . LYS B 1 393 ? 108.299 93.775  141.496 1.00 83.53  ? 380 LYS B NZ  1 
ATOM   6143 N N   . ALA B 1 394 ? 112.255 98.718  139.206 1.00 79.63  ? 381 ALA B N   1 
ATOM   6144 C CA  . ALA B 1 394 ? 112.203 100.139 139.534 1.00 80.44  ? 381 ALA B CA  1 
ATOM   6145 C C   . ALA B 1 394 ? 112.887 100.977 138.459 1.00 84.17  ? 381 ALA B C   1 
ATOM   6146 O O   . ALA B 1 394 ? 112.256 101.827 137.821 1.00 86.47  ? 381 ALA B O   1 
ATOM   6147 C CB  . ALA B 1 394 ? 112.843 100.384 140.901 1.00 79.67  ? 381 ALA B CB  1 
ATOM   6148 N N   . TYR B 1 395 ? 114.182 100.749 138.242 1.00 84.14  ? 382 TYR B N   1 
ATOM   6149 C CA  . TYR B 1 395 ? 114.961 101.486 137.247 1.00 85.27  ? 382 TYR B CA  1 
ATOM   6150 C C   . TYR B 1 395 ? 115.058 100.644 135.979 1.00 86.72  ? 382 TYR B C   1 
ATOM   6151 O O   . TYR B 1 395 ? 115.860 99.709  135.900 1.00 85.82  ? 382 TYR B O   1 
ATOM   6152 C CB  . TYR B 1 395 ? 116.341 101.842 137.789 1.00 84.44  ? 382 TYR B CB  1 
ATOM   6153 C CG  . TYR B 1 395 ? 116.370 103.117 138.601 1.00 87.85  ? 382 TYR B CG  1 
ATOM   6154 C CD1 . TYR B 1 395 ? 117.573 103.671 139.018 1.00 88.30  ? 382 TYR B CD1 1 
ATOM   6155 C CD2 . TYR B 1 395 ? 115.194 103.768 138.951 1.00 87.84  ? 382 TYR B CD2 1 
ATOM   6156 C CE1 . TYR B 1 395 ? 117.605 104.838 139.759 1.00 83.52  ? 382 TYR B CE1 1 
ATOM   6157 C CE2 . TYR B 1 395 ? 115.216 104.934 139.693 1.00 84.41  ? 382 TYR B CE2 1 
ATOM   6158 C CZ  . TYR B 1 395 ? 116.422 105.464 140.094 1.00 79.72  ? 382 TYR B CZ  1 
ATOM   6159 O OH  . TYR B 1 395 ? 116.446 106.625 140.832 1.00 75.28  ? 382 TYR B OH  1 
ATOM   6160 N N   . LYS B 1 396 ? 114.245 100.986 134.982 1.00 87.64  ? 383 LYS B N   1 
ATOM   6161 C CA  . LYS B 1 396 ? 114.209 100.240 133.733 1.00 87.35  ? 383 LYS B CA  1 
ATOM   6162 C C   . LYS B 1 396 ? 115.461 100.528 132.902 1.00 88.77  ? 383 LYS B C   1 
ATOM   6163 O O   . LYS B 1 396 ? 116.377 101.239 133.323 1.00 86.05  ? 383 LYS B O   1 
ATOM   6164 C CB  . LYS B 1 396 ? 112.947 100.589 132.946 1.00 83.44  ? 383 LYS B CB  1 
ATOM   6165 C CG  . LYS B 1 396 ? 111.674 100.600 133.777 1.00 79.89  ? 383 LYS B CG  1 
ATOM   6166 C CD  . LYS B 1 396 ? 111.389 99.241  134.395 1.00 83.31  ? 383 LYS B CD  1 
ATOM   6167 C CE  . LYS B 1 396 ? 111.116 98.187  133.334 1.00 90.21  ? 383 LYS B CE  1 
ATOM   6168 N NZ  . LYS B 1 396 ? 110.750 96.873  133.934 1.00 86.02  ? 383 LYS B NZ  1 
ATOM   6169 N N   . ASP B 1 397 ? 115.500 99.950  131.704 1.00 91.13  ? 384 ASP B N   1 
ATOM   6170 C CA  . ASP B 1 397 ? 116.585 100.209 130.768 1.00 90.56  ? 384 ASP B CA  1 
ATOM   6171 C C   . ASP B 1 397 ? 116.389 101.563 130.099 1.00 84.86  ? 384 ASP B C   1 
ATOM   6172 O O   . ASP B 1 397 ? 115.312 101.853 129.570 1.00 82.93  ? 384 ASP B O   1 
ATOM   6173 C CB  . ASP B 1 397 ? 116.659 99.107  129.712 1.00 86.80  ? 384 ASP B CB  1 
ATOM   6174 C CG  . ASP B 1 397 ? 117.224 97.813  130.257 1.00 89.63  ? 384 ASP B CG  1 
ATOM   6175 O OD1 . ASP B 1 397 ? 118.179 97.871  131.060 1.00 90.03  ? 384 ASP B OD1 1 
ATOM   6176 O OD2 . ASP B 1 397 ? 116.715 96.736  129.881 1.00 92.36  ? 384 ASP B OD2 1 
ATOM   6177 N N   . LYS B 1 398 ? 117.433 102.384 130.114 1.00 78.08  ? 385 LYS B N   1 
ATOM   6178 C CA  . LYS B 1 398 ? 117.397 103.715 129.529 1.00 74.27  ? 385 LYS B CA  1 
ATOM   6179 C C   . LYS B 1 398 ? 118.223 103.741 128.249 1.00 68.56  ? 385 LYS B C   1 
ATOM   6180 O O   . LYS B 1 398 ? 118.922 102.783 127.909 1.00 66.33  ? 385 LYS B O   1 
ATOM   6181 C CB  . LYS B 1 398 ? 117.914 104.761 130.523 1.00 75.29  ? 385 LYS B CB  1 
ATOM   6182 C CG  . LYS B 1 398 ? 117.399 104.583 131.945 1.00 79.30  ? 385 LYS B CG  1 
ATOM   6183 C CD  . LYS B 1 398 ? 115.881 104.518 131.994 1.00 84.36  ? 385 LYS B CD  1 
ATOM   6184 C CE  . LYS B 1 398 ? 115.391 104.271 133.411 1.00 82.04  ? 385 LYS B CE  1 
ATOM   6185 N NZ  . LYS B 1 398 ? 113.914 104.092 133.472 1.00 83.22  ? 385 LYS B NZ  1 
ATOM   6186 N N   . ASN B 1 399 ? 118.126 104.855 127.530 1.00 67.43  ? 386 ASN B N   1 
ATOM   6187 C CA  . ASN B 1 399 ? 118.893 105.016 126.304 1.00 56.69  ? 386 ASN B CA  1 
ATOM   6188 C C   . ASN B 1 399 ? 120.379 105.110 126.620 1.00 57.92  ? 386 ASN B C   1 
ATOM   6189 O O   . ASN B 1 399 ? 120.785 105.761 127.586 1.00 62.15  ? 386 ASN B O   1 
ATOM   6190 C CB  . ASN B 1 399 ? 118.437 106.262 125.550 1.00 51.22  ? 386 ASN B CB  1 
ATOM   6191 C CG  . ASN B 1 399 ? 116.947 106.266 125.284 1.00 54.83  ? 386 ASN B CG  1 
ATOM   6192 O OD1 . ASN B 1 399 ? 116.342 107.319 125.084 1.00 56.81  ? 386 ASN B OD1 1 
ATOM   6193 N ND2 . ASN B 1 399 ? 116.344 105.084 125.283 1.00 55.46  ? 386 ASN B ND2 1 
ATOM   6194 N N   . LYS B 1 400 ? 121.193 104.437 125.807 1.00 51.97  ? 387 LYS B N   1 
ATOM   6195 C CA  . LYS B 1 400 ? 122.635 104.480 126.017 1.00 49.00  ? 387 LYS B CA  1 
ATOM   6196 C C   . LYS B 1 400 ? 123.235 105.789 125.520 1.00 47.04  ? 387 LYS B C   1 
ATOM   6197 O O   . LYS B 1 400 ? 124.161 106.325 126.139 1.00 43.73  ? 387 LYS B O   1 
ATOM   6198 C CB  . LYS B 1 400 ? 123.301 103.286 125.331 1.00 50.77  ? 387 LYS B CB  1 
ATOM   6199 C CG  . LYS B 1 400 ? 124.796 103.192 125.576 1.00 53.48  ? 387 LYS B CG  1 
ATOM   6200 C CD  . LYS B 1 400 ? 125.364 101.869 125.092 1.00 55.26  ? 387 LYS B CD  1 
ATOM   6201 C CE  . LYS B 1 400 ? 125.115 101.667 123.610 1.00 48.50  ? 387 LYS B CE  1 
ATOM   6202 N NZ  . LYS B 1 400 ? 125.985 100.597 123.053 1.00 54.41  ? 387 LYS B NZ  1 
ATOM   6203 N N   . TYR B 1 401 ? 122.722 106.319 124.415 1.00 49.43  ? 388 TYR B N   1 
ATOM   6204 C CA  . TYR B 1 401 ? 123.224 107.552 123.828 1.00 43.03  ? 388 TYR B CA  1 
ATOM   6205 C C   . TYR B 1 401 ? 122.258 108.697 124.099 1.00 45.16  ? 388 TYR B C   1 
ATOM   6206 O O   . TYR B 1 401 ? 121.045 108.558 123.920 1.00 51.03  ? 388 TYR B O   1 
ATOM   6207 C CB  . TYR B 1 401 ? 123.429 107.395 122.320 1.00 41.84  ? 388 TYR B CB  1 
ATOM   6208 C CG  . TYR B 1 401 ? 124.375 106.282 121.940 1.00 38.43  ? 388 TYR B CG  1 
ATOM   6209 C CD1 . TYR B 1 401 ? 125.746 106.430 122.088 1.00 38.70  ? 388 TYR B CD1 1 
ATOM   6210 C CD2 . TYR B 1 401 ? 123.898 105.087 121.423 1.00 39.08  ? 388 TYR B CD2 1 
ATOM   6211 C CE1 . TYR B 1 401 ? 126.615 105.417 121.739 1.00 43.04  ? 388 TYR B CE1 1 
ATOM   6212 C CE2 . TYR B 1 401 ? 124.759 104.069 121.071 1.00 40.42  ? 388 TYR B CE2 1 
ATOM   6213 C CZ  . TYR B 1 401 ? 126.115 104.238 121.232 1.00 42.81  ? 388 TYR B CZ  1 
ATOM   6214 O OH  . TYR B 1 401 ? 126.977 103.226 120.883 1.00 42.37  ? 388 TYR B OH  1 
ATOM   6215 N N   . ARG B 1 402 ? 122.804 109.829 124.528 1.00 43.14  ? 389 ARG B N   1 
ATOM   6216 C CA  . ARG B 1 402 ? 121.999 111.015 124.769 1.00 45.55  ? 389 ARG B CA  1 
ATOM   6217 C C   . ARG B 1 402 ? 121.578 111.645 123.447 1.00 48.01  ? 389 ARG B C   1 
ATOM   6218 O O   . ARG B 1 402 ? 122.241 111.481 122.419 1.00 42.44  ? 389 ARG B O   1 
ATOM   6219 C CB  . ARG B 1 402 ? 122.778 112.026 125.608 1.00 50.57  ? 389 ARG B CB  1 
ATOM   6220 C CG  . ARG B 1 402 ? 123.503 111.414 126.793 1.00 53.27  ? 389 ARG B CG  1 
ATOM   6221 C CD  . ARG B 1 402 ? 124.334 112.450 127.525 1.00 55.44  ? 389 ARG B CD  1 
ATOM   6222 N NE  . ARG B 1 402 ? 123.501 113.481 128.132 1.00 56.68  ? 389 ARG B NE  1 
ATOM   6223 C CZ  . ARG B 1 402 ? 122.998 113.407 129.355 1.00 58.02  ? 389 ARG B CZ  1 
ATOM   6224 N NH1 . ARG B 1 402 ? 123.228 112.365 130.135 1.00 55.30  ? 389 ARG B NH1 1 
ATOM   6225 N NH2 . ARG B 1 402 ? 122.244 114.405 129.807 1.00 62.73  ? 389 ARG B NH2 1 
ATOM   6226 N N   . PHE B 1 403 ? 120.462 112.370 123.479 1.00 53.92  ? 390 PHE B N   1 
ATOM   6227 C CA  . PHE B 1 403 ? 119.964 113.023 122.277 1.00 53.14  ? 390 PHE B CA  1 
ATOM   6228 C C   . PHE B 1 403 ? 119.070 114.191 122.666 1.00 56.42  ? 390 PHE B C   1 
ATOM   6229 O O   . PHE B 1 403 ? 118.582 114.278 123.796 1.00 59.36  ? 390 PHE B O   1 
ATOM   6230 C CB  . PHE B 1 403 ? 119.202 112.044 121.377 1.00 47.35  ? 390 PHE B CB  1 
ATOM   6231 C CG  . PHE B 1 403 ? 117.884 111.597 121.941 1.00 49.96  ? 390 PHE B CG  1 
ATOM   6232 C CD1 . PHE B 1 403 ? 117.827 110.604 122.901 1.00 49.12  ? 390 PHE B CD1 1 
ATOM   6233 C CD2 . PHE B 1 403 ? 116.700 112.163 121.502 1.00 54.78  ? 390 PHE B CD2 1 
ATOM   6234 C CE1 . PHE B 1 403 ? 116.616 110.190 123.418 1.00 47.44  ? 390 PHE B CE1 1 
ATOM   6235 C CE2 . PHE B 1 403 ? 115.486 111.752 122.015 1.00 50.59  ? 390 PHE B CE2 1 
ATOM   6236 C CZ  . PHE B 1 403 ? 115.445 110.765 122.974 1.00 45.30  ? 390 PHE B CZ  1 
ATOM   6237 N N   . GLU B 1 404 ? 118.867 115.089 121.704 1.00 53.73  ? 391 GLU B N   1 
ATOM   6238 C CA  . GLU B 1 404 ? 117.974 116.228 121.852 1.00 63.27  ? 391 GLU B CA  1 
ATOM   6239 C C   . GLU B 1 404 ? 117.170 116.380 120.569 1.00 68.30  ? 391 GLU B C   1 
ATOM   6240 O O   . GLU B 1 404 ? 117.701 116.181 119.473 1.00 63.51  ? 391 GLU B O   1 
ATOM   6241 C CB  . GLU B 1 404 ? 118.752 117.516 122.154 1.00 67.58  ? 391 GLU B CB  1 
ATOM   6242 C CG  . GLU B 1 404 ? 117.879 118.736 122.410 1.00 74.56  ? 391 GLU B CG  1 
ATOM   6243 C CD  . GLU B 1 404 ? 118.692 119.993 122.654 1.00 77.67  ? 391 GLU B CD  1 
ATOM   6244 O OE1 . GLU B 1 404 ? 119.927 119.881 122.807 1.00 72.80  ? 391 GLU B OE1 1 
ATOM   6245 O OE2 . GLU B 1 404 ? 118.099 121.091 122.689 1.00 84.75  ? 391 GLU B OE2 1 
ATOM   6246 N N   . ILE B 1 405 ? 115.894 116.731 120.706 1.00 73.81  ? 392 ILE B N   1 
ATOM   6247 C CA  . ILE B 1 405 ? 114.966 116.782 119.583 1.00 74.99  ? 392 ILE B CA  1 
ATOM   6248 C C   . ILE B 1 405 ? 114.401 118.193 119.466 1.00 76.05  ? 392 ILE B C   1 
ATOM   6249 O O   . ILE B 1 405 ? 114.132 118.852 120.476 1.00 75.85  ? 392 ILE B O   1 
ATOM   6250 C CB  . ILE B 1 405 ? 113.837 115.739 119.747 1.00 77.82  ? 392 ILE B CB  1 
ATOM   6251 C CG1 . ILE B 1 405 ? 112.832 115.828 118.595 1.00 79.96  ? 392 ILE B CG1 1 
ATOM   6252 C CG2 . ILE B 1 405 ? 113.141 115.901 121.089 1.00 78.43  ? 392 ILE B CG2 1 
ATOM   6253 C CD1 . ILE B 1 405 ? 111.683 114.849 118.712 1.00 85.32  ? 392 ILE B CD1 1 
ATOM   6254 N N   . MET B 1 406 ? 114.236 118.658 118.228 1.00 75.36  ? 393 MET B N   1 
ATOM   6255 C CA  . MET B 1 406 ? 113.628 119.955 117.952 1.00 79.08  ? 393 MET B CA  1 
ATOM   6256 C C   . MET B 1 406 ? 113.010 119.908 116.559 1.00 77.76  ? 393 MET B C   1 
ATOM   6257 O O   . MET B 1 406 ? 113.131 118.914 115.838 1.00 73.80  ? 393 MET B O   1 
ATOM   6258 C CB  . MET B 1 406 ? 114.646 121.091 118.079 1.00 81.64  ? 393 MET B CB  1 
ATOM   6259 C CG  . MET B 1 406 ? 115.802 121.007 117.104 1.00 74.69  ? 393 MET B CG  1 
ATOM   6260 S SD  . MET B 1 406 ? 117.039 119.808 117.621 1.00 69.44  ? 393 MET B SD  1 
ATOM   6261 C CE  . MET B 1 406 ? 117.504 120.480 119.213 1.00 66.26  ? 393 MET B CE  1 
ATOM   6262 N N   . GLY B 1 407 ? 112.341 120.998 116.182 1.00 81.05  ? 394 GLY B N   1 
ATOM   6263 C CA  . GLY B 1 407 ? 111.526 121.005 114.980 1.00 79.56  ? 394 GLY B CA  1 
ATOM   6264 C C   . GLY B 1 407 ? 112.042 121.792 113.789 1.00 77.88  ? 394 GLY B C   1 
ATOM   6265 O O   . GLY B 1 407 ? 113.172 121.590 113.335 1.00 78.46  ? 394 GLY B O   1 
ATOM   6266 N N   . GLU B 1 408 ? 111.201 122.690 113.270 1.00 78.96  ? 395 GLU B N   1 
ATOM   6267 C CA  . GLU B 1 408 ? 111.450 123.416 112.029 1.00 82.59  ? 395 GLU B CA  1 
ATOM   6268 C C   . GLU B 1 408 ? 111.817 124.878 112.287 1.00 81.61  ? 395 GLU B C   1 
ATOM   6269 O O   . GLU B 1 408 ? 111.485 125.760 111.492 1.00 78.32  ? 395 GLU B O   1 
ATOM   6270 C CB  . GLU B 1 408 ? 110.225 123.320 111.117 1.00 83.73  ? 395 GLU B CB  1 
ATOM   6271 C CG  . GLU B 1 408 ? 110.458 123.648 109.640 1.00 79.50  ? 395 GLU B CG  1 
ATOM   6272 C CD  . GLU B 1 408 ? 110.674 122.416 108.787 1.00 79.06  ? 395 GLU B CD  1 
ATOM   6273 O OE1 . GLU B 1 408 ? 110.979 121.347 109.353 1.00 81.85  ? 395 GLU B OE1 1 
ATOM   6274 O OE2 . GLU B 1 408 ? 110.534 122.518 107.550 1.00 73.05  ? 395 GLU B OE2 1 
ATOM   6275 N N   . GLU B 1 409 ? 112.492 125.155 113.405 1.00 80.77  ? 396 GLU B N   1 
ATOM   6276 C CA  . GLU B 1 409 ? 112.765 126.545 113.759 1.00 79.39  ? 396 GLU B CA  1 
ATOM   6277 C C   . GLU B 1 409 ? 113.754 127.193 112.795 1.00 76.02  ? 396 GLU B C   1 
ATOM   6278 O O   . GLU B 1 409 ? 113.552 128.339 112.375 1.00 79.93  ? 396 GLU B O   1 
ATOM   6279 C CB  . GLU B 1 409 ? 113.273 126.640 115.199 1.00 81.93  ? 396 GLU B CB  1 
ATOM   6280 C CG  . GLU B 1 409 ? 114.441 125.730 115.540 1.00 83.00  ? 396 GLU B CG  1 
ATOM   6281 C CD  . GLU B 1 409 ? 114.011 124.485 116.288 1.00 83.29  ? 396 GLU B CD  1 
ATOM   6282 O OE1 . GLU B 1 409 ? 113.061 123.814 115.835 1.00 80.05  ? 396 GLU B OE1 1 
ATOM   6283 O OE2 . GLU B 1 409 ? 114.619 124.183 117.336 1.00 87.08  ? 396 GLU B OE2 1 
ATOM   6284 N N   . GLU B 1 410 ? 114.825 126.490 112.431 1.00 71.63  ? 397 GLU B N   1 
ATOM   6285 C CA  . GLU B 1 410 ? 115.918 127.080 111.661 1.00 69.82  ? 397 GLU B CA  1 
ATOM   6286 C C   . GLU B 1 410 ? 116.380 126.146 110.548 1.00 67.76  ? 397 GLU B C   1 
ATOM   6287 O O   . GLU B 1 410 ? 117.571 125.879 110.384 1.00 60.99  ? 397 GLU B O   1 
ATOM   6288 C CB  . GLU B 1 410 ? 117.088 127.446 112.570 1.00 67.06  ? 397 GLU B CB  1 
ATOM   6289 C CG  . GLU B 1 410 ? 116.788 128.528 113.606 1.00 76.46  ? 397 GLU B CG  1 
ATOM   6290 C CD  . GLU B 1 410 ? 116.778 129.937 113.028 1.00 82.35  ? 397 GLU B CD  1 
ATOM   6291 O OE1 . GLU B 1 410 ? 116.167 130.156 111.960 1.00 77.07  ? 397 GLU B OE1 1 
ATOM   6292 O OE2 . GLU B 1 410 ? 117.387 130.832 113.648 1.00 88.27  ? 397 GLU B OE2 1 
ATOM   6293 N N   . ILE B 1 411 ? 115.439 125.626 109.764 1.00 71.22  ? 398 ILE B N   1 
ATOM   6294 C CA  . ILE B 1 411 ? 115.757 124.813 108.595 1.00 65.00  ? 398 ILE B CA  1 
ATOM   6295 C C   . ILE B 1 411 ? 114.999 125.373 107.399 1.00 61.20  ? 398 ILE B C   1 
ATOM   6296 O O   . ILE B 1 411 ? 113.802 125.665 107.498 1.00 66.12  ? 398 ILE B O   1 
ATOM   6297 C CB  . ILE B 1 411 ? 115.423 123.324 108.819 1.00 66.45  ? 398 ILE B CB  1 
ATOM   6298 C CG1 . ILE B 1 411 ? 115.540 122.538 107.511 1.00 66.11  ? 398 ILE B CG1 1 
ATOM   6299 C CG2 . ILE B 1 411 ? 114.047 123.161 109.446 1.00 69.14  ? 398 ILE B CG2 1 
ATOM   6300 C CD1 . ILE B 1 411 ? 116.938 122.508 106.939 1.00 58.54  ? 398 ILE B CD1 1 
ATOM   6301 N N   . ALA B 1 412 ? 115.697 125.534 106.278 1.00 56.48  ? 399 ALA B N   1 
ATOM   6302 C CA  . ALA B 1 412 ? 115.124 126.083 105.055 1.00 60.86  ? 399 ALA B CA  1 
ATOM   6303 C C   . ALA B 1 412 ? 114.961 124.963 104.038 1.00 67.45  ? 399 ALA B C   1 
ATOM   6304 O O   . ALA B 1 412 ? 115.927 124.260 103.725 1.00 70.10  ? 399 ALA B O   1 
ATOM   6305 C CB  . ALA B 1 412 ? 116.002 127.199 104.490 1.00 55.29  ? 399 ALA B CB  1 
ATOM   6306 N N   . PHE B 1 413 ? 113.745 124.803 103.523 1.00 71.85  ? 400 PHE B N   1 
ATOM   6307 C CA  . PHE B 1 413 ? 113.421 123.747 102.569 1.00 72.98  ? 400 PHE B CA  1 
ATOM   6308 C C   . PHE B 1 413 ? 112.629 124.363 101.425 1.00 78.68  ? 400 PHE B C   1 
ATOM   6309 O O   . PHE B 1 413 ? 111.462 124.726 101.601 1.00 83.00  ? 400 PHE B O   1 
ATOM   6310 C CB  . PHE B 1 413 ? 112.634 122.624 103.246 1.00 77.40  ? 400 PHE B CB  1 
ATOM   6311 C CG  . PHE B 1 413 ? 112.525 121.377 102.422 1.00 82.59  ? 400 PHE B CG  1 
ATOM   6312 C CD1 . PHE B 1 413 ? 113.662 120.684 102.044 1.00 82.41  ? 400 PHE B CD1 1 
ATOM   6313 C CD2 . PHE B 1 413 ? 111.289 120.889 102.038 1.00 88.57  ? 400 PHE B CD2 1 
ATOM   6314 C CE1 . PHE B 1 413 ? 113.568 119.533 101.288 1.00 84.53  ? 400 PHE B CE1 1 
ATOM   6315 C CE2 . PHE B 1 413 ? 111.188 119.737 101.283 1.00 86.53  ? 400 PHE B CE2 1 
ATOM   6316 C CZ  . PHE B 1 413 ? 112.329 119.058 100.907 1.00 84.90  ? 400 PHE B CZ  1 
ATOM   6317 N N   . LYS B 1 414 ? 113.260 124.484 100.259 1.00 75.93  ? 401 LYS B N   1 
ATOM   6318 C CA  . LYS B 1 414 ? 112.668 125.152 99.109  1.00 77.00  ? 401 LYS B CA  1 
ATOM   6319 C C   . LYS B 1 414 ? 112.644 124.221 97.904  1.00 83.22  ? 401 LYS B C   1 
ATOM   6320 O O   . LYS B 1 414 ? 113.539 123.388 97.730  1.00 79.74  ? 401 LYS B O   1 
ATOM   6321 C CB  . LYS B 1 414 ? 113.436 126.430 98.761  1.00 73.42  ? 401 LYS B CB  1 
ATOM   6322 C CG  . LYS B 1 414 ? 113.471 127.458 99.878  1.00 76.86  ? 401 LYS B CG  1 
ATOM   6323 C CD  . LYS B 1 414 ? 112.080 127.958 100.220 1.00 78.91  ? 401 LYS B CD  1 
ATOM   6324 C CE  . LYS B 1 414 ? 112.136 129.015 101.309 1.00 76.04  ? 401 LYS B CE  1 
ATOM   6325 N NZ  . LYS B 1 414 ? 110.788 129.544 101.653 1.00 75.05  ? 401 LYS B NZ  1 
ATOM   6326 N N   . MET B 1 415 ? 111.611 124.374 97.076  1.00 90.68  ? 402 MET B N   1 
ATOM   6327 C CA  . MET B 1 415 ? 111.420 123.586 95.867  1.00 95.37  ? 402 MET B CA  1 
ATOM   6328 C C   . MET B 1 415 ? 111.236 124.525 94.684  1.00 97.81  ? 402 MET B C   1 
ATOM   6329 O O   . MET B 1 415 ? 110.678 125.617 94.830  1.00 93.70  ? 402 MET B O   1 
ATOM   6330 C CB  . MET B 1 415 ? 110.203 122.654 96.007  1.00 98.99  ? 402 MET B CB  1 
ATOM   6331 C CG  . MET B 1 415 ? 109.872 121.830 94.769  1.00 101.98 ? 402 MET B CG  1 
ATOM   6332 S SD  . MET B 1 415 ? 108.361 120.866 94.973  1.00 105.15 ? 402 MET B SD  1 
ATOM   6333 C CE  . MET B 1 415 ? 108.174 120.167 93.335  1.00 104.51 ? 402 MET B CE  1 
ATOM   6334 N N   . ILE B 1 416 ? 111.712 124.104 93.515  1.00 101.43 ? 403 ILE B N   1 
ATOM   6335 C CA  . ILE B 1 416 ? 111.595 124.876 92.284  1.00 101.14 ? 403 ILE B CA  1 
ATOM   6336 C C   . ILE B 1 416 ? 110.544 124.204 91.410  1.00 105.13 ? 403 ILE B C   1 
ATOM   6337 O O   . ILE B 1 416 ? 110.707 123.046 91.008  1.00 106.97 ? 403 ILE B O   1 
ATOM   6338 C CB  . ILE B 1 416 ? 112.933 124.982 91.543  1.00 98.93  ? 403 ILE B CB  1 
ATOM   6339 C CG1 . ILE B 1 416 ? 114.002 125.601 92.446  1.00 95.10  ? 403 ILE B CG1 1 
ATOM   6340 C CG2 . ILE B 1 416 ? 112.762 125.794 90.274  1.00 103.37 ? 403 ILE B CG2 1 
ATOM   6341 C CD1 . ILE B 1 416 ? 115.367 125.680 91.799  1.00 93.21  ? 403 ILE B CD1 1 
ATOM   6342 N N   . ARG B 1 417 ? 109.467 124.929 91.103  1.00 108.23 ? 404 ARG B N   1 
ATOM   6343 C CA  . ARG B 1 417 ? 108.399 124.411 90.258  1.00 114.74 ? 404 ARG B CA  1 
ATOM   6344 C C   . ARG B 1 417 ? 108.311 125.136 88.918  1.00 116.43 ? 404 ARG B C   1 
ATOM   6345 O O   . ARG B 1 417 ? 107.270 125.081 88.256  1.00 120.25 ? 404 ARG B O   1 
ATOM   6346 C CB  . ARG B 1 417 ? 107.057 124.489 90.988  1.00 118.22 ? 404 ARG B CB  1 
ATOM   6347 C CG  . ARG B 1 417 ? 106.608 125.902 91.334  1.00 113.81 ? 404 ARG B CG  1 
ATOM   6348 C CD  . ARG B 1 417 ? 105.106 125.959 91.594  1.00 113.52 ? 404 ARG B CD  1 
ATOM   6349 N NE  . ARG B 1 417 ? 104.705 125.171 92.754  1.00 119.64 ? 404 ARG B NE  1 
ATOM   6350 C CZ  . ARG B 1 417 ? 104.446 125.677 93.953  1.00 116.35 ? 404 ARG B CZ  1 
ATOM   6351 N NH1 . ARG B 1 417 ? 104.546 126.974 94.192  1.00 114.67 ? 404 ARG B NH1 1 
ATOM   6352 N NH2 . ARG B 1 417 ? 104.075 124.861 94.935  1.00 112.13 ? 404 ARG B NH2 1 
ATOM   6353 N N   . THR B 1 418 ? 109.378 125.837 88.522  1.00 116.59 ? 405 THR B N   1 
ATOM   6354 C CA  . THR B 1 418 ? 109.498 126.555 87.251  1.00 120.00 ? 405 THR B CA  1 
ATOM   6355 C C   . THR B 1 418 ? 108.555 127.752 87.175  1.00 116.82 ? 405 THR B C   1 
ATOM   6356 O O   . THR B 1 418 ? 108.617 128.535 86.221  1.00 112.37 ? 405 THR B O   1 
ATOM   6357 C CB  . THR B 1 418 ? 109.247 125.628 86.055  1.00 121.13 ? 405 THR B CB  1 
ATOM   6358 O OG1 . THR B 1 418 ? 107.859 125.277 85.999  1.00 120.15 ? 405 THR B OG1 1 
ATOM   6359 C CG2 . THR B 1 418 ? 110.081 124.364 86.174  1.00 116.83 ? 405 THR B CG2 1 
ATOM   6360 N N   . ASN B 1 419 ? 107.691 127.912 88.171  1.00 115.52 ? 406 ASN B N   1 
ATOM   6361 C CA  . ASN B 1 419 ? 106.887 129.122 88.315  1.00 109.28 ? 406 ASN B CA  1 
ATOM   6362 C C   . ASN B 1 419 ? 107.800 130.211 88.862  1.00 105.90 ? 406 ASN B C   1 
ATOM   6363 O O   . ASN B 1 419 ? 108.134 130.225 90.050  1.00 104.31 ? 406 ASN B O   1 
ATOM   6364 C CB  . ASN B 1 419 ? 105.690 128.855 89.219  1.00 110.56 ? 406 ASN B CB  1 
ATOM   6365 C CG  . ASN B 1 419 ? 105.014 130.123 89.694  1.00 111.25 ? 406 ASN B CG  1 
ATOM   6366 O OD1 . ASN B 1 419 ? 105.519 130.801 90.583  1.00 106.36 ? 406 ASN B OD1 1 
ATOM   6367 N ND2 . ASN B 1 419 ? 103.860 130.443 89.110  1.00 117.53 ? 406 ASN B ND2 1 
ATOM   6368 N N   . VAL B 1 420 ? 108.213 131.127 87.982  1.00 110.49 ? 407 VAL B N   1 
ATOM   6369 C CA  . VAL B 1 420 ? 109.356 131.991 88.269  1.00 110.44 ? 407 VAL B CA  1 
ATOM   6370 C C   . VAL B 1 420 ? 109.079 132.905 89.459  1.00 105.26 ? 407 VAL B C   1 
ATOM   6371 O O   . VAL B 1 420 ? 109.969 133.160 90.281  1.00 97.86  ? 407 VAL B O   1 
ATOM   6372 C CB  . VAL B 1 420 ? 109.746 132.786 87.008  1.00 105.84 ? 407 VAL B CB  1 
ATOM   6373 C CG1 . VAL B 1 420 ? 108.556 133.568 86.470  1.00 100.22 ? 407 VAL B CG1 1 
ATOM   6374 C CG2 . VAL B 1 420 ? 110.921 133.706 87.301  1.00 101.33 ? 407 VAL B CG2 1 
ATOM   6375 N N   . SER B 1 421 ? 107.851 133.415 89.578  1.00 107.04 ? 408 SER B N   1 
ATOM   6376 C CA  . SER B 1 421 ? 107.571 134.342 90.669  1.00 102.71 ? 408 SER B CA  1 
ATOM   6377 C C   . SER B 1 421 ? 107.680 133.678 92.034  1.00 101.01 ? 408 SER B C   1 
ATOM   6378 O O   . SER B 1 421 ? 108.147 134.318 92.982  1.00 98.22  ? 408 SER B O   1 
ATOM   6379 C CB  . SER B 1 421 ? 106.183 134.958 90.502  1.00 105.52 ? 408 SER B CB  1 
ATOM   6380 O OG  . SER B 1 421 ? 105.876 135.806 91.595  1.00 105.24 ? 408 SER B OG  1 
ATOM   6381 N N   . HIS B 1 422 ? 107.365 132.389 92.136  1.00 101.66 ? 409 HIS B N   1 
ATOM   6382 C CA  . HIS B 1 422 ? 107.434 131.698 93.415  1.00 99.20  ? 409 HIS B CA  1 
ATOM   6383 C C   . HIS B 1 422 ? 108.846 131.265 93.787  1.00 94.35  ? 409 HIS B C   1 
ATOM   6384 O O   . HIS B 1 422 ? 109.200 131.321 94.966  1.00 91.21  ? 409 HIS B O   1 
ATOM   6385 C CB  . HIS B 1 422 ? 106.508 130.476 93.406  1.00 97.74  ? 409 HIS B CB  1 
ATOM   6386 C CG  . HIS B 1 422 ? 106.821 129.471 94.468  1.00 98.86  ? 409 HIS B CG  1 
ATOM   6387 N ND1 . HIS B 1 422 ? 106.505 129.665 95.795  1.00 101.02 ? 409 HIS B ND1 1 
ATOM   6388 C CD2 . HIS B 1 422 ? 107.419 128.258 94.396  1.00 99.31  ? 409 HIS B CD2 1 
ATOM   6389 C CE1 . HIS B 1 422 ? 106.895 128.614 96.495  1.00 102.64 ? 409 HIS B CE1 1 
ATOM   6390 N NE2 . HIS B 1 422 ? 107.452 127.747 95.670  1.00 102.44 ? 409 HIS B NE2 1 
ATOM   6391 N N   . VAL B 1 423 ? 109.679 130.866 92.821  1.00 93.45  ? 410 VAL B N   1 
ATOM   6392 C CA  . VAL B 1 423 ? 111.082 130.613 93.146  1.00 88.33  ? 410 VAL B CA  1 
ATOM   6393 C C   . VAL B 1 423 ? 111.783 131.920 93.506  1.00 89.35  ? 410 VAL B C   1 
ATOM   6394 O O   . VAL B 1 423 ? 112.626 131.957 94.414  1.00 87.87  ? 410 VAL B O   1 
ATOM   6395 C CB  . VAL B 1 423 ? 111.795 129.861 92.002  1.00 88.60  ? 410 VAL B CB  1 
ATOM   6396 C CG1 . VAL B 1 423 ? 111.732 130.629 90.700  1.00 91.56  ? 410 VAL B CG1 1 
ATOM   6397 C CG2 . VAL B 1 423 ? 113.250 129.559 92.373  1.00 84.95  ? 410 VAL B CG2 1 
ATOM   6398 N N   . VAL B 1 424 ? 111.436 133.015 92.822  1.00 91.45  ? 411 VAL B N   1 
ATOM   6399 C CA  . VAL B 1 424 ? 111.984 134.317 93.194  1.00 88.66  ? 411 VAL B CA  1 
ATOM   6400 C C   . VAL B 1 424 ? 111.537 134.700 94.598  1.00 85.72  ? 411 VAL B C   1 
ATOM   6401 O O   . VAL B 1 424 ? 112.323 135.231 95.391  1.00 79.91  ? 411 VAL B O   1 
ATOM   6402 C CB  . VAL B 1 424 ? 111.591 135.382 92.153  1.00 94.12  ? 411 VAL B CB  1 
ATOM   6403 C CG1 . VAL B 1 424 ? 111.816 136.786 92.700  1.00 96.41  ? 411 VAL B CG1 1 
ATOM   6404 C CG2 . VAL B 1 424 ? 112.400 135.179 90.886  1.00 94.18  ? 411 VAL B CG2 1 
ATOM   6405 N N   . GLY B 1 425 ? 110.275 134.424 94.934  1.00 89.19  ? 412 GLY B N   1 
ATOM   6406 C CA  . GLY B 1 425 ? 109.809 134.678 96.286  1.00 88.51  ? 412 GLY B CA  1 
ATOM   6407 C C   . GLY B 1 425 ? 110.533 133.839 97.319  1.00 86.72  ? 412 GLY B C   1 
ATOM   6408 O O   . GLY B 1 425 ? 110.870 134.325 98.401  1.00 82.46  ? 412 GLY B O   1 
ATOM   6409 N N   . GLN B 1 426 ? 110.778 132.567 97.002  1.00 85.72  ? 413 GLN B N   1 
ATOM   6410 C CA  . GLN B 1 426 ? 111.499 131.696 97.924  1.00 79.64  ? 413 GLN B CA  1 
ATOM   6411 C C   . GLN B 1 426 ? 112.910 132.211 98.180  1.00 75.43  ? 413 GLN B C   1 
ATOM   6412 O O   . GLN B 1 426 ? 113.351 132.302 99.333  1.00 75.34  ? 413 GLN B O   1 
ATOM   6413 C CB  . GLN B 1 426 ? 111.540 130.268 97.378  1.00 80.83  ? 413 GLN B CB  1 
ATOM   6414 C CG  . GLN B 1 426 ? 110.214 129.534 97.461  1.00 87.54  ? 413 GLN B CG  1 
ATOM   6415 C CD  . GLN B 1 426 ? 110.265 128.153 96.834  1.00 92.10  ? 413 GLN B CD  1 
ATOM   6416 O OE1 . GLN B 1 426 ? 109.589 127.230 97.287  1.00 89.60  ? 413 GLN B OE1 1 
ATOM   6417 N NE2 . GLN B 1 426 ? 111.057 128.008 95.777  1.00 92.28  ? 413 GLN B NE2 1 
ATOM   6418 N N   . LEU B 1 427 ? 113.633 132.567 97.116  1.00 72.94  ? 414 LEU B N   1 
ATOM   6419 C CA  . LEU B 1 427 ? 114.990 133.065 97.316  1.00 68.03  ? 414 LEU B CA  1 
ATOM   6420 C C   . LEU B 1 427 ? 114.995 134.425 98.001  1.00 72.97  ? 414 LEU B C   1 
ATOM   6421 O O   . LEU B 1 427 ? 115.892 134.708 98.803  1.00 72.86  ? 414 LEU B O   1 
ATOM   6422 C CB  . LEU B 1 427 ? 115.745 133.125 95.990  1.00 64.71  ? 414 LEU B CB  1 
ATOM   6423 C CG  . LEU B 1 427 ? 115.976 131.750 95.362  1.00 60.40  ? 414 LEU B CG  1 
ATOM   6424 C CD1 . LEU B 1 427 ? 116.597 131.895 93.984  1.00 62.05  ? 414 LEU B CD1 1 
ATOM   6425 C CD2 . LEU B 1 427 ? 116.852 130.881 96.239  1.00 66.11  ? 414 LEU B CD2 1 
ATOM   6426 N N   . ASP B 1 428 ? 113.999 135.267 97.720  1.00 75.72  ? 415 ASP B N   1 
ATOM   6427 C CA  . ASP B 1 428 ? 113.887 136.543 98.415  1.00 73.43  ? 415 ASP B CA  1 
ATOM   6428 C C   . ASP B 1 428 ? 113.636 136.343 99.903  1.00 72.72  ? 415 ASP B C   1 
ATOM   6429 O O   . ASP B 1 428 ? 114.148 137.102 100.732 1.00 73.93  ? 415 ASP B O   1 
ATOM   6430 C CB  . ASP B 1 428 ? 112.770 137.378 97.794  1.00 79.44  ? 415 ASP B CB  1 
ATOM   6431 C CG  . ASP B 1 428 ? 112.563 138.695 98.510  1.00 82.97  ? 415 ASP B CG  1 
ATOM   6432 O OD1 . ASP B 1 428 ? 113.345 139.633 98.258  1.00 83.45  ? 415 ASP B OD1 1 
ATOM   6433 O OD2 . ASP B 1 428 ? 111.624 138.791 99.330  1.00 85.34  ? 415 ASP B OD2 1 
ATOM   6434 N N   . ASP B 1 429 ? 112.826 135.345 100.261 1.00 71.84  ? 416 ASP B N   1 
ATOM   6435 C CA  . ASP B 1 429 ? 112.596 135.053 101.672 1.00 72.63  ? 416 ASP B CA  1 
ATOM   6436 C C   . ASP B 1 429 ? 113.844 134.481 102.332 1.00 69.63  ? 416 ASP B C   1 
ATOM   6437 O O   . ASP B 1 429 ? 114.102 134.740 103.514 1.00 69.33  ? 416 ASP B O   1 
ATOM   6438 C CB  . ASP B 1 429 ? 111.412 134.099 101.834 1.00 72.98  ? 416 ASP B CB  1 
ATOM   6439 C CG  . ASP B 1 429 ? 111.368 133.455 103.209 1.00 71.92  ? 416 ASP B CG  1 
ATOM   6440 O OD1 . ASP B 1 429 ? 111.828 132.300 103.334 1.00 68.40  ? 416 ASP B OD1 1 
ATOM   6441 O OD2 . ASP B 1 429 ? 110.893 134.105 104.167 1.00 72.43  ? 416 ASP B OD2 1 
ATOM   6442 N N   . ILE B 1 430 ? 114.612 133.672 101.597 1.00 68.14  ? 417 ILE B N   1 
ATOM   6443 C CA  . ILE B 1 430 ? 115.885 133.191 102.132 1.00 64.35  ? 417 ILE B CA  1 
ATOM   6444 C C   . ILE B 1 430 ? 116.822 134.362 102.398 1.00 64.54  ? 417 ILE B C   1 
ATOM   6445 O O   . ILE B 1 430 ? 117.481 134.425 103.442 1.00 66.41  ? 417 ILE B O   1 
ATOM   6446 C CB  . ILE B 1 430 ? 116.532 132.164 101.186 1.00 66.68  ? 417 ILE B CB  1 
ATOM   6447 C CG1 . ILE B 1 430 ? 115.665 130.911 101.074 1.00 69.67  ? 417 ILE B CG1 1 
ATOM   6448 C CG2 . ILE B 1 430 ? 117.921 131.796 101.682 1.00 59.22  ? 417 ILE B CG2 1 
ATOM   6449 C CD1 . ILE B 1 430 ? 116.340 129.767 100.357 1.00 56.16  ? 417 ILE B CD1 1 
ATOM   6450 N N   . ARG B 1 431 ? 116.896 135.305 101.456 1.00 65.82  ? 418 ARG B N   1 
ATOM   6451 C CA  . ARG B 1 431 ? 117.725 136.491 101.652 1.00 64.33  ? 418 ARG B CA  1 
ATOM   6452 C C   . ARG B 1 431 ? 117.245 137.311 102.842 1.00 65.76  ? 418 ARG B C   1 
ATOM   6453 O O   . ARG B 1 431 ? 118.056 137.812 103.630 1.00 65.27  ? 418 ARG B O   1 
ATOM   6454 C CB  . ARG B 1 431 ? 117.718 137.359 100.395 1.00 66.92  ? 418 ARG B CB  1 
ATOM   6455 C CG  . ARG B 1 431 ? 118.352 136.755 99.162  1.00 64.53  ? 418 ARG B CG  1 
ATOM   6456 C CD  . ARG B 1 431 ? 118.311 137.771 98.030  1.00 63.49  ? 418 ARG B CD  1 
ATOM   6457 N NE  . ARG B 1 431 ? 118.781 137.234 96.760  1.00 68.03  ? 418 ARG B NE  1 
ATOM   6458 C CZ  . ARG B 1 431 ? 120.051 137.214 96.383  1.00 68.27  ? 418 ARG B CZ  1 
ATOM   6459 N NH1 . ARG B 1 431 ? 121.013 137.664 97.171  1.00 63.25  ? 418 ARG B NH1 1 
ATOM   6460 N NH2 . ARG B 1 431 ? 120.364 136.729 95.186  1.00 69.60  ? 418 ARG B NH2 1 
ATOM   6461 N N   . LYS B 1 432 ? 115.928 137.477 102.975 1.00 67.08  ? 419 LYS B N   1 
ATOM   6462 C CA  . LYS B 1 432 ? 115.374 138.310 104.037 1.00 65.94  ? 419 LYS B CA  1 
ATOM   6463 C C   . LYS B 1 432 ? 115.697 137.745 105.413 1.00 65.55  ? 419 LYS B C   1 
ATOM   6464 O O   . LYS B 1 432 ? 116.111 138.479 106.317 1.00 66.92  ? 419 LYS B O   1 
ATOM   6465 C CB  . LYS B 1 432 ? 113.861 138.444 103.851 1.00 68.66  ? 419 LYS B CB  1 
ATOM   6466 C CG  . LYS B 1 432 ? 113.079 138.706 105.133 1.00 72.04  ? 419 LYS B CG  1 
ATOM   6467 C CD  . LYS B 1 432 ? 113.371 140.079 105.717 1.00 75.83  ? 419 LYS B CD  1 
ATOM   6468 C CE  . LYS B 1 432 ? 112.621 140.294 107.022 1.00 81.29  ? 419 LYS B CE  1 
ATOM   6469 N NZ  . LYS B 1 432 ? 112.837 141.664 107.565 1.00 79.39  ? 419 LYS B NZ  1 
ATOM   6470 N N   . ASN B 1 433 ? 115.504 136.440 105.594 1.00 66.43  ? 420 ASN B N   1 
ATOM   6471 C CA  . ASN B 1 433 ? 115.687 135.781 106.886 1.00 61.70  ? 420 ASN B CA  1 
ATOM   6472 C C   . ASN B 1 433 ? 116.703 134.661 106.712 1.00 61.25  ? 420 ASN B C   1 
ATOM   6473 O O   . ASN B 1 433 ? 116.333 133.520 106.393 1.00 62.97  ? 420 ASN B O   1 
ATOM   6474 C CB  . ASN B 1 433 ? 114.358 135.250 107.418 1.00 61.65  ? 420 ASN B CB  1 
ATOM   6475 C CG  . ASN B 1 433 ? 114.414 134.916 108.892 1.00 68.55  ? 420 ASN B CG  1 
ATOM   6476 O OD1 . ASN B 1 433 ? 115.490 134.749 109.464 1.00 69.05  ? 420 ASN B OD1 1 
ATOM   6477 N ND2 . ASN B 1 433 ? 113.248 134.811 109.517 1.00 76.86  ? 420 ASN B ND2 1 
ATOM   6478 N N   . PRO B 1 434 ? 117.991 134.942 106.896 1.00 54.09  ? 421 PRO B N   1 
ATOM   6479 C CA  . PRO B 1 434 ? 119.001 133.887 106.759 1.00 53.15  ? 421 PRO B CA  1 
ATOM   6480 C C   . PRO B 1 434 ? 118.784 132.787 107.786 1.00 56.20  ? 421 PRO B C   1 
ATOM   6481 O O   . PRO B 1 434 ? 118.396 133.044 108.926 1.00 60.24  ? 421 PRO B O   1 
ATOM   6482 C CB  . PRO B 1 434 ? 120.321 134.629 106.992 1.00 47.64  ? 421 PRO B CB  1 
ATOM   6483 C CG  . PRO B 1 434 ? 119.941 135.834 107.785 1.00 49.34  ? 421 PRO B CG  1 
ATOM   6484 C CD  . PRO B 1 434 ? 118.581 136.228 107.301 1.00 52.54  ? 421 PRO B CD  1 
ATOM   6485 N N   . ARG B 1 435 ? 119.030 131.549 107.365 1.00 50.40  ? 422 ARG B N   1 
ATOM   6486 C CA  . ARG B 1 435 ? 118.854 130.387 108.220 1.00 48.60  ? 422 ARG B CA  1 
ATOM   6487 C C   . ARG B 1 435 ? 120.106 129.525 108.163 1.00 42.76  ? 422 ARG B C   1 
ATOM   6488 O O   . ARG B 1 435 ? 120.874 129.573 107.201 1.00 38.51  ? 422 ARG B O   1 
ATOM   6489 C CB  . ARG B 1 435 ? 117.614 129.578 107.817 1.00 53.02  ? 422 ARG B CB  1 
ATOM   6490 C CG  . ARG B 1 435 ? 116.337 130.069 108.483 1.00 60.36  ? 422 ARG B CG  1 
ATOM   6491 C CD  . ARG B 1 435 ? 115.091 129.454 107.868 1.00 59.03  ? 422 ARG B CD  1 
ATOM   6492 N NE  . ARG B 1 435 ? 114.794 130.015 106.556 1.00 58.76  ? 422 ARG B NE  1 
ATOM   6493 C CZ  . ARG B 1 435 ? 113.652 129.836 105.907 1.00 66.42  ? 422 ARG B CZ  1 
ATOM   6494 N NH1 . ARG B 1 435 ? 112.668 129.119 106.424 1.00 64.44  ? 422 ARG B NH1 1 
ATOM   6495 N NH2 . ARG B 1 435 ? 113.491 130.393 104.710 1.00 71.42  ? 422 ARG B NH2 1 
ATOM   6496 N N   . LYS B 1 436 ? 120.304 128.732 109.220 1.00 43.01  ? 423 LYS B N   1 
ATOM   6497 C CA  . LYS B 1 436 ? 121.560 128.006 109.380 1.00 37.91  ? 423 LYS B CA  1 
ATOM   6498 C C   . LYS B 1 436 ? 121.790 127.018 108.245 1.00 39.82  ? 423 LYS B C   1 
ATOM   6499 O O   . LYS B 1 436 ? 122.901 126.925 107.712 1.00 39.50  ? 423 LYS B O   1 
ATOM   6500 C CB  . LYS B 1 436 ? 121.580 127.287 110.726 1.00 35.96  ? 423 LYS B CB  1 
ATOM   6501 C CG  . LYS B 1 436 ? 121.448 128.207 111.919 1.00 40.25  ? 423 LYS B CG  1 
ATOM   6502 C CD  . LYS B 1 436 ? 121.571 127.432 113.210 1.00 38.57  ? 423 LYS B CD  1 
ATOM   6503 C CE  . LYS B 1 436 ? 122.900 126.713 113.271 1.00 39.00  ? 423 LYS B CE  1 
ATOM   6504 N NZ  . LYS B 1 436 ? 124.032 127.661 113.114 1.00 38.02  ? 423 LYS B NZ  1 
ATOM   6505 N N   . PHE B 1 437 ? 120.759 126.274 107.858 1.00 43.13  ? 424 PHE B N   1 
ATOM   6506 C CA  . PHE B 1 437 ? 120.861 125.283 106.797 1.00 35.69  ? 424 PHE B CA  1 
ATOM   6507 C C   . PHE B 1 437 ? 119.861 125.608 105.700 1.00 38.21  ? 424 PHE B C   1 
ATOM   6508 O O   . PHE B 1 437 ? 118.700 125.918 105.981 1.00 48.54  ? 424 PHE B O   1 
ATOM   6509 C CB  . PHE B 1 437 ? 120.601 123.870 107.324 1.00 29.47  ? 424 PHE B CB  1 
ATOM   6510 C CG  . PHE B 1 437 ? 121.224 123.593 108.659 1.00 32.25  ? 424 PHE B CG  1 
ATOM   6511 C CD1 . PHE B 1 437 ? 122.561 123.260 108.759 1.00 31.62  ? 424 PHE B CD1 1 
ATOM   6512 C CD2 . PHE B 1 437 ? 120.466 123.653 109.814 1.00 35.95  ? 424 PHE B CD2 1 
ATOM   6513 C CE1 . PHE B 1 437 ? 123.132 123.001 109.987 1.00 32.95  ? 424 PHE B CE1 1 
ATOM   6514 C CE2 . PHE B 1 437 ? 121.031 123.394 111.044 1.00 34.19  ? 424 PHE B CE2 1 
ATOM   6515 C CZ  . PHE B 1 437 ? 122.366 123.068 111.131 1.00 32.01  ? 424 PHE B CZ  1 
ATOM   6516 N N   . VAL B 1 438 ? 120.310 125.529 104.451 1.00 33.81  ? 425 VAL B N   1 
ATOM   6517 C CA  . VAL B 1 438 ? 119.455 125.762 103.295 1.00 41.39  ? 425 VAL B CA  1 
ATOM   6518 C C   . VAL B 1 438 ? 119.455 124.508 102.433 1.00 51.88  ? 425 VAL B C   1 
ATOM   6519 O O   . VAL B 1 438 ? 120.502 123.888 102.222 1.00 53.35  ? 425 VAL B O   1 
ATOM   6520 C CB  . VAL B 1 438 ? 119.903 126.995 102.482 1.00 41.15  ? 425 VAL B CB  1 
ATOM   6521 C CG1 . VAL B 1 438 ? 119.693 128.264 103.287 1.00 40.44  ? 425 VAL B CG1 1 
ATOM   6522 C CG2 . VAL B 1 438 ? 121.355 126.872 102.065 1.00 40.05  ? 425 VAL B CG2 1 
ATOM   6523 N N   . CYS B 1 439 ? 118.273 124.123 101.958 1.00 56.60  ? 426 CYS B N   1 
ATOM   6524 C CA  . CYS B 1 439 ? 118.110 122.960 101.092 1.00 57.45  ? 426 CYS B CA  1 
ATOM   6525 C C   . CYS B 1 439 ? 117.327 123.394 99.861  1.00 63.66  ? 426 CYS B C   1 
ATOM   6526 O O   . CYS B 1 439 ? 116.134 123.701 99.957  1.00 69.13  ? 426 CYS B O   1 
ATOM   6527 C CB  . CYS B 1 439 ? 117.398 121.820 101.823 1.00 60.80  ? 426 CYS B CB  1 
ATOM   6528 S SG  . CYS B 1 439 ? 117.249 120.285 100.873 1.00 62.65  ? 426 CYS B SG  1 
ATOM   6529 N N   . LEU B 1 440 ? 117.992 123.419 98.710  1.00 62.65  ? 427 LEU B N   1 
ATOM   6530 C CA  . LEU B 1 440 ? 117.385 123.842 97.449  1.00 67.76  ? 427 LEU B CA  1 
ATOM   6531 C C   . LEU B 1 440 ? 117.264 122.623 96.541  1.00 77.13  ? 427 LEU B C   1 
ATOM   6532 O O   . LEU B 1 440 ? 118.252 122.173 95.954  1.00 78.11  ? 427 LEU B O   1 
ATOM   6533 C CB  . LEU B 1 440 ? 118.207 124.947 96.793  1.00 61.77  ? 427 LEU B CB  1 
ATOM   6534 C CG  . LEU B 1 440 ? 118.343 126.246 97.586  1.00 54.80  ? 427 LEU B CG  1 
ATOM   6535 C CD1 . LEU B 1 440 ? 119.195 127.246 96.830  1.00 55.26  ? 427 LEU B CD1 1 
ATOM   6536 C CD2 . LEU B 1 440 ? 116.976 126.831 97.891  1.00 59.45  ? 427 LEU B CD2 1 
ATOM   6537 N N   . ASN B 1 441 ? 116.050 122.091 96.427  1.00 80.57  ? 428 ASN B N   1 
ATOM   6538 C CA  . ASN B 1 441 ? 115.794 120.949 95.559  1.00 87.74  ? 428 ASN B CA  1 
ATOM   6539 C C   . ASN B 1 441 ? 115.578 121.432 94.131  1.00 98.71  ? 428 ASN B C   1 
ATOM   6540 O O   . ASN B 1 441 ? 114.690 122.253 93.874  1.00 100.32 ? 428 ASN B O   1 
ATOM   6541 C CB  . ASN B 1 441 ? 114.580 120.163 96.050  1.00 83.11  ? 428 ASN B CB  1 
ATOM   6542 C CG  . ASN B 1 441 ? 114.892 119.304 97.259  1.00 80.99  ? 428 ASN B CG  1 
ATOM   6543 O OD1 . ASN B 1 441 ? 114.877 119.780 98.393  1.00 84.37  ? 428 ASN B OD1 1 
ATOM   6544 N ND2 . ASN B 1 441 ? 115.173 118.029 97.021  1.00 74.35  ? 428 ASN B ND2 1 
ATOM   6545 N N   . ASP B 1 442 ? 116.392 120.932 93.205  1.00 104.78 ? 429 ASP B N   1 
ATOM   6546 C CA  . ASP B 1 442 ? 116.257 121.248 91.788  1.00 106.41 ? 429 ASP B CA  1 
ATOM   6547 C C   . ASP B 1 442 ? 115.613 120.057 91.085  1.00 106.89 ? 429 ASP B C   1 
ATOM   6548 O O   . ASP B 1 442 ? 116.184 118.962 91.044  1.00 107.37 ? 429 ASP B O   1 
ATOM   6549 C CB  . ASP B 1 442 ? 117.609 121.596 91.167  1.00 106.06 ? 429 ASP B CB  1 
ATOM   6550 C CG  . ASP B 1 442 ? 118.634 120.493 91.338  1.00 106.99 ? 429 ASP B CG  1 
ATOM   6551 O OD1 . ASP B 1 442 ? 118.697 119.903 92.435  1.00 106.40 ? 429 ASP B OD1 1 
ATOM   6552 O OD2 . ASP B 1 442 ? 119.372 120.211 90.369  1.00 103.09 ? 429 ASP B OD2 1 
ATOM   6553 N N   . ASN B 1 443 ? 114.412 120.268 90.554  1.00 105.15 ? 430 ASN B N   1 
ATOM   6554 C CA  . ASN B 1 443 ? 113.733 119.281 89.723  1.00 107.70 ? 430 ASN B CA  1 
ATOM   6555 C C   . ASN B 1 443 ? 113.108 119.965 88.518  1.00 108.76 ? 430 ASN B C   1 
ATOM   6556 O O   . ASN B 1 443 ? 111.989 119.640 88.105  1.00 110.35 ? 430 ASN B O   1 
ATOM   6557 C CB  . ASN B 1 443 ? 112.684 118.507 90.519  1.00 107.63 ? 430 ASN B CB  1 
ATOM   6558 C CG  . ASN B 1 443 ? 111.627 119.407 91.119  1.00 104.57 ? 430 ASN B CG  1 
ATOM   6559 O OD1 . ASN B 1 443 ? 111.914 120.524 91.545  1.00 101.44 ? 430 ASN B OD1 1 
ATOM   6560 N ND2 . ASN B 1 443 ? 110.390 118.924 91.153  1.00 103.87 ? 430 ASN B ND2 1 
ATOM   6561 N N   . ILE B 1 444 ? 113.827 120.933 87.944  1.00 109.80 ? 431 ILE B N   1 
ATOM   6562 C CA  . ILE B 1 444 ? 113.299 121.688 86.816  1.00 114.35 ? 431 ILE B CA  1 
ATOM   6563 C C   . ILE B 1 444 ? 113.052 120.748 85.645  1.00 117.78 ? 431 ILE B C   1 
ATOM   6564 O O   . ILE B 1 444 ? 113.875 119.878 85.332  1.00 119.23 ? 431 ILE B O   1 
ATOM   6565 C CB  . ILE B 1 444 ? 114.258 122.826 86.428  1.00 113.57 ? 431 ILE B CB  1 
ATOM   6566 C CG1 . ILE B 1 444 ? 114.560 123.718 87.635  1.00 110.88 ? 431 ILE B CG1 1 
ATOM   6567 C CG2 . ILE B 1 444 ? 113.669 123.663 85.303  1.00 112.59 ? 431 ILE B CG2 1 
ATOM   6568 C CD1 . ILE B 1 444 ? 115.882 123.417 88.316  1.00 108.14 ? 431 ILE B CD1 1 
ATOM   6569 N N   . ASP B 1 445 ? 111.897 120.918 84.995  1.00 117.88 ? 432 ASP B N   1 
ATOM   6570 C CA  . ASP B 1 445 ? 111.507 120.022 83.912  1.00 118.24 ? 432 ASP B CA  1 
ATOM   6571 C C   . ASP B 1 445 ? 112.470 120.105 82.734  1.00 120.05 ? 432 ASP B C   1 
ATOM   6572 O O   . ASP B 1 445 ? 112.572 119.153 81.951  1.00 121.36 ? 432 ASP B O   1 
ATOM   6573 C CB  . ASP B 1 445 ? 110.081 120.345 83.463  1.00 115.21 ? 432 ASP B CB  1 
ATOM   6574 C CG  . ASP B 1 445 ? 109.535 119.334 82.476  1.00 119.21 ? 432 ASP B CG  1 
ATOM   6575 O OD1 . ASP B 1 445 ? 109.357 118.160 82.863  1.00 123.30 ? 432 ASP B OD1 1 
ATOM   6576 O OD2 . ASP B 1 445 ? 109.277 119.714 81.316  1.00 118.96 ? 432 ASP B OD2 1 
ATOM   6577 N N   . HIS B 1 446 ? 113.166 121.233 82.584  1.00 119.10 ? 433 HIS B N   1 
ATOM   6578 C CA  . HIS B 1 446 ? 114.150 121.515 81.542  1.00 115.71 ? 433 HIS B CA  1 
ATOM   6579 C C   . HIS B 1 446 ? 113.526 121.633 80.158  1.00 116.69 ? 433 HIS B C   1 
ATOM   6580 O O   . HIS B 1 446 ? 114.245 121.920 79.193  1.00 113.05 ? 433 HIS B O   1 
ATOM   6581 C CB  . HIS B 1 446 ? 115.277 120.472 81.492  1.00 114.31 ? 433 HIS B CB  1 
ATOM   6582 C CG  . HIS B 1 446 ? 116.162 120.481 82.700  1.00 118.28 ? 433 HIS B CG  1 
ATOM   6583 N ND1 . HIS B 1 446 ? 115.862 121.198 83.838  1.00 118.50 ? 433 HIS B ND1 1 
ATOM   6584 C CD2 . HIS B 1 446 ? 117.341 119.862 82.945  1.00 122.07 ? 433 HIS B CD2 1 
ATOM   6585 C CE1 . HIS B 1 446 ? 116.817 121.019 84.733  1.00 118.16 ? 433 HIS B CE1 1 
ATOM   6586 N NE2 . HIS B 1 446 ? 117.726 120.212 84.217  1.00 123.04 ? 433 HIS B NE2 1 
ATOM   6587 N N   . ASN B 1 447 ? 112.216 121.420 80.022  1.00 119.19 ? 434 ASN B N   1 
ATOM   6588 C CA  . ASN B 1 447 ? 111.523 121.666 78.766  1.00 116.97 ? 434 ASN B CA  1 
ATOM   6589 C C   . ASN B 1 447 ? 110.803 123.005 78.748  1.00 117.90 ? 434 ASN B C   1 
ATOM   6590 O O   . ASN B 1 447 ? 110.499 123.514 77.664  1.00 118.27 ? 434 ASN B O   1 
ATOM   6591 C CB  . ASN B 1 447 ? 110.516 120.545 78.483  1.00 113.96 ? 434 ASN B CB  1 
ATOM   6592 C CG  . ASN B 1 447 ? 111.165 119.175 78.441  1.00 113.02 ? 434 ASN B CG  1 
ATOM   6593 O OD1 . ASN B 1 447 ? 111.684 118.753 77.408  1.00 110.82 ? 434 ASN B OD1 1 
ATOM   6594 N ND2 . ASN B 1 447 ? 111.138 118.472 79.567  1.00 113.42 ? 434 ASN B ND2 1 
ATOM   6595 N N   . HIS B 1 448 ? 110.523 123.578 79.915  1.00 118.77 ? 435 HIS B N   1 
ATOM   6596 C CA  . HIS B 1 448 ? 109.966 124.920 79.982  1.00 121.69 ? 435 HIS B CA  1 
ATOM   6597 C C   . HIS B 1 448 ? 110.985 125.927 79.468  1.00 122.88 ? 435 HIS B C   1 
ATOM   6598 O O   . HIS B 1 448 ? 112.186 125.808 79.729  1.00 119.14 ? 435 HIS B O   1 
ATOM   6599 C CB  . HIS B 1 448 ? 109.565 125.254 81.419  1.00 118.82 ? 435 HIS B CB  1 
ATOM   6600 C CG  . HIS B 1 448 ? 108.710 126.477 81.543  1.00 119.50 ? 435 HIS B CG  1 
ATOM   6601 N ND1 . HIS B 1 448 ? 108.421 127.061 82.758  1.00 117.21 ? 435 HIS B ND1 1 
ATOM   6602 C CD2 . HIS B 1 448 ? 108.074 127.221 80.608  1.00 121.65 ? 435 HIS B CD2 1 
ATOM   6603 C CE1 . HIS B 1 448 ? 107.648 128.114 82.565  1.00 118.57 ? 435 HIS B CE1 1 
ATOM   6604 N NE2 . HIS B 1 448 ? 107.423 128.234 81.269  1.00 122.74 ? 435 HIS B NE2 1 
ATOM   6605 N N   . LYS B 1 449 ? 110.501 126.926 78.726  1.00 126.06 ? 436 LYS B N   1 
ATOM   6606 C CA  . LYS B 1 449 ? 111.397 127.928 78.161  1.00 124.21 ? 436 LYS B CA  1 
ATOM   6607 C C   . LYS B 1 449 ? 112.067 128.775 79.234  1.00 120.48 ? 436 LYS B C   1 
ATOM   6608 O O   . LYS B 1 449 ? 113.076 129.429 78.950  1.00 115.30 ? 436 LYS B O   1 
ATOM   6609 C CB  . LYS B 1 449 ? 110.633 128.825 77.187  1.00 125.09 ? 436 LYS B CB  1 
ATOM   6610 C CG  . LYS B 1 449 ? 111.511 129.456 76.122  1.00 128.79 ? 436 LYS B CG  1 
ATOM   6611 C CD  . LYS B 1 449 ? 112.115 128.393 75.219  1.00 129.63 ? 436 LYS B CD  1 
ATOM   6612 C CE  . LYS B 1 449 ? 113.193 128.975 74.322  1.00 134.33 ? 436 LYS B CE  1 
ATOM   6613 N NZ  . LYS B 1 449 ? 114.338 129.502 75.114  1.00 137.78 ? 436 LYS B NZ  1 
ATOM   6614 N N   . ASP B 1 450 ? 111.538 128.773 80.456  1.00 121.95 ? 437 ASP B N   1 
ATOM   6615 C CA  . ASP B 1 450 ? 112.105 129.532 81.561  1.00 119.87 ? 437 ASP B CA  1 
ATOM   6616 C C   . ASP B 1 450 ? 113.113 128.728 82.373  1.00 113.60 ? 437 ASP B C   1 
ATOM   6617 O O   . ASP B 1 450 ? 113.528 129.183 83.444  1.00 108.09 ? 437 ASP B O   1 
ATOM   6618 C CB  . ASP B 1 450 ? 110.991 130.043 82.479  1.00 122.74 ? 437 ASP B CB  1 
ATOM   6619 C CG  . ASP B 1 450 ? 110.043 130.994 81.773  1.00 120.17 ? 437 ASP B CG  1 
ATOM   6620 O OD1 . ASP B 1 450 ? 110.169 131.157 80.541  1.00 121.29 ? 437 ASP B OD1 1 
ATOM   6621 O OD2 . ASP B 1 450 ? 109.174 131.580 82.451  1.00 117.73 ? 437 ASP B OD2 1 
ATOM   6622 N N   . ALA B 1 451 ? 113.505 127.543 81.898  1.00 114.03 ? 438 ALA B N   1 
ATOM   6623 C CA  . ALA B 1 451 ? 114.509 126.758 82.609  1.00 107.15 ? 438 ALA B CA  1 
ATOM   6624 C C   . ALA B 1 451 ? 115.831 127.509 82.698  1.00 97.16  ? 438 ALA B C   1 
ATOM   6625 O O   . ALA B 1 451 ? 116.478 127.522 83.753  1.00 94.32  ? 438 ALA B O   1 
ATOM   6626 C CB  . ALA B 1 451 ? 114.703 125.407 81.922  1.00 111.85 ? 438 ALA B CB  1 
ATOM   6627 N N   . GLN B 1 452 ? 116.247 128.145 81.601  1.00 98.54  ? 439 GLN B N   1 
ATOM   6628 C CA  . GLN B 1 452 ? 117.447 128.972 81.645  1.00 98.67  ? 439 GLN B CA  1 
ATOM   6629 C C   . GLN B 1 452 ? 117.265 130.166 82.570  1.00 93.83  ? 439 GLN B C   1 
ATOM   6630 O O   . GLN B 1 452 ? 118.222 130.593 83.223  1.00 91.92  ? 439 GLN B O   1 
ATOM   6631 C CB  . GLN B 1 452 ? 117.823 129.439 80.239  1.00 100.47 ? 439 GLN B CB  1 
ATOM   6632 C CG  . GLN B 1 452 ? 118.358 128.335 79.341  1.00 97.78  ? 439 GLN B CG  1 
ATOM   6633 C CD  . GLN B 1 452 ? 118.881 128.862 78.019  1.00 98.22  ? 439 GLN B CD  1 
ATOM   6634 O OE1 . GLN B 1 452 ? 118.625 130.008 77.649  1.00 99.03  ? 439 GLN B OE1 1 
ATOM   6635 N NE2 . GLN B 1 452 ? 119.623 128.027 77.301  1.00 100.61 ? 439 GLN B NE2 1 
ATOM   6636 N N   . THR B 1 453 ? 116.052 130.720 82.638  1.00 92.05  ? 440 THR B N   1 
ATOM   6637 C CA  . THR B 1 453 ? 115.799 131.829 83.553  1.00 90.37  ? 440 THR B CA  1 
ATOM   6638 C C   . THR B 1 453 ? 115.954 131.394 85.007  1.00 85.29  ? 440 THR B C   1 
ATOM   6639 O O   . THR B 1 453 ? 116.556 132.110 85.815  1.00 83.65  ? 440 THR B O   1 
ATOM   6640 C CB  . THR B 1 453 ? 114.405 132.404 83.310  1.00 98.92  ? 440 THR B CB  1 
ATOM   6641 O OG1 . THR B 1 453 ? 114.278 132.782 81.933  1.00 102.53 ? 440 THR B OG1 1 
ATOM   6642 C CG2 . THR B 1 453 ? 114.173 133.626 84.186  1.00 96.30  ? 440 THR B CG2 1 
ATOM   6643 N N   . VAL B 1 454 ? 115.421 130.222 85.358  1.00 87.26  ? 441 VAL B N   1 
ATOM   6644 C CA  . VAL B 1 454 ? 115.582 129.709 86.717  1.00 83.88  ? 441 VAL B CA  1 
ATOM   6645 C C   . VAL B 1 454 ? 117.048 129.405 87.000  1.00 78.35  ? 441 VAL B C   1 
ATOM   6646 O O   . VAL B 1 454 ? 117.548 129.656 88.104  1.00 77.10  ? 441 VAL B O   1 
ATOM   6647 C CB  . VAL B 1 454 ? 114.692 128.472 86.932  1.00 86.84  ? 441 VAL B CB  1 
ATOM   6648 C CG1 . VAL B 1 454 ? 114.972 127.844 88.284  1.00 87.70  ? 441 VAL B CG1 1 
ATOM   6649 C CG2 . VAL B 1 454 ? 113.223 128.850 86.816  1.00 88.34  ? 441 VAL B CG2 1 
ATOM   6650 N N   . LYS B 1 455 ? 117.757 128.854 86.012  1.00 80.84  ? 442 LYS B N   1 
ATOM   6651 C CA  . LYS B 1 455 ? 119.186 128.605 86.176  1.00 78.11  ? 442 LYS B CA  1 
ATOM   6652 C C   . LYS B 1 455 ? 119.942 129.899 86.448  1.00 73.32  ? 442 LYS B C   1 
ATOM   6653 O O   . LYS B 1 455 ? 120.795 129.953 87.343  1.00 73.93  ? 442 LYS B O   1 
ATOM   6654 C CB  . LYS B 1 455 ? 119.736 127.914 84.929  1.00 88.73  ? 442 LYS B CB  1 
ATOM   6655 C CG  . LYS B 1 455 ? 121.244 128.008 84.761  1.00 92.24  ? 442 LYS B CG  1 
ATOM   6656 C CD  . LYS B 1 455 ? 121.955 126.808 85.364  1.00 98.78  ? 442 LYS B CD  1 
ATOM   6657 C CE  . LYS B 1 455 ? 123.448 126.860 85.076  1.00 97.04  ? 442 LYS B CE  1 
ATOM   6658 N NZ  . LYS B 1 455 ? 124.155 125.631 85.530  1.00 98.93  ? 442 LYS B NZ  1 
ATOM   6659 N N   . ALA B 1 456 ? 119.631 130.955 85.694  1.00 72.67  ? 443 ALA B N   1 
ATOM   6660 C CA  . ALA B 1 456 ? 120.284 132.242 85.903  1.00 72.57  ? 443 ALA B CA  1 
ATOM   6661 C C   . ALA B 1 456 ? 119.940 132.825 87.266  1.00 71.69  ? 443 ALA B C   1 
ATOM   6662 O O   . ALA B 1 456 ? 120.801 133.411 87.928  1.00 72.23  ? 443 ALA B O   1 
ATOM   6663 C CB  . ALA B 1 456 ? 119.896 133.216 84.791  1.00 75.24  ? 443 ALA B CB  1 
ATOM   6664 N N   . VAL B 1 457 ? 118.687 132.681 87.701  1.00 70.81  ? 444 VAL B N   1 
ATOM   6665 C CA  . VAL B 1 457 ? 118.286 133.203 89.007  1.00 66.04  ? 444 VAL B CA  1 
ATOM   6666 C C   . VAL B 1 457 ? 119.033 132.482 90.124  1.00 64.06  ? 444 VAL B C   1 
ATOM   6667 O O   . VAL B 1 457 ? 119.509 133.105 91.082  1.00 65.50  ? 444 VAL B O   1 
ATOM   6668 C CB  . VAL B 1 457 ? 116.762 133.097 89.187  1.00 66.20  ? 444 VAL B CB  1 
ATOM   6669 C CG1 . VAL B 1 457 ? 116.386 133.284 90.645  1.00 64.45  ? 444 VAL B CG1 1 
ATOM   6670 C CG2 . VAL B 1 457 ? 116.061 134.134 88.329  1.00 72.03  ? 444 VAL B CG2 1 
ATOM   6671 N N   . LEU B 1 458 ? 119.135 131.155 90.027  1.00 66.69  ? 445 LEU B N   1 
ATOM   6672 C CA  . LEU B 1 458 ? 119.854 130.399 91.048  1.00 66.46  ? 445 LEU B CA  1 
ATOM   6673 C C   . LEU B 1 458 ? 121.343 130.723 91.035  1.00 62.50  ? 445 LEU B C   1 
ATOM   6674 O O   . LEU B 1 458 ? 121.972 130.811 92.095  1.00 59.46  ? 445 LEU B O   1 
ATOM   6675 C CB  . LEU B 1 458 ? 119.625 128.901 90.857  1.00 72.31  ? 445 LEU B CB  1 
ATOM   6676 C CG  . LEU B 1 458 ? 118.593 128.277 91.801  1.00 69.89  ? 445 LEU B CG  1 
ATOM   6677 C CD1 . LEU B 1 458 ? 119.085 128.348 93.232  1.00 60.11  ? 445 LEU B CD1 1 
ATOM   6678 C CD2 . LEU B 1 458 ? 117.241 128.959 91.672  1.00 72.44  ? 445 LEU B CD2 1 
ATOM   6679 N N   . ARG B 1 459 ? 121.926 130.903 89.846  1.00 66.68  ? 446 ARG B N   1 
ATOM   6680 C CA  . ARG B 1 459 ? 123.318 131.331 89.766  1.00 62.93  ? 446 ARG B CA  1 
ATOM   6681 C C   . ARG B 1 459 ? 123.504 132.699 90.410  1.00 59.75  ? 446 ARG B C   1 
ATOM   6682 O O   . ARG B 1 459 ? 124.497 132.934 91.107  1.00 62.84  ? 446 ARG B O   1 
ATOM   6683 C CB  . ARG B 1 459 ? 123.778 131.350 88.309  1.00 69.10  ? 446 ARG B CB  1 
ATOM   6684 C CG  . ARG B 1 459 ? 125.236 131.723 88.125  1.00 68.04  ? 446 ARG B CG  1 
ATOM   6685 C CD  . ARG B 1 459 ? 126.129 130.812 88.938  1.00 73.70  ? 446 ARG B CD  1 
ATOM   6686 N NE  . ARG B 1 459 ? 125.954 129.412 88.572  1.00 81.84  ? 446 ARG B NE  1 
ATOM   6687 C CZ  . ARG B 1 459 ? 126.736 128.757 87.726  1.00 81.35  ? 446 ARG B CZ  1 
ATOM   6688 N NH1 . ARG B 1 459 ? 127.767 129.344 87.141  1.00 79.31  ? 446 ARG B NH1 1 
ATOM   6689 N NH2 . ARG B 1 459 ? 126.478 127.480 87.461  1.00 83.96  ? 446 ARG B NH2 1 
ATOM   6690 N N   . ASP B 1 460 ? 122.558 133.614 90.183  1.00 60.78  ? 447 ASP B N   1 
ATOM   6691 C CA  . ASP B 1 460 ? 122.628 134.940 90.789  1.00 64.34  ? 447 ASP B CA  1 
ATOM   6692 C C   . ASP B 1 460 ? 122.557 134.853 92.307  1.00 61.76  ? 447 ASP B C   1 
ATOM   6693 O O   . ASP B 1 460 ? 123.330 135.512 93.010  1.00 59.34  ? 447 ASP B O   1 
ATOM   6694 C CB  . ASP B 1 460 ? 121.499 135.820 90.248  1.00 65.39  ? 447 ASP B CB  1 
ATOM   6695 C CG  . ASP B 1 460 ? 121.601 137.260 90.716  1.00 67.91  ? 447 ASP B CG  1 
ATOM   6696 O OD1 . ASP B 1 460 ? 122.727 137.720 90.997  1.00 70.50  ? 447 ASP B OD1 1 
ATOM   6697 O OD2 . ASP B 1 460 ? 120.551 137.932 90.811  1.00 69.69  ? 447 ASP B OD2 1 
ATOM   6698 N N   . PHE B 1 461 ? 121.644 134.031 92.828  1.00 61.42  ? 448 PHE B N   1 
ATOM   6699 C CA  . PHE B 1 461 ? 121.546 133.846 94.272  1.00 58.24  ? 448 PHE B CA  1 
ATOM   6700 C C   . PHE B 1 461 ? 122.836 133.272 94.846  1.00 57.21  ? 448 PHE B C   1 
ATOM   6701 O O   . PHE B 1 461 ? 123.359 133.771 95.851  1.00 57.48  ? 448 PHE B O   1 
ATOM   6702 C CB  . PHE B 1 461 ? 120.364 132.937 94.602  1.00 58.02  ? 448 PHE B CB  1 
ATOM   6703 C CG  . PHE B 1 461 ? 120.190 132.691 96.067  1.00 54.82  ? 448 PHE B CG  1 
ATOM   6704 C CD1 . PHE B 1 461 ? 119.574 133.635 96.872  1.00 59.50  ? 448 PHE B CD1 1 
ATOM   6705 C CD2 . PHE B 1 461 ? 120.644 131.521 96.643  1.00 53.82  ? 448 PHE B CD2 1 
ATOM   6706 C CE1 . PHE B 1 461 ? 119.414 133.412 98.225  1.00 61.61  ? 448 PHE B CE1 1 
ATOM   6707 C CE2 . PHE B 1 461 ? 120.488 131.292 97.991  1.00 57.57  ? 448 PHE B CE2 1 
ATOM   6708 C CZ  . PHE B 1 461 ? 119.871 132.238 98.785  1.00 59.95  ? 448 PHE B CZ  1 
ATOM   6709 N N   . TYR B 1 462 ? 123.363 132.220 94.216  1.00 61.58  ? 449 TYR B N   1 
ATOM   6710 C CA  . TYR B 1 462 ? 124.579 131.585 94.714  1.00 59.07  ? 449 TYR B CA  1 
ATOM   6711 C C   . TYR B 1 462 ? 125.760 132.547 94.695  1.00 57.65  ? 449 TYR B C   1 
ATOM   6712 O O   . TYR B 1 462 ? 126.535 132.605 95.656  1.00 53.71  ? 449 TYR B O   1 
ATOM   6713 C CB  . TYR B 1 462 ? 124.899 130.340 93.887  1.00 62.02  ? 449 TYR B CB  1 
ATOM   6714 C CG  . TYR B 1 462 ? 123.974 129.172 94.134  1.00 57.20  ? 449 TYR B CG  1 
ATOM   6715 C CD1 . TYR B 1 462 ? 123.202 129.106 95.284  1.00 57.11  ? 449 TYR B CD1 1 
ATOM   6716 C CD2 . TYR B 1 462 ? 123.878 128.133 93.220  1.00 59.34  ? 449 TYR B CD2 1 
ATOM   6717 C CE1 . TYR B 1 462 ? 122.358 128.039 95.515  1.00 58.33  ? 449 TYR B CE1 1 
ATOM   6718 C CE2 . TYR B 1 462 ? 123.037 127.062 93.442  1.00 68.95  ? 449 TYR B CE2 1 
ATOM   6719 C CZ  . TYR B 1 462 ? 122.279 127.020 94.590  1.00 67.26  ? 449 TYR B CZ  1 
ATOM   6720 O OH  . TYR B 1 462 ? 121.441 125.951 94.811  1.00 72.89  ? 449 TYR B OH  1 
ATOM   6721 N N   . GLU B 1 463 ? 125.918 133.310 93.610  1.00 58.66  ? 450 GLU B N   1 
ATOM   6722 C CA  . GLU B 1 463 ? 127.036 134.243 93.528  1.00 56.03  ? 450 GLU B CA  1 
ATOM   6723 C C   . GLU B 1 463 ? 126.877 135.385 94.523  1.00 58.77  ? 450 GLU B C   1 
ATOM   6724 O O   . GLU B 1 463 ? 127.862 135.834 95.121  1.00 62.93  ? 450 GLU B O   1 
ATOM   6725 C CB  . GLU B 1 463 ? 127.172 134.784 92.105  1.00 55.97  ? 450 GLU B CB  1 
ATOM   6726 C CG  . GLU B 1 463 ? 127.624 133.755 91.074  1.00 59.71  ? 450 GLU B CG  1 
ATOM   6727 C CD  . GLU B 1 463 ? 129.128 133.522 91.076  1.00 62.58  ? 450 GLU B CD  1 
ATOM   6728 O OE1 . GLU B 1 463 ? 129.794 133.876 92.072  1.00 61.91  ? 450 GLU B OE1 1 
ATOM   6729 O OE2 . GLU B 1 463 ? 129.650 132.990 90.075  1.00 63.90  ? 450 GLU B OE2 1 
ATOM   6730 N N   . SER B 1 464 ? 125.649 135.876 94.711  1.00 58.12  ? 451 SER B N   1 
ATOM   6731 C CA  . SER B 1 464 ? 125.425 136.944 95.676  1.00 56.60  ? 451 SER B CA  1 
ATOM   6732 C C   . SER B 1 464 ? 125.721 136.477 97.094  1.00 51.94  ? 451 SER B C   1 
ATOM   6733 O O   . SER B 1 464 ? 126.302 137.222 97.891  1.00 50.27  ? 451 SER B O   1 
ATOM   6734 C CB  . SER B 1 464 ? 123.990 137.455 95.565  1.00 58.60  ? 451 SER B CB  1 
ATOM   6735 O OG  . SER B 1 464 ? 123.715 138.423 96.562  1.00 56.90  ? 451 SER B OG  1 
ATOM   6736 N N   . MET B 1 465 ? 125.330 135.246 97.432  1.00 54.00  ? 452 MET B N   1 
ATOM   6737 C CA  . MET B 1 465 ? 125.554 134.768 98.792  1.00 52.86  ? 452 MET B CA  1 
ATOM   6738 C C   . MET B 1 465 ? 127.028 134.485 99.065  1.00 56.17  ? 452 MET B C   1 
ATOM   6739 O O   . MET B 1 465 ? 127.486 134.663 100.198 1.00 54.66  ? 452 MET B O   1 
ATOM   6740 C CB  . MET B 1 465 ? 124.710 133.520 99.060  1.00 51.30  ? 452 MET B CB  1 
ATOM   6741 C CG  . MET B 1 465 ? 124.270 133.368 100.509 1.00 50.12  ? 452 MET B CG  1 
ATOM   6742 S SD  . MET B 1 465 ? 123.211 131.933 100.788 1.00 63.64  ? 452 MET B SD  1 
ATOM   6743 C CE  . MET B 1 465 ? 122.521 132.335 102.393 1.00 58.25  ? 452 MET B CE  1 
ATOM   6744 N N   . PHE B 1 466 ? 127.783 134.044 98.059  1.00 60.17  ? 453 PHE B N   1 
ATOM   6745 C CA  . PHE B 1 466 ? 129.207 133.753 98.232  1.00 56.55  ? 453 PHE B CA  1 
ATOM   6746 C C   . PHE B 1 466 ? 129.936 134.140 96.958  1.00 57.92  ? 453 PHE B C   1 
ATOM   6747 O O   . PHE B 1 466 ? 130.164 133.304 96.073  1.00 57.93  ? 453 PHE B O   1 
ATOM   6748 C CB  . PHE B 1 466 ? 129.460 132.282 98.560  1.00 54.19  ? 453 PHE B CB  1 
ATOM   6749 C CG  . PHE B 1 466 ? 128.524 131.713 99.581  1.00 50.00  ? 453 PHE B CG  1 
ATOM   6750 C CD1 . PHE B 1 466 ? 128.728 131.931 100.932 1.00 47.35  ? 453 PHE B CD1 1 
ATOM   6751 C CD2 . PHE B 1 466 ? 127.451 130.944 99.189  1.00 48.73  ? 453 PHE B CD2 1 
ATOM   6752 C CE1 . PHE B 1 466 ? 127.869 131.402 101.873 1.00 46.10  ? 453 PHE B CE1 1 
ATOM   6753 C CE2 . PHE B 1 466 ? 126.592 130.414 100.123 1.00 47.72  ? 453 PHE B CE2 1 
ATOM   6754 C CZ  . PHE B 1 466 ? 126.804 130.645 101.467 1.00 47.64  ? 453 PHE B CZ  1 
ATOM   6755 N N   . PRO B 1 467 ? 130.319 135.406 96.825  1.00 53.88  ? 454 PRO B N   1 
ATOM   6756 C CA  . PRO B 1 467 ? 131.020 135.841 95.611  1.00 57.82  ? 454 PRO B CA  1 
ATOM   6757 C C   . PRO B 1 467 ? 132.516 135.572 95.658  1.00 62.37  ? 454 PRO B C   1 
ATOM   6758 O O   . PRO B 1 467 ? 133.160 135.432 94.613  1.00 61.39  ? 454 PRO B O   1 
ATOM   6759 C CB  . PRO B 1 467 ? 130.726 137.343 95.570  1.00 58.36  ? 454 PRO B CB  1 
ATOM   6760 C CG  . PRO B 1 467 ? 130.607 137.715 97.001  1.00 57.30  ? 454 PRO B CG  1 
ATOM   6761 C CD  . PRO B 1 467 ? 130.005 136.535 97.716  1.00 52.66  ? 454 PRO B CD  1 
ATOM   6762 N N   . ILE B 1 468 ? 133.076 135.500 96.859  1.00 64.15  ? 455 ILE B N   1 
ATOM   6763 C CA  . ILE B 1 468 ? 134.528 135.349 97.008  1.00 65.32  ? 455 ILE B CA  1 
ATOM   6764 C C   . ILE B 1 468 ? 134.935 133.940 96.590  1.00 68.41  ? 455 ILE B C   1 
ATOM   6765 O O   . ILE B 1 468 ? 134.354 132.958 97.085  1.00 68.15  ? 455 ILE B O   1 
ATOM   6766 C CB  . ILE B 1 468 ? 134.949 135.633 98.450  1.00 63.10  ? 455 ILE B CB  1 
ATOM   6767 C CG1 . ILE B 1 468 ? 134.606 137.073 98.841  1.00 66.85  ? 455 ILE B CG1 1 
ATOM   6768 C CG2 . ILE B 1 468 ? 136.436 135.379 98.625  1.00 66.01  ? 455 ILE B CG2 1 
ATOM   6769 C CD1 . ILE B 1 468 ? 133.285 137.220 99.565  1.00 69.44  ? 455 ILE B CD1 1 
ATOM   6770 N N   . PRO B 1 469 ? 135.905 133.785 95.689  1.00 69.34  ? 456 PRO B N   1 
ATOM   6771 C CA  . PRO B 1 469 ? 136.407 132.444 95.372  1.00 65.28  ? 456 PRO B CA  1 
ATOM   6772 C C   . PRO B 1 469 ? 137.005 131.779 96.602  1.00 64.52  ? 456 PRO B C   1 
ATOM   6773 O O   . PRO B 1 469 ? 137.593 132.433 97.467  1.00 62.07  ? 456 PRO B O   1 
ATOM   6774 C CB  . PRO B 1 469 ? 137.472 132.706 94.301  1.00 67.09  ? 456 PRO B CB  1 
ATOM   6775 C CG  . PRO B 1 469 ? 137.102 134.030 93.714  1.00 72.80  ? 456 PRO B CG  1 
ATOM   6776 C CD  . PRO B 1 469 ? 136.525 134.822 94.849  1.00 72.30  ? 456 PRO B CD  1 
ATOM   6777 N N   . SER B 1 470 ? 136.842 130.463 96.676  1.00 68.67  ? 457 SER B N   1 
ATOM   6778 C CA  . SER B 1 470 ? 137.255 129.704 97.845  1.00 68.84  ? 457 SER B CA  1 
ATOM   6779 C C   . SER B 1 470 ? 138.690 129.204 97.700  1.00 74.84  ? 457 SER B C   1 
ATOM   6780 O O   . SER B 1 470 ? 139.292 129.246 96.625  1.00 80.57  ? 457 SER B O   1 
ATOM   6781 C CB  . SER B 1 470 ? 136.309 128.528 98.080  1.00 59.16  ? 457 SER B CB  1 
ATOM   6782 O OG  . SER B 1 470 ? 136.746 127.745 99.175  1.00 56.95  ? 457 SER B OG  1 
ATOM   6783 N N   . GLN B 1 471 ? 139.236 128.720 98.818  1.00 68.30  ? 458 GLN B N   1 
ATOM   6784 C CA  . GLN B 1 471 ? 140.590 128.181 98.829  1.00 68.43  ? 458 GLN B CA  1 
ATOM   6785 C C   . GLN B 1 471 ? 140.711 126.893 98.026  1.00 70.27  ? 458 GLN B C   1 
ATOM   6786 O O   . GLN B 1 471 ? 141.824 126.519 97.644  1.00 73.85  ? 458 GLN B O   1 
ATOM   6787 C CB  . GLN B 1 471 ? 141.040 127.928 100.267 1.00 69.46  ? 458 GLN B CB  1 
ATOM   6788 C CG  . GLN B 1 471 ? 140.884 129.124 101.185 1.00 68.88  ? 458 GLN B CG  1 
ATOM   6789 C CD  . GLN B 1 471 ? 141.223 128.796 102.624 1.00 73.09  ? 458 GLN B CD  1 
ATOM   6790 O OE1 . GLN B 1 471 ? 141.270 127.628 103.012 1.00 72.07  ? 458 GLN B OE1 1 
ATOM   6791 N NE2 . GLN B 1 471 ? 141.464 129.827 103.424 1.00 69.88  ? 458 GLN B NE2 1 
ATOM   6792 N N   . PHE B 1 472 ? 139.597 126.211 97.762  1.00 68.33  ? 459 PHE B N   1 
ATOM   6793 C CA  . PHE B 1 472 ? 139.602 124.921 97.088  1.00 69.62  ? 459 PHE B CA  1 
ATOM   6794 C C   . PHE B 1 472 ? 139.438 125.042 95.577  1.00 72.84  ? 459 PHE B C   1 
ATOM   6795 O O   . PHE B 1 472 ? 139.312 124.019 94.897  1.00 72.41  ? 459 PHE B O   1 
ATOM   6796 C CB  . PHE B 1 472 ? 138.500 124.023 97.654  1.00 64.84  ? 459 PHE B CB  1 
ATOM   6797 C CG  . PHE B 1 472 ? 138.487 123.944 99.154  1.00 60.24  ? 459 PHE B CG  1 
ATOM   6798 C CD1 . PHE B 1 472 ? 139.444 123.211 99.834  1.00 61.24  ? 459 PHE B CD1 1 
ATOM   6799 C CD2 . PHE B 1 472 ? 137.507 124.593 99.883  1.00 56.57  ? 459 PHE B CD2 1 
ATOM   6800 C CE1 . PHE B 1 472 ? 139.429 123.137 101.213 1.00 58.21  ? 459 PHE B CE1 1 
ATOM   6801 C CE2 . PHE B 1 472 ? 137.486 124.522 101.260 1.00 55.39  ? 459 PHE B CE2 1 
ATOM   6802 C CZ  . PHE B 1 472 ? 138.448 123.793 101.926 1.00 58.81  ? 459 PHE B CZ  1 
ATOM   6803 N N   . GLU B 1 473 ? 139.443 126.259 95.037  1.00 73.77  ? 460 GLU B N   1 
ATOM   6804 C CA  . GLU B 1 473 ? 139.199 126.487 93.621  1.00 75.45  ? 460 GLU B CA  1 
ATOM   6805 C C   . GLU B 1 473 ? 140.402 127.145 92.957  1.00 81.63  ? 460 GLU B C   1 
ATOM   6806 O O   . GLU B 1 473 ? 141.169 127.871 93.596  1.00 82.72  ? 460 GLU B O   1 
ATOM   6807 C CB  . GLU B 1 473 ? 137.966 127.363 93.410  1.00 69.14  ? 460 GLU B CB  1 
ATOM   6808 C CG  . GLU B 1 473 ? 136.699 126.761 93.960  1.00 70.31  ? 460 GLU B CG  1 
ATOM   6809 C CD  . GLU B 1 473 ? 135.482 127.574 93.602  1.00 69.23  ? 460 GLU B CD  1 
ATOM   6810 O OE1 . GLU B 1 473 ? 135.623 128.525 92.806  1.00 69.92  ? 460 GLU B OE1 1 
ATOM   6811 O OE2 . GLU B 1 473 ? 134.388 127.267 94.116  1.00 70.83  ? 460 GLU B OE2 1 
ATOM   6812 N N   . LEU B 1 474 ? 140.556 126.874 91.659  1.00 85.23  ? 461 LEU B N   1 
ATOM   6813 C CA  . LEU B 1 474 ? 141.531 127.562 90.828  1.00 95.05  ? 461 LEU B CA  1 
ATOM   6814 C C   . LEU B 1 474 ? 140.827 128.693 90.097  1.00 102.39 ? 461 LEU B C   1 
ATOM   6815 O O   . LEU B 1 474 ? 139.963 128.421 89.250  1.00 107.08 ? 461 LEU B O   1 
ATOM   6816 C CB  . LEU B 1 474 ? 142.166 126.600 89.826  1.00 95.36  ? 461 LEU B CB  1 
ATOM   6817 C CG  . LEU B 1 474 ? 142.849 125.344 90.377  1.00 87.30  ? 461 LEU B CG  1 
ATOM   6818 C CD1 . LEU B 1 474 ? 143.155 124.356 89.256  1.00 82.46  ? 461 LEU B CD1 1 
ATOM   6819 C CD2 . LEU B 1 474 ? 144.116 125.685 91.164  1.00 89.51  ? 461 LEU B CD2 1 
ATOM   6820 N N   . PRO B 1 475 ? 141.141 129.959 90.376  1.00 104.37 ? 462 PRO B N   1 
ATOM   6821 C CA  . PRO B 1 475 ? 140.500 131.042 89.619  1.00 112.73 ? 462 PRO B CA  1 
ATOM   6822 C C   . PRO B 1 475 ? 141.011 131.086 88.189  1.00 116.40 ? 462 PRO B C   1 
ATOM   6823 O O   . PRO B 1 475 ? 142.133 131.532 87.928  1.00 118.65 ? 462 PRO B O   1 
ATOM   6824 C CB  . PRO B 1 475 ? 140.886 132.302 90.406  1.00 115.50 ? 462 PRO B CB  1 
ATOM   6825 C CG  . PRO B 1 475 ? 141.295 131.808 91.761  1.00 104.32 ? 462 PRO B CG  1 
ATOM   6826 C CD  . PRO B 1 475 ? 141.919 130.470 91.515  1.00 99.08  ? 462 PRO B CD  1 
ATOM   6827 N N   . ARG B 1 476 ? 140.179 130.625 87.256  1.00 121.69 ? 463 ARG B N   1 
ATOM   6828 C CA  . ARG B 1 476 ? 140.558 130.463 85.860  1.00 130.24 ? 463 ARG B CA  1 
ATOM   6829 C C   . ARG B 1 476 ? 139.407 130.923 84.979  1.00 139.25 ? 463 ARG B C   1 
ATOM   6830 O O   . ARG B 1 476 ? 138.240 130.840 85.371  1.00 141.87 ? 463 ARG B O   1 
ATOM   6831 C CB  . ARG B 1 476 ? 140.901 129.001 85.533  1.00 130.53 ? 463 ARG B CB  1 
ATOM   6832 C CG  . ARG B 1 476 ? 141.853 128.325 86.511  1.00 124.15 ? 463 ARG B CG  1 
ATOM   6833 C CD  . ARG B 1 476 ? 143.264 128.870 86.402  1.00 126.41 ? 463 ARG B CD  1 
ATOM   6834 N NE  . ARG B 1 476 ? 143.815 128.656 85.070  1.00 133.28 ? 463 ARG B NE  1 
ATOM   6835 C CZ  . ARG B 1 476 ? 144.440 127.553 84.683  1.00 133.52 ? 463 ARG B CZ  1 
ATOM   6836 N NH1 . ARG B 1 476 ? 144.624 126.536 85.508  1.00 126.56 ? 463 ARG B NH1 1 
ATOM   6837 N NH2 . ARG B 1 476 ? 144.892 127.469 83.435  1.00 134.86 ? 463 ARG B NH2 1 
ATOM   6838 N N   . GLU B 1 477 ? 139.745 131.386 83.776  1.00 142.36 ? 464 GLU B N   1 
ATOM   6839 C CA  . GLU B 1 477 ? 138.768 131.886 82.808  1.00 147.87 ? 464 GLU B CA  1 
ATOM   6840 C C   . GLU B 1 477 ? 137.809 132.884 83.464  1.00 155.21 ? 464 GLU B C   1 
ATOM   6841 O O   . GLU B 1 477 ? 136.603 132.663 83.572  1.00 159.46 ? 464 GLU B O   1 
ATOM   6842 C CB  . GLU B 1 477 ? 137.999 130.731 82.158  1.00 146.34 ? 464 GLU B CB  1 
ATOM   6843 C CG  . GLU B 1 477 ? 138.717 130.057 80.992  1.00 145.15 ? 464 GLU B CG  1 
ATOM   6844 C CD  . GLU B 1 477 ? 139.698 128.985 81.429  1.00 141.98 ? 464 GLU B CD  1 
ATOM   6845 O OE1 . GLU B 1 477 ? 140.537 129.255 82.312  1.00 136.66 ? 464 GLU B OE1 1 
ATOM   6846 O OE2 . GLU B 1 477 ? 139.624 127.864 80.883  1.00 142.87 ? 464 GLU B OE2 1 
ATOM   6847 N N   . TYR B 1 478 ? 138.398 133.991 83.917  1.00 155.45 ? 465 TYR B N   1 
ATOM   6848 C CA  . TYR B 1 478 ? 137.635 135.013 84.620  1.00 159.42 ? 465 TYR B CA  1 
ATOM   6849 C C   . TYR B 1 478 ? 136.486 135.526 83.761  1.00 168.32 ? 465 TYR B C   1 
ATOM   6850 O O   . TYR B 1 478 ? 136.643 135.758 82.559  1.00 169.10 ? 465 TYR B O   1 
ATOM   6851 C CB  . TYR B 1 478 ? 138.547 136.173 85.021  1.00 156.56 ? 465 TYR B CB  1 
ATOM   6852 C CG  . TYR B 1 478 ? 139.128 136.048 86.411  1.00 155.19 ? 465 TYR B CG  1 
ATOM   6853 C CD1 . TYR B 1 478 ? 138.311 136.123 87.530  1.00 155.18 ? 465 TYR B CD1 1 
ATOM   6854 C CD2 . TYR B 1 478 ? 140.492 135.867 86.605  1.00 151.51 ? 465 TYR B CD2 1 
ATOM   6855 C CE1 . TYR B 1 478 ? 138.833 136.014 88.804  1.00 148.00 ? 465 TYR B CE1 1 
ATOM   6856 C CE2 . TYR B 1 478 ? 141.024 135.758 87.878  1.00 146.63 ? 465 TYR B CE2 1 
ATOM   6857 C CZ  . TYR B 1 478 ? 140.188 135.832 88.973  1.00 142.76 ? 465 TYR B CZ  1 
ATOM   6858 O OH  . TYR B 1 478 ? 140.710 135.723 90.242  1.00 135.95 ? 465 TYR B OH  1 
ATOM   6859 N N   . ARG B 1 479 ? 135.325 135.693 84.392  1.00 172.00 ? 466 ARG B N   1 
ATOM   6860 C CA  . ARG B 1 479 ? 134.116 136.185 83.731  1.00 171.45 ? 466 ARG B CA  1 
ATOM   6861 C C   . ARG B 1 479 ? 133.734 135.313 82.538  1.00 169.47 ? 466 ARG B C   1 
ATOM   6862 O O   . ARG B 1 479 ? 133.353 134.153 82.704  1.00 167.94 ? 466 ARG B O   1 
ATOM   6863 C CB  . ARG B 1 479 ? 134.292 137.642 83.287  1.00 169.70 ? 466 ARG B CB  1 
ATOM   6864 C CG  . ARG B 1 479 ? 134.015 138.679 84.375  1.00 165.10 ? 466 ARG B CG  1 
ATOM   6865 C CD  . ARG B 1 479 ? 135.078 138.677 85.465  1.00 164.32 ? 466 ARG B CD  1 
ATOM   6866 N NE  . ARG B 1 479 ? 134.836 139.712 86.463  1.00 167.03 ? 466 ARG B NE  1 
ATOM   6867 C CZ  . ARG B 1 479 ? 135.579 139.897 87.546  1.00 165.62 ? 466 ARG B CZ  1 
ATOM   6868 N NH1 . ARG B 1 479 ? 136.621 139.126 87.811  1.00 162.06 ? 466 ARG B NH1 1 
ATOM   6869 N NH2 . ARG B 1 479 ? 135.268 140.881 88.385  1.00 166.13 ? 466 ARG B NH2 1 
HETATM 6870 C C1  . NAG C 2 .   ? 129.828 149.766 114.015 1.00 80.99  ? 501 NAG A C1  1 
HETATM 6871 C C2  . NAG C 2 .   ? 130.664 150.356 115.159 1.00 82.68  ? 501 NAG A C2  1 
HETATM 6872 C C3  . NAG C 2 .   ? 132.053 150.745 114.658 1.00 82.46  ? 501 NAG A C3  1 
HETATM 6873 C C4  . NAG C 2 .   ? 132.703 149.604 113.884 1.00 79.92  ? 501 NAG A C4  1 
HETATM 6874 C C5  . NAG C 2 .   ? 131.744 149.131 112.790 1.00 81.85  ? 501 NAG A C5  1 
HETATM 6875 C C6  . NAG C 2 .   ? 132.272 147.988 111.951 1.00 84.92  ? 501 NAG A C6  1 
HETATM 6876 C C7  . NAG C 2 .   ? 129.571 151.594 116.994 1.00 87.72  ? 501 NAG A C7  1 
HETATM 6877 C C8  . NAG C 2 .   ? 128.915 152.906 117.349 1.00 87.66  ? 501 NAG A C8  1 
HETATM 6878 N N2  . NAG C 2 .   ? 130.010 151.505 115.725 1.00 85.95  ? 501 NAG A N2  1 
HETATM 6879 O O3  . NAG C 2 .   ? 132.815 151.118 115.776 1.00 82.61  ? 501 NAG A O3  1 
HETATM 6880 O O4  . NAG C 2 .   ? 133.909 150.097 113.347 1.00 84.07  ? 501 NAG A O4  1 
HETATM 6881 O O5  . NAG C 2 .   ? 130.543 148.719 113.404 1.00 80.33  ? 501 NAG A O5  1 
HETATM 6882 O O6  . NAG C 2 .   ? 133.261 148.463 111.070 1.00 87.52  ? 501 NAG A O6  1 
HETATM 6883 O O7  . NAG C 2 .   ? 129.685 150.694 117.811 1.00 86.90  ? 501 NAG A O7  1 
HETATM 6884 C C1  . NAG D 2 .   ? 102.917 116.219 160.297 1.00 116.03 ? 502 NAG A C1  1 
HETATM 6885 C C2  . NAG D 2 .   ? 102.181 116.452 161.625 1.00 120.16 ? 502 NAG A C2  1 
HETATM 6886 C C3  . NAG D 2 .   ? 101.077 115.411 161.799 1.00 120.29 ? 502 NAG A C3  1 
HETATM 6887 C C4  . NAG D 2 .   ? 100.170 115.380 160.574 1.00 123.17 ? 502 NAG A C4  1 
HETATM 6888 C C5  . NAG D 2 .   ? 101.022 115.187 159.316 1.00 121.44 ? 502 NAG A C5  1 
HETATM 6889 C C6  . NAG D 2 .   ? 100.221 115.174 158.032 1.00 119.30 ? 502 NAG A C6  1 
HETATM 6890 C C7  . NAG D 2 .   ? 103.430 117.470 163.491 1.00 122.77 ? 502 NAG A C7  1 
HETATM 6891 C C8  . NAG D 2 .   ? 104.401 117.179 164.609 1.00 117.20 ? 502 NAG A C8  1 
HETATM 6892 N N2  . NAG D 2 .   ? 103.089 116.407 162.741 1.00 124.19 ? 502 NAG A N2  1 
HETATM 6893 O O3  . NAG D 2 .   ? 100.366 115.725 162.966 1.00 125.67 ? 502 NAG A O3  1 
HETATM 6894 O O4  . NAG D 2 .   ? 99.260  114.320 160.758 1.00 126.62 ? 502 NAG A O4  1 
HETATM 6895 O O5  . NAG D 2 .   ? 101.978 116.227 159.244 1.00 120.43 ? 502 NAG A O5  1 
HETATM 6896 O O6  . NAG D 2 .   ? 99.465  113.990 157.952 1.00 118.87 ? 502 NAG A O6  1 
HETATM 6897 O O7  . NAG D 2 .   ? 102.998 118.597 163.299 1.00 124.16 ? 502 NAG A O7  1 
HETATM 6898 C C1  . NAG E 2 .   ? 130.022 96.350  134.901 1.00 109.32 ? 501 NAG B C1  1 
HETATM 6899 C C2  . NAG E 2 .   ? 131.182 97.205  134.362 1.00 114.55 ? 501 NAG B C2  1 
HETATM 6900 C C3  . NAG E 2 .   ? 132.553 96.610  134.684 1.00 112.62 ? 501 NAG B C3  1 
HETATM 6901 C C4  . NAG E 2 .   ? 132.620 96.219  136.152 1.00 114.92 ? 501 NAG B C4  1 
HETATM 6902 C C5  . NAG E 2 .   ? 131.469 95.250  136.420 1.00 114.44 ? 501 NAG B C5  1 
HETATM 6903 C C6  . NAG E 2 .   ? 131.498 94.622  137.798 1.00 111.69 ? 501 NAG B C6  1 
HETATM 6904 C C7  . NAG E 2 .   ? 130.364 98.390  132.360 1.00 118.16 ? 501 NAG B C7  1 
HETATM 6905 C C8  . NAG E 2 .   ? 130.371 98.372  130.852 1.00 121.00 ? 501 NAG B C8  1 
HETATM 6906 N N2  . NAG E 2 .   ? 131.048 97.388  132.941 1.00 119.52 ? 501 NAG B N2  1 
HETATM 6907 O O3  . NAG E 2 .   ? 133.532 97.558  134.350 1.00 101.33 ? 501 NAG B O3  1 
HETATM 6908 O O4  . NAG E 2 .   ? 133.876 95.625  136.381 1.00 115.09 ? 501 NAG B O4  1 
HETATM 6909 O O5  . NAG E 2 .   ? 130.259 95.962  136.238 1.00 111.26 ? 501 NAG B O5  1 
HETATM 6910 O O6  . NAG E 2 .   ? 132.651 93.824  137.948 1.00 105.92 ? 501 NAG B O6  1 
HETATM 6911 O O7  . NAG E 2 .   ? 129.774 99.255  132.991 1.00 113.88 ? 501 NAG B O7  1 
HETATM 6912 C C1  . NAG F 2 .   ? 103.065 131.598 89.458  1.00 120.37 ? 502 NAG B C1  1 
HETATM 6913 C C2  . NAG F 2 .   ? 101.602 131.142 89.417  1.00 121.54 ? 502 NAG B C2  1 
HETATM 6914 C C3  . NAG F 2 .   ? 100.678 132.284 89.819  1.00 120.56 ? 502 NAG B C3  1 
HETATM 6915 C C4  . NAG F 2 .   ? 101.057 132.692 91.234  1.00 116.24 ? 502 NAG B C4  1 
HETATM 6916 C C5  . NAG F 2 .   ? 102.526 133.125 91.269  1.00 116.65 ? 502 NAG B C5  1 
HETATM 6917 C C6  . NAG F 2 .   ? 102.982 133.440 92.679  1.00 111.27 ? 502 NAG B C6  1 
HETATM 6918 C C7  . NAG F 2 .   ? 101.198 131.150 86.944  1.00 120.97 ? 502 NAG B C7  1 
HETATM 6919 C C8  . NAG F 2 .   ? 100.799 130.233 85.814  1.00 117.39 ? 502 NAG B C8  1 
HETATM 6920 N N2  . NAG F 2 .   ? 101.256 130.547 88.148  1.00 123.10 ? 502 NAG B N2  1 
HETATM 6921 O O3  . NAG F 2 .   ? 99.355  131.825 89.740  1.00 124.61 ? 502 NAG B O3  1 
HETATM 6922 O O4  . NAG F 2 .   ? 100.185 133.722 91.643  1.00 110.88 ? 502 NAG B O4  1 
HETATM 6923 O O5  . NAG F 2 .   ? 103.351 132.094 90.751  1.00 118.08 ? 502 NAG B O5  1 
HETATM 6924 O O6  . NAG F 2 .   ? 104.019 134.391 92.675  1.00 105.86 ? 502 NAG B O6  1 
HETATM 6925 O O7  . NAG F 2 .   ? 101.436 132.332 86.743  1.00 120.23 ? 502 NAG B O7  1 
# 
